Biochemical Characterization of the L-Plastin-Actin Interaction Shows a Resemblance with that of α-Actinin and Allows a Distinction to Be Made between the Two Actin-Binding Domains of the Molecule

Biochemistry

Volumn 43, Issue 9, 2004, Pages 2428-2437

  Lebart, M C ^a   Hubert, F ^a   Boiteau, C ^a   Venteo S ^a   Roustan, C ^a   Benyamin, Y ^a  

^a PSL RESEARCH UNIVERSITY   (France)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; CENTRIFUGATION; CROSSLINKING; DEPOLYMERIZATION; INTERFACES (MATERIALS); MOLECULAR DYNAMICS; PHOSPHORUS COMPOUNDS;

ISOFORMS; PLASTIN-ACTIN INTERACTIONS;

BIOCHEMISTRY;

ACTIN; ALPHA ACTININ; F ACTIN; L PLASTIN; PEPTIDE DERIVATIVE; PHOSPHATIDYLINOSITIDE; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; BINDING AFFINITY; CENTRIFUGATION; CROSS LINKING; DEPOLYMERIZATION; FLUORESCENCE; MOLECULAR MODEL; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FAMILY; PROTEIN PROTEIN INTERACTION;

ACTININ; ACTINS; AMINO ACID SEQUENCE; BINDING, COMPETITIVE; CROSS-LINKING REAGENTS; MICROFILAMENT PROTEINS; PHOSPHATIDYLINOSITOLS; PHOSPHOPROTEINS; POLYMERS; PROTEIN BINDING; PROTEIN ISOFORMS; PROTEIN STRUCTURE, TERTIARY;

EID: 1542297717     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi030151p     Document Type: Article

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