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10.1101/gad.257568.114 http://scihub22266oqcxt.onion/10.1101/gad.257568.114 C4421984!4421984 !25917549     free     free     free 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\25917549 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Genes+Dev 2015 ; 29 (9 ): 961-74 Nephropedia Template TP {{tp|p=25917549 |t=2015. Structural mechanisms of DREAM complex assembly and regulation |pdf=|usr=}}{{25917549 }} gab.com Text Structural mechanisms of DREAM complex assembly and regulation JO: Genes Dev http://www.kidney.de/pget.php?&tw=1&pmid=25917549 #FOAvip The DREAM complex represses cell cycle genes during quiescence through scaffolding MuvB proteins with E2F4/5 and the Rb tumor suppressor paralog p107 or p130. Upon cell cycle entry, MuvB dissociates from p107/p130 and recruits B-Myb and FoxM1 for up-regulating mitotic gene expression. To understand the biochemical mechanisms underpinning DREAM function and regulation, we investigated the structural basis for DREAM assembly. We identified a sequence in the MuvB component LIN52 that binds directly to the pocket domains of p107 and p130 when phosphorylated on the DYRK1A kinase site S28. A crystal structure of the LIN52-p107 complex reveals that LIN52 uses a suboptimal LxSxExL sequence together with the phosphate at nearby S28 to bind the LxCxE cleft of the pocket domain with high affinity. The structure explains the specificity for p107/p130 over Rb in the DREAM complex and how the complex is disrupted by viral oncoproteins. Based on insights from the structure, we addressed how DREAM is disassembled upon cell cycle entry. We found that p130 and B-Myb can both bind the core MuvB complex simultaneously but that cyclin-dependent kinase phosphorylation of p130 weakens its association. Together, our data inform a novel target interface for studying MuvB and p130 function and the design of inhibitors that prevent tumor escape in quiescence. Twit Text FOAVip Structural mechanisms of DREAM complex assembly and regulation ????Genes Dev http://www.kidney.de/pget.php?&tw=1&pmid=25917549 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25917549 #FOAvip English Wikipedia <ref>{{Cite pmid|25917549 }}</ref> Structural mechanisms of DREAM complex assembly and regulation #MMPMID25917549 Guiley KZ ; Liban TJ ; Felthousen JG ; Ramanan P ; Litovchick L ; Rubin SM Genes Dev 2015[May]; 29 (9 ): 961-74 PMID25917549 show ga The DREAM complex represses cell cycle genes during quiescence through scaffolding MuvB proteins with E2F4/5 and the Rb tumor suppressor paralog p107 or p130. Upon cell cycle entry, MuvB dissociates from p107/p130 and recruits B-Myb and FoxM1 for up-regulating mitotic gene expression. To understand the biochemical mechanisms underpinning DREAM function and regulation, we investigated the structural basis for DREAM assembly. We identified a sequence in the MuvB component LIN52 that binds directly to the pocket domains of p107 and p130 when phosphorylated on the DYRK1A kinase site S28. A crystal structure of the LIN52-p107 complex reveals that LIN52 uses a suboptimal LxSxExL sequence together with the phosphate at nearby S28 to bind the LxCxE cleft of the pocket domain with high affinity. The structure explains the specificity for p107/p130 over Rb in the DREAM complex and how the complex is disrupted by viral oncoproteins. Based on insights from the structure, we addressed how DREAM is disassembled upon cell cycle entry. We found that p130 and B-Myb can both bind the core MuvB complex simultaneously but that cyclin-dependent kinase phosphorylation of p130 weakens its association. Together, our data inform a novel target interface for studying MuvB and p130 function and the design of inhibitors that prevent tumor escape in quiescence. |*Gene Expression Regulation [MESH] |Cell Cycle Proteins/metabolism [MESH] |Cell Cycle/*genetics [MESH] |Crystallization [MESH] |Humans [MESH] |Multiprotein Complexes/*chemistry/*metabolism [MESH] |Phosphorylation [MESH] |Protein Binding [MESH] |Protein Structure, Tertiary [MESH] |Retinoblastoma-Like Protein p107/chemistry/metabolism [MESH] |Retinoblastoma-Like Protein p130/chemistry/metabolism [MESH] |Sequence Alignment [MESH]Structural mechanisms of DREAM complex assembly and regulation (epmc).pdf DeepDyve Pubget Overpricing