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10.1007/s00018-017-2478-0 http://scihub22266oqcxt.onion/10.1007/s00018-017-2478-0 C5487894!5487894 !28243699     free     free     free Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\28243699 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Cell+Mol+Life+Sci 2017 ; 74 (13 ): 2413-2438 Nephropedia Template TP {{tp|p=28243699 |t=2017. Deciphering the BAR code of membrane modulators |pdf=|usr=}}{{28243699 }} gab.com Text Deciphering the BAR code of membrane modulators JO: Cell Mol Life Sci http://www.kidney.de/pget.php?&tw=1&pmid=28243699 #FOAvip The BAR domain is the eponymous domain of the "BAR-domain protein superfamily", a large and diverse set of mostly multi-domain proteins that play eminent roles at the membrane cytoskeleton interface. BAR domain homodimers are the functional units that peripherally associate with lipid membranes and are involved in membrane sculpting activities. Differences in their intrinsic curvatures and lipid-binding properties account for a large variety in membrane modulating properties. Membrane activities of BAR domains are further modified and regulated by intramolecular or inter-subunit domains, by intermolecular protein interactions, and by posttranslational modifications. Rather than providing detailed cell biological information on single members of this superfamily, this review focuses on biochemical, biophysical, and structural aspects and on recent findings that paradigmatically promote our understanding of processes driven and modulated by BAR domains. Twit Text FOAVip Deciphering the BAR code of membrane modulators ????Cell Mol Life Sci http://www.kidney.de/pget.php?&tw=1&pmid=28243699 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28243699 #FOAvip English Wikipedia <ref>{{Cite pmid|28243699 }}</ref> Deciphering the BAR code of membrane modulators #MMPMID28243699 Salzer U ; Kostan J ; Djinovi?-Carugo K Cell Mol Life Sci 2017[Jul]; 74 (13 ): 2413-2438 PMID28243699 show ga The BAR domain is the eponymous domain of the "BAR-domain protein superfamily", a large and diverse set of mostly multi-domain proteins that play eminent roles at the membrane cytoskeleton interface. BAR domain homodimers are the functional units that peripherally associate with lipid membranes and are involved in membrane sculpting activities. Differences in their intrinsic curvatures and lipid-binding properties account for a large variety in membrane modulating properties. Membrane activities of BAR domains are further modified and regulated by intramolecular or inter-subunit domains, by intermolecular protein interactions, and by posttranslational modifications. Rather than providing detailed cell biological information on single members of this superfamily, this review focuses on biochemical, biophysical, and structural aspects and on recent findings that paradigmatically promote our understanding of processes driven and modulated by BAR domains. |Animals [MESH] |Cell Membrane/*metabolism [MESH] |Humans [MESH] |Membrane Proteins/*chemistry/*metabolism [MESH] |Phosphorylation [MESH] |Protein Binding [MESH] |Protein Domains [MESH]Deciphering the BAR code of membrane modulators (epmc).pdf DeepDyve Pubget Overpricing