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10.1002/bies.201500085 http://scihub22266oqcxt.onion/10.1002/bies.201500085 C4862669!4862669!26387779     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 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       Bioessays 2015 ; 37 (11): 1184-92 Nephropedia Template TP {{tp|p=26387779|t=2015. How the TRPA1 receptor transmits painful stimuli: Inner workings revealed by electron cryomicroscopy |pdf=|usr=}}{{26387779}} gab.com Text How the TRPA1 receptor transmits painful stimuli: Inner workings revealed by electron cryomicroscopy JO: Bioessays http://www.kidney.de/pget.php?&tw=1&pmid=26387779 #FOAvip A new high-resolution structure of a pain-sensing ion channel, TRPA1, provides a molecular scaffold to understand channel function. Unexpected structural features include a TRP-domain helix similar to TRPV1, a novel ligand-binding site, and an unusual C-terminal coiled coil stabilized by inositol hexakisphosphate (IP6). TRP-domain helices, which structurally act as a nexus for communication between the channel gates and its other domains, may thus be a feature conserved across the entire TRP family and, possibly, other allosterically-gated channels. Similarly, the TRPA1 antagonist-binding site could also represent a druggable location in other ion channels. Combined with known TRPA1 functional properties, the structural role for IP6 leads us to propose that polyphosphate unbinding could act as a molecular kill switch for TRPA1 inactivation. Finally, although packing of the TRPA1 membrane-proximal region hints at a mechanism for electrophile sensing, the details of how TRPA1 responds to noxious reactive electrophiles and temperature await future studies. Twit Text FOAVip How the TRPA1 receptor transmits painful stimuli: Inner workings revealed by electron cryomicroscopy ????Bioessays http://www.kidney.de/pget.php?&tw=1&pmid=26387779 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26387779 #FOAvip English Wikipedia <ref>{{Cite pmid|26387779}}</ref> How the TRPA1 receptor transmits painful stimuli: Inner workings revealed by electron cryomicroscopy #MMPMID26387779 Brewster MSJ; Gaudet R Bioessays 2015[Nov]; 37 (11): 1184-92 PMID26387779show ga A new high-resolution structure of a pain-sensing ion channel, TRPA1, provides a molecular scaffold to understand channel function. Unexpected structural features include a TRP-domain helix similar to TRPV1, a novel ligand-binding site, and an unusual C-terminal coiled coil stabilized by inositol hexakisphosphate (IP6). TRP-domain helices, which structurally act as a nexus for communication between the channel gates and its other domains, may thus be a feature conserved across the entire TRP family and, possibly, other allosterically-gated channels. Similarly, the TRPA1 antagonist-binding site could also represent a druggable location in other ion channels. Combined with known TRPA1 functional properties, the structural role for IP6 leads us to propose that polyphosphate unbinding could act as a molecular kill switch for TRPA1 inactivation. Finally, although packing of the TRPA1 membrane-proximal region hints at a mechanism for electrophile sensing, the details of how TRPA1 responds to noxious reactive electrophiles and temperature await future studies. äHow the TRPA1 receptor transmits painful stimuli: Inner workings revea(epmc).pdf DeepDyve Pubget Overpricing