T. Kanazawa

发表

Modification of Histidine 5 in Sarcoplasmic Reticulum Ca2+-ATPase by Diethyl Pyrocarbonate Causes Strong Inhibition of Formation of the Phosphoenzyme Intermediate from Inorganic Phosphate*

T. Saino, K. Yamasaki, T. Daiho, 1997, The Journal of Biological Chemistry.

Coincidence of H+ binding and Ca2+ dissociation in the sarcoplasmic reticulum Ca-ATPase during ATP hydrolysis.

M. Yamaguchi, T. Kanazawa, 1985, The Journal of biological chemistry.

Formation and decomposition of a phosphorylated intermediate in the reaction of Na+-K+ dependent ATPase

Y. Tonomura, M. Saito, T. Kanazawa, 1970 .

Reduction of disulfide bonds in sarcoplasmic reticulum Ca(2+)-ATPase by dithiothreitol causes inhibition of phosphoenzyme isomerization in catalytic cycle. This reduction requires binding of both purine nucleotide and Ca2+ to enzyme.

T. Daiho, T. Kanazawa, 1994, The Journal of biological chemistry.

Some acyl phosphate-like properties of P32-labeled sodium-potassium-activated adenosine triphosphatase.

K. Nagano, M. Nakao, T. Nakao, 1965, Biochemical and biophysical research communications.

[Properties of a phosphorylated protein as a reaction intermediate of Na+-K+ sensitive ATPase].

Y. Tonomura, M. Saito, T. Kanazawa, 1967, Journal of biochemistry.

Room temperature negative differential resistance of CdF2∕CaF2 double-barrier resonant tunneling diode structures grown on Si(100) substrates

M. Asada, Ryo Fujii, M. Watanabe, 2007 .

Phosphoenzyme formation from ATP in the ATPase of sarcoplasmic reticulum. Effect of KCl or ATP and slow dissociation of ATP from precursor enzyme-ATP complex.

M. Shigekawa, T. Kanazawa, 1982, The Journal of biological chemistry.

Identification of Arginyl Residues Located at the ATP Binding Site of Sarcoplasmic Reticulum Ca2+-ATPase

Hiroshi Suzuki, K. Yamasaki, T. Daiho, 1996, The Journal of Biological Chemistry.

Deletions or Specific Substitutions of a Few Residues in the NH2-terminal Region (Ala3 to Thr9) of Sarcoplasmic Reticulum Ca2+-ATPase Cause Inactivation and Rapid Degradation of the Enzyme Expressed in COS-1 Cells*

Hiroshi Suzuki, T. Saino, K. Yamasaki, 1999, The Journal of Biological Chemistry.

Mutations of Arg198 in sarcoplasmic reticulum Ca2+‐ATPase cause inhibition of hydrolysis of the phosphoenzyme intermediate formed from inorganic phosphate

Hiroshi Suzuki, T. Saino, K. Yamasaki, 1999, FEBS letters.

Modification of Arginine-198 in Sarcoplasmic Reticulum Ca2+-ATPase by 1,2-Cyclohexanedione Causes Inhibition of Formation of the Phosphoenzyme Intermediate from Inorganic Phosphate*

T. Saino, T. Daiho, T. Kanazawa, 1997, The Journal of Biological Chemistry.

Source of the oxygen in the C-O-P linkage of the acyl phosphate in transport adenosine triphosphatases.

P. Boyer, A. Dahms, T. Kanazawa, 1973, The Journal of biological chemistry.

Occurrence and characteristics of a rapid exchange of phosphate oxygens catalyzed by sarcoplasmic reticulum vesicles.

P. Boyer, T. Kanazawa, 1973, The Journal of biological chemistry.

Quasi-irreversible inactivation of the sarcoplasmic reticulum Ca(2+)-ATPase by simultaneous tight binding of magnesium and fluoride to the catalytic site.

T. Daiho, T. Kanazawa, T. Kubota, 1993, Biochimica et biophysica acta.

[Molecular mechanism of muscle contraction].

Y. Tonomura, T. Kanazawa, 1961, Tanpakushitsu kakusan koso. Protein, nucleic acid, enzyme.

Reduction in Water Activity Greatly Retards the Phosphoryl Transfer from ATP to Enzyme Protein in the Catalytic Cycle of Sarcoplasmic Reticulum Ca-ATPase (*)

Hiroshi Suzuki, T. Kanazawa, 1996, The Journal of Biological Chemistry.

A conformational change of N-iodoacetyl-N'-(5-sulfo-1-naphthyl)ethylenediamine-labeled sarcoplasmic reticulum Ca2+-ATPase upon ATP binding to the catalytic site.

H. Suzuki, H. Kuwayama, T. Kanazawa, 1987, The Journal of biological chemistry.

Stoichiometry of Phosphorylation to Fluorescein 5-Isothiocyanate Binding in the Ca2+-ATPase of Sarcoplasmic Reticulum Vesicles*

Hiroshi Suzuki, T. Kanazawa, S. Nakamura, 1997, The Journal of Biological Chemistry.

Role of Mg2+ in the Ca2+-Ca2+ exchange mediated by the membrane-bound (Ca2+, Mg2+)-ATPase of sarcoplasmic reticulum vesicles.

Y. Takakuwa, T. Kanazawa, 1982, The Journal of biological chemistry.

Slow transition of phosphoenzyme from ADP-sensitive to ADP-insensitive forms in solubilized Ca2+, Mg2+-ATPase of sarcoplasmic reticulum: evidence for retarded dissociation of Ca2+ from the phosphoenzyme.

Y. Takakuwa, T. Kanazawa, 1979, Biochemical and biophysical research communications.

Fluorometric study on conformational changes in the catalytic cycle of sarcoplasmic reticulum Ca2+-ATPase

Hiroshi Suzuki, K. Yamasaki, T. Kanazawa, 1995, Bioscience reports.

The Tryptophan Fluorescence Change upon Conformational Transition of the Phosphoenzyme Intermediate in Sarcoplasmic Reticulum Ca-ATPase Is Revealed in the Absence of K and the Presence of Lasalocid (*)

Hiroshi Suzuki, T. Kanazawa, 1995, The Journal of Biological Chemistry.

Effects of divalent cations bound to the catalytic site on ATP-induced conformational changes in the sarcoplasmic reticulum Ca(2+)-ATPase: stopped-flow analysis of the fluorescence of N-acetyl-N'-(5-sulfo-1-naphthyl)ethylenediamine attached to cysteine-674.

H. Suzuki, T. Kanazawa, S. Nakamura, 1994, Biochemistry.

Characterization of the phosphoenzyme that is involved in the Ca2+ -Ca2+ exchange catalyzed by the Ca2+ -ATPase of sarcoplasmic reticulum vesicles.

T. Kanazawa, S. Inao, 1986, Biochimica et biophysica acta.

Ca2+−Ca2+ EXCHANGE MEDIATED BY THE MEMBRANE-BOUND (Ca2+, Mg2+)-ATPase OF SARCOPLASMIC RETICULUM VESICLES

Y. Takakuwa, T. Kanazawa, 1985 .

Ca2+-Ca2+ exchange catalyzed by the membrane-bound Ca2+, Mg2+-ATPase of sarcoplasmic reticulum vesicles.

Y. Takakuwa, T. Kanazawa, 1984, Current topics in cellular regulation.

Phosphorylation of solubilized sarcoplasmic reticulum by orthophosphate and its thermodynamic characteristics. The dominant role of entropy in the phosphorylation.

T. Kanazawa, 1975, The Journal of biological chemistry.

Protonation of the sarcoplasmic reticulum Ca-ATPase during ATP hydrolysis.

M. Yamaguchi, T. Kanazawa, 1984, The Journal of biological chemistry.

Reaction mechanism of (Ca2+, Mg2+)-ATPase of sarcoplasmic reticulum vesicles. I. Phosphoenzyme with bound Ca2+ which is exposed to the external medium.

Y. Takakuwa, T. Kanazawa, 1981, The Journal of biological chemistry.

Reaction mechanism of (Ca2+, Mg2+)-ATPase of sarcoplasmic reticulum vesicles. II. (ATP, ADP)-dependent Ca2+-Ca2+ exchange across the membranes.

Y. Takakuwa, T. Kanazawa, 1981, The Journal of biological chemistry.

The ATP-induced change of tryptophan fluorescence reflects a conformational change upon formation of ADP-sensitive phosphoenzyme in the sarcoplasmic reticulum Ca(2+)-ATPase. Stopped-flow spectrofluorometry and continuous flow-rapid quenching method.

H. Suzuki, T. Kanazawa, S. Nakamura, 1994, The Journal of biological chemistry.

3'-O-(5-fluoro-2,4-dinitrophenyl)-ATP exclusively labels Lys-492 at the active site of the sarcoplasmic reticulum Ca(2+)-ATPase.

K. Yamasaki, T. Daiho, T. Kanazawa, 1994, The Journal of biological chemistry.

Labeling of lysine 492 with pyridoxal 5'-phosphate in the sarcoplasmic reticulum Ca(2+)-ATPase. Lysine 492 residue is located outside the fluorescein 5-isothiocyanate-binding region in or near the ATP binding site.

T. Daiho, K. Yamagata, T. Kanazawa, 1993, The Journal of biological chemistry.

Inhibition by A23187 of conformational changes involved in the Ca(2+)-induced activation of sarcoplasmic reticulum Ca(2+)-ATPase.

T. Kanazawa, H. Ohmiya, 1991, Journal of biochemistry.

Characterization of the substrate-induced conformational change of N-iodoacetyl-N'-(5-sulfo-1-naphthyl)ethylenediamine-labeled sarcoplasmic reticulum Ca2(+)-ATPase by using different kinds of substrate.

H. Suzuki, T. Kanazawa, K. Kubo, 1990, Biochimica et biophysica acta.

Selective inhibition by lasalocid of hydrolysis of the ADP-insensitive phosphoenzyme in the catalytic cycle of sarcoplasmic reticulum Ca2(+)-ATPase.

T. Kawashima, H. Hara, T. Kanazawa, 1990, The Journal of biological chemistry.

Changes in the steady-state fluorescence anisotropy of N-iodoacetyl-N'-(5-sulfo-1-naphthyl)ethylenediamine attached to the specific thiol of sarcoplasmic reticulum Ca2+-ATPase throughout the catalytic cycle.

H. Suzuki, T. Kanazawa, K. Kubo, 1989, The Journal of biological chemistry.

Conformational changes in the vicinity of the N-iodoacetyl-N'-(5-sulfo-1-naphthyl)ethylenediamine attached to the specific thiol of sarcoplasmic reticulum Ca2+-ATPase throughout the catalytic cycle.

H. Suzuki, T. Kanazawa, M. Obara, 1988, The Journal of biological chemistry.

Selective inhibition by ionophore A23187 of the enzyme isomerization in the catalytic cycle of sarcoplasmic reticulum Ca2+-ATPase.

H. Hara, T. Kanazawa, 1986, The Journal of biological chemistry.

ATP formation from ADP and a phosphorylated intermediate of Ca2+-dependent ATPase in fragmented sarcoplasmic reticulum.

Y. Tonomura, T. Kanazawa, S. Yamada, 1970, Journal of biochemistry.

Reaction mechanism of (Ca2+, Mg2+)-ATPase of sarcoplasmic reticulum. The role of Mg2+ that activates hydrolysis of the phosphoenzyme.

Y. Takakuwa, T. Kanazawa, 1982, The Journal of biological chemistry.

Acetylphosphate-induced Ca2+-Ca2+ exchange that is mediated by (Ca2+,Mg2+)-ATPase in sarcoplasmic reticulum vesicles.

Y. Takakuwa, T. Kanazawa, 1984, Journal of biochemistry.

ENTROPY-DRIVEN PHOSPHORYLATION WITH Pi OF THE TRANSPORT ATPase OF SARCOPLASMIC RETICULUM

Y. Takakuwa, F. Katabami, T. Kanazawa, 1979 .

Formation and decomposition of a phosphorylated intermediate in the reaction of Na plus-K plus dependent ATPase.

Y. Tonomura, M. Saito, T. Kanazawa, 1970, Journal of biochemistry.

Stoichiometry of tight binding of magnesium and fluoride to phosphorylation and high-affinity binding of ATP, vanadate, and calcium in the sarcoplasmic reticulum Ca(2+)-ATPase.

T. Daiho, T. Kanazawa, T. Kubota, 1993, Biochemistry.

Existence of a low-affinity ATP-binding site in the unphosphorylated Ca2(+)-ATPase of sarcoplasmic reticulum vesicles: evidence from binding of 2',3'-O-(2,4,6-trinitrocyclohexadienylidene)-[3H]AMP and -[3H]ATP.

H. Suzuki, T. Kanazawa, T. Kubota, 1990, Biochemistry.

Formation of a reactive myosin-phosphate complex as a key reaction in muscle contraction.

Y. Tonomura, T. Kanazawa, 1965, The Journal of biological chemistry.

Reaction mechanism of the Ca 2+ -dependent ATPase of sarcoplasmic reticulum from skeletal muscle. VI. Co-operative transition of ATPase activity during the initial phase.

Y. Tonomura, T. Yamamoto, T. Kanazawa, 1971, Journal of biochemistry.