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  1. Kazuo Yamasaki, Takashi Daiho, and Hiroshi Suzuki.
       Remarkable Stability of Solubilized and Delipidated Sarcoplasimc Reticulum Ca2+-ATPase with Tightly Bound Fluoride and Magnesium against Detergent-induced
       Denaturation.J. Biol. Chem. in press, 2002
 
  2. Stefania Danko, Kazuo Yamasaki, Takashi Daiho, Hiroshi Suzuki, and Chikashi Toyoshima.
       Organization of cytoplasmic domains of sarcoplasmic reticulum Ca2+-ATPase in E1P and E1ATP states: a limited proteolysis study. FEBS Letters, Vol.505, 129-135, 2001
       (Hiroshi Suzuki; corresponding author)
  3. Takashi Daiho, Kazuo Yamasaki, Tomoyuki Saino, Mika Kamidochi, Katsuhiko Satoh, Hajime Iizuka,andHiroshi Suzuki.
       Mutations of Either or both of Cys876 and Cys888 of Sarcoplasmic Reticulum Ca2+-ATPase Resultin a Complete Loss of Ca2+Transport Activity without a Loss of
       Ca2+-ATPase activity.J. Biol. Chem.Vol.276(35), 32771-32778, 2001
  4. Hidetoshi Takahashi, Yoshiaki Atsuta, Katsuhiko Sato, Akemi Ishida-Yamamoto, Hiroshi Suzuki, and Hajime Iizuka.
       Novel mutations of ATP2A2 gene in Japanese patients of Darier's disease. J. Dermatol. Sci. Vol.26(3), 169-172, 2001
  5. —é–Ø@—TBCa2+ƒ|ƒ“ƒvBƒVƒŠ[ƒYEƒoƒCƒIƒTƒCƒGƒ“ƒX‚ÌV¢‹I Vol.12uŠ´ŠoŠíН‚Æ”]“àî•ñˆ—vi“ú–{¶‰»Šw‰ïE‹¤—§o”ÅjAˆóü’†A2001
  6. —é–Ø@—TBœŠi‹Ø‚ÌŽûkE’oŠÉ‚̃XƒCƒbƒ`‚͉½‚©H\\‹»•±Žûk˜AŠÖB‰^“®‚Æ•ªŽq¶•¨ŠwQ&A(‘åCŠÙ‘“X)Aˆóü’†A2001
  7. Stefania Danko, Takashi Daiho, Kazuo Yamasaki, Mika Kamidochi, Hiroshi Suzuki, and Chikashi Toyoshima.
       ADP-insensitive phosphoenzyme intermediate of sarcoplasmic reticulum Ca2+-ATPase has a compact conformation resistant to proteinase K, V8 protease and trypsin.
      FEBS Letters, Vol.498(2-3), 277-282, 2001 (Hiroshi Suzuki; corresponding author)
  8. Hiroshi Suzuki, Takashi Daiho, Kazuo Yamasaki, and Tohru Kanazawa.
       Only half of the Ca2+-ATPase molecules present in sarcoplasmic reticulum vesicles can be phosphorylated with ATP or Inorganic phosphate.
      in Na/K-ATPase and Related ATPases. (K.Taniguchi and S.Kaya Eds.) pp.381-388, 2000, Elsevier, North Holland,
  9. Takashi Daiho, Kazuo Yamasaki, Hiroshi Suzuki, Tomoyuki Saino, and Tohru Kanazawa.
       Deletions or specific substitutions of a few residents in the NH2-terminal Ala3-Thr9 region of sarcoplasmic reticulum Ca2+-ATPase cause inactivation and rapid degradation of
       the enzyme expressed in COS-1 cells. in Na/K-ATPase and Related ATPases. (K.Taniguchi and S.Kaya Eds.) pp.293-296, 2000, Elsevier, North Holland,
10. Kazuo Yamasaki, Takashi Daiho, Hiroshi Suzuki, Tomoyuki Saino, and Tohru Kanazawa.
       Mutations ofarginine-198 in sarcoplasmic reticulum Ca2+-ATPase cause inhibition of hydrolysis of the phosphoenzyme intermediate formed from inorganic phosphate.
      in Na/K-ATPase and Related ATPases. (K.Taniguchi and S.Kaya Eds.) pp.297-300, 2000, Elsevier, North Holland,
11. Takashi Daiho, Kazuo Yamasaki, Hiroshi Suzuki, Tomoyuki Saino, and Tohru Kanazawa.
       Deletions or Specific Substitutions of a Few Residues in the NH2-terminal Region (Ala3-Thr9) of Sarcoplasmic Reticulum Ca2+-ATPase Cause Inactivation and Rapid
       Degradation of the Enzyme Expressed in COS-1 Cells. J. Biol. Chem. Vol.274(34), 23910-23915, 1999
12. Takashi Daiho, Hiroshi Suzuki, Kazuo Yamasaki, Tomoyuki Saino, and Tohru Kanazawa.
       Mutations of Arg198 in Sarcoplasmic Reticulum Ca2+-ATPase Cause Inhibition of Hydrolysis of the Phosphoenzyme Intermediate Formed from Inorganic Phosphate.
      FEBS Letters Vol. 444(1), 54-58, 1999
13. Hiroshi Suzuki and Tohru Kanazawa.
       Formation of the ADP-Insensitive Phosphoenzyme Intermediate in the Sarcoplasmic Reticulum Ca2+-ATPase of Which both Cys344 and Cys364 Are Modified by
       N-Ethylmaleimide. Biochemistry Vol.38 (2), 820-825, 1999
14. —é–Ø@—TBCa2+ƒ|ƒ“ƒv\\Œ`Ž¿–Œ‚Ƭ–E‘ÌB’`”’Ž¿ŠjŽ_y‘fVol.43 (10)i‘Ч†FƒJƒ‹ƒVƒEƒ€‚ƃVƒOƒiƒ‹“`’BjA1610-1621A1998
15. Satoshi Nakamura, Hiroshi Suzuki and Tohru Kanazawa.
       Stoichiometry of Phosphorylation to Fluorescein 5-Isothiocyanate Binding in the Ca2+-ATPase of Sarcoplasmic Reticulum Vesicles.
      J. Biol. Chem. Vol.272 (10), 6232-6237, 1997
16. Keisuke Kimura, Hiroshi Suzuki, Takashi Daiho, Kazuo Yamasaki, and Tohru Kanazawa.
       Identification of Arginyl Residues Located at the ATP Binding Site of Sarcoplasmic Reticulum Ca2+-ATPase: Modification with 1,2-Cyclohexanedione.
      J. Biol. Chem. Vol.271 (46), 28933-28941, 1996
17. Hiroshi Suzuki and Tohru Kanazawa.
       Reduction in Water Activity Greatly Retards the Phosphoryl Transfer from ATP to Enzyme Protein in the Catalytic Cycle of Sarcoplasmic Reticulum Ca2+-ATPase.
      J. Biol. Chem. Vol.271 (10), 5481-5486, 1996
18. Tohru Kanazawa, Hiroshi Suzuki, Takashi Daiho, and Kazuo Yamasaki.
       Fluorometric Study on Conformational Changes in the Catalytic Cycle of Sarcoplasmic Reticulum Ca2+-ATPase. Bioscience Reports Vol.15 (5), 317-326, 1995
19. Hiroshi Suzuki and Tohru Kanazawa.
       The Tryptophan Fluorescence Change upon Conformational Transition of the Phosphoenzyme Intermediate in Sarcoplasmic Reticulum Ca2+-ATPase Is Revealed in the
       Absence of K{and the Presence of Lasalocid. J. Biol. Chem. Vol.270 (7), 3089-3093, 1995
20. Hiroshi Suzuki, Satoshi Nakamura, and Tohru Kanazawa.
       Effects of Divalent Cations Bound to the Catalytic Site on ATP-Induced Conformational Changes in the Sarcoplasmic Reticulum Ca2+-ATPase: Stopped-Flow Analysis of the
       Fluorescence of N-Acetyl-N'-(5-sulfo-1-naphthyl)ethylenediamine Attached to Cysteine-674. Biochemistry Vol.33 (27), 8240-8246, 1994
21. Satoshi Nakamura, Hiroshi Suzuki, and Tohru Kanazawa.
       The ATP-induced Change of Tryptophan Fluorescence Reflects a Conformational Change upon Formation of ADP-sensitive Phosphoenzyme in the Sarcoplasmic Reticulum
       Ca2+-ATPase: Stopped-Flow Spectrofluorometry and Continuous Flow-Rapid Quenching Method. J. Biol. Chem. Vol.269 (23), 16015-16019, 1994
22. —é–Ø@—TB‹Ø¬–E‘ÌCa2+-ATPƒA[ƒ[B¶‰»ŠwA‘æ64Šªi‘æ12†jA1444-1449A1992
23. Hiroshi Suzuki, Tatsuya Kubota, Koji Kubo, and Tohru Kanazawa.
       Existence of a Low-affinity ATP-binding Site in the Unphosphorylated Ca2+-ATPase of Sarcoplasmic Reticulum Vesicles: Evidence from Bionding of
       2',3'-0-(2,4,6-Trinitrocyclohexandienylidene)-[3H]AMP and -[3H] ATP. Biochemistry Vol.29 (30), 7040-7045, 1990
24. Koji Kubo, Hiroshi Suzuki, and Tohru Kanazawa.
       Characterization of the Substrate-induced Conformational Change of N-Iodoacetyl-N'-(5-sulfo-1-naphthyl)ethylenediamine-lebeled Sarcoplasamic Reticulum Ca2+-ATPase
       by Using Different Kinds of Substrate.Biochimi. Biophys. Acta Vol.1040(2), 251-259, 1990
25. Hiroshi Suzuki, Mitsuhiro Obara, Koji Kubo, and Tohru Kanazawa.
       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.J. Biol. Chem. Vol.264 (2), 920-927, 1989
26. Hiroshi Suzuki, Yoshifusa Kondo, Aida D. Carlos, and John C. Seidel.
       Effects of Phosphorylation, MgATP, and Ionic Strength on the Rates of Papain Degradation of Heavy and Light Chains of Smooth Muscle Heavy Meromyosin at the
       S1-S2 Junction. J. Biol. Chem. Vol.263 (22), 10974-10979, 1988
27. Mithsuhiro Obara, Hiroshi Suzuki, and Tohru Kanazawa.
       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.J. Biol. Chem. Vol.263 (8), 3690-3697, 1988
28. Hiroshi Suzuki, Mitsuhiro Obara, Hideto Kuwayama, and Tohru Kanazawa.
       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
       through the Catalytic Cycle.Calcium Signal and Cell Response (K. Yagi and T. Miyazaki Eds.) 332-334, 1988
29. Hiroshi Suzuki, Mitsuhiro Obara, Hideto Kuwayama, and Tohru Kanazawa.
       A Conformational Change of N-Iodoacetyl-N'-(5-sulfo-1-naphthyul)ethylenediamine-labeled Sarcoplasmic Reticulum Ca2+-ATPase upon ATP Binding to the Catalytic Site.
      J. Biol. Chem. Vol.262 (32), 15448-15456, 1987
30. Sumitra Nag, Hiroshi Suzuki, Jan Sosinski, and John C. Seidel.
       Conformational Changes in Myosin and Heavy Meromyosin from Chicken Gizzard Associated with Phosphorylation.
      Regulation and Contraction of Smooth Muscle (Siegman, M. J., Somlyo, A. P., and Stephens, N. L. Eds.) Vol.91-108, 1987
31. Hiroshi Suzuki, Walter F. Stafford, III, Henry S. Slayter, and John C. Seidel.
       A Conformational Transition in Gizzard Heavy Meromyosin Involving the Head-Tail Junction, Resulting in Changes in Sedimentation Coefficient, ATPase Activity, and
       Orientation of Heads.J. Biol. Chem. Vol.260, 14810-14817, 1985
32. T. S. Chandra, Narindar Nath, Hiroshi Suzuki, and John C. Seidel.
       Modification of Thiols of Gizzard Myosin Alters ATPase Activity, Stability of Myosin Filaments, and the 6-10S Conformational Transition.
      J. Biol.Chem. Vol.260, 202-207, 1985
33. —é–Ø@—TB•½ŠŠ‹ØŽûk§Œä‚Ì•ªŽq‹@\|Œy½‚ÌƒŠƒ“Ž_‰»‚È‚ç‚тɒEƒŠƒ“Ž_‰»‚É‚æ‚éƒ~ƒIƒVƒ“•ªŽq‚ÌŒ`‘ԕω»|BŒŒŠÇu–¬ŠÇŒ¤‹†vA6ŠªA157-169A1983
34. Hiroshi Suzuki, Toshio Kamata, Hirofumi Onishi, and Shizuo Watanabe.
       Adenosine Triphosphate-Induced Reversible Change in the Conformation of Chicken Gizzard Myosin and Heavy Meromyosin. J. Biochem.Vol.91, 1699-1705, 1982
35. Hiroshi Suzuki, Koui Takahashi, Hirofumi Onishi, and Shizuo Watanabe.
       Reversible Changes in the State of Phosphorylation of Gizzard Myosin, in That of Gizzard Myosin Assembly, in the ATPase Activity of Gizzard Myosin, in That of Actomyosin
       and in the Superprecipitation Activity. J. Biochem.Vol.91, 1687-1698, 1982
36. Hiroshi Suzuki, Sawako Suzuki, and Shizuo Watanabe.
       High Concentrations of Magnesium for Formation of Thick-Filaments of Chicken Gizzard Myosin.J. Biochem. Vol.89, 871-878, 1981
37. Hiroshi Suzuki, Kunihiko Konno, Ken-ichi Arai, and Shizuo Watanabe.
       ATP-Induced Tension Development in Glycerinated Fibers of Scallop Adductor Striated Muscle: Role of Regulatory Light Chain of Myosin in Calcium Regulation of Muscle
       Contraction.J. Biochem.Vol.88, 909-911, 1980
38. Hiroshi Suzuki, Hirofumi Onishi, Koui Takahashi, and Shizuo Watanabe.
       Structure and Function of Chicken Gizzard Myosin. J. Biochem. Vol.84, 1529-1542, 1978
39. Hiroshi Suzuki, Kayoko Nakamura, Koui Takahashi, and Shizuo Watanabe.
       Adenosine Triphosphatase Activity and "Thick Filament" Formation of Chicken Gizzard Myosin in Low Salt Media. J. Biochem. Vol.83, 835-847, 1978
40. Hirofumi Onishi, Yoosuke Yamada, Mitsuo Ikebe, Hiroshi Suzuki, and Shizuo Watanabe.
       The ATPase Reaction in the Steady State and in the Initial Burst Catalyzed by Chicken Gizzard Myosin in 0.6 M KC1. J. Biochem. Vol.83, 129-135, 1978

 
 
 

‘å@•Û@@‹M@Žk
 

  1. Kazuo Yamasaki, Takashi Daiho, and Hiroshi Suzuki.
       Remarkable Stability of Solubilized and Delipidated Sarcoplasimc Reticulum Ca2+-ATPase with Tightly Bound Fluoride and Magnesium against Detergent-induced
       Denaturation. J. Biol. Chem. in press, 2002
  2. Stefania Danko, Kazuo Yamasaki, Takashi Daiho, Hiroshi Suzuki, and Chikashi Toyoshima.
       Organization of cytoplasmic domains of sarcoplasmic reticulum Ca2+-ATPase in E1P and E1ATP states: a limited proteolysis study. FEBS Letters, Vol.505, 129-135, 2001
  3. Takashi Daiho, Kazuo Yamasaki, Tomoyuki Saino, Mika Kamidochi, Katsuhiko Satoh, Hajime Iizuka, and Hiroshi Suzuki.
       Mutations of Either or both of Cys876 and Cys888 of Sarcoplasmic Reticulum Ca2+-ATPase Result in a Complete Loss of Ca2+ Transport Activity without a Loss of
       Ca2+-ATPase activity, J. Biol. Chem. Vol.276(35), 32771-32778, 2001
  4. Stefania Danko, Takashi Daiho, Kazuo Yamasaki, Mika Kamidochi, Hiroshi Suzuki, and Chikashi Toyoshima.
       ADP-insensitive phosphoenzyme intermediate of sarcoplasmic reticulum Ca2+-ATPase has a compact conformation resistant to proteinase K, V8 protease and trypsin.
      FEBS Letters, Vol. 498(2-3), 277-282, 2001
  5. Hiroshi Suzuki, Takashi Daiho, Kazuo Yamasaki, and Tohru Kanazawa.
       Only half of the Ca2+-ATPase molecules present in sarcoplasmic reticulum vesicles can be phosphorylated with ATP or Inorganic phosphate.
      Na/K-ATPase and Related ATPases.(K.Taniguchi and S.Kaya Eds.)Elsevier, North Holland, 381-388, 2000
  6. Takashi Daiho, Kazuo Yamasaki, Hiroshi Suzuki, Tomoyuki Saino, and Tohru Kanazawa.
       Deletions or specific substitutions of a few residents in the NH2-terminal Ala3-Thr9 region of sarcoprasmic reticulum Ca2+-ATPase cause inactivation and rapid degradation
       of the enzyme expressed in COS-1 cells. Na/K-ATPase and Related ATPases.(K.Taniguchi and S.Kaya Eds.)Elsevier, North Holland, 293-296, 2000
  7. Kazuo Yamasaki, Takashi Daiho, Hiroshi Suzuki, Tomoyuki Saino, and Tohru Kanazawa.
       Mutations of arginine-198 in sarcoplasmic reticulum Ca2+-ATPase cause inhibition of hydrolysis of the phosphoenzyme intermediate formed from inorganic phosphate.
      Na/K-ATPase and Related ATPases.(K.Taniguchi and S.Kaya Eds.)Elsevier, North Holland, 297-300, 2000
  8. Takashi Daiho, Kazuo Yamasaki, Hiroshi Suzuki, Tomoyuki Saino, and Tohru Kanazawa.
       Deletions or Specific Substitutions of a Few Residues in the NH2-terminal Region (Ala3-Thr9) of Sarcoplasmic Reticulum Ca2+-ATPase Cause Inactivation and Rapid
       Degradation of the Enzyme Expressed in COS-1 Cells. J. Biol. Chem. Vol.274 (34), 23910-23915, 1999
  9. Takashi Daiho, Hiroshi Suzuki, Kazuo Yamasaki, Tomoyuki Saino, and Tohru Kanazawa.
       Mutations of Arg198 in Sarcoplasmic Reticulum Ca2+-ATPase Cause Inhibition of Hydrolysis of the Phosphoenzyme Intermediate Formed from Inorganic Phosphate.
      FEBS Letters Vol. 444 (1), 54-58, 1999
10. Kazuo Yamasaki, Takashi Daiho, Tomoyuki Saino, and Tohru Kanazawa.
       Modification of Histidine 5 in Sarcoplasmic Reticulum Ca2+-ATPase by Dietyl Pyrocarbonate Causes Strong Inhibition of Formation of Phosphoenzyme Intermediate from
       Inorganic Phosphate. J. Biol. Chem. Vol.272 (49), 30627-30636, 1997
11. Tomoyuki Saino, Takashi Daiho, and Tohru Kanazawa.
       Modification of Arginine-198 in Sarcoplasmic Reticulum Ca2+-ATPase by 1,2-Cyclohexanedione Causes Inhibition of Formation of the Phosphoenzyme Intermediate from
       Inorganic Phosphate. J. Biol. Chem. Vol.272 (34), 21142-21150, 1997
12. Keisuke Kimura, Hiroshi Suzuki, Takashi Daiho, Kazuo Yamasaki, and Tohru Kanazawa.
       Identification of Arginyl Residues Located at the ATP Binding Site of Sarcoplasmic Reticulum Ca2+-ATPase. Modification with 1,2-Cyclohexanedione.
      J. Biol. Chem. Vol.271 (46), 28933-28941, 1996
13. Tohru Kanazawa, Hiroshi Suzuki, Takashi Daiho, and Kazuo Yamasaki.
       Fluorometric Study on Conformational Changes in the Catalytic Cycle of Sarcoplasmic Reticulum Ca2+-ATPase. Bioscience Reports Vol.15 (5), 317-326, 1995
14. Takashi Daiho and Tohru Kanazawa.
       Reduction of Disulfide Bonds in Sarcoplasmic Reticulum Ca2+-ATPase by Dithiothreitol Causes Inhibition of Phosphoenzyme Isomerization in Catalytic Cycle : This Reduction
       Requires Binding of Both Purine Nucleotide and Ca2+to Enzyme. J. Biol. Chem., Vol.269, 11060-11064 , 1994
15. Kazuo Yamasaki, Takashi Daiho, and Tohru Kanazawa.
       3'-O-(5-Fluoro-2,4-dinitrophenyl)-ATP Exclusively Labels Lys-492 at the Active Site of the Sarcoplasmic Reticulum Ca2+-ATPase.
      J. Biol. Chem., Vol.269, 4129-4134, 1994
16. Kazuo Yamasaki, Takashi Daiho, and Tohru Kanazawa.
       Labeling of Lysine 492 with Pyridoxal 5'-Phosphate in the Sarcoplasmic Reticulum Ca2+-ATPase : Lysine 492 Residue is Located Outside the Fluorescein
       5-Isothiocyanate-Binding Region in or near the ATP Binding Site. J. Biol. Chem., Vol.268, 20930-20936, 1993
17. Takashi Daiho, Tatsuya Kubota, and Tohru Kanazawa.
       Stoichiometry of Tight Binding of Magnesium and Fluoride to Phosphorylation and High-Affinity Binding of ATP, Vanadate, and Calcium in the Sarcoplasmic Reticulum
       Ca2+-ATPase. Biochemistry, Vol.32, 10021-10026, 1993
18. Tatsuya Kubota, Takashi Daiho, and Tohru Kanazawa.
       Quasi-irreversible Inactivation of the Sarcoplasmic Reticulum Ca2+-ATPase by Simultaneous Tight Binding of Magnesium and Fluoride to the Catalytic Site.
      Biochim. Biophys. Acta, Vol.1163, 131-143, 1993
19. Yamamoto, T., Daiho, T., and Takisawa, H.
       Reconstitution of Calcium Transport from Monomeric ATPase of Sarcoplasmic Reticulum.
      Perspectives of Biological Energy Transduction,(Mukohata, Y., Morales, M.F., and Fleischer, S.)   147-154, 1987
20. Daiho, T., Takisawa, H., and Yamamoto, T.
       Inhibition of hydrolysis of phosphorylated Ca2+,Mg2+-ATPase of the sarcoplasmic reticulum by Ca2+ inside and outside the vesicles.
      J. Biochem.(Tokyo) Vol.97(2), 643-653, 1985

 
 
 

ŽR@è@@˜a@¶
 

  1. Kazuo Yamasaki, Takashi Daiho, and Hiroshi Suzuki.
       Remarkable Stability of Solubilized and Delipidated Sarcoplasimc Reticulum Ca2+-ATPase with Tightly Bound Fluoride and Magnesium against Detergent-induced
       Denaturation. J. Biol. Chem. in press, 2002
  2. Stefania Danko, Kazuo Yamasaki, Takashi Daiho, Hiroshi Suzuki, and Chikashi Toyoshima.
       Organization of cytoplasmic domains of sarcoplasmic reticulum Ca2+-ATPase in E1P and E1ATP states: a limited proteolysis study.
      FEBS Letters, Vol.505, 129-135, 2001
  3. Takashi Daiho, Kazuo Yamasaki, Tomoyuki Saino, Mika Kamidochi, Katsuhiko Satoh, Hajime Iizuka, and Hiroshi Suzuki.
       Mutations of Either or both of Cys876 and Cys888 of Sarcoplasmic Reticulum Ca2+-ATPase Result in a Complete Loss of Ca2+ Transport Activity without a Loss of
       Ca2+-ATPase activity, J. Biol. Chem. Vol.276(35), 32771-32778, 2001
  4. Stefania Danko, Takashi Daiho, Kazuo Yamasaki, Mika Kamidochi, Hiroshi Suzuki, and Chikashi Toyoshima.
       ADP-insensitive phosphoenzyme intermediate of sarcoplasmic reticulum Ca2+-ATPase has a compact conformation resistant to proteinase K, V8 protease and trypsin.
      FEBS Letters, Vol. 498(2-3), 277-282, 2001
  5. Hiroshi Suzuki, Takashi Daiho, Kazuo Yamasaki, and Tohru Kanazawa.
       Only half of the Ca2+-ATPase molecules present in sarcoplasmic reticulum vesicles can be phosphorylated with ATP or Inorganic phosphate.
      Na/K-ATPase and Related ATPases.(K.Taniguchi and S.Kaya Eds.)Elsevier, North Holland, 381-388, 2000
  6. Takashi Daiho, Kazuo Yamasaki, Hiroshi Suzuki, Tomoyuki Saino, and Tohru Kanazawa.
       Deletions or specific substitutions of a few residents in the NH2-terminal Ala3-Thr9 region of sarcoprasmic reticulum Ca2+-ATPase cause inactivation and rapid degradation
       of the enzyme expressed in COS-1 cells. Na/K-ATPase and Related ATPases.(K.Taniguchi and S.Kaya Eds.)Elsevier, North Holland, 293-296, 2000
  7. Kazuo Yamasaki, Takashi Daiho, Hiroshi Suzuki, Tomoyuki Saino, and Tohru Kanazawa.
       Mutations of arginine-198 in sarcoplasmic reticulum Ca2+ATPase cause inhibition of hydrolysis of the phosphoenzyme intermediate formed from inorganic phosphate.
      Na/K-ATPase and Related ATPases.(K.Taniguchi and S.Kaya Eds.)Elsevier, North Holland, 297-300, 2000
  8. Takashi Daiho, Kazuo Yamasaki, Hiroshi Suzuki, Tomoyuki Saino, and Tohru Kanazawa.
       Deletions or Specific Substitutions of a Few Residues in the NH2-terminal Region (Ala3-Thr9) of Sarcoplasmic Reticulum Ca2+-ATPase Cause Inactivation and Rapid
       Degradation of the Enzyme Expressed in COS-1 Cells. J. Biol. Chem. Vol.274 (34), 23910-23915, 1999
  9. Takashi Daiho, Hiroshi Suzuki, Kazuo Yamasaki, Tomoyuki Saino, and Tohru Kanazawa.
       Mutations of Arg198 in Sarcoplasmic Reticulum Ca2+-ATPase Cause Inhibition of Hydrolysis of the Phosphoenzyme Intermediate Formed from Inorganic Phosphate.
      FEBS Letters Vol. 444 (1), 54-58, 1999
10. Kazuo Yamasaki, Takashi Daiho, Tomoyuki Saino, and Tohru Kanazawa.
       Modification of Histidine 5 in Sarcoplasmic Reticulum Ca2+-ATPase by Dietyl Pyrocarbonate Causes Strong Inhibition of Formation of Phosphoenzyme Intermediate from
       Inorganic Phosphate. J. Biol. Chem. Vol.272 (49), 30627-30636, 1997
11. Keisuke Kimura, Hiroshi Suzuki, Takashi Daiho, Kazuo Yamasaki, and Tohru Kanazawa.
       Identification of Arginyl Residues Located at the ATP Binding Site of Sarcoplasmic Reticulum Ca2+-ATPase. Modification with 1,2-Cyclohexanedione.
      J. Biol. Chem. Vol.271 (46), 28933-28941, 1996

 
 
 

‰Á@“¡@@‘@•c

  1. Tomoko Tazawa, Sanae Kato, Tsuyoshi Kato, and Kunihiko Konnno.

       Role of neck region in the thermal aggregation of myosin. J.Agric.Food.Chem. Vol.50, 196-202, 2002
  2. Kunihiko Konno, Takeshi Yamamoto, Masayuki Takahashi,  and Sanae Kato.
       Early structural changes in myosin rod upon heating of carp myofibrils. J.Agric.Food.Chem. Vol.48, 4905-4909, 2000
  3. Sanae Kato and Isao Yumoto.
       Detection of the Na+-translocating NADH-quinone reductase in marine bacteria using a PCR technique. Canadian Journal of Microbiology, Vol.46, 325-332, 2000
  4. Sanae Kato and Kunihiko Konno. Filament Formation of Carboxyl- and Amino-Group-Modified Carp Myosin Rod. Fisheries Science, Vol.66, 124-129,2000
  5. Sanae Kato, Hiroaki Koseki, and Kunihiko Konno. Oligomerization of carp myosin which retains its ATPase activity. Fisheries Science, Vol.62(6), 985-989,1996
  6. Sanae Kato and Kunihiko Konno. Substructure of tilapia myosin rod and its filament forming ability. Fisheries Science, Vol.62(3), 439-443,1996
  7. Sanae Kato and Kunihiko Konno. Isolation of carp myosin rod and its structural stability. “ú–{…ŽYŠw‰ïŽA59ŠªA539-544A1993
  8. ¬ŠÖG–¾A‰Á“¡‘•cA¡–ì‹vm•FBƒRƒC‹ØŒ´üˆÛ‰Á”M•Ï«‚Ì•qŠ´‚ÈŽw•W‚Æ‚µ‚Ẵ~ƒIƒVƒ“’Šo«‚̒ቺA“ú–{…ŽYŠw‰ïŽA59ŠªA515-518A1993

  9. Sanae Kato and Kunihiko Konno. Filament-forming domain of carp dorsal myosin rod. J. Biochem. Vol.113, 43-47,1993

10. ¡–ì‹vm•FA‰Á“¡‘•cBƒRƒC‹ØŒ´üˆÛ‚ðo”­Þ—¿‚Æ‚µ‚½ƒ~ƒIƒVƒ“ƒTƒuƒtƒ‰ƒOƒƒ“ƒg-1‚̊ȕւȒ²»–@A“ú–{…ŽYŠw‰ïŽA56ŠªA1885-1890A1990

11. ‰Á“¡‘•cA¡–ì‹vm•FBƒLƒ‚ƒgƒŠƒvƒVƒ“Á‰»«‚©‚ç‚Ý‚½ƒRƒCƒ~ƒIƒVƒ“‚Ì\‘¢“Á«A“ú–{…ŽYŠw‰ïŽA56ŠªA1877-1880A1990