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肌浆网蛋白质中的离子通道

Ion pathways in proteins of the sarcoplasmic reticulum.

作者信息

MacLennan D H, Reithmeier R A, Shoshan V, Campbell K P, LeBel D, Herrmann T R, Shamoo A E

出版信息

Ann N Y Acad Sci. 1980;358:138-48. doi: 10.1111/j.1749-6632.1980.tb15392.x.

DOI:10.1111/j.1749-6632.1980.tb15392.x
PMID:6259987
Abstract

In summary, we have begun to characterize three different ion pathways in the sarcoplasmic reticulum. Ca2+-ionophoric activity has been traced to a 13,000-dalton CNBr fragment localized at the amino terminus of the ATPase molecule... The pathway involved in Ca2+ release can be distinguished from the pathway involved in Ca2+ uptake by its insensitivity to quercetin. An anion pathway is sensitive to DIDS and appears to be localized in the ATPase molecule

摘要

总之,我们已开始对肌浆网中的三种不同离子通道进行表征。钙离子载体活性已追溯至位于ATP酶分子氨基末端的一个13000道尔顿的溴化氰片段……参与钙离子释放的通道可因其对槲皮素不敏感而与参与钙离子摄取的通道区分开来。一种阴离子通道对二异丁基氨磺酰苯甲酸盐(DIDS)敏感,且似乎位于ATP酶分子中

相似文献

1
Ion pathways in proteins of the sarcoplasmic reticulum.肌浆网蛋白质中的离子通道
Ann N Y Acad Sci. 1980;358:138-48. doi: 10.1111/j.1749-6632.1980.tb15392.x.
2
The sarcoplasmic reticulum Ca2+-ATPase.肌浆网Ca2+ -ATP酶
Mol Cell Biochem. 1982 Feb 5;42(2):83-107. doi: 10.1007/BF00222696.
3
The pH dependence of the Ca2+, Mg2+-ATPase of sarcoplasmic reticulum: evidence that the Ca2+ translocator bears a doubly negative charge.肌浆网Ca2+、Mg2+-ATP酶的pH依赖性:Ca2+转运体带有双负电荷的证据。
J Membr Biol. 1983;74(1):25-40. doi: 10.1007/BF01870592.
4
Calcium transport and release by sarcoplasmic reticulum: a mini-review.
Soc Gen Physiol Ser. 1979;33:61-75.
5
[Interaction between free fatty acids and Ca2+-dependent ATPase from sarcoplasmic reticulum membranes].[游离脂肪酸与肌浆网膜上钙依赖性ATP酶之间的相互作用]
Biokhimiia. 1981 May;46(5):809-24.
6
[Mechanisms of the regulation and integration of ion transport across membranes].[跨膜离子转运的调节与整合机制]
Nauchnye Doki Vyss Shkoly Biol Nauki. 1982(1):5-16.
7
Structural relationship between the calcium- and magnesium-transporting ATPase of sarcoplasmic reticulum and the membrane.
Ann N Y Acad Sci. 1980;358:149-58. doi: 10.1111/j.1749-6632.1980.tb15393.x.
8
Interaction of chemical probes with sarcoplasmic reticulum membranes.化学探针与肌浆网膜的相互作用。
Biochim Biophys Acta. 1980 Oct 2;601(3):620-9. doi: 10.1016/0005-2736(80)90563-5.
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[Ca2+-dependent ATPases of the sarcoplasmic reticulum of skeletal and cardiac muscles and their ion-transporting fragments].[骨骼肌和心肌肌浆网的钙依赖性ATP酶及其离子转运片段]
Biull Vsesoiuznogo Kardiol Nauchn Tsentra AMN SSSR. 1981;4(2):7-15.
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Studies of Ca2+ release from sarcoplasmic reticulum.
Ann N Y Acad Sci. 1982;402:470-7. doi: 10.1111/j.1749-6632.1982.tb25769.x.

引用本文的文献

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Sarcolipin alters SERCA1a interdomain communication by impairing binding of both calcium and ATP.肌联蛋白通过破坏钙和 ATP 的结合来改变 SERCA1a 结构域间的通讯。
Sci Rep. 2021 Jan 15;11(1):1641. doi: 10.1038/s41598-021-81061-6.
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Phospholamban and sarcolipin: Are they functionally redundant or distinct regulators of the Sarco(Endo)Plasmic Reticulum Calcium ATPase?受磷蛋白和肌浆网脂质蛋白:它们是肌浆(内质)网钙ATP酶功能上的冗余调节因子还是不同的调节因子?
J Mol Cell Cardiol. 2016 Feb;91:81-91. doi: 10.1016/j.yjmcc.2015.12.030. Epub 2015 Dec 29.
3
Calcium Uptake in Crude Tissue Preparation.
粗组织制剂中的钙摄取
Methods Mol Biol. 2016;1377:161-70. doi: 10.1007/978-1-4939-3179-8_16.
4
Sarcolipin uncouples hydrolysis of ATP from accumulation of Ca2+ by the Ca2+-ATPase of skeletal-muscle sarcoplasmic reticulum.肌浆球蛋白可使骨骼肌肌浆网中Ca2+-ATP酶将ATP水解与Ca2+蓄积的过程解偶联。
Biochem J. 2002 Jan 15;361(Pt 2):277-86. doi: 10.1042/0264-6021:3610277.
5
Monovalent ion and calcium ion fluxes in sarcoplasmic reticulum.肌浆网中的单价离子和钙离子通量
Mol Cell Biochem. 1983;55(1):65-82. doi: 10.1007/BF00229243.
6
Critical effects from lipid-protein interaction in membranes. II. Interpretation of experimental results.膜中脂蛋白相互作用的关键效应。II. 实验结果解读
Biophys J. 1981 Nov;36(2):347-57. doi: 10.1016/S0006-3495(81)84736-4.
7
A proton gradient controls a calcium-release channel in sarcoplasmic reticulum.质子梯度控制肌浆网中的钙释放通道。
Proc Natl Acad Sci U S A. 1981 Aug;78(8):4828-32. doi: 10.1073/pnas.78.8.4828.
8
Energy coupling to ATP synthesis by the proton-translocating ATPase.质子转运ATP酶将能量与ATP合成相偶联。
J Membr Biol. 1982;67(1):1-12. doi: 10.1007/BF01868643.