The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Glycopeptide-specific monoclonal antibodies suggest new roles for O-GlcNAc
Open accessAbstract
Studies of post-translational modification by β-N-acetyl-D-glucosamine (O-GlcNAc) are hampered by a lack of efficient tools such as O-GlcNAc specific antibodies that can be employed for detection, isolation, and site localization. We have obtained a large panel of O-GlcNAc-specific IgG MAbs having a broad spectrum of binding partners by combining three-component immunogen methodology with hybridoma technology. Immunoprecipitation followed by large-scale shotgun proteomics led to the identification of more than 200 mammalian O-GlcNAc modified proteins, including a large number of novel glycoproteins. A substantial number of the glycoproteins were only enriched by one of the antibodies and this observation combined with results of inhibition ELISAs suggests that the antibodies in addition to their O-GlcNAc-dependence also appear to have different, but overlapping, local peptide determinants. The MAbs made it possible to delineate differentially modified proteins of liver in response to trauma-hemorrhage and resuscitation in a rat model.
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Cites
Cycling of O-linked β-N-acetylglucosamine on nucleocytoplasmic proteins
Hart, G. W., Housley, M. P., & Slawson, C. (2007) · Nature · doi:10.1038/nature05815 · Cited by 1,418
Ramirez-Correa, G. A., Jin, W., Wang, Z., Zhong, X., Gao, W. D., Dias, W. B., Vecoli, C., Hart, G. W., & Murphy, A. M. (2008) · Circulation Research · doi:10.1161/circresaha.108.184978 · Cited by 145
Cited by
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Hallmarks of glycosylation in cancer
Munkley, J., & Elliott, D. J. (2016) · Oncotarget · doi:10.18632/oncotarget.8155 · Cited by 521
Mapping O-GlcNAc modification sites on tau and generation of a site-specific O-GlcNAc tau antibody
Yuzwa, S. A., Yadav, A. K., Skorobogatko, Y., Clark, T., Vosseller, K., & Vocadlo, D. J. (2011) · Amino Acids · doi:10.1007/s00726-010-0705-1 · Cited by 130
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
Metadata
- Authors
- Teo, C. F., Ingale, S., Wolfert, M. A., Elsayed, G. A., Nöt, L. G., Chatham, J. C., Wells, L., & Boons, G.-J.
- Venue
- Nature Chemical Biology
- Published
- 2010-03-21
- Volume
- 6
- Issue
- 5
- Pages
- 338-343
- ISSN
- 1552-4450 (ISSN-L)
- 1552-4469
- OpenAlex
- W2070859810
- Cited by
- 181
- References
- 2
- FWCI
- 6.73
- Type
- journal article
- Language
- en
- Open access
- green
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- Teo, C. F., Ingale, S., Wolfert, M. A., Elsayed, G. A., Nöt, L. G., Chatham, J. C., Wells, L., & Boons, G.-J. (2010). Glycopeptide-specific monoclonal antibodies suggest new roles for O-GlcNAc. Nature Chemical Biology. https://doi.org/10.1038/nchembio.338
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