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.

10.1038/ncomms11523 http://scihub22266oqcxt.onion/10.1038/ncomms11523 C4866515!4866515!27161080     free     free     free Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 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=27161080|t=2016. Phosphatidylserine exposure is required for ADAM17 sheddase function |pdf=|usr=}}{{27161080}} gab.com Text Phosphatidylserine exposure is required for ADAM17 sheddase function JO: Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=27161080 #FOAvip ADAM17, a prominent member of the ?Disintegrin and Metalloproteinase' (ADAM) family, controls vital cellular functions through cleavage of transmembrane substrates. Here we present evidence that surface exposure of phosphatidylserine (PS) is pivotal for ADAM17 to exert sheddase activity. PS exposure is tightly coupled to substrate shedding provoked by diverse ADAM17 activators. PS dependency is demonstrated in the following: (a) in Raji cells undergoing apoptosis; (b) in mutant PSA-3 cells with manipulatable PS content; and (c) in Scott syndrome lymphocytes genetically defunct in their capacity to externalize PS in response to intracellular Ca2+ elevation. Soluble phosphorylserine but not phosphorylcholine inhibits substrate cleavage. The isolated membrane proximal domain (MPD) of ADAM17 binds to PS but not to phosphatidylcholine liposomes. A cationic PS-binding motif is identified in this domain, replacement of which abrogates liposome-binding and renders the protease incapable of cleaving its substrates in cells. We speculate that surface-exposed PS directs the protease to its targets where it then executes its shedding function. Twit Text FOAVip Phosphatidylserine exposure is required for ADAM17 sheddase function ????Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=27161080 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27161080 #FOAvip English Wikipedia <ref>{{Cite pmid|27161080}}</ref> Phosphatidylserine exposure is required for ADAM17 sheddase function #MMPMID27161080 Sommer A; Kordowski F; Büch J; Maretzky T; Evers A; Andrä J; Düsterhöft S; Michalek M; Lorenzen I; Somasundaram P; Tholey A; Sönnichsen FD; Kunzelmann K; Heinbockel L; Nehls C; Gutsmann T; Grötzinger J; Bhakdi S; Reiss K Nat Commun 2016[]; 7 (ä): ä PMID27161080show ga ADAM17, a prominent member of the ?Disintegrin and Metalloproteinase' (ADAM) family, controls vital cellular functions through cleavage of transmembrane substrates. Here we present evidence that surface exposure of phosphatidylserine (PS) is pivotal for ADAM17 to exert sheddase activity. PS exposure is tightly coupled to substrate shedding provoked by diverse ADAM17 activators. PS dependency is demonstrated in the following: (a) in Raji cells undergoing apoptosis; (b) in mutant PSA-3 cells with manipulatable PS content; and (c) in Scott syndrome lymphocytes genetically defunct in their capacity to externalize PS in response to intracellular Ca2+ elevation. Soluble phosphorylserine but not phosphorylcholine inhibits substrate cleavage. The isolated membrane proximal domain (MPD) of ADAM17 binds to PS but not to phosphatidylcholine liposomes. A cationic PS-binding motif is identified in this domain, replacement of which abrogates liposome-binding and renders the protease incapable of cleaving its substrates in cells. We speculate that surface-exposed PS directs the protease to its targets where it then executes its shedding function. äPhosphatidylserine exposure is required for ADAM17 sheddase function (epmc).pdf DeepDyve Pubget Overpricing