The central role of tRNA in genetic code expansion

The development of orthogonal translation systems (OTSs) for genetic code expansion (GCE) has allowed for the incorporation of a diverse array of non-canonical amino acids (ncAA) into proteins. Transfer RNA, the central molecule in the translation of the genetic message into proteins, plays a signif...

Full description

Saved in:
Bibliographic Details
Published inBiochimica et biophysica acta Vol. 1861; no. 11; pp. 3001 - 3008
Main Authors Reynolds, Noah M., Vargas-Rodriguez, Oscar, Söll, Dieter, Crnković, Ana
Format Journal Article
LanguageEnglish
Published Netherlands Elsevier B.V 01.11.2017
Elsevier
Subjects
Online AccessGet full text

Cover

Loading…
Abstract The development of orthogonal translation systems (OTSs) for genetic code expansion (GCE) has allowed for the incorporation of a diverse array of non-canonical amino acids (ncAA) into proteins. Transfer RNA, the central molecule in the translation of the genetic message into proteins, plays a significant role in the efficiency of ncAA incorporation. Here we review the biochemical basis of OTSs for genetic code expansion. We focus on the role of tRNA and discuss strategies used to engineer tRNA for the improvement of ncAA incorporation into proteins. The engineering of orthogonal tRNAs for GCE has significantly improved the incorporation of ncAAs. However, there are numerous unintended consequences of orthogonal tRNA engineering that cannot be predicted ab initio. Genetic code expansion has allowed for the incorporation of a great diversity of ncAAs and novel chemistries into proteins, making significant contributions to our understanding of biological molecules and interactions. This article is part of a Special Issue entitled “Biochemistry of Synthetic Biology - Recent Developments” Guest Editor: Dr. Ilka Heinemann and Dr. Patrick O'Donoghue. [Display omitted] •Transfer RNA is the central molecule in the translation of nucleic acid into protein.•Engineering of orthogonal tRNA (o-tRNA) interactions with host translational machinery aids genetic code expansion (GCE).•There are many unexpected outcomes of o-tRNA engineering.•Full orthogonality of tRNAs devoted to GCE is vital for cellular fitness.
AbstractList The development of orthogonal translation systems (OTSs) for genetic code expansion (GCE) has allowed for the incorporation of a diverse array of non-canonical amino acids (ncAA) into proteins. Transfer RNA, the central molecule in the translation of the genetic message into proteins, plays a significant role in the efficiency of ncAA incorporation. Here we review the biochemical basis of OTSs for genetic code expansion. We focus on the role of tRNA and discuss strategies used to engineer tRNA for the improvement of ncAA incorporation into proteins. The engineering of orthogonal tRNAs for GCE has significantly improved the incorporation of ncAAs. However, there are numerous unintended consequences of orthogonal tRNA engineering that cannot be predicted ab initio. Genetic code expansion has allowed for the incorporation of a great diversity of ncAAs and novel chemistries into proteins, making significant contributions to our understanding of biological molecules and interactions. This article is part of a Special Issue entitled "Biochemistry of Synthetic Biology - Recent Developments" Guest Editor: Dr. Ilka Heinemann and Dr. Patrick O'Donoghue.
The development of orthogonal translation systems (OTSs) for genetic code expansion (GCE) has allowed for the incorporation of a diverse array of non-canonical amino acids (ncAA) into proteins. Transfer RNA, the central molecule in the translation of the genetic message into proteins, plays a significant role in the efficiency of ncAA incorporation.BACKGROUNDThe development of orthogonal translation systems (OTSs) for genetic code expansion (GCE) has allowed for the incorporation of a diverse array of non-canonical amino acids (ncAA) into proteins. Transfer RNA, the central molecule in the translation of the genetic message into proteins, plays a significant role in the efficiency of ncAA incorporation.Here we review the biochemical basis of OTSs for genetic code expansion. We focus on the role of tRNA and discuss strategies used to engineer tRNA for the improvement of ncAA incorporation into proteins.SCOPE OF REVIEWHere we review the biochemical basis of OTSs for genetic code expansion. We focus on the role of tRNA and discuss strategies used to engineer tRNA for the improvement of ncAA incorporation into proteins.The engineering of orthogonal tRNAs for GCE has significantly improved the incorporation of ncAAs. However, there are numerous unintended consequences of orthogonal tRNA engineering that cannot be predicted ab initio.MAJOR CONCLUSIONSThe engineering of orthogonal tRNAs for GCE has significantly improved the incorporation of ncAAs. However, there are numerous unintended consequences of orthogonal tRNA engineering that cannot be predicted ab initio.Genetic code expansion has allowed for the incorporation of a great diversity of ncAAs and novel chemistries into proteins, making significant contributions to our understanding of biological molecules and interactions. This article is part of a Special Issue entitled "Biochemistry of Synthetic Biology - Recent Developments" Guest Editor: Dr. Ilka Heinemann and Dr. Patrick O'Donoghue.GENERAL SIGNIFICANCEGenetic code expansion has allowed for the incorporation of a great diversity of ncAAs and novel chemistries into proteins, making significant contributions to our understanding of biological molecules and interactions. This article is part of a Special Issue entitled "Biochemistry of Synthetic Biology - Recent Developments" Guest Editor: Dr. Ilka Heinemann and Dr. Patrick O'Donoghue.
The development of orthogonal translation systems (OTSs) for genetic code expansion (GCE) has allowed for the incorporation of a diverse array of non-canonical amino acids (ncAA) into proteins. Transfer RNA, the central molecule in the translation of the genetic message into proteins, plays a significant role in the efficiency of ncAA incorporation. Here we review the biochemical basis of OTSs for genetic code expansion. We focus on the role of tRNA and discuss strategies used to engineer tRNA for the improvement of ncAA incorporation into proteins. The engineering of orthogonal tRNAs for GCE has significantly improved the incorporation of ncAAs. However, there are numerous unintended consequences of orthogonal tRNA engineering that cannot be predicted ab initio. Genetic code expansion has allowed for the incorporation of a great diversity of ncAAs and novel chemistries into proteins, making significant contributions to our understanding of biological molecules and interactions. This article is part of a Special Issue entitled “Biochemistry of Synthetic Biology - Recent Developments” Guest Editor: Dr. Ilka Heinemann and Dr. Patrick O'Donoghue. [Display omitted] •Transfer RNA is the central molecule in the translation of nucleic acid into protein.•Engineering of orthogonal tRNA (o-tRNA) interactions with host translational machinery aids genetic code expansion (GCE).•There are many unexpected outcomes of o-tRNA engineering.•Full orthogonality of tRNAs devoted to GCE is vital for cellular fitness.
The development of orthogonal translation systems (OTSs) for genetic code expansion (GCE) has allowed for the incorporation of a diverse array of non-canonical amino acids (ncAA) into proteins. Transfer RNA, the central molecule in the translation of the genetic message into proteins, plays a significant role in the efficiency of ncAA incorporation.Here we review the biochemical basis of OTSs for genetic code expansion. We focus on the role of tRNA and discuss strategies used to engineer tRNA for the improvement of ncAA incorporation into proteins.The engineering of orthogonal tRNAs for GCE has significantly improved the incorporation of ncAAs. However, there are numerous unintended consequences of orthogonal tRNA engineering that cannot be predicted ab initio.Genetic code expansion has allowed for the incorporation of a great diversity of ncAAs and novel chemistries into proteins, making significant contributions to our understanding of biological molecules and interactions. This article is part of a Special Issue entitled “Biochemistry of Synthetic Biology - Recent Developments” Guest Editor: Dr. Ilka Heinemann and Dr. Patrick O'Donoghue.
Not provided.
Author Söll, Dieter
Reynolds, Noah M.
Vargas-Rodriguez, Oscar
Crnković, Ana
AuthorAffiliation b Department of Chemistry, Yale University, New Haven, Connecticut 06520-8114, USA
a Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06520-8114, USA
AuthorAffiliation_xml – name: a Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06520-8114, USA
– name: b Department of Chemistry, Yale University, New Haven, Connecticut 06520-8114, USA
Author_xml – sequence: 1
  givenname: Noah M.
  surname: Reynolds
  fullname: Reynolds, Noah M.
  email: noah.reynolds@yale.edu
  organization: Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520-8114, USA
– sequence: 2
  givenname: Oscar
  surname: Vargas-Rodriguez
  fullname: Vargas-Rodriguez, Oscar
  organization: Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520-8114, USA
– sequence: 3
  givenname: Dieter
  surname: Söll
  fullname: Söll, Dieter
  organization: Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520-8114, USA
– sequence: 4
  givenname: Ana
  surname: Crnković
  fullname: Crnković, Ana
  email: ana.crnkovic@yale.edu
  organization: Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520-8114, USA
BackLink https://www.ncbi.nlm.nih.gov/pubmed/28323071$$D View this record in MEDLINE/PubMed
https://www.osti.gov/biblio/1538022$$D View this record in Osti.gov
BookMark eNqFkUtv1DAUhS1URKeFf4BQxIpNwvU7YYFUVbykCiRU1pZj33Q8ythDnKnov6-jGSpgQb3xwucen_udM3ISU0RCXlJoKFD1dtP0vb3B2DCgugHeAGVPyIq2mtUtgDohK-AgakGVPCVnOW-gHNnJZ-SUtZxx0HRF2PUaK4dxnuxYTWnEKg3V_P3rRRViVdxxDq5yyWOFv3Y25pDic_J0sGPGF8f7nPz4-OH68nN99e3Tl8uLq9rJtptr3XneYq9sS1mnFPVi4IzCYIdW8GHonEKuvRQahPBaCtZ3TPJBeAQvpXP8nLw_-O72_Rb9MaTZTWFrpzuTbDB_v8SwNjfp1kgFnEtdDF4fDFKeg8kuzOjWLsWIbjZU8hYYK6I3x1-m9HOPeTbbkB2Oo42Y9tmwAk0oqbR6VFrQL4tqCUX66s_sD6F_gy8CcRC4KeU84fAgoWCWfs3GHPo1S78GuCn9lrF3_4yVrexcWikEwvjY8BEoltZuA04LE4wOfZgWJD6F_xvcAwRqwGk
CitedBy_id crossref_primary_10_1021_acs_biochem_9b00746
crossref_primary_10_1534_genetics_117_203232
crossref_primary_10_1016_j_cbpa_2018_07_016
crossref_primary_10_1021_acssynbio_2c00267
crossref_primary_10_1021_acssynbio_7b00421
crossref_primary_10_1016_j_tim_2023_09_002
crossref_primary_10_1093_nar_gkae1112
crossref_primary_10_3389_fgene_2024_1420331
crossref_primary_10_3390_ijms20092294
crossref_primary_10_1038_s42003_020_1074_2
crossref_primary_10_1021_acs_chemrev_4c00329
crossref_primary_10_1021_acssynbio_8b00100
crossref_primary_10_1021_acs_chemrev_3c00850
crossref_primary_10_1021_acssynbio_0c00298
crossref_primary_10_1021_acs_chemrev_3c00878
crossref_primary_10_3390_ijms26020539
crossref_primary_10_1002_cbic_202000338
crossref_primary_10_1016_j_copbio_2022_102691
crossref_primary_10_1002_wrna_1530
crossref_primary_10_1021_acs_biochem_2c00711
crossref_primary_10_1534_g3_120_401876
crossref_primary_10_3390_ijms22020895
crossref_primary_10_1261_rna_071720_119
crossref_primary_10_3390_bioengineering5010011
crossref_primary_10_1016_j_jbc_2024_107679
Cites_doi 10.1038/ncomms9130
10.1074/jbc.273.21.12685
10.1038/nature07611
10.1021/bi00344a019
10.1093/emboj/21.11.2769
10.1038/nchem.1919
10.1016/0092-8674(75)90129-4
10.1002/j.1460-2075.1984.tb01934.x
10.1016/S0092-8674(00)80123-3
10.1002/anie.201301094
10.1016/S0022-2836(66)80022-0
10.1073/pnas.1424127112
10.1146/annurev.micro.091208.073210
10.1042/bj1600185
10.1002/anie.200904035
10.1016/j.mib.2008.02.003
10.1021/ja040175z
10.1093/femsre/fuv004
10.1002/1873-3468.12182
10.1038/228057a0
10.1021/ja075557u
10.1093/nar/gks1007
10.1074/jbc.M111.279810
10.1016/j.jmb.2007.08.010
10.1038/nchembio.1823
10.1073/pnas.142220099
10.1093/nar/18.23.6815
10.1006/jmbi.1993.1277
10.1021/acssynbio.5b00197
10.1093/nar/29.20.4125
10.1073/pnas.0608762103
10.1016/j.jmb.2009.01.021
10.1039/C4SC01534G
10.1021/ja104609m
10.1080/10409230600602634
10.1073/pnas.251438898
10.1016/0022-2836(74)90449-5
10.1021/ja407511q
10.1093/nar/gkq707
10.1093/nar/26.19.4374
10.1016/j.jmb.2003.12.080
10.1093/nar/gkv800
10.1038/nature09929
10.1038/331723a0
10.1038/nn1932
10.1038/nsmb.1370
10.1016/j.cbpa.2008.01.027
10.1093/nar/26.22.5017
10.1073/pnas.0307029101
10.1016/j.jmb.2007.05.017
10.1016/S0167-4781(03)00045-9
10.1038/nrmicro2472
10.1021/ja3063524
10.1002/wrna.64
10.1074/jbc.M801838200
10.1126/science.1060077
10.1093/nar/gkf589
10.1126/science.1207203
10.1074/jbc.C400304200
10.1016/j.tibs.2005.10.006
10.1016/j.febslet.2009.11.053
10.1261/rna.033654.112
10.1021/ja046843y
10.1016/j.molcel.2007.09.015
10.1021/acs.biochem.5b01167
10.1021/ja000595y
10.1016/j.cbpa.2015.06.008
10.1016/S0022-5193(88)80327-8
10.1146/annurev.biochem.74.061903.155440
10.1016/S0021-9258(18)54137-5
10.1093/nar/gkq521
10.1073/pnas.1222641110
10.1016/j.bbapap.2014.03.002
10.1093/emboj/cdf362
10.1038/nchembio.657
10.1016/0092-8674(83)90398-7
10.1073/pnas.75.4.1759
10.1016/j.bbrc.2008.04.164
10.1038/nsmb.2003
10.1126/science.1084772
10.1073/pnas.61.2.768
10.1101/gad.1956510
10.1021/ja073487l
10.1021/ja2054034
10.1016/j.jmb.2009.10.030
10.1002/pro.322
10.1021/acs.biochem.6b00157
10.1126/science.1064242
10.1126/science.277.5331.1453
10.1074/jbc.M115.640060
10.1016/S0969-2126(99)80021-5
10.4161/15476286.2014.992273
10.1038/srep17196
10.1073/pnas.0803531105
10.1016/j.jmb.2015.09.003
10.1073/pnas.1102128108
10.1128/MCB.16.3.907
10.1016/S0021-9258(17)30417-9
10.1093/nar/gku1248
10.1021/cb200542j
10.1016/j.copbio.2011.12.027
10.1016/j.jmb.2005.05.022
10.1038/nmeth864
10.1016/j.str.2010.12.017
10.1016/S1074-5521(03)00123-6
10.1261/rna.042234.113
10.1016/j.bbaexp.2005.02.011
10.1074/jbc.M212890200
10.1021/acs.biochem.5b01185
10.1021/ja800894n
10.1093/nar/gku1087
10.1093/nar/29.23.4767
10.1016/B978-0-12-386497-0.00003-7
10.1038/nature13440
10.1016/S1074-5521(96)90169-6
10.1021/acs.biochem.5b00870
10.1093/nar/gkl1151
10.1038/nsmb.1423
10.1093/nar/gkp001
10.1073/pnas.0603965103
10.1126/science.2452483
10.1111/1574-6968.12371
10.1016/j.gene.2011.06.015
10.1074/jbc.274.50.35601
10.1038/nbt.2714
10.1126/science.270.5241.1464
10.1093/nar/gkw608
10.1146/annurev.biochem.69.1.617
ContentType Journal Article
Copyright 2017 Elsevier B.V.
Copyright © 2017 Elsevier B.V. All rights reserved.
Copyright_xml – notice: 2017 Elsevier B.V.
– notice: Copyright © 2017 Elsevier B.V. All rights reserved.
CorporateAuthor Yale Univ., New Haven, CT (United States)
CorporateAuthor_xml – name: Yale Univ., New Haven, CT (United States)
DBID AAYXX
CITATION
CGR
CUY
CVF
ECM
EIF
NPM
7X8
7S9
L.6
OTOTI
5PM
DOI 10.1016/j.bbagen.2017.03.012
DatabaseName CrossRef
Medline
MEDLINE
MEDLINE (Ovid)
MEDLINE
MEDLINE
PubMed
MEDLINE - Academic
AGRICOLA
AGRICOLA - Academic
OSTI.GOV
PubMed Central (Full Participant titles)
DatabaseTitle CrossRef
MEDLINE
Medline Complete
MEDLINE with Full Text
PubMed
MEDLINE (Ovid)
MEDLINE - Academic
AGRICOLA
AGRICOLA - Academic
DatabaseTitleList MEDLINE
MEDLINE - Academic

AGRICOLA

Database_xml – sequence: 1
  dbid: NPM
  name: PubMed
  url: https://proxy.k.utb.cz/login?url=http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed
  sourceTypes: Index Database
– sequence: 2
  dbid: EIF
  name: MEDLINE
  url: https://proxy.k.utb.cz/login?url=https://www.webofscience.com/wos/medline/basic-search
  sourceTypes: Index Database
DeliveryMethod fulltext_linktorsrc
Discipline Chemistry
Biology
EISSN 1872-8006
1878-2434
EndPage 3008
ExternalDocumentID PMC5603357
1538022
28323071
10_1016_j_bbagen_2017_03_012
S0304416517300958
Genre Research Support, U.S. Gov't, Non-P.H.S
Review
Journal Article
Research Support, N.I.H., Extramural
GrantInformation_xml – fundername: NIGMS NIH HHS
  grantid: R35 GM122560
– fundername: NIGMS NIH HHS
  grantid: R01 GM022854
– fundername: NIGMS NIH HHS
  grantid: R37 GM022854
GroupedDBID ---
--K
--M
.~1
0R~
1B1
1RT
1~.
1~5
23N
3O-
4.4
457
4G.
53G
5GY
5RE
5VS
7-5
71M
8P~
9JM
AACTN
AAEDT
AAEDW
AAIAV
AAIKJ
AAKOC
AALRI
AAOAW
AAQFI
AAQXK
AAXUO
ABEFU
ABFNM
ABGSF
ABMAC
ABUDA
ABXDB
ABYKQ
ACDAQ
ACIUM
ACRLP
ADBBV
ADEZE
ADMUD
ADUVX
AEBSH
AEHWI
AEKER
AFKWA
AFTJW
AFXIZ
AGHFR
AGRDE
AGUBO
AGYEJ
AHHHB
AIEXJ
AIKHN
AITUG
AJBFU
AJOXV
ALMA_UNASSIGNED_HOLDINGS
AMFUW
AMRAJ
ASPBG
AVWKF
AXJTR
AZFZN
BKOJK
BLXMC
CS3
DOVZS
EBS
EFJIC
EFLBG
EJD
EO8
EO9
EP2
EP3
FDB
FEDTE
FGOYB
FIRID
FNPLU
FYGXN
G-2
G-Q
GBLVA
HLW
HVGLF
HZ~
IHE
J1W
KOM
LX3
M41
MO0
N9A
O-L
O9-
OAUVE
OHT
OZT
P-8
P-9
PC.
Q38
R2-
ROL
RPZ
SBG
SCC
SDF
SDG
SDP
SES
SEW
SPCBC
SSU
SSZ
T5K
UQL
WH7
WUQ
XJT
XPP
~G-
AAHBH
AATTM
AAXKI
AAYWO
AAYXX
ABWVN
ACRPL
ACVFH
ADCNI
ADNMO
AEIPS
AEUPX
AFJKZ
AFPUW
AGCQF
AGQPQ
AGRNS
AIGII
AIIUN
AKBMS
AKRWK
AKYEP
ANKPU
APXCP
BNPGV
CITATION
SSH
CGR
CUY
CVF
ECM
EFKBS
EIF
NPM
7X8
7S9
L.6
AALMO
ABPIF
ABPTK
OTOTI
-~X
5PM
ABJNI
F5P
TWZ
Y6R
ID FETCH-LOGICAL-c589t-79d38eb6a8129661d4f3210faf843ff9c6e37d547044d7542b9253f4de0d55cc3
IEDL.DBID .~1
ISSN 0304-4165
0006-3002
IngestDate Thu Aug 21 14:09:26 EDT 2025
Fri May 19 02:14:24 EDT 2023
Mon Jul 21 10:50:32 EDT 2025
Fri Jul 11 03:32:42 EDT 2025
Mon Jul 21 06:02:48 EDT 2025
Tue Jul 01 00:22:09 EDT 2025
Thu Apr 24 22:53:14 EDT 2025
Fri Feb 23 02:34:14 EST 2024
IsDoiOpenAccess false
IsOpenAccess true
IsPeerReviewed true
IsScholarly true
Issue 11
Keywords Genetic code expansion
Non-canonical amino acids
Synthetic biology
Aminoacyl-tRNA synthetases
Transfer RNA
Orthogonal tRNAs
Language English
License Copyright © 2017 Elsevier B.V. All rights reserved.
LinkModel DirectLink
MergedId FETCHMERGED-LOGICAL-c589t-79d38eb6a8129661d4f3210faf843ff9c6e37d547044d7542b9253f4de0d55cc3
Notes ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
ObjectType-Review-3
content type line 23
FG02-98ER20311
USDOE Office of Science (SC)
OpenAccessLink https://www.sciencedirect.com/science/article/am/pii/S0304416517300958
PMID 28323071
PQID 1879661750
PQPubID 23479
PageCount 8
ParticipantIDs pubmedcentral_primary_oai_pubmedcentral_nih_gov_5603357
osti_scitechconnect_1538022
proquest_miscellaneous_2000465676
proquest_miscellaneous_1879661750
pubmed_primary_28323071
crossref_primary_10_1016_j_bbagen_2017_03_012
crossref_citationtrail_10_1016_j_bbagen_2017_03_012
elsevier_sciencedirect_doi_10_1016_j_bbagen_2017_03_012
ProviderPackageCode CITATION
AAYXX
PublicationCentury 2000
PublicationDate 2017-11-01
PublicationDateYYYYMMDD 2017-11-01
PublicationDate_xml – month: 11
  year: 2017
  text: 2017-11-01
  day: 01
PublicationDecade 2010
PublicationPlace Netherlands
PublicationPlace_xml – name: Netherlands
– name: United States
PublicationTitle Biochimica et biophysica acta
PublicationTitleAlternate Biochim Biophys Acta Gen Subj
PublicationYear 2017
Publisher Elsevier B.V
Elsevier
Publisher_xml – name: Elsevier B.V
– name: Elsevier
References Des Soye, Patel, Isaacs, Jewett (bb0020) 2015; 28
Xu, Chen, Xin, Chen, Jin, Wang (bb0280) 2001; 29
Rauch, Porter, Mehl, Perona (bb0560) 2016; 55
Ryu, Schultz (bb0100) 2006; 3
Naganuma, Sekine, Chong, Guo, Yang, Gamper, Hou, Schimmel, Yokoyama (bb0235) 2014; 510
Bershtein, Tawfik (bb0670) 2008; 12
Wan, Tharp, Liu (bb0315) 2014; 1844
Yamada, Matsugi, Ishikura, Murao (bb0500) 2005; 1728
Chin, Cropp, Chu, Meggers, Schultz (bb0185) 2003; 10
Louie, Jurnak (bb0470) 1985; 24
Giegé, Eriani (bb0035) 2014
Machnicka, Olchowik, Grosjean, Bujnicki (bb0590) 2014; 11
Fredrik Pettersson, Ardell, Kirsebom (bb0080) 2005; 351
Ieong, Pavlov, Kwiatkowski, Forster, Ehrenberg (bb0410) 2012; 134
Beier, Barciszewska, Sickinger (bb0545) 1984; 3
Kiga, Sakamoto, Kodama, Kigawa, Matsuda, Yabuki, Shirouzu, Harada, Nakayama, Takio, Hasegawa, Endo, Hirao, Yokoyama (bb0350) 2002; 99
Soma, Himeno (bb0270) 1998; 26
Hoesl, Budisa (bb0010) 2012; 23
Abelson, Trotta, Li (bb0130) 1998; 273
Yamada, Matsugi, Ishikura (bb0495) 2003; 1626
Aerni, Shifman, Rogulina, O'Donoghue, Rinehart (bb0645) 2015; 43
Chin, Cropp, Anderson, Mukherji, Zhang, Schultz (bb0255) 2003; 301
McClain, Foss (bb0230) 1988; 240
Dale, Uhlenbeck (bb0055) 2005; 30
Mukai, Wakiyama, Sakamoto, Yokoyama (bb0165) 2010; 19
Richardson, First (bb0360) 2016; 55
Rodriguez-Hernandez, Perona (bb0555) 2011; 19
Chen, Schultz, Brock (bb0190) 2007; 371
Schrader, Chapman, Uhlenbeck (bb0405) 2011; 108
Fan, Xiong, Reynolds, Söll (bb0415) 2015
Novoa, Vargas-Rodriguez, Lange, Goto, Suga, Musier-Forsyth, Ribas de Pouplana (bb0340) 2015; 290
Ellefson, Meyer, Hughes, Cannon, Brodbelt, Ellington (bb0300) 2014; 32
Mittelstaet, Konevega, Rodnina (bb0465) 2013; 135
Ogle, Ramakrishnan (bb0060) 2005; 74
Stortchevoi, Varshney, RajBhandary (bb0390) 2003; 278
Pirman, Barber, Aerni, Ma, Haimovich, Rogulina, Isaacs, Rinehart (bb0105) 2015; 6
Maraia, Lamichhane (bb0030) 2011; 2
Summerer, Chen, Wu, Deiters, Chin, Schultz (bb0195) 2006; 103
Steer, Schimmel (bb0250) 1999; 274
Ling, Reynolds, Ibba (bb0050) 2009; 63
Mukai, Hayashi, Iraha, Sato, Ohtake, Yokoyama, Sakamoto (bb0635) 2010; 38
Dennis, Bremer (bb0395) 1974; 84
Schiffer, Rosch, Marchfelder (bb0125) 2002; 21
Grosjean, Westhof (bb0515) 2016; 44
Hughes, Ellington (bb0295) 2010; 38
Schmeing, Voorhees, Kelley, Ramakrishnan (bb0660) 2011; 18
Biddle, Schmitt, Fisk (bb0575) 2015; 54
Walker, Engelke (bb0095) 2006; 41
Johnson, Xu, Shen, Takimoto, Schultz, Schmitz, Xiang, Ecker, Briggs, Wang (bb0640) 2011; 7
Bohlke, Budisa (bb0520) 2014; 351
Kothe, Wieden, Mohr, Rodnina (bb0485) 2004; 336
Edwards, Schimmel (bb0180) 1990; 10
Scolnick, Tompkins, Caskey, Nirenberg (bb0630) 1968; 61
Perona, Gruic-Sovulj (bb0330) 2014; 344
Hohn, Park, O'Donoghue, Schnitzbauer, Söll (bb0605) 2006; 103
Mukai, Kobayashi, Hino, Yanagisawa, Sakamoto, Yokoyama (bb0160) 2008; 371
Cantara, Murphy, Demirci, Agris (bb0530) 2013; 110
Altman (bb0075) 1975; 4
Drabkin, Park, RajBhandary (bb0140) 1996; 16
Hou, Schimmel (bb0225) 1988
Himeno, Hasegawa, Ueda, Watanabe, Shimizu (bb0240) 1990; 18
Ho, Reynolds, Rivera, Connolly, Guo, Ling, Pappin, Church, Söll (bb0320) 2016; 5
Lajoie, Söll, Church (bb0025) 2016; 428
Suzuki, Miyauchi, Suzuki, Yokobori, Shigi, Kondow, Takeuchi, Yamagishi, Watanabe (bb0535) 2011; 286
Biddle, Schmitt, Fisk (bb0580) 2016; 44
Dewe, Whipple, Chernyakov, Jaramillo, Phizicky (bb0215) 2012; 18
Wang, Magliery, Liu, Schultz (bb0245) 2000; 122
Nissen, Thirup, Kjeldgaard, Nyborg (bb0380) 1999; 7
Wang, Brock, Herberich, Schultz (bb0015) 2001; 292
Cload, Liu, Froland, Schultz (bb0435) 1996; 3
Young, Ahmad, Yin, Schultz (bb0085) 2010; 395
Doi, Ohtsuki, Shimizu, Ueda, Sisido (bb0460) 2007; 129
Rogalski, Karcher, Bock (bb0510) 2008; 15
Richardson, First (bb0355) 2016; 55
Wang, Takimoto, Louie, Baiga, Noel, Lee, Slesinger, Wang (bb0155) 2007; 10
Dumas, Lercher, Spicer, Davis (bb0005) 2015; 6
LaRiviere, Wolfson, Uhlenbeck (bb0370) 2001; 294
Maranhao, Ellington (bb0615) 2016
Guo, Melancon, Lee, Groff, Schultz (bb0420) 2009; 48
George, Aguirre, Spratt, Bi, Jeffery, Shaw, O'Donoghue (bb0650) 2016
Herring, Ambrogelly, Polycarpo, Söll (bb0305) 2007; 35
Takemoto, Spremulli, Benkowski, Ueda, Yokogawa, Watanabe (bb0525) 2009; 37
Nozawa, O'Donoghue, Gundllapalli, Araiso, Ishitani, Umehara, Söll, Nureki (bb0310) 2009; 457
Roy, Leszyk, Mangus, Jacobson (bb0665) 2015; 112
Chatterjee, Xiao, Yang, Soundararajan, Schultz (bb0290) 2013; 52
Schrader, Chapman, Uhlenbeck (bb0385) 2009; 386
Christian, Hou (bb0595) 2007; 373
Hancock, Uprety, Deiters, Chin (bb0205) 2010; 132
Rodnina (bb0475) 2012; 86
Asahara, Himeno, Tamura, Hasegawa, Watanabe, Shimizu (bb0265) 1993; 231
Jakubowski (bb0365) 1988; 133
Wang, Sachdeva, Cox, Wilf, Lang, Wallace, Mehl, Chin (bb0325) 2014; 6
Youngman, He, Nikstad, Green (bb0625) 2007; 28
Greiss, Chin (bb0175) 2011; 133
Shepherd, Ibba (bb0090) 2015; 39
Lagerkvist (bb0505) 1978; 75
Shao, Singh, Slade, Jones, Balasubramanian (bb0210) 2015; 5
Zhang, Alfonta, Tian, Bursulaya, Uryu, King, Schultz (bb0285) 2004; 101
Ieong, Pavlov, Kwiatkowski, Ehrenberg, Forster (bb0445) 2014; 20
Gustilo, Vendeix, Agris (bb0570) 2008; 11
Crick (bb0490) 1966; 19
Hirsh (bb0655) 1970; 228
Phizicky, Hopper (bb0065) 2010; 24
Nissen, Kjeldgaard, Thirup, Polekhina, Reshetnikova, Clark, Nyborg (bb0375) 1995; 270
Ito, Honda, Suzuki, Miyoshi, Murakami, Yao, Uchiumi (bb0480) 2014; 42
Park, Hohn, Umehara, Guo, Osborne, Benner, Noren, Rinehart, Söll (bb0450) 2011; 333
Hopper, Pai, Engelke (bb0135) 2010; 584
Leinfelder, Zehelein, Mandrand-Berthelot, Bock (bb0620) 1988; 331
Esvelt, Carlson, Liu (bb0675) 2011; 472
Hauenstein, Hou, Perona (bb0565) 2008; 283
Sakamoto, Hayashi, Sakamoto, Kiga, Nakayama, Soma, Kobayashi, Kitabatake, Takio, Saito, Shirouzu, Hirao, Yokoyama (bb0150) 2002; 30
Wang, Wang (bb0200) 2008; 130
Beier, Grimm (bb0540) 2001; 29
Orioli, Pascali, Pagano, Teichmann, Dieci (bb0120) 2012; 493
Zhang, Tan, Dickson, Nalam, Cornish, Forster (bb0440) 2007; 129
Rogerson, Sachdeva, Wang, Haq, Kazlauskaite, Hancock, Huguenin-Dezot, Muqit, Fry, Bayliss, Chin (bb0600) 2015; 11
Ibba, Söll (bb0040) 2000; 69
Allison, Goh, Hall (bb0115) 1983; 34
An, Musier-Forsyth (bb0335) 2004; 279
Blattner, Plunkett, Bloch, Perna, Burland, Riley, Collado-Vides, Glasner, Rode, Mayhew, Gregor, Davis, Kirkpatrick, Goeden, Rose, Mau, Shao (bb0070) 1997; 277
Wolf, Gerber, Keller (bb0585) 2002; 21
Machnicka, Milanowska, Osman Oglou, Purta, Kurkowska, Olchowik, Januszewski, Kalinowski, Dunin-Horkawicz, Rother, Helm, Bujnicki, Grosjean (bb0550) 2013; 41
Yesland, Nelson, Feathers, Johnson (bb0275) 1993; 268
Giege, Sissler, Florentz (bb0220) 1998; 26
Hecht, Alford, Kuroda, Kitano (bb0425) 1978; 253
Zhang, Liu, Slater, Hou (bb0610) 2008; 15
Wu, Deiters, Cropp, King, Schultz (bb0260) 2004; 126
Li, Deutscher (bb0110) 1996; 86
Kohrer, Xie, Kellerer, Varshney, RajBhandary (bb0145) 2001; 98
Parrish, She, Xiang, Coin, Shen, Briggs, Dillin, Wang (bb0170) 2012; 7
Reynolds, Lazazzera, Ibba (bb0045) 2010; 8
Oki, Sakamoto, Kobayashi, Sasaki, Yokoyama (bb0345) 2008; 105
Young, Bremer (bb0400) 1976; 160
Gan, Perez, Carlson, Ntai, Isaacs, Kelleher, Jewett (bb0455) 2016
Ramaswamy, Saito, Murakami, Shiba, Suga (bb0430) 2004; 126
Takemoto (10.1016/j.bbagen.2017.03.012_bb0525) 2009; 37
Richardson (10.1016/j.bbagen.2017.03.012_bb0355) 2016; 55
Grosjean (10.1016/j.bbagen.2017.03.012_bb0515) 2016; 44
Mukai (10.1016/j.bbagen.2017.03.012_bb0160) 2008; 371
Scolnick (10.1016/j.bbagen.2017.03.012_bb0630) 1968; 61
Blattner (10.1016/j.bbagen.2017.03.012_bb0070) 1997; 277
Chin (10.1016/j.bbagen.2017.03.012_bb0185) 2003; 10
Ellefson (10.1016/j.bbagen.2017.03.012_bb0300) 2014; 32
Kothe (10.1016/j.bbagen.2017.03.012_bb0485) 2004; 336
Shepherd (10.1016/j.bbagen.2017.03.012_bb0090) 2015; 39
Perona (10.1016/j.bbagen.2017.03.012_bb0330) 2014; 344
Des Soye (10.1016/j.bbagen.2017.03.012_bb0020) 2015; 28
Wang (10.1016/j.bbagen.2017.03.012_bb0325) 2014; 6
Machnicka (10.1016/j.bbagen.2017.03.012_bb0550) 2013; 41
Guo (10.1016/j.bbagen.2017.03.012_bb0420) 2009; 48
An (10.1016/j.bbagen.2017.03.012_bb0335) 2004; 279
Edwards (10.1016/j.bbagen.2017.03.012_bb0180) 1990; 10
Li (10.1016/j.bbagen.2017.03.012_bb0110) 1996; 86
Greiss (10.1016/j.bbagen.2017.03.012_bb0175) 2011; 133
Summerer (10.1016/j.bbagen.2017.03.012_bb0195) 2006; 103
Bohlke (10.1016/j.bbagen.2017.03.012_bb0520) 2014; 351
Kohrer (10.1016/j.bbagen.2017.03.012_bb0145) 2001; 98
Louie (10.1016/j.bbagen.2017.03.012_bb0470) 1985; 24
Ryu (10.1016/j.bbagen.2017.03.012_bb0100) 2006; 3
Wang (10.1016/j.bbagen.2017.03.012_bb0200) 2008; 130
Esvelt (10.1016/j.bbagen.2017.03.012_bb0675) 2011; 472
Hancock (10.1016/j.bbagen.2017.03.012_bb0205) 2010; 132
Soma (10.1016/j.bbagen.2017.03.012_bb0270) 1998; 26
Drabkin (10.1016/j.bbagen.2017.03.012_bb0140) 1996; 16
Wu (10.1016/j.bbagen.2017.03.012_bb0260) 2004; 126
Doi (10.1016/j.bbagen.2017.03.012_bb0460) 2007; 129
Hughes (10.1016/j.bbagen.2017.03.012_bb0295) 2010; 38
Ling (10.1016/j.bbagen.2017.03.012_bb0050) 2009; 63
Himeno (10.1016/j.bbagen.2017.03.012_bb0240) 1990; 18
Gan (10.1016/j.bbagen.2017.03.012_bb0455) 2016
Novoa (10.1016/j.bbagen.2017.03.012_bb0340) 2015; 290
Hoesl (10.1016/j.bbagen.2017.03.012_bb0010) 2012; 23
Hirsh (10.1016/j.bbagen.2017.03.012_bb0655) 1970; 228
LaRiviere (10.1016/j.bbagen.2017.03.012_bb0370) 2001; 294
Dale (10.1016/j.bbagen.2017.03.012_bb0055) 2005; 30
Maraia (10.1016/j.bbagen.2017.03.012_bb0030) 2011; 2
Maranhao (10.1016/j.bbagen.2017.03.012_bb0615) 2016
Park (10.1016/j.bbagen.2017.03.012_bb0450) 2011; 333
Orioli (10.1016/j.bbagen.2017.03.012_bb0120) 2012; 493
Zhang (10.1016/j.bbagen.2017.03.012_bb0285) 2004; 101
Naganuma (10.1016/j.bbagen.2017.03.012_bb0235) 2014; 510
Nissen (10.1016/j.bbagen.2017.03.012_bb0380) 1999; 7
Ogle (10.1016/j.bbagen.2017.03.012_bb0060) 2005; 74
Cantara (10.1016/j.bbagen.2017.03.012_bb0530) 2013; 110
Schrader (10.1016/j.bbagen.2017.03.012_bb0385) 2009; 386
Dewe (10.1016/j.bbagen.2017.03.012_bb0215) 2012; 18
Richardson (10.1016/j.bbagen.2017.03.012_bb0360) 2016; 55
Rodriguez-Hernandez (10.1016/j.bbagen.2017.03.012_bb0555) 2011; 19
McClain (10.1016/j.bbagen.2017.03.012_bb0230) 1988; 240
Youngman (10.1016/j.bbagen.2017.03.012_bb0625) 2007; 28
Rauch (10.1016/j.bbagen.2017.03.012_bb0560) 2016; 55
Machnicka (10.1016/j.bbagen.2017.03.012_bb0590) 2014; 11
Fan (10.1016/j.bbagen.2017.03.012_bb0415) 2015
Rogerson (10.1016/j.bbagen.2017.03.012_bb0600) 2015; 11
Leinfelder (10.1016/j.bbagen.2017.03.012_bb0620) 1988; 331
Mukai (10.1016/j.bbagen.2017.03.012_bb0165) 2010; 19
Biddle (10.1016/j.bbagen.2017.03.012_bb0580) 2016; 44
Johnson (10.1016/j.bbagen.2017.03.012_bb0640) 2011; 7
Zhang (10.1016/j.bbagen.2017.03.012_bb0440) 2007; 129
Beier (10.1016/j.bbagen.2017.03.012_bb0545) 1984; 3
Chatterjee (10.1016/j.bbagen.2017.03.012_bb0290) 2013; 52
Xu (10.1016/j.bbagen.2017.03.012_bb0280) 2001; 29
Giegé (10.1016/j.bbagen.2017.03.012_bb0035) 2014
Hohn (10.1016/j.bbagen.2017.03.012_bb0605) 2006; 103
Yamada (10.1016/j.bbagen.2017.03.012_bb0500) 2005; 1728
Wang (10.1016/j.bbagen.2017.03.012_bb0155) 2007; 10
Yesland (10.1016/j.bbagen.2017.03.012_bb0275) 1993; 268
Asahara (10.1016/j.bbagen.2017.03.012_bb0265) 1993; 231
Rodnina (10.1016/j.bbagen.2017.03.012_bb0475) 2012; 86
Ibba (10.1016/j.bbagen.2017.03.012_bb0040) 2000; 69
Reynolds (10.1016/j.bbagen.2017.03.012_bb0045) 2010; 8
Gustilo (10.1016/j.bbagen.2017.03.012_bb0570) 2008; 11
Sakamoto (10.1016/j.bbagen.2017.03.012_bb0150) 2002; 30
Ieong (10.1016/j.bbagen.2017.03.012_bb0410) 2012; 134
Dumas (10.1016/j.bbagen.2017.03.012_bb0005) 2015; 6
Biddle (10.1016/j.bbagen.2017.03.012_bb0575) 2015; 54
Yamada (10.1016/j.bbagen.2017.03.012_bb0495) 2003; 1626
Stortchevoi (10.1016/j.bbagen.2017.03.012_bb0390) 2003; 278
Kiga (10.1016/j.bbagen.2017.03.012_bb0350) 2002; 99
Cload (10.1016/j.bbagen.2017.03.012_bb0435) 1996; 3
Walker (10.1016/j.bbagen.2017.03.012_bb0095) 2006; 41
Mukai (10.1016/j.bbagen.2017.03.012_bb0635) 2010; 38
Oki (10.1016/j.bbagen.2017.03.012_bb0345) 2008; 105
Herring (10.1016/j.bbagen.2017.03.012_bb0305) 2007; 35
Jakubowski (10.1016/j.bbagen.2017.03.012_bb0365) 1988; 133
Dennis (10.1016/j.bbagen.2017.03.012_bb0395) 1974; 84
Roy (10.1016/j.bbagen.2017.03.012_bb0665) 2015; 112
Mittelstaet (10.1016/j.bbagen.2017.03.012_bb0465) 2013; 135
Chin (10.1016/j.bbagen.2017.03.012_bb0255) 2003; 301
Abelson (10.1016/j.bbagen.2017.03.012_bb0130) 1998; 273
Nissen (10.1016/j.bbagen.2017.03.012_bb0375) 1995; 270
Rogalski (10.1016/j.bbagen.2017.03.012_bb0510) 2008; 15
Wang (10.1016/j.bbagen.2017.03.012_bb0245) 2000; 122
Bershtein (10.1016/j.bbagen.2017.03.012_bb0670) 2008; 12
Hecht (10.1016/j.bbagen.2017.03.012_bb0425) 1978; 253
Schiffer (10.1016/j.bbagen.2017.03.012_bb0125) 2002; 21
Parrish (10.1016/j.bbagen.2017.03.012_bb0170) 2012; 7
Zhang (10.1016/j.bbagen.2017.03.012_bb0610) 2008; 15
Wang (10.1016/j.bbagen.2017.03.012_bb0015) 2001; 292
Ito (10.1016/j.bbagen.2017.03.012_bb0480) 2014; 42
Hauenstein (10.1016/j.bbagen.2017.03.012_bb0565) 2008; 283
Pirman (10.1016/j.bbagen.2017.03.012_bb0105) 2015; 6
Nozawa (10.1016/j.bbagen.2017.03.012_bb0310) 2009; 457
Aerni (10.1016/j.bbagen.2017.03.012_bb0645) 2015; 43
Lajoie (10.1016/j.bbagen.2017.03.012_bb0025) 2016; 428
Suzuki (10.1016/j.bbagen.2017.03.012_bb0535) 2011; 286
Wolf (10.1016/j.bbagen.2017.03.012_bb0585) 2002; 21
Lagerkvist (10.1016/j.bbagen.2017.03.012_bb0505) 1978; 75
Christian (10.1016/j.bbagen.2017.03.012_bb0595) 2007; 373
Young (10.1016/j.bbagen.2017.03.012_bb0085) 2010; 395
George (10.1016/j.bbagen.2017.03.012_bb0650) 2016
Shao (10.1016/j.bbagen.2017.03.012_bb0210) 2015; 5
Ramaswamy (10.1016/j.bbagen.2017.03.012_bb0430) 2004; 126
Young (10.1016/j.bbagen.2017.03.012_bb0400) 1976; 160
Altman (10.1016/j.bbagen.2017.03.012_bb0075) 1975; 4
Hou (10.1016/j.bbagen.2017.03.012_bb0225) 1988
Crick (10.1016/j.bbagen.2017.03.012_bb0490) 1966; 19
Allison (10.1016/j.bbagen.2017.03.012_bb0115) 1983; 34
Hopper (10.1016/j.bbagen.2017.03.012_bb0135) 2010; 584
Ho (10.1016/j.bbagen.2017.03.012_bb0320) 2016; 5
Schmeing (10.1016/j.bbagen.2017.03.012_bb0660) 2011; 18
Giege (10.1016/j.bbagen.2017.03.012_bb0220) 1998; 26
Fredrik Pettersson (10.1016/j.bbagen.2017.03.012_bb0080) 2005; 351
Ieong (10.1016/j.bbagen.2017.03.012_bb0445) 2014; 20
Schrader (10.1016/j.bbagen.2017.03.012_bb0405) 2011; 108
Chen (10.1016/j.bbagen.2017.03.012_bb0190) 2007; 371
Wan (10.1016/j.bbagen.2017.03.012_bb0315) 2014; 1844
Beier (10.1016/j.bbagen.2017.03.012_bb0540) 2001; 29
Phizicky (10.1016/j.bbagen.2017.03.012_bb0065) 2010; 24
Steer (10.1016/j.bbagen.2017.03.012_bb0250) 1999; 274
21819153 - J Am Chem Soc. 2011 Sep 14;133(36):14196-9
24919148 - Nature. 2014 Jun 26;510(7506):507-11
8510145 - J Mol Biol. 1993 May 20;231(2):219-29
4917265 - Nature. 1970 Oct 3;228(5266):57
9742237 - Nucleic Acids Res. 1998 Oct 1;26(19):4374-81
24755590 - Nat Chem. 2014 May;6(5):393-403
27448410 - Nucleic Acids Res. 2016 Sep 30;44(17 ):8020-40
16595295 - Crit Rev Biochem Mol Biol. 2006 Mar-Apr;41(2):77-102
17560600 - J Mol Biol. 2007 Aug 3;371(1):112-22
27987323 - Biotechnol Bioeng. 2017 May;114(5):1074-1086
20925334 - J Am Chem Soc. 2010 Oct 27;132(42):14819-24
12097643 - Proc Natl Acad Sci U S A. 2002 Jul 23;99(15):9715-20
20702426 - Nucleic Acids Res. 2010 Dec;38(22):8188-95
21572561 - Wiley Interdiscip Rev RNA. 2011 May-Jun;2(3):362-75
8622693 - Mol Cell Biol. 1996 Mar;16(3):907-13
26544153 - ACS Synth Biol. 2016 Feb 19;5(2):163-71
19118381 - Nature. 2009 Feb 26;457(7233):1163-7
18471995 - Biochem Biophys Res Commun. 2008 Jul 11;371(4):818-22
15037065 - J Mol Biol. 2004 Mar 5;336(5):1011-21
21079633 - Nat Rev Microbiol. 2010 Dec;8(12):849-56
5969078 - J Mol Biol. 1966 Aug;19(2):548-55
15187228 - Proc Natl Acad Sci U S A. 2004 Jun 15;101(24):8882-7
12110595 - EMBO J. 2002 Jul 15;21(14):3841-51
17603477 - Nat Neurosci. 2007 Aug;10(8):1063-72
21712079 - Gene. 2012 Feb 10;493(2):185-94
18378185 - Curr Opin Microbiol. 2008 Apr;11(2):134-40
16785423 - Proc Natl Acad Sci U S A. 2006 Jun 27;103(26):9785-9
9000011 - Chem Biol. 1996 Dec;3(12):1033-8
21926996 - Nat Chem Biol. 2011 Sep 18;7(11):779-86
18559342 - J Biol Chem. 2008 Aug 8;283(32):21997-2006
18042450 - Mol Cell. 2007 Nov 30;28(4):533-43
16002088 - J Mol Biol. 2005 Aug 5;351(1):9-15
26890980 - Biochemistry. 2016 Mar 15;55(10):1541-53
2263446 - Nucleic Acids Res. 1990 Dec 11;18(23):6815-9
27096575 - FEBS Lett. 2016 May;590(10 ):1530-42
19379069 - Annu Rev Microbiol. 2009;63:61-78
21868676 - Science. 2011 Aug 26;333(6046):1151-4
9278503 - Science. 1997 Sep 5;277(5331):1453-62
12409460 - Nucleic Acids Res. 2002 Nov 1;30(21):4692-9
17868690 - J Mol Biol. 2007 Oct 26;373(3):623-32
16453524 - EMBO J. 1984 May;3(5):1091-6
15521721 - J Am Chem Soc. 2004 Nov 10;126(44):14306-7
21378964 - Nat Struct Mol Biol. 2011 Apr;18(4):432-6
26350500 - Nat Commun. 2015 Sep 09;6:8130
26030730 - Nat Chem Biol. 2015 Jul;11(7):496-503
22895820 - RNA. 2012 Oct;18(10):1886-96
19852970 - J Mol Biol. 2010 Jan 15;395(2):361-74
10966471 - Annu Rev Biochem. 2000;69:617-50
10585437 - J Biol Chem. 1999 Dec 10;274(50):35601-6
17958427 - J Am Chem Soc. 2007 Nov 21;129(46):14458-62
19931532 - FEBS Lett. 2010 Jan 21;584(2):310-7
27915288 - Nucleic Acids Res. 2016 Dec 1;44(21):10042-10050
27064538 - Biochemistry. 2016 May 3;55(17 ):2526-37
1090377 - Cell. 1975 Jan;4(1):21-9
22237016 - Curr Opin Biotechnol. 2012 Oct;23(5):751-7
19151083 - Nucleic Acids Res. 2009 Apr;37(5):1616-27
22554080 - ACS Chem Biol. 2012 Jul 20;7(7):1292-302
24185096 - Nat Biotechnol. 2014 Jan;32(1):97-101
2467143 - J Theor Biol. 1988 Aug 8;133(3):363-70
16554830 - Nat Methods. 2006 Apr;3(4):263-5
18193063 - Nat Struct Mol Biol. 2008 Feb;15(2):192-8
4879404 - Proc Natl Acad Sci U S A. 1968 Oct;61(2):768-74
23057558 - J Am Chem Soc. 2012 Oct 31;134(43):17955-62
11717406 - Proc Natl Acad Sci U S A. 2001 Dec 4;98(25):14310-5
26536053 - Biochemistry. 2015 Dec 22;54(50):7355-64
2963963 - Nature. 1988 Feb 25;331(6158):723-5
12837384 - Chem Biol. 2003 Jun;10(6):511-9
8756732 - Cell. 1996 Aug 9;86(3):503-12
12639964 - J Biol Chem. 2003 May 16;278(20):17672-9
11600701 - Nucleic Acids Res. 2001 Oct 15;29(20):4125-33
8416930 - J Biol Chem. 1993 Jan 5;268(1):217-20
26186264 - Curr Opin Chem Biol. 2015 Oct;28:83-90
20571084 - Nucleic Acids Res. 2010 Oct;38(19):6813-30
248056 - J Biol Chem. 1978 Jul 10;253(13):4517-20
20810645 - Genes Dev. 2010 Sep 1;24(17):1832-60
1690848 - Mol Cell Biol. 1990 Apr;10 (4):1633-41
26250114 - Nucleic Acids Res. 2015 Dec 15;43(22):e156
4618855 - J Mol Biol. 1974 Apr 15;84(3):407-22
27600875 - ACS Synth Biol. 2017 Jan 20;6(1):108-119
25724653 - J Biol Chem. 2015 Apr 17;290(16):10495-503
18284924 - Curr Opin Chem Biol. 2008 Apr;12(2):151-8
24433543 - FEMS Microbiol Lett. 2014 Feb;351(2):133-44
23554007 - Angew Chem Int Ed Engl. 2013 May 3;52(19):5106-9
24631543 - Biochim Biophys Acta. 2014 Jun;1844(6):1059-70
25378305 - Nucleic Acids Res. 2015 Jan;43(2):e8
2452483 - Science. 1988 May 6;240(4853):793-6
15952884 - Annu Rev Biochem. 2005;74:129-77
17267409 - Nucleic Acids Res. 2007;35(4):1270-8
20052681 - Protein Sci. 2010 Mar;19(3):440-8
26694948 - Biochemistry. 2016 Jan 26;55(3):618-28
6352054 - Cell. 1983 Sep;34(2):655-64
23781103 - Proc Natl Acad Sci U S A. 2013 Jul 2;110(27):10964-9
17110438 - Proc Natl Acad Sci U S A. 2006 Nov 28;103(48):18095-100
11588263 - Science. 2001 Oct 5;294(5540):165-8
9801296 - Nucleic Acids Res. 1998 Nov 15;26(22):5017-35
28553457 - Chem Sci. 2015 Jan 1;6(1):50-69
15833716 - Biochim Biophys Acta. 2005 May 1;1728(3):143-9
3910093 - Biochemistry. 1985 Nov 5;24(23):6433-9
26348789 - J Mol Biol. 2016 Feb 27;428(5 Pt B):1004-21
18425141 - Nat Struct Mol Biol. 2008 May;15(5):507-14
15366888 - J Am Chem Soc. 2004 Sep 22;126(37):11454-5
19856359 - Angew Chem Int Ed Engl. 2009;48(48):9148-51
17718568 - J Am Chem Soc. 2007 Sep 19;129(37):11316-7
7491491 - Science. 1995 Dec 1;270(5241):1464-72
16260144 - Trends Biochem Sci. 2005 Dec;30(12):659-65
3285220 - Nature. 1988 May 12;333(6169):140-5
18426210 - J Am Chem Soc. 2008 May 14;130(19):6066-7
21402928 - Proc Natl Acad Sci U S A. 2011 Mar 29;108(13):5215-20
21873425 - J Biol Chem. 2011 Oct 14;286(41):35494-8
23118484 - Nucleic Acids Res. 2013 Jan;41(Database issue):D262-7
273907 - Proc Natl Acad Sci U S A. 1978 Apr;75(4):1759-62
22243582 - Adv Protein Chem Struct Biol. 2012;86:95-128
26597962 - Sci Rep. 2015 Nov 24;5:17196
12697332 - Biochim Biophys Acta. 2003 Apr 15;1626(1-3):75-82
25796611 - FEMS Microbiol Rev. 2015 May;39(3):280-300
19452597 - J Mol Biol. 2009 Mar 13;386(5):1255-64
25611331 - RNA Biol. 2014;11(12):1619-29
10368282 - Structure. 1999 Feb 15;7(2):143-56
9582290 - J Biol Chem. 1998 May 22;273(21):12685-8
795428 - Biochem J. 1976 Nov 15;160(2):185-94
23852030 - Top Curr Chem. 2014;344:1-41
25733896 - Proc Natl Acad Sci U S A. 2015 Mar 10;112(10):3038-43
15322138 - J Biol Chem. 2004 Oct 8;279(41):42359-62
12920298 - Science. 2003 Aug 15;301(5635):964-7
25428348 - Nucleic Acids Res. 2014 Dec 16;42(22):14042-52
11313494 - Science. 2001 Apr 20;292(5516):498-500
18765802 - Proc Natl Acad Sci U S A. 2008 Sep 9;105(36):13298-303
12032089 - EMBO J. 2002 Jun 3;21(11):2769-77
21478873 - Nature. 2011 Apr 28;472(7344):499-503
24671767 - RNA. 2014 May;20(5):632-43
24079513 - J Am Chem Soc. 2013 Nov 13;135(45):17031-8
11726686 - Nucleic Acids Res. 2001 Dec 1;29(23):4767-82
21397189 - Structure. 2011 Mar 9;19(3):386-96
References_xml – volume: 74
  start-page: 129
  year: 2005
  end-page: 177
  ident: bb0060
  article-title: Structural insights into translational fidelity
  publication-title: Annu. Rev. Biochem.
– volume: 44
  start-page: 10042
  year: 2016
  end-page: 10050
  ident: bb0580
  article-title: Modification of orthogonal tRNAs: unexpected consequences for sense codon reassignment
  publication-title: Nucleic Acids Res.
– volume: 6
  start-page: 8130
  year: 2015
  ident: bb0105
  article-title: A flexible codon in genomically recoded
  publication-title: Nat. Commun.
– volume: 19
  start-page: 548
  year: 1966
  end-page: 555
  ident: bb0490
  article-title: Codon-anticodon pairing: the wobble hypothesis
  publication-title: J. Mol. Biol.
– volume: 7
  start-page: 1292
  year: 2012
  end-page: 1302
  ident: bb0170
  article-title: Expanding the genetic code of
  publication-title: ACS Chem. Biol.
– volume: 10
  start-page: 1633
  year: 1990
  end-page: 1641
  ident: bb0180
  article-title: A bacterial amber suppressor in
  publication-title: Mol. Cell. Biol.
– volume: 11
  start-page: 496
  year: 2015
  end-page: 503
  ident: bb0600
  article-title: Efficient genetic encoding of phosphoserine and its nonhydrolyzable analog
  publication-title: Nat. Chem. Biol.
– volume: 75
  start-page: 1759
  year: 1978
  end-page: 1762
  ident: bb0505
  article-title: “Two out of three”: an alternative method for codon reading
  publication-title: Proc. Natl. Acad. Sci. U. S. A.
– volume: 457
  start-page: 1163
  year: 2009
  end-page: 1167
  ident: bb0310
  article-title: Pyrrolysyl-tRNA synthetase–tRNA
  publication-title: Nature
– volume: 126
  start-page: 14306
  year: 2004
  end-page: 14307
  ident: bb0260
  article-title: A genetically encoded photocaged amino acid
  publication-title: J. Am. Chem. Soc.
– volume: 32
  start-page: 97
  year: 2014
  end-page: 101
  ident: bb0300
  article-title: Directed evolution of genetic parts and circuits by compartmentalized partnered replication
  publication-title: Nat. Biotechnol.
– volume: 253
  start-page: 4517
  year: 1978
  end-page: 4520
  ident: bb0425
  article-title: “Chemical aminoacylation” of tRNA's
  publication-title: J. Biol. Chem.
– volume: 371
  start-page: 112
  year: 2007
  end-page: 122
  ident: bb0190
  article-title: An improved system for the generation and analysis of mutant proteins containing unnatural amino acids in
  publication-title: J. Mol. Biol.
– volume: 52
  start-page: 5106
  year: 2013
  end-page: 5109
  ident: bb0290
  article-title: A tryptophanyl-tRNA synthetase/tRNA pair for unnatural amino acid mutagenesis in
  publication-title: Angew. Chem. Int. Ed.
– volume: 55
  start-page: 1541
  year: 2016
  end-page: 1553
  ident: bb0355
  article-title: Altering the enantioselectivity of tyrosyl-tRNA synthetase by insertion of a stereospecific editing domain
  publication-title: Biochemistry
– volume: 228
  start-page: 57
  year: 1970
  ident: bb0655
  article-title: Tryptophan tRNA of
  publication-title: Nature
– volume: 15
  start-page: 192
  year: 2008
  end-page: 198
  ident: bb0510
  article-title: Superwobbling facilitates translation with reduced tRNA sets
  publication-title: Nat. Struct. Mol. Biol.
– volume: 63
  start-page: 61
  year: 2009
  end-page: 78
  ident: bb0050
  article-title: Aminoacyl-tRNA synthesis and translational quality control
  publication-title: Annu. Rev. Microbiol.
– volume: 278
  start-page: 17672
  year: 2003
  end-page: 17679
  ident: bb0390
  article-title: Common location of determinants in initiator transfer RNAs for initiator-elongator discrimination in bacteria and in eukaryotes
  publication-title: J. Biol. Chem.
– volume: 373
  start-page: 623
  year: 2007
  end-page: 632
  ident: bb0595
  article-title: Distinct determinants of tRNA recognition by the TrmD and Trm5 methyl transferases
  publication-title: J. Mol. Biol.
– volume: 294
  start-page: 165
  year: 2001
  end-page: 168
  ident: bb0370
  article-title: Uniform binding of aminoacyl-tRNAs to elongation factor Tu by thermodynamic compensation
  publication-title: Science
– volume: 292
  start-page: 498
  year: 2001
  end-page: 500
  ident: bb0015
  article-title: Expanding the genetic code of
  publication-title: Science
– volume: 351
  start-page: 9
  year: 2005
  end-page: 15
  ident: bb0080
  article-title: The length of the 5′ leader of
  publication-title: J. Mol. Biol.
– volume: 133
  start-page: 14196
  year: 2011
  end-page: 14199
  ident: bb0175
  article-title: Expanding the genetic code of an animal
  publication-title: J. Am. Chem. Soc.
– volume: 55
  start-page: 618
  year: 2016
  end-page: 628
  ident: bb0560
  article-title: Improved incorporation of noncanonical amino acids by an engineered tRNA
  publication-title: Biochemistry
– volume: 5
  start-page: 17196
  year: 2015
  ident: bb0210
  article-title: Site specific genetic incorporation of azidophenylalanine in
  publication-title: Sci. Rep.
– volume: 371
  start-page: 818
  year: 2008
  end-page: 822
  ident: bb0160
  article-title: Adding
  publication-title: Biochem. Biophys. Res. Commun.
– volume: 11
  start-page: 134
  year: 2008
  end-page: 140
  ident: bb0570
  article-title: tRNA's modifications bring order to gene expression
  publication-title: Curr. Opin. Microbiol.
– volume: 428
  start-page: 1004
  year: 2016
  end-page: 1021
  ident: bb0025
  article-title: Overcoming challenges in engineering the genetic code
  publication-title: J. Mol. Biol.
– volume: 98
  start-page: 14310
  year: 2001
  end-page: 14315
  ident: bb0145
  article-title: Import of amber and ochre suppressor tRNAs into mammalian cells: a general approach to site-specific insertion of amino acid analogues into proteins
  publication-title: Proc. Natl. Acad. Sci. U. S. A.
– volume: 279
  start-page: 42359
  year: 2004
  end-page: 42362
  ident: bb0335
  article-title: Trans-editing of Cys-tRNA Pro by
  publication-title: J. Biol. Chem.
– year: 2014
  ident: bb0035
  article-title: Transfer RNA recognition and aminoacylation by synthetases
  publication-title: eLS
– volume: 38
  start-page: 6813
  year: 2010
  end-page: 6830
  ident: bb0295
  article-title: Rational design of an orthogonal tryptophanyl nonsense suppressor tRNA
  publication-title: Nucleic Acids Res.
– volume: 19
  start-page: 386
  year: 2011
  end-page: 396
  ident: bb0555
  article-title: Heat maps for intramolecular communication in an RNP enzyme encoding glutamine
  publication-title: Structure
– year: 2016
  ident: bb0650
  article-title: Generation of phospho-ubiquitin variants by orthogonal translation reveals codon skipping
  publication-title: FEBS Lett.
– volume: 21
  start-page: 3841
  year: 2002
  end-page: 3851
  ident: bb0585
  article-title: tadA, an essential tRNA-specific adenosine deaminase from
  publication-title: EMBO J.
– volume: 34
  start-page: 655
  year: 1983
  end-page: 664
  ident: bb0115
  article-title: The promoter sequence of a yeast tRNA
  publication-title: Cell
– volume: 10
  start-page: 511
  year: 2003
  end-page: 519
  ident: bb0185
  article-title: Progress toward an expanded eukaryotic genetic code
  publication-title: Chem. Biol.
– volume: 15
  start-page: 507
  year: 2008
  end-page: 514
  ident: bb0610
  article-title: Aminoacylation of tRNA with phosphoserine for synthesis of cysteinyl-tRNA
  publication-title: Nat. Struct. Mol. Biol.
– volume: 21
  start-page: 2769
  year: 2002
  end-page: 2777
  ident: bb0125
  article-title: Assigning a function to a conserved group of proteins: the tRNA 3′-processing enzymes
  publication-title: EMBO J.
– year: 2016
  ident: bb0615
  article-title: Evolving orthogonal suppressor tRNAs to incorporate modified amino acids
  publication-title: ACS Synth. Biol.
– volume: 20
  start-page: 632
  year: 2014
  end-page: 643
  ident: bb0445
  article-title: A tRNA body with high affinity for EF-Tu hastens ribosomal incorporation of unnatural amino acids
  publication-title: RNA
– volume: 18
  start-page: 1886
  year: 2012
  end-page: 1896
  ident: bb0215
  article-title: The yeast rapid tRNA decay pathway competes with elongation factor 1A for substrate tRNAs and acts on tRNAs lacking one or more of several modifications
  publication-title: RNA
– volume: 86
  start-page: 95
  year: 2012
  end-page: 128
  ident: bb0475
  article-title: Quality control of mRNA decoding on the bacterial ribosome
  publication-title: Adv. Protein Chem. Struct. Biol.
– volume: 130
  start-page: 6066
  year: 2008
  end-page: 6067
  ident: bb0200
  article-title: New methods enabling efficient incorporation of unnatural amino acids in yeast
  publication-title: J. Am. Chem. Soc.
– volume: 29
  start-page: 4767
  year: 2001
  end-page: 4782
  ident: bb0540
  article-title: Misreading of termination codons in eukaryotes by natural nonsense suppressor tRNAs
  publication-title: Nucleic Acids Res.
– volume: 19
  start-page: 440
  year: 2010
  end-page: 448
  ident: bb0165
  article-title: Genetic encoding of non-natural amino acids in
  publication-title: Protein Sci.
– volume: 101
  start-page: 8882
  year: 2004
  end-page: 8887
  ident: bb0285
  article-title: Selective incorporation of 5-hydroxytryptophan into proteins in mammalian cells
  publication-title: Proc. Natl. Acad. Sci. U. S. A.
– volume: 336
  start-page: 1011
  year: 2004
  end-page: 1021
  ident: bb0485
  article-title: Interaction of helix D of elongation factor Tu with helices 4 and 5 of protein L7/12 on the ribosome
  publication-title: J. Mol. Biol.
– volume: 270
  start-page: 1464
  year: 1995
  end-page: 1472
  ident: bb0375
  article-title: Crystal-structure of the ternary complex of Phe-Trna
  publication-title: Science
– volume: 69
  start-page: 617
  year: 2000
  end-page: 650
  ident: bb0040
  article-title: Aminoacyl-tRNA synthesis
  publication-title: Annu. Rev. Biochem.
– volume: 6
  start-page: 50
  year: 2015
  end-page: 69
  ident: bb0005
  article-title: Designing logical codon reassignment – expanding the chemistry in biology
  publication-title: Chem. Sci.
– volume: 240
  start-page: 793
  year: 1988
  end-page: 797
  ident: bb0230
  article-title: Changing the identity of a tRNA by introducing a GU wobble pair near the 3′ acceptor end
  publication-title: Science
– volume: 12
  start-page: 151
  year: 2008
  end-page: 158
  ident: bb0670
  article-title: Advances in laboratory evolution of enzymes
  publication-title: Curr. Opin. Chem. Biol.
– volume: 231
  start-page: 219
  year: 1993
  end-page: 229
  ident: bb0265
  article-title: Recognition nucleotides of
  publication-title: J. Mol. Biol.
– volume: 129
  start-page: 14458
  year: 2007
  end-page: 14462
  ident: bb0460
  article-title: Elongation factor Tu mutants expand amino acid tolerance of protein biosynthesis system
  publication-title: J. Am. Chem. Soc.
– volume: 38
  start-page: 8188
  year: 2010
  end-page: 8195
  ident: bb0635
  article-title: Codon reassignment in the
  publication-title: Nucleic Acids Res.
– volume: 268
  start-page: 217
  year: 1993
  end-page: 220
  ident: bb0275
  article-title: Identity of
  publication-title: J. Biol. Chem.
– volume: 8
  start-page: 849
  year: 2010
  end-page: 856
  ident: bb0045
  article-title: Cellular mechanisms that control mistranslation
  publication-title: Nat. Rev. Microbiol.
– volume: 273
  start-page: 12685
  year: 1998
  end-page: 12688
  ident: bb0130
  article-title: tRNA splicing
  publication-title: J. Biol. Chem.
– volume: 42
  start-page: 14042
  year: 2014
  end-page: 14052
  ident: bb0480
  article-title: Molecular insights into the interaction of the ribosomal stalk protein with elongation factor 1a
  publication-title: Nucleic Acids Res.
– volume: 30
  start-page: 659
  year: 2005
  end-page: 665
  ident: bb0055
  article-title: Amino acid specificity in translation
  publication-title: Trends Biochem. Sci.
– volume: 103
  start-page: 18095
  year: 2006
  end-page: 18100
  ident: bb0605
  article-title: Emergence of the universal genetic code imprinted in an RNA record
  publication-title: Proc. Natl. Acad. Sci. U. S. A.
– volume: 26
  start-page: 5017
  year: 1998
  end-page: 5035
  ident: bb0220
  article-title: Universal rules and idiosyncratic features in tRNA identity
  publication-title: Nucleic Acids Res.
– volume: 99
  start-page: 9715
  year: 2002
  end-page: 9720
  ident: bb0350
  article-title: An engineered
  publication-title: Proc. Natl. Acad. Sci. U. S. A.
– volume: 134
  start-page: 17955
  year: 2012
  end-page: 17962
  ident: bb0410
  article-title: Inefficient delivery but fast peptide bond formation of unnatural
  publication-title: J. Am. Chem. Soc.
– volume: 493
  start-page: 185
  year: 2012
  end-page: 194
  ident: bb0120
  article-title: RNA polymerase III transcription control elements: themes and variations
  publication-title: Gene
– volume: 283
  start-page: 21997
  year: 2008
  end-page: 22006
  ident: bb0565
  article-title: The homotetrameric phosphoseryl-tRNA synthetase from
  publication-title: J. Biol. Chem.
– year: 2015
  ident: bb0415
  article-title: Rationally evolving tRNA
  publication-title: Nucleic Acids Res.
– volume: 3
  start-page: 263
  year: 2006
  end-page: 265
  ident: bb0100
  article-title: Efficient incorporation of unnatural amino acids into proteins in
  publication-title: Nat. Methods
– volume: 24
  start-page: 6433
  year: 1985
  end-page: 6439
  ident: bb0470
  article-title: Kinetic studies of
  publication-title: Biochemistry
– volume: 10
  start-page: 1063
  year: 2007
  end-page: 1072
  ident: bb0155
  article-title: Genetically encoding unnatural amino acids for cellular and neuronal studies
  publication-title: Nat. Neurosci.
– volume: 344
  start-page: 1
  year: 2014
  end-page: 41
  ident: bb0330
  article-title: Synthetic and editing mechanisms of aminoacyl-tRNA synthetases
  publication-title: Top. Curr. Chem.
– volume: 290
  start-page: 10495
  year: 2015
  end-page: 10503
  ident: bb0340
  article-title: Ancestral AlaX editing enzymes for control of genetic code fidelity are not tRNA-specific
  publication-title: J. Biol. Chem.
– volume: 29
  start-page: 4125
  year: 2001
  end-page: 4133
  ident: bb0280
  article-title: Species-specific differences in the operational RNA code for aminoacylation of tRNA
  publication-title: Nucleic Acids Res.
– volume: 1626
  start-page: 75
  year: 2003
  end-page: 82
  ident: bb0495
  article-title: tRNA
  publication-title: Biochim. Biophys. Acta
– volume: 2
  start-page: 362
  year: 2011
  end-page: 375
  ident: bb0030
  article-title: 3′ processing of eukaryotic precursor tRNAs
  publication-title: Wiley Interdiscip. Rev. RNA
– volume: 274
  start-page: 35601
  year: 1999
  end-page: 35606
  ident: bb0250
  article-title: Major anticodon-binding region missing from an archaebacterial tRNA synthetase
  publication-title: J. Biol. Chem.
– volume: 129
  start-page: 11316
  year: 2007
  end-page: 11317
  ident: bb0440
  article-title: Specificity of translation for N-alkyl amino acids
  publication-title: J. Am. Chem. Soc.
– volume: 286
  start-page: 35494
  year: 2011
  end-page: 35498
  ident: bb0535
  article-title: Taurine-containing uridine modifications in tRNA anticodons are required to decipher non-universal genetic codes in ascidian mitochondria
  publication-title: J. Biol. Chem.
– volume: 3
  start-page: 1033
  year: 1996
  end-page: 1038
  ident: bb0435
  article-title: Development of improved tRNAs for
  publication-title: Chem. Biol.
– volume: 3
  start-page: 1091
  year: 1984
  end-page: 1096
  ident: bb0545
  article-title: The molecular basis for the differential translation of TMV RNA in tobacco protoplasts and wheat germ extracts
  publication-title: EMBO J.
– volume: 277
  start-page: 1453
  year: 1997
  end-page: 1462
  ident: bb0070
  article-title: The complete genome sequence of
  publication-title: Science
– volume: 30
  start-page: 4692
  year: 2002
  end-page: 4699
  ident: bb0150
  article-title: Site-specific incorporation of an unnatural amino acid into proteins in mammalian cells
  publication-title: Nucleic Acids Res.
– volume: 112
  start-page: 3038
  year: 2015
  end-page: 3043
  ident: bb0665
  article-title: Nonsense suppression by near-cognate tRNAs employs alternative base pairing at codon positions 1 and 3
  publication-title: Proc. Natl. Acad. Sci. U. S. A.
– volume: 5
  start-page: 163
  year: 2016
  end-page: 171
  ident: bb0320
  article-title: Efficient reassignment of a frequent serine codon in wild-type
  publication-title: ACS Synth. Biol.
– volume: 126
  start-page: 11454
  year: 2004
  end-page: 11455
  ident: bb0430
  article-title: Designer ribozymes: programming the tRNA specificity into flexizyme
  publication-title: J. Am. Chem. Soc.
– volume: 135
  start-page: 17031
  year: 2013
  end-page: 17038
  ident: bb0465
  article-title: A kinetic safety gate controlling the delivery of unnatural amino acids to the ribosome
  publication-title: J. Am. Chem. Soc.
– volume: 133
  start-page: 363
  year: 1988
  end-page: 370
  ident: bb0365
  article-title: Negative correlation between the abundance of
  publication-title: J. Theor. Biol.
– volume: 108
  start-page: 5215
  year: 2011
  end-page: 5220
  ident: bb0405
  article-title: Tuning the affinity of aminoacyl-tRNA to elongation factor Tu for optimal decoding
  publication-title: Proc. Natl. Acad. Sci. U. S. A.
– volume: 510
  start-page: 507
  year: 2014
  end-page: 511
  ident: bb0235
  article-title: The selective tRNA aminoacylation mechanism based on a single G·U pair
  publication-title: Nature
– volume: 105
  start-page: 13298
  year: 2008
  end-page: 13303
  ident: bb0345
  article-title: Transplantation of a tyrosine editing domain into a tyrosyl-tRNA synthetase variant enhances its specificity for a tyrosine analog
  publication-title: Proc. Natl. Acad. Sci. U. S. A.
– volume: 395
  start-page: 361
  year: 2010
  end-page: 374
  ident: bb0085
  article-title: An enhanced system for unnatural amino acid mutagenesis in
  publication-title: J. Mol. Biol.
– volume: 301
  start-page: 964
  year: 2003
  end-page: 967
  ident: bb0255
  article-title: An expanded eukaryotic genetic code
  publication-title: Science
– volume: 61
  start-page: 768
  year: 1968
  end-page: 774
  ident: bb0630
  article-title: Release factors differing in specificity for terminator codons
  publication-title: Proc. Natl. Acad. Sci. U. S. A.
– volume: 84
  start-page: 407
  year: 1974
  end-page: 422
  ident: bb0395
  article-title: Differential rate of ribosomal protein synthesis in
  publication-title: J. Mol. Biol.
– volume: 386
  start-page: 1255
  year: 2009
  end-page: 1264
  ident: bb0385
  article-title: Understanding the sequence specificity of tRNA binding to elongation factor Tu using tRNA mutagenesis
  publication-title: J. Mol. Biol.
– volume: 35
  start-page: 1270
  year: 2007
  end-page: 1278
  ident: bb0305
  article-title: Recognition of pyrrolysine tRNA by the
  publication-title: Nucleic Acids Res.
– volume: 54
  start-page: 7355
  year: 2015
  end-page: 7364
  ident: bb0575
  article-title: Evaluating sense codon reassignment with a simple fluorescence screen
  publication-title: Biochemistry
– volume: 1728
  start-page: 143
  year: 2005
  end-page: 149
  ident: bb0500
  article-title: tRNA
  publication-title: Biochim. Biophys. Acta
– volume: 110
  start-page: 10964
  year: 2013
  end-page: 10969
  ident: bb0530
  article-title: Expanded use of sense codons is regulated by modified cytidines in tRNA
  publication-title: Proc. Natl. Acad. Sci. U. S. A.
– volume: 7
  start-page: 143
  year: 1999
  end-page: 156
  ident: bb0380
  article-title: The crystal structure of Cys-tRNA
  publication-title: Structure
– year: 1988
  ident: bb0225
  article-title: A Simple Structural Feature is a Major Determinant of the Identity of a Transfer RNA
– volume: 37
  start-page: 1616
  year: 2009
  end-page: 1627
  ident: bb0525
  article-title: Unconventional decoding of the AUA codon as methionine by mitochondrial tRNA
  publication-title: Nucleic Acids Res.
– volume: 18
  start-page: 6815
  year: 1990
  end-page: 6819
  ident: bb0240
  article-title: Conversion of aminoacylation specificity from tRNA
  publication-title: Nucleic Acids Res.
– volume: 6
  start-page: 393
  year: 2014
  end-page: 403
  ident: bb0325
  article-title: Optimized orthogonal translation of unnatural amino acids enables spontaneous protein double-labelling and FRET
  publication-title: Nat. Chem.
– volume: 39
  start-page: 280
  year: 2015
  end-page: 300
  ident: bb0090
  article-title: Bacterial transfer RNAs
  publication-title: FEMS Microbiol. Rev.
– volume: 28
  start-page: 533
  year: 2007
  end-page: 543
  ident: bb0625
  article-title: Stop codon recognition by release factors induces structural rearrangement of the ribosomal decoding center that is productive for peptide release
  publication-title: Mol. Cell
– volume: 1844
  start-page: 1059
  year: 2014
  end-page: 1070
  ident: bb0315
  article-title: Pyrrolysyl-tRNA synthetase: an ordinary enzyme but an outstanding genetic code expansion tool
  publication-title: Biochim. Biophys. Acta BBA Proteins Proteomics
– volume: 11
  start-page: 1619
  year: 2014
  end-page: 1629
  ident: bb0590
  article-title: Distribution and frequencies of post-transcriptional modifications in tRNAs
  publication-title: RNA Biol.
– volume: 41
  start-page: 77
  year: 2006
  end-page: 102
  ident: bb0095
  article-title: Ribonuclease P: the evolution of an ancient RNA enzyme
  publication-title: Crit. Rev. Biochem. Mol. Biol.
– volume: 55
  start-page: 2526
  year: 2016
  end-page: 2537
  ident: bb0360
  article-title: Hyperactive editing domain variants switch the stereospecificity of tyrosyl-tRNA synthetase
  publication-title: Biochemistry
– year: 2016
  ident: bb0455
  article-title: Translation system engineering in
  publication-title: Biotechnol. Bioeng.
– volume: 584
  start-page: 310
  year: 2010
  end-page: 317
  ident: bb0135
  article-title: Cellular dynamics of tRNAs and their genes
  publication-title: FEBS Lett.
– volume: 44
  start-page: 8020
  year: 2016
  end-page: 8040
  ident: bb0515
  article-title: An integrated, structure- and energy-based view of the genetic code
  publication-title: Nucleic Acids Res.
– volume: 28
  start-page: 83
  year: 2015
  end-page: 90
  ident: bb0020
  article-title: Repurposing the translation apparatus for synthetic biology
  publication-title: Curr. Opin. Chem. Biol.
– volume: 41
  start-page: D262
  year: 2013
  end-page: D267
  ident: bb0550
  article-title: MODOMICS: a database of RNA modification pathways—2013 update
  publication-title: Nucleic Acids Res.
– volume: 103
  start-page: 9785
  year: 2006
  end-page: 9789
  ident: bb0195
  article-title: A genetically encoded fluorescent amino acid
  publication-title: Proc. Natl. Acad. Sci. U. S. A.
– volume: 160
  start-page: 185
  year: 1976
  end-page: 194
  ident: bb0400
  article-title: Polypeptide-chain-elongation rate in
  publication-title: Biochem. J.
– volume: 122
  start-page: 5010
  year: 2000
  end-page: 5011
  ident: bb0245
  article-title: A new functional suppressor tRNA/aminoacyl–tRNA synthetase pair for the
  publication-title: J. Am. Chem. Soc.
– volume: 132
  start-page: 14819
  year: 2010
  end-page: 14824
  ident: bb0205
  article-title: Expanding the genetic code of yeast for incorporation of diverse unnatural amino acids via a pyrrolysyl-tRNA synthetase/tRNA pair
  publication-title: J. Am. Chem. Soc.
– volume: 351
  start-page: 133
  year: 2014
  end-page: 144
  ident: bb0520
  article-title: Sense codon emancipation for proteome-wide incorporation of noncanonical amino acids: rare isoleucine codon AUA as a target for genetic code expansion
  publication-title: FEMS Microbiol. Lett.
– volume: 333
  start-page: 1151
  year: 2011
  end-page: 1154
  ident: bb0450
  article-title: Expanding the genetic code of
  publication-title: Science
– volume: 331
  start-page: 723
  year: 1988
  end-page: 725
  ident: bb0620
  article-title: Gene for a novel tRNA species that accepts
  publication-title: Nature
– volume: 7
  start-page: 779
  year: 2011
  end-page: 786
  ident: bb0640
  article-title: RF1 knockout allows ribosomal incorporation of unnatural amino acids at multiple sites
  publication-title: Nat. Chem. Biol.
– volume: 4
  start-page: 21
  year: 1975
  end-page: 29
  ident: bb0075
  article-title: Biosynthesis of transfer RNA in
  publication-title: Cell
– volume: 86
  start-page: 503
  year: 1996
  end-page: 512
  ident: bb0110
  article-title: Maturation pathways for
  publication-title: Cell
– volume: 24
  start-page: 1832
  year: 2010
  end-page: 1860
  ident: bb0065
  article-title: tRNA biology charges to the front
  publication-title: Genes Dev.
– volume: 472
  start-page: 499
  year: 2011
  end-page: 503
  ident: bb0675
  article-title: A system for the continuous directed evolution of biomolecules
  publication-title: Nature
– volume: 16
  start-page: 907
  year: 1996
  end-page: 913
  ident: bb0140
  article-title: Amber suppression in mammalian cells dependent upon expression of an
  publication-title: Mol. Cell. Biol.
– volume: 43
  year: 2015
  ident: bb0645
  article-title: Revealing the amino acid composition of proteins within an expanded genetic code
  publication-title: Nucleic Acids Res.
– volume: 23
  start-page: 751
  year: 2012
  end-page: 757
  ident: bb0010
  article-title: Recent advances in genetic code engineering in
  publication-title: Curr. Opin. Biotechnol.
– volume: 18
  start-page: 432
  year: 2011
  end-page: U461
  ident: bb0660
  article-title: How mutations in tRNA distant from the anticodon affect the fidelity of decoding
  publication-title: Nat. Struct. Mol. Biol.
– volume: 26
  start-page: 4374
  year: 1998
  end-page: 4381
  ident: bb0270
  article-title: Cross-species aminoacylation of tRNA with a long variable arm between
  publication-title: Nucleic Acids Res.
– volume: 48
  start-page: 9148
  year: 2009
  end-page: 9151
  ident: bb0420
  article-title: Evolution of amber suppressor tRNAs for efficient bacterial production of proteins containing nonnatural amino acids
  publication-title: Angew. Chem. Int. Ed. Eng.
– volume: 6
  start-page: 8130
  year: 2015
  ident: 10.1016/j.bbagen.2017.03.012_bb0105
  article-title: A flexible codon in genomically recoded Escherichia coli permits programmable protein phosphorylation
  publication-title: Nat. Commun.
  doi: 10.1038/ncomms9130
– volume: 273
  start-page: 12685
  year: 1998
  ident: 10.1016/j.bbagen.2017.03.012_bb0130
  article-title: tRNA splicing
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.273.21.12685
– volume: 457
  start-page: 1163
  year: 2009
  ident: 10.1016/j.bbagen.2017.03.012_bb0310
  article-title: Pyrrolysyl-tRNA synthetase–tRNAPyl structure reveals the molecular basis of orthogonality
  publication-title: Nature
  doi: 10.1038/nature07611
– volume: 24
  start-page: 6433
  year: 1985
  ident: 10.1016/j.bbagen.2017.03.012_bb0470
  article-title: Kinetic studies of Escherichia coli elongation factor Tu-guanosine 5′-triphosphate-aminoacyl-tRNA complexes
  publication-title: Biochemistry
  doi: 10.1021/bi00344a019
– volume: 21
  start-page: 2769
  year: 2002
  ident: 10.1016/j.bbagen.2017.03.012_bb0125
  article-title: Assigning a function to a conserved group of proteins: the tRNA 3′-processing enzymes
  publication-title: EMBO J.
  doi: 10.1093/emboj/21.11.2769
– volume: 6
  start-page: 393
  year: 2014
  ident: 10.1016/j.bbagen.2017.03.012_bb0325
  article-title: Optimized orthogonal translation of unnatural amino acids enables spontaneous protein double-labelling and FRET
  publication-title: Nat. Chem.
  doi: 10.1038/nchem.1919
– volume: 4
  start-page: 21
  year: 1975
  ident: 10.1016/j.bbagen.2017.03.012_bb0075
  article-title: Biosynthesis of transfer RNA in Escherichia coli
  publication-title: Cell
  doi: 10.1016/0092-8674(75)90129-4
– volume: 3
  start-page: 1091
  year: 1984
  ident: 10.1016/j.bbagen.2017.03.012_bb0545
  article-title: The molecular basis for the differential translation of TMV RNA in tobacco protoplasts and wheat germ extracts
  publication-title: EMBO J.
  doi: 10.1002/j.1460-2075.1984.tb01934.x
– volume: 86
  start-page: 503
  year: 1996
  ident: 10.1016/j.bbagen.2017.03.012_bb0110
  article-title: Maturation pathways for E. coli tRNA precursors: a random multienzyme process in vivo
  publication-title: Cell
  doi: 10.1016/S0092-8674(00)80123-3
– volume: 52
  start-page: 5106
  year: 2013
  ident: 10.1016/j.bbagen.2017.03.012_bb0290
  article-title: A tryptophanyl-tRNA synthetase/tRNA pair for unnatural amino acid mutagenesis in E. coli
  publication-title: Angew. Chem. Int. Ed.
  doi: 10.1002/anie.201301094
– volume: 19
  start-page: 548
  year: 1966
  ident: 10.1016/j.bbagen.2017.03.012_bb0490
  article-title: Codon-anticodon pairing: the wobble hypothesis
  publication-title: J. Mol. Biol.
  doi: 10.1016/S0022-2836(66)80022-0
– volume: 112
  start-page: 3038
  year: 2015
  ident: 10.1016/j.bbagen.2017.03.012_bb0665
  article-title: Nonsense suppression by near-cognate tRNAs employs alternative base pairing at codon positions 1 and 3
  publication-title: Proc. Natl. Acad. Sci. U. S. A.
  doi: 10.1073/pnas.1424127112
– volume: 63
  start-page: 61
  year: 2009
  ident: 10.1016/j.bbagen.2017.03.012_bb0050
  article-title: Aminoacyl-tRNA synthesis and translational quality control
  publication-title: Annu. Rev. Microbiol.
  doi: 10.1146/annurev.micro.091208.073210
– volume: 160
  start-page: 185
  year: 1976
  ident: 10.1016/j.bbagen.2017.03.012_bb0400
  article-title: Polypeptide-chain-elongation rate in Escherichia coli B/r as a function of growth rate
  publication-title: Biochem. J.
  doi: 10.1042/bj1600185
– volume: 44
  start-page: 10042
  year: 2016
  ident: 10.1016/j.bbagen.2017.03.012_bb0580
  article-title: Modification of orthogonal tRNAs: unexpected consequences for sense codon reassignment
  publication-title: Nucleic Acids Res.
– volume: 48
  start-page: 9148
  year: 2009
  ident: 10.1016/j.bbagen.2017.03.012_bb0420
  article-title: Evolution of amber suppressor tRNAs for efficient bacterial production of proteins containing nonnatural amino acids
  publication-title: Angew. Chem. Int. Ed. Eng.
  doi: 10.1002/anie.200904035
– volume: 11
  start-page: 134
  year: 2008
  ident: 10.1016/j.bbagen.2017.03.012_bb0570
  article-title: tRNA's modifications bring order to gene expression
  publication-title: Curr. Opin. Microbiol.
  doi: 10.1016/j.mib.2008.02.003
– volume: 126
  start-page: 14306
  year: 2004
  ident: 10.1016/j.bbagen.2017.03.012_bb0260
  article-title: A genetically encoded photocaged amino acid
  publication-title: J. Am. Chem. Soc.
  doi: 10.1021/ja040175z
– volume: 39
  start-page: 280
  year: 2015
  ident: 10.1016/j.bbagen.2017.03.012_bb0090
  article-title: Bacterial transfer RNAs
  publication-title: FEMS Microbiol. Rev.
  doi: 10.1093/femsre/fuv004
– year: 2016
  ident: 10.1016/j.bbagen.2017.03.012_bb0650
  article-title: Generation of phospho-ubiquitin variants by orthogonal translation reveals codon skipping
  publication-title: FEBS Lett.
  doi: 10.1002/1873-3468.12182
– volume: 228
  start-page: 57
  year: 1970
  ident: 10.1016/j.bbagen.2017.03.012_bb0655
  article-title: Tryptophan tRNA of Escherichia coli
  publication-title: Nature
  doi: 10.1038/228057a0
– volume: 129
  start-page: 14458
  year: 2007
  ident: 10.1016/j.bbagen.2017.03.012_bb0460
  article-title: Elongation factor Tu mutants expand amino acid tolerance of protein biosynthesis system
  publication-title: J. Am. Chem. Soc.
  doi: 10.1021/ja075557u
– volume: 41
  start-page: D262
  year: 2013
  ident: 10.1016/j.bbagen.2017.03.012_bb0550
  article-title: MODOMICS: a database of RNA modification pathways—2013 update
  publication-title: Nucleic Acids Res.
  doi: 10.1093/nar/gks1007
– volume: 286
  start-page: 35494
  year: 2011
  ident: 10.1016/j.bbagen.2017.03.012_bb0535
  article-title: Taurine-containing uridine modifications in tRNA anticodons are required to decipher non-universal genetic codes in ascidian mitochondria
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M111.279810
– volume: 373
  start-page: 623
  year: 2007
  ident: 10.1016/j.bbagen.2017.03.012_bb0595
  article-title: Distinct determinants of tRNA recognition by the TrmD and Trm5 methyl transferases
  publication-title: J. Mol. Biol.
  doi: 10.1016/j.jmb.2007.08.010
– volume: 11
  start-page: 496
  year: 2015
  ident: 10.1016/j.bbagen.2017.03.012_bb0600
  article-title: Efficient genetic encoding of phosphoserine and its nonhydrolyzable analog
  publication-title: Nat. Chem. Biol.
  doi: 10.1038/nchembio.1823
– volume: 99
  start-page: 9715
  year: 2002
  ident: 10.1016/j.bbagen.2017.03.012_bb0350
  article-title: An engineered Escherichia coli tyrosyl-tRNA synthetase for site-specific incorporation of an unnatural amino acid into proteins in eukaryotic translation and its application in a wheat germ cell-free system
  publication-title: Proc. Natl. Acad. Sci. U. S. A.
  doi: 10.1073/pnas.142220099
– volume: 18
  start-page: 6815
  year: 1990
  ident: 10.1016/j.bbagen.2017.03.012_bb0240
  article-title: Conversion of aminoacylation specificity from tRNATyr to tRNASer in vitro
  publication-title: Nucleic Acids Res.
  doi: 10.1093/nar/18.23.6815
– volume: 231
  start-page: 219
  year: 1993
  ident: 10.1016/j.bbagen.2017.03.012_bb0265
  article-title: Recognition nucleotides of Escherichia coli tRNALeu and its elements facilitating discrimination from tRNASer and tRNATyr
  publication-title: J. Mol. Biol.
  doi: 10.1006/jmbi.1993.1277
– volume: 5
  start-page: 163
  year: 2016
  ident: 10.1016/j.bbagen.2017.03.012_bb0320
  article-title: Efficient reassignment of a frequent serine codon in wild-type Escherichia coli
  publication-title: ACS Synth. Biol.
  doi: 10.1021/acssynbio.5b00197
– volume: 29
  start-page: 4125
  year: 2001
  ident: 10.1016/j.bbagen.2017.03.012_bb0280
  article-title: Species-specific differences in the operational RNA code for aminoacylation of tRNATrp
  publication-title: Nucleic Acids Res.
  doi: 10.1093/nar/29.20.4125
– volume: 103
  start-page: 18095
  year: 2006
  ident: 10.1016/j.bbagen.2017.03.012_bb0605
  article-title: Emergence of the universal genetic code imprinted in an RNA record
  publication-title: Proc. Natl. Acad. Sci. U. S. A.
  doi: 10.1073/pnas.0608762103
– volume: 386
  start-page: 1255
  year: 2009
  ident: 10.1016/j.bbagen.2017.03.012_bb0385
  article-title: Understanding the sequence specificity of tRNA binding to elongation factor Tu using tRNA mutagenesis
  publication-title: J. Mol. Biol.
  doi: 10.1016/j.jmb.2009.01.021
– volume: 6
  start-page: 50
  year: 2015
  ident: 10.1016/j.bbagen.2017.03.012_bb0005
  article-title: Designing logical codon reassignment – expanding the chemistry in biology
  publication-title: Chem. Sci.
  doi: 10.1039/C4SC01534G
– volume: 132
  start-page: 14819
  year: 2010
  ident: 10.1016/j.bbagen.2017.03.012_bb0205
  article-title: Expanding the genetic code of yeast for incorporation of diverse unnatural amino acids via a pyrrolysyl-tRNA synthetase/tRNA pair
  publication-title: J. Am. Chem. Soc.
  doi: 10.1021/ja104609m
– volume: 41
  start-page: 77
  year: 2006
  ident: 10.1016/j.bbagen.2017.03.012_bb0095
  article-title: Ribonuclease P: the evolution of an ancient RNA enzyme
  publication-title: Crit. Rev. Biochem. Mol. Biol.
  doi: 10.1080/10409230600602634
– volume: 98
  start-page: 14310
  year: 2001
  ident: 10.1016/j.bbagen.2017.03.012_bb0145
  article-title: Import of amber and ochre suppressor tRNAs into mammalian cells: a general approach to site-specific insertion of amino acid analogues into proteins
  publication-title: Proc. Natl. Acad. Sci. U. S. A.
  doi: 10.1073/pnas.251438898
– volume: 84
  start-page: 407
  year: 1974
  ident: 10.1016/j.bbagen.2017.03.012_bb0395
  article-title: Differential rate of ribosomal protein synthesis in Escherichia coli B/r
  publication-title: J. Mol. Biol.
  doi: 10.1016/0022-2836(74)90449-5
– volume: 135
  start-page: 17031
  year: 2013
  ident: 10.1016/j.bbagen.2017.03.012_bb0465
  article-title: A kinetic safety gate controlling the delivery of unnatural amino acids to the ribosome
  publication-title: J. Am. Chem. Soc.
  doi: 10.1021/ja407511q
– volume: 38
  start-page: 8188
  year: 2010
  ident: 10.1016/j.bbagen.2017.03.012_bb0635
  article-title: Codon reassignment in the Escherichia coli genetic code
  publication-title: Nucleic Acids Res.
  doi: 10.1093/nar/gkq707
– volume: 26
  start-page: 4374
  year: 1998
  ident: 10.1016/j.bbagen.2017.03.012_bb0270
  article-title: Cross-species aminoacylation of tRNA with a long variable arm between Escherichia coli and Saccharomyces cerevisiae
  publication-title: Nucleic Acids Res.
  doi: 10.1093/nar/26.19.4374
– volume: 336
  start-page: 1011
  year: 2004
  ident: 10.1016/j.bbagen.2017.03.012_bb0485
  article-title: Interaction of helix D of elongation factor Tu with helices 4 and 5 of protein L7/12 on the ribosome
  publication-title: J. Mol. Biol.
  doi: 10.1016/j.jmb.2003.12.080
– year: 2015
  ident: 10.1016/j.bbagen.2017.03.012_bb0415
  article-title: Rationally evolving tRNAPyl for efficient incorporation of noncanonical amino acids
  publication-title: Nucleic Acids Res.
  doi: 10.1093/nar/gkv800
– volume: 472
  start-page: 499
  year: 2011
  ident: 10.1016/j.bbagen.2017.03.012_bb0675
  article-title: A system for the continuous directed evolution of biomolecules
  publication-title: Nature
  doi: 10.1038/nature09929
– volume: 331
  start-page: 723
  year: 1988
  ident: 10.1016/j.bbagen.2017.03.012_bb0620
  article-title: Gene for a novel tRNA species that accepts l-serine and cotranslationally inserts selenocysteine
  publication-title: Nature
  doi: 10.1038/331723a0
– volume: 10
  start-page: 1063
  year: 2007
  ident: 10.1016/j.bbagen.2017.03.012_bb0155
  article-title: Genetically encoding unnatural amino acids for cellular and neuronal studies
  publication-title: Nat. Neurosci.
  doi: 10.1038/nn1932
– volume: 15
  start-page: 192
  year: 2008
  ident: 10.1016/j.bbagen.2017.03.012_bb0510
  article-title: Superwobbling facilitates translation with reduced tRNA sets
  publication-title: Nat. Struct. Mol. Biol.
  doi: 10.1038/nsmb.1370
– volume: 12
  start-page: 151
  year: 2008
  ident: 10.1016/j.bbagen.2017.03.012_bb0670
  article-title: Advances in laboratory evolution of enzymes
  publication-title: Curr. Opin. Chem. Biol.
  doi: 10.1016/j.cbpa.2008.01.027
– volume: 26
  start-page: 5017
  year: 1998
  ident: 10.1016/j.bbagen.2017.03.012_bb0220
  article-title: Universal rules and idiosyncratic features in tRNA identity
  publication-title: Nucleic Acids Res.
  doi: 10.1093/nar/26.22.5017
– volume: 101
  start-page: 8882
  year: 2004
  ident: 10.1016/j.bbagen.2017.03.012_bb0285
  article-title: Selective incorporation of 5-hydroxytryptophan into proteins in mammalian cells
  publication-title: Proc. Natl. Acad. Sci. U. S. A.
  doi: 10.1073/pnas.0307029101
– volume: 371
  start-page: 112
  year: 2007
  ident: 10.1016/j.bbagen.2017.03.012_bb0190
  article-title: An improved system for the generation and analysis of mutant proteins containing unnatural amino acids in Saccharomyces cerevisiae
  publication-title: J. Mol. Biol.
  doi: 10.1016/j.jmb.2007.05.017
– volume: 1626
  start-page: 75
  year: 2003
  ident: 10.1016/j.bbagen.2017.03.012_bb0495
  article-title: tRNA1Ser(G34) with the anticodon GGA can recognize not only UCC and UCU codons but also UCA and UCG codons
  publication-title: Biochim. Biophys. Acta
  doi: 10.1016/S0167-4781(03)00045-9
– volume: 8
  start-page: 849
  year: 2010
  ident: 10.1016/j.bbagen.2017.03.012_bb0045
  article-title: Cellular mechanisms that control mistranslation
  publication-title: Nat. Rev. Microbiol.
  doi: 10.1038/nrmicro2472
– volume: 134
  start-page: 17955
  year: 2012
  ident: 10.1016/j.bbagen.2017.03.012_bb0410
  article-title: Inefficient delivery but fast peptide bond formation of unnatural l-aminoacyl-tRNAs in translation
  publication-title: J. Am. Chem. Soc.
  doi: 10.1021/ja3063524
– volume: 2
  start-page: 362
  year: 2011
  ident: 10.1016/j.bbagen.2017.03.012_bb0030
  article-title: 3′ processing of eukaryotic precursor tRNAs
  publication-title: Wiley Interdiscip. Rev. RNA
  doi: 10.1002/wrna.64
– volume: 283
  start-page: 21997
  year: 2008
  ident: 10.1016/j.bbagen.2017.03.012_bb0565
  article-title: The homotetrameric phosphoseryl-tRNA synthetase from Methanosarcina mazei exhibits half-of-the-sites activity
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M801838200
– volume: 292
  start-page: 498
  year: 2001
  ident: 10.1016/j.bbagen.2017.03.012_bb0015
  article-title: Expanding the genetic code of Escherichia coli
  publication-title: Science
  doi: 10.1126/science.1060077
– volume: 30
  start-page: 4692
  year: 2002
  ident: 10.1016/j.bbagen.2017.03.012_bb0150
  article-title: Site-specific incorporation of an unnatural amino acid into proteins in mammalian cells
  publication-title: Nucleic Acids Res.
  doi: 10.1093/nar/gkf589
– volume: 333
  start-page: 1151
  year: 2011
  ident: 10.1016/j.bbagen.2017.03.012_bb0450
  article-title: Expanding the genetic code of Escherichia coli with phosphoserine
  publication-title: Science
  doi: 10.1126/science.1207203
– volume: 279
  start-page: 42359
  year: 2004
  ident: 10.1016/j.bbagen.2017.03.012_bb0335
  article-title: Trans-editing of Cys-tRNA Pro by Haemophilus influenzae YbaK protein
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.C400304200
– volume: 30
  start-page: 659
  year: 2005
  ident: 10.1016/j.bbagen.2017.03.012_bb0055
  article-title: Amino acid specificity in translation
  publication-title: Trends Biochem. Sci.
  doi: 10.1016/j.tibs.2005.10.006
– volume: 584
  start-page: 310
  year: 2010
  ident: 10.1016/j.bbagen.2017.03.012_bb0135
  article-title: Cellular dynamics of tRNAs and their genes
  publication-title: FEBS Lett.
  doi: 10.1016/j.febslet.2009.11.053
– volume: 18
  start-page: 1886
  year: 2012
  ident: 10.1016/j.bbagen.2017.03.012_bb0215
  article-title: The yeast rapid tRNA decay pathway competes with elongation factor 1A for substrate tRNAs and acts on tRNAs lacking one or more of several modifications
  publication-title: RNA
  doi: 10.1261/rna.033654.112
– volume: 126
  start-page: 11454
  year: 2004
  ident: 10.1016/j.bbagen.2017.03.012_bb0430
  article-title: Designer ribozymes: programming the tRNA specificity into flexizyme
  publication-title: J. Am. Chem. Soc.
  doi: 10.1021/ja046843y
– volume: 28
  start-page: 533
  year: 2007
  ident: 10.1016/j.bbagen.2017.03.012_bb0625
  article-title: Stop codon recognition by release factors induces structural rearrangement of the ribosomal decoding center that is productive for peptide release
  publication-title: Mol. Cell
  doi: 10.1016/j.molcel.2007.09.015
– volume: 55
  start-page: 1541
  year: 2016
  ident: 10.1016/j.bbagen.2017.03.012_bb0355
  article-title: Altering the enantioselectivity of tyrosyl-tRNA synthetase by insertion of a stereospecific editing domain
  publication-title: Biochemistry
  doi: 10.1021/acs.biochem.5b01167
– volume: 122
  start-page: 5010
  year: 2000
  ident: 10.1016/j.bbagen.2017.03.012_bb0245
  article-title: A new functional suppressor tRNA/aminoacyl–tRNA synthetase pair for the in vivo incorporation of unnatural amino acids into proteins
  publication-title: J. Am. Chem. Soc.
  doi: 10.1021/ja000595y
– volume: 28
  start-page: 83
  year: 2015
  ident: 10.1016/j.bbagen.2017.03.012_bb0020
  article-title: Repurposing the translation apparatus for synthetic biology
  publication-title: Curr. Opin. Chem. Biol.
  doi: 10.1016/j.cbpa.2015.06.008
– volume: 133
  start-page: 363
  year: 1988
  ident: 10.1016/j.bbagen.2017.03.012_bb0365
  article-title: Negative correlation between the abundance of Escherichia coli aminoacyl-tRNA families and their affinities for elongation factor Tu-GTP
  publication-title: J. Theor. Biol.
  doi: 10.1016/S0022-5193(88)80327-8
– volume: 74
  start-page: 129
  year: 2005
  ident: 10.1016/j.bbagen.2017.03.012_bb0060
  article-title: Structural insights into translational fidelity
  publication-title: Annu. Rev. Biochem.
  doi: 10.1146/annurev.biochem.74.061903.155440
– volume: 268
  start-page: 217
  year: 1993
  ident: 10.1016/j.bbagen.2017.03.012_bb0275
  article-title: Identity of Saccharomyces cerevisiae tRNATrp is not changed by an anticodon mutation that creates an amber suppressor
  publication-title: J. Biol. Chem.
  doi: 10.1016/S0021-9258(18)54137-5
– volume: 38
  start-page: 6813
  year: 2010
  ident: 10.1016/j.bbagen.2017.03.012_bb0295
  article-title: Rational design of an orthogonal tryptophanyl nonsense suppressor tRNA
  publication-title: Nucleic Acids Res.
  doi: 10.1093/nar/gkq521
– volume: 110
  start-page: 10964
  year: 2013
  ident: 10.1016/j.bbagen.2017.03.012_bb0530
  article-title: Expanded use of sense codons is regulated by modified cytidines in tRNA
  publication-title: Proc. Natl. Acad. Sci. U. S. A.
  doi: 10.1073/pnas.1222641110
– volume: 1844
  start-page: 1059
  year: 2014
  ident: 10.1016/j.bbagen.2017.03.012_bb0315
  article-title: Pyrrolysyl-tRNA synthetase: an ordinary enzyme but an outstanding genetic code expansion tool
  publication-title: Biochim. Biophys. Acta BBA Proteins Proteomics
  doi: 10.1016/j.bbapap.2014.03.002
– year: 2016
  ident: 10.1016/j.bbagen.2017.03.012_bb0615
  article-title: Evolving orthogonal suppressor tRNAs to incorporate modified amino acids
  publication-title: ACS Synth. Biol.
– volume: 21
  start-page: 3841
  year: 2002
  ident: 10.1016/j.bbagen.2017.03.012_bb0585
  article-title: tadA, an essential tRNA-specific adenosine deaminase from Escherichia coli
  publication-title: EMBO J.
  doi: 10.1093/emboj/cdf362
– volume: 7
  start-page: 779
  year: 2011
  ident: 10.1016/j.bbagen.2017.03.012_bb0640
  article-title: RF1 knockout allows ribosomal incorporation of unnatural amino acids at multiple sites
  publication-title: Nat. Chem. Biol.
  doi: 10.1038/nchembio.657
– year: 1988
  ident: 10.1016/j.bbagen.2017.03.012_bb0225
– volume: 34
  start-page: 655
  year: 1983
  ident: 10.1016/j.bbagen.2017.03.012_bb0115
  article-title: The promoter sequence of a yeast tRNATyr gene
  publication-title: Cell
  doi: 10.1016/0092-8674(83)90398-7
– volume: 75
  start-page: 1759
  year: 1978
  ident: 10.1016/j.bbagen.2017.03.012_bb0505
  article-title: “Two out of three”: an alternative method for codon reading
  publication-title: Proc. Natl. Acad. Sci. U. S. A.
  doi: 10.1073/pnas.75.4.1759
– volume: 371
  start-page: 818
  year: 2008
  ident: 10.1016/j.bbagen.2017.03.012_bb0160
  article-title: Adding l-lysine derivatives to the genetic code of mammalian cells with engineered pyrrolysyl-tRNA synthetases
  publication-title: Biochem. Biophys. Res. Commun.
  doi: 10.1016/j.bbrc.2008.04.164
– volume: 18
  start-page: 432
  year: 2011
  ident: 10.1016/j.bbagen.2017.03.012_bb0660
  article-title: How mutations in tRNA distant from the anticodon affect the fidelity of decoding
  publication-title: Nat. Struct. Mol. Biol.
  doi: 10.1038/nsmb.2003
– volume: 301
  start-page: 964
  year: 2003
  ident: 10.1016/j.bbagen.2017.03.012_bb0255
  article-title: An expanded eukaryotic genetic code
  publication-title: Science
  doi: 10.1126/science.1084772
– volume: 61
  start-page: 768
  year: 1968
  ident: 10.1016/j.bbagen.2017.03.012_bb0630
  article-title: Release factors differing in specificity for terminator codons
  publication-title: Proc. Natl. Acad. Sci. U. S. A.
  doi: 10.1073/pnas.61.2.768
– volume: 24
  start-page: 1832
  year: 2010
  ident: 10.1016/j.bbagen.2017.03.012_bb0065
  article-title: tRNA biology charges to the front
  publication-title: Genes Dev.
  doi: 10.1101/gad.1956510
– volume: 129
  start-page: 11316
  year: 2007
  ident: 10.1016/j.bbagen.2017.03.012_bb0440
  article-title: Specificity of translation for N-alkyl amino acids
  publication-title: J. Am. Chem. Soc.
  doi: 10.1021/ja073487l
– volume: 133
  start-page: 14196
  year: 2011
  ident: 10.1016/j.bbagen.2017.03.012_bb0175
  article-title: Expanding the genetic code of an animal
  publication-title: J. Am. Chem. Soc.
  doi: 10.1021/ja2054034
– volume: 344
  start-page: 1
  year: 2014
  ident: 10.1016/j.bbagen.2017.03.012_bb0330
  article-title: Synthetic and editing mechanisms of aminoacyl-tRNA synthetases
  publication-title: Top. Curr. Chem.
– volume: 395
  start-page: 361
  year: 2010
  ident: 10.1016/j.bbagen.2017.03.012_bb0085
  article-title: An enhanced system for unnatural amino acid mutagenesis in E. coli
  publication-title: J. Mol. Biol.
  doi: 10.1016/j.jmb.2009.10.030
– volume: 19
  start-page: 440
  year: 2010
  ident: 10.1016/j.bbagen.2017.03.012_bb0165
  article-title: Genetic encoding of non-natural amino acids in Drosophila melanogaster Schneider 2 cells
  publication-title: Protein Sci.
  doi: 10.1002/pro.322
– volume: 55
  start-page: 2526
  year: 2016
  ident: 10.1016/j.bbagen.2017.03.012_bb0360
  article-title: Hyperactive editing domain variants switch the stereospecificity of tyrosyl-tRNA synthetase
  publication-title: Biochemistry
  doi: 10.1021/acs.biochem.6b00157
– volume: 294
  start-page: 165
  year: 2001
  ident: 10.1016/j.bbagen.2017.03.012_bb0370
  article-title: Uniform binding of aminoacyl-tRNAs to elongation factor Tu by thermodynamic compensation
  publication-title: Science
  doi: 10.1126/science.1064242
– volume: 277
  start-page: 1453
  year: 1997
  ident: 10.1016/j.bbagen.2017.03.012_bb0070
  article-title: The complete genome sequence of Escherichia coli K-12
  publication-title: Science
  doi: 10.1126/science.277.5331.1453
– volume: 290
  start-page: 10495
  year: 2015
  ident: 10.1016/j.bbagen.2017.03.012_bb0340
  article-title: Ancestral AlaX editing enzymes for control of genetic code fidelity are not tRNA-specific
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M115.640060
– volume: 7
  start-page: 143
  year: 1999
  ident: 10.1016/j.bbagen.2017.03.012_bb0380
  article-title: The crystal structure of Cys-tRNACys-EF-Tu-GDPNP reveals general and specific features in the ternary complex and in tRNA
  publication-title: Structure
  doi: 10.1016/S0969-2126(99)80021-5
– volume: 11
  start-page: 1619
  year: 2014
  ident: 10.1016/j.bbagen.2017.03.012_bb0590
  article-title: Distribution and frequencies of post-transcriptional modifications in tRNAs
  publication-title: RNA Biol.
  doi: 10.4161/15476286.2014.992273
– volume: 5
  start-page: 17196
  year: 2015
  ident: 10.1016/j.bbagen.2017.03.012_bb0210
  article-title: Site specific genetic incorporation of azidophenylalanine in Schizosaccharomyces pombe
  publication-title: Sci. Rep.
  doi: 10.1038/srep17196
– volume: 105
  start-page: 13298
  year: 2008
  ident: 10.1016/j.bbagen.2017.03.012_bb0345
  article-title: Transplantation of a tyrosine editing domain into a tyrosyl-tRNA synthetase variant enhances its specificity for a tyrosine analog
  publication-title: Proc. Natl. Acad. Sci. U. S. A.
  doi: 10.1073/pnas.0803531105
– volume: 428
  start-page: 1004
  year: 2016
  ident: 10.1016/j.bbagen.2017.03.012_bb0025
  article-title: Overcoming challenges in engineering the genetic code
  publication-title: J. Mol. Biol.
  doi: 10.1016/j.jmb.2015.09.003
– volume: 108
  start-page: 5215
  year: 2011
  ident: 10.1016/j.bbagen.2017.03.012_bb0405
  article-title: Tuning the affinity of aminoacyl-tRNA to elongation factor Tu for optimal decoding
  publication-title: Proc. Natl. Acad. Sci. U. S. A.
  doi: 10.1073/pnas.1102128108
– volume: 16
  start-page: 907
  year: 1996
  ident: 10.1016/j.bbagen.2017.03.012_bb0140
  article-title: Amber suppression in mammalian cells dependent upon expression of an Escherichia coli aminoacyl-tRNA synthetase gene
  publication-title: Mol. Cell. Biol.
  doi: 10.1128/MCB.16.3.907
– volume: 253
  start-page: 4517
  year: 1978
  ident: 10.1016/j.bbagen.2017.03.012_bb0425
  article-title: “Chemical aminoacylation” of tRNA's
  publication-title: J. Biol. Chem.
  doi: 10.1016/S0021-9258(17)30417-9
– volume: 42
  start-page: 14042
  year: 2014
  ident: 10.1016/j.bbagen.2017.03.012_bb0480
  article-title: Molecular insights into the interaction of the ribosomal stalk protein with elongation factor 1a
  publication-title: Nucleic Acids Res.
  doi: 10.1093/nar/gku1248
– volume: 7
  start-page: 1292
  year: 2012
  ident: 10.1016/j.bbagen.2017.03.012_bb0170
  article-title: Expanding the genetic code of Caenorhabditis elegans using bacterial aminoacyl-tRNA synthetase/tRNA pairs
  publication-title: ACS Chem. Biol.
  doi: 10.1021/cb200542j
– volume: 23
  start-page: 751
  year: 2012
  ident: 10.1016/j.bbagen.2017.03.012_bb0010
  article-title: Recent advances in genetic code engineering in Escherichia coli
  publication-title: Curr. Opin. Biotechnol.
  doi: 10.1016/j.copbio.2011.12.027
– volume: 351
  start-page: 9
  year: 2005
  ident: 10.1016/j.bbagen.2017.03.012_bb0080
  article-title: The length of the 5′ leader of Escherichia coli tRNA precursors influences bacterial growth
  publication-title: J. Mol. Biol.
  doi: 10.1016/j.jmb.2005.05.022
– volume: 3
  start-page: 263
  year: 2006
  ident: 10.1016/j.bbagen.2017.03.012_bb0100
  article-title: Efficient incorporation of unnatural amino acids into proteins in Escherichia coli
  publication-title: Nat. Methods
  doi: 10.1038/nmeth864
– volume: 19
  start-page: 386
  year: 2011
  ident: 10.1016/j.bbagen.2017.03.012_bb0555
  article-title: Heat maps for intramolecular communication in an RNP enzyme encoding glutamine
  publication-title: Structure
  doi: 10.1016/j.str.2010.12.017
– volume: 10
  start-page: 511
  year: 2003
  ident: 10.1016/j.bbagen.2017.03.012_bb0185
  article-title: Progress toward an expanded eukaryotic genetic code
  publication-title: Chem. Biol.
  doi: 10.1016/S1074-5521(03)00123-6
– year: 2014
  ident: 10.1016/j.bbagen.2017.03.012_bb0035
  article-title: Transfer RNA recognition and aminoacylation by synthetases
– volume: 20
  start-page: 632
  year: 2014
  ident: 10.1016/j.bbagen.2017.03.012_bb0445
  article-title: A tRNA body with high affinity for EF-Tu hastens ribosomal incorporation of unnatural amino acids
  publication-title: RNA
  doi: 10.1261/rna.042234.113
– volume: 1728
  start-page: 143
  year: 2005
  ident: 10.1016/j.bbagen.2017.03.012_bb0500
  article-title: Bacillus subtilis tRNAPro with the anticodon mo5UGG can recognize the codon CCC
  publication-title: Biochim. Biophys. Acta
  doi: 10.1016/j.bbaexp.2005.02.011
– volume: 278
  start-page: 17672
  year: 2003
  ident: 10.1016/j.bbagen.2017.03.012_bb0390
  article-title: Common location of determinants in initiator transfer RNAs for initiator-elongator discrimination in bacteria and in eukaryotes
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M212890200
– volume: 55
  start-page: 618
  year: 2016
  ident: 10.1016/j.bbagen.2017.03.012_bb0560
  article-title: Improved incorporation of noncanonical amino acids by an engineered tRNATyr suppressor
  publication-title: Biochemistry
  doi: 10.1021/acs.biochem.5b01185
– volume: 130
  start-page: 6066
  year: 2008
  ident: 10.1016/j.bbagen.2017.03.012_bb0200
  article-title: New methods enabling efficient incorporation of unnatural amino acids in yeast
  publication-title: J. Am. Chem. Soc.
  doi: 10.1021/ja800894n
– volume: 43
  year: 2015
  ident: 10.1016/j.bbagen.2017.03.012_bb0645
  article-title: Revealing the amino acid composition of proteins within an expanded genetic code
  publication-title: Nucleic Acids Res.
  doi: 10.1093/nar/gku1087
– volume: 29
  start-page: 4767
  year: 2001
  ident: 10.1016/j.bbagen.2017.03.012_bb0540
  article-title: Misreading of termination codons in eukaryotes by natural nonsense suppressor tRNAs
  publication-title: Nucleic Acids Res.
  doi: 10.1093/nar/29.23.4767
– volume: 86
  start-page: 95
  year: 2012
  ident: 10.1016/j.bbagen.2017.03.012_bb0475
  article-title: Quality control of mRNA decoding on the bacterial ribosome
  publication-title: Adv. Protein Chem. Struct. Biol.
  doi: 10.1016/B978-0-12-386497-0.00003-7
– volume: 510
  start-page: 507
  year: 2014
  ident: 10.1016/j.bbagen.2017.03.012_bb0235
  article-title: The selective tRNA aminoacylation mechanism based on a single G·U pair
  publication-title: Nature
  doi: 10.1038/nature13440
– volume: 3
  start-page: 1033
  year: 1996
  ident: 10.1016/j.bbagen.2017.03.012_bb0435
  article-title: Development of improved tRNAs for in vitro biosynthesis of proteins containing unnatural amino acids
  publication-title: Chem. Biol.
  doi: 10.1016/S1074-5521(96)90169-6
– volume: 54
  start-page: 7355
  year: 2015
  ident: 10.1016/j.bbagen.2017.03.012_bb0575
  article-title: Evaluating sense codon reassignment with a simple fluorescence screen
  publication-title: Biochemistry
  doi: 10.1021/acs.biochem.5b00870
– volume: 35
  start-page: 1270
  year: 2007
  ident: 10.1016/j.bbagen.2017.03.012_bb0305
  article-title: Recognition of pyrrolysine tRNA by the Desulfitobacterium hafniense pyrrolysyl-tRNA synthetase
  publication-title: Nucleic Acids Res.
  doi: 10.1093/nar/gkl1151
– volume: 15
  start-page: 507
  year: 2008
  ident: 10.1016/j.bbagen.2017.03.012_bb0610
  article-title: Aminoacylation of tRNA with phosphoserine for synthesis of cysteinyl-tRNACys
  publication-title: Nat. Struct. Mol. Biol.
  doi: 10.1038/nsmb.1423
– volume: 37
  start-page: 1616
  year: 2009
  ident: 10.1016/j.bbagen.2017.03.012_bb0525
  article-title: Unconventional decoding of the AUA codon as methionine by mitochondrial tRNAMet with the anticodon f5CAU as revealed with a mitochondrial in vitro translation system
  publication-title: Nucleic Acids Res.
  doi: 10.1093/nar/gkp001
– volume: 103
  start-page: 9785
  year: 2006
  ident: 10.1016/j.bbagen.2017.03.012_bb0195
  article-title: A genetically encoded fluorescent amino acid
  publication-title: Proc. Natl. Acad. Sci. U. S. A.
  doi: 10.1073/pnas.0603965103
– volume: 240
  start-page: 793
  year: 1988
  ident: 10.1016/j.bbagen.2017.03.012_bb0230
  article-title: Changing the identity of a tRNA by introducing a GU wobble pair near the 3′ acceptor end
  publication-title: Science
  doi: 10.1126/science.2452483
– volume: 351
  start-page: 133
  year: 2014
  ident: 10.1016/j.bbagen.2017.03.012_bb0520
  article-title: Sense codon emancipation for proteome-wide incorporation of noncanonical amino acids: rare isoleucine codon AUA as a target for genetic code expansion
  publication-title: FEMS Microbiol. Lett.
  doi: 10.1111/1574-6968.12371
– volume: 493
  start-page: 185
  year: 2012
  ident: 10.1016/j.bbagen.2017.03.012_bb0120
  article-title: RNA polymerase III transcription control elements: themes and variations
  publication-title: Gene
  doi: 10.1016/j.gene.2011.06.015
– volume: 274
  start-page: 35601
  year: 1999
  ident: 10.1016/j.bbagen.2017.03.012_bb0250
  article-title: Major anticodon-binding region missing from an archaebacterial tRNA synthetase
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.274.50.35601
– volume: 32
  start-page: 97
  year: 2014
  ident: 10.1016/j.bbagen.2017.03.012_bb0300
  article-title: Directed evolution of genetic parts and circuits by compartmentalized partnered replication
  publication-title: Nat. Biotechnol.
  doi: 10.1038/nbt.2714
– year: 2016
  ident: 10.1016/j.bbagen.2017.03.012_bb0455
  article-title: Translation system engineering in Escherichia coli enhances non-canonical amino acid incorporation into proteins
  publication-title: Biotechnol. Bioeng.
– volume: 270
  start-page: 1464
  year: 1995
  ident: 10.1016/j.bbagen.2017.03.012_bb0375
  article-title: Crystal-structure of the ternary complex of Phe-TrnaPhe, EF-Tu, and a GTP analog
  publication-title: Science
  doi: 10.1126/science.270.5241.1464
– volume: 44
  start-page: 8020
  year: 2016
  ident: 10.1016/j.bbagen.2017.03.012_bb0515
  article-title: An integrated, structure- and energy-based view of the genetic code
  publication-title: Nucleic Acids Res.
  doi: 10.1093/nar/gkw608
– volume: 10
  start-page: 1633
  year: 1990
  ident: 10.1016/j.bbagen.2017.03.012_bb0180
  article-title: A bacterial amber suppressor in Saccharomyces cerevisiae is selectively recognized by a bacterial aminoacyl-tRNA synthetase
  publication-title: Mol. Cell. Biol.
– volume: 69
  start-page: 617
  year: 2000
  ident: 10.1016/j.bbagen.2017.03.012_bb0040
  article-title: Aminoacyl-tRNA synthesis
  publication-title: Annu. Rev. Biochem.
  doi: 10.1146/annurev.biochem.69.1.617
– reference: 4879404 - Proc Natl Acad Sci U S A. 1968 Oct;61(2):768-74
– reference: 19118381 - Nature. 2009 Feb 26;457(7233):1163-7
– reference: 19931532 - FEBS Lett. 2010 Jan 21;584(2):310-7
– reference: 21873425 - J Biol Chem. 2011 Oct 14;286(41):35494-8
– reference: 9742237 - Nucleic Acids Res. 1998 Oct 1;26(19):4374-81
– reference: 26186264 - Curr Opin Chem Biol. 2015 Oct;28:83-90
– reference: 16453524 - EMBO J. 1984 May;3(5):1091-6
– reference: 10966471 - Annu Rev Biochem. 2000;69:617-50
– reference: 2452483 - Science. 1988 May 6;240(4853):793-6
– reference: 12920298 - Science. 2003 Aug 15;301(5635):964-7
– reference: 26250114 - Nucleic Acids Res. 2015 Dec 15;43(22):e156
– reference: 18471995 - Biochem Biophys Res Commun. 2008 Jul 11;371(4):818-22
– reference: 18042450 - Mol Cell. 2007 Nov 30;28(4):533-43
– reference: 15952884 - Annu Rev Biochem. 2005;74:129-77
– reference: 22554080 - ACS Chem Biol. 2012 Jul 20;7(7):1292-302
– reference: 18765802 - Proc Natl Acad Sci U S A. 2008 Sep 9;105(36):13298-303
– reference: 11600701 - Nucleic Acids Res. 2001 Oct 15;29(20):4125-33
– reference: 26350500 - Nat Commun. 2015 Sep 09;6:8130
– reference: 16260144 - Trends Biochem Sci. 2005 Dec;30(12):659-65
– reference: 10585437 - J Biol Chem. 1999 Dec 10;274(50):35601-6
– reference: 9801296 - Nucleic Acids Res. 1998 Nov 15;26(22):5017-35
– reference: 26694948 - Biochemistry. 2016 Jan 26;55(3):618-28
– reference: 2263446 - Nucleic Acids Res. 1990 Dec 11;18(23):6815-9
– reference: 9582290 - J Biol Chem. 1998 May 22;273(21):12685-8
– reference: 23057558 - J Am Chem Soc. 2012 Oct 31;134(43):17955-62
– reference: 9000011 - Chem Biol. 1996 Dec;3(12):1033-8
– reference: 28553457 - Chem Sci. 2015 Jan 1;6(1):50-69
– reference: 12697332 - Biochim Biophys Acta. 2003 Apr 15;1626(1-3):75-82
– reference: 23852030 - Top Curr Chem. 2014;344:1-41
– reference: 11313494 - Science. 2001 Apr 20;292(5516):498-500
– reference: 273907 - Proc Natl Acad Sci U S A. 1978 Apr;75(4):1759-62
– reference: 21079633 - Nat Rev Microbiol. 2010 Dec;8(12):849-56
– reference: 25724653 - J Biol Chem. 2015 Apr 17;290(16):10495-503
– reference: 19852970 - J Mol Biol. 2010 Jan 15;395(2):361-74
– reference: 18426210 - J Am Chem Soc. 2008 May 14;130(19):6066-7
– reference: 23554007 - Angew Chem Int Ed Engl. 2013 May 3;52(19):5106-9
– reference: 16595295 - Crit Rev Biochem Mol Biol. 2006 Mar-Apr;41(2):77-102
– reference: 22237016 - Curr Opin Biotechnol. 2012 Oct;23(5):751-7
– reference: 16002088 - J Mol Biol. 2005 Aug 5;351(1):9-15
– reference: 20810645 - Genes Dev. 2010 Sep 1;24(17):1832-60
– reference: 15833716 - Biochim Biophys Acta. 2005 May 1;1728(3):143-9
– reference: 21402928 - Proc Natl Acad Sci U S A. 2011 Mar 29;108(13):5215-20
– reference: 24671767 - RNA. 2014 May;20(5):632-43
– reference: 25428348 - Nucleic Acids Res. 2014 Dec 16;42(22):14042-52
– reference: 15322138 - J Biol Chem. 2004 Oct 8;279(41):42359-62
– reference: 27096575 - FEBS Lett. 2016 May;590(10 ):1530-42
– reference: 18284924 - Curr Opin Chem Biol. 2008 Apr;12(2):151-8
– reference: 12837384 - Chem Biol. 2003 Jun;10(6):511-9
– reference: 26597962 - Sci Rep. 2015 Nov 24;5:17196
– reference: 21926996 - Nat Chem Biol. 2011 Sep 18;7(11):779-86
– reference: 26544153 - ACS Synth Biol. 2016 Feb 19;5(2):163-71
– reference: 27915288 - Nucleic Acids Res. 2016 Dec 1;44(21):10042-10050
– reference: 248056 - J Biol Chem. 1978 Jul 10;253(13):4517-20
– reference: 26348789 - J Mol Biol. 2016 Feb 27;428(5 Pt B):1004-21
– reference: 17868690 - J Mol Biol. 2007 Oct 26;373(3):623-32
– reference: 27064538 - Biochemistry. 2016 May 3;55(17 ):2526-37
– reference: 26890980 - Biochemistry. 2016 Mar 15;55(10):1541-53
– reference: 25733896 - Proc Natl Acad Sci U S A. 2015 Mar 10;112(10):3038-43
– reference: 1690848 - Mol Cell Biol. 1990 Apr;10 (4):1633-41
– reference: 24079513 - J Am Chem Soc. 2013 Nov 13;135(45):17031-8
– reference: 8756732 - Cell. 1996 Aug 9;86(3):503-12
– reference: 18425141 - Nat Struct Mol Biol. 2008 May;15(5):507-14
– reference: 17267409 - Nucleic Acids Res. 2007;35(4):1270-8
– reference: 18193063 - Nat Struct Mol Biol. 2008 Feb;15(2):192-8
– reference: 24185096 - Nat Biotechnol. 2014 Jan;32(1):97-101
– reference: 24433543 - FEMS Microbiol Lett. 2014 Feb;351(2):133-44
– reference: 12097643 - Proc Natl Acad Sci U S A. 2002 Jul 23;99(15):9715-20
– reference: 21572561 - Wiley Interdiscip Rev RNA. 2011 May-Jun;2(3):362-75
– reference: 24755590 - Nat Chem. 2014 May;6(5):393-403
– reference: 7491491 - Science. 1995 Dec 1;270(5241):1464-72
– reference: 26030730 - Nat Chem Biol. 2015 Jul;11(7):496-503
– reference: 3285220 - Nature. 1988 May 12;333(6169):140-5
– reference: 17718568 - J Am Chem Soc. 2007 Sep 19;129(37):11316-7
– reference: 25378305 - Nucleic Acids Res. 2015 Jan;43(2):e8
– reference: 4917265 - Nature. 1970 Oct 3;228(5266):57
– reference: 11588263 - Science. 2001 Oct 5;294(5540):165-8
– reference: 8510145 - J Mol Biol. 1993 May 20;231(2):219-29
– reference: 20925334 - J Am Chem Soc. 2010 Oct 27;132(42):14819-24
– reference: 22243582 - Adv Protein Chem Struct Biol. 2012;86:95-128
– reference: 15037065 - J Mol Biol. 2004 Mar 5;336(5):1011-21
– reference: 18378185 - Curr Opin Microbiol. 2008 Apr;11(2):134-40
– reference: 26536053 - Biochemistry. 2015 Dec 22;54(50):7355-64
– reference: 25611331 - RNA Biol. 2014;11(12):1619-29
– reference: 21378964 - Nat Struct Mol Biol. 2011 Apr;18(4):432-6
– reference: 21868676 - Science. 2011 Aug 26;333(6046):1151-4
– reference: 27987323 - Biotechnol Bioeng. 2017 May;114(5):1074-1086
– reference: 20052681 - Protein Sci. 2010 Mar;19(3):440-8
– reference: 16785423 - Proc Natl Acad Sci U S A. 2006 Jun 27;103(26):9785-9
– reference: 17603477 - Nat Neurosci. 2007 Aug;10(8):1063-72
– reference: 27448410 - Nucleic Acids Res. 2016 Sep 30;44(17 ):8020-40
– reference: 17958427 - J Am Chem Soc. 2007 Nov 21;129(46):14458-62
– reference: 5969078 - J Mol Biol. 1966 Aug;19(2):548-55
– reference: 17560600 - J Mol Biol. 2007 Aug 3;371(1):112-22
– reference: 12639964 - J Biol Chem. 2003 May 16;278(20):17672-9
– reference: 10368282 - Structure. 1999 Feb 15;7(2):143-56
– reference: 11717406 - Proc Natl Acad Sci U S A. 2001 Dec 4;98(25):14310-5
– reference: 20702426 - Nucleic Acids Res. 2010 Dec;38(22):8188-95
– reference: 12110595 - EMBO J. 2002 Jul 15;21(14):3841-51
– reference: 21712079 - Gene. 2012 Feb 10;493(2):185-94
– reference: 15521721 - J Am Chem Soc. 2004 Nov 10;126(44):14306-7
– reference: 2467143 - J Theor Biol. 1988 Aug 8;133(3):363-70
– reference: 12409460 - Nucleic Acids Res. 2002 Nov 1;30(21):4692-9
– reference: 19856359 - Angew Chem Int Ed Engl. 2009;48(48):9148-51
– reference: 8622693 - Mol Cell Biol. 1996 Mar;16(3):907-13
– reference: 24631543 - Biochim Biophys Acta. 2014 Jun;1844(6):1059-70
– reference: 21819153 - J Am Chem Soc. 2011 Sep 14;133(36):14196-9
– reference: 21478873 - Nature. 2011 Apr 28;472(7344):499-503
– reference: 19151083 - Nucleic Acids Res. 2009 Apr;37(5):1616-27
– reference: 3910093 - Biochemistry. 1985 Nov 5;24(23):6433-9
– reference: 795428 - Biochem J. 1976 Nov 15;160(2):185-94
– reference: 19452597 - J Mol Biol. 2009 Mar 13;386(5):1255-64
– reference: 25796611 - FEMS Microbiol Rev. 2015 May;39(3):280-300
– reference: 15366888 - J Am Chem Soc. 2004 Sep 22;126(37):11454-5
– reference: 8416930 - J Biol Chem. 1993 Jan 5;268(1):217-20
– reference: 20571084 - Nucleic Acids Res. 2010 Oct;38(19):6813-30
– reference: 11726686 - Nucleic Acids Res. 2001 Dec 1;29(23):4767-82
– reference: 22895820 - RNA. 2012 Oct;18(10):1886-96
– reference: 2963963 - Nature. 1988 Feb 25;331(6158):723-5
– reference: 23781103 - Proc Natl Acad Sci U S A. 2013 Jul 2;110(27):10964-9
– reference: 15187228 - Proc Natl Acad Sci U S A. 2004 Jun 15;101(24):8882-7
– reference: 1090377 - Cell. 1975 Jan;4(1):21-9
– reference: 4618855 - J Mol Biol. 1974 Apr 15;84(3):407-22
– reference: 9278503 - Science. 1997 Sep 5;277(5331):1453-62
– reference: 23118484 - Nucleic Acids Res. 2013 Jan;41(Database issue):D262-7
– reference: 19379069 - Annu Rev Microbiol. 2009;63:61-78
– reference: 16554830 - Nat Methods. 2006 Apr;3(4):263-5
– reference: 21397189 - Structure. 2011 Mar 9;19(3):386-96
– reference: 27600875 - ACS Synth Biol. 2017 Jan 20;6(1):108-119
– reference: 12032089 - EMBO J. 2002 Jun 3;21(11):2769-77
– reference: 6352054 - Cell. 1983 Sep;34(2):655-64
– reference: 17110438 - Proc Natl Acad Sci U S A. 2006 Nov 28;103(48):18095-100
– reference: 24919148 - Nature. 2014 Jun 26;510(7506):507-11
– reference: 18559342 - J Biol Chem. 2008 Aug 8;283(32):21997-2006
SSID ssj0000595
ssj0025309
Score 2.3619423
SecondaryResourceType review_article
Snippet The development of orthogonal translation systems (OTSs) for genetic code expansion (GCE) has allowed for the incorporation of a diverse array of non-canonical...
Not provided.
SourceID pubmedcentral
osti
proquest
pubmed
crossref
elsevier
SourceType Open Access Repository
Aggregation Database
Index Database
Enrichment Source
Publisher
StartPage 3001
SubjectTerms amino acids
Amino Acyl-tRNA Synthetases - genetics
Amino Acyl-tRNA Synthetases - metabolism
Aminoacyl-tRNA synthetases
Animals
Biochemistry & Molecular Biology
Biophysics
genetic code
Genetic Code - genetics
Genetic code expansion
Humans
Models, Molecular
Non-canonical amino acids
Orthogonal tRNAs
Protein Biosynthesis - genetics
Protein Engineering - methods
proteins
RNA, Transfer - physiology
Synthetic biology
Synthetic Biology - methods
Transfer RNA
Title The central role of tRNA in genetic code expansion
URI https://dx.doi.org/10.1016/j.bbagen.2017.03.012
https://www.ncbi.nlm.nih.gov/pubmed/28323071
https://www.proquest.com/docview/1879661750
https://www.proquest.com/docview/2000465676
https://www.osti.gov/biblio/1538022
https://pubmed.ncbi.nlm.nih.gov/PMC5603357
Volume 1861
hasFullText 1
inHoldings 1
isFullTextHit
isPrint
link http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1La9tAEB6CQ2kvJUlfzost9Kpa0u5qtUdjEtyY-JA2NLdF-6IORQ6JA-2lvz0zerh1aQj0ZGTPitXM7OzIO983AB-cCEFLXSW5LdJEeKmSyjt850kr512aWh0InHw-L6aX4uxKXm3BpMfCUFllF_vbmN5E6-6bUafN0c1iMfpMh3qYTsiMKNe1JMCvEIq8_OOv32UemD7I9iRBJCTdw-eaGi9rcdESC2qmGqrTLH9sexosccX9Kwv9u5jyj93pdAdedmklG7cz34WtUO_Bs7bR5M89eD7p-7q9ghw9g3W3YVRcyJaRrS7mY7aoGc6TUI2MkO4s_MBQQf-mvYbL05Mvk2nSdU5InCz1KlHa8zLYosLtG99nMi8iYXViFUvBY9SuCFx5KRRq0FMPXKtzyaPwIfVSOsffwKBe1uEdMDRWRpz5eVGWQqKgLTNno46481euLIfAe4UZ19GKU3eL76avH7s2rZoNqdmk3KCah5CsR920tBpPyKveFmbDPQxG_idGHpDpaBSx4joqH8JhFOgxfRnC-96iBs1AhyVVHZb3d4a6sKPmMKF6XCZvsLeyUMUQ3rZesH4aagGF8TPDmW_4x1qAeL03f6kX3xp-b0xCOZdq_7-f-QBe0FULmTyEwer2Phxh7rSyx83iOIbt8afZdE6fs4uvswdNNhiV
linkProvider Elsevier
linkToHtml http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwtV1Lb9QwEB6VRahcEJTXUh5GgmPYJLYT-8ChKlRb2u4BWqk3E7_EVlW2olvRXvqn-IPM5LGwiKoSUq8bO-vMjGe-xDPfALxxIgQtdZXktkgT4WWZVN7hO09aOe_S1OpAxcl7k2J8ID4dysMV-NnXwlBaZef7W5_eeOvul1EnzdHJdDr6Qod6CCdkRpTrWqous3InXPzA97bT99sfUMlv83zr4_7mOOlaCyROKj1PSu25CraoML4h4M-8iFTMEquoBI9RuyLw0ktR4l94ahJrdS55FD6kXkrnON73FtwW6C6obcK7y995JYhXZHt0IRJaXl-v1ySVWYtegmhXs7LhVs3yq-LhYIZb_F-w9-_szT_C4dZ9uNfhWLbRiuoBrIR6De60nS0v1mB1s28k9xByNEXW3YZRNiObRTb_PNlg05rhOqmMklFpPQvn6Jvo890jOLgReT6GQT2rw1NgaB0ZkfTnhVJC4kCrMmejjgg1KqfUEHgvMOM6HnNqp3Fs-oS1I9OK2ZCYTcoNinkIyWLWScvjcc34steFWbJHg6HmmpnrpDqaRTS8jvKVcBpFFsRLQ3jda9SgGuh0pqrD7OzUUNt3lBwiuKvH5E2xryzKYghPWitYPA31nEKHneHKl-xjMYCIxJev1NNvDaE4ol7OZfnsv5_5FayO9_d2ze72ZGcd7tKVtl7zOQzm38_CCwRuc_uy2SgMvt70zvwF4yRR1A
openUrl ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=The+central+role+of+tRNA+in+genetic+code+expansion&rft.jtitle=Biochimica+et+biophysica+acta.+General+subjects&rft.au=Reynolds%2C+Noah+M&rft.au=Vargas-Rodriguez%2C+Oscar&rft.au=S%C3%B6ll%2C+Dieter&rft.au=Crnkovi%C4%87%2C+Ana&rft.date=2017-11-01&rft.issn=0304-4165&rft.volume=1861&rft.issue=11+Pt+B&rft.spage=3001&rft_id=info:doi/10.1016%2Fj.bbagen.2017.03.012&rft_id=info%3Apmid%2F28323071&rft.externalDocID=28323071
thumbnail_l http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0304-4165&client=summon
thumbnail_m http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0304-4165&client=summon
thumbnail_s http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0304-4165&client=summon