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10.1016/j.str.2016.10.012 http://scihub22266oqcxt.onion/10.1016/j.str.2016.10.012 C5444293!5444293!27889206     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=27889206&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 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 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 245.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\27889206.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Structure 2016 ; 24 (12): 2217-26 Nephropedia Template TP {{tp|p=27889206|t=2016. ProtLID, a residue-based pharmacophore approach to identify cognate protein ligands in the Immunoglobulin Superfamily |pdf=|usr=}}{{27889206}} gab.com Text ProtLID, a residue-based pharmacophore approach to identify cognate protein ligands in the Immunoglobulin Superfamily JO: Structure http://www.kidney.de/pget.php?&tw=1&pmid=27889206 #FOAvip Members of extracellular Immunoglobulin Superfamily (IgSFs) play a key role in immune regulation through the control of the co-stimulatory pathway, and have emerged as potent drug targets in cancers, infectious diseases, and autoimmunity. Despite the difficult experimental access to this class of proteins, single structures of ectodomains of IgSF proteins are solved with regularity. However, the most biologically critical challenge for this class of proteins is the identification of their cognate ligands that communicate intercellular signals. We describe a conceptually novel method, Protein Ligand Interface Design (ProtLID), for the problem of identifying cognate ligands from a sub-proteome for a given target receptor protein. ProtLID designs an optimal protein interface for a given receptor by running extensive molecular dynamics simulations of single residue probes. The type and location of residue preferences establish a residue-based pharmacophore, which is subsequently used to find potential matches among candidate ligands within a sub-proteome. Twit Text FOAVip ProtLID, a residue-based pharmacophore approach to identify cognate protein ligands in the Immunoglobulin Superfamily ????Structure http://www.kidney.de/pget.php?&tw=1&pmid=27889206 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27889206 #FOAvip English Wikipedia <ref>{{Cite pmid|27889206}}</ref> ProtLID, a residue-based pharmacophore approach to identify cognate protein ligands in the Immunoglobulin Superfamily #MMPMID27889206 Yap EH; Fiser A Structure 2016[Dec]; 24 (12): 2217-26 PMID27889206show ga Members of extracellular Immunoglobulin Superfamily (IgSFs) play a key role in immune regulation through the control of the co-stimulatory pathway, and have emerged as potent drug targets in cancers, infectious diseases, and autoimmunity. Despite the difficult experimental access to this class of proteins, single structures of ectodomains of IgSF proteins are solved with regularity. However, the most biologically critical challenge for this class of proteins is the identification of their cognate ligands that communicate intercellular signals. We describe a conceptually novel method, Protein Ligand Interface Design (ProtLID), for the problem of identifying cognate ligands from a sub-proteome for a given target receptor protein. ProtLID designs an optimal protein interface for a given receptor by running extensive molecular dynamics simulations of single residue probes. The type and location of residue preferences establish a residue-based pharmacophore, which is subsequently used to find potential matches among candidate ligands within a sub-proteome. äProtLID, a residue-based pharmacophore approach to identify cognate pr(epmc).pdf DeepDyve Pubget Overpricing