Increased diversity of the hla-b40 ligandome by the presentation of peptides phosphorylated at their main anchor residue

Molecular and Cellular Proteomics

Volumn 13, Issue 2, 2014, Pages 462-474

  Marcilla, Miguel ^a   Alpizar, Adan ^a   Lombardia, Manuel ^a   Ramos Fernandez, Antonio ^a   Ramos, Manuel ^b   Albar, Juan Pablo ^a  

^a CENTRO NACIONAL DE BIOTECNOLOGÍA   (Spain)

^b INSTITUTO DE SALUD CARLOS III   (Spain)

Author keywords

[No Author keywords available]

Indexed keywords

ALIPHATIC COMPOUND; ASPARTIC ACID; GLUTAMIC ACID; HLA B40 ANTIGEN; LIGAND; METAL ION; METHIONINE; PHENYLALANINE; PHOSPHOPEPTIDE; PHOSPHOSERINE; SYNTHETIC PEPTIDE;

ANTIGEN PRESENTATION; ARTICLE; BINDING AFFINITY; BINDING ASSAY; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; HUMAN; HUMAN CELL; IMMOBILIZED METAL AFFINITY CHROMATOGRAPHY; MASS SPECTROMETRY; PEPTIDOMICS; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN MOTIF; PROTEIN PHOSPHORYLATION; SEQUENCE ANALYSIS;

AMINO ACID SEQUENCE; ANTIGEN PRESENTATION; ANTIGENIC VARIATION; BINDING SITES; EPITOPE MAPPING; HLA-B40 ANTIGEN; HUMANS; LIGANDS; PEPTIDE FRAGMENTS; PHOSPHOPROTEINS; PHOSPHORYLATION; PROTEIN INTERACTION MAPPING; PROTEOME; T-LYMPHOCYTES, CYTOTOXIC;

EID: 84893340488     PISSN: 15359476     EISSN: 15359484     Source Type: Journal    
DOI: 10.1074/mcp.M113.034314     Document Type: Article

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