Evidence map›Paper›PMID 41185119›Full record

ArticleProteins2026

Human Citrate Synthase Post-Translational Modification Mimics and Molecular Dynamic Simulations Demonstrate Attenuation of Acetyl-CoA/CoA Binding.

Noah Shackelford, Zach Zavodny, Nathan Fancher, Michael A Moxley

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Proteins, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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

4 authors.

Noah ShackelfordDepartment of Chemistry, University of Nebraska at Kearney, Kearney, USA.
Zach ZavodnyDepartment of Chemistry, University of Nebraska at Kearney, Kearney, USA.
Nathan FancherDepartment of Chemistry, University of Nebraska at Kearney, Kearney, USA.
Michael A MoxleyDepartment of Chemistry, University of Nebraska at Kearney, Kearney, USA.ORCID 0000-0002-6988-1964

Funding

UNMC Structural Biology CoreP20GM103427 · NIGMS · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI PAUL L SORGEN · 2012 to 2026
$59.2M
Pyruvate Dehydrogenase Complex Activation as a Strategy to Ameliorate Metabolic DiseaseR15GM152925 · NIGMS · UNIVERSITY OF NEBRASKA KEARNEY · PI MOXLEY, MICHAEL A · 2023 to 2023
$403k
NIGMS NIH HHSNIGMS NIH HHS P20 GM103427NIGMS NIH HHS R15 GM152925
6 · The paper itself

Abstract

Human citrate synthase (hCS) is a mitochondrial enzyme that catalyzes the aldol condensation of acetyl coenzyme A (AcCoA) to oxaloacetate to form citrate in the TCA cycle. CS activity is important for aerobic exercise performance and basic metabolic function as a housekeeping enzyme. It has been shown through several mass spectrometry-based physiological studies that CS is post-translationally modified (PTM) on numerous residues via acetylation, phosphorylation, and methylation reactions. Few follow-up studies have been reported on the impact of PTMs on CS activity. Thus, we kinetically characterized several hCS PTM mimics near and distant from the active site by site-directed mutagenesis coupled with steady-state kinetics. Most modifications had a negative impact on AcCoA k

Indexed as

Acetyl Coenzyme ACitrate (si)-SynthaseProtein Processing, Post-TranslationalAcetylationBinding SitesCatalytic DomainHumansKineticsMolecular Dynamics SimulationMutagenesis, Site-DirectedProtein BindingAcetyl Coenzyme ACitrate (si)-Synthaseenzyme kineticsmolecular dynamicspost‐translational modifications

Identifiers

PMID41185119
PMCPMC12616816

What OpenQuestion holds

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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.