PreprintAll rights reservedbioRxiv
A conformational switch governs the dual role of liquid-liquid phase separation in amyloid fibrillization
- 1The University of Sydney
Related
- Cooperative IDR-folded domain interplay governs HP1α phase separation and underlies biphasic regulation by pathogenic poly-PR
- Conformational Heterogeneity and Local Electronic Structure in Wild-Type and Arctic Amyloid-Β42
- The Abundance of Phenylalanine in the DNAJB6b Linker Governs Its Role in Amyloid Suppression
- Single-Chain Conformational Fluctuation Regulates Phase Separation of Intrinsically Disordered Proteins.
- Phase separation reshapes the conformational energy landscape of a chaperone to prime its activity
BibTeX
@misc{li2026conformational,
title = {{A conformational switch governs the dual role of liquid-liquid phase separation in amyloid fibrillization}},
author = {T. Li and B. Williams and Q. Han and M. Steain and M. Sunde and Y. Shen},
howpublished = {bioRxiv},
year = {2026},
month = sep,
doi = {10.64898/2026.09.12.751119},
url = {https://www.biorxiv.org/content/10.64898/2026.09.12.751119v1},
}
RIS
TY - UNPB
TI - A conformational switch governs the dual role of liquid-liquid phase separation in amyloid fibrillization
AU - T. Li
AU - B. Williams
AU - Q. Han
AU - M. Steain
AU - M. Sunde
AU - Y. Shen
PY - 2026
DA - 2026/09/12
PB - bioRxiv
DO - 10.64898/2026.09.12.751119
UR - https://www.biorxiv.org/content/10.64898/2026.09.12.751119v1
ER -