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本文引用的文献

1
Conserved S/T Residues of the Human Chaperone DNAJB6 Are Required for Effective Inhibition of Aβ42 Amyloid Fibril Formation.人类伴侣蛋白DNAJB6的保守丝氨酸/苏氨酸残基是有效抑制Aβ42淀粉样纤维形成所必需的。
Biochemistry. 2018 Aug 14;57(32):4891-4902. doi: 10.1021/acs.biochem.8b00353. Epub 2018 Jul 30.
2
Mapping interactions with the chaperone network reveals factors that protect against tau aggregation.绘制与伴侣蛋白网络的相互作用图谱揭示了防止 tau 聚集的因素。
Nat Struct Mol Biol. 2018 May;25(5):384-393. doi: 10.1038/s41594-018-0057-1. Epub 2018 Apr 30.
3
Chaperone-Mediated Sec61 Channel Gating during ER Import of Small Precursor Proteins Overcomes Sec61 Inhibitor-Reinforced Energy Barrier.伴侣蛋白介导的 Sec61 通道门控在小分子前体蛋白的内质网导入过程中克服了 Sec61 抑制剂增强的能量障碍。
Cell Rep. 2018 May 1;23(5):1373-1386. doi: 10.1016/j.celrep.2018.03.122.
4
Structural modelling of the DNAJB6 oligomeric chaperone shows a peptide-binding cleft lined with conserved S/T-residues at the dimer interface.对 DNAJB6 寡聚伴侣的结构建模表明,二聚体界面处的保守 S/T 残基排列在肽结合裂隙的边缘。
Sci Rep. 2018 Mar 26;8(1):5199. doi: 10.1038/s41598-018-23035-9.
5
Protein Disaggregation in Multicellular Organisms.多细胞生物中的蛋白去聚集
Trends Biochem Sci. 2018 Apr;43(4):285-300. doi: 10.1016/j.tibs.2018.02.003. Epub 2018 Feb 28.
6
High-throughput screen for inhibitors of protein-protein interactions in a reconstituted heat shock protein 70 (Hsp70) complex.高通量筛选重组热休克蛋白 70(Hsp70)复合物中蛋白质-蛋白质相互作用抑制剂。
J Biol Chem. 2018 Mar 16;293(11):4014-4025. doi: 10.1074/jbc.RA117.001575. Epub 2018 Feb 2.
7
Chaperoning the guardian of the genome. The two-faced role of molecular chaperones in p53 tumor suppressor action.分子伴侣监管基因组守护者:p53 肿瘤抑制因子作用的双重角色
Biochim Biophys Acta Rev Cancer. 2018 Apr;1869(2):161-174. doi: 10.1016/j.bbcan.2017.12.004. Epub 2018 Jan 31.
8
Hsp70 at the membrane: driving protein translocation.膜上的 HSP70:驱动蛋白易位。
BMC Biol. 2018 Jan 17;16(1):11. doi: 10.1186/s12915-017-0474-3.
9
Bap (Sil1) regulates the molecular chaperone BiP by coupling release of nucleotide and substrate.Bap (Sil1) 通过偶联核苷酸和底物的释放来调节分子伴侣 BiP。
Nat Struct Mol Biol. 2018 Jan;25(1):90-100. doi: 10.1038/s41594-017-0012-6. Epub 2018 Jan 1.
10
Nucleotide exchange factors Fes1 and HspBP1 mimic substrate to release misfolded proteins from Hsp70.核苷酸交换因子 Fes1 和 HspBP1 模拟底物,将错误折叠的蛋白质从 Hsp70 中释放出来。
Nat Struct Mol Biol. 2018 Jan;25(1):83-89. doi: 10.1038/s41594-017-0008-2. Epub 2018 Jan 1.

J 结构域蛋白的功能、进化和结构。

Function, evolution, and structure of J-domain proteins.

机构信息

Department of Cell Biology, University Medical Center Groningen, University of Groningen, Groningen, The Netherlands.

Department of Molecular Biosciences, The Wenner-Gren Institute, Stockholm University, SE-106 91, Stockholm, Sweden.

出版信息

Cell Stress Chaperones. 2019 Jan;24(1):7-15. doi: 10.1007/s12192-018-0948-4. Epub 2018 Nov 26.

DOI:10.1007/s12192-018-0948-4
PMID:30478692
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC6363617/
Abstract

Hsp70 chaperone systems are very versatile machines present in nearly all living organisms and in nearly all intracellular compartments. They function in many fundamental processes through their facilitation of protein (re)folding, trafficking, remodeling, disaggregation, and degradation. Hsp70 machines are regulated by co-chaperones. J-domain containing proteins (JDPs) are the largest family of Hsp70 co-chaperones and play a determining role functionally specifying and directing Hsp70 functions. Many features of JDPs are not understood; however, a number of JDP experts gathered at a recent CSSI-sponsored workshop in Gdansk (Poland) to discuss various aspects of J-domain protein function, evolution, and structure. In this report, we present the main findings and the consensus reached to help direct future developments in the field of Hsp70 research.

摘要

Hsp70 伴侣系统是非常通用的机器,存在于几乎所有的生物体内和几乎所有的细胞内隔室中。它们通过促进蛋白质(再)折叠、运输、重塑、解聚和降解,在许多基本过程中发挥作用。Hsp70 机器受共伴侣的调节。含 J 结构域的蛋白质(JDPs)是 Hsp70 共伴侣中最大的家族,在功能上起着决定作用,指定和指导 Hsp70 的功能。许多 JDP 的特征尚未被理解;然而,一些 JDP 专家在最近在波兰格但斯克举行的由 CSSI 赞助的研讨会上聚集在一起,讨论 J 结构域蛋白功能、进化和结构的各个方面。在本报告中,我们提出了主要的发现和达成的共识,以帮助指导 Hsp70 研究领域的未来发展。