Evidence map›Paper›PMID 38994669›Full record

ReviewEssays in biochemistry2024

Acetylation, ADP-ribosylation and methylation of malate dehydrogenase.

Misty L Kuhn, John F Rakus, Delphine Quenet

Abstract readReview
In one paragraph

Review in Essays in biochemistry, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. 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.

Misty L KuhnDepartment of Chemistry and Biochemistry, San Francisco State University, San Francisco, CA, U.S.A.
John F RakusSchool of Sciences, University of Louisiana at Monroe, Monroe, LA, U.S.A.
Delphine QuenetDepartment of Biochemistry, Larner College of Medicine, University of Vermont, Burlington, VT, U.S.A.ORCID 0000-0002-8554-2049

Funding

Investigating the structure, function, and regulation of polyamine acetyltransferasesR35GM133506 · NIGMS · SAN FRANCISCO STATE UNIVERSITY · PI Misty Kuhn · 2019 to 2026
$2.9M
National Institute of General Medical Sciences (NIGMS) R35GM133506NIGMS NIH HHS R35 GM133506
6 · The paper itself

Abstract

Metabolism within an organism is regulated by various processes, including post-translational modifications (PTMs). These types of chemical modifications alter the molecular, biochemical, and cellular properties of proteins and allow the organism to respond quickly to different environments, energy states, and stresses. Malate dehydrogenase (MDH) is a metabolic enzyme that is conserved in all domains of life and is extensively modified post-translationally. Due to the central role of MDH, its modification can alter metabolic flux, including the Krebs cycle, glycolysis, and lipid and amino acid metabolism. Despite the importance of both MDH and its extensively post-translationally modified landscape, comprehensive characterization of MDH PTMs, and their effects on MDH structure, function, and metabolic flux remains underexplored. Here, we review three types of MDH PTMs - acetylation, ADP-ribosylation, and methylation - and explore what is known in the literature and how these PTMs potentially affect the 3D structure, enzymatic activity, and interactome of MDH. Finally, we briefly discuss the potential involvement of PTMs in the dynamics of metabolons that include MDH.

Indexed as

ADP-RibosylationMalate DehydrogenaseProtein Processing, Post-TranslationalAcetylationAnimalsHumansMethylationMalate DehydrogenaseAcetylationADP-ribosylationMalate DehydrogenaseMetabolonMethylationPost-translational modifications

Identifiers

PMID38994669
PMCPMC11451102

What OpenQuestion holds

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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.