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10.1016/j.bpj.2015.07.034 http://scihub22266oqcxt.onion/10.1016/j.bpj.2015.07.034 C4576322!4576322!26300339     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=26300339&cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215       Biophys+J 2015 ; 109 (6): 1282-94 Nephropedia Template TP {{tp|p=26300339|t=2015. Cardiolipin Interactions with Proteins |pdf=|usr=}}{{26300339}} gab.com Text Cardiolipin Interactions with Proteins JO: Biophys J http://www.kidney.de/pget.php?&tw=1&pmid=26300339 #FOAvip Cardiolipins (CL) represent unique phospholipids of bacteria and eukaryotic mitochondria with four acyl chains and two phosphate groups that have been implicated in numerous functions from energy metabolism to apoptosis. Many proteins are known to interact with CL, and several cocrystal structures of protein-CL complexes exist. In this work, we describe the collection of the first systematic and, to the best of our knowledge, the comprehensive gold standard data set of all known CL-binding proteins. There are 62 proteins in this data set, 21 of which have nonredundant crystal structures with bound CL molecules available. Using binding patch analysis of amino acid frequencies, secondary structures and loop supersecondary structures considering phosphate and acyl chain binding regions together and separately, we gained a detailed understanding of the general structural and dynamic features involved in CL binding to proteins. Exhaustive docking of CL to all known structures of proteins experimentally shown to interact with CL demonstrated the validity of the docking approach, and provides a rich source of information for experimentalists who may wish to validate predictions. Twit Text FOAVip Cardiolipin Interactions with Proteins ????Biophys J http://www.kidney.de/pget.php?&tw=1&pmid=26300339 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26300339 #FOAvip English Wikipedia <ref>{{Cite pmid|26300339}}</ref> Cardiolipin Interactions with Proteins #MMPMID26300339 Planas-Iglesias J; Dwarakanath H; Mohammadyani D; Yanamala N; Kagan V; Klein-Seetharaman J Biophys J 2015[Sep]; 109 (6): 1282-94 PMID26300339show ga Cardiolipins (CL) represent unique phospholipids of bacteria and eukaryotic mitochondria with four acyl chains and two phosphate groups that have been implicated in numerous functions from energy metabolism to apoptosis. Many proteins are known to interact with CL, and several cocrystal structures of protein-CL complexes exist. In this work, we describe the collection of the first systematic and, to the best of our knowledge, the comprehensive gold standard data set of all known CL-binding proteins. There are 62 proteins in this data set, 21 of which have nonredundant crystal structures with bound CL molecules available. Using binding patch analysis of amino acid frequencies, secondary structures and loop supersecondary structures considering phosphate and acyl chain binding regions together and separately, we gained a detailed understanding of the general structural and dynamic features involved in CL binding to proteins. Exhaustive docking of CL to all known structures of proteins experimentally shown to interact with CL demonstrated the validity of the docking approach, and provides a rich source of information for experimentalists who may wish to validate predictions. äCardiolipin Interactions with Proteins (epmc).pdf DeepDyve Pubget Overpricing