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10.3389/fimmu.2017.01118 http://scihub22266oqcxt.onion/10.3389/fimmu.2017.01118 C5604083!5604083!28959259     free     free     free Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Front+Immunol 2017 ; 8 (ä): ä Nephropedia Template TP {{tp|p=28959259|t=2017. Transmembrane Helices Are an Overlooked Source of Major Histocompatibility Complex Class I Epitopes |pdf=|usr=}}{{28959259}} gab.com Text Transmembrane Helices Are an Overlooked Source of Major Histocompatibility Complex Class I Epitopes JO: Front Immunol http://www.kidney.de/pget.php?&tw=1&pmid=28959259 #FOAvip About a fourth of the human proteome is anchored by transmembrane helices (TMHs) to lipid membranes. TMHs require multiple hydrophobic residues for spanning membranes, and this shows a striking resemblance with the requirements for peptide binding to major histocompatibility complex (MHC) class I. It, therefore, comes as no surprise that bioinformatics analysis predicts an over-representation of TMHs among strong MHC class I (MHC-I) binders. Published peptide elution studies confirm that TMHs are indeed presented by MHC-I. This raises the question how membrane proteins are processed for MHC-I (cross-)presentation, with current research focusing on soluble antigens. The presentation of membrane-buried peptides is likely important in health and disease, as TMHs are considerably conserved and their presentation might prevent escape mutations by pathogens. Therefore, it could contribute to the disease correlations described for many human leukocyte antigen haplotypes. Twit Text FOAVip Transmembrane Helices Are an Overlooked Source of Major Histocompatibility Complex Class I Epitopes ????Front Immunol http://www.kidney.de/pget.php?&tw=1&pmid=28959259 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28959259 #FOAvip English Wikipedia <ref>{{Cite pmid|28959259}}</ref> Transmembrane Helices Are an Overlooked Source of Major Histocompatibility Complex Class I Epitopes #MMPMID28959259 Bianchi F; Textor J; van den Bogaart G Front Immunol 2017[]; 8 (ä): ä PMID28959259show ga About a fourth of the human proteome is anchored by transmembrane helices (TMHs) to lipid membranes. TMHs require multiple hydrophobic residues for spanning membranes, and this shows a striking resemblance with the requirements for peptide binding to major histocompatibility complex (MHC) class I. It, therefore, comes as no surprise that bioinformatics analysis predicts an over-representation of TMHs among strong MHC class I (MHC-I) binders. Published peptide elution studies confirm that TMHs are indeed presented by MHC-I. This raises the question how membrane proteins are processed for MHC-I (cross-)presentation, with current research focusing on soluble antigens. The presentation of membrane-buried peptides is likely important in health and disease, as TMHs are considerably conserved and their presentation might prevent escape mutations by pathogens. Therefore, it could contribute to the disease correlations described for many human leukocyte antigen haplotypes. äTransmembrane Helices Are an Overlooked Source of Major Histocompatibi(epmc).pdf DeepDyve Pubget Overpricing