CoChat
Sign Up
Cited by 364Glycosylation and Glycoproteins ResearchAlzheimer's disease research and treatmentsCarbohydrate Chemistry and Synthesis

The DOI matches its Crossref record; 61 of the 61 references it cites were found in a registry or an index.

The Microtubule-associated Protein Tau Is Extensively Modified with O-linked N-acetylglucosamine

Open access
Arnold, C. Shane, Johnson, GailV.W., Cole, Robert N., Dong, Dennis L.-Y., Lee, Michael, Hart, Gerald W.·1996·Journal of Biological Chemistry
DOI 10.1074/jbc.271.46.28741
Open this paper in CoChat — free account

Abstract

Tau is a family of phosphoproteins that are important in modulating microtubule stability in neurons. In Alzheimer's disease tau is abnormally hyperphosphorylated, no longer binds microtubules, and self-assembles to form paired helical filaments that likely contribute to neuron death. Here we demonstrate that normal bovine tau is multiply modified by Ser(Thr)-O-linked N-acetylglucosamine, a dynamic and abundant post-translational modification that is often reciprocal to Ser(Thr)-phosphorylation. O-GlcNAcylation of tau was demonstrated by blotting with succinylated wheat germ agglutinin and by probing with bovine milk beta(1,4)galactosyltransferase. Structural analyses confirm the linkage and the saccharide structure. Tau splicing variants are multiply O-GlcNAcylated at similar sites, with an average stoichiometry of greater than 4 mol of O-linked N-acetylglucosamine/mol of tau. However, the number of sites occupied appears to be greater than 12, suggesting substoichiometric occupancy at any given site. A similar relationship between average stoichiometry and site-occupancy has also been described for the phosphorylation of tau. Site-specific or stoichiometric changes in O-GlcNAcylation may not only modulate tau function but may also play a role in the formation of paired helical filaments.

Overview

Integrity signals

Registry

Crossref · 10.1074/jbc.271.46.28741

Cites

61 of 61 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Verification

Claims the paper makes

We couldn’t retrieve this paper’s full text, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Citations

Cites

Show all 61 references

Research works printed but not linked: 3

  1. Himmler, 1989, Mol. Cell. Biol., 9, 1381
  2. Shaw, 1996, Oncogene, 12, 921
  3. Schaffner, 1973, Anal. Biochem., 197, 65

Cited by

Sorted by citations

Items 301–364 of 364

Related

See all

Metadata

Authors
Arnold, C. S., Johnson, G. W., Cole, R. N., Dong, D. L.-Y., Lee, M., & Hart, G. W.
Affiliations
University of Alabama at Birmingham (US)
Corresponding author
Hart, Gerald W.
ORCID
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1996-11
Volume
271
Issue
46
Pages
28741-28744
ISSN
0021-9258 (ISSN-L)
DOI
10.1074/jbc.271.46.28741
OpenAlex
W2066371153
Cited by
361
References
61
Citations by year
2026: 3 · 2025: 12 · 2024: 17 · 2023: 10 · 2022: 12 · 2021: 17 · 2020: 20 · 2019: 13 · 2018: 19 · 2017: 13 · 2016: 18 · 2015: 11 · 2014: 18 · 2013: 12 · 2012: 10
FWCI
2.15
Type
journal article
Language
en
Open access
Licence
Locations
  • Journal of Biological Chemistry (publishedVersion, cc-by-nc-nd)
  • PubMed (publishedVersion)
Funders
  • National Institutes of Health (5r01ns027538-10)
  • National Cancer Institute (R01CA42486, R01CA042486)
  • National Institute of General Medical Sciences (T32GM008111, 5-T32-GM08111-10)
  • National Institute of Neurological Disorders and Stroke (R01 NS 27538)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
  • Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
  • Physical Sciences › Chemistry › Organic Chemistry › Carbohydrate Chemistry and Synthesis
Keywords
tau protein, O-GlcNAcylation, N-acetylglucosamine, post-translational modification, paired helical filaments, Alzheimer's disease, microtubule binding, phosphorylation, site occupancy
MeSH terms
Acetylglucosamine, Amino Acid Sequence, Animals, Brain Chemistry, Cattle, Galactosyltransferases, Glycosylation, Molecular Sequence Data, Phosphorylation, tau Proteins

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