Biochemical characterization of the Rho GTPase-regulated actin assembly by diaphanous-related formins, mDia1 and Daam1, in platelets

Journal of Biological Chemistry

Volumn 283, Issue 13, 2008, Pages 8746-8755

  Higashi, Tomohito ^a   Ikeda, Tomoyuki ^a   Shirakawa, Ryutaro ^a   Kondo, Hirokazu ^a   Kawato, Mitsunori ^a   Horiguchi, Masahito ^a   Okuda, Tomohiko ^a   Okawa, Katsuya ^a   Fukai, Shuya ^b,c   Nureki, Osamu ^c,d   Kita, Toru ^a   Horiuchi, Hisanori ^a  

^a KYOTO UNIVERSITY   (Japan)

^b UNIVERSITY OF TOKYO   (Japan)

^c TOKYO INSTITUTE OF TECHNOLOGY   (Japan)

^d RIKEN YOKOHAMA INSTITUTE   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

BLOOD SUBSTITUTES; CHROMATOGRAPHIC ANALYSIS; COLUMN CHROMATOGRAPHY; FILAMENTS (LAMP); FLOW INTERACTIONS; FLUORESCENCE; LIGHT EMISSION; LUMINESCENCE;

ACTIN FILAMENTS; BINDING DOMAINS; BIOCHEMICAL CHARACTERIZATIONS; CYTOSOL; DO-MAINS; FLUORESCENCE INTENSITIES; FORMINS; INHIBITORY DOMAINS; INITIAL VELOCITIES; INTRAMOLECULAR INTERACTIONS; PHALLOIDIN; RHO GTPASES;

PLATELETS;

ACTIN; BINDING PROTEIN; DISHEVELLED ASSOCIATED ACTIVATOR OF MORPHOGENESIS 1 PROTEIN; MDIA 1 PROTEIN; PHALLOIDIN; PROTEIN CDC42; RAC1 PROTEIN; RHO GUANINE NUCLEOTIDE BINDING PROTEIN; RHOA GUANINE NUCLEOTIDE BINDING PROTEIN; RHOB GUANINE NUCLEOTIDE BINDING PROTEIN; RHODAMINE; THROMBIN; UNCLASSIFIED DRUG; DAAM1 PROTEIN, HUMAN; DIAPH1 PROTEIN, HUMAN; SIGNAL TRANSDUCING ADAPTOR PROTEIN;

ACTIN FILAMENT; ARTICLE; CELL STIMULATION; COLUMN CHROMATOGRAPHY; COMPETITIVE INHIBITION; CONTROLLED STUDY; CYTOSOL; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DOMAIN; PROTEIN ISOLATION; REGULATORY MECHANISM; STAINING; STIMULATION; THROMBOCYTE; VELOCITY; AMINO ACID SEQUENCE; BIOCHEMISTRY; CHEMISTRY; GENETICS; HUMAN; KINETICS; METABOLISM; MOLECULAR GENETICS; PROTEIN BINDING;

ACTINS; ADAPTOR PROTEINS, SIGNAL TRANSDUCING; AMINO ACID SEQUENCE; BIOCHEMISTRY; BLOOD PLATELETS; HUMANS; KINETICS; MOLECULAR SEQUENCE DATA; PROTEIN BINDING; RHO GTP-BINDING PROTEINS;

EID: 43749120730     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M707839200     Document Type: Article

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