Evidence map›Paper›PMID 32569524›Full record

ReviewAnnual review of biochemistry2020

Ribonucleotide Reductases: Structure, Chemistry, and Metabolism Suggest New Therapeutic Targets.

Brandon L Greene, Gyunghoon Kang, Chang Cui, Marina Bennati, Daniel G Nocera, Catherine L Drennan, JoAnne Stubbe

Open access · bronzeAbstract readReview
In one paragraph

Review in Annual review of biochemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 134 papers.

0numbers the graph read from it
0cells of the map it votes in
134citing papers in PubMed
9.4field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

134 citing papers in PubMed, 216 citations in OpenAlex.

  1. Article
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  8. ThebioRxiv : the preprint server for biology · 2026
    Article
  9. Low-barrier hydrogen bond powers long-range radical transfer in the metal-free ribonucleotide reductase.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  10. Article
  11. Article
  12. Article
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  14. Review
  15. Allosteric gating of radical transport in ribonucleotide reductase.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  16. Article
  17. Conformationally gated multisite proton-coupled electron transfer in the ribonucleotide reductaseProceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  18. Article
  19. Multi omics network toxicology andFrontiers in cell and developmental biology · 2026
    Article
  20. Differential Evolution for Docking Simulations.Methods in molecular biology (Clifton, N.J.) · 2026
    Article

74 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 4 institutions in 2 countries.

Brandon L GreeneDepartment of Chemistry and Biochemistry, University of California, Santa Barbara, California 93106, USA.
Gyunghoon KangDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA; email: stubbe@mit.edu.
Chang CuiDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA; email: stubbe@mit.edu.
Marina BennatiMax Planck Institute for Biophysical Chemistry, 37077 Göttingen, Germany.
Daniel G NoceraDepartment of Chemistry and Chemical Biology, Harvard University, Cambridge, Massachusetts 02138, USA.
Catherine L DrennanDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA; email: stubbe@mit.edu.
JoAnne StubbeDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA; email: stubbe@mit.edu.
Harvard University · USIIT@MIT · USHoward Hughes Medical Institute · USUniversitätsmedizin Göttingen · DE

Funding

Structure-Function Studies of Ribonucleotide ReductaseR01GM047274 · NIGMS · MICHIGAN STATE UNIVERSITY · PI DANIEL G. NOCERA · 1992 to 2026
$9.9M
Metalloenzyme structure, function and assemblyR35GM126982 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI CATHERINE L DRENNAN · 2018 to 2026
$3.4M
NIGMS NIH HHS R01 GM047274NIGMS NIH HHS R35 GM126982
6 · The paper itself

Abstract

Ribonucleotide reductases (RNRs) catalyze the de novo conversion of nucleotides to deoxynucleotides in all organisms, controlling their relative ratios and abundance. In doing so, they play an important role in fidelity of DNA replication and repair. RNRs' central role in nucleic acid metabolism has resulted in five therapeutics that inhibit human RNRs. In this review, we discuss the structural, dynamic, and mechanistic aspects of RNR activity and regulation, primarily for the human and

Indexed as

Anti-Bacterial AgentsAntineoplastic AgentsBiocatalysisDrug DiscoveryEnzyme InhibitorsEscherichia coliEscherichia coli InfectionsHumansMolecular Docking SimulationNeoplasmsNucleotidesOxidation-ReductionProtein Structure, SecondaryProtein SubunitsRibonucleotide ReductasesSmall Molecule LibrariesAnti-Bacterial AgentsAntineoplastic AgentsEnzyme InhibitorsNucleotidesProtein SubunitsRibonucleotide ReductasesSmall Molecule Librariesmechanismsribonucleotide reductasesstructurestherapeutics

Identifiers

PMID32569524
PMCPMC7316142
OpenAlexW3035812011

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.