Yazawa Michio | Division Of Chemistry Faculty Of Science Hokkaido University

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著作論文

Reactivies of Cys^ (SH1) in Intermediate States of Myosin Subfragment-1 ATPase
Secondary Structure and Ca^-Binding Property of the N-Terminal Half Domain of Calmodulin from Yeast Saccharomyces cerevisiae as Studied by NMR
Conformations of Vertebrate Striated Muscle Myosin Monomers in Equilibrium with Filaments
Asymmetric Photocross-Linking of Singly Phosphorylated Smooth Muscle Heavy Meromyosin
Identification and Characterization of a Novel Calcineurin-Binding Protein in Scallop Testis
IDENTIFICATION AS HEAT-SHOCK PROTEINS OF CALCIUM-DEPENDENT CALMODULIN BINDING PROTEIN FROM RAT SPERMATOGENIC CELLS(Developmental Biology)(Proceedings of the Seventy-Third Annual Meeting of the Zoological Society of Japan)
Essential Light Chain Modulates Phosphorylation-Dependent Regulation of Smooth Muscle Myosin
Functional Role of the C-Terminal Domain of Smooth Muscle Myosin Light Chain Kinase on the Phosphorylation of Smooth Muscle Myosin
Two New Modes of Smooth Muscle Myosin Regulation by the Interaction between the Two Regulatory Light Chains, and by the S2 Domain
Conformation,Filament Assembly,and Activity of Single-Headed Smooth Muscle Myosin
Crosslinking of Telokin to Chicken Gizzard Smooth Muscle Myosin
Molecular Cloning of cDNA Encoding Two Subunits of Calcineurin from Scallop Testis : Demonstration of Stage-Specific Expression during Maturation of the Testis
Mapping phosphorylation site of the regulatory light chain in smooth muscle myosin by immuno-electron microscopy
Identification of Trimeric Myosin Phosphatase ( PP1M ) as a Targer for a Novel PKC-Potentiated Protein Phosphatase-1 Inhibitory Protein ( CPI17 ) in Porcine Aorta Smooth Muscle
Dynamic assembly properties of nonmuscle myosin II isoforms revealed by combination of fluorescence correlation spectroscopy and fluorescence cross-correlation spectroscopy
Two New Modes of Smooth Muscle Myosin Regulation by the Interaction between the Two Regulatory Light Chains, and by the S2 Domain.

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