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10.1111/febs.14039 http://scihub22266oqcxt.onion/10.1111/febs.14039 28196299!7163952!28196299     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=28196299&cmd=llinks): Failed to open stream: HTTP request failed! 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Activity-based probes for the ubiquitin conjugation-deconjugation machinery: new chemistries, new tools, and new insights |pdf=|usr=}}{{28196299}} gab.com Text Activity-based probes for the ubiquitin conjugation-deconjugation machinery: new chemistries, new tools, and new insights JO: FEBS J http://www.kidney.de/pget.php?&tw=1&pmid=28196299 #FOAvip The reversible post-translational modification of proteins by ubiquitin and ubiquitin-like proteins regulates almost all cellular processes, by affecting protein degradation, localization, and complex formation. Deubiquitinases (DUBs) are proteases that remove ubiquitin modifications or cleave ubiquitin chains. Most DUBs are cysteine proteases, which makes them well suited for study by activity-based probes. These DUB probes report on deubiquitinase activity by reacting covalently with the active site in an enzyme-catalyzed manner. They have proven to be important tools to study DUB selectivity and proteolytic activity in different settings, to identify novel DUBs, and to characterize deubiquitinase inhibitors. Inspired by the efficacy of activity-based probes for DUBs, several groups have recently reported probes for the ubiquitin conjugation machinery (E1, E2, and E3 enzymes). Many of these enzymes, while not proteases, also posses active site cysteine residues and can be targeted by covalent probes. In this review, we will discuss how features of the probe (cysteine-reactive group, recognition element, and reporter tag) affect reactivity and suitability for certain experimental applications. We will also review the diverse applications of the current probes, and discuss the need for new probe types to study emerging aspects of ubiquitin biology. Twit Text FOAVip Activity-based probes for the ubiquitin conjugation-deconjugation machinery: new chemistries, new tools, and new insights ????FEBS J http://www.kidney.de/pget.php?&tw=1&pmid=28196299 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28196299 #FOAvip English Wikipedia <ref>{{Cite pmid|28196299}}</ref> Activity-based probes for the ubiquitin conjugation-deconjugation machinery: new chemistries, new tools, and new insights #MMPMID28196299 Hewings DS; Flygare JA; Bogyo M; Wertz IE FEBS J 2017[May]; 284 (10): 1555-1576 PMID28196299show ga The reversible post-translational modification of proteins by ubiquitin and ubiquitin-like proteins regulates almost all cellular processes, by affecting protein degradation, localization, and complex formation. Deubiquitinases (DUBs) are proteases that remove ubiquitin modifications or cleave ubiquitin chains. Most DUBs are cysteine proteases, which makes them well suited for study by activity-based probes. These DUB probes report on deubiquitinase activity by reacting covalently with the active site in an enzyme-catalyzed manner. They have proven to be important tools to study DUB selectivity and proteolytic activity in different settings, to identify novel DUBs, and to characterize deubiquitinase inhibitors. Inspired by the efficacy of activity-based probes for DUBs, several groups have recently reported probes for the ubiquitin conjugation machinery (E1, E2, and E3 enzymes). Many of these enzymes, while not proteases, also posses active site cysteine residues and can be targeted by covalent probes. In this review, we will discuss how features of the probe (cysteine-reactive group, recognition element, and reporter tag) affect reactivity and suitability for certain experimental applications. We will also review the diverse applications of the current probes, and discuss the need for new probe types to study emerging aspects of ubiquitin biology. |Animals[MESH] |Deubiquitinating Enzymes/metabolism[MESH] |Humans[MESH] |Peptide Hydrolases/metabolism[MESH] |Proteasome Endopeptidase Complex/metabolism[MESH] |Protein Processing, Post-Translational[MESH] |Ubiquitin-Specific Proteases/metabolism[MESH]Activity-based probes for the ubiquitin conjugation-deconjugation mach(epmc).pdf DeepDyve Pubget Overpricing