Proteome‐wide identification of mycobacterial pupylation targets
Proteome‐wide identification of mycobacterial pupylation targets
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Publisher
London: Nature Publishing Group UK
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Language
English
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London: Nature Publishing Group UK
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Contents
Mycobacteria use a unique system for covalently modifying proteins based on the conjugation of a small protein, referred to as prokaryotic ubiquitin‐like protein (PUP). In this study, we report a proteome‐wide analysis of endogenous pupylation targets in the model organism
Mycobacterium smegmatis
. On affinity capture, a total of 243 candidat...
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Proteome‐wide identification of mycobacterial pupylation targets
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TN_cdi_doaj_primary_oai_doaj_org_article_1e3255fd776f4025bd206adab5773334
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_1e3255fd776f4025bd206adab5773334
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ISSN
1744-4292
E-ISSN
1744-4292
DOI
10.1038/msb.2010.39
