The DOI matches its Crossref record; 126 of the 126 references it cites were found in a registry or an index.
Ribonucleotide Reductases
Abstract
Ribonucleotide reductases (RNRs) transform RNA building blocks to DNA building blocks by catalyzing the substitution of the 2′OH-group of a ribonucleotide with a hydrogen by a mechanism involving protein radicals. Three classes of RNRs employ different mechanisms for the generation of the protein radical. Recent structural studies of members from each class have led to a deeper understanding of their catalytic mechanism and allosteric regulation by nucleoside triphosphates. The main emphasis of this review is on regulation of RNR at the molecular and cellular level. Conformational transitions induced by nucleotide binding determine the regulation of substrate specificity. An intricate interplay between gene activation, enzyme inhibition, and protein degradation regulates, together with the allosteric effects, enzyme activity and provides the appropriate amount of deoxynucleotides for DNA replication and repair. In spite of large differences in the amino acid sequences, basic structural features are remarkably similar and suggest a common evolutionary origin for the three classes.
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Cites
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DeGregori, J., Kowalik, T., & Nevins, J. R. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.8.4215 · Cited by 919
A ribonucleotide reductase gene involved in a p53-dependent cell-cycle checkpoint for DNA damage
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Thymidine Phosphorylase Gene Mutations in MNGIE, a Human Mitochondrial Disorder
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Three-dimensional structure of the free radical protein of ribonucleotide reductase
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Self-citationStubbe, J., Nocera, D. G., Yee, C. S., & Chang, M. C. Y. (2003) · Chemical Reviews · doi:10.1021/cr020421u · Cited by 823
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INTERACTIONS BETWEEN DEOXYRIBONUCLEOTIDE AND DNA SYNTHESIS
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Ciccia, A., & Elledge, S. J. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.09.019 · Cited by 4,368
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Wilson, W. R., & Hay, M. P. (2011) · Nature Reviews Cancer · doi:10.1038/nrc3064 · Cited by 3,172
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Metadata
- Authors
- Nordlund, P., & Reichard, P.
- Venue
- Annual Review of Biochemistry
- Publisher
- Annual Reviews
- Published
- 2006-06-01
- Volume
- 75
- Issue
- 1
- Pages
- 681-706
- ISSN
- 0066-4154 (ISSN-L)
- 1545-4509
- OpenAlex
- W4256321774
- Cited by
- 1,079
- References
- 126
- FWCI
- 2.36
- Type
- journal article
- Language
- en
- Open access
- closed
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
