Evidence map›Paper›PMID 21456967›Full record

ReviewAnnual review of biochemistry2011

Class I ribonucleotide reductases: metallocofactor assembly and repair in vitro and in vivo.

Joseph A Cotruvo, Joanne Stubbe

Abstract readReview
In one paragraph

Review in Annual review of biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 132 papers.

0numbers the graph read from it
0cells of the map it votes in
132citing papers in PubMed
–field-weighted citation impact
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

132 citing papers in PubMed.

  1. Article
  2. Article
  3. Transition metal activation reframes SAMHD1 regulation.bioRxiv : the preprint server for biology · 2026
    Article
  4. 50 Years of Giese Reaction - a Personal View.Angewandte Chemie (International ed. in English) · 2026
    Review
  5. Article
  6. 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
  7. Article
  8. Ferroptosis and cancer: when iron turns against tumors.Cellular and molecular life sciences : CMLS · 2025
    Review
  9. Article
  10. Journal of bacteriology · 2025
    Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Electron transfer in biological systems.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2024
    Review
  17. Article
  18. ConservedBiochemistry · 2024
    Article
  19. Article
  20. Article

72 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

2 authors.

Joseph A CotruvoDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA. jcotruvo@mit.edu
Joanne Stubbe

Funding

Ribonucleotide Reductase: Structure and FunctionR01GM029595 · NIGMS · UNIVERSITY OF WISCONSIN MADISON · PI STUBBE, JOANNE · 1985 to 2016
$6.9M
Ribonucleotide Reductase Regulation: Diferric Y* assembly/maintenance and Sml1R01GM081393 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI STUBBE, JOANNE · 2008 to 2016
$3.9M
MECHANISM OF DINUCLEAR FE-Y. FORMATION OF NDP REDUCTASER37GM029595 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI STUBBE, JOANNE · 1988 to 1997
–
NIGMS NIH HHS GM29595NIGMS NIH HHS GM81393NIGMS NIH HHS R01 GM029595NIGMS NIH HHS R01 GM081393
6 · The paper itself

Abstract

Incorporation of metallocofactors essential for the activity of many enyzmes is a major mechanism of posttranslational modification. The cellular machinery required for these processes in the case of mono- and dinuclear nonheme iron and manganese cofactors has remained largely elusive. In addition, many metallocofactors can be converted to inactive forms, and pathways for their repair have recently come to light. The class I ribonucleotide reductases (RNRs) catalyze the conversion of nucleotides to deoxynucleotides and require dinuclear metal clusters for activity: an Fe(III)Fe(III)-tyrosyl radical (Y•) cofactor (class Ia), a Mn(III)Mn(III)-Y• cofactor (class Ib), and a Mn(IV)Fe(III) cofactor (class Ic). The class Ia, Ib, and Ic RNRs are structurally homologous and contain almost identical metal coordination sites. Recent progress in our understanding of the mechanisms by which the cofactor of each of these RNRs is generated in vitro and in vivo and by which the damaged cofactors are repaired is providing insight into how nature prevents mismetallation and orchestrates active cluster formation in high yields.

Indexed as

Bacterial ProteinsCoenzymesElectron Spin Resonance SpectroscopyFungal ProteinsHumansMetalsModels, MolecularMolecular StructureProtein ConformationRibonucleotide ReductasesSpectroscopy, MossbauerBacterial ProteinsCoenzymesFungal ProteinsMetalsRibonucleotide Reductases

Identifiers

PMID21456967
PMCPMC4703083

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.