Evidence map›Paper›PMID 38546289›Full record

ArticleBiochemistry2024

Glycerol 3-Phosphate Dehydrogenase: Role of the Protein Conformational Change in Activation of a Readily Reversible Enzyme-Catalyzed Hydride Transfer Reaction.

Judith R Cristobal, Rania Hegazy, John P Richard

Open access · greenAbstract read
PubMed Full text at PMC Publisher
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 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.7field-weighted citation impact, top 32% 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

4 citing papers in PubMed, 3 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. 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

3 authors at 1 institution in 1 country.

Judith R CristobalDepartment of Chemistry, University at Buffalo, SUNY, Buffalo, New York 14260-3000, United States.
Rania HegazyDepartment of Chemistry, University at Buffalo, SUNY, Buffalo, New York 14260-3000, United States.ORCID 0000-0002-2073-658X
John P RichardDepartment of Chemistry, University at Buffalo, SUNY, Buffalo, New York 14260-3000, United States.ORCID 0000-0002-0440-2387
University at Buffalo, State University of New York · US

Funding

Studies on Enzyme Activation and Novel Modes of Inhibition. Administrative Supplement for EquipmentR35GM134881 · NIGMS · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI John P Richard · 2020 to 2026
$2.5M
Activation of Enzymes for Catalysis: The Role of Substrate-Induced Structural ChangesR01GM116921 · NIGMS · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI RICHARD, JOHN P · 2016 to 2019
$1.3M
NIGMS NIH HHS R01 GM116921NIGMS NIH HHS R35 GM134881
6 · The paper itself

Abstract

Kinetic parameters are reported for glycerol 3-phosphate dehydrogenase (GPDH)-catalyzed hydride transfer from the whole substrate glycerol 3-phosphate (G3P) or truncated substrate ethylene glycol (EtG) to NAD, and for activation of the hydride transfer reaction of EtG by phosphite dianion. These kinetic parameters were combined with parameters for enzyme-catalyzed hydride transfer in the microscopic reverse direction to give the reaction equilibrium constants

Indexed as

Glycerolphosphate DehydrogenaseGlycerophosphatesPhosphitesCatalysisKineticsNADalpha-glycerophosphoric acidGlycerolphosphate DehydrogenaseGlycerophosphatesNADPhosphites

Identifiers

PMID38546289
PMCPMC11025551
OpenAlexW4393258988

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.