Biological Liquid-Liquid Phase Separation, Biomolecular Condensates, and Membraneless Organelles

This reprint presents recent developments in the field of biological liquid-liquid phase separation (LLPS, also known as biomolecular condensation). LLPS and related biogenesis of various membraneless organelles (MLOs) and biomolecular condensates (BMCs) represent fundamental molecular mechanisms go...

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Bibliographic Details
Other Authors: Uversky, Vladimir N. (Editor)
Format: Electronic Book Chapter
Language:English
Published: Basel MDPI - Multidisciplinary Digital Publishing Institute 2023
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Online Access:DOAB: download the publication
DOAB: description of the publication
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520 |a This reprint presents recent developments in the field of biological liquid-liquid phase separation (LLPS, also known as biomolecular condensation). LLPS and related biogenesis of various membraneless organelles (MLOs) and biomolecular condensates (BMCs) represent fundamental molecular mechanisms governing the spatio-temporal organization of the intracellular space. In fact, MLOs and BMCs, being liquid droplets, represent specific compartments within a cell that are not enclosed by a lipid membrane. Most biological LLPS processes are reversible, and many MLOs/BMCs exist transiently; they rapidly emerge when conditions are changed and rapidly disintegrate as soon as the original conditions are restored, thereby showing a characteristic "now you see me, now you don't" behavior. Numerous MLOs/BMCs are found inside eukaryotic cells, where they exist as liquid droplets (or cellular bodies, puncta, etc.) in the cytoplasm, nucleoplasm, mitochondrial matrix, and stroma of chloroplasts. Furthermore, MLOs/BMCs are commonly observed in Archaea, bacteria, and, likely, viruses. MLOs/BMCs have numerous crucial functions, and their biogenesis is known to be controlled by various external factors and environmental cues, such as changes in temperature, pH, and ionic strength of the solution. All of these have garnered the close attention of many researchers to biological LLPS, MLOs, and BMCs. 
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653 |a Alzheimer's disease 
653 |a amyloid aggregation 
653 |a lipid bilayer 
653 |a cholesterol 
653 |a time-lapse AFM imaging 
653 |a molecular dynamics 
653 |a liquid-liquid phase separation (LLPS) 
653 |a membraneless organelles 
653 |a phase-separated condensates 
653 |a human diseases 
653 |a liquid-liquid phase separation 
653 |a intrinsically disordered proteins 
653 |a proteins with low complexity 
653 |a P-body 
653 |a Nst1 
653 |a polyampholyte domain 
653 |a aggregation-prone domain 
653 |a Saccharomyces cerevisiae 
653 |a membrane-less organelle 
653 |a nuclear speckle 
653 |a nucleolus 
653 |a phase separation 
653 |a chromatin organization 
653 |a nuclear condensate 
653 |a intrinsically disordered region 
653 |a transcription 
653 |a DNA damage repair 
653 |a super-enhancer 
653 |a quantitative imaging 
653 |a CTP synthase 
653 |a cytoophidium 
653 |a fluorescence recovery after photobleaching (FRAP) 
653 |a stimulated emission depletion (STED) 
653 |a Drosophila 
653 |a epithelium 
653 |a follicle cell 
653 |a ingression 
653 |a paramyxoviruses 
653 |a Hendra virus 
653 |a amyloid-like fibrils 
653 |a Taylor Dispersion Analysis (TDA) 
653 |a negative staining Transmission Electron Microscopy (ns-TEM) 
653 |a Polyethylene glycol (PEG) precipitation assays 
653 |a Congo Red 
653 |a Small-Angle X-ray Scattering (SAXS) 
653 |a actin 
653 |a actin polymerization 
653 |a actin-binding proteins 
653 |a coacervate 
653 |a membrane 
653 |a signaling proteins 
653 |a n/a 
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