Skip to search form
Skip to main content
Skip to account menu
Semantic Scholar
Semantic Scholar's Logo
Search 227,741,289 papers from all fields of science
Search
Sign In
Create Free Account
Ribonucleotide Reductase
Known as:
EC 1.17.4.-
, Ribonucleotide Reductases [Chemical/Ingredient]
, Ribonucleotide Reductases
Expand
Ribonucleotide Reductase is a heterodimeric cytoplasmic enzyme essential in dividing cells that reduces ribonucleotides to deoxyribonucleotide…
Expand
National Institutes of Health
Create Alert
Alert
Related topics
Related topics
39 relations
Broader (2)
Alcohol Oxidoreductases
Iron-Sulfur Proteins
DNA Replication
Fludarabine phosphate
Gemcitabine Elaidate
Gemcitabine hydrochloride
Expand
Narrower (10)
ICP10 protein, herpes simplex virus type 2
NrdB protein, E coli
NrdF protein, E coli
NrdF protein, bacteria
Expand
Papers overview
Semantic Scholar uses AI to extract papers important to this topic.
Highly Cited
2003
Highly Cited
2003
The chemistry and biochemistry of the copper–radical interaction
W. Kaim
2003
Corpus ID: 48358314
This Perspective describes the plausible oxidation state combinations of Cun/Lm systems where Lm is an O- or N-based redox system…
Expand
Highly Cited
1996
Highly Cited
1996
Two Conserved Tyrosine Residues in Protein R1 Participate in an Intermolecular Electron Transfer in Ribonucleotide Reductase*
M. Ekberg
,
M. Sahlin
,
M. Eriksson
,
B. Sjöberg
Journal of Biological Chemistry
1996
Corpus ID: 42879845
The enzyme ribonucleotide reductase consists of two nonidentical proteins, R1 and R2, which are each inactive alone. R1 contains…
Expand
Highly Cited
1996
Highly Cited
1996
The Anaerobic Escherichia coli Ribonucleotide Reductase
S. Ollagnier
,
E. Mulliez
,
J. Gaillard
,
R. Eliasson
,
M. Fontecave
,
P. Reichard
Journal of Biological Chemistry
1996
Corpus ID: 13494888
During anaerobic growth Escherichia coli uses a specific ribonucleoside triphosphate reductase for the production of…
Expand
Highly Cited
1991
Highly Cited
1991
Purification and characterization of recombinant mouse and herpes simplex virus ribonucleotide reductase R2 subunit.
Graham J. Mann
,
A. Graeslund
,
El Ichiro Ochiai
,
R. Ingemarson
,
L. Thelander
Biochemistry
1991
Corpus ID: 33253073
Overexpression of recombinant mouse and herpes simplex virus ribonucleotide reductase small subunit (protein R2) has been…
Expand
Highly Cited
1988
Highly Cited
1988
Ribonucleotide reductase of Brevibacterium ammoniagenes is a manganese enzyme.
A. Willing
,
H. Follmann
,
G. Auling
European Journal of Biochemistry
1988
Corpus ID: 1119081
Ribonucleotide reduction and not DNA replication is the site for the specific manganese requirement of DNA synthesis and cell…
Expand
Highly Cited
1988
Highly Cited
1988
Ribonucleotide reductase encoded by herpes simplex virus is a determinant of the pathogenicity of the virus in mice and a valid antiviral target.
C. Jm
,
I. McDougall
,
H. Marsden
,
V. Preston
,
Ryan Dm
,
J. Subak-Sharpe
Journal of General Virology
1988
Corpus ID: 7015610
The role of the herpes simplex virus (HSV)-encoded ribonucleotide reductase (RR) in the pathogenicity of the virus has been…
Expand
Highly Cited
1987
Highly Cited
1987
Magnetic interaction between the tyrosyl free radical and the antiferromagnetically coupled iron center in ribonucleotide reductase.
M. Sahlin
,
L. Petersson
,
A. Gräslund
,
A. Ehrenberg
,
B. Sjöberg
,
L. Thelander
Biochemistry
1987
Corpus ID: 21497954
Ribonucleotide reductases from Escherichia coli and from mammalian cells are heterodimeric enzymes. One of the subunits, in the…
Expand
Highly Cited
1983
Highly Cited
1983
Ribonucleotide reductase induced by herpes simplex virus has a virus-specified constituent.
B. Dutia
Journal of General Virology
1983
Corpus ID: 26147855
Ribonucleotide reductase, an enzyme found in all prokaryotic and eukaryotic cells that synthesize DNA, is induced by herpes…
Expand
Highly Cited
1977
Highly Cited
1977
Nature of the free radical in ribonucleotide reductase from Escherichia coli.
B. Sjöberg
,
P. Reichard
Journal of Biological Chemistry
1977
Corpus ID: 45640973
Ribonucleotide reductase from Escherichia coli consists of two nonidentical subunits, proteins B1 and B2. The active site of the…
Expand
Highly Cited
1966
Highly Cited
1966
Regulation of mammalian deoxyribonucleotide biosynthesis by nucleotides as activators and inhibitors.
E. Moore
,
Robert
,
B.
,
Hurlbert
Journal of Biological Chemistry
1966
Corpus ID: 8901474
By clicking accept or continuing to use the site, you agree to the terms outlined in our
Privacy Policy
(opens in a new tab)
,
Terms of Service
(opens in a new tab)
, and
Dataset License
(opens in a new tab)
ACCEPT & CONTINUE