Evidence map›Paper›PMID 24798336›Full record

ReviewThe Journal of biological chemistry2014

The pyruvate dehydrogenase complexes: structure-based function and regulation.

Mulchand S Patel, Natalia S Nemeria, William Furey, Frank Jordan

Open access · hybridAbstract readReview
In one paragraph

Review in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 358 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
358citing papers in PubMed, 1 pooled it
15.1field-weighted citation impact, top 1% 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

358 citing papers in PubMed, 1 synthesis or guideline pooled it, 660 citations in OpenAlex.

  1. Pooled it
  2. Trial
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Proteomic Analysis of Dairy Cows with Persistent Subclinical Hypocalcemia.Animals : an open access journal from MDPI · 2026
    Article
  10. Review
  11. Review
  12. Article
  13. Review
  14. Research Advances in Plant Pyruvate Kinase.International journal of molecular sciences · 2026
    Review
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Review

298 more citing papers are in PubMed but not listed here.

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

4 authors at 3 institutions in 1 country.

Mulchand S PatelFrom the Department of Biochemistry, School of Medicine and Biomedical Sciences, University at Buffalo, the State University of New York, Buffalo, New York 14214, mspatel@buffalo.edu.
Natalia S Nemeriathe Department of Chemistry, Rutgers, the State University of New Jersey, Newark, New Jersey 07102.
William Fureythe Department of Pharmacology and Chemical Biology, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15261, and the Veterans Affairs Medical Center, Pittsburgh, Pennsylvania 15240.
Frank Jordanthe Department of Chemistry, Rutgers, the State University of New Jersey, Newark, New Jersey 07102, frjordan@rutgers.edu.
Rutgers, The State University of New Jersey · USUniversity at Buffalo, State University of New York · USUniversity of Pittsburgh · US

Funding

STRUCTURE AND MECHANISM OF YEAST PYRUVATE DECARBOXYLASER01GM050380 · NIGMS · RUTGERS THE STATE UNIV OF NJ NEWARK · PI JORDAN, FRANK · 1993 to 2013
$3.0M
Pyruvate Dehydrogenase E1: Structure-Function StudiesR01GM061791 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI FUREY, WILLIAM F · 2000 to 2012
$2.7M
INBORN ERRORS OF PYRUVATE METABOLISMR01DK020478 · NIDDK · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI PATEL, MULCHAND S · 1988 to 1999
–
NIDDK NIH HHS DK 20478NIGMS NIH HHS GM050380NIGMS NIH HHS GM061791NIGMS NIH HHS R01 GM050380NIGMS NIH HHS R01 GM061791
6 · The paper itself

Abstract

The pyruvate dehydrogenase complexes (PDCs) from all known living organisms comprise three principal catalytic components for their mission: E1 and E2 generate acetyl-coenzyme A, whereas the FAD/NAD(+)-dependent E3 performs redox recycling. Here we compare bacterial (Escherichia coli) and human PDCs, as they represent the two major classes of the superfamily of 2-oxo acid dehydrogenase complexes with different assembly of, and interactions among components. The human PDC is subject to inactivation at E1 by serine phosphorylation by four kinases, an inactivation reversed by the action of two phosphatases. Progress in our understanding of these complexes important in metabolism is reviewed.

Indexed as

Catalytic DomainAmino Acid SequenceAnimalsEscherichia coliHumansMolecular Sequence DataProtein BindingPyruvate Dehydrogenase ComplexPyruvate Dehydrogenase ComplexCovalent RegulationEnzyme CatalysisProtein-Protein InteractionPyruvate Dehydrogenase Complex (PDC)Pyruvate Dehydrogenase Kinase (PDC Kinase)

Identifiers

PMID24798336
PMCPMC4059105
OpenAlexW2088417711

What OpenQuestion holds

Textmetadata
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.