ADIP, a novel afadin- and α-actinin-binding protein localized at cell-cell adherens junctions

Journal of Biological Chemistry

Volumn 278, Issue 6, 2003, Pages 4103-4111

  Asada, Masanori ^a   Irie, Kenji ^a   Morimoto, Koji ^b   Yamada, Akio ^a   Ikeda, Wataru ^a   Takeuchi, Masakazu ^b   Takai, Yoshimi ^a  

^a OSAKA UNIVERSITY GRADUATE SCHOOL OF MEDICINE   (Japan)

^b KAN Research Institute Inc ^*  (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ABSORPTION; ADHESION; CELLS; IMMUNOLOGY; TISSUE;

CELL-CELL ADHESION;

PROTEINS;

ACTIN BINDING PROTEIN; AFADIN BINDING PROTEIN; AFADIN DIL DOMAIN INTERACTING PROTEIN; ALPHA ACTININ; ALPHA CATENIN; AMINO ACID; BINDING PROTEIN; CALCIUM; CATENIN; CELL ADHESION MOLECULE; CELL PROTEIN; CYTOPLASM PROTEIN; IMMUNOGLOBULIN; NECTIN; UNCLASSIFIED DRUG; UVOMORULIN; ACTININ; ADIP PROTEIN, MOUSE; ADIP PROTEIN, RAT; AFADIN; CARRIER PROTEIN; KINESIN; MLLT4 PROTEIN, HUMAN; MLLT4 PROTEIN, MOUSE; MYOSIN; PRIMER DNA;

ACTIN FILAMENT; ANIMAL CELL; ANIMAL TISSUE; ARTICLE; CELL JUNCTION; CONTROLLED STUDY; CYTOSKELETON; EXTRACELLULAR MATRIX; HUMAN; HUMAN CELL; IMMUNOELECTRON MICROSCOPY; IMMUNOFLUORESCENCE MICROSCOPY; INTESTINE EPITHELIUM CELL; MOUSE; NONHUMAN; NORTHERN BLOTTING; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN LOCALIZATION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; TISSUE DISTRIBUTION; TWO HYBRID SYSTEM; WESTERN BLOTTING; AMINO ACID SEQUENCE; ANIMAL; CELL CULTURE; CELL FRACTIONATION; CHEMISTRY; DOG; GENETICS; METABOLISM; MOLECULAR GENETICS; RAT; SEQUENCE HOMOLOGY; SERODIAGNOSIS;

ANIMALIA;

ACTININ; ADHERENS JUNCTIONS; AMINO ACID SEQUENCE; ANIMALS; BASE SEQUENCE; CARRIER PROTEINS; CELLS, CULTURED; DNA PRIMERS; DOGS; HUMANS; KINESIN; MICE; MICROFILAMENT PROTEINS; MOLECULAR SEQUENCE DATA; MYOSINS; PRECIPITIN TESTS; PROTEIN BINDING; RATS; SEQUENCE HOMOLOGY, AMINO ACID; SUBCELLULAR FRACTIONS; TWO-HYBRID SYSTEM TECHNIQUES;

EID: 0037423380     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M209832200     Document Type: Article

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