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

机译：肌浆网Ca2 + -ATPase中Arg198的突变导致抑制无机磷酸盐形成的磷酸酶中间体的水解

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Daiho Takashi; Suzuki Hiroshi; Yamasaki Kazuo; Saino Tomoyuki; Kanazawa Tohru;
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年度 1999
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1. Mutations of Arg198 in sarcoplasmic reticulum Ca2+‐ATPase cause inhibition of hydrolysis of the phosphoenzyme intermediate formed from inorganic phosphate [J] . Daiho Takashi, Kanazawa Tohru, Saino Tomoyuki, FEBS Letters . 1999,第1期

机译：肌浆网Ca2 + -ATPase中Arg198的突变会抑制无机磷酸盐形成的磷酸酶中间体的水解
2. Formation of the ADP-insensitive phosphoenzyme intermediate in the sarcoplasmic reticulum Ca2+-ATPase of which both Cys344 and Cys364 are modified by N-ethylmaleimide. [J] . Suzuki H, Kanazawa T Biochemistry . 1999,第2期

机译：在肌浆网Ca2 + -ATPase中形成ADP不敏感的磷酸酶中间体，其Cys344和Cys364均被N-乙基马来酰亚胺修饰。
3. Protonation and hydrogen bonding of Ca2+ site residues in the E2P phosphoenzyme intermediate of sarcoplasmic reticulum Ca2+-ATPase studied by a combination of infrared Spectroscopy and electrostatic calculations [J] . Andersson J, Hauser K, Karjalainen EL, Biophysical Journal . 2008,第2期

机译：结合红外光谱和静电计算研究的肌浆网Ca2 + -ATPase E2P磷酸酶中间体中Ca2 +位残基的质子化和氢键结合
4. Measurement of conformational states of Ca2+-ATPase in sarcoplasmic reticulum using phosphorescence anisotropy [C] . Liqun Yang, A.Rubtsov Moscow State Univ. Moscow Russia, Daniel McStay, Conference on microscopy, holography, and interferometry in biomedicine . 1994

机译：使用磷光各向异性测量Ca2 + -ATP酶的构象状态
5. Phosphorylated Intermediates of Ca＾<2+> ,Mg＾<2+> -Dependent ATPase of the Sarcoplasmic Reticulum from Skeletal Muscle [D] . Takisawa, Haruhiko -1

机译：骨骼肌肌质网Ca ＾ 2 +，Mg ＾ 2 +-依赖性ATP酶的磷酸化中间体
6. Protonation and Hydrogen Bonding of Ca2+ Site Residues in the E2P Phosphoenzyme Intermediate of Sarcoplasmic Reticulum Ca2+-ATPase Studied by a Combination of Infrared Spectroscopy and Electrostatic Calculations [O] . Julia Andersson, Karin Hauser, Eeva-Liisa Karjalainen, 2008

机译：结合红外光谱法和静电学计算研究肌浆网Ca2 + -ATPase E2P磷酸酶中间体中Ca2 +位点残基的质子化和氢键结合
7. ADP-insensitive phosphoenzyme intermediate of sarcoplasmic reticulum Ca2+-ATPase has a compact conformation resistant to proteinase K, V8 protease and trypsin [O] . Danko Stefania, Daiho Takashi, Yamasaki Kazuo, 2001

机译：肌浆网Ca2 + -ATPase的ADP不敏感磷酸酶中间体具有紧凑的构象，可抵抗蛋白酶K，V8蛋白酶和胰蛋白酶
8. Exp 31 P NMR Studies of Oriented Multilayers Formed from Isolated Sarcoplasmic Reticulum and Reconstituted Sarcoplasmic Reticulum: Evidence That Boundary-Layer Phospholipid Is Not Immobilized [R] . McLaughlin, A. C., Herbette, L., Blasie, J. K., 1981

机译：从分离的肌浆网和重建的肌浆网形成的定向多层膜的Exp 31 p NmR研究：边界层磷脂未固定的证据

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

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