Dynamical Structures of Hsp70 and Hsp70-Hsp40 Complexes.
TLDR
The power of nuclear magnetic resonance spectroscopy is highlighted to untangle complex relationships behind molecular chaperones and their mechanism(s) of action.About:
This article is published in Structure.The article was published on 2016-07-06 and is currently open access. It has received 85 citations till now. The article focuses on the topics: Co-chaperone & Proteostasis.read more
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Methods to validate Hsp90 inhibitor specificity, to identify off-target effects, and to rethink approaches for further clinical development.
Len Neckers,Brian S. J. Blagg,Timothy A.J. Haystead,Jane B. Trepel,Luke Whitesell,Luke Whitesell,Didier Picard +6 more
TL;DR: F feasible approaches to achieve clinical efficacy and confidence in target specificity and mechanism of action are provided and additional considerations to improve the clinical efficacy of Hsp90 inhibitors in treating cancer and other diseases are discussed.
Journal ArticleDOI
Post-translational modifications of Hsp70 family proteins: Expanding the chaperone code
TL;DR: The history of the Hsp70 chaperones, its currently understood regulation and functions, and thoughts on what the future of research into the chaperone code may entail are discussed.
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Hsp70 molecular chaperones: multifunctional allosteric holding and unfolding machines.
Eugenia M. Clerico,Wenli Meng,Alexandra Pozhidaeva,Karishma Bhasne,Constantine Petridis,Lila M. Gierasch +5 more
TL;DR: Structural insights into the molecular mechanism of this allosterically regulated binding have emerged and provided deep insight into the deceptively simple Hsp70 molecular machine that is so widely harnessed by nature for diverse cellular functions.
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Structural and functional analysis of the Hsp70/Hsp40 chaperone system.
Qinglian Liu,Ce Liang,Lei Zhou +2 more
TL;DR: This review will focus on recent progress in understanding the molecular mechanism of the Hsp70s and Hsp40s chaperone system through structural and functional analysis.
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Modeling Hsp70/Hsp40 interaction by multi-scale molecular simulations and coevolutionary sequence analysis
Duccio Malinverni,Alfredo Jost Lopez,Paolo De Los Rios,Gerhard Hummer,Gerhard Hummer,Alessandro Barducci,Alessandro Barducci +6 more
TL;DR: An evolutionarily conserved interaction surface formed by helix II of the DnaJ J-domain and a structurally contiguous region of DnaK, involving lobe IIA of the nucleotide binding domain, the inter-domain linker, and the β-basket of the substrate binding domain is identified.
References
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Protein Misfolding, Functional Amyloid, and Human Disease
TL;DR: The relative importance of the common main-chain and side-chain interactions in determining the propensities of proteins to aggregate is discussed and some of the evidence that the oligomeric fibril precursors are the primary origins of pathological behavior is described.
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Protein folding and misfolding
TL;DR: The manner in which a newly synthesized chain of amino acids transforms itself into a perfectly folded protein depends both on the intrinsic properties of the amino-acid sequence and on multiple contributing influences from the crowded cellular milieu.
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Molecular Chaperones in the Cytosol: from Nascent Chain to Folded Protein
TL;DR: Understanding how the thousands of different proteins synthesized in a cell use this chaperone machinery has profound implications for biotechnology and medicine.
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Hsp70 chaperones: cellular functions and molecular mechanism.
Matthias P. Mayer,Bernd Bukau +1 more
TL;DR: This work has shown that for specific tasks the Hsp70 cycle is coupled to the action of other chaperones, such as Hsp90 and Hsp100, and this ATPase cycle is controlled by co-chaperones of the family of J-domain proteins, which target H Sp70s to their substrates, and by nucleotide exchange factors, which determine the lifetime of the HSp70-substrate complex.
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Dynamic personalities of proteins.
TL;DR: The dream is to 'watch' proteins in action in real time at atomic resolution, which requires addition of a fourth dimension, time, to structural biology so that the positions in space and time of all atoms in a protein can be described in detail.