1994
Differential regulation of skeletal muscle myosin‐II and brush border myosin‐I enzymology and mechanochemistry by bacterially produced tropomyosin isoforms
Fanning A, Wolenski J, Mooseker M, Izant J. Differential regulation of skeletal muscle myosin‐II and brush border myosin‐I enzymology and mechanochemistry by bacterially produced tropomyosin isoforms. Cytoskeleton 1994, 29: 29-45. PMID: 7820856, DOI: 10.1002/cm.970290104.Peer-Reviewed Original ResearchMeSH KeywordsActinsAmino Acid SequenceAnimalsCa(2+) Mg(2+)-ATPaseCarrier ProteinsCell MovementChick EmbryoDNA, ComplementaryEscherichia coliIntestinal MucosaMicrofilament ProteinsMicrovilliMolecular Sequence DataMolecular WeightMuscle ProteinsMyosinsProtein BindingRecombinant Fusion ProteinsRecombinant ProteinsSequence HomologySpecies SpecificityTropomyosinVertebratesXenopusConceptsAlpha-tropomyosinMuscle myosin IIMyosin enzymologyMyosin isoformsTwo- toStriated MuscleMgATPase activityDifferential regulationBrush border myosinDetectable effectIsoformsLow affinityChimeric tropomyosinsMuscle tropomyosinMuscle alpha-tropomyosinSkeletal muscle myosin IIActinTropomyosin isoformsMuscle myosinF-actin
1989
Partial deduced sequence of the 110-kD-calmodulin complex of the avian intestinal microvillus shows that this mechanoenzyme is a member of the myosin I family.
Garcia A, Coudrier E, Carboni J, Anderson J, Vandekerkhove J, Mooseker M, Louvard D, Arpin M. Partial deduced sequence of the 110-kD-calmodulin complex of the avian intestinal microvillus shows that this mechanoenzyme is a member of the myosin I family. Journal Of Cell Biology 1989, 109: 2895-2903. PMID: 2687288, PMCID: PMC2115973, DOI: 10.1083/jcb.109.6.2895.Peer-Reviewed Original Research