Hsp70 diversification and repurposing across the tree of life: Lessons from the evolutionary and mechanistic trajectory of the Hsp70–Hsp110 chaperone system
Pierre Goloubinoff, Paolo De Los Rios, Mathieu E Rebeaud · 2026
Read Hsp70 diversification and repurposing across the tree of life: Lessons from the evolutionary and mechanistic trajectory of the Hsp70–Hsp110 chaperone system by Pierre Goloubinoff, Paolo De Los Rios, Mathieu E Rebeaud (2026) in the Tower of Babel, a free online library of public-domain works preserved in clean, searchable text. No sign-up. The full text is served as a plain-text file at a predictable URL, where text is present: https://antarctic-labs.com/tower-of-babel/pmc-13580251.txt.
Description
A peer-reviewed research article from Europe PMC (2026). The 70 kDa Heat Shock Proteins (Hsp70s) are molecular chaperones ubiquitous in most free‐living bacteria and archaea, and in the cytosol and ATP‐containing organelles of eukaryotic cells, where they act as ATP‐fueled nanomachines that unfold, remodel, and translocate polypeptides. In bacteria, Hsp70 (DnaK) operates with the J‐domain cochaperone DnaJ and the nucleotide exchange factor (NEF) GrpE, which accelerates ADP release and ATP rebinding.
Catalog record
| CREATOR | Pierre Goloubinoff, Paolo De Los Rios, Mathieu E Rebeaud |
|---|---|
| YEAR | 2026 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 37 KB |
| VERSION | 1.0 |
| LICENSE | CC BY 4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |