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10.1586/14789450.2014.971763 http://scihub22266oqcxt.onion/10.1586/14789450.2014.971763 C4312474!4312474 !25327788     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 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\25327788 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Expert+Rev+Proteomics 2014 ; 11 (6 ): 653-5 Nephropedia Template TP {{tp|p=25327788 |t=2014. Prothrombin structure: unanticipated features and opportunities |pdf=|usr=}}{{25327788 }} gab.com Text Prothrombin structure: unanticipated features and opportunities JO: Expert Rev Proteomics http://www.kidney.de/pget.php?&tw=1&pmid=25327788 #FOAvip The structure of prothrombin has eluded investigators for decades but recent efforts have succeeded in revealing the architecture of this important clotting factor. Unanticipated features have emerged outlining the significant flexibility of the zymogen due to linker regions connecting the ? carboxyglutamic domain, kringles and protease domain. A new, structure-based framework helps in defining a molecular mechanism of prothrombin activation, rationalizes the severe bleeding phenotypes of several naturally occurring mutations and identifies targets for drug design. Twit Text FOAVip Prothrombin structure: unanticipated features and opportunities ????Expert Rev Proteomics http://www.kidney.de/pget.php?&tw=1&pmid=25327788 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25327788 #FOAvip English Wikipedia <ref>{{Cite pmid|25327788 }}</ref> Prothrombin structure: unanticipated features and opportunities #MMPMID25327788 Pozzi N ; Di Cera E Expert Rev Proteomics 2014[Dec]; 11 (6 ): 653-5 PMID25327788 show ga The structure of prothrombin has eluded investigators for decades but recent efforts have succeeded in revealing the architecture of this important clotting factor. Unanticipated features have emerged outlining the significant flexibility of the zymogen due to linker regions connecting the ? carboxyglutamic domain, kringles and protease domain. A new, structure-based framework helps in defining a molecular mechanism of prothrombin activation, rationalizes the severe bleeding phenotypes of several naturally occurring mutations and identifies targets for drug design. |Humans [MESH] |Mutation [MESH] |Protein Structure, Tertiary [MESH]Prothrombin structure: unanticipated features and opportunities (epmc).pdf DeepDyve Pubget Overpricing