The DOI matches its Crossref record; 48 of the 48 references it cites were found in a registry or an index.
Global Mapping of the Topography and Magnitude of Proteolytic Events in Apoptosis
Open accessAbstract
SUMMARY Proteolysis is a key regulatory process that promotes the (in)activation, translocation, and/or degradation of proteins. As such, there is considerable interest in methods to comprehensively characterize proteolytic pathways in biological systems. Here, we describe a robust and versatile proteomic platform that enables direct visualization of the topography and magnitude of proteolytic events on a global scale. We use this method to generate a proteome-wide map of proteolytic events induced by the intrinsic apoptotic pathway. This profile contained 91 characterized caspase substrates as well as 170 additional proteins not previously known to be cleaved during apoptosis. Surprisingly, the vast majority of proteolyzed proteins, regardless of the extent of cleavage, yielded persistent fragments that correspond to discrete protein domains, suggesting that the generation of active effector proteins may be a principal function of apoptotic proteolytic cascades.
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Julien, O., & Wells, J. A. (2017) · Cell Death & Differentiation · doi:10.1038/cdd.2017.44 · Cited by 816
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Slavoff, S. A., Mitchell, A. J., Schwaid, A. G., Cabili, M. N., Ma, J., Levin, J. Z., Karger, A. D., Budnik, B. A., Rinn, J. L., & Saghatelian, A. (2013) · Nature Chemical Biology · doi:10.1038/nchembio.1120 · Cited by 686
Caspase Substrates and Cellular Remodeling
Crawford, E. D., & Wells, J. A. (2011) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061809-121639 · Cited by 339
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Metadata
- Authors
- Dix, M. M., Simon, G. M., & Cravatt, B. F.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2008-08
- Volume
- 134
- Issue
- 4
- Pages
- 679-691
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2060470491
- Cited by
- 366
- References
- 48
- FWCI
- 15.62
- Type
- journal article
- Language
- en
- Open access
- bronze
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