Actin polymerization is controlled by residue size at position 204

Biochemistry and Cell Biology

Volumn 87, Issue 6, 2009, Pages 853-865

  Yates, Susan P ^a,b   Loncar, Ana ^a   Dawson, John F ^a  

^a UNIVERSITY OF GUELPH   (Canada)

^b QUEEN S UNIVERSITY   (Canada)

Author keywords

Actin polymerization; Critical concentration; Mutagenesis; Nucleotide

Indexed keywords

ACTIN FILAMENT; ACTIN POLYMERIZATION; COLD TEMPERATURES; CRITICAL CONCENTRATION; DOUBLE MUTANTS; ENERGY MINIMIZATION; F-ACTIN; HIGH CONCENTRATION; HYPEROSMOLARITY; IN-VITRO; PHYSIOLOGICAL CONCENTRATIONS; SINGLE MUTATION; SUBDOMAIN; WILD TYPES; YEAST ACTIN;

CONCENTRATION (PROCESS); FILAMENTS (LAMP); MUTAGENESIS; NUCLEOTIDES; PHOSPHORYLATION; POLYMERIZATION; YEAST;

PROTEINS;

ACTIN; ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; ALANINE; CYSTEINE; F ACTIN; GLYCINE; SERINE;

ACTIN FILAMENT; ACTIN POLYMERIZATION; AMINO ACID SEQUENCE; ARTICLE; CONTROLLED STUDY; FUNGAL STRAIN; MOLECULAR SIZE; NONHUMAN; PROTEIN DOMAIN; PROTEIN EXPRESSION; SACCHAROMYCES CEREVISIAE; SEQUENCE ANALYSIS; TEMPERATURE SENSITIVE CLONE;

ACTINS; ADENOSINE TRIPHOSPHATASES; ADENOSINE TRIPHOSPHATE; MICROFILAMENTS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; POLYMERS; PROTEIN STRUCTURE, QUATERNARY; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS;

EID: 74549145228     PISSN: 08298211     EISSN: 12086002     Source Type: Journal    
DOI: 10.1139/O09-039     Document Type: Article

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