Liquid–liquid phase separation in tumor biology

X Tong, R Tang, J Xu, W Wang, Y Zhao, X Yu… - Signal Transduction and …, 2022 - nature.com
Liquid–liquid phase separation (LLPS) is a novel principle for explaining the precise spatial
and temporal regulation in living cells. LLPS compartmentalizes proteins and nucleic acids …

Protein misfolding and amyloid nucleation through liquid–liquid phase separation

S Mukherjee, M Poudyal, K Dave, P Kadu… - Chemical Society …, 2024 - pubs.rsc.org
Liquid–liquid phase separation (LLPS) is an emerging phenomenon in cell physiology and
diseases. The weak multivalent interaction prerequisite for LLPS is believed to be facilitated …

CryoEM structure of the low-complexity domain of hnRNPA2 and its conversion to pathogenic amyloid

J Lu, Q Cao, MP Hughes, MR Sawaya… - Nature …, 2020 - nature.com
Abstract hnRNPA2 is a human ribonucleoprotein (RNP) involved in RNA metabolism. It
forms fibrils both under cellular stress and in mutated form in neurodegenerative conditions …

Molecular structure and interactions within amyloid-like fibrils formed by a low-complexity protein sequence from FUS

M Lee, U Ghosh, KR Thurber, M Kato… - Nature communications, 2020 - nature.com
Protein domains without the usual distribution of amino acids, called low complexity (LC)
domains, can be prone to self-assembly into amyloid-like fibrils. Self-assembly of LC …

Proteostatic imbalance and protein spreading in amyotrophic lateral sclerosis

ME Cicardi, L Marrone, M Azzouz, D Trotti - The EMBO journal, 2021 - embopress.org
Amyotrophic lateral sclerosis (ALS) is a fatal neurodegenerative disorder whose exact
causative mechanisms are still under intense investigation. Several lines of evidence …

Insights into the atomistic mechanisms of phosphorylation in disrupting liquid–liquid phase separation and aggregation of the FUS low-complexity domain

Z Lao, X Dong, X Liu, F Li, Y Chen… - Journal of Chemical …, 2022 - ACS Publications
Fused in sarcoma (FUS), a nuclear RNA binding protein, can not only undergo liquid–liquid
phase separation (LLPS) to form dynamic biomolecular condensates but also aggregate into …

Intrinsically disordered protein condensate-modified surface for mitigation of biofouling and foreign body response

R Chang, JL Chen, GY Zhang, Y Li… - Journal of the …, 2022 - ACS Publications
Mitigation of biofouling and the host's foreign body response (FBR) is a critical challenge
with biomedical implants. The surface coating with various anti-fouling materials provides a …

Molecular structure of an amyloid fibril formed by FUS low-complexity domain

Y Sun, S Zhang, J Hu, Y Tao, W Xia, J Gu, Y Li, Q Cao… - Iscience, 2022 - cell.com
FUS is a multifunctional nuclear protein which undergoes liquid–liquid phase separation in
response to stress and DNA damage. Dysregulation of FUS dynamic phase separation …

Prediction and characterization of liquid-liquid phase separation of minimalistic peptides

Y Tang, S Bera, Y Yao, J Zeng, Z Lao, X Dong… - Cell Reports Physical …, 2021 - cell.com
Liquid-liquid phase separation (LLPS) of proteins mediates the assembly of biomolecular
condensates involved in physiological and pathological processes. Identifying the …

Real-time observation of structure and dynamics during the liquid-to-solid transition of FUS LC

RF Berkeley, M Kashefi, GT Debelouchina - Biophysical journal, 2021 - cell.com
A subset of the proteins found in pathological protein fibrils also exhibit tendencies for liquid-
liquid phase separation (LLPS) both in vitro and in cells. The mechanisms underlying the …