Use my Search Websuite to scan PubMed, PMCentral, Journal Hosts and Journal Archives, FullText. Kick-your-searchterm to multiple Engines kick-your-query now !>

A dictionary by aggregated review articles of nephrology, medicine and the life sciences Your one-stop-run pathway from word to the immediate pdf of peer-reviewed on-topic knowledge.

10.1016/j.cell.2016.09.048 http://scihub22266oqcxt.onion/10.1016/j.cell.2016.09.048 C6055481!6055481!27768895     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=27768895&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 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Cell 2016 ; 167 (3): 763-773.e11 Nephropedia Template TP {{tp|p=27768895|t=2016. The Structure of the Polycystic Kidney Disease Channel PKD2 in Lipid Nanodiscs |pdf=|usr=}}{{27768895}} gab.com Text The Structure of the Polycystic Kidney Disease Channel PKD2 in Lipid Nanodiscs JO: Cell http://www.kidney.de/pget.php?&tw=1&pmid=27768895 #FOAvip The Polycystic Kidney Disease 2 (pkd2) gene is mutated in autosomal dominant polycystic kidney disease (ADPKD), one of the most common human monogenic disorders. Here, we present the cryo-EM structure of PKD2 in lipid bilayers at 3.0 Å resolution, which establishes PKD2 as a homotetrameric ion channel and provides insight into potential mechanisms for its activation. The PKD2 voltage-sensor domain retains two of four gating charges commonly found in those of voltage-gated ion channels. The PKD2 ion permeation pathway is constricted at the selectivity filter and near the cytoplasmic end of S6, suggesting that two gates regulate ion conduction. The extracellular domain of PKD2, a hotspot for ADPKD pathogenic mutations, contributes to channel assembly and strategically interacts with the transmembrane core, likely serving as a physical substrate for extracellular stimuli to allosterically gate the channel. Finally, our structure establishes the molecular basis for the majority of pathogenic mutations in pkd2-related ADPKD. Twit Text FOAVip The Structure of the Polycystic Kidney Disease Channel PKD2 in Lipid Nanodiscs ????Cell http://www.kidney.de/pget.php?&tw=1&pmid=27768895 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27768895 #FOAvip English Wikipedia <ref>{{Cite pmid|27768895}}</ref> The Structure of the Polycystic Kidney Disease Channel PKD2 in Lipid Nanodiscs #MMPMID27768895 Shen PS; Yang X; DeCaen PG; Liu X; Bulkley D; Clapham DE; Cao E Cell 2016[Oct]; 167 (3): 763-773.e11 PMID27768895show ga The Polycystic Kidney Disease 2 (pkd2) gene is mutated in autosomal dominant polycystic kidney disease (ADPKD), one of the most common human monogenic disorders. Here, we present the cryo-EM structure of PKD2 in lipid bilayers at 3.0 Å resolution, which establishes PKD2 as a homotetrameric ion channel and provides insight into potential mechanisms for its activation. The PKD2 voltage-sensor domain retains two of four gating charges commonly found in those of voltage-gated ion channels. The PKD2 ion permeation pathway is constricted at the selectivity filter and near the cytoplasmic end of S6, suggesting that two gates regulate ion conduction. The extracellular domain of PKD2, a hotspot for ADPKD pathogenic mutations, contributes to channel assembly and strategically interacts with the transmembrane core, likely serving as a physical substrate for extracellular stimuli to allosterically gate the channel. Finally, our structure establishes the molecular basis for the majority of pathogenic mutations in pkd2-related ADPKD. äThe Structure of the Polycystic Kidney Disease Channel PKD2 in Lipid N(epmc).pdf DeepDyve Pubget Overpricing