Evidence map›Paper›PMID 41634442›Full record

ArticleNature chemical biology2026

Functional analysis of O-GlcNAcylation by networking of OGT interactors and substrates.

Matthew E Griffin, John W Thompson, Yao Xiao, Michael J Sweredoski, Elizabeth H Jensen, Rita B Aksenfeld, Helena Awad, Terry D Kim, Andrew L Schacht, Priya Choudhry and 5 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Nature chemical biology, 2026. 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. Bioorthogonal Chemistry in Neurobiology: From Imaging to Proteomics.Chembiochem : a European journal of chemical biology · 2026
    Review
  2. Review
  3. Review
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

15 authors.

Matthew E Griffin *Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA, USA. griffin@uci.edu.ORCID http://orcid.org/0000-0001-9549-4418
John W Thompson *Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA, USA.
Yao XiaoDivision of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA, USA.
Michael J SweredoskiProteome Exploration Laboratory, Beckman Institute, California Institute of Technology, Pasadena, CA, USA.
Elizabeth H JensenDivision of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA, USA.
Rita B AksenfeldDivision of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA, USA.ORCID http://orcid.org/0000-0002-2911-9211
Helena AwadDivision of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA, USA.ORCID http://orcid.org/0009-0003-0707-212X
Terry D KimDivision of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA, USA.
Andrew L SchachtDivision of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA, USA.
Priya ChoudhryDivision of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA, USA.ORCID http://orcid.org/0000-0002-4438-1576
Yelena KoldobskayaDivision of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA, USA.
Brett LomenickProteome Exploration Laboratory, Beckman Institute, California Institute of Technology, Pasadena, CA, USA.ORCID http://orcid.org/0000-0002-5023-9998
Spiros D GarbisProteome Exploration Laboratory, Beckman Institute, California Institute of Technology, Pasadena, CA, USA.ORCID http://orcid.org/0000-0002-1050-0805
Annie MoradianProteome Exploration Laboratory, Beckman Institute, California Institute of Technology, Pasadena, CA, USA.
Linda C Hsieh-WilsonDivision of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA, USA. lhw@caltech.edu.ORCID http://orcid.org/0000-0001-5661-1714

Funding

UCLA-Caltech Medical Scientist Training ProgramT32GM008042 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI AJIJOLA, OLUJIMI A, DAWSON, DAVID WAYNE · 1985 to 2023
$29.9M
PREDOCTORAL TRAINING IN BIOLOGY AND CHEMISTRYT32GM007616 · NIGMS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI STERNBERG, PAUL WARREN · 1985 to 2019
$22.9M
Chemical Approaches to Understand O-GlcNAc Glycosylation and Its Roles in NeurodegenerationR01AG060540 · NIA · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI Linda C Hsieh-Wilson · 2024 to 2026
$2.4M
The Role of Cdk5 O-GlcNAcylation in Neurodegeneration and Alzheimer's DiseaseF30AG055314 · NIA · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI THOMPSON, JOHN · 2017 to 2019
$99k
NIA NIH HHS F30 AG055314NIA NIH HHS R01 AG060540NIGMS NIH HHS T32 GM007616NIGMS NIH HHS T32 GM008042U.S. Department of Health & Human Services | National Institutes of Health (NIH) R01AG060540
6 · The paper itself

Abstract

The post-translational modification (PTM) of proteins by O-linked β-N-acetyl-D-glucosamine (O-GlcNAcylation) is widely found across the proteome and regulates diverse cellular processes, from transcription and translation to signal transduction and metabolism. However, most functional studies to date have focused on individual modifications, overlooking other simultaneous O-GlcNAcylation events that work together to coordinate cellular activities. Here we describe networking of O-GlcNAc transferase interactors and substrates (NOTISE), a systems-level approach that monitors O-GlcNAcylation rapidly and comprehensively across the proteome to reveal important functional and regulatory relationships. The NOTISE method integrates affinity purification-mass spectrometry and site-specific chemoproteomic technologies with network generation to connect putative upstream regulators and downstream targets of O-GlcNAcylation. The resulting data-rich networks identify critical conserved activities of O-GlcNAcylation and tissue-specific functions. This holistic and unbiased approach provides a broadly applicable framework to catalyze investigations into the functional roles of coordinated, multisubstrate PTMs in specific cellular and physiological contexts.

Indexed as

AcetylglucosamineN-AcetylglucosaminyltransferasesProtein Processing, Post-TranslationalAnimalsGlycosylationHumansMass SpectrometryProteomeProteomicsSubstrate SpecificityAcetylglucosamineN-AcetylglucosaminyltransferasesO-GlcNAc transferaseProteome

Identifiers

PMID41634442
PMCPMC13423809

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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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.