Student or educator? Sign up with your school email and get 6 months of Pro free.
Cited by 158

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

O-GlcNAc Transferase Is in a Functional Complex with Protein Phosphatase 1 Catalytic Subunits

Open access
Wells, Lance, Kreppel, Lisa K., Comer, Frank I., Wadzinski, Brian E., Hart, Gerald W.·2004·Journal of Biological Chemistry

Abstract

A hallmark of signal transduction is the dynamic and inducible post-translational modification of proteins. In addition to the well characterized phosphorylation of proteins, other modifications have been shown to be regulatory, including O-linked beta-N-acetylglucosamine (O-GlcNAc). O-GlcNAc modifies serine and threonine residues on a myriad of nuclear and cytosolic proteins, and for several proteins there appears to be a reciprocal relationship between phosphorylation and O-GlcNAc modification. Here we report further evidence of this yin-yang relationship by demonstrating that O-GlcNAc transferase, the enzyme that adds O-GlcNAc to proteins, exists in stable and active complexes with the serine/threonine phosphatases PP1beta and PP1gamma, enzymes that remove phosphate from proteins. The existence of this complex highlights the importance of understanding the dynamic relationship between O-GlcNAc and phosphate in modulating protein function in many cellular processes and disease states such as Alzheimer's disease and type II diabetes.

Overview

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1074/jbc.m406481200

Cites

1 of 1 references verified0 citation errors · 0 not checkable

Statistics

Verification

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Citations

Cites

Show all 1 references

Cited by

See all 158

Metadata

Authors
Wells, L., Kreppel, L. K., Comer, F. I., Wadzinski, B. E., & Hart, G. W.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
2004-09
Volume
279
Issue
37
Pages
38466-38470
ISSN
0021-9258 (ISSN-L)
OpenAlex
W2009324889
Cited by
158
References
1
FWCI
2.08
Type
journal article
Language
en
Open access
hybrid

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

How to cite

Cite CoChat for the checks on this page, and the paper for its own findings.

This page
CoChat. (2026). Citation check: O-GlcNAc Transferase Is in a Functional Complex with Protein Phosphatase 1 Catalytic Subunits. https://app.cochat.ai/papers/10.1074/jbc.m406481200
The paper
Wells, L., Kreppel, L. K., Comer, F. I., Wadzinski, B. E., & Hart, G. W. (2004). O-GlcNAc Transferase Is in a Functional Complex with Protein Phosphatase 1 Catalytic Subunits. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.m406481200

Data sources

Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.