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10.1073/pnas.1500973112 http://scihub22266oqcxt.onion/10.1073/pnas.1500973112 C4394253!4394253!25831525     free     free     free Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Proc+Natl+Acad+Sci+U+S+A 2015 ; 112 (14): E1754-62 Nephropedia Template TP {{tp|p=25831525|t=2015. TCR contact residue hydrophobicity is a hallmark of immunogenic CD8+ T cell epitopes |pdf=|usr=}}{{25831525}} gab.com Text TCR contact residue hydrophobicity is a hallmark of immunogenic CD8+ T cell epitopes JO: Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=25831525 #FOAvip The design of effective T-cell vaccines against pathogens and tumor antigens is challenged by the highly inefficient identification of the subset of peptides from a given antigen that effectively stimulate an immune response. Here we report that the relative hydrophobicity of T-cell receptor contact residues is markedly enriched in immunogenic major histocompatibility complex class I epitopes in both human and murine MHCs, and in both self and pathogen-derived immunogenic epitopes. Incorporating hydrophobicity into T-cell epitope prediction models increases the efficiency of epitope identification, which will manifest in the time and cost of T-cell vaccine development. Amino acid hydrophobicity may represent a biochemical basis by which T cells discriminate immunogenic epitopes within the background of self peptides. Twit Text FOAVip TCR contact residue hydrophobicity is a hallmark of immunogenic CD8+ T cell epitopes ????Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=25831525 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25831525 #FOAvip English Wikipedia <ref>{{Cite pmid|25831525}}</ref> TCR contact residue hydrophobicity is a hallmark of immunogenic CD8+ T cell epitopes #MMPMID25831525 Chowell D; Krishna S; Becker PD; Cocita C; Shu J; Tan X; Greenberg PD; Klavinskis LS; Blattman JN; Anderson KS Proc Natl Acad Sci U S A 2015[Apr]; 112 (14): E1754-62 PMID25831525show ga The design of effective T-cell vaccines against pathogens and tumor antigens is challenged by the highly inefficient identification of the subset of peptides from a given antigen that effectively stimulate an immune response. Here we report that the relative hydrophobicity of T-cell receptor contact residues is markedly enriched in immunogenic major histocompatibility complex class I epitopes in both human and murine MHCs, and in both self and pathogen-derived immunogenic epitopes. Incorporating hydrophobicity into T-cell epitope prediction models increases the efficiency of epitope identification, which will manifest in the time and cost of T-cell vaccine development. Amino acid hydrophobicity may represent a biochemical basis by which T cells discriminate immunogenic epitopes within the background of self peptides. äTCR contact residue hydrophobicity is a hallmark of immunogenic CD8+ T(epmc).pdf DeepDyve Pubget Overpricing