Evidence map›Paper›PMID 41313771›Full record

ArticleScience advances2025

How ATP and dATP reposition class III ribonucleotide reductase cone domains to regulate enzyme activity.

Gisele A Andree, Kelsey R Miller-Brown, Zhuangyu Zhao, Ally K Smith, Christopher D Dawson, Daniel J Deredge, Catherine L Drennan

Abstract read
In one paragraph

Article in Science advances, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing 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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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.

Gisele A AndreeDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.ORCID 0000-0002-5620-6951
Kelsey R Miller-BrownDepartment of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.ORCID 0000-0003-1963-2908
Zhuangyu ZhaoDepartment of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.ORCID 0000-0002-5368-4130
Ally K SmithDepartment of Pharmaceutical Sciences, University of Maryland School of Pharmacy, Baltimore, MD 21201, USA.ORCID 0000-0003-4539-1714
Christopher D DawsonDepartment of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
Daniel J DeredgeDepartment of Pharmaceutical Sciences, University of Maryland School of Pharmacy, Baltimore, MD 21201, USA.ORCID 0000-0002-6897-6523
Catherine L DrennanDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.ORCID 0000-0001-5486-2755

Funding

TRAINING GRANTS IN ENVIROMENTAL TOXICOLOGYT32ES007020 · NIEHS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI ESSIGMANN, JOHN M · 1985 to 2024
$13.1M
Metalloenzyme structure, function and assemblyR35GM126982 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI CATHERINE L DRENNAN · 2018 to 2026
$3.4M
Graduate Training at The Chemistry Biology InterfaceT32GM066706 · NIGMS · UNIVERSITY OF MARYLAND BALTIMORE COUNTY · PI SELEY-RADTKE, KATHERINE L, SMITH, AARON T · 2004 to 2023
$3.3M
Structural Determination and Design of Drug Interactions with Ribonucleotide ReductaseF32GM143840 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI MILLER, KELSEY ROSE · 2021 to 2023
$205k
NIEHS NIH HHS T32 ES007020NIGMS NIH HHS F32 GM143840NIGMS NIH HHS R35 GM126982NIGMS NIH HHS T32 GM066706
6 · The paper itself

Abstract

Ribonucleotide reductases (RNRs) catalyze the conversion of ribonucleotides to deoxyribonucleotides. In the majority of cases, RNR activity is allosterically regulated by the cellular 2'-deoxyadenosine 5'-triphosphate (dATP)/adenosine 5'-triphosphate (ATP) ratio. To investigate allosteric activity regulation in anaerobic or class III (glycyl radical containing) RNRs, we determine cryo-electron microscopy structures of the class III RNR from

Indexed as

Adenosine TriphosphateDeoxyadenine NucleotidesRibonucleotide ReductasesAllosteric RegulationCatalytic DomainCryoelectron MicroscopyModels, MolecularProtein BindingProtein ConformationProtein Domains2'-deoxyadenosine triphosphateAdenosine TriphosphateDeoxyadenine NucleotidesRibonucleotide Reductases

Identifiers

PMID41313771
PMCPMC12662201

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.