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A novel aspect of calpain activation.

作者信息

Suzuki K, Sorimachi H

机构信息

Institute of Molecular and Cellular Biosciences, University of Tokyo, Japan.

出版信息

FEBS Lett. 1998 Aug 14;433(1-2):1-4. doi: 10.1016/s0014-5793(98)00856-4.

DOI:10.1016/s0014-5793(98)00856-4
PMID:9738920
Abstract

Calpain, a Ca2+-dependent biomodulator, alters the properties of substrate proteins by cleaving them at a limited number of specific sites. Recent studies of the structure-function relationship of calpain and X-ray analysis of its Ca2+-binding domain have revealed hitherto unknown features of the regulation of calpain activity. A novel dissociation/autolysis mechanism for the activation of calpain at the membrane is proposed, which incorporates recent findings from structure-function studies of calpain, and its implications are discussed.

摘要

相似文献

1
A novel aspect of calpain activation.
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2
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Autolytic transition of mu-calpain upon activation as resolved by antibodies distinguishing between the pre- and post-autolysis forms.
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Autolysis of calpain large subunit inducing irreversible dissociation of stoichiometric heterodimer of calpain.钙蛋白酶大亚基的自溶诱导钙蛋白酶化学计量异源二聚体的不可逆解离。
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Autolysis parallels activation of mu-calpain.自溶与微钙蛋白酶的激活同时发生。
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Mu-calpain binds to lipid bilayers via the exposed hydrophobic surface of its Ca2+-activated conformation.微钙蛋白酶通过其钙激活构象暴露的疏水表面与脂质双层结合。
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