Reply to Bernardi: The mitochondrial permeability transition pore and the ATP synthase.
作者信息
Walker John E, Carroll Joe, He Jiuya
机构信息
Medical Research Council Mitochondrial Biology Unit, University of Cambridge, Cambridge CB2 0XY, United Kingdom
Medical Research Council Mitochondrial Biology Unit, University of Cambridge, Cambridge CB2 0XY, United Kingdom.
出版信息
Proc Natl Acad Sci U S A. 2020 Feb 11;117(6):2745-2746. doi: 10.1073/pnas.1921409117. Epub 2020 Jan 28.
Abstract
摘要
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Mechanisms for Ca-dependent permeability transition in mitochondria.线粒体中钙依赖性通透性转变的机制。
Proc Natl Acad Sci U S A. 2020 Feb 11;117(6):2743-2744. doi: 10.1073/pnas.1921035117. Epub 2020 Jan 28.
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Persistence of the permeability transition pore in human mitochondria devoid of an assembled ATP synthase.人线粒体中缺乏组装的 ATP 合酶时通透性转换孔的持续存在。
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Permeability transition in human mitochondria persists in the absence of peripheral stalk subunits of ATP synthase.人线粒体通透性转换在 ATP 合酶外周 stalk 亚基缺失的情况下仍然存在。
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Persistence of the mitochondrial permeability transition in the absence of subunit c of human ATP synthase.人 ATP 合酶亚基 c 缺失时线粒体通透性转换的持续存在。
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Dimers of mitochondrial ATP synthase form the permeability transition pore.线粒体 ATP 合酶二聚体形成了通透性转换孔。
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Allosteric inhibition of the Ca2+-activated hydrophilic channel of the mitochondrial inner membrane by nucleotides.核苷酸对线粒体内膜Ca2+激活的亲水性通道的变构抑制作用。
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