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Cited by 538

The DOI matches its Crossref record; 38 of the 38 references it cites were found in a registry or an index.

A chemical approach for identifying O -GlcNAc-modified proteins in cells

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Vocadlo, David J., Hang, Howard C., Kim, Eun-Ju, Hanover, John A., Bertozzi, Carolyn R.·2003·Proceedings of the National Academy of Sciences

Abstract

The glycosylation of serine and threonine residues with a single GlcNAc moiety is a dynamic posttranslational modification of many nuclear and cytoplasmic proteins. We describe a chemical strategy directed toward identifying O -GlcNAc-modified proteins from living cells or proteins modified in vitro . We demonstrate, in vitro , that each enzyme in the hexosamine salvage pathway, and the enzymes that affect this dynamic modification (UDP-GlcNAc:polypeptidtyltransferase and O -GlcNAcase), tolerate analogues of their natural substrates in which the N -acyl side chain has been modified to bear a bio-orthogonal azide moiety. Accordingly, treatment of cells with N -azidoacetylglucosamine results in the metabolic incorporation of the azido sugar into nuclear and cytoplasmic proteins. These O -azidoacetylglucosamine-modified proteins can be covalently derivatized with various biochemical probes at the site of protein glycosylation by using the Staudinger ligation. The approach was validated by metabolic labeling of nuclear pore protein p62, which is known to be posttranslationally modified with O -GlcNAc. This strategy will prove useful for both the identification of O -GlcNAc-modified proteins and the elucidation of the specific residues that bear this saccharide.

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Metadata

Authors
Vocadlo, D. J., Hang, H. C., Kim, E.-J., Hanover, J. A., & Bertozzi, C. R.
Venue
Proceedings of the National Academy of Sciences
Published
2003-07-21
Volume
100
Issue
16
Pages
9116-9121
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2089693526
Cited by
538
References
38
FWCI
6.00
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: A chemical approach for identifying O -GlcNAc-modified proteins in cells. https://app.cochat.ai/papers/10.1073/pnas.1632821100
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Vocadlo, D. J., Hang, H. C., Kim, E.-J., Hanover, J. A., & Bertozzi, C. R. (2003). A chemical approach for identifying O -GlcNAc-modified proteins in cells. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.1632821100

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