Eyes on Translation

Translation is a fundamental biological process by which ribosomes decode genetic information into proteins. The regulation of this process plays a key role in tuning protein levels, allowing cells to respond rapidly to changes in the environment and to synthesize proteins with precise timing and at...

Full description

Saved in:
Bibliographic Details
Published inMolecular cell Vol. 63; no. 6; pp. 918 - 925
Main Authors Chekulaeva, Marina, Landthaler, Markus
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 15.09.2016
Subjects
Online AccessGet full text

Cover

Loading…
Abstract Translation is a fundamental biological process by which ribosomes decode genetic information into proteins. The regulation of this process plays a key role in tuning protein levels, allowing cells to respond rapidly to changes in the environment and to synthesize proteins with precise timing and at specific subcellular locations. Despite detailed biochemical and structural insight into the mechanism of protein synthesis, translational dynamics and localization in a cellular context are less well understood. Here, we summarize recent efforts to quantify and visualize translation, focusing on four publications (Morisaki et al., 2016; Wang et al., 2016; Wu et al., 2016; Yan et al., 2016) describing novel approaches to imaging in real time the synthesis of nascent peptides from individual mRNAs in living cells. Translation is a key step of gene expression, regulated via multiple mechanisms. In this issue of Molecular Cell, Chekulaeva and Landthaler review recent advances in quantification and visualization of translation, focusing on novel imaging approaches to studying translation dynamics of single mRNAs in live cells.
AbstractList Translation is a fundamental biological process by which ribosomes decode genetic information into proteins. The regulation of this process plays a key role in tuning protein levels, allowing cells to respond rapidly to changes in the environment and to synthesize proteins with precise timing and at specific subcellular locations. Despite detailed biochemical and structural insight into the mechanism of protein synthesis, translational dynamics and localization in a cellular context are less well understood. Here, we summarize recent efforts to quantify and visualize translation, focusing on four publications (Morisaki et al., 2016; Wang et al., 2016; Wu et al., 2016; Yan et al., 2016) describing novel approaches to imaging in real time the synthesis of nascent peptides from individual mRNAs in living cells.
Translation is a fundamental biological process by which ribosomes decode genetic information into proteins. The regulation of this process plays a key role in tuning protein levels, allowing cells to respond rapidly to changes in the environment and to synthesize proteins with precise timing and at specific subcellular locations. Despite detailed biochemical and structural insight into the mechanism of protein synthesis, translational dynamics and localization in a cellular context are less well understood. Here, we summarize recent efforts to quantify and visualize translation, focusing on four publications (Morisaki et al., 2016; Wang et al., 2016; Wu et al., 2016; Yan et al., 2016) describing novel approaches to imaging in real time the synthesis of nascent peptides from individual mRNAs in living cells. Translation is a key step of gene expression, regulated via multiple mechanisms. In this issue of Molecular Cell, Chekulaeva and Landthaler review recent advances in quantification and visualization of translation, focusing on novel imaging approaches to studying translation dynamics of single mRNAs in live cells.
Author Landthaler, Markus
Chekulaeva, Marina
Author_xml – sequence: 1
  givenname: Marina
  surname: Chekulaeva
  fullname: Chekulaeva, Marina
  email: marina.chekulaeva@mdc-berlin.de
  organization: Berlin Institute for Medical Systems Biology, Max Delbrück Center for Molecular Medicine, 13125 Berlin, Germany
– sequence: 2
  givenname: Markus
  surname: Landthaler
  fullname: Landthaler, Markus
  email: markus.landthaler@mdc-berlin.de
  organization: Berlin Institute for Medical Systems Biology, Max Delbrück Center for Molecular Medicine, 13125 Berlin, Germany
BackLink https://www.ncbi.nlm.nih.gov/pubmed/27635758$$D View this record in MEDLINE/PubMed
BookMark eNp9kDtrwzAUhUVJaR7t1LWUjF3sXsmyLS-FEtIHBLqks5Cla1CwrVRyCvn3VXDasdN98N17OGdOJr3rkZA7CikFWjzu0s61GtuUxSkFkUJGL8iMQlUmnBZ8cu5ZWeRTMg9hB0B5LqorMo27LC9zMSO36yOGpeuXW6_60KrBuv6aXDaqDXhzrgvy-bLert6Szcfr--p5k2gOYkhK07CM5bUBpEZoMAZNXgJDUSLXXDFRKZZxxjSvKct5VtCyqrUBpRoGoskW5GH8u_fu64BhkJ0N0VGrenSHIKlgUAATVESUj6j2LgSPjdx72yl_lBTkKQ65k2Mc8hSHBCFjHPHs_qxwqDs0f0e__iPwNAIYfX5b9DJoi71GYz3qQRpn_1f4ARc3cik
CitedBy_id crossref_primary_10_3389_fcell_2023_1151318
crossref_primary_10_1038_s41576_020_0258_4
crossref_primary_10_1134_S1022795423030110
crossref_primary_10_1139_cjm_2019_0624
crossref_primary_10_1186_s13229_020_00349_y
crossref_primary_10_1038_nrm_2017_91
crossref_primary_10_1074_jbc_RA120_013454
crossref_primary_10_1016_j_meegid_2020_104432
crossref_primary_10_1021_acs_analchem_3c03365
crossref_primary_10_1016_j_conb_2017_05_005
crossref_primary_10_1016_j_neures_2018_10_003
crossref_primary_10_1101_cshperspect_a034728
crossref_primary_10_1016_j_molcel_2020_09_014
crossref_primary_10_1016_j_expneurol_2023_114454
crossref_primary_10_1371_journal_pgen_1007117
crossref_primary_10_1137_19M1250571
crossref_primary_10_31857_S0016675823030116
crossref_primary_10_3389_fgene_2021_796060
crossref_primary_10_3389_fnsyn_2018_00029
crossref_primary_10_1002_wrna_1590
crossref_primary_10_1016_j_physd_2023_133881
Cites_doi 10.1016/j.cell.2009.01.042
10.1038/nn.2580
10.1126/science.aaa3380
10.1073/pnas.0907143106
10.1016/j.cell.2015.05.054
10.1016/S0021-9258(18)67090-5
10.1038/nmeth.2401
10.1016/j.molcel.2015.02.032
10.1126/science.1168978
10.1038/nmeth.1314
10.1083/jcb.201112145
10.1126/science.1257522
10.1016/j.celrep.2014.10.042
10.1002/pmic.200800275
10.1038/nrm2548
10.1126/science.1257521
10.1111/j.1432-1033.1977.tb11256.x
10.1016/j.cell.2011.10.002
10.1038/nmeth.3319
10.1016/j.cell.2016.04.034
10.1126/science.aaf1084
10.1126/science.aaf0899
10.1126/science.1197142
10.1073/pnas.0601637103
10.1016/j.cell.2008.10.028
10.1073/pnas.1216880109
10.1038/nature06716
10.1016/j.cell.2014.09.039
10.1042/BST20150126
10.1016/j.cell.2016.04.040
10.1038/nbt.2356
ContentType Journal Article
Copyright 2016 Elsevier Inc.
Copyright © 2016 Elsevier Inc. All rights reserved.
Copyright_xml – notice: 2016 Elsevier Inc.
– notice: Copyright © 2016 Elsevier Inc. All rights reserved.
DBID 6I.
AAFTH
CGR
CUY
CVF
ECM
EIF
NPM
AAYXX
CITATION
7X8
DOI 10.1016/j.molcel.2016.08.031
DatabaseName ScienceDirect Open Access Titles
Elsevier:ScienceDirect:Open Access
Medline
MEDLINE
MEDLINE (Ovid)
MEDLINE
MEDLINE
PubMed
CrossRef
MEDLINE - Academic
DatabaseTitle MEDLINE
Medline Complete
MEDLINE with Full Text
PubMed
MEDLINE (Ovid)
CrossRef
MEDLINE - Academic
DatabaseTitleList MEDLINE - Academic
MEDLINE

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 Biology
EISSN 1097-4164
EndPage 925
ExternalDocumentID 10_1016_j_molcel_2016_08_031
27635758
S1097276516304786
Genre Journal Article
Review
GroupedDBID ---
--K
-DZ
-~X
0R~
123
1~5
2WC
4.4
457
4G.
5RE
62-
6I.
7-5
AACTN
AAEDW
AAFTH
AAIAV
AAKRW
AAKUH
AALRI
AAUCE
AAVLU
AAXJY
AAXUO
ABJNI
ABMAC
ABMWF
ABVKL
ACGFO
ACGFS
ACNCT
ADBBV
ADEZE
ADJPV
AEFWE
AENEX
AEXQZ
AFFNX
AFTJW
AGKMS
AITUG
ALKID
ALMA_UNASSIGNED_HOLDINGS
AMRAJ
ASPBG
AVWKF
AZFZN
BAWUL
CS3
DIK
DU5
E3Z
EBS
EJD
F5P
FCP
FDB
FEDTE
FIRID
HH5
HVGLF
IH2
IHE
IXB
J1W
JIG
KQ8
L7B
M3Z
M41
N9A
NCXOZ
O-L
O9-
OK1
P2P
RCE
RIG
ROL
RPZ
SDG
SES
SSZ
TR2
WQ6
ZA5
0SF
AAEDT
AAHBH
AAMRU
ADVLN
AKAPO
AKRWK
CGR
CUY
CVF
ECM
EIF
NPM
.55
.GJ
29M
3O-
53G
5VS
AAIKJ
AAQFI
AAQXK
AAYXX
ADMUD
AGHFR
CITATION
FGOYB
HZ~
OZT
R2-
UHS
X7M
ZGI
ZXP
7X8
ID FETCH-LOGICAL-c408t-7df2325bd0e1d8c0dded5702e87e4c4a289a23422c4b125436179bcd0aaf208f3
IEDL.DBID ABVKL
ISSN 1097-2765
IngestDate Thu Oct 24 23:06:50 EDT 2024
Thu Sep 26 17:40:14 EDT 2024
Sat Sep 28 08:46:09 EDT 2024
Fri Feb 23 02:30:35 EST 2024
IsDoiOpenAccess true
IsOpenAccess true
IsPeerReviewed true
IsScholarly true
Issue 6
Keywords mRNA localization
single molecule
translation
fluorescent protein
single cell
imaging
Language English
License This article is made available under the Elsevier license.
Copyright © 2016 Elsevier Inc. All rights reserved.
LinkModel DirectLink
MergedId FETCHMERGED-LOGICAL-c408t-7df2325bd0e1d8c0dded5702e87e4c4a289a23422c4b125436179bcd0aaf208f3
Notes ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-3
content type line 23
ObjectType-Review-1
OpenAccessLink https://www.sciencedirect.com/science/article/pii/S1097276516304786
PMID 27635758
PQID 1820602818
PQPubID 23479
PageCount 8
ParticipantIDs proquest_miscellaneous_1820602818
crossref_primary_10_1016_j_molcel_2016_08_031
pubmed_primary_27635758
elsevier_sciencedirect_doi_10_1016_j_molcel_2016_08_031
PublicationCentury 2000
PublicationDate 2016-09-15
PublicationDateYYYYMMDD 2016-09-15
PublicationDate_xml – month: 09
  year: 2016
  text: 2016-09-15
  day: 15
PublicationDecade 2010
PublicationPlace United States
PublicationPlace_xml – name: United States
PublicationTitle Molecular cell
PublicationTitleAlternate Mol Cell
PublicationYear 2016
Publisher Elsevier Inc
Publisher_xml – name: Elsevier Inc
References Dieterich, Hodas, Gouzer, Shadrin, Ngo, Triller, Tirrell, Schuman (bib6) 2010; 13
Howden, Geoghegan, Katsch, Efstathiou, Bhushan, Boutureira, Thomas, Trudgian, Kessler, Dieterich (bib12) 2013; 10
Wen, Lancaster, Hodges, Zeri, Yoshimura, Noller, Bustamante, Tinoco (bib27) 2008; 452
Sanz, Yang, Su, Morris, McKnight, Amieux (bib17) 2009; 106
Sonenberg, Hinnebusch (bib22) 2009; 136
tom Dieck, Kochen, Hanus, Heumüller, Bartnik, Nassim-Assir, Merk, Mosler, Garg, Bunse (bib25) 2015; 12
Ingolia, Ghaemmaghami, Newman, Weissman (bib13) 2009; 324
Simms, Hudson, Mosior, Rangwala, Zaher (bib21) 2014; 9
Aviner, Geiger, Elroy-Stein (bib1) 2013; 1
Sternberg, Doudna (bib23) 2015; 58
Besse, Ephrussi (bib2) 2008; 9
Holland, Fachinetti, Han, Cleveland (bib11) 2012; 109
Ingolia, Lareau, Weissman (bib14) 2011; 147
David, Dolan, Hickman, Knowlton, Clavarino, Pierre, Bennink, Yewdell (bib4) 2012; 197
Dieterich, Link, Graumann, Tirrell, Schuman (bib5) 2006; 103
Heiman, Schaefer, Gong, Peterson, Day, Ramsey, Suárez-Fariñas, Schwarz, Stephan, Surmeier (bib10) 2008; 135
Wu, Eliscovich, Yoon, Singer (bib30) 2016; 352
Tanenbaum, Gilbert, Qi, Weissman, Vale (bib24) 2014; 159
Siddiqui, Sonenberg (bib20) 2015; 43
Eichelbaum, Winter, Berriel Diaz, Herzig, Krijgsveld (bib7) 2012; 30
Halstead, Lionnet, Wilbertz, Wippich, Ephrussi, Singer, Chao (bib9) 2015; 347
Schwanhäusser, Gossen, Dittmar, Selbach (bib19) 2009; 9
Fresno, Jiménez, Vázquez (bib8) 1977; 72
Wu, Buxbaum, Katz, Yoon, Singer (bib29) 2015; 162
Schmidt, Clavarino, Ceppi, Pierre (bib18) 2009; 6
Williams, Jan, Weissman (bib28) 2014; 346
Morisaki, Lyon, DeLuca, DeLuca, English, Zhang, Lavis, Grimm, Viswanathan, Looger (bib16) 2016; 352
Yan, Hoek, Vale, Tanenbaum (bib31) 2016; 165
Yanagitani, Kimata, Kadokura, Kohno (bib32) 2011; 331
Boström, Wettesten, Borén, Bondjers, Wiklund, Olofsson (bib3) 1986; 261
Wang, Han, Zhou, Zhuang (bib26) 2016; 165
Jan, Williams, Weissman (bib15) 2014; 346
Eichelbaum (10.1016/j.molcel.2016.08.031_bib7) 2012; 30
Holland (10.1016/j.molcel.2016.08.031_bib11) 2012; 109
Schwanhäusser (10.1016/j.molcel.2016.08.031_bib19) 2009; 9
Yan (10.1016/j.molcel.2016.08.031_bib31) 2016; 165
Fresno (10.1016/j.molcel.2016.08.031_bib8) 1977; 72
Heiman (10.1016/j.molcel.2016.08.031_bib10) 2008; 135
tom Dieck (10.1016/j.molcel.2016.08.031_bib25) 2015; 12
Schmidt (10.1016/j.molcel.2016.08.031_bib18) 2009; 6
Jan (10.1016/j.molcel.2016.08.031_bib15) 2014; 346
Morisaki (10.1016/j.molcel.2016.08.031_bib16) 2016; 352
Tanenbaum (10.1016/j.molcel.2016.08.031_bib24) 2014; 159
David (10.1016/j.molcel.2016.08.031_bib4) 2012; 197
Sonenberg (10.1016/j.molcel.2016.08.031_bib22) 2009; 136
Yanagitani (10.1016/j.molcel.2016.08.031_bib32) 2011; 331
Wang (10.1016/j.molcel.2016.08.031_bib26) 2016; 165
Dieterich (10.1016/j.molcel.2016.08.031_bib6) 2010; 13
Ingolia (10.1016/j.molcel.2016.08.031_bib14) 2011; 147
Aviner (10.1016/j.molcel.2016.08.031_bib1) 2013; 1
Wen (10.1016/j.molcel.2016.08.031_bib27) 2008; 452
Wu (10.1016/j.molcel.2016.08.031_bib29) 2015; 162
Ingolia (10.1016/j.molcel.2016.08.031_bib13) 2009; 324
Sanz (10.1016/j.molcel.2016.08.031_bib17) 2009; 106
Sternberg (10.1016/j.molcel.2016.08.031_bib23) 2015; 58
Besse (10.1016/j.molcel.2016.08.031_bib2) 2008; 9
Siddiqui (10.1016/j.molcel.2016.08.031_bib20) 2015; 43
Williams (10.1016/j.molcel.2016.08.031_bib28) 2014; 346
Wu (10.1016/j.molcel.2016.08.031_bib30) 2016; 352
Howden (10.1016/j.molcel.2016.08.031_bib12) 2013; 10
Dieterich (10.1016/j.molcel.2016.08.031_bib5) 2006; 103
Simms (10.1016/j.molcel.2016.08.031_bib21) 2014; 9
Boström (10.1016/j.molcel.2016.08.031_bib3) 1986; 261
Halstead (10.1016/j.molcel.2016.08.031_bib9) 2015; 347
References_xml – volume: 9
  start-page: 971
  year: 2008
  end-page: 980
  ident: bib2
  article-title: Translational control of localized mRNAs: restricting protein synthesis in space and time
  publication-title: Nat. Rev. Mol. Cell Biol.
  contributor:
    fullname: Ephrussi
– volume: 6
  start-page: 275
  year: 2009
  end-page: 277
  ident: bib18
  article-title: SUnSET, a nonradioactive method to monitor protein synthesis
  publication-title: Nat. Methods
  contributor:
    fullname: Pierre
– volume: 12
  start-page: 411
  year: 2015
  end-page: 414
  ident: bib25
  article-title: Direct visualization of newly synthesized target proteins in situ
  publication-title: Nat. Methods
  contributor:
    fullname: Bunse
– volume: 346
  start-page: 1257521
  year: 2014
  ident: bib15
  article-title: Principles of ER cotranslational translocation revealed by proximity-specific ribosome profiling
  publication-title: Science
  contributor:
    fullname: Weissman
– volume: 347
  start-page: 1367
  year: 2015
  end-page: 1671
  ident: bib9
  article-title: Translation. An RNA biosensor for imaging the first round of translation from single cells to living animals
  publication-title: Science
  contributor:
    fullname: Chao
– volume: 13
  start-page: 897
  year: 2010
  end-page: 905
  ident: bib6
  article-title: In situ visualization and dynamics of newly synthesized proteins in rat hippocampal neurons
  publication-title: Nat. Neurosci.
  contributor:
    fullname: Schuman
– volume: 331
  start-page: 586
  year: 2011
  end-page: 589
  ident: bib32
  article-title: Translational pausing ensures membrane targeting and cytoplasmic splicing of XBP1u mRNA
  publication-title: Science
  contributor:
    fullname: Kohno
– volume: 352
  start-page: 1425
  year: 2016
  end-page: 1429
  ident: bib16
  article-title: Real-time quantification of single RNA translation dynamics in living cells
  publication-title: Science
  contributor:
    fullname: Looger
– volume: 324
  start-page: 218
  year: 2009
  end-page: 223
  ident: bib13
  article-title: Genome-wide analysis in vivo of translation with nucleotide resolution using ribosome profiling
  publication-title: Science
  contributor:
    fullname: Weissman
– volume: 159
  start-page: 635
  year: 2014
  end-page: 646
  ident: bib24
  article-title: A protein-tagging system for signal amplification in gene expression and fluorescence imaging
  publication-title: Cell
  contributor:
    fullname: Vale
– volume: 9
  start-page: 205
  year: 2009
  end-page: 209
  ident: bib19
  article-title: Global analysis of cellular protein translation by pulsed SILAC
  publication-title: Proteomics
  contributor:
    fullname: Selbach
– volume: 30
  start-page: 984
  year: 2012
  end-page: 990
  ident: bib7
  article-title: Selective enrichment of newly synthesized proteins for quantitative secretome analysis
  publication-title: Nat. Biotechnol.
  contributor:
    fullname: Krijgsveld
– volume: 1
  start-page: e27516
  year: 2013
  ident: bib1
  article-title: PUNCH-P for global translatome profiling: methodology, insights and comparison to other techniques
  publication-title: Translation (Austin)
  contributor:
    fullname: Elroy-Stein
– volume: 165
  start-page: 990
  year: 2016
  end-page: 1001
  ident: bib26
  article-title: Real-time imaging of translation on single mRNA transcripts in live cells
  publication-title: Cell
  contributor:
    fullname: Zhuang
– volume: 10
  start-page: 343
  year: 2013
  end-page: 346
  ident: bib12
  article-title: QuaNCAT: quantitating proteome dynamics in primary cells
  publication-title: Nat. Methods
  contributor:
    fullname: Dieterich
– volume: 147
  start-page: 789
  year: 2011
  end-page: 802
  ident: bib14
  article-title: Ribosome profiling of mouse embryonic stem cells reveals the complexity and dynamics of mammalian proteomes
  publication-title: Cell
  contributor:
    fullname: Weissman
– volume: 58
  start-page: 568
  year: 2015
  end-page: 574
  ident: bib23
  article-title: Expanding the biologist’s toolkit with CRISPR-Cas9
  publication-title: Mol. Cell
  contributor:
    fullname: Doudna
– volume: 136
  start-page: 731
  year: 2009
  end-page: 745
  ident: bib22
  article-title: Regulation of translation initiation in eukaryotes: mechanisms and biological targets
  publication-title: Cell
  contributor:
    fullname: Hinnebusch
– volume: 197
  start-page: 45
  year: 2012
  end-page: 57
  ident: bib4
  article-title: Nuclear translation visualized by ribosome-bound nascent chain puromycylation
  publication-title: J. Cell Biol.
  contributor:
    fullname: Yewdell
– volume: 9
  start-page: 1256
  year: 2014
  end-page: 1264
  ident: bib21
  article-title: An active role for the ribosome in determining the fate of oxidized mRNA
  publication-title: Cell Rep.
  contributor:
    fullname: Zaher
– volume: 72
  start-page: 323
  year: 1977
  end-page: 330
  ident: bib8
  article-title: Inhibition of translation in eukaryotic systems by harringtonine
  publication-title: Eur. J. Biochem.
  contributor:
    fullname: Vázquez
– volume: 103
  start-page: 9482
  year: 2006
  end-page: 9487
  ident: bib5
  article-title: Selective identification of newly synthesized proteins in mammalian cells using bioorthogonal noncanonical amino acid tagging (BONCAT)
  publication-title: Proc. Natl. Acad. Sci. USA
  contributor:
    fullname: Schuman
– volume: 106
  start-page: 13939
  year: 2009
  end-page: 13944
  ident: bib17
  article-title: Cell-type-specific isolation of ribosome-associated mRNA from complex tissues
  publication-title: Proc. Natl. Acad. Sci. USA
  contributor:
    fullname: Amieux
– volume: 346
  start-page: 748
  year: 2014
  end-page: 751
  ident: bib28
  article-title: Targeting and plasticity of mitochondrial proteins revealed by proximity-specific ribosome profiling
  publication-title: Science
  contributor:
    fullname: Weissman
– volume: 135
  start-page: 738
  year: 2008
  end-page: 748
  ident: bib10
  article-title: A translational profiling approach for the molecular characterization of CNS cell types
  publication-title: Cell
  contributor:
    fullname: Surmeier
– volume: 162
  start-page: 211
  year: 2015
  end-page: 220
  ident: bib29
  article-title: Quantifying protein-mRNA interactions in single live cells
  publication-title: Cell
  contributor:
    fullname: Singer
– volume: 165
  start-page: 976
  year: 2016
  end-page: 989
  ident: bib31
  article-title: Dynamics of translation of single mRNA molecules in vivo
  publication-title: Cell
  contributor:
    fullname: Tanenbaum
– volume: 261
  start-page: 13800
  year: 1986
  end-page: 13806
  ident: bib3
  article-title: Pulse-chase studies of the synthesis and intracellular transport of apolipoprotein B-100 in Hep G2 cells
  publication-title: J. Biol. Chem.
  contributor:
    fullname: Olofsson
– volume: 352
  start-page: 1430
  year: 2016
  end-page: 1435
  ident: bib30
  article-title: Translation dynamics of single mRNAs in live cells and neurons
  publication-title: Science
  contributor:
    fullname: Singer
– volume: 452
  start-page: 598
  year: 2008
  end-page: 603
  ident: bib27
  article-title: Following translation by single ribosomes one codon at a time
  publication-title: Nature
  contributor:
    fullname: Tinoco
– volume: 43
  start-page: 763
  year: 2015
  end-page: 772
  ident: bib20
  article-title: Signalling to eIF4E in cancer
  publication-title: Biochem. Soc. Trans.
  contributor:
    fullname: Sonenberg
– volume: 109
  start-page: E3350
  year: 2012
  end-page: E3357
  ident: bib11
  article-title: Inducible, reversible system for the rapid and complete degradation of proteins in mammalian cells
  publication-title: Proc. Natl. Acad. Sci. USA
  contributor:
    fullname: Cleveland
– volume: 136
  start-page: 731
  year: 2009
  ident: 10.1016/j.molcel.2016.08.031_bib22
  article-title: Regulation of translation initiation in eukaryotes: mechanisms and biological targets
  publication-title: Cell
  doi: 10.1016/j.cell.2009.01.042
  contributor:
    fullname: Sonenberg
– volume: 1
  start-page: e27516
  year: 2013
  ident: 10.1016/j.molcel.2016.08.031_bib1
  article-title: PUNCH-P for global translatome profiling: methodology, insights and comparison to other techniques
  publication-title: Translation (Austin)
  contributor:
    fullname: Aviner
– volume: 13
  start-page: 897
  year: 2010
  ident: 10.1016/j.molcel.2016.08.031_bib6
  article-title: In situ visualization and dynamics of newly synthesized proteins in rat hippocampal neurons
  publication-title: Nat. Neurosci.
  doi: 10.1038/nn.2580
  contributor:
    fullname: Dieterich
– volume: 347
  start-page: 1367
  year: 2015
  ident: 10.1016/j.molcel.2016.08.031_bib9
  article-title: Translation. An RNA biosensor for imaging the first round of translation from single cells to living animals
  publication-title: Science
  doi: 10.1126/science.aaa3380
  contributor:
    fullname: Halstead
– volume: 106
  start-page: 13939
  year: 2009
  ident: 10.1016/j.molcel.2016.08.031_bib17
  article-title: Cell-type-specific isolation of ribosome-associated mRNA from complex tissues
  publication-title: Proc. Natl. Acad. Sci. USA
  doi: 10.1073/pnas.0907143106
  contributor:
    fullname: Sanz
– volume: 162
  start-page: 211
  year: 2015
  ident: 10.1016/j.molcel.2016.08.031_bib29
  article-title: Quantifying protein-mRNA interactions in single live cells
  publication-title: Cell
  doi: 10.1016/j.cell.2015.05.054
  contributor:
    fullname: Wu
– volume: 261
  start-page: 13800
  year: 1986
  ident: 10.1016/j.molcel.2016.08.031_bib3
  article-title: Pulse-chase studies of the synthesis and intracellular transport of apolipoprotein B-100 in Hep G2 cells
  publication-title: J. Biol. Chem.
  doi: 10.1016/S0021-9258(18)67090-5
  contributor:
    fullname: Boström
– volume: 10
  start-page: 343
  year: 2013
  ident: 10.1016/j.molcel.2016.08.031_bib12
  article-title: QuaNCAT: quantitating proteome dynamics in primary cells
  publication-title: Nat. Methods
  doi: 10.1038/nmeth.2401
  contributor:
    fullname: Howden
– volume: 58
  start-page: 568
  year: 2015
  ident: 10.1016/j.molcel.2016.08.031_bib23
  article-title: Expanding the biologist’s toolkit with CRISPR-Cas9
  publication-title: Mol. Cell
  doi: 10.1016/j.molcel.2015.02.032
  contributor:
    fullname: Sternberg
– volume: 324
  start-page: 218
  year: 2009
  ident: 10.1016/j.molcel.2016.08.031_bib13
  article-title: Genome-wide analysis in vivo of translation with nucleotide resolution using ribosome profiling
  publication-title: Science
  doi: 10.1126/science.1168978
  contributor:
    fullname: Ingolia
– volume: 6
  start-page: 275
  year: 2009
  ident: 10.1016/j.molcel.2016.08.031_bib18
  article-title: SUnSET, a nonradioactive method to monitor protein synthesis
  publication-title: Nat. Methods
  doi: 10.1038/nmeth.1314
  contributor:
    fullname: Schmidt
– volume: 197
  start-page: 45
  year: 2012
  ident: 10.1016/j.molcel.2016.08.031_bib4
  article-title: Nuclear translation visualized by ribosome-bound nascent chain puromycylation
  publication-title: J. Cell Biol.
  doi: 10.1083/jcb.201112145
  contributor:
    fullname: David
– volume: 346
  start-page: 748
  year: 2014
  ident: 10.1016/j.molcel.2016.08.031_bib28
  article-title: Targeting and plasticity of mitochondrial proteins revealed by proximity-specific ribosome profiling
  publication-title: Science
  doi: 10.1126/science.1257522
  contributor:
    fullname: Williams
– volume: 9
  start-page: 1256
  year: 2014
  ident: 10.1016/j.molcel.2016.08.031_bib21
  article-title: An active role for the ribosome in determining the fate of oxidized mRNA
  publication-title: Cell Rep.
  doi: 10.1016/j.celrep.2014.10.042
  contributor:
    fullname: Simms
– volume: 9
  start-page: 205
  year: 2009
  ident: 10.1016/j.molcel.2016.08.031_bib19
  article-title: Global analysis of cellular protein translation by pulsed SILAC
  publication-title: Proteomics
  doi: 10.1002/pmic.200800275
  contributor:
    fullname: Schwanhäusser
– volume: 9
  start-page: 971
  year: 2008
  ident: 10.1016/j.molcel.2016.08.031_bib2
  article-title: Translational control of localized mRNAs: restricting protein synthesis in space and time
  publication-title: Nat. Rev. Mol. Cell Biol.
  doi: 10.1038/nrm2548
  contributor:
    fullname: Besse
– volume: 346
  start-page: 1257521
  year: 2014
  ident: 10.1016/j.molcel.2016.08.031_bib15
  article-title: Principles of ER cotranslational translocation revealed by proximity-specific ribosome profiling
  publication-title: Science
  doi: 10.1126/science.1257521
  contributor:
    fullname: Jan
– volume: 72
  start-page: 323
  year: 1977
  ident: 10.1016/j.molcel.2016.08.031_bib8
  article-title: Inhibition of translation in eukaryotic systems by harringtonine
  publication-title: Eur. J. Biochem.
  doi: 10.1111/j.1432-1033.1977.tb11256.x
  contributor:
    fullname: Fresno
– volume: 147
  start-page: 789
  year: 2011
  ident: 10.1016/j.molcel.2016.08.031_bib14
  article-title: Ribosome profiling of mouse embryonic stem cells reveals the complexity and dynamics of mammalian proteomes
  publication-title: Cell
  doi: 10.1016/j.cell.2011.10.002
  contributor:
    fullname: Ingolia
– volume: 12
  start-page: 411
  year: 2015
  ident: 10.1016/j.molcel.2016.08.031_bib25
  article-title: Direct visualization of newly synthesized target proteins in situ
  publication-title: Nat. Methods
  doi: 10.1038/nmeth.3319
  contributor:
    fullname: tom Dieck
– volume: 165
  start-page: 976
  year: 2016
  ident: 10.1016/j.molcel.2016.08.031_bib31
  article-title: Dynamics of translation of single mRNA molecules in vivo
  publication-title: Cell
  doi: 10.1016/j.cell.2016.04.034
  contributor:
    fullname: Yan
– volume: 352
  start-page: 1430
  year: 2016
  ident: 10.1016/j.molcel.2016.08.031_bib30
  article-title: Translation dynamics of single mRNAs in live cells and neurons
  publication-title: Science
  doi: 10.1126/science.aaf1084
  contributor:
    fullname: Wu
– volume: 352
  start-page: 1425
  year: 2016
  ident: 10.1016/j.molcel.2016.08.031_bib16
  article-title: Real-time quantification of single RNA translation dynamics in living cells
  publication-title: Science
  doi: 10.1126/science.aaf0899
  contributor:
    fullname: Morisaki
– volume: 331
  start-page: 586
  year: 2011
  ident: 10.1016/j.molcel.2016.08.031_bib32
  article-title: Translational pausing ensures membrane targeting and cytoplasmic splicing of XBP1u mRNA
  publication-title: Science
  doi: 10.1126/science.1197142
  contributor:
    fullname: Yanagitani
– volume: 103
  start-page: 9482
  year: 2006
  ident: 10.1016/j.molcel.2016.08.031_bib5
  article-title: Selective identification of newly synthesized proteins in mammalian cells using bioorthogonal noncanonical amino acid tagging (BONCAT)
  publication-title: Proc. Natl. Acad. Sci. USA
  doi: 10.1073/pnas.0601637103
  contributor:
    fullname: Dieterich
– volume: 135
  start-page: 738
  year: 2008
  ident: 10.1016/j.molcel.2016.08.031_bib10
  article-title: A translational profiling approach for the molecular characterization of CNS cell types
  publication-title: Cell
  doi: 10.1016/j.cell.2008.10.028
  contributor:
    fullname: Heiman
– volume: 109
  start-page: E3350
  year: 2012
  ident: 10.1016/j.molcel.2016.08.031_bib11
  article-title: Inducible, reversible system for the rapid and complete degradation of proteins in mammalian cells
  publication-title: Proc. Natl. Acad. Sci. USA
  doi: 10.1073/pnas.1216880109
  contributor:
    fullname: Holland
– volume: 452
  start-page: 598
  year: 2008
  ident: 10.1016/j.molcel.2016.08.031_bib27
  article-title: Following translation by single ribosomes one codon at a time
  publication-title: Nature
  doi: 10.1038/nature06716
  contributor:
    fullname: Wen
– volume: 159
  start-page: 635
  year: 2014
  ident: 10.1016/j.molcel.2016.08.031_bib24
  article-title: A protein-tagging system for signal amplification in gene expression and fluorescence imaging
  publication-title: Cell
  doi: 10.1016/j.cell.2014.09.039
  contributor:
    fullname: Tanenbaum
– volume: 43
  start-page: 763
  year: 2015
  ident: 10.1016/j.molcel.2016.08.031_bib20
  article-title: Signalling to eIF4E in cancer
  publication-title: Biochem. Soc. Trans.
  doi: 10.1042/BST20150126
  contributor:
    fullname: Siddiqui
– volume: 165
  start-page: 990
  year: 2016
  ident: 10.1016/j.molcel.2016.08.031_bib26
  article-title: Real-time imaging of translation on single mRNA transcripts in live cells
  publication-title: Cell
  doi: 10.1016/j.cell.2016.04.040
  contributor:
    fullname: Wang
– volume: 30
  start-page: 984
  year: 2012
  ident: 10.1016/j.molcel.2016.08.031_bib7
  article-title: Selective enrichment of newly synthesized proteins for quantitative secretome analysis
  publication-title: Nat. Biotechnol.
  doi: 10.1038/nbt.2356
  contributor:
    fullname: Eichelbaum
SSID ssj0014589
Score 2.3902395
SecondaryResourceType review_article
Snippet Translation is a fundamental biological process by which ribosomes decode genetic information into proteins. The regulation of this process plays a key role in...
SourceID proquest
crossref
pubmed
elsevier
SourceType Aggregation Database
Index Database
Publisher
StartPage 918
SubjectTerms Cell Line, Tumor
Fluorescent Dyes - chemistry
fluorescent protein
Humans
imaging
Mass Spectrometry - methods
Molecular Imaging - methods
mRNA localization
Protein Biosynthesis
Protein Synthesis Inhibitors - pharmacology
Recombinant Fusion Proteins - genetics
Recombinant Fusion Proteins - metabolism
Ribosomes - drug effects
Ribosomes - genetics
Ribosomes - metabolism
RNA, Messenger - genetics
RNA, Messenger - metabolism
Sequence Analysis, RNA
single cell
single molecule
Single-Cell Analysis - methods
Staining and Labeling - methods
translation
Title Eyes on Translation
URI https://dx.doi.org/10.1016/j.molcel.2016.08.031
https://www.ncbi.nlm.nih.gov/pubmed/27635758
https://search.proquest.com/docview/1820602818
Volume 63
hasFullText 1
inHoldings 1
isFullTextHit
isPrint
link http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1LawIxEB58UOiltPZlH2Kh12ASk008qij2ZQ-tRXoJ2WwWLO0qVQ_--yb7EHqQQo9ZNmz222HyZWfmG4BbaTXXAZXIYBwiZgKDNBMMWSlCIiMSS-t_DTyNg9GE3U_5tAT9ohbGp1Xmvj_z6am3zq-0cjRbi9ms9eJjp1QE3DEKLzETlKFKHft1xl7t9t4eHrfBBMbTTnj-fuQnFBV0aZrX1_zTWB-DIEGq5dkmu3aoXQw03YmGh3CQU8hmN1vlEZRsUoO9rKnk5hhqg41dNudJM92GslS3E5gMB6_9EcpbHyDDsFwhEcWO6vAwwpZE0mDnhCIuMHUQWmaYdsckTduMUsNC4uvZHRHphCbCWscUy7h9CpVknthzaArmzlzcsA4jPiobakoCLZyPM7Fw0LA6oOJ11SJTuFBF6teHyuBRHh7l-1W2SR1EgYn69aWUc8J_zLwpIFTOiH1kQid2vl6qVEUee2GqOpxl2G7XQlPJPC4v_v3cS9j3I5_lQfgVVFbfa3vtqMQqbOSm0oDy3bTnRuP-9Pn9Bwqyxeo
link.rule.ids 315,783,787,3515,27583,27938,27939,45677,45888
linkProvider Elsevier
linkToHtml http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1JTwIxGP2CEKMXo7jhionXhra003JEIkFZLoLh1nQ6nQSjAxE48O9tZyHxQEy8zkwzndfmfa_zbQCP0mquAyqRwThEzAQGaSYYslKEREYkltb_GhiOgt6EvU75tASdIhfGh1Xm3J9xesrW-ZVGjmZjMZs13rzvlIqAO0XhS8wEe1BxakC4E1il_fTeH2ydCYynnfD888gPKDLo0jCvr_mnsd4HQYK0lmeT7LJQuxRoaom6x3CUS8h6O5vlCZRsUoX9rKnk5hSqzxu7rM-TemqGslC3M5h0n8edHspbHyDDsFwhEcVO6vAwwpZE0mBHQhEXmDoILTNMu2OSpk1GqWEh8fnsToi0QhNhrWOKZdw8h3IyT-wl1AVzZy5uWIsR75UNNSWBFo7jTCwcNKwGqPhctcgqXKgi9OtDZfAoD4_y_SqbpAaiwET9WinlSPiPkQ8FhMptYu-Z0Imdr5cqrSKPfWGqGlxk2G7nQtOSeVxe_fu993DQGw8HavAy6l_Dob_jIz4Iv4Hy6nttb52sWIV3-bb5AZwmxh8
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=Eyes+on+Translation&rft.jtitle=Molecular+cell&rft.au=Chekulaeva%2C+Marina&rft.au=Landthaler%2C+Markus&rft.date=2016-09-15&rft.eissn=1097-4164&rft.volume=63&rft.issue=6&rft.spage=918&rft.epage=925&rft_id=info:doi/10.1016%2Fj.molcel.2016.08.031&rft.externalDBID=NO_FULL_TEXT
thumbnail_l http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=1097-2765&client=summon
thumbnail_m http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=1097-2765&client=summon
thumbnail_s http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=1097-2765&client=summon