Structural dynamics of IRE1 and its interaction with unfolded peptides
Elena Spinetti, Grzegorz Ścibisz, Gülsün Elif Karagöz, Roberto Covino, Qiang Cui, Elena Spinetti, Grzegorz Ścibisz, Gülsün Elif Karagöz, Roberto Covino · 2026
Read Structural dynamics of IRE1 and its interaction with unfolded peptides by Elena Spinetti, Grzegorz Ścibisz, Gülsün Elif Karagöz, Roberto Covino, Qiang Cui, Elena Spinetti, Grzegorz Ścibisz, Gülsün Elif Karagöz, Roberto Covino (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/PMC13395458.txt.
Description
Elena Spinetti and co-authors model, in 2026, how a cell stress sensor grabs unfolded proteins. The sensor, IRE1, sits in the cell's folding workshop and fires a rescue program under strain. No clear picture showed it touching unfolded chains directly. The team ran long atom-level simulations of the sensor's sensing part.
The sensor's head did grip unfolded protein bits in two pockets at its centre. Those grips could steady larger sensor clusters that switch the program on. A helper named BiP was also shown blocking the cluster face, which keeps the sensor quiet in calm times. The model settles clashing past claims, the authors say. It maps the first step of the stress alarm.
Catalog record
| CREATOR | Elena Spinetti, Grzegorz Ścibisz, Gülsün Elif Karagöz, Roberto Covino, Qiang Cui, Elena Spinetti, Grzegorz Ścibisz, Gülsün Elif Karagöz, Roberto Covino |
|---|---|
| YEAR | 2026 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 152486 |
| LICENSE | https://creativecommons.org/licenses/by/4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |