The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.
O-GlcNAc profiling: from proteins to proteomes
Open accessAbstract
O-linked β-D-N-acetylglucosamine (O-GlcNAc) modification (O-GlcNAcylation) onto serine and threonine residues of proteins is an important post-translational modification (PTM), which is involved in many crucial biological processes including transcription, translation, proteasomal degradation, and signal transduction. Aberrant protein O-GlcNAcylation is directly linked to the pathological progression of chronic diseases including diabetes, cancer, and neurodegenerative disorders. Identification, site mapping, and quantification of O-GlcNAc proteins are a prerequisite to decipher their functions. In this review, we mainly focus on technological developments regarding O-GlcNAc protein profiling. Specifically, on one hand, we show how these techniques are being used for the comprehensive characterization of certain targeted proteins in which biologists are most interested. On the other hand, we present several newly developed approaches for O-GlcNAcomic profiling as well as how they provide us with a systems perspective to crosstalk amongst different PTMs and complicated biological events. Promising technical trends are also highlighted to evoke more efforts by diverse laboratories, which would further expand our understanding of the physiological and pathological roles of protein O-GlcNAcylation in chronic diseases.
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Cites
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Self-citationMapping O-GlcNAc modification sites on tau and generation of a site-specific O-GlcNAc tau antibody
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Cited by
Mass spectrometry approaches to glycomic and glycoproteomic analyses
Ruhaak, L. R., Xu, G., Li, Q., Goonatilleke, E., & Lebrilla, C. B. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00732 · Cited by 395
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Mass Spectrometry-Based Detection and Assignment of Protein Posttranslational Modifications
Doll, S., & Burlingame, A. L. (2015) · ACS Chemical Biology · doi:10.1021/cb500904b · Cited by 261
O-GlcNAc regulates gene expression by controlling detained intron splicing
Tan, Z.-W., Fei, G., Paulo, J. A., Bellaousov, S., Martin, S. E. S., Duveau, D. Y., Thomas, C. J., Gygi, S. P., Boutz, P. L., & Walker, S. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa263 · Cited by 119
Qin, W., Myers, S. A., Carey, D. K., Carr, S. A., & Ting, A. Y. (2021) · Nature Communications · doi:10.1038/s41467-021-25259-2 · Cited by 84
Metadata
- Authors
- Ma, J., & Hart, G. W.
- Venue
- Clinical Proteomics
- Published
- 2014-03-05
- Volume
- 11
- Issue
- 1
- Pages
- 8-8
- ISSN
- 1542-6416 (ISSN-L)
- 1559-0275
- OpenAlex
- W2107601138
- Cited by
- 276
- References
- 9
- FWCI
- 11.68
- Type
- journal article
- Language
- en
- Open access
- gold
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