Evidence map›Paper›PMID 21336276›Full record

ArticleNature structural & molecular biology2011

Structural basis for allosteric regulation of human ribonucleotide reductase by nucleotide-induced oligomerization.

James Wesley Fairman, Sanath Ranjan Wijerathna, Md Faiz Ahmad, Hai Xu, Ryo Nakano, Shalini Jha, Jay Prendergast, R Martin Welin, Susanne Flodin, Annette Roos and 4 more

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 111 papers.

0numbers the graph read from it
0cells of the map it votes in
111citing papers in PubMed
8.2field-weighted citation impact, top 2% 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

111 citing papers in PubMed, 175 citations in OpenAlex.

  1. Trial
  2. Review
  3. Article
  4. 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
  5. Article
  6. Article
  7. Frontiers in oncology · 2025
    Article
  8. Article
  9. Article
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  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
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  17. Article
  18. Review
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  20. Article

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

14 authors at 4 institutions in 2 countries.

James Wesley FairmanDepartment of Biochemistry, University of Tennessee, Knoxville, TN, USA.
Sanath Ranjan Wijerathna
Md Faiz Ahmad
Hai Xu
Ryo Nakano
Shalini Jha
Jay Prendergast
R Martin Welin
Susanne Flodin
Annette Roos
Pär Nordlund
Zongli Li
Thomas Walz
Chris Godfrey Dealwis
Case Western Reserve University · USKarolinska Institutet · SEHarvard University · USUniversity of Tennessee at Knoxville · US

Funding

Case Center for Synchrotron BiosciencesP30EB009998 · NIBIB · CASE WESTERN RESERVE UNIVERSITY · PI CHANCE, MARK R · 2009 to 2018
$8.4M
Structure-Function and Inhibition of Rnr1R01CA100827 · NCI · UNIVERSITY OF TENNESSEE KNOXVILLE · PI DEALWIS, CHRIS G · 2003 to 2011
$2.5M
Howard Hughes Medical InstituteNCI NIH HHS 2R01CA100827-04A1NCI NIH HHS 3R01CA100827-07S1NCI NIH HHS R01 CA100827NIBIB NIH HHS P30 EB009998Wellcome Trust
6 · The paper itself

Abstract

Ribonucleotide reductase (RR) is an α(n)β(n) (RR1-RR2) complex that maintains balanced dNTP pools by reducing NDPs to dNDPs. RR1 is the catalytic subunit, and RR2 houses the free radical required for catalysis. RR is allosterically regulated by its activator ATP and its inhibitor dATP, which regulate RR activity by inducing oligomerization of RR1. Here, we report the first X-ray structures of human RR1 bound to TTP alone, dATP alone, TTP-GDP, TTP-ATP, and TTP-dATP. These structures provide insights into regulation of RR by ATP or dATP. At physiological dATP concentrations, RR1 forms inactive hexamers. We determined the first X-ray structure of the RR1-dATP hexamer and used single-particle electron microscopy to visualize the α(6)-ββ'-dATP holocomplex. Site-directed mutagenesis and functional assays confirm that hexamerization is a prerequisite for inhibition by dATP. Our data indicate a mechanism for regulating RR activity by dATP-induced oligomerization.

Indexed as

Catalytic DomainAllosteric RegulationCrystallography, X-RayDeoxyadenine NucleotidesHumansModels, MolecularMutagenesis, Site-DirectedNucleotidesProtein MultimerizationRibonucleotide ReductasesSaccharomyces cerevisiae2'-deoxyadenosine triphosphateDeoxyadenine NucleotidesNucleotidesRibonucleotide Reductases

Identifiers

PMID21336276
PMCPMC3101628
OpenAlexW2083269101

What OpenQuestion holds

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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.