Evidence map›Paper›PMID 30855138›Full record

ArticleBiochemistry2019

Structures of Class Id Ribonucleotide Reductase Catalytic Subunits Reveal a Minimal Architecture for Deoxynucleotide Biosynthesis.

Hannah R Rose, Ailiena O Maggiolo, Molly J McBride, Gavin M Palowitch, Maria-Eirini Pandelia, Katherine M Davis, Neela H Yennawar, Amie K Boal

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.7field-weighted citation impact, top 35% 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

8 citing papers in PubMed, 11 citations in OpenAlex.

  1. Article
  2. Why is manganese so valuable to bacterial pathogens?Frontiers in cellular and infection microbiology · 2023
    Review
  3. Article
  4. Article
  5. Article
  6. Radicals in Biology: Your Life Is in Their Hands.Journal of the American Chemical Society · 2021
    Article
  7. Article
  8. 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

8 authors at 2 institutions in 1 country.

Hannah R RoseDepartment of Chemistry , The Pennsylvania State University , University Park , Pennsylvania 16802 , United States.ORCID 0000-0002-7982-2001
Ailiena O MaggioloDepartment of Chemistry , The Pennsylvania State University , University Park , Pennsylvania 16802 , United States.
Molly J McBrideDepartment of Chemistry , The Pennsylvania State University , University Park , Pennsylvania 16802 , United States.
Gavin M PalowitchDepartment of Biochemistry and Molecular Biology , The Pennsylvania State University , University Park , Pennsylvania 16802 , United States.
Maria-Eirini PandeliaDepartment of Biochemistry , Brandeis University , Waltham , Massachusetts 02453 , United States.
Katherine M DavisDepartment of Chemistry , The Pennsylvania State University , University Park , Pennsylvania 16802 , United States.ORCID 0000-0002-0258-8907
Neela H YennawarHuck Institutes of the Life Sciences , The Pennsylvania State University , University Park , Pennsylvania 16802 , United States.
Amie K BoalDepartment of Chemistry , The Pennsylvania State University , University Park , Pennsylvania 16802 , United States.ORCID 0000-0002-1234-8472
Pennsylvania State University · USBrandeis University · US

Funding

Overall (pp. 40-62)P41GM103485 · NIGMS · CORNELL UNIVERSITY · PI CERIONE, RICHARD A. · 2012 to 2018
$15.5M
Mapping the Structural Basis for Mechanistic Diversity in Metalloenzyme SuperfamiliesR35GM119707 · NIGMS · PENNSYLVANIA STATE UNIVERSITY, THE · PI Amie K Boal · 2016 to 2026
$5.0M
High-Speed High-Sensitivity Detector for X-ray Micro-Crystallography at GM/CA@APSS10OD012289 · OD · UNIVERSITY OF CHICAGO · PI FISCHETTI, ROBERT F. · 2014 to 2014
$2.0M
Functional diversification of the HD-superfamily; the Hydrolase/Oxygenase DilemmaR00GM111978 · NIGMS · BRANDEIS UNIVERSITY · PI PANDELIA, MARIA-EIRINI · 2016 to 2018
$740k
Structure determination of reaction intermediates in macromolecular complexesR00GM100011 · NIGMS · PENNSYLVANIA STATE UNIVERSITY, THE · PI BOAL, AMIE K · 2013 to 2015
$729k
NIGMS NIH HHS P41 GM103485NIGMS NIH HHS R00 GM100011NIGMS NIH HHS R00 GM111978NIGMS NIH HHS R35 GM119707NIH HHS S10 OD012289
6 · The paper itself

Abstract

Class I ribonucleotide reductases (RNRs) share a common mechanism of nucleotide reduction in a catalytic α subunit. All RNRs initiate catalysis with a thiyl radical, generated in class I enzymes by a metallocofactor in a separate β subunit. Class Id RNRs use a simple mechanism of cofactor activation involving oxidation of a Mn

Indexed as

Catalytic DomainProtein ConformationActinobacillusAdenosine TriphosphateAllosteric RegulationAmino Acid SequenceBiocatalysisCrystallography, X-RayDeoxyribonucleotidesFlavobacteriumModels, MolecularPhylogenyRibonucleotide ReductasesScattering, Small AngleSequence Homology, Amino AcidX-Ray DiffractionAdenosine TriphosphateDeoxyribonucleotidesRibonucleotide Reductases

Identifiers

PMID30855138
PMCPMC6456427
OpenAlexW2412762869

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.