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10.1042/BJ20141186 http://scihub22266oqcxt.onion/10.1042/BJ20141186 C4405237!4405237!25656054     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       Biochem+J 2015 ; 466 (1): 13-28 Nephropedia Template TP {{tp|p=25656054|t=2015. Diversification of importin-? isoforms in cellular trafficking and disease states |pdf=|usr=}}{{25656054}} gab.com Text Diversification of importin- isoforms in cellular trafficking and disease states JO: Biochem J http://www.kidney.de/pget.php?&tw=1&pmid=25656054 #FOAvip The human genome encodes seven isoforms of importin ? which are grouped into three subfamilies known as ?1, ?2 and ?3. All isoforms share a fundamentally conserved architecture that consists of an N-terminal, autoinhibitory, importin-?-binding (IBB) domain and a C-terminal Arm (Armadillo)-core that associates with nuclear localization signal (NLS) cargoes. Despite striking similarity in amino acid sequence and 3D structure, importin-? isoforms display remarkable substrate specificity in vivo. In the present review, we look at key differences among importin-? isoforms and provide a comprehensive inventory of known viral and cellular cargoes that have been shown to associate preferentially with specific isoforms. We illustrate how the diversification of the adaptor importin ? into seven isoforms expands the dynamic range and regulatory control of nucleocytoplasmic transport, offering unexpected opportunities for pharmacological intervention. The emerging view of importin ? is that of a key signalling molecule, with isoforms that confer preferential nuclear entry and spatiotemporal specificity on viral and cellular cargoes directly linked to human diseases. Twit Text FOAVip Diversification of importin- isoforms in cellular trafficking and disease states ????Biochem J http://www.kidney.de/pget.php?&tw=1&pmid=25656054 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25656054 #FOAvip English Wikipedia <ref>{{Cite pmid|25656054}}</ref> Diversification of importin-? isoforms in cellular trafficking and disease states #MMPMID25656054 Pumroy RA; Cingolani G Biochem J 2015[Feb]; 466 (1): 13-28 PMID25656054show ga The human genome encodes seven isoforms of importin ? which are grouped into three subfamilies known as ?1, ?2 and ?3. All isoforms share a fundamentally conserved architecture that consists of an N-terminal, autoinhibitory, importin-?-binding (IBB) domain and a C-terminal Arm (Armadillo)-core that associates with nuclear localization signal (NLS) cargoes. Despite striking similarity in amino acid sequence and 3D structure, importin-? isoforms display remarkable substrate specificity in vivo. In the present review, we look at key differences among importin-? isoforms and provide a comprehensive inventory of known viral and cellular cargoes that have been shown to associate preferentially with specific isoforms. We illustrate how the diversification of the adaptor importin ? into seven isoforms expands the dynamic range and regulatory control of nucleocytoplasmic transport, offering unexpected opportunities for pharmacological intervention. The emerging view of importin ? is that of a key signalling molecule, with isoforms that confer preferential nuclear entry and spatiotemporal specificity on viral and cellular cargoes directly linked to human diseases. äDiversification of importin-? isoforms in cellular trafficking and dis(epmc).pdf DeepDyve Pubget Overpricing