Modulation of FcγRI (CD64) ligand binding by blocking peptides of periplakin

Journal of Biological Chemistry

Volumn 279, Issue 32, 2004, Pages 33875-33881

  Beekman, Jeffrey M ^a,b   Bakema, Jantine E ^a,b   Van Der Linden, Joke ^a   Tops, Bastiaan ^a   Hinten, Marja ^a   Van Vugt, Martine ^a,c   Van De Winkel, Jan G J ^a,c   Leusen, Jeanette H W ^a  

^a UNIVERSITY MEDICAL CENTER UTRECHT   (Netherlands)

^b Medarex Europe   (Netherlands)

^c GENMAB   (Netherlands)

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBODIES; CELL CULTURE; DATA REDUCTION; POLYPEPTIDES; SUBSTITUTION REACTIONS;

CYTOPLASMIC DOMAINS; INTRACELLULAR DOMAINS;

BIOCHEMISTRY;

ALANINE; CD64 ANTIGEN; CELL RECEPTOR; FC RECEPTOR; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 2; MUTANT PROTEIN; PEPTIDE; PERIPLAKIN; SYNTHETIC PEPTIDE; TRANSACTIVATOR PROTEIN; CYTOSKELETON PROTEIN; HYBRID PROTEIN; PEPTIDE FRAGMENT; PLAKIN; PPL PROTEIN, HUMAN; PPL PROTEIN, MOUSE;

ALPHA CHAIN; AMINO ACID SUBSTITUTION; ANTIGEN PRESENTATION; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; HUMAN; HUMAN CELL; IMMUNOCOMPETENT CELL; IMMUNOREGULATION; INTERNALIZATION; LEUKOCYTE; LIGAND BINDING; MODULATION; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN ENGINEERING; PROTEIN INTERACTION; AMINO ACID SEQUENCE; ANIMAL; BINDING SITE; CHEMISTRY; ERYTHROCYTE; FLOW CYTOMETRY; GENETIC TRANSFECTION; GENETICS; IMMUNOLOGY; METABOLISM; MOLECULAR GENETICS; MOUSE; MUTAGENESIS; POLYMERASE CHAIN REACTION; ROSETTE FORMATION; SACCHAROMYCES CEREVISIAE; STRUCTURE ACTIVITY RELATION; TWO HYBRID SYSTEM;

ALANINE; AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; CYTOSKELETAL PROTEINS; ERYTHROCYTES; FLOW CYTOMETRY; HUMANS; MICE; MOLECULAR SEQUENCE DATA; MUTAGENESIS; PEPTIDE FRAGMENTS; PLAKINS; POLYMERASE CHAIN REACTION; RECEPTORS, IGG; RECOMBINANT FUSION PROTEINS; ROSETTE FORMATION; SACCHAROMYCES CEREVISIAE; STRUCTURE-ACTIVITY RELATIONSHIP; TRANSFECTION; TWO-HYBRID SYSTEM TECHNIQUES;

EID: 4043133804     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M401018200     Document Type: Article

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