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10.1021/cb2004059 http://scihub22266oqcxt.onion/10.1021/cb2004059 C4805399!4805399!22196026     free     free     free       ACS+Chem+Biol 2012 ; 7 (1): 52-63 Nephropedia Template TP {{tp|p=22196026|t=2012. Unraveling the Complexity of Ubiquitin Signaling |pdf=|usr=}}{{22196026}} gab.com Text Unraveling the Complexity of Ubiquitin Signaling JO: ACS Chem Biol http://www.kidney.de/pget.php?&tw=1&pmid=22196026 #FOAvip Protein ubiquitination, the covalent attachment of ubiquitin to target proteins, has emerged as one of the most prevalent posttranslational modifications (PTMs), regulating nearly every cellular pathway. The diversity of signaling associated with this particular PTM stems from the myriad ways in which a target protein can be modified by ubiquitin, e.g., monoubiquitin, multi-monoubiquitin, and polyubiquitin linkages. In this Review, we focus on developments in both enzymatic and chemical methods that engender ubiquitin with new chemical and physical properties. Moreover, we highlight how these methods have enabled studies directed toward (i) characterizing enzymes responsible for reversing the ubiquitin modification, (ii) understanding the influence of ubiquitin on protein function and crosstalk with other PTMs, and (iii) uncovering the impact of polyubiquitin chain linkage and length on downstream signaling events. Twit Text FOAVip Unraveling the Complexity of Ubiquitin Signaling ????ACS Chem Biol http://www.kidney.de/pget.php?&tw=1&pmid=22196026 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=22196026 #FOAvip English Wikipedia <ref>{{Cite pmid|22196026}}</ref> Unraveling the Complexity of Ubiquitin Signaling #MMPMID22196026 Strieter ER; Korasick DA ACS Chem Biol 2012[Jan]; 7 (1): 52-63 PMID22196026show ga Protein ubiquitination, the covalent attachment of ubiquitin to target proteins, has emerged as one of the most prevalent posttranslational modifications (PTMs), regulating nearly every cellular pathway. The diversity of signaling associated with this particular PTM stems from the myriad ways in which a target protein can be modified by ubiquitin, e.g., monoubiquitin, multi-monoubiquitin, and polyubiquitin linkages. In this Review, we focus on developments in both enzymatic and chemical methods that engender ubiquitin with new chemical and physical properties. Moreover, we highlight how these methods have enabled studies directed toward (i) characterizing enzymes responsible for reversing the ubiquitin modification, (ii) understanding the influence of ubiquitin on protein function and crosstalk with other PTMs, and (iii) uncovering the impact of polyubiquitin chain linkage and length on downstream signaling events. äUnraveling the Complexity of Ubiquitin Signaling (epmc).pdf DeepDyve Pubget Overpricing