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[Measurement of the distance between the sulfhydryl groups of class S1 myosin and its ATPase-active centers].

作者信息

Kulikov A V, Zhdanov R I, Charkviani G G, Eristavi T A

出版信息

Dokl Akad Nauk SSSR. 1979;248(4):982-4.

PMID:228917
Abstract
摘要

相似文献

1
[Measurement of the distance between the sulfhydryl groups of class S1 myosin and its ATPase-active centers].
Dokl Akad Nauk SSSR. 1979;248(4):982-4.
2
[Localization of metallo-acceptor centers specifically binding divalent cations in myosin molecules].[肌球蛋白分子中特异性结合二价阳离子的金属受体中心的定位]
Biofizika. 1981 Sep-Oct;26(5):931-2.
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Biokhimiia. 1989 Sep;54(9):1485-9.
4
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Local conformational change of myosin detected by tryptic digestibility. I. Monovalent and divalent ion-dependent conformation of the active site of myosin A ATPase.通过胰蛋白酶消化率检测的肌球蛋白局部构象变化。I. 肌球蛋白A ATP酶活性位点的单价和二价离子依赖性构象
J Biochem. 1974 Nov;76(5):1049-59.
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[Estimation of the distance between sulfhydryl groups S1 and specific binding centers for divalent metal ions in myosin].[肌球蛋白中巯基 S1 与二价金属离子特异性结合中心之间距离的估算]
Biofizika. 1981 Sep-Oct;26(5):920-3.
8
Alanine scanning mutagenesis of the switch I region in the ATPase site of Dictyostelium discoideum myosin II.盘基网柄菌肌球蛋白II的ATP酶位点中开关I区域的丙氨酸扫描诱变
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Opening of the myosin nucleotide triphosphate binding domain during the ATPase cycle.
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Biokhimiia. 1973 May-Jun;38(3):448-53.

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1
Unusual features of the Ca2+-ATPase activity of myosin from fast skeletal muscle of the frog: effect of actin and SH1 thiol group modification.
J Muscle Res Cell Motil. 1983 Apr;4(2):191-206. doi: 10.1007/BF00712030.