Evidence map›Paper›PMID 37918804›Full record

ReviewThe Journal of biological chemistry2023

Understanding and exploiting the roles of O-GlcNAc in neurodegenerative diseases.

Matthew R Pratt, David J Vocadlo

Open access · goldAbstract readReview
In one paragraph

Review in The Journal of biological chemistry, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
7.1field-weighted citation impact, top 2% 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

29 citing papers in PubMed, 46 citations in OpenAlex.

  1. Article
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  7. Glucosamine as a regulator of O-GlcNAc signaling: linking metabolism to disease pathogenesis.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2026
    Review
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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

2 authors at 2 institutions in 2 countries.

Matthew R PrattDepartment of Chemistry and Department of Biological Sciences, University of Southern California, Los Angeles, California, USA. Electronic address: matthew.pratt@usc.edu.
David J VocadloDepartment of Chemistry, Simon Fraser University, Burnaby, British Columbia, Canada; Department of Molecular Biology and Biochemistry, Simon Fraser University, Burnaby, British Columbia, Canada. Electronic address: dvocadlo@sfu.ca.
Simon Fraser University · CAUniversity of Southern California · US

Funding

Functional Analysis of O-GlcNAc using Synthetic Protein ChemistryR01GM114537 · NIGMS · UNIVERSITY OF SOUTHERN CALIFORNIA · PI PRATT, MATTHEW ROBERT · 2015 to 2024
$3.1M
Chemical Tools for the Investigation and Manipulation of Protein GlycosylationR01GM125939 · NIGMS · UNIVERSITY OF SOUTHERN CALIFORNIA · PI PRATT, MATTHEW ROBERT · 2017 to 2025
$2.4M
CIHRNIGMS NIH HHS R01 GM114537NIGMS NIH HHS R01 GM125939
6 · The paper itself

Abstract

O-GlcNAc is a common modification found on nuclear and cytoplasmic proteins. Determining the catalytic mechanism of the enzyme O-GlcNAcase (OGA), which removes O-GlcNAc from proteins, enabled the creation of potent and selective inhibitors of this regulatory enzyme. Such inhibitors have served as important tools in helping to uncover the cellular and organismal physiological roles of this modification. In addition, OGA inhibitors have been important for defining the augmentation of O-GlcNAc as a promising disease-modifying approach to combat several neurodegenerative diseases including both Alzheimer's disease and Parkinson's disease. These studies have led to development and optimization of OGA inhibitors for clinical application. These compounds have been shown to be well tolerated in early clinical studies and are steadily advancing into the clinic. Despite these advances, the mechanisms by which O-GlcNAc protects against these various types of neurodegeneration are a topic of continuing interest since improved insight may enable the creation of more targeted strategies to modulate O-GlcNAc for therapeutic benefit. Relevant pathways on which O-GlcNAc has been found to exert beneficial effects include autophagy, necroptosis, and processing of the amyloid precursor protein. More recently, the development and application of chemical methods enabling the synthesis of homogenous proteins have clarified the biochemical effects of O-GlcNAc on protein aggregation and uncovered new roles for O-GlcNAc in heat shock response. Here, we discuss the features of O-GlcNAc in neurodegenerative diseases, the application of inhibitors to identify the roles of this modification, and the biochemical effects of O-GlcNAc on proteins and pathways associated with neurodegeneration.

Indexed as

Alzheimer DiseaseN-AcetylglucosaminyltransferasesParkinson DiseaseAcetylglucosamineAmyloid beta-Protein Precursorbeta-N-AcetylhexosaminidasesEnzyme InhibitorsHumansProtein Processing, Post-TranslationalAcetylglucosamineAmyloid beta-Protein Precursorbeta-N-AcetylhexosaminidasesEnzyme InhibitorsN-AcetylglucosaminyltransferasesAlzheimer's diseaseclinical developmentenzyme inhibitorsneurodegenerationO-GlcNAcprotein synthesissynucleintau

Identifiers

PMID37918804
PMCPMC10687168
OpenAlexW4388074463

What Socratic holds

Textmetadata
LicenceCC BY
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 Socratic graph.