How Leiomodin and Tropomodulin use a common fold for different actin assembly functions

Nature Communications

Volumn 6, Issue , 2015, Pages

  Boczkowska, Malgorzata ^a   Rebowski, Grzegorz ^a   Kremneva, Elena ^b   Lappalainen, Pekka ^b   Dominguez, Roberto ^a  

^a UNIVERSITY OF PENNSYLVANIA   (United States)

^b UNIVERSITY OF HELSINKI   (Finland)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; LEIOMODIN; POLYPEPTIDE; PROTEIN; TROPOMODULIN; TROPOMYOSIN; UNCLASSIFIED DRUG; ACTIN BINDING PROTEIN; LEIOMODIN 2 PROTEIN, HUMAN; MUSCLE PROTEIN; PROTEIN BINDING; TMOD1 PROTEIN, HUMAN;

CELLS AND CELL COMPONENTS; CHEMICAL BINDING; NUCLEATION; PEPTIDE; PROTEIN; SPECIALIZATION;

ARTICLE; CONTROLLED STUDY; PROTEIN ASSEMBLY; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN LOCALIZATION; SARCOMERE; ACTIN FILAMENT; CHEMISTRY; GENETICS; HUMAN; METABOLISM; PROTEIN TERTIARY STRUCTURE;

ACTIN CYTOSKELETON; ACTINS; HUMANS; MICROFILAMENT PROTEINS; MUSCLE PROTEINS; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; TROPOMODULIN;

EID: 84941762912     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms9314     Document Type: Article

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