Molecular basis of the recognition of nephronectin by integrin α8β1

Journal of Biological Chemistry

Volumn 284, Issue 21, 2009, Pages 14524-14536

  Sato, Yuya ^a   Uemura, Toshihiko ^a   Morimitsu, Keisuke ^a   Sato Nishiuchi, Ryoko ^a   Manabe, Ri Ichiroh ^a   Takagi, Junichi ^a   Yamada, Masashi ^a   Sekiguchi, Kiyotoshi ^a  

^a OSAKA UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

AFFINITY BINDING; ALANINE-SCANNING MUTAGENESIS; ARG GLY ASPS; BINDING ACTIVITIES; COMPLEMENTATION; DELETION MUTANTS; DISSOCIATION CONSTANT; EXTRACELLULAR MATRICES; INTEGRIN; LIGAND INTERACTIONS; MOLECULAR BASIS; RGD MOTIF; TERMINAL SIDES;

ACTIVATION ANALYSIS; AMINES; BINDING SITES; DISSOCIATION;

LIGANDS;

ALPHA8BETA1 INTEGRIN; ARGINYLGLYCYLASPARTIC ACID; GLUTAMYLISOLEUCYLGLUTAMIC ACID; INTEGRIN; LEUCYLPHENYLALANYLGLUTAMYLISOLEUCYLPHENYLALANYLGLUTAMYLISOLEUCYLGLUTAMYLARGININE; MEMBRANE PROTEIN; NEPHRONECTIN; PEPTIDE; UNCLASSIFIED DRUG; ARGINYL-GLYCYL-ASPARTIC ACID; INTEGRIN ALPHA8BETA1; OLIGOPEPTIDE; PEPTIDE FRAGMENT; RECOMBINANT PROTEIN; SCLEROPROTEIN;

AMINO ACID SEQUENCE; ANIMAL CELL; ARTICLE; BINDING AFFINITY; BINDING SITE; CARBOXY TERMINAL SEQUENCE; CELL ADHESION; CONTROLLED STUDY; DELETION MUTANT; GENETIC COMPLEMENTATION; HUMAN; HUMAN CELL; LIGAND BINDING; MOLECULAR RECOGNITION; MOUSE; MUTAGENESIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN FUNCTION; PROTEIN INTERACTION; PROTEIN MOTIF; AMINO ACID SUBSTITUTION; ANIMAL; CHEMISTRY; CHICKEN; ISOLATION AND PURIFICATION; KINETICS; METABOLISM; MOLECULAR GENETICS; TUMOR CELL LINE;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMALS; CELL ADHESION; CELL LINE, TUMOR; CHICKENS; EXTRACELLULAR MATRIX PROTEINS; GENETIC COMPLEMENTATION TEST; HUMANS; INTEGRINS; KINETICS; MICE; MOLECULAR SEQUENCE DATA; OLIGOPEPTIDES; PEPTIDE FRAGMENTS; PROTEIN BINDING; RECOMBINANT PROTEINS;

EID: 67649771331     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M900200200     Document Type: Article

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