Cloning, sequencing and expression of ribonucleotide reductase R2 from Trypanosoma brucei

Ribonucleotide reductase (RR) is an attractive drug target molecule. The gene of the R2 protein of Trypanosoma brucei RR ( nrd B) has been cloned. It encodes a protein of 337 residues which shows about 60% identity with other eukaryotic R2 proteins. All residues which bind the iron center, the tyros...

Full description

Saved in:
Bibliographic Details
Published inFEBS letters Vol. 414; no. 2; pp. 449 - 453
Main Authors Dormeyer, Matthias, Schöneck, Ralf, Dittmar, Gunnar A.G., Krauth-Siegel, R. Luise
Format Journal Article
LanguageEnglish
Published England Elsevier B.V 08.09.1997
Subjects
Online AccessGet full text

Cover

Loading…
Abstract Ribonucleotide reductase (RR) is an attractive drug target molecule. The gene of the R2 protein of Trypanosoma brucei RR ( nrd B) has been cloned. It encodes a protein of 337 residues which shows about 60% identity with other eukaryotic R2 proteins. All residues which bind the iron center, the tyrosyl radical or are supposed to participate in the radical transfer are conserved in the trypanosomal protein sequence. Overexpression of the gene in E. coli resulted in 2–5 mg pure R2 protein from 100 ml bacterial cell culture. Northern blot analysis revealed a transcript of 1.85 kb in bloodstream and procyclic forms of the parasite.
AbstractList Ribonucleotide reductase (RR) is an attractive drug target molecule. The gene of the R2 protein of Trypanosoma brucei RR (nrd B) has been cloned. It encodes a protein of 337 residues which shows about 60% identity with other eukaryotic R2 proteins. All residues which bind the iron center, the tyrosyl radical or are supposed to participate in the radical transfer are conserved in the trypanosomal protein sequence. Overexpression of the gene in E. coli resulted in 2-5 mg pure R2 protein from 100 ml bacterial cell culture. Northern blot analysis revealed a transcript of 1.85 kb in bloodstream and procyclic forms of the parasite.
Ribonucleotide reductase (RR) is an attractive drug target molecule. The gene of the R2 protein of Trypanosoma brucei RR ( nrd B) has been cloned. It encodes a protein of 337 residues which shows about 60% identity with other eukaryotic R2 proteins. All residues which bind the iron center, the tyrosyl radical or are supposed to participate in the radical transfer are conserved in the trypanosomal protein sequence. Overexpression of the gene in E. coli resulted in 2–5 mg pure R2 protein from 100 ml bacterial cell culture. Northern blot analysis revealed a transcript of 1.85 kb in bloodstream and procyclic forms of the parasite.
Ribonucleotide reductase (RR) is an attractive drug target molecule. The gene of the R2 protein of Trypanosoma brucei RR ( nrd B ) has been cloned. It encodes a protein of 337 residues which shows about 60% identity with other eukaryotic R2 proteins. All residues which bind the iron center, the tyrosyl radical or are supposed to participate in the radical transfer are conserved in the trypanosomal protein sequence. Overexpression of the gene in E. coli resulted in 2–5 mg pure R2 protein from 100 ml bacterial cell culture. Northern blot analysis revealed a transcript of 1.85 kb in bloodstream and procyclic forms of the parasite.
Author Krauth-Siegel, R. Luise
Dittmar, Gunnar A.G.
Dormeyer, Matthias
Schöneck, Ralf
Author_xml – sequence: 1
  givenname: Matthias
  surname: Dormeyer
  fullname: Dormeyer, Matthias
  organization: Biochemie-Zentrum Heidelberg, Ruprecht-Karls-Universität, Im Neuenheimer Feld 328, D-69120 Heidelberg, Germany
– sequence: 2
  givenname: Ralf
  surname: Schöneck
  fullname: Schöneck, Ralf
  organization: Biochemie-Zentrum Heidelberg, Ruprecht-Karls-Universität, Im Neuenheimer Feld 328, D-69120 Heidelberg, Germany
– sequence: 3
  givenname: Gunnar A.G.
  surname: Dittmar
  fullname: Dittmar, Gunnar A.G.
  organization: Abteilung Biochemie der Zelle, Deutsches Krebsforschungszentrum, Im Neuenheimer Feld 280, D-69120 Heidelberg, Germany
– sequence: 4
  givenname: R. Luise
  surname: Krauth-Siegel
  fullname: Krauth-Siegel, R. Luise
  email: krauth-siegel@novsrv1.pio1.uni-heidelberg.de
  organization: Biochemie-Zentrum Heidelberg, Ruprecht-Karls-Universität, Im Neuenheimer Feld 328, D-69120 Heidelberg, Germany
BackLink https://www.ncbi.nlm.nih.gov/pubmed/9315738$$D View this record in MEDLINE/PubMed
BookMark eNqNkV1vFCEUhompqdvqT2jClR-Jo3wMMFw1ummtSRMTrRdeEQbOGMwMrLCj7r-X2d300noF57wv7wGeM3QSUwSELih5QwmVb78QQttGKM1favWKUMJlwx-hFe0Ub3gruxO0urc8QWel_CC17qg-RaeaU6F4t0Lf1mOKIX5_jQv8nCG6usc2egx_NhlKCSniNOAc-hRnN0LaBg84g5_d1hbAnxkecprwXd5tbEwlTRb3eXYQnqLHgx0LPDuu5-jr9dXd-qa5_fTh4_rdbeMEF7yR3AunKefWCSeFs1SrviWtE6JXnjFGve2tIu0gaiEZ8Uz3Q8sdVS1hwvJz9OKQu8mpvqBszRSKg3G0EdJcTKck41JqUp3P_-ms_8SIaPmDRloTqdKyGsXB6HIqJcNgNjlMNu8MJWahZPaUzILAaGX2lMwy4OI4YO4n8PenjliqfnPQf4cRdv8Xaq6v3rO9sgha7dvLqMtDFFQGvwJkU1yonMGHDG5rfAoPXPYv1Im2Sg
CitedBy_id crossref_primary_10_1016_S0014_5793_98_00793_5
crossref_primary_10_1074_jbc_275_11_7547
crossref_primary_10_1017_S0031182009991880
crossref_primary_10_1515_BC_2003_062
crossref_primary_10_1016_S0020_7519_01_00310_1
crossref_primary_10_1016_j_cbpb_2017_07_001
crossref_primary_10_3390_molecules27196574
crossref_primary_10_3390_antiox12050984
crossref_primary_10_1007_s00239_013_9583_y
crossref_primary_10_1016_S0006_2952_98_00324_4
crossref_primary_10_1017_S0031182007003046
crossref_primary_10_1074_jbc_M010352200
crossref_primary_10_1016_S0014_5793_00_01533_7
crossref_primary_10_1099_0022_1317_81_2_307
Cites_doi 10.1021/bi00135a009
10.1093/emboj/16.10.2590
10.1002/(SICI)1097-0134(199601)24:1<73::AID-PROT5>3.0.CO;2-P
10.1007/978-3-642-79488-9_10
10.1021/bi00013a016
10.1016/S0968-0004(97)01003-7
10.1016/0166-6851(96)02675-8
10.1111/j.1550-7408.1980.tb04241.x
10.3109/10425179209020807
10.1016/0166-6851(94)90080-9
10.1016/S0021-9258(18)71625-6
10.1016/S0021-9258(18)89423-6
10.1128/MCB.6.10.3433
10.1146/annurev.mi.46.100192.003403
10.1006/jmbi.1996.0546
10.1016/0014-5793(90)80449-S
10.1096/fasebj.9.12.7672506
10.1042/bst0110366
10.1111/j.1432-1033.1997.00739.x
10.1016/1074-5521(95)90084-5
10.1038/372695a0
10.1093/nar/24.15.2942
10.1007/BFb0111318
10.1038/345593a0
10.1146/annurev.bi.55.070186.003413
ContentType Journal Article
Copyright 1997 Federation of European Biochemical Societies. All rights reserved.
FEBS Letters 414 (1997) 1873-3468 © 2015 Federation of European Biochemical Societies
Copyright_xml – notice: 1997 Federation of European Biochemical Societies. All rights reserved.
– notice: FEBS Letters 414 (1997) 1873-3468 © 2015 Federation of European Biochemical Societies
DBID 6I.
AAFTH
CGR
CUY
CVF
ECM
EIF
NPM
AAYXX
CITATION
7TM
8FD
FR3
M7N
P64
RC3
7X8
7ST
C1K
SOI
DOI 10.1016/S0014-5793(97)01036-3
DatabaseName ScienceDirect Open Access Titles
Elsevier:ScienceDirect:Open Access
Medline
MEDLINE
MEDLINE (Ovid)
MEDLINE
MEDLINE
PubMed
CrossRef
Nucleic Acids Abstracts
Technology Research Database
Engineering Research Database
Algology Mycology and Protozoology Abstracts (Microbiology C)
Biotechnology and BioEngineering Abstracts
Genetics Abstracts
MEDLINE - Academic
Environment Abstracts
Environmental Sciences and Pollution Management
Environment Abstracts
DatabaseTitle MEDLINE
Medline Complete
MEDLINE with Full Text
PubMed
MEDLINE (Ovid)
CrossRef
Genetics Abstracts
Engineering Research Database
Technology Research Database
Algology Mycology and Protozoology Abstracts (Microbiology C)
Nucleic Acids Abstracts
Biotechnology and BioEngineering Abstracts
MEDLINE - Academic
Environment Abstracts
Environmental Sciences and Pollution Management
DatabaseTitleList Genetics Abstracts
Environment Abstracts
MEDLINE - Academic


CrossRef
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 Anatomy & Physiology
Chemistry
Biology
EISSN 1873-3468
EndPage 453
ExternalDocumentID 10_1016_S0014_5793_97_01036_3
9315738
FEB2S0014579397010363
S0014579397010363
Genre article
Research Support, Non-U.S. Gov't
Journal Article
Comparative Study
GroupedDBID ---
--K
-~X
.55
.~1
0R~
0SF
1B1
1OC
1~.
1~5
24P
29H
2WC
33P
4.4
4G.
53G
5GY
5RE
5VS
6I.
7-5
71M
8P~
AABNK
AACTN
AAEDW
AAESR
AAFTH
AAHHS
AAIKJ
AAJUZ
AALRI
AANLZ
AAQFI
AAQXK
AASGY
AAXRX
AAXUO
AAZKR
ABBQC
ABCUV
ABEFU
ABFNM
ABFRF
ABGSF
ABHUG
ABJNI
ABLJU
ABMAC
ABQWH
ABVKL
ABXDB
ABXGK
ACAHQ
ACCFJ
ACCZN
ACGFO
ACGFS
ACGOF
ACIUM
ACMXC
ACNCT
ACPOU
ACXBN
ACXQS
ADAWD
ADBBV
ADBTR
ADDAD
ADEOM
ADEZE
ADIYS
ADKYN
ADMGS
ADMUD
ADOZA
ADQTV
ADUVX
ADXAS
ADZMN
ADZOD
AEEZP
AEFWE
AEGXH
AEKER
AENEX
AEQDE
AEQOU
AEUQT
AEUYR
AEXQZ
AFBPY
AFFNX
AFFPM
AFGKR
AFPWT
AFVGU
AFZJQ
AGHFR
AGJLS
AGYEJ
AHBTC
AHPSJ
AI.
AIACR
AIAGR
AITUG
AIURR
AIWBW
AJBDE
AJRQY
ALMA_UNASSIGNED_HOLDINGS
AMRAJ
AMYDB
AZFZN
AZVAB
BAWUL
BFHJK
BMXJE
C45
CBWCG
CS3
DCZOG
DIK
DOVZS
DRFUL
DRMAN
DRSTM
DU5
E3Z
EBS
EJD
EMOBN
EO8
EO9
EP2
EP3
F5P
FDB
FEDTE
FGOYB
FIRID
FNPLU
FUBAC
G-Q
GBLVA
GI5
GX1
HVGLF
HZ~
IHE
IXB
J1W
KBYEO
L7B
LATKE
LCYCR
LEEKS
LITHE
LOXES
LUTES
LX3
LYRES
M41
MEWTI
MO0
MRFUL
MRMAN
MRSTM
MSFUL
MSMAN
MSSTM
MVM
MXFUL
MXMAN
MXSTM
N9A
NCXOZ
O-L
O9-
OK1
OVD
OZT
P-8
P-9
P2P
P2W
PC.
Q38
R2-
R9-
RIG
RNS
ROL
RPZ
SCC
SDF
SDG
SDP
SEL
SES
SEW
SFE
SSZ
SUPJJ
SV3
TEORI
TR2
UHB
UNMZH
VH1
WBKPD
WH7
WIH
WIJ
WIK
WIN
WOHZO
WXSBR
X7M
XFK
Y6R
YK3
ZA5
ZGI
ZZTAW
~02
AAHBH
ADVLN
AITYG
AKRWK
ALUQN
HGLYW
CGR
CUY
CVF
ECM
EIF
NPM
AAYXX
CITATION
7TM
8FD
FR3
M7N
P64
RC3
7X8
7ST
C1K
SOI
ID FETCH-LOGICAL-c5353-63d5c9133ac5c65ca197b404c55b7d2221daba704f5222620d29bf43c174025a3
IEDL.DBID ABVKL
ISSN 0014-5793
IngestDate Thu Aug 15 22:41:39 EDT 2024
Sat Aug 17 03:04:02 EDT 2024
Fri Aug 16 10:04:28 EDT 2024
Fri Aug 23 03:10:11 EDT 2024
Sat Sep 28 08:36:59 EDT 2024
Sat Aug 24 00:57:06 EDT 2024
Fri Feb 23 02:16:31 EST 2024
IsDoiOpenAccess true
IsOpenAccess true
IsPeerReviewed true
IsScholarly true
Issue 2
Keywords RR
R2
nrd B
Ribonucleotide reductase
Drug target
IPTG
T.b
Trypanosoma brucei
Trypanothione
Ni-NTA
R1
Language English
License http://www.elsevier.com/open-access/userlicense/1.0
LinkModel DirectLink
MergedId FETCHMERGED-LOGICAL-c5353-63d5c9133ac5c65ca197b404c55b7d2221daba704f5222620d29bf43c174025a3
Notes ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-1
content type line 23
ObjectType-Article-1
ObjectType-Feature-2
OpenAccessLink https://www.sciencedirect.com/science/article/pii/S0014579397010363
PMID 9315738
PQID 16231796
PQPubID 23462
PageCount 5
ParticipantIDs proquest_miscellaneous_876236690
proquest_miscellaneous_79320543
proquest_miscellaneous_16231796
crossref_primary_10_1016_S0014_5793_97_01036_3
pubmed_primary_9315738
wiley_primary_10_1016_S0014_5793_97_01036_3_FEB2S0014579397010363
elsevier_sciencedirect_doi_10_1016_S0014_5793_97_01036_3
PublicationCentury 1900
PublicationDate September 08, 1997
PublicationDateYYYYMMDD 1997-09-08
PublicationDate_xml – month: 09
  year: 1997
  text: September 08, 1997
  day: 08
PublicationDecade 1990
PublicationPlace England
PublicationPlace_xml – name: England
PublicationTitle FEBS letters
PublicationTitleAlternate FEBS Lett
PublicationYear 1997
Publisher Elsevier B.V
Publisher_xml – name: Elsevier B.V
References Thelander, Berg (bib10) 1986; 6
Rova, Goodtzova, Ingemarson, Behravan, Gräslund, Thelander (bib16) 1995; 34
Lammers, Follmann (bib3) 1983; 54
Fricker, Klein (bib18) 1983; 11
Dumas, Ouellette, Tovar, Cunningham, Fairlamb, Tamar, Olivier, Papadopoulou (bib28) 1997; 16
Carlson, Fuchs, Messing (bib12) 1984; 81
Chakrabarti, Schuster, Chakrabarti (bib11) 1993; 90
Hofer, Schmidt, Gräslund, Thelander (bib29) 1997; 94
Liuzzi, Déziel, Moss, Beaulieu, Bonneau, Bousquet, Chafouleas, Garneau, Jaramillo, Krogsrud, Lagacé, McCollum, Nawoot, Guindon (bib21) 1994; 372
Tovar, Fairlamb (bib27) 1996; 24
Reichard (bib5) 1997; 22
Holmgren (bib4) 1989; 264
Sjöberg (bib7) 1995; vol. 9
Kauppi, Nielsen, Ramaswamy, Kjøller Larsen, Thelander, Thelander, Eklund (bib14) 1996; 262
Schöneck, Billaut-Mulot, Numrich, Ouaissi, Krauth-Siegel (bib24) 1997; 243
Jacoby, Schlichting, Lantwin, Kabsch, Krauth-Siegel (bib26) 1996; 24
Nordlund, Sjöberg, Eklund (bib13) 1990; 345
Brun (bib17) 1980; 27
Yang, Spanevello, Celiker, Hirschmann, Rubin, Cooperman (bib20) 1990; 272
Mutomba, Wang (bib19) 1996; 80
Thelander, Gräslund, Thelander (bib23) 1985; 260
Borst (bib8) 1986; 55
Krauth-Siegel, Schöneck (bib2) 1995; 9
Stubbe, van der Donk (bib6) 1995; 2
Rubin, Salem, Li, Yang, Mama, Wang, Fisher, Hamann, Cooperman (bib22) 1993; 90
Pavloff, Rivard, Masson, Shen, Mes-Masson (bib9) 1992; 2
Priest, Hajduk (bib25) 1994; 65
Fairlamb, Cerami (bib1) 1992; 46
Climent, Sjöberg, Huang (bib15) 1992; 31
1995; 9
1980; 27
1984; 81
1990; 345
1997; 22
1986; 55
1994; 372
1995; 34
1983; 54
1993; 90
1996; 262
1995; 2
1992; 31
1985; 260
1983; 11
1994; 65
1997; 94
1989; 264
1997; 243
1986; 6
1997; 16
1992; 46
1996; 80
1996; 24
1992; 2
1990; 272
e_1_2_1_20_1
e_1_2_1_23_1
e_1_2_1_24_1
e_1_2_1_21_1
e_1_2_1_22_1
e_1_2_1_27_1
e_1_2_1_28_1
e_1_2_1_25_1
e_1_2_1_26_1
e_1_2_1_29_1
e_1_2_1_7_1
e_1_2_1_8_1
e_1_2_1_30_1
e_1_2_1_5_1
e_1_2_1_6_1
e_1_2_1_3_1
e_1_2_1_12_1
e_1_2_1_4_1
e_1_2_1_13_1
e_1_2_1_10_1
e_1_2_1_2_1
e_1_2_1_11_1
e_1_2_1_16_1
e_1_2_1_17_1
e_1_2_1_14_1
e_1_2_1_15_1
e_1_2_1_9_1
e_1_2_1_18_1
e_1_2_1_19_1
References_xml – volume: 2
  start-page: 793
  year: 1995
  end-page: 801
  ident: bib6
  publication-title: Chem. Biol.
  contributor:
    fullname: van der Donk
– volume: 81
  start-page: 4294
  year: 1984
  end-page: 4297
  ident: bib12
  publication-title: Proc. Natl. Acad. Sci. USA
  contributor:
    fullname: Messing
– volume: 80
  start-page: 89
  year: 1996
  end-page: 102
  ident: bib19
  publication-title: Mol. Biochem. Parasitol.
  contributor:
    fullname: Wang
– volume: 243
  start-page: 739
  year: 1997
  end-page: 747
  ident: bib24
  publication-title: Eur. J. Biochem.
  contributor:
    fullname: Krauth-Siegel
– volume: 24
  start-page: 2942
  year: 1996
  end-page: 2949
  ident: bib27
  publication-title: Nucleic Acids Res.
  contributor:
    fullname: Fairlamb
– volume: 16
  start-page: 2590
  year: 1997
  end-page: 2598
  ident: bib28
  publication-title: EMBO J.
  contributor:
    fullname: Papadopoulou
– volume: 260
  start-page: 2737
  year: 1985
  end-page: 2741
  ident: bib23
  publication-title: J. Biol. Chem.
  contributor:
    fullname: Thelander
– volume: 262
  start-page: 706
  year: 1996
  end-page: 720
  ident: bib14
  publication-title: J. Mol. Biol.
  contributor:
    fullname: Eklund
– volume: 6
  start-page: 3433
  year: 1986
  end-page: 3442
  ident: bib10
  publication-title: Mol. Cell. Biol.
  contributor:
    fullname: Berg
– volume: 31
  start-page: 4801
  year: 1992
  end-page: 4807
  ident: bib15
  publication-title: Biochemistry
  contributor:
    fullname: Huang
– volume: 9
  start-page: 1138
  year: 1995
  end-page: 1146
  ident: bib2
  publication-title: FASEB J.
  contributor:
    fullname: Schöneck
– volume: 55
  start-page: 701
  year: 1986
  end-page: 732
  ident: bib8
  publication-title: Ann. Rev. Biochem.
  contributor:
    fullname: Borst
– volume: 27
  start-page: 122
  year: 1980
  end-page: 128
  ident: bib17
  publication-title: J. Protozool.
  contributor:
    fullname: Brun
– volume: 22
  start-page: 81
  year: 1997
  end-page: 85
  ident: bib5
  publication-title: Trends Biochem. Sci.
  contributor:
    fullname: Reichard
– volume: 272
  start-page: 61
  year: 1990
  end-page: 64
  ident: bib20
  publication-title: FEBS Lett.
  contributor:
    fullname: Cooperman
– volume: 24
  start-page: 73
  year: 1996
  end-page: 80
  ident: bib26
  publication-title: Proteins
  contributor:
    fullname: Krauth-Siegel
– volume: 94
  start-page: 6959
  year: 1997
  end-page: 6964
  ident: bib29
  publication-title: Proc. Natl. Acad. Sci. USA
  contributor:
    fullname: Thelander
– volume: 65
  start-page: 291
  year: 1994
  end-page: 304
  ident: bib25
  publication-title: Mol. Biochem. Parasitol.
  contributor:
    fullname: Hajduk
– volume: 46
  start-page: 695
  year: 1992
  end-page: 729
  ident: bib1
  publication-title: Ann. Rev. Microbiol.
  contributor:
    fullname: Cerami
– volume: 54
  start-page: 27
  year: 1983
  end-page: 91
  ident: bib3
  publication-title: Structure and Bonding
  contributor:
    fullname: Follmann
– volume: 2
  start-page: 227
  year: 1992
  end-page: 234
  ident: bib9
  publication-title: DNA Seq.
  contributor:
    fullname: Mes-Masson
– volume: 372
  start-page: 695
  year: 1994
  end-page: 698
  ident: bib21
  publication-title: Nature
  contributor:
    fullname: Guindon
– volume: 90
  start-page: 12020
  year: 1993
  end-page: 12024
  ident: bib11
  publication-title: Proc. Natl. Acad. Sci.
  contributor:
    fullname: Chakrabarti
– volume: 34
  start-page: 4267
  year: 1995
  end-page: 4275
  ident: bib16
  publication-title: Biochem.
  contributor:
    fullname: Thelander
– volume: 264
  start-page: 13963
  year: 1989
  end-page: 13966
  ident: bib4
  publication-title: J. Biol. Chem.
  contributor:
    fullname: Holmgren
– volume: vol. 9
  start-page: 192
  year: 1995
  end-page: 221
  ident: bib7
  publication-title: Nucleic Acids and Molecular Biology
  contributor:
    fullname: Sjöberg
– volume: 345
  start-page: 593
  year: 1990
  end-page: 598
  ident: bib13
  publication-title: Nature
  contributor:
    fullname: Eklund
– volume: 90
  start-page: 9280
  year: 1993
  end-page: 9284
  ident: bib22
  publication-title: Proc. Natl. Acad. Sci. USA
  contributor:
    fullname: Cooperman
– volume: 11
  start-page: 366
  year: 1983
  end-page: 367
  ident: bib18
  publication-title: Biochem. Soc. Trans.
  contributor:
    fullname: Klein
– volume: 9
  start-page: 192
  year: 1995
  end-page: 221
– volume: 2
  start-page: 227
  year: 1992
  end-page: 234
  publication-title: DNA Seq.
– volume: 6
  start-page: 3433
  year: 1986
  end-page: 3442
  publication-title: Mol. Cell. Biol.
– volume: 34
  start-page: 4267
  year: 1995
  end-page: 4275
  publication-title: Biochem.
– volume: 80
  start-page: 89
  year: 1996
  end-page: 102
  publication-title: Mol. Biochem. Parasitol.
– volume: 243
  start-page: 739
  year: 1997
  end-page: 747
  publication-title: Eur. J. Biochem.
– volume: 264
  start-page: 13963
  year: 1989
  end-page: 13966
  publication-title: J. Biol. Chem.
– volume: 260
  start-page: 2737
  year: 1985
  end-page: 2741
  publication-title: J. Biol. Chem.
– volume: 90
  start-page: 9280
  year: 1993
  end-page: 9284
– volume: 27
  start-page: 122
  year: 1980
  end-page: 128
  publication-title: J. Protozool.
– volume: 272
  start-page: 61
  year: 1990
  end-page: 64
  publication-title: FEBS Lett.
– volume: 24
  start-page: 73
  year: 1996
  end-page: 80
  publication-title: Proteins
– volume: 22
  start-page: 81
  year: 1997
  end-page: 85
  publication-title: Trends Biochem. Sci.
– volume: 372
  start-page: 695
  year: 1994
  end-page: 698
  publication-title: Nature
– volume: 262
  start-page: 706
  year: 1996
  end-page: 720
  publication-title: J. Mol. Biol.
– volume: 65
  start-page: 291
  year: 1994
  end-page: 304
  publication-title: Mol. Biochem. Parasitol.
– volume: 24
  start-page: 2942
  year: 1996
  end-page: 2949
  publication-title: Nucleic Acids Res.
– volume: 16
  start-page: 2590
  year: 1997
  end-page: 2598
  publication-title: EMBO J.
– volume: 9
  start-page: 1138
  year: 1995
  end-page: 1146
  publication-title: FASEB J.
– volume: 94
  start-page: 6959
  year: 1997
  end-page: 6964
– volume: 345
  start-page: 593
  year: 1990
  end-page: 598
  publication-title: Nature
– volume: 31
  start-page: 4801
  year: 1992
  end-page: 4807
  publication-title: Biochemistry
– volume: 90
  start-page: 12020
  year: 1993
  end-page: 12024
– volume: 11
  start-page: 366
  year: 1983
  end-page: 367
  publication-title: Biochem. Soc. Trans.
– volume: 2
  start-page: 793
  year: 1995
  end-page: 801
  publication-title: Chem. Biol.
– volume: 46
  start-page: 695
  year: 1992
  end-page: 729
  publication-title: Ann. Rev. Microbiol.
– volume: 81
  start-page: 4294
  year: 1984
  end-page: 4297
– volume: 55
  start-page: 701
  year: 1986
  end-page: 732
  publication-title: Ann. Rev. Biochem.
– volume: 54
  start-page: 27
  year: 1983
  end-page: 91
  publication-title: Structure and Bonding
– ident: e_1_2_1_16_1
  doi: 10.1021/bi00135a009
– ident: e_1_2_1_29_1
  doi: 10.1093/emboj/16.10.2590
– ident: e_1_2_1_27_1
  doi: 10.1002/(SICI)1097-0134(199601)24:1<73::AID-PROT5>3.0.CO;2-P
– ident: e_1_2_1_8_1
  doi: 10.1007/978-3-642-79488-9_10
– ident: e_1_2_1_17_1
  doi: 10.1021/bi00013a016
– ident: e_1_2_1_6_1
  doi: 10.1016/S0968-0004(97)01003-7
– ident: e_1_2_1_20_1
  doi: 10.1016/0166-6851(96)02675-8
– ident: e_1_2_1_18_1
  doi: 10.1111/j.1550-7408.1980.tb04241.x
– ident: e_1_2_1_23_1
– ident: e_1_2_1_10_1
  doi: 10.3109/10425179209020807
– ident: e_1_2_1_26_1
  doi: 10.1016/0166-6851(94)90080-9
– ident: e_1_2_1_5_1
  doi: 10.1016/S0021-9258(18)71625-6
– ident: e_1_2_1_24_1
  doi: 10.1016/S0021-9258(18)89423-6
– ident: e_1_2_1_11_1
  doi: 10.1128/MCB.6.10.3433
– ident: e_1_2_1_12_1
– ident: e_1_2_1_2_1
  doi: 10.1146/annurev.mi.46.100192.003403
– ident: e_1_2_1_15_1
  doi: 10.1006/jmbi.1996.0546
– ident: e_1_2_1_21_1
  doi: 10.1016/0014-5793(90)80449-S
– ident: e_1_2_1_3_1
  doi: 10.1096/fasebj.9.12.7672506
– ident: e_1_2_1_19_1
  doi: 10.1042/bst0110366
– ident: e_1_2_1_25_1
  doi: 10.1111/j.1432-1033.1997.00739.x
– ident: e_1_2_1_7_1
  doi: 10.1016/1074-5521(95)90084-5
– ident: e_1_2_1_22_1
  doi: 10.1038/372695a0
– ident: e_1_2_1_28_1
  doi: 10.1093/nar/24.15.2942
– ident: e_1_2_1_30_1
– ident: e_1_2_1_13_1
– ident: e_1_2_1_4_1
  doi: 10.1007/BFb0111318
– ident: e_1_2_1_14_1
  doi: 10.1038/345593a0
– ident: e_1_2_1_9_1
  doi: 10.1146/annurev.bi.55.070186.003413
SSID ssj0001819
Score 1.6775588
Snippet Ribonucleotide reductase (RR) is an attractive drug target molecule. The gene of the R2 protein of Trypanosoma brucei RR ( nrd B) has been cloned. It encodes a...
Ribonucleotide reductase (RR) is an attractive drug target molecule. The gene of the R2 protein of Trypanosoma brucei RR (nrd B) has been cloned. It encodes a...
Ribonucleotide reductase (RR) is an attractive drug target molecule. The gene of the R2 protein of Trypanosoma brucei RR ( nrd B ) has been cloned. It encodes...
SourceID proquest
crossref
pubmed
wiley
elsevier
SourceType Aggregation Database
Index Database
Publisher
StartPage 449
SubjectTerms Amino Acid Sequence
Animals
Cloning, Molecular
DNA, Complementary
DNA, Protozoan - chemistry
Drug target
Escherichia coli
Escherichia coli - enzymology
Genes, Protozoan
Humans
Mice
Molecular Sequence Data
Plasmodium falciparum - enzymology
Recombinant Proteins - biosynthesis
Recombinant Proteins - chemistry
Ribonucleotide reductase
Ribonucleotide Reductases - biosynthesis
Ribonucleotide Reductases - chemistry
Ribonucleotide Reductases - genetics
Sequence Alignment
Sequence Homology, Amino Acid
Trypanosoma brucei
Trypanosoma brucei brucei - enzymology
Trypanosoma brucei brucei - genetics
Trypanothione
Title Cloning, sequencing and expression of ribonucleotide reductase R2 from Trypanosoma brucei
URI https://dx.doi.org/10.1016/S0014-5793(97)01036-3
https://onlinelibrary.wiley.com/doi/abs/10.1016%2FS0014-5793%2897%2901036-3
https://www.ncbi.nlm.nih.gov/pubmed/9315738
https://search.proquest.com/docview/16231796
https://search.proquest.com/docview/79320543
https://search.proquest.com/docview/876236690
Volume 414
hasFullText 1
inHoldings 1
isFullTextHit
isPrint
link http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV3daxQxEB_6geiL1NbiqW3zIKLgtrubj7083h09qic-lFbPp5CvhQW7W65XsC_-7U6yuy2lHEqfNoQkbDKTmd8kMxOAd3ooS-8Klhjtw9FNKRItnA02j_c5Rw3oo7fFN3Fyzr7M-XwNJn0sTHCr7GR_K9OjtO5qjrrVPLqsqhDjmzGO7CWL8FaBoOuwmSP6xd25ORp_n329FcioxFoUnLEkdLgL5GkHiZUfZPExjpPQVSrqIQS9j2ijSppuwfMOS5JR-7svYM3X27AzqtGOvrgh70n07ozH5tvwZNyXnk76N9524OfkVzyO_UQ6l2osE1074n93DrI1aUqyqExTh8THzbJynixCutclqj9ympMQn0LOFjcoVZqr5kITE7ilegnn0-OzyUnSPbaQWE45TQR13Eq0WLXlVnCrM1kYljLLuSkcoojMaaOLlJWI2EIWe5dLUzJq0aRB3KTpLmzUTe1fAUmNLQ0aRt4Zw2hqTOpDAK3PuC8ZGlADOOzXV122OTXUnbMZEkQFgqhwMx4IougAhj0V1D3mUCj3_9X1oKeawrUNtyG69s31lcoQ-KE0Eqtb4Eg5Ilocg6xoEVQJFUKmA9htOeJ2QpJmvKDDAYwih_zfRNX0eJw_YOzXj5_-G3jW5tuVSTp8CxvLxbXfQxS1NPuwfvgn2-_2SvjOTn_MsPbzfPwXkCgUPg
link.rule.ids 315,783,787,3513,4509,27581,27936,27937,45597,45675,45886
linkProvider Elsevier
linkToHtml http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV3dSxwxEB-spdiX0mrFq1bzUEoLXd3dfOzl8Tw8rq31oZxgn0K-Fhbqrpwn1Bf_9k6yux4ih6VvISTDJjM785tkZgLwQQ9l6V3BEqN9OLopRaKFs8Hn8T7naAF9jLY4E9Nz9u2CX6zBuM-FCWGVne5vdXrU1l3PUbebR1dVFXJ8M8ZRvGQR3ioQ9Bk8ZwEfo1Af3i3jPNCEtRg4Y0kYvkzjaUnEzk-y-BypJHSVgXoMQB_i2WiQJq_hVYckyaj92Dew5utN2BrV6EVf3pKPJMZ2xkPzTXhx3Lc2xv0Lb1vwa_w7HsZ-IV1ANbaJrh3xf7rw2Jo0JZlXpqlD2eNmUTlP5qHY6wKNH_mZk5CdQmbzW9QpzXVzqYkJslK9hfPJyWw8TbqnFhLLKaeJoI5bif6qttwKbnUmC8NSZjk3hUMMkTltdJGyEvFaqGHvcmlKRi06NIiaNN2G9bqp_Q6Q1NjSoFvknTGMpsakPqTP-oz7kqH7NIDDfn_VVVtRQy1DzZAhKjBEhXvxwBBFBzDsuaAeiIZCrf_U1IOeawr3NtyF6No3N9cqQ9iHukisHoGUcsSzSIOsGBEMCRVCpgPYbiXifkGSZrygwwGMooT820LV5OQ4fyTW7_5_-QewMZ39OFWnX8--78LLtvKuTNLhHqwv5jf-PeKphdmP_8tf0fMSYA
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=Cloning%2C+sequencing+and+expression+of+ribonucleotide+reductase+R2+from+Trypanosoma+brucei&rft.jtitle=FEBS+letters&rft.au=Dormeyer%2C+Matthias&rft.au=Sch%C3%B6neck%2C+Ralf&rft.au=Dittmar%2C+Gunnar+A.G.&rft.au=Krauth-Siegel%2C+R.+Luise&rft.date=1997-09-08&rft.pub=Elsevier+B.V&rft.issn=0014-5793&rft.eissn=1873-3468&rft.volume=414&rft.issue=2&rft.spage=449&rft.epage=453&rft_id=info:doi/10.1016%2FS0014-5793%2897%2901036-3&rft.externalDocID=S0014579397010363
thumbnail_l http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0014-5793&client=summon
thumbnail_m http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0014-5793&client=summon
thumbnail_s http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0014-5793&client=summon