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10.1007/s00018-017-2478-0

http://scihub22266oqcxt.onion/10.1007/s00018-017-2478-0
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C5487894!5487894!28243699
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suck abstract from ncbi

pmid28243699      Cell+Mol+Life+Sci 2017 ; 74 (13): 2413-38
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  • Deciphering the BAR code of membrane modulators #MMPMID28243699
  • Salzer U; Kostan J; Djinovi?-Carugo K
  • Cell Mol Life Sci 2017[]; 74 (13): 2413-38 PMID28243699show 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.
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