bioRxiv
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bioRxiv
Nucleolar dynamics are determined by the ordered assembly of the ribosome
Soft matter
Multicompartment calcium alginate microreactors to reduce substrate inhibition in enzyme cascade reactions
Nature chemistry
The interface of condensates of the hnRNPA1 low-complexity domain promotes formation of amyloid fibrils
Protein science : a publication of the Protein Society
The variable domain from dynamin-related protein 1 promotes liquid-liquid phase separation that enhances its interaction with cardiolipin-containing membranes
Cells
Emerging Roles of Ubiquitination in Biomolecular Condensates
Cells
Spontaneous Confinement of mRNA Molecules at Biomolecular Condensate Boundaries
Biomolecules
The Properties and Domain Requirements for Phase Separation of the Sup35 Prion Protein In Vivo
Genes
Relating the Biogenesis and Function of P Bodies in Drosophila to Human Disease
Nature communications
Thermodynamic forces from protein and water govern condensate formation of an intrinsically disordered protein domain
The FEBS journal
The regulation of liquid-liquid phase separated condensates containing nucleic acids
The New phytologist
Actomyosin-driven motility and coalescence of phase-separated viral inclusion bodies are required for efficient replication of a plant rhabdovirus
The Journal of cell biology
Nucleolar condensates: A cellular machinery necessary for T cell activation
Angewandte Chemie (International ed in English)
Synthetic Membraneless Droplets for Synaptic-Like Clustering of Lipid Vesicles
bioRxiv
Alternative splicing regulation in plants by effectors of symbiotic arbuscular mycorrhizal fungi
Molecular cell
Hormone-induced enhancer assembly requires an optimal level of hormone receptor multivalent interactions
Journal of cell science
Axin phosphorylation in condensates counteracts tankyrase-mediated degradation
The journal of physical chemistry letters
Cross-Talk of Cation-π Interactions with Electrostatic and Aromatic Interactions: A Salt-Dependent Trade-off in Biomolecular Condensates
Biophysical journal
Crowder titrations enable the quantification of driving forces for macromolecular phase separation
bioRxiv