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10.1038/srep28488 http://scihub22266oqcxt.onion/10.1038/srep28488 C4917820!4917820!27335147     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=27335147&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 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Sci+Rep 2016 ; 6 (ä): ä Nephropedia Template TP {{tp|p=27335147|t=2016. Structural basis for autoinhibition and its relief of MOB1 in the Hippo pathway |pdf=|usr=}}{{27335147}} gab.com Text Structural basis for autoinhibition and its relief of MOB1 in the Hippo pathway JO: Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=27335147 #FOAvip MOB1 protein is a key regulator of large tumor suppressor 1/2 (LATS1/2) kinases in the Hippo pathway. MOB1 is present in an autoinhibited form and is activated by MST1/2-mediated phosphorylation, although the precise mechanisms responsible for autoinhibition and activation are unknown due to lack of an autoinhibited MOB1 structure. Here, we report on the crystal structure of full-length MOB1B in the autoinhibited form and a complex between the MOB1B core domain and the N-terminal regulation (NTR) domain of LATS1. The structure of full-length MOB1B shows that the N-terminal extension forms a short ?-strand, the SN strand, followed by a long conformationally flexible positively-charged linker and ?-helix, the Switch helix, which blocks the LATS1 binding surface of MOB1B. The Switch helix is stabilized by ?-sheet formation of the SN strand with the S2 strand of the MOB1 core domain. Phosphorylation of Thr12 and Thr35 residues structurally accelerates dissociation of the Switch helix from the LATS1-binding surface by the ?pull-the-string? mechanism, thereby enabling LATS1 binding. Twit Text FOAVip Structural basis for autoinhibition and its relief of MOB1 in the Hippo pathway ????Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=27335147 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27335147 #FOAvip English Wikipedia <ref>{{Cite pmid|27335147}}</ref> Structural basis for autoinhibition and its relief of MOB1 in the Hippo pathway #MMPMID27335147 Kim SY; Tachioka Y; Mori T; Hakoshima T Sci Rep 2016[]; 6 (ä): ä PMID27335147show ga MOB1 protein is a key regulator of large tumor suppressor 1/2 (LATS1/2) kinases in the Hippo pathway. MOB1 is present in an autoinhibited form and is activated by MST1/2-mediated phosphorylation, although the precise mechanisms responsible for autoinhibition and activation are unknown due to lack of an autoinhibited MOB1 structure. Here, we report on the crystal structure of full-length MOB1B in the autoinhibited form and a complex between the MOB1B core domain and the N-terminal regulation (NTR) domain of LATS1. The structure of full-length MOB1B shows that the N-terminal extension forms a short ?-strand, the SN strand, followed by a long conformationally flexible positively-charged linker and ?-helix, the Switch helix, which blocks the LATS1 binding surface of MOB1B. The Switch helix is stabilized by ?-sheet formation of the SN strand with the S2 strand of the MOB1 core domain. Phosphorylation of Thr12 and Thr35 residues structurally accelerates dissociation of the Switch helix from the LATS1-binding surface by the ?pull-the-string? mechanism, thereby enabling LATS1 binding. äStructural basis for autoinhibition and its relief of MOB1 in the Hipp(epmc).pdf DeepDyve Pubget Overpricing