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本文引用的文献

1
The binding mode of ATP revealed by the solution structure of the N-domain of human ATP7A.人源 ATP7A N 结构域溶液结构揭示的 ATP 结合模式。
J Biol Chem. 2010 Jan 22;285(4):2537-44. doi: 10.1074/jbc.M109.054262. Epub 2009 Nov 16.
2
Copper redistribution in Atox1-deficient mouse fibroblast cells.铜在 Atox1 缺陷型小鼠成纤维细胞中的重新分布。
J Biol Inorg Chem. 2010 Jan;15(1):99-105. doi: 10.1007/s00775-009-0598-1. Epub 2009 Oct 29.
3
Lysine-60 in copper chaperone Atox1 plays an essential role in adduct formation with a target Wilson disease domain.铜伴侣蛋白 Atox1 中的赖氨酸-60 在与靶威尔逊病结构域形成加合物方面发挥着重要作用。
J Am Chem Soc. 2009 Nov 18;131(45):16371-3. doi: 10.1021/ja9058266.
4
Mutant SOD1 in neuronal mitochondria causes toxicity and mitochondrial dynamics abnormalities.神经元线粒体中的突变 SOD1 导致毒性和线粒体动力学异常。
Hum Mol Genet. 2009 Dec 1;18(23):4552-64. doi: 10.1093/hmg/ddp421. Epub 2009 Sep 24.
5
Response of gram-positive bacteria to copper stress.革兰氏阳性菌对铜胁迫的响应。
J Biol Inorg Chem. 2010 Jan;15(1):3-14. doi: 10.1007/s00775-009-0588-3. Epub 2009 Sep 23.
6
Solution structures of the actuator domain of ATP7A and ATP7B, the Menkes and Wilson disease proteins.ATP7A和ATP7B(门克斯病和威尔逊病相关蛋白)的调控结构域的溶液结构
Biochemistry. 2009 Aug 25;48(33):7849-55. doi: 10.1021/bi901003k.
7
NMR structural analysis of the soluble domain of ZiaA-ATPase and the basis of selective interactions with copper metallochaperone Atx1.ZiaA-ATPase 可溶性结构域的 NMR 结构分析及其与铜金属伴侣蛋白 Atx1 选择性相互作用的基础。
J Biol Inorg Chem. 2010 Jan;15(1):87-98. doi: 10.1007/s00775-009-0568-7. Epub 2009 Jul 16.
8
The right to choose: multiple pathways for activating copper,zinc superoxide dismutase.选择权:激活铜锌超氧化物歧化酶的多种途径
J Biol Chem. 2009 Sep 11;284(37):24679-83. doi: 10.1074/jbc.R109.040410. Epub 2009 Jul 8.
9
Mitochondrial ATP-independent chaperones.
IUBMB Life. 2009 Sep;61(9):909-14. doi: 10.1002/iub.235.
10
Phosphorylation regulates copper-responsive trafficking of the Menkes copper transporting P-type ATPase.磷酸化调节 Menkes 铜转运 P 型 ATP 酶的铜反应性转运。
Int J Biochem Cell Biol. 2009 Dec;41(12):2403-12. doi: 10.1016/j.biocel.2009.06.008. Epub 2009 Jul 2.

细胞内铜分布:一种基于机制的系统生物学方法。

Cellular copper distribution: a mechanistic systems biology approach.

机构信息

Department of Chemistry, Magnetic Resonance Center CERM, University of Florence, Via Luigi Sacconi 6, Sesto Fiorentino, Florence, Italy.

出版信息

Cell Mol Life Sci. 2010 Aug;67(15):2563-89. doi: 10.1007/s00018-010-0330-x. Epub 2010 Mar 24.

DOI:10.1007/s00018-010-0330-x
PMID:20333435
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC11115773/
Abstract

Copper is an essential but potentially harmful trace element required in many enzymatic processes involving redox chemistry. Cellular copper homeostasis in mammals is predominantly maintained by regulating copper transport through the copper import CTR proteins and the copper exporters ATP7A and ATP7B. Once copper is imported into the cell, several pathways involving a number of copper proteins are responsible for trafficking it specifically where it is required for cellular life, thus avoiding the release of harmful free copper ions. In this study we review recent progress made in understanding the molecular mechanisms of copper transport in cells by analyzing structural features of copper proteins, their mode of interaction, and their thermodynamic and kinetic parameters, thus contributing to systems biology of copper within the cell.

摘要

铜是一种必需的但潜在有害的微量元素,在许多涉及氧化还原化学的酶促过程中都需要它。哺乳动物的细胞内铜稳态主要通过调节铜的转运来维持,这个过程涉及铜输入 CTR 蛋白和铜输出 ATP7A 和 ATP7B。一旦铜被导入细胞,涉及许多铜蛋白的几种途径负责将其专门运输到细胞生命所需的地方,从而避免释放有害的游离铜离子。在这项研究中,我们通过分析铜蛋白的结构特征、它们的相互作用模式以及它们的热力学和动力学参数,来综述细胞内铜转运的分子机制的最新进展,从而为细胞内铜的系统生物学做出贡献。