Evidence map›Paper›PMID 23663976›Full record

ReviewProgress in molecular biology and translational science2013

The structural basis for the allosteric regulation of ribonucleotide reductase.

Md Faiz Ahmad, Chris G Dealwis

Abstract readReview
In one paragraph

Review in Progress in molecular biology and translational science, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
8.1field-weighted citation impact, top 3% 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

21 citing papers in PubMed, 34 citations in OpenAlex.

  1. Hypermutability ofEmerging microbes & infections · 2025
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  20. Ribonucleotide reductases: essential enzymes for bacterial life.Frontiers in cellular and infection microbiology · 2014
    Review
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 at 1 institution in 1 country.

Md Faiz AhmadDepartment of Pharmacology, School of Medicine, Case Western Reserve University, Cleveland, Ohio, USA.
Chris G Dealwis
Case Western Reserve University · US

Funding

Structure-Function and Inhibition of Rnr1R01CA100827 · NCI · UNIVERSITY OF TENNESSEE KNOXVILLE · PI DEALWIS, CHRIS G · 2003 to 2011
$2.5M
Investigating the structural assembly of RNR multimersR01GM100887 · NIGMS · CASE WESTERN RESERVE UNIVERSITY · PI DEALWIS, CHRIS G · 2012 to 2015
$1.2M
NCI NIH HHS R01 CA100827NCI NIH HHS R01CA100827-04A1NIGMS NIH HHS 1R01GM100887-01NIGMS NIH HHS R01 GM100887
6 · The paper itself

Abstract

Ribonucleotide reductases (RRs) catalyze a crucial step of de novo DNA synthesis by converting ribonucleoside diphosphates to deoxyribonucleoside diphosphates. Tight control of the dNTP pool is essential for cellular homeostasis. The activity of the enzyme is tightly regulated at the S-phase by allosteric regulation. Recent structural studies by our group and others provided the molecular basis for understanding how RR recognizes substrates, how it interacts with chemotherapeutic agents, and how it is regulated by its allosteric regulators ATP and dATP. This review discusses the molecular basis of allosteric regulation and substrate recognition of RR, and particularly the discovery that subunit oligomerization is an important prerequisite step in enzyme inhibition.

Indexed as

Allosteric RegulationAllosteric SiteAnimalsHumansMolecular Targeted TherapyProtein SubunitsRibonucleotide ReductasesStructure-Activity RelationshipProtein SubunitsRibonucleotide Reductases

Identifiers

PMID23663976
PMCPMC4059395
OpenAlexW1446668622

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.