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.

10.1177/1535370214561586 http://scihub22266oqcxt.onion/10.1177/1535370214561586 C4374002!4374002!25662954     free     free     free Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Exp+Biol+Med+(Maywood) 2015 ; 240 (3): 361-74 Nephropedia Template TP {{tp|p=25662954|t=2015. Structural insights into the functional versatility of WW domain-containing oxidoreductase tumor suppressor |pdf=|usr=}}{{25662954}} gab.com Text Structural insights into the functional versatility of WW domain-containing oxidoreductase tumor suppressor JO: Exp Biol Med (Maywood) http://www.kidney.de/pget.php?&tw=1&pmid=25662954 #FOAvip Recent work on WW domain-containing oxidoreductase (WWOX) tumor suppressor is beginning to shed new light on both the molecular mechanism of action of its WW domains as well as the contiguous catalytic domain. Herein, the structural basis underlying the ability of WW1 domain to bind to various physiological ligands and how the orphan WW2 tandem partner synergizes its ligand binding in the context of WW1?WW2 tandem module of WWOX is discussed. Notably, the WW domains within the WW1?WW2 tandem module physically associate so as to adopt a fixed spatial orientation relative to each other. In this manner, the association of WW2 domain with WW1 hinders ligand binding to the latter. Consequently, ligand binding to WW1 domain not only results in the displacement of WW2 lid but also disrupts the fixed orientation of WW domains in the liganded conformation. Equally importantly, structure-guided functional approach suggests that the catalytic domain of WWOX likely serves as a retinal oxidoreductase that catalyzes the reversible oxidation and reduction of all-trans-retinal. Collectively, this review provides structural insights into the functional versatility of a key signaling protein with important implications on its biology. Twit Text FOAVip Structural insights into the functional versatility of WW domain-containing oxidoreductase tumor suppressor ????Exp Biol Med (Maywood) http://www.kidney.de/pget.php?&tw=1&pmid=25662954 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25662954 #FOAvip English Wikipedia <ref>{{Cite pmid|25662954}}</ref> Structural insights into the functional versatility of WW domain-containing oxidoreductase tumor suppressor #MMPMID25662954 Farooq A Exp Biol Med (Maywood) 2015[Mar]; 240 (3): 361-74 PMID25662954show ga Recent work on WW domain-containing oxidoreductase (WWOX) tumor suppressor is beginning to shed new light on both the molecular mechanism of action of its WW domains as well as the contiguous catalytic domain. Herein, the structural basis underlying the ability of WW1 domain to bind to various physiological ligands and how the orphan WW2 tandem partner synergizes its ligand binding in the context of WW1?WW2 tandem module of WWOX is discussed. Notably, the WW domains within the WW1?WW2 tandem module physically associate so as to adopt a fixed spatial orientation relative to each other. In this manner, the association of WW2 domain with WW1 hinders ligand binding to the latter. Consequently, ligand binding to WW1 domain not only results in the displacement of WW2 lid but also disrupts the fixed orientation of WW domains in the liganded conformation. Equally importantly, structure-guided functional approach suggests that the catalytic domain of WWOX likely serves as a retinal oxidoreductase that catalyzes the reversible oxidation and reduction of all-trans-retinal. Collectively, this review provides structural insights into the functional versatility of a key signaling protein with important implications on its biology. äStructural insights into the functional versatility of WW domain-conta(epmc).pdf DeepDyve Pubget Overpricing