Publication

Large-Scale Conformational Transitions and Dimerization Are Encoded in the Amino-Acid Sequences of Hsp70 Chaperones

Related publications (34)

About
Privacy
Disclaimer

Graph Chatbot

Chat with Graph Search

Ask any question about EPFL courses, lectures, exercises, research, news, etc. or try the example questions below.

DISCLAIMER: The Graph Chatbot is not programmed to provide explicit or categorical answers to your questions. Rather, it transforms your questions into API requests that are distributed across the various IT services officially administered by EPFL. Its purpose is solely to collect and recommend relevant references to content that you can explore to help you answer your questions.

Large-Scale Conformational Transitions and Dimerization Are Encoded in the Amino-Acid Sequences of Hsp70 Chaperones

Graph Chatbot

Chat with Graph Search

Chaperones convert the energy from ATP into the nonequilibrium stabilization of native proteins

Three branches to rule them all? UPR signalling in response to chemically versus misfolded proteins-induced ER stress

Non equilibrium thermodynamics of protein organization

Molecular chaperones inject energy from ATP hydrolysis into the non-equilibrium stabilisation of native proteins

Evolution of an intricate J-protein network driving protein disaggregation in eukaryotes

Cytoplasmic Ubiquitin-Specific Protease 19 (USP19) Modulates Aggregation of Polyglutamine-Expanded Ataxin-3 and Huntingtin through the HSP90 Chaperone

Experimental Milestones in the Discovery of Molecular Chaperones as Polypeptide Unfolding Enzymes

Mathematical models and computational methods for the analysis of genome-scale protein synthesis

A Novel Pulse-Chase SILAC Strategy Measures Changes in Protein Decay and Synthesis Rates Induced by Perturbation of Proteostasis with an Hsp90 Inhibitor

Dynamic Impacts of the Inhibition of the Molecular Chaperone Hsp90 on the T-Cell Proteome Have Implications for Anti-Cancer Therapy