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10.1038/srep13570 http://scihub22266oqcxt.onion/10.1038/srep13570 C4550876!4550876 !26310724     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=26310724 &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       Sci+Rep 2015 ; 5 (?): 13570 Nephropedia Template TP {{tp|p=26310724 |t=2015. Discovery of ?-Mangostin as an Amyloidogenesis Inhibitor |pdf=|usr=}}{{26310724 }} gab.com Text Discovery of -Mangostin as an Amyloidogenesis Inhibitor JO: Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=26310724 #FOAvip Transthyretin (TTR) is a homotetrameric protein involved in human hereditary amyloidoses. The discovery and development of small molecules that inhibit the amyloid fibril formation of TTR is one of the therapeutic strategies for these diseases. Herein, we discovered that ?-mangostin (?-M) is an effective inhibitor against the amyloid fibril formation of V30M amyloidogenic TTR. In-vitro binding assays revealed that ?-M was the most potent of the selected xanthone derivatives, and it bound to the thyroxine (T4)-binding sites and stabilized the TTR tetramer. X-ray crystallographic analysis revealed the diagonal binding mode of ?-M and the two binding sites of chloride ions at the T4-binding site. One of the chloride ions was replaced with a water molecule in the ?-mangostin complex, which is a methylated derivative of ?-M. The stronger inhibitory potency of ?-M could be explained by the additional hydrogen bonds with the chloride ion. The present study establishes ?-M as a novel inhibitor of TTR fibrillization. Twit Text FOAVip Discovery of -Mangostin as an Amyloidogenesis Inhibitor ????Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=26310724 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26310724 #FOAvip English Wikipedia <ref>{{Cite pmid|26310724 }}</ref> Discovery of ?-Mangostin as an Amyloidogenesis Inhibitor #MMPMID26310724 Yokoyama T ; Ueda M ; Ando Y ; Mizuguchi M Sci Rep 2015[Aug]; 5 (?): 13570 PMID26310724 show ga Transthyretin (TTR) is a homotetrameric protein involved in human hereditary amyloidoses. The discovery and development of small molecules that inhibit the amyloid fibril formation of TTR is one of the therapeutic strategies for these diseases. Herein, we discovered that ?-mangostin (?-M) is an effective inhibitor against the amyloid fibril formation of V30M amyloidogenic TTR. In-vitro binding assays revealed that ?-M was the most potent of the selected xanthone derivatives, and it bound to the thyroxine (T4)-binding sites and stabilized the TTR tetramer. X-ray crystallographic analysis revealed the diagonal binding mode of ?-M and the two binding sites of chloride ions at the T4-binding site. One of the chloride ions was replaced with a water molecule in the ?-mangostin complex, which is a methylated derivative of ?-M. The stronger inhibitory potency of ?-M could be explained by the additional hydrogen bonds with the chloride ion. The present study establishes ?-M as a novel inhibitor of TTR fibrillization. |Amyloid/*antagonists & inhibitors/metabolism [MESH] |Binding Sites [MESH] |Chlorides/metabolism [MESH] |Crystallography, X-Ray [MESH] |Humans [MESH] |Hydrogen Bonding [MESH] |Ions [MESH]Discovery of ?-Mangostin as an Amyloidogenesis Inhibitor (epmc).pdf DeepDyve Pubget Overpricing