Specificity for latent C termini links the E3 ubiquitin ligase CHIP to caspases
Specificity for latent C termini links the E3 ubiquitin ligase CHIP to caspases
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Publisher
New York: Nature Publishing Group US
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Language
English
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Publisher
New York: Nature Publishing Group US
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Contents
Protein–protein interactions between E3 ubiquitin ligases and protein termini help shape the proteome. These interactions are sensitive to proteolysis, which alters the ensemble of cellular N and C termini. Here we describe a mechanism wherein caspase activity reveals latent C termini that are then recognized by the E3 ubiquitin ligase CHIP. Using...
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Full title
Specificity for latent C termini links the E3 ubiquitin ligase CHIP to caspases
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TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_6693490
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_6693490
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ISSN
1552-4450
E-ISSN
1552-4469
DOI
10.1038/s41589-019-0322-6
