The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Substrate Specificities of Caspase Family Proteases
Open accessAbstract
The caspase family represents a new class of intracellular cysteine proteases with known or suspected roles in cytokine maturation and apoptosis. These enzymes display a preference for Asp in the P1 position of substrates. To clarify differences in the biological roles of the interleukin-1beta converting enzyme (ICE) family proteases, we have examined in detail the specificities beyond the P1 position of caspase-1, -2, -3, -4, -6, and -7 toward minimal length peptide substrates in vitro. We find differences and similarities between the enzymes that suggest a functional subgrouping of the family different from that based on overall sequence alignment. The primary specificities of ICE homologs explain many observed enzyme preferences for macromolecular substrates and can be used to support predictions of their natural function(s). The results also suggest the design of optimal peptidic substrates and inhibitors.
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Boldin, M. P., Varfolomeev, E. E., Pancer, Z., Mett, I. L., Camonis, J. H., & Wallach, D. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.14.7795 · Cited by 993
Cited by
Mammalian Caspases: Structure, Activation, Substrates, and Functions During Apoptosis
Earnshaw, W. C., Martins, L. M., & Kaufmann, S. H. (1999) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.68.1.383 · Cited by 2,760
Caspases: Intracellular Signaling by Proteolysis
Salvesen, G. S., & Dixit, V. M. (1997) · Cell · doi:10.1016/s0092-8674(00)80430-4 · Cited by 2,117
Caspase structure, proteolytic substrates, and function during apoptotic cell death
Nicholson, D. (1999) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4400598 · Cited by 1,543
Activation and Cleavage of Caspase-3 in Apoptosis Induced by Experimental Cerebral Ischemia
Namura, S., Zhu, J., Fink, K., Endres, M., Srinivasan, A., Tomaselli, K. J., Yuan, J., & Moskowitz, M. A. (1998) · The Journal of Neuroscience · doi:10.1523/jneurosci.18-10-03659.1998 · Cited by 893
Julien, O., & Wells, J. A. (2017) · Cell Death & Differentiation · doi:10.1038/cdd.2017.44 · Cited by 816
Metadata
- Authors
- Talanian, R. V., Quinlan, C., Trautz, S., Hackett, M. C., Mankovich, J. A., Banach, D., Ghayur, T., Brady, K. D., & Wong, W. W.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1997-04
- Volume
- 272
- Issue
- 15
- Pages
- 9677-9682
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1977219317
- Cited by
- 876
- References
- 1
- FWCI
- 21.71
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Talanian, R. V., Quinlan, C., Trautz, S., Hackett, M. C., Mankovich, J. A., Banach, D., Ghayur, T., Brady, K. D., & Wong, W. W. (1997). Substrate Specificities of Caspase Family Proteases. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.272.15.9677
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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