Publications related to GroEL | EPFL Graph Search

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.

GroEL

Graph Chatbot

Chat with Graph Search

Stable -Synuclein Oligomers Strongly Inhibit Chaperone Activity of the Hsp70 System by Weak Interactions with J-domain Co-chaperones

Structure and function of the molecular chaperone Hsp104 from yeast

Hsp104 targets multiple intermediates on the amyloid pathway and suppresses the seeding capacity of Abeta fibrils and protofibrils

Complementing structural information of modular proteins with small angle neutron scattering and contrast variation

Active solubilization and refolding of stable protein aggregates by cooperative unfolding action of individual hsp70 chaperones

Increased stability upon heptamerization of the pore-forming toxin aerolysin

Temperature-dependent NMR and CD spectra of β-peptides. On the thermal stability of β-peptide helixes. Is the folding process of β-peptides non-cooperative?

The staphylococcal alpha-toxin pore has a flexible conformation

The nucleation of monomeric parallel beta-sheet-like structures and their self-assembly in aqueous solution

Conformational changes in aerolysin during the transition from the water-soluble protoxin to the membrane channel