The two ADF-H domains of twinfilin play functionally distinct roles in interactions with actin monomers

Molecular Biology of the Cell

Volumn 13, Issue 11, 2002, Pages 3811-3821

  Ojala, Pauli J ^a   Paavilainen, Ville O ^a   Vartiainen, Maria K ^a   Tuma, Roman ^a   Weeds, Alan G ^b   Lappalainen, Pekka ^a  

^a UNIVERSITY OF HELSINKI   (Finland)

^b MRC LABORATORY OF MOLECULAR BIOLOGY   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; BINDING PROTEIN; G ACTIN; MONOMER; TWINFILIN; UNCLASSIFIED DRUG; ACTIN BINDING PROTEIN; ACTIN DEPOLYMERIZING FACTOR; ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; HYBRID PROTEIN; PTK9 PROTEIN, MOUSE;

ARTICLE; BINDING AFFINITY; BINDING SITE; CARBOXY TERMINAL SEQUENCE; CELL FUNCTION; COMPLEX FORMATION; CONCENTRATION RESPONSE; CONFORMATIONAL TRANSITION; DYNAMICS; GEL PERMEATION CHROMATOGRAPHY; LIGHT SCATTERING; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY; AMINO ACID SEQUENCE; ANIMAL; BIOLOGICAL MODEL; CHEMISTRY; GENETICS; MACROMOLECULE; METABOLISM; MOLECULAR GENETICS; MOUSE; PROTEIN BINDING; PROTEIN CONFORMATION; SEQUENCE ALIGNMENT;

ACTIN DEPOLYMERIZING FACTORS; ACTINS; ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; MACROMOLECULAR SUBSTANCES; MICE; MICROFILAMENT PROTEINS; MODELS, BIOLOGICAL; MOLECULAR SEQUENCE DATA; PROTEIN BINDING; PROTEIN CONFORMATION; RECOMBINANT FUSION PROTEINS; SEQUENCE ALIGNMENT;

EID: 0036854364     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E02-03-0157     Document Type: Article

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