bioRxiv
Most Recent
The journal of physical chemistry letters
Concentration Quantification of the Low-Complexity Domain of Fused in Sarcoma inside a Single Droplet and Effects of Solution Parameters
Journal of chemical information and modeling
Insights into the Atomistic Mechanisms of Phosphorylation in Disrupting Liquid-Liquid Phase Separation and Aggregation of the FUS Low-Complexity Domain
International journal of molecular sciences
BIAPSS: A Comprehensive Physicochemical Analyzer of Proteins Undergoing Liquid-Liquid Phase Separation
Jill Bouchard
Editor in Chief, Condensates.com
Here’s a handy new database for all things phase separation. I’ve saved it in our library of Resources–check it out here: https://condensates.com/resources/biapss/
bioRxiv
The oncogenic fusion protein EWS-FLI1 promotes premature ageing of biomolecular condensates by catalyzing fibril formation
Nature communications
Dynamic arrest and aging of biomolecular condensates are modulated by low-complexity domains, RNA and biochemical activity
Biophysical journal
Modulation of assembly of TDP-43 low-complexity domain by heparin: From droplets to amyloid fibrils
Frontiers in cell and developmental biology
Sequence Determinants of TDP-43 Ribonucleoprotein Condensate Formation and Axonal Transport in Neurons
bioRxiv
The interface of condensates of the hnRNPA1 low complexity domain promotes formation of amyloid fibrils
Molecular plant
Histone Methyltransferase SUVR2 Promotes the DSB Repair via Chromatin Remodeling and Liquid-Liquid Phase Separation
bioRxiv
Condensates of disordered proteins have small-world network structures and interfaces defined by expanded conformations
iScience
Hsp70 exhibits a liquid-liquid phase separation ability and chaperones condensed FUS against amyloid aggregation
RNA biology
F/YGG-motif is an intrinsically disordered nucleic-acid binding motif
Nature Communications
Heterozygous frameshift variants in HNRNPA2B1 cause early-onset oculopharyngeal muscular dystrophy
bioRxiv
Designing multiphase biomolecular condensates by coevolution of protein mixtures
Molecular cell
Tuning levels of low-complexity domain interactions to modulate endogenous oncogenic transcription
Nature communications
Low complexity RGG-motif sequence is required for Processing body (P-body) disassembly
Apr
19
The Journal of biological chemistry
Bioinformatic identification of TRK-fused gene protein (TFG) as a previously unrecognized amyloidogenic protein
bioRxiv