Evaluation of competing J domain:Hsp70 complex models in light of existing mutational and NMR data.
作者信息
Sousa Rui, Jiang Jianwen, Lafer Eileen M, Hinck Andrew P, Wang Liping, Taylor Alexander B, Maes E Guy
出版信息
Proc Natl Acad Sci U S A. 2012 Mar 27;109(13):E734; author reply E735. doi: 10.1073/pnas.1120597109. Epub 2012 Mar 7.
Abstract
摘要
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本文引用的文献
1
Heat shock protein 70 kDa chaperone/DnaJ cochaperone complex employs an unusual dynamic interface.热休克蛋白 70 kDa 伴侣蛋白/DnaJ 共伴侣复合物采用一种不寻常的动态界面。
Proc Natl Acad Sci U S A. 2011 Nov 22;108(47):18966-71. doi: 10.1073/pnas.1111220108. Epub 2011 Nov 7.
2
Structural basis of J cochaperone binding and regulation of Hsp70.J 辅助伴侣蛋白与 Hsp70 结合及调控的结构基础
Mol Cell. 2007 Nov 9;28(3):422-33. doi: 10.1016/j.molcel.2007.08.022.
3
Hsc70 contacts helix III of the J domain from polyomavirus T antigens: addressing a dilemma in the chaperone hypothesis of how they release E2F from pRb.热休克蛋白70（Hsc70）与多瘤病毒T抗原J结构域的螺旋III相互作用：解决伴侣蛋白假说中关于它们如何从视网膜母细胞瘤蛋白（pRb）释放E2F这一困境。
Biochemistry. 2006 Jun 6;45(22):6917-29. doi: 10.1021/bi060411d.
4
Role of the J-domain in the cooperation of Hsp40 with Hsp70.J结构域在热休克蛋白40（Hsp40）与热休克蛋白70（Hsp70）协同作用中的作用。
Proc Natl Acad Sci U S A. 1998 May 26;95(11):6108-13. doi: 10.1073/pnas.95.11.6108.
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