The oligomeric status of syndecan-4 regulates syndecan-4 interaction with α-actinin

European Journal of Cell Biology

Volumn 87, Issue 10, 2008, Pages 807-815

  Choi, Youngsil ^a   Kim, Seungin ^a   Lee, Junghyun ^a   Ko, Sung gun ^b   Lee, Weontae ^b   Han, Inn Oc ^c   Woods, Anne ^d   Oh, Eok Soo ^a  

^a Ewha Womans University   (South Korea)

^b Yonsei University   (South Korea)

^c Inha University   (South Korea)

^d UNIVERSITY OF ALABAMA AT BIRMINGHAM   (United States)

Author keywords

Actinin; Cytoskeletal organization; Focal adhesion; Oligomerization; Syndecan 4

Indexed keywords

ALPHA ACTININ; DIMER; GLUTATHIONE TRANSFERASE; MONOMER; OLIGOMER; PAXILLIN; PHOSPHATIDYLINOSITOL 4,5 BISPHOSPHATE; RECOMBINANT PROTEIN; SYNDECAN 4; TALIN; VINCULIN;

ANIMAL CELL; ARTICLE; CYTOPLASM; CYTOSKELETON; EMBRYO; EMBRYO CELL; FIBROBLAST; GENETIC REGULATION; NONHUMAN; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN PHOSPHORYLATION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; RAT;

ACTININ; AMINO ACID SEQUENCE; ANIMALS; CELL MEMBRANE; CELLS, CULTURED; CYTOPLASM; CYTOSKELETON; FOCAL ADHESIONS; MEMBRANE GLYCOPROTEINS; MOLECULAR SEQUENCE DATA; PHOSPHATIDYLINOSITOL 4,5-DIPHOSPHATE; PHOSPHORYLATION; PROTEIN STRUCTURE, TERTIARY; RATS; SYNDECAN-4;

RATTUS;

EID: 51249107328     PISSN: 01719335     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ejcb.2008.04.005     Document Type: Article

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