Predominant naturally processed peptides bound to HLA-DR1 are derived from MHC-related molecules and are heterogeneous in size

Nature

Volumn 358, Issue 6389, 1992, Pages 764-768

  Chicz, Roman M ^a   Urban, Robert G ^a   Lane, William S ^a   Gorga, Joan C ^a,b   Stern, Lawrence J ^a   Vignali, Dario A A ^a   Strominger, Jack L ^a  

^a HARVARD UNIVERSITY   (United States)

^b CHILDREN S HOSPITAL OF PITTSBURGH   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

HLA DR1 ANTIGEN; MAJOR HISTOCOMPATIBILITY ANTIGEN;

ARTICLE; HUMAN; PRIORITY JOURNAL; PROTEIN PROCESSING;

ALPHA-FETOPROTEINS; AMINO ACID SEQUENCE; BINDING SITES; COMPARATIVE STUDY; HISTOCOMPATIBILITY ANTIGENS CLASS II; HLA-A2 ANTIGEN; HLA-DR1 ANTIGEN; MOLECULAR SEQUENCE DATA; NA(+)-K(+)-EXCHANGING ATPASE; PEPTIDES; PROTEIN BINDING; RECEPTORS, TRANSFERRIN; SEQUENCE ALIGNMENT; STRUCTURE-ACTIVITY RELATIONSHIP; SUPPORT, NON-U.S. GOV'T;

EID: 0026733449     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/358764a0     Document Type: Article

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