Tapasin facilitation of natural HLA-A and -B allomorphs is strongly influenced by peptide length, depends on stability, and separates closely related allomorphs

Journal of Immunology

Volumn 191, Issue 7, 2013, Pages 3939-3947

  Geironson, Linda ^a   Thuring, Camilla ^a   Harndahl, Mikkel ^b   Rasmussen, Michael ^b   Buus, Søren ^b   Røder, Gustav ^b   Paulsson, Kajsa M ^a  

^a LUND UNIVERSITY   (Sweden)

^b Institute of International Health Immunology and Microbiology   (Denmark)

Author keywords

[No Author keywords available]

Indexed keywords

HLA A ANTIGEN; HLA B ANTIGEN; TAPASIN;

ANTIGEN BINDING; ARTICLE; COMPLEX FORMATION; ESCHERICHIA COLI; NONHUMAN; PEPTIDE LIBRARY; PEPTIDE SYNTHESIS; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN PROCESSING; PROTEIN STABILITY;

ANTIGEN PRESENTATION; HLA-A ANTIGENS; HLA-B ANTIGENS; HUMANS; MEMBRANE TRANSPORT PROTEINS; PEPTIDES; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN STABILITY;

EID: 84885094858     PISSN: 00221767     EISSN: 15506606     Source Type: Journal    
DOI: 10.4049/jimmunol.1201741     Document Type: Article

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