The DOI matches its Crossref record; 14 of the 14 references it cites were found in a registry or an index.
A Chemoenzymatic Approach toward the Rapid and Sensitive Detection of O -GlcNAc Posttranslational Modifications
Abstract
We report a new chemoenzymatic strategy for the rapid and sensitive detection of O-GlcNAc posttranslational modifications. The approach exploits the ability of an engineered mutant of beta-1,4-galactosyltransferase to selectively transfer an unnatural ketone functionality onto O-GlcNAc glycosylated proteins. Once transferred, the ketone moiety serves as a versatile handle for the attachment of biotin, thereby enabling chemiluminescent detection of the modified protein. Importantly, this approach permits the rapid visualization of proteins that are at the limits of detection using traditional methods. Moreover, it bypasses the need for radioactive precursors and captures the glycosylated species without perturbing metabolic pathways. We anticipate that this general chemoenzymatic strategy will have broad application to the study of posttranslational modifications.
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Cites
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Self-citationIdentification of GlcNAcylation sites of peptides and α-crystallin using Q-TOF mass spectrometry
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Cited by
Hart, G. W., Slawson, C., Ramirez-Correa, G., & Lagerlof, O. (2011) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060608-102511 · Cited by 1,317
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The Hexosamine Signaling Pathway: Deciphering the "O-GlcNAc Code"
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β- N -acetylglucosamine (O-GlcNAc) is part of the histone code
Sakabe, K., Wang, Z., & Hart, G. W. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1009023107 · Cited by 373
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Self-citation
Metadata
- Authors
- Khidekel, N., Arndt, S., Lamarre-Vincent, N., Lippert, A., Poulin-Kerstien, K. G., Ramakrishnan, B., Qasba, P. K., & Hsieh-Wilson, L. C.
- Venue
- Journal of the American Chemical Society
- Publisher
- American Chemical Society (ACS)
- Published
- 2003-12-01
- Volume
- 125
- Issue
- 52
- Pages
- 16162-16163
- ISSN
- 0002-7863 (ISSN-L)
- 1520-5126
- OpenAlex
- W2083510841
- Cited by
- 288
- References
- 14
- FWCI
- 2.47
- Type
- journal article
- Language
- en
- Open access
- closed
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