F-actin and G-actin binding are uncoupled by mutation of conserved tyrosine residues in maize actin depolymerizing factor (ZmADF)

Proceedings of the National Academy of Sciences of the United States of America

Volumn 94, Issue 18, 1997, Pages 9973-9978

  Jiang, Chang Jie ^a   Weeds, Alan G ^b   Khan, Safina ^a   Hussey, Patrick J ^a  

^a UNIVERSITY OF LONDON   (United Kingdom)

^b Med Res Cncl of Molecular Biology   (United Kingdom)

Author keywords

Cofilin; Cytoskeleton; Destrin or human actin depolymerizing factor; Tertiary structure

Indexed keywords

F ACTIN; G ACTIN;

AMINO ACID SEQUENCE; ARTICLE; BINDING AFFINITY; CYTOSKELETON; DEPOLYMERIZATION; GENE MUTATION; HYDROGEN BOND; MAIZE; PLANT; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; PROTEIN PHOSPHORYLATION; PROTEIN PURIFICATION; PROTEIN TERTIARY STRUCTURE; SITE DIRECTED MUTAGENESIS; VISCOMETRY;

ACTIN DEPOLYMERIZING FACTORS; ACTINS; AMINO ACID SEQUENCE; CARRIER PROTEINS; CONSERVED SEQUENCE; CYTOSKELETAL PROTEINS; DESTRIN; DIMERIZATION; HUMANS; MOLECULAR SEQUENCE DATA; PLANT PROTEINS; PROTEIN CONFORMATION; SEQUENCE ALIGNMENT; TYROSINE; ZEA MAYS;

ACANTHAMOEBA; ZEA MAYS;

EID: 0030930427     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.94.18.9973     Document Type: Article

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