Evidence map›Paper›PMID 39164005›Full record

ArticleBiochemistry2024

How ATP and dATP Act as Molecular Switches to Regulate Enzymatic Activity in the Prototypical Bacterial Class Ia Ribonucleotide Reductase.

Michael A Funk, Christina M Zimanyi, Gisele A Andree, Allison E Hamilos, Catherine L Drennan

Abstract read
In one paragraph

Article in Biochemistry, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing 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

10 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. 2.6-Å resolution cryo-EM structure of a class Ia ribonucleotide reductase trapped with mechanism-based inhibitor NProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
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

5 authors.

Michael A FunkDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, United States.ORCID 0000-0003-1898-9008
Christina M ZimanyiDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, United States.ORCID 0000-0002-6782-507X
Gisele A AndreeDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, United States.ORCID 0000-0002-5620-6951
Allison E HamilosDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, United States.
Catherine L DrennanDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, United States.ORCID 0000-0001-5486-2755

Funding

User Training and OutreachP30GM124165 · NIGMS · CORNELL UNIVERSITY · PI Nozomi Ando, J Christopher Fromme · 2018 to 2026
$34.2M
TOXICOLOGY CORE UNITP30ES002109 · NIEHS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI YAFFE, MICHAEL B · 1985 to 2020
$25.6M
Interdepartmental Biotechnology Training ProgramT32GM008334 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI WITTRUP, KARL DANE · 1989 to 2018
$15.2M
Metalloenzyme structure, function and assemblyR35GM126982 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI CATHERINE L DRENNAN · 2018 to 2026
$3.4M
Pixel Array Detector for Macromolecular CrystallographyS10OD021527 · OD · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2016 to 2016
$2.0M
Pixel Array Detector for X-ray CrystallographyS10RR029205 · NCRR · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2010 to 2010
$1.8M
NCRR NIH HHS S10 RR029205NIEHS NIH HHS P30 ES002109NIGMS NIH HHS P30 GM124165NIGMS NIH HHS R35 GM126982NIGMS NIH HHS T32 GM008334NIH HHS S10 OD021527
6 · The paper itself

Abstract

Class Ia ribonucleotide reductases (RNRs) are allosterically regulated by ATP and dATP to maintain the appropriate deoxyribonucleotide levels inside the cell for DNA biosynthesis and repair. RNR activity requires precise positioning of the β

Indexed as

Adenosine TriphosphateDeoxyadenine NucleotidesEscherichia coliEscherichia coli ProteinsRibonucleotide ReductasesAllosteric RegulationBinding SitesCrystallography, X-RayModels, MolecularProtein Conformation2'-deoxyadenosine triphosphateAdenosine TriphosphateDeoxyadenine NucleotidesEscherichia coli ProteinsRibonucleotide Reductases

Identifiers

PMID39164005
PMCPMC11447812

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.