Evidence map›Paper›PMID 39927985›Full record

ArticleGlycobiology2025

A reference dataset of O-GlcNAc proteins in quadriceps skeletal muscle from mice.

Ruchi Jaiswal, Yimin Liu, Michael Petriello, Xiangmin Zhang, Zhengping Yi, Charlie Fehl

Abstract read
In one paragraph

Article in Glycobiology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Review
  2. Review
  3. 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

6 authors.

Ruchi JaiswalDepartment of Pharmaceutical Sciences, Eugene Applebaum College of Pharmacy, Wayne State University, 259 Mack Avenue, Detroit, Michigan 48201, United States.
Yimin LiuDepartment of Chemistry, Wayne State University, 5101 Cass Avenue, Detroit, Michigan 48202, United States.
Michael PetrielloInstitute of Environmental Health Sciences and Department of Pharmacology, Wayne State University, 6135 Woodward Avenue, Detroit, Michigan 48202, United States.
Xiangmin ZhangDepartment of Pharmaceutical Sciences, Eugene Applebaum College of Pharmacy, Wayne State University, 259 Mack Avenue, Detroit, Michigan 48201, United States.
Zhengping YiDepartment of Pharmaceutical Sciences, Eugene Applebaum College of Pharmacy, Wayne State University, 259 Mack Avenue, Detroit, Michigan 48201, United States.
Charlie FehlDepartment of Chemistry, Wayne State University, 5101 Cass Avenue, Detroit, Michigan 48202, United States.ORCID 0000-0001-6182-0879

Funding

Regional Pilot And Feasibility Study Grants ProgramP30DK020572 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI DAVID P OLSON · 2013 to 2026
$24.3M
Spatiotemporal tools to interrogate O-GlcNAc functions in metabolic signaling and diseaseR35GM142637 · NIGMS · WAYNE STATE UNIVERSITY · PI Charlie Fehl · 2021 to 2026
$2.6M
PFAS increases susceptibility to infection-mediated PTBR01ES035692 · NIEHS · WAYNE STATE UNIVERSITY · PI Michael Curtis Petriello · 2024 to 2026
$1.7M
Mechanistic study of Small-molecular Therapy in diabetic Wound HealingR01DK128937 · NIDDK · WAYNE STATE UNIVERSITY · PI WANG, JIEMEI, YI, ZHENGPING · 2021 to 2024
$1.6M
NIDDK NIH HHS P30 DK020572NIDDK NIH HHS R01 DK128937NIEHS NIH HHS R01 ES035692NIGMS NIH HHS R35 GM142637NIH/NIEHS R01ES035692-01A1NIH/NIGMS R35GM142637NSF CAREER CHE-2235508
6 · The paper itself

Abstract

A key nutrient sensing process in all animal tissues is the dynamic attachment of O-linked N-acetylglucosamine (O-GlcNAc). Determining the targets and roles of O-GlcNAc glycoproteins has the potential to reveal insights into healthy and diseased metabolic states. In cell studies, thousands of proteins are known to be O-GlcNAcylated, but reference datasets for most tissue types in animals are lacking. Here, we apply a chemoenzymatic labeling study to compile a high coverage dataset of quadriceps skeletal muscle O-GlcNAc glycoproteins from mice. Our dataset contains over 550 proteins, and > 80% of the dataset matched known O-GlcNAc proteins. This dataset was further annotated via bioinformatics, revealing the distribution, protein interactions, and gene ontology (GO) functions of these skeletal muscle proteins. We compared these quadriceps glycoproteins with a high-coverage O-GlcNAc enrichment profile from mouse hearts and describe the key overlap and differences between these tissue types. Quadriceps muscles can be used for biopsies, so we envision this dataset to have potential biomedical relevance in detecting aberrant glycoproteins in metabolic diseases and physiological studies. This new knowledge adds to the growing collection of tissues with high-coverage O-GlcNAc profiles, which we anticipate will further the systems biology of O-GlcNAc mechanisms, functions, and roles in disease.

Indexed as

AcetylglucosamineGlycoproteinsMuscle, SkeletalQuadriceps MuscleAnimalsMiceAcetylglucosamineGlycoproteinsglycoproteomicsmouse quadricepsO-GlcNAcskeletal muscletissue atlas

Identifiers

PMID39927985
PMCPMC12032608

What Socratic holds

Textmetadata
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Registered trials

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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 Socratic graph.