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10.1007/s00018-009-8712-7 http://scihub22266oqcxt.onion/10.1007/s00018-009-8712-7 19194658!11115538!19194658     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=19194658&cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\19194658.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Cell+Mol+Life+Sci 2009 ; 66 (11-12): 1924-38 Nephropedia Template TP {{tp|p=19194658|t=2009. Regulation of cullin-RING E3 ubiquitin-ligases by neddylation and dimerization |pdf=|usr=}}{{19194658}} gab.com Text Regulation of cullin-RING E3 ubiquitin-ligases by neddylation and dimerization JO: Cell Mol Life Sci http://www.kidney.de/pget.php?&tw=1&pmid=19194658 #FOAvip Cullin-RING E3 ubiquitin-Ligases (CRLs) are the most prominent class of ubiquitin-ligases. By controlling the stability of a cohort of key regulators, CRLs impinge on many cellular and biological processes such as immunity, development, transcription, cell signalling and cell cycle progression. CRLs are multi-subunit complexes composed of a catalytic site and a substrate recognition module nucleated around a cullin scaffold protein. Most eukaryotic genomes encode at least five distinct cullins, and each of these cullins recruits a specific substrate-recognition module such that CRL complexes are modular. Despite their considerable diversity, CRLs are regulated by similar mechanisms. In particular, recent observations indicate that conformational variability induced by CRL dimerization and by conjugation of the ubiquitin-like protein NEDD8 on the cullin subunit stimulates substrate polyubiquitination. In this review, we discuss the composition of CRL complexes and the various molecular mechanisms controlling their activity. Twit Text FOAVip Regulation of cullin-RING E3 ubiquitin-ligases by neddylation and dimerization ????Cell Mol Life Sci http://www.kidney.de/pget.php?&tw=1&pmid=19194658 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=19194658 #FOAvip English Wikipedia <ref>{{Cite pmid|19194658}}</ref> Regulation of cullin-RING E3 ubiquitin-ligases by neddylation and dimerization #MMPMID19194658 Merlet J; Burger J; Gomes JE; Pintard L Cell Mol Life Sci 2009[Jun]; 66 (11-12): 1924-38 PMID19194658show ga Cullin-RING E3 ubiquitin-Ligases (CRLs) are the most prominent class of ubiquitin-ligases. By controlling the stability of a cohort of key regulators, CRLs impinge on many cellular and biological processes such as immunity, development, transcription, cell signalling and cell cycle progression. CRLs are multi-subunit complexes composed of a catalytic site and a substrate recognition module nucleated around a cullin scaffold protein. Most eukaryotic genomes encode at least five distinct cullins, and each of these cullins recruits a specific substrate-recognition module such that CRL complexes are modular. Despite their considerable diversity, CRLs are regulated by similar mechanisms. In particular, recent observations indicate that conformational variability induced by CRL dimerization and by conjugation of the ubiquitin-like protein NEDD8 on the cullin subunit stimulates substrate polyubiquitination. In this review, we discuss the composition of CRL complexes and the various molecular mechanisms controlling their activity. |*Protein Multimerization[MESH] |Animals[MESH] |Arabidopsis Proteins/metabolism[MESH] |Cullin Proteins/chemistry/*metabolism[MESH] |Drosophila Proteins/metabolism[MESH] |Enzyme Activation[MESH] |NEDD8 Protein[MESH] |Phosphorylation[MESH] |Protein Binding[MESH] |Saccharomyces cerevisiae Proteins/metabolism[MESH] |Substrate Specificity[MESH] |Ubiquitination[MESH]Regulation of cullin-RING E3 ubiquitin-ligases by neddylation and dime(epmc).pdf DeepDyve Pubget Overpricing