The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.
Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling
Open accessAbstract
Protein ubiquitination is a post-translational modification (PTM) that regulates various aspects of protein function by different mechanisms. Characterization of ubiquitination has lagged behind that of smaller PTMs, such as phosphorylation, largely because of the difficulty of isolating and identifying peptides derived from the ubiquitinated portion of proteins. To address this issue, we generated a monoclonal antibody that enriches for peptides containing lysine residues modified by diglycine, an adduct left at sites of ubiquitination after trypsin digestion. We use mass spectrometry to identify 374 diglycine-modified lysines on 236 ubiquitinated proteins from HEK293 cells, including 80 proteins containing multiple sites of ubiquitination. Seventy-two percent of these proteins and 92% of the ubiquitination sites do not appear to have been reported previously. Ubiquitin remnant profiling of the multi-ubiquitinated proteins proliferating cell nuclear antigen (PCNA) and tubulin α-1A reveals differential regulation of ubiquitination at specific sites by microtubule inhibitors, demonstrating the effectiveness of our method to characterize the dynamics of lysine ubiquitination.
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DAVID: Database for Annotation, Visualization, and Integrated Discovery
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Lysine acetylation targets protein complexes and co-regulates major cellular functions
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Cited by
Hornbeck, P. V., Kornhauser, J. M., Tkachev, S., Zhang, B., Skrzypek, E., Murray, B., Latham, V., & Sullivan, M. (2012) · Nucleic Acids Research · doi:10.1093/nar/gkr1122 · Cited by 1,646
Protein Analysis by Shotgun/Bottom-up Proteomics
Zhang, Y., Fonslow, B. R., Shan, B., Baek, M.-C., & Yates, J. R. (2013) · Chemical Reviews · doi:10.1021/cr3003533 · Cited by 1,491
The mitochondrial deubiquitinase USP30 opposes parkin-mediated mitophagy
Bingol, B., Tea, J. S., Phu, L., Reichelt, M., Bakalarski, C. E., Song, Q., Foreman, O., Kirkpatrick, D. S., & Sheng, M. (2014) · Nature · doi:10.1038/nature13418 · Cited by 855
Quantitative, High-Resolution Proteomics for Data-Driven Systems Biology
Cox, J., & Mann, M. (2011) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061308-093216 · Cited by 685
The tubulin code: Molecular components, readout mechanisms, and functions
Janke, C. (2014) · Journal of Cell Biology · doi:10.1083/jcb.201406055 · Cited by 532
Metadata
- Authors
- Xu, G., Paige, J. S., & Jaffrey, S. R.
- Venue
- Nature Biotechnology
- Published
- 2010-07-18
- Volume
- 28
- Issue
- 8
- Pages
- 868-873
- ISSN
- 0733-222X (ISSN-L)
- 1087-0156
- 1546-1696
- OpenAlex
- W2061184183
- Cited by
- 534
- References
- 7
- FWCI
- 12.29
- Type
- journal article
- Language
- en
- Open access
- green
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