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10.1038/ncomms12437 http://scihub22266oqcxt.onion/10.1038/ncomms12437 C4992140!4992140!27534274     free     free     free Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Nat+Commun 2016 ; 7 (ä): ä Nephropedia Template TP {{tp|p=27534274|t=2016. The hydrolethalus syndrome protein HYLS-1 regulates formation of the ciliary gate |pdf=|usr=}}{{27534274}} gab.com Text The hydrolethalus syndrome protein HYLS-1 regulates formation of the ciliary gate JO: Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=27534274 #FOAvip Transition fibres (TFs), together with the transition zone (TZ), are basal ciliary structures thought to be crucial for cilium biogenesis and function by acting as a ciliary gate to regulate selective protein entry and exit. Here we demonstrate that the centriolar and basal body protein HYLS-1, the C. elegans orthologue of hydrolethalus syndrome protein 1, is required for TF formation, TZ organization and ciliary gating. Loss of HYLS-1 compromises the docking and entry of intraflagellar transport (IFT) particles, ciliary gating for both membrane and soluble proteins, and axoneme assembly. Additional depletion of the TF component DYF-19 in hyls-1 mutants further exacerbates TZ anomalies and completely abrogates ciliogenesis. Our data support an important role for HYLS-1 and TFs in establishment of the ciliary gate and underline the importance of selective protein entry for cilia assembly. Twit Text FOAVip The hydrolethalus syndrome protein HYLS-1 regulates formation of the ciliary gate ????Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=27534274 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27534274 #FOAvip English Wikipedia <ref>{{Cite pmid|27534274}}</ref> The hydrolethalus syndrome protein HYLS-1 regulates formation of the ciliary gate #MMPMID27534274 Wei Q; Zhang Y; Schouteden C; Zhang Y; Zhang Q; Dong J; Wonesch V; Ling K; Dammermann A; Hu J Nat Commun 2016[]; 7 (ä): ä PMID27534274show ga Transition fibres (TFs), together with the transition zone (TZ), are basal ciliary structures thought to be crucial for cilium biogenesis and function by acting as a ciliary gate to regulate selective protein entry and exit. Here we demonstrate that the centriolar and basal body protein HYLS-1, the C. elegans orthologue of hydrolethalus syndrome protein 1, is required for TF formation, TZ organization and ciliary gating. Loss of HYLS-1 compromises the docking and entry of intraflagellar transport (IFT) particles, ciliary gating for both membrane and soluble proteins, and axoneme assembly. Additional depletion of the TF component DYF-19 in hyls-1 mutants further exacerbates TZ anomalies and completely abrogates ciliogenesis. Our data support an important role for HYLS-1 and TFs in establishment of the ciliary gate and underline the importance of selective protein entry for cilia assembly. äThe hydrolethalus syndrome protein HYLS-1 regulates formation of the c(epmc).pdf DeepDyve Pubget Overpricing