The multiple facets of the Hsp90 machine

The Ninth International Conference on the Hsp90 Chaperone Machine concluded in October 2018, in Leysin, Switzerland. The program highlighted findings in various areas, including integrated insights into the molecular mechanism of Hsp90, cochaperones, and clients’ structure and function.

[1]  W. Balch,et al.  Bridging Genomics to Phenomics at Atomic Resolution through Variation Spatial Profiling , 2018, Cell reports.

[2]  L. Pearl,et al.  The Structure of the R2TP Complex Defines a Platform for Recruiting Diverse Client Proteins to the HSP90 Molecular Chaperone System , 2017, Structure.

[3]  L. Neckers,et al.  Phosphorylation induced cochaperone unfolding promotes kinase recruitment and client class-specific Hsp90 phosphorylation , 2018, Nature Communications.

[4]  Paola Picotti,et al.  Measuring protein structural changes on a proteome-wide scale using limited proteolysis-coupled mass spectrometry , 2017, Nature Protocols.

[5]  D. Agard,et al.  How Hsp90 and Cdc37 Lubricate Kinase Molecular Switches. , 2017, Trends in biochemical sciences.

[6]  D. Picard,et al.  Luminescence resonance energy transfer between genetically encoded donor and acceptor for protein-protein interaction studies in the molecular chaperone HSP70/HSP90 complexes , 2018, Scientific Reports.

[7]  Wei Li,et al.  A fragment of secreted Hsp90α carries properties that enable it to accelerate effectively both acute and diabetic wound healing in mice. , 2011, The Journal of clinical investigation.

[8]  J. Hoskins,et al.  Functional and physical interaction between yeast Hsp90 and Hsp70 , 2018, Proceedings of the National Academy of Sciences.

[9]  Zihai Li,et al.  Structural and Functional Analysis of GRP94 in the Closed State Reveals an Essential Role for the Pre-N Domain and a Potential Client-Binding Site. , 2017, Cell reports.

[10]  Junpeng Deng,et al.  Structure-guided design of an Hsp90β N-terminal isoform-selective inhibitor , 2018, Nature Communications.

[11]  A. Edkins,et al.  LRP1 is required for novobiocin-mediated fibronectin turnover , 2018, Scientific Reports.

[12]  J. Buchner,et al.  The HSP90 chaperone machinery , 2017, Nature Reviews Molecular Cell Biology.

[13]  P. Verstreken,et al.  Hsp90 Mediates Membrane Deformation and Exosome Release. , 2018, Molecular cell.

[14]  V. Uversky,et al.  Human cyclophilin 40 unravels neurotoxic amyloids , 2017, PLoS biology.

[15]  M. Mollapour,et al.  The mTOR Independent Function of Tsc1 and FNIPs. , 2018, Trends in biochemical sciences.

[16]  E. Mandelkow,et al.  Structure and pro-toxic mechanism of the human Hsp90/PPIase/Tau complex , 2018, Nature Communications.

[17]  V. Méjean,et al.  Hsp90 Is Essential under Heat Stress in the Bacterium Shewanella oneidensis. , 2017, Cell reports.

[18]  T. Hugel,et al.  Using Three-color Single-molecule FRET to Study the Correlation of Protein Interactions. , 2018, Journal of Visualized Experiments.

[19]  B. Coulombe,et al.  The PAQosome, an R2TP-Based Chaperone for Quaternary Structure Formation. , 2018, Trends in biochemical sciences.

[20]  D. Westhead,et al.  A PQM-1-Mediated Response Triggers Transcellular Chaperone Signaling and Regulates Organismal Proteostasis , 2018, Cell reports.