Mechano-dependent sorbitol accumulation supports biomolecular condensate. [PDF]
Condensed droplets of protein regulate many cellular functions, yet the physiological conditions regulating their formation remain largely unexplored.
Torrino S +17 more
europepmc +4 more sources
Conformational Dynamics of Intrinsically Disordered Proteins Regulate Biomolecular Condensate Chemistry. [PDF]
Motions in biomolecules are critical for biochemical reactions. In cells, many biochemical reactions are executed inside of biomolecular condensates formed by ultradynamic intrinsically disordered proteins.
Abyzov A, Blackledge M, Zweckstetter M.
europepmc +4 more sources
Poly(ADP-ribose): A Dynamic Trigger for Biomolecular Condensate Formation. [PDF]
Poly(ADP-ribose) (PAR) is a nucleic acid-like protein modification that can seed the formation of microscopically visible cellular compartments that lack enveloping membranes, recently termed biomolecular condensates.
Leung AKL.
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Biomolecular condensate phase diagrams with a combinatorial microdroplet platform. [PDF]
A central concept for characterising phase-separating systems is the phase diagram but generation of such diagrams for biomolecular systems is typically slow and low-throughput.
Arter WE +16 more
europepmc +2 more sources
ATP-induced cross-linking of a biomolecular condensate. [PDF]
DEAD-box helicases are important regulators of biomolecular condensates. However, the mechanisms through which these enzymes affect the dynamics of biomolecular condensates have not been systematically explored.
Coupe S, Fakhri N.
europepmc +2 more sources
Structured protein domains enter the spotlight: modulators of biomolecular condensate form and function. [PDF]
Biomolecular condensates are membraneless organelles that concentrate proteins and nucleic acids. One of the primary components of condensates is multidomain proteins, whose domains can be broadly classified as structured and disordered. While structured
Hess N, Joseph JA.
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Systematic discovery of biomolecular condensate-specific protein phosphorylation. [PDF]
Reversible protein phosphorylation is an important mechanism for regulating (dis)assembly of biomolecular condensates. However, condensate-specific phosphosites remain largely unknown, thereby limiting our understanding of the underlying mechanisms. Here,
Sridharan S +9 more
europepmc +2 more sources
Protein compactness and interaction valency define the architecture of a biomolecular condensate across scales. [PDF]
Non-membrane-bound biomolecular condensates have been proposed to represent an important mode of subcellular organization in diverse biological settings.
Polyansky AA +4 more
europepmc +2 more sources
Amino acid transfer free energies reveal thermodynamic driving forces in biomolecular condensate formation. [PDF]
The self-assembly of intrinsically disordered proteins into biomolecular condensates shows a dependence on the primary sequence of the protein, leading to sequence-dependent phase separation.
Rekhi S, Mittal J.
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The material properties of a bacterial-derived biomolecular condensate tune biological function in natural and synthetic systems. [PDF]
“Intracellular phase separation is emerging as a universal principle for organizing biochemical reactions in time and space. Here the authors show that PopZ condensate dynamics support cell division and using PopZ modular architecture, the tunable PopTag
Lasker K +12 more
europepmc +2 more sources

