Evidence map›Paper›PMID 40920962›Full record

ArticleBiochemistry2025

Stereochemistry and Charged State Influence Effector Outcomes of d-2-Hydroxyglutarate Dehydrogenase Ligands.

Joanna Afokai Quaye, Giovanni Gadda

Abstract read
In one paragraph

Article in Biochemistry, 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

2 authors.

Joanna Afokai QuayeDepartment of Chemistry, Georgia State University, Atlanta, Georgia 30302-3965, United States.ORCID 0000-0002-7041-4570
Giovanni GaddaDepartment of Chemistry, Georgia State University, Atlanta, Georgia 30302-3965, United States.ORCID 0000-0002-7508-4195

Funding

Resource for Biocomputing Visualization and InformaticsP41GM103311 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI FERRIN, THOMAS E · 2012 to 2017
$8.2M
NIGMS NIH HHS P41 GM103311
6 · The paper itself

Abstract

d-2-Hydroxyglutarate dehydrogenase (D2HGDH) has recently received considerable attention due to the involvement of d-2-hydroxyglutarate in various medical conditions. This enzyme has been reported to diverge in substrate scope depending on whether its source is prokaryotic or eukaryotic. The D2HGDH from

Indexed as

Alcohol OxidoreductasesBacterial ProteinsMalatesPseudomonas aeruginosaCatalytic DomainEnzyme InhibitorsGlutaratesLigandsStereoisomerismSubstrate Specificity2-hydroxyglutarate dehydrogenaseAlcohol Oxidoreductasesalpha-hydroxyglutarateBacterial ProteinsEnzyme InhibitorsGlutaratesLigandsMalatesmalic acid

Identifiers

PMID40920962
PMCPMC12509308

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.