Importance of a Lys113-Glu195 intermonomer ionic bond in F-actin stabilization and regulation by yeast formins Bni1p and Bnr1p

Journal of Biological Chemistry

Volumn 288, Issue 26, 2013, Pages 19140-19153

  Wen, Kuo Kuang ^a   McKane, Melissa ^a   Rubenstein, Peter A ^a  

^a UNIVERSITY OF IOWA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN POLYMERIZATION; ACTIN-BINDING PROTEINS; ALLOSTERIC COMMUNICATION; ALLOSTERIC EFFECT; CRITICAL CONCENTRATION; DOUBLE MUTANTS; IONIC INTERACTION; SINGLE FILAMENTS;

AMINO ACIDS; MONOMERS; POLYMERIZATION; RESTORATION; STABILIZATION;

PROTEINS;

ACTIN BINDING PROTEIN; BNI1P PROTEIN; BNR1 PROTEIN; F ACTIN; FUNGAL PROTEIN; G ACTIN; GLUTAMINE; LYSINE; PHALLOIDIN; UNCLASSIFIED DRUG; ACTIN; BNI1 PROTEIN, S CEREVISIAE; BNR1 PROTEIN, S CEREVISIAE; CONTRACTILE PROTEIN; CYTOSKELETON PROTEIN; GLUTAMIC ACID; METHENAMINE; SACCHAROMYCES CEREVISIAE PROTEIN;

ACTIN POLYMERIZATION; ALLOSTERISM; ALPHA HELIX; AMINO ACID SEQUENCE; ARTICLE; CELL SIZE; CELL STRUCTURE; CHEMICAL BOND; CIRCULAR DICHROISM; CONTROLLED STUDY; CULTURE MEDIUM; CYTOLOGY; CYTOSKELETON; DIMERIZATION; ELECTRON MICROSCOPY; GENE MUTATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY; PROTEIN STRUCTURE; SACCHAROMYCES CEREVISIAE; SITE DIRECTED MUTAGENESIS; STEADY STATE; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; ENZYMOLOGY; GENE EXPRESSION REGULATION; MITOCHONDRION; MUTAGENESIS SITE-SPECIFIC; MUTATION; POLYMERIZATION; PROTEIN BINDING; YEAST;

ACTIN; CONTRACTILE PROTEIN; CYTOSKELETON; FORMIN; MUTAGENESIS SITE-SPECIFIC; POLYMERIZATION; YEAST;

ACTINS; ALLOSTERIC SITE; CIRCULAR DICHROISM; CYTOSKELETAL PROTEINS; CYTOSKELETON; GENE EXPRESSION REGULATION, FUNGAL; GLUTAMIC ACID; LYSINE; MICROFILAMENT PROTEINS; MITOCHONDRIA; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; MUTATION; PROTEIN BINDING; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS;

EID: 84879567003     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.474122     Document Type: Article

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