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Volumn 1, Issue 5, 2000, Pages 399-410
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The tail domain of myosin M catalyses nucleotide exchange on Rac1 GTPases and can induce actin-driven surface protrusions.
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Author keywords
[No Author keywords available]
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Indexed keywords
ACTIN;
LIGAND;
MYOM PROTEIN, DICTYOSTELIUM DISCOIDEUM;
MYOSIN;
PRIMER DNA;
PROTOZOAL PROTEIN;
RAC1 PROTEIN;
AMINO ACID SEQUENCE;
ANIMAL;
ARTICLE;
BIOLOGICAL MODEL;
CHEMISTRY;
COMPARATIVE STUDY;
DICTYOSTELIUM;
GENETICS;
GROWTH, DEVELOPMENT AND AGING;
HUMAN;
METABOLISM;
MOLECULAR GENETICS;
NUCLEOTIDE SEQUENCE;
OSMOTIC PRESSURE;
PHOSPHORYLATION;
PROTEIN BINDING;
PROTEIN TERTIARY STRUCTURE;
SEQUENCE HOMOLOGY;
ACTINS;
AMINO ACID SEQUENCE;
ANIMALS;
BASE SEQUENCE;
DICTYOSTELIUM;
DNA PRIMERS;
HUMANS;
LIGANDS;
MODELS, BIOLOGICAL;
MOLECULAR SEQUENCE DATA;
MYOSINS;
OSMOTIC PRESSURE;
PHOSPHORYLATION;
PROTEIN BINDING;
PROTEIN STRUCTURE, TERTIARY;
PROTOZOAN PROTEINS;
RAC1 GTP-BINDING PROTEIN;
SEQUENCE HOMOLOGY, AMINO ACID;
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EID: 0034189703
PISSN: 13989219
EISSN: None
Source Type: Journal
DOI: 10.1034/j.1600-0854.2000.010505.x Document Type: Article |
Times cited : (23)
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References (0)
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