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Title[redir]:
Protein Phase Separation: A New Phase in Cell Biology - PMC
Description:
Cellular compartments and organelles organize biological matter. Most well-known organelles are separated by a membrane boundary from their surrounding milieu. There are also many so-called membraneless organelles and recent studies suggest that ...
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Keywords {🔍}
doi, phase, pubmed, google, scholar, pmc, free, article, separation, cell, protein, proteins, organelles, membraneless, rna, formation, interactions, stress, transitions, cellular, biol, granules, jcell, nature, cells, nuclear, droplets, liquid, aggregation, sgs, assemblies, material, disordered, assembly, form, molecular, disease, liquids, mol, function, components, domains, bodies, idrs, fus, science, properties, transition, tdp, physical,
Topics {✒️}
pmc beta search /n-rich aggregation-prone regions disordered low-complexity domains stress-inducible rnp granules identifying fibril-forming segments aggregating dipeptide-repeat proteins isotropic short-range potentials precisely sol–gel transitions possess rna-binding domains c9orf72 ggggcc repeat high rna/protein stoichiometries labile β-zipper regions c-terminal domain amyotrophic lateral sclerosis stress-triggered phase separation low-complexity domain atpase-modulated stress granules intrinsically disordered proteins/regions higher-order assembly resembles ggggcc repeat expansion [google scholar] 29 [google scholar] 51 glutamine/asparagine-rich domain frontotemporal lobar degeneration-tdp proline–arginine dipeptide repeats post-transcriptional gene regulation intermolecular base-pairing interactions alzheimer-related protein tau intrinsically disordered region protein droplet/gel creates super-resolution microscopy analysis binary-liquid phase separation direct protein–protein interactions liquid–liquid phase separation liquid-liquid phase separation low-complexity domains flory-huggins solution theory transcriptional activation potential higher-order protein assemblies allowing free diffusion dipeptide repeat protein stress granule assembly full-length protein drives pathological fibrillization poly-dipeptides encoded sequence-intrinsic driving forces high-resolution structural studies membrane-bound cellular compartment low concentration region controlled dissolution/condensation
Questions {❓}
- As these proteins are significantly enriched in multivalent proteins, the question inevitably arises as to what determines the specificity and ensures the integrity of these assemblies: how is fusion of distinct membraneless organelles prevented?
- Can we harness our growing understanding of biological phase separation to develop novel therapeutic treatment options?
- How Is Specificity Generated and Maintained?
- How can we investigate the internal organization of membraneless organelles in living systems?
- How do disease mutations and aging specifically affect phase separation of membraneless organelle components?
- How exactly are multivalent interactions encoded in IDRs?
- Put simply, how is the cell able to avoid spontaneous and uncontrollable phase separation?
- Road Toward Novel Therapy?
- What Is the Function of Membraneless Organelles?
- What are the differences between physiological and pathological assemblies?
- What are the essential and nonessential components of different membraneless organelles, and what are their sequence and structural properties?
- What are the exact biological functions of phase separation?
- Which principles target proteins and RNAs to specific phases and what prevents the coalescence of distinct membraneless organelles?
- Which regulatory pathways are involved?
- Why do diseases associated with protein aggregation display such profound cell type specificity?
- Yet why do cells need such compartments?
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- How much does https://scholar.google.com/scholar_lookup?journal=Proc%20Natl%20Acad%20Sci%20U%20S%20A&title=The%20disordered%20P%20granule%20protein%20LAF-1%20drives%20phase%20separation%20into%20droplets%20with%20tunable%20viscosity%20and%20dynamics&author=S%20Elbaum-Garfinkle&volume=112&publication_year=2015&pages=7189-7194&pmid=26015579&doi=10.1073/pnas.1504822112& make?
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- See how much https://doi.org/10.7554/eLife.31486 makes per month
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- Revenue of https://doi.org/10.1073/pnas.1509317112
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- https://doi.org/10.1007/s00401-008-0408-9's total income per month
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- Financial intake of https://doi.org/10.1038/s41467-017-00062-0
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- Learn how profitable https://scholar.google.com/scholar_lookup?journal=J%20Cell%20Biol&title=P%20granules%20extend%20the%20nuclear%20pore%20complex%20environment%20in%20the%20C.%20elegans%20germ%20line&author=DL%20Updike&volume=192&publication_year=2011&pages=939-948&pmid=21402789&doi=10.1083/jcb.201010104& is on a monthly basis
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- https://scholar.google.com/scholar_lookup?journal=Hum%20Mol%20Genet&title=Cellular%20toxicity%20of%20expanded%20RNA%20repeats:%20focus%20on%20RNA%20foci&author=M%20Wojciechowska&author=WJ%20Krzyzosiak&volume=20&publication_year=2011&pages=3811-3821&pmid=21729883&doi=10.1093/hmg/ddr299&'s financial summary
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- https://scholar.google.com/scholar_lookup?journal=Science&title=The%20C9orf72%20GGGGCC%20repeat%20is%20translated%20into%20aggregating%20dipeptide-repeat%20proteins%20in%20FTLD/ALS&author=K%20Mori&volume=339&publication_year=2013&pages=1335-1338&pmid=23393093&doi=10.1126/science.1232927&'s financial summary
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- How much revenue does https://scholar.google.com/scholar_lookup?journal=Neuron&title=Unconventional%20translation%20of%20C9ORF72%20GGGGCC%20expansion%20generates%20insoluble%20polypeptides%20specific%20to%20c9FTD/ALS&author=PE%20Ash&volume=77&publication_year=2013&pages=639-646&pmid=23415312&doi=10.1016/j.neuron.2013.02.004& bring in?
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- nihcesxway5.hub.nih.gov
Name Servers:
- dns1-ncbi.ncbi.nlm.nih.gov
- dns2-ncbi.ncbi.nlm.nih.gov
- lhcns1.nlm.nih.gov
- lhcns2.nlm.nih.gov
CDN Services {📦}
- Ncbi