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Structure-function relationships in the Ca(2+)-ATPase of sarcoplasmic reticulum studied by use of the substrate analogue CrATP and site-directed mutagenesis. Comparison with the Na+,K(+)-ATPase.

作者信息

Vilsen B

机构信息

Department of Physiology, University of Aarhus, Denmark.

出版信息

Acta Physiol Scand Suppl. 1995;624:1-146.

PMID:7484166
Abstract
摘要

相似文献

1
Structure-function relationships in the Ca(2+)-ATPase of sarcoplasmic reticulum studied by use of the substrate analogue CrATP and site-directed mutagenesis. Comparison with the Na+,K(+)-ATPase.
Acta Physiol Scand Suppl. 1995;624:1-146.
2
Carboxy-terminal regions of the sarcoplasmic/endoplasmic reticulum Ca(2+)- and the Na+/K(+)-ATPases control their K+ sensitivity.肌浆网/内质网Ca(2+) -ATP酶和Na+/K(+) -ATP酶的羧基末端区域控制着它们对K+的敏感性。
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[Structure-function rearrangements in the calcium-activated ATPase of sarcoplasmic reticulum studied by its own fluorescence].
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Probing of membrane topology and stability of sarcoplasmic reticulum Ca(2+)-ATPase and Na+,K+ -ATPase with sequence-specific antibodies.利用序列特异性抗体探究肌浆网Ca(2+) -ATP酶和Na+,K+ -ATP酶的膜拓扑结构和稳定性
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钠钾ATP酶跨膜片段M1中甘氨酸94的突变会干扰E2P构象中钠和钾的结合。
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