Ross, C. A. & Poirier, M. A. Protein aggregation and neurodegenerative disease. Nat. Med. 10, S10–S17 (2004).Article
PubMed
Google Scholar
Willbold, D., Strodel, B., Schröder, G. F., Hoyer, W. & Heise, H. Amyloid-type protein aggregation and prion-like properties of amyloids. Chem. Rev. 121, 8285–8307 (2021).Article
CAS
PubMed
Google Scholar
Dobson, C. M. The amyloid phenomenon and its links with human disease. Cold Spring Harb. Perspect. Biol. 9, a023648 (2017).Article
PubMed
PubMed Central
Google Scholar
Emin, D. et al. Small soluble α-synuclein aggregates are the toxic species in Parkinson’s disease. Nat. Commun. 13, 5512 (2022).Article
CAS
PubMed
PubMed Central
Google Scholar
Cascella, R. et al. Probing the origin of the toxicity of oligomeric aggregates of α-synuclein with antibodies. ACS Chem. Biol. 14, 1352–1362 (2019).Article
CAS
PubMed
PubMed Central
Google Scholar
Meisl, G. et al. Uncovering the universality of self-replication in protein aggregation and its link to disease. Sci. Adv. 8, 6831 (2022).Article
Google Scholar
Alberti, S. & Hyman, A. A. Biomolecular condensates at the nexus of cellular stress, protein aggregation disease and ageing. Nat. Rev. Mol. Cell Biol. 22, 196–213 (2021).Article
CAS
PubMed
Google Scholar
Alberti, S. & Hyman, A. A. Are aberrant phase transitions a driver of cellular aging? BioEssays 38, 959–968 (2016).Article
CAS
PubMed
PubMed Central
Google Scholar
Vazquez, D. S., Toledo, P. L., Gianotti, A. R. & Ermácora, M. R. Protein conformation and biomolecular condensates. Curr. Res. Struct. Biol. 4, 285–307 (2022).Article
CAS
PubMed
PubMed Central
Google Scholar
Nakashima, K. K., Vibhute, M. A. & Spruijt, E. Biomolecular chemistry in liquid phase separated compartments. Front. Mol. Biosci. 6, 21 (2019).Article
CAS
PubMed
PubMed Central
Google Scholar
Bhattacharya, A. et al. Lipid sponge droplets as programmable synthetic organelles. Proc. Natl Acad. Sci. USA 117, 18206–18215 (2020).Article
CAS
PubMed
PubMed Central
Google Scholar
de Jong, B. Coacervation. Proc. R. Acad. Amst. 32, 849–856 (1929).
Google Scholar
Banani, S. F., Lee, H. O., Hyman, A. A. & Rosen, M. K. Biomolecular condensates: organizers of cellular biochemistry. Nat. Rev. Mol. Cell Biol. 18, 285–298 (2017).Article
CAS
PubMed
PubMed Central
Google Scholar
Peeples, W. & Rosen, M. K. Mechanistic dissection of increased enzymatic rate in a phase-separated compartment. Nat. Chem. Biol. 17, 693–702 (2021).Article
CAS
PubMed
PubMed Central
Google Scholar
Zhang, Y., Narlikar, G. J. & Kutateladze, T. G. Enzymatic reactions inside biological condensates. J. Mol. Biol. 433, 166624 (2021).Article
CAS
PubMed
Google Scholar
Molliex, A. et al. Phase separation by low complexity domains promotes stress granule assembly and drives pathological fibrillization. Cell 163, 123–133 (2015).Article
CAS
PubMed
PubMed Central
Google Scholar
Nedelsky, N. B. & Taylor, J. P. Pathological phase transitions in ALS-FTD impair dynamic RNA–protein granules. RNA 28, 97–113 (2022).Article
CAS
PubMed
PubMed Central
Google Scholar
Dewey, C. M. et al. TDP-43 aggregation in neurodegeneration: are stress granules the key? Brain Res. 1462, 16–25 (2012).Article
CAS
PubMed
PubMed Central
Google Scholar
Törnquist, M. et al. Secondary nucleation in amyloid formation. Chem. Commun. 54, 8667–8684 (2018).Article
Google Scholar
Michaels, T. C. T. et al. Chemical kinetics for bridging molecular mechanisms and macroscopic measurements of amyloid fibril formation. Annu. Rev. Phys. Chem. 69, 273–298 (2018).Article
CAS
PubMed
Google Scholar
Sinnige, T. et al. Kinetic analysis reveals that independent nucleation events determine the progression of polyglutamine aggregation in C. elegans. Proc. Natl Acad. Sci. USA 118, e2021888118 (2021).Article
CAS
PubMed
PubMed Central
Google Scholar
Ignatova, Z. & Gierasch, L. M. Monitoring protein stability and aggregation in vivo by real-time fluorescent labeling. Proc. Natl Acad. Sci. USA 101, 523–528 (2004).Article
CAS
PubMed
Google Scholar
Lipiński, W. P. et al. Biomolecular condensates can both accelerate and suppress aggregation of α-synuclein. Sci. Adv. 8, eabq6495 (2022).Article
PubMed
PubMed Central
Google Scholar
Knowles, T. P. J., Vendruscolo, M. & Dobson, C. M. The amyloid state and its association with protein misfolding diseases. Nat. Rev. Mol. Cell Biol. 15, 384–396 (2014).Article
CAS
PubMed
Google Scholar
Farzadfard, A. et al. Thermodynamic characterization of amyloid polymorphism by microfluidic transient incomplete separation. Chem. Sci. 15, 2528–2544 (2024).Article
CAS
PubMed
PubMed Central
Google Scholar
Weber, C., Michaels, T. & Mahadevan, L. Spatial control of irreversible protein aggregation. eLife 8, 42315 (2019).Article
Google Scholar
Khurana, R. et al. Mechanism of thioflavin T binding to amyloid fibrils. J. Struct. Biol. 151, 229–238 (2005).Article
CAS
PubMed
Google Scholar
Wetzel, R. Amyloids, prions & other aggregates. Methods Enzymol. 309, 3–820 (1999).
Google Scholar
Hellstrand, E., Boland, B., Walsh, D. M. & Linse, S. Amyloid β-protein aggregation produces highly reproducible kinetic data and occurs by a two-phase process. ACS Chem. Neurosci. 1, 13–18 (2010).Article
CAS
PubMed
Google Scholar
Zurlo, E. et al. In situ kinetic measurements of α-synuclein aggregation reveal large population of short-lived oligomers. PLoS ONE 16, e0245548 (2021).Article
CAS
PubMed
PubMed Central
Google Scholar
Fakhree, M. A. A., Nolten, I. S., Blum, C. & Claessens, M. M. A. E. Different conformational subensembles of the intrinsically disordered protein α-synuclein in cells. J. Phys. Chem. Lett. 9, 1249–1253 (2018).Article
CAS
PubMed
PubMed Central
Google Scholar
Veldhuis, G., Segers-Nolten, I., Ferlemann, E. & Subramaniam, V. Single-molecule FRET reveals structural heterogeneity of SDS-bound α-synuclein. ChemBioChem 10, 436–439 (2009).Article
CAS
PubMed
Google Scholar
Iljina, M. et al. Quantitative analysis of co-oligomer formation by amyloid-beta peptide isoforms. Sci. Rep. 6, 28658 (2016).Article
CAS
PubMed
PubMed Central
Google Scholar
Tittelmeier, J., Druffel-Augustin, S., Alik, A., Melki, R. & Nussbaum-Krammer, C. Dissecting aggregation and seeding dynamics of α-Syn polymorphs using the phasor approach to FLIM. Commun. Biol. 5, 1345 (2022).Article
PubMed
PubMed Central
Google Scholar
Ray, S. et al. Mass photometric detection and quantification of nanoscale α-synuclein phase separation. Nat. Chem. 15, 1306–1316 (2023).Article
CAS
PubMed
Google Scholar
Murakami, T. et al. ALS/FTD mutation-induced phase transition of FUS liquid droplets and reversible hydrogels into irreversible hydrogels impairs RNP granule function. Neuron 88, 678–690 (2015).Article
CAS
PubMed
PubMed Central
Google Scholar
Lin, Y., Protter, D. S. W., Rosen, M. K. & Parker, R. Formation and maturation of phase-separated liquid droplets by RNA-binding proteins. Mol. Cell 60, 208–219 (2015).Article
CAS
PubMed
PubMed Central
Google Scholar
Mathieu, C., Pappu, R. V. & Taylor, J. P. Beyond aggregation: pathological phase transitions in neurodegenerative disease. Science 370, 55–60 (2020).Article
Google Scholar
Patel, A. et al. A liquid-to-solid phase transition of the ALS protein FUS accelerated by disease mutation. Cell 162, 1066–1077 (2015).Article
CAS
PubMed
Google Scholar
Kim, H. J. et al. Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS. Nature 495, 467–473 (2013).Article
CAS
PubMed
PubMed Central
Google Scholar
Conicella, A. E., Zerze, G. H., Mittal, J. & Fawzi, N. L. ALS mutations disrupt phase separation mediated by α-helical structure in the TDP-43 low-complexity C-terminal domain. Structure 24, 1537–1549 (2016).Article
CAS
PubMed
PubMed Central
Google Scholar
Kang, H. et al. PARIS undergoes liquid–liquid phase separation and poly(ADP‐ribose)‐mediated solidification. EMBO Rep. 24, e56166 (2023).Article
CAS
PubMed
Google Scholar
Gruijs da Silva, L. A. et al. Disease‐linked TDP‐43 hyperphosphorylation suppresses TDP‐43 condensation and aggregation. EMBO J. 41, e108443 (2022).Article
CAS
PubMed
PubMed Central
Google Scholar
Tomaszewski, A. et al. Solid-to-liquid phase transition in the dissolution of cytosolic misfolded-protein aggregates. iScience 26, 108334 (2023).Article
PubMed
PubMed Central
Google Scholar
Linsenmeier, M. et al. The interface of condensates of the hnRNPA1 low-complexity domain promotes formation of amyloid fibrils. Nat. Chem. 15, 1340–1349 (2023).Article
CAS
PubMed
PubMed Central
Google Scholar
Wegmann, S. et al. Tau protein liquid–liquid phase separation can initiate tau aggregation. EMBO J. 37, e98049 (2018).Article
PubMed
PubMed Central
Google Scholar
Boyko, S. et al. Liquid-liquid phase separation of tau protein: the crucial role of electrostatic interactions. J. Biol. Chem. 294, 11054–11059 (2019).Article
CAS
PubMed
PubMed Central
Google Scholar
Wen, J. et al. Conformational expansion of tau in condensates promotes irreversible aggregation. J. Am. Chem. Soc. 143, 13056–13064 (2021).Article
CAS
PubMed
Google Scholar
Boyko, S., Surewicz, K. & Surewicz, W. K. Regulatory mechanisms of tau protein fibrillation under the conditions of liquid–liquid phase separation. Proc. Natl Acad. Sci. USA 117, 31882–31890 (2020).Article
CAS
PubMed
PubMed Central
Google Scholar
Ray, S. et al. Synuclein aggregation nucleates through liquid–liquid phase separation. Nat. Chem. 12, 705–716 (2020).Article
CAS
PubMed
Google Scholar
Ray, S. et al. Spatiotemporal solidification of α-synuclein inside the liquid droplets. Preprint at https://doi.org/10.1101/2021.10.20.465113 (2021).Sawner, A. S. et al. Modulating α-synuclein liquid-liquid phase separation. Biochem 60, 3676–3696 (2021).Article
CAS
Google Scholar
Hardenberg, M. C. et al. Observation of an α-synuclein liquid droplet state and its maturation into Lewy body-like assemblies. J. Mol. Cell Biol. 13, 282–294 (2021).CAS
PubMed
PubMed Central
Google Scholar
Küffner, A. M. et al. Sequestration within biomolecular condensates inhibits Aβ-42 amyloid formation. Chem. Sci. 12, 4373–4382 (2021).Article
PubMed
PubMed Central
Google Scholar
Choi, C. H., Lee, D. S. W., Sanders, D. W. & Brangwynne, C. P. Condensate interfaces can accelerate protein aggregation. Biophys. J. 123, 1404–1413 (2023).Article
PubMed
PubMed Central
Google Scholar
Shen, Y. et al. Biomolecular condensates undergo a generic shear-mediated liquid-to-solid transition. Nat. Nanotechnol. 15, 841–847 (2020).Article
CAS
PubMed
PubMed Central
Google Scholar
Riback, J. A. et al. Composition-dependent thermodynamics of intracellular phase separation. Nature 581, 209–214 (2020).Article
CAS
PubMed
PubMed Central
Google Scholar
Elbaum-Garfinkle, S. et al. The disordered P granule protein LAF-1 drives phase separation into droplets with tunable viscosity and dynamics. Proc. Natl Acad. Sci. USA 112, 7189–7194 (2015).Article
CAS
PubMed
PubMed Central
Google Scholar
Onuchic, P. L., Milin, A. N., Alshareedah, I., Deniz, A. A. & Banerjee, P. R. Divalent cations can control a switch-like behavior in heterotypic and homotypic RNA coacervates. Sci. Rep. 9, 12161 (2019).Article
PubMed
PubMed Central
Google Scholar
McCall, P. M. et al. Partitioning and enhanced self-assembly of actin in polypeptide coacervates. Biophys. J. 114, 1636–1645 (2018).Article
CAS
PubMed
PubMed Central
Google Scholar
Samanta, N. et al. Sequestration of proteins in stress granules relies on the in-cell but not the in vitro folding stability. J. Am. Chem. Soc. 143, 19909–19918 (2021).Article
CAS
PubMed
Google Scholar
Frottin, F. et al. The nucleolus functions as a phase-separated protein quality control compartment. Science 365, 342–347 (2019).Article
CAS
PubMed
Google Scholar
Bauermann, J., Laha, S., McCall, P. M., Jülicher, F. & Weber, C. A. Chemical kinetics and mass action in coexisting phases. J. Am. Chem. Soc. 144, 19294–19304 (2022).Article
CAS
PubMed
PubMed Central
Google Scholar
Michaels, T. C. T., Mahadevan, L. & Weber, C. A. Enhanced potency of aggregation inhibitors mediated by liquid condensates. Phys. Rev. Res. 4, 043173 (2022).Article
CAS
Google Scholar
Stender, E. G. P. et al. Capillary flow experiments for thermodynamic and kinetic characterization of protein liquid-liquid phase separation. Nat. Commun. 12, 7289 (2021).Article
CAS
PubMed
PubMed Central
Google Scholar
Taylor, N. O., Wei, M. T., Stone, H. A. & Brangwynne, C. P. Quantifying dynamics in phase-separated condensates using fluorescence recovery after photobleaching. Biophys. J. 117, 1285–1300 (2019).Article
CAS
PubMed
PubMed Central
Google Scholar
Yewdall, N. A., André, A. A. M., Lu, T. & Spruijt, E. Coacervates as models of membraneless organelles. Curr. Opin. Colloid Interface Sci. 52, 101416 (2021).Article
CAS
Google Scholar
Pönisch, W., Michaels, T. C. T. & Weber, C. A. Aggregation controlled by condensate rheology. Biophys. J. 122, 197–214 (2023).Article
PubMed
Google Scholar
Ahmad, B., Chen, Y. & Lapidus, L. J. Aggregation of α-synuclein is kinetically controlled by intramolecular diffusion. Proc. Natl Acad. Sci. USA 109, 2336–2341 (2012).Article
CAS
PubMed
PubMed Central
Google Scholar
Wei, M. T. et al. Phase behaviour of disordered proteins underlying low density and high permeability of liquid organelles. Nat. Chem. 9, 1118–1125 (2017).Article
CAS
PubMed
PubMed Central
Google Scholar
Wang, H., Kelley, F. M., Milovanovic, D., Schuster, B. S. & Shi, Z. Surface tension and viscosity of protein condensates quantified by micropipette aspiration. Biophys. Rep. 1, 100011 (2021).CAS
Google Scholar
Li, J., Uversky, V. N. & Fink, A. L. Effect of familial Parkinson’s disease point mutations A30P and A53T on the structural properties, aggregation, and fibrillation of human α-synuclein. Biochem 40, 11604–11613 (2001).Article
CAS
Google Scholar
Murthy, A. C. et al. Molecular interactions underlying liquid–liquid phase separation of the FUS low-complexity domain. Nat. Struct. Mol. Biol. 26, 637–648 (2019).Article
CAS
PubMed
PubMed Central
Google Scholar
Smisdom, N. et al. Fluorescence recovery after photobleaching on the confocal laser-scanning microscope: generalized model without restriction on the size of the photobleached disk. J. Biomed. Opt. 16, 046021 (2011).Article
PubMed
Google Scholar
Axelrod, D., Koppel, D. E., Schlessinger, J., Elson, E. & Webb, W. W. Mobility measurement by analysis of fluorescence photobleaching recovery kinetics. Biophys. J. 16, 1055–1069 (1976).Article
CAS
PubMed
PubMed Central
Google Scholar
Jawerth, L. M. et al. Salt-dependent rheology and surface tension of protein condensates using optical traps. Phys. Rev. Lett. 121, 258101 (2018).Article
CAS
PubMed
Google Scholar
Zhou, H. X. Determination of condensate material properties from droplet deformation. J. Phys. Chem. B 124, 8372–8379 (2020).Article
CAS
PubMed
PubMed Central
Google Scholar
Kalwarczyk, T. et al. Motion of nanoprobes in complex liquids within the framework of the length-scale dependent viscosity model. Adv. Colloid Interface Sci. 223, 55–63 (2015).Article
CAS
PubMed
Google Scholar
Bubak, G. et al. Quantifying nanoscale viscosity and structures of living cells nucleus from mobility measurements. J. Phys. Chem. Lett. 12, 294–301 (2021).Article
CAS
PubMed
Google Scholar
Munishkina, L. A., Cooper, E. M., Uversky, V. N. & Fink, A. L. The effect of macromolecular crowding on protein aggregation and amyloid fibril formation. J. Mol. Recognit. 17, 456–464 (2004).Article
CAS
PubMed
Google Scholar
Vagenende, V., Yap, M. G. S. & Trout, B. L. Mechanisms of protein stabilization and prevention of protein aggregation by glycerol. Biochem 48, 11084–11096 (2009).Article
CAS
Google Scholar
Roussel, M. R. Foundations of Chemical Kinetics (IOP Publishing, 2023).Abyzov, A., Blackledge, M. & Zweckstetter, M. Conformational dynamics of intrinsically disordered proteins regulate biomolecular condensate chemistry. Chem. Rev. 122, 6719–6748 (2022).Article
CAS
PubMed
PubMed Central
Google Scholar
Rubinstein, M. & Colby, R. H. Polymer Physics (Oxford Univ. Press, 2003).Garaizar, A. et al. Aging can transform single-component protein condensates into multiphase architectures. Proc. Natl Acad. Sci. USA 119, e2119800119 (2022).Article
CAS
PubMed
PubMed Central
Google Scholar
Breydo, L. et al. The crowd you’re in with: effects of different types of crowding agents on protein aggregation. Biochim. Biophys. Acta Proteins Proteom. 1844, 346–357 (2014).Article
CAS
Google Scholar
Schreck, J. S., Bridstrup, J. & Yuan, J. M. Investigating the effects of molecular crowding on the kinetics of protein aggregation. J. Phys. Chem. B 124, 9829–9839 (2020).Article
CAS
PubMed
Google Scholar
Grigolato, F. & Arosio, P. The role of surfaces on amyloid formation. Biophys. Chem. 270, 106533 (2021).Article
CAS
PubMed
Google Scholar
Galvagnion, C. et al. Lipid vesicles trigger α-synuclein aggregation by stimulating primary nucleation. Nat. Chem. Biol. 11, 229–234 (2015).Article
CAS
PubMed
PubMed Central
Google Scholar
Marie, G. et al. Acceleration of α-synuclein aggregation by exosomes. J. Biol. Chem. 290, 2969–2982 (2015).Article
Google Scholar
Morinaga, A. et al. Critical role of interfaces and agitation on the nucleation of Aβ amyloid fibrils at low concentrations of Aβ monomers. Biochim. Biophys. Acta Proteins Proteom. 1804, 986–995 (2010).Article
CAS
Google Scholar
Gray, J. J. The interaction of proteins with solid surfaces. Curr. Opin. Struct. Biol. 14, 110–115 (2004).Article
CAS
PubMed
Google Scholar
Zapadka, K. L., Becher, F. J., Gomes dos Santos, A. L. & Jackson, S. E. Factors affecting the physical stability (aggregation) of peptide therapeutics. Interface Focus 7, 20170030 (2017).Article
PubMed
PubMed Central
Google Scholar
Camino, J. D., Gracia, P. & Cremades, N. The role of water in the primary nucleation of protein amyloid aggregation. Biophys. Chem. 269, 106520 (2021).Article
CAS
PubMed
Google Scholar
Folkmann, A. W., Putnam, A., Lee, C. F. & Seydoux, G. Regulation of biomolecular condensates by interfacial protein clusters. Science 373, 1218–1224 (2021).Article
CAS
PubMed
PubMed Central
Google Scholar
Garcia-Jove Navarro, M. et al. RNA is a critical element for the sizing and the composition of phase-separated RNA–protein condensates. Nat. Commun. 10, 3230 (2019).Article
PubMed
PubMed Central
Google Scholar
Welsh, T. J. et al. Surface electrostatics govern the emulsion stability of biomolecular condensates. Nano Lett. 22, 612–621 (2022).Article
CAS
PubMed
Google Scholar
Vabulas, R. M., Raychaudhuri, S., Hayer-Hartl, M. & Hartl, F. U. Protein folding in the cytoplasm and the heat shock response. Cold Spring Harb. Perspect. Biol. 2, a004390 (2010).Article
CAS
PubMed
PubMed Central
Google Scholar
Chirita, C. N., Congdon, E. E., Yin, H. & Kuret, J. Triggers of full-length tau aggregation: a role for partially folded intermediates. Biochemistry 44, 5862–5872 (2005).Article
CAS
PubMed
Google Scholar
Menon, S. & Mondal, J. Conformational plasticity in α-synuclein and how crowded environment modulates it. J. Phys. Chem. B 127, 4032–4049 (2023).Article
CAS
PubMed
Google Scholar
Farag, M. et al. Condensates formed by prion-like low-complexity domains have small-world network structures and interfaces defined by expanded conformations. Nat. Commun. 13, 7722 (2022).Article
CAS
PubMed
PubMed Central
Google Scholar
Ohgita, T. et al. Intramolecular interaction kinetically regulates fibril formation by human and mouse α-synuclein. Sci. Rep. 13, 10885 (2023).Article
CAS
PubMed
PubMed Central
Google Scholar
Kumari, P. et al. Structural insights into α-synuclein monomer–fibril interactions. Proc. Natl Acad. Sci. USA 118, e2012171118 (2021).Article
CAS
PubMed
PubMed Central
Google Scholar
Guseva, S. et al. Liquid-liquid phase separation modifies the dynamic properties of intrinsically disordered proteins. J. Am. Chem. Soc. 145, 10548–10563 (2023).Article
CAS
PubMed
PubMed Central
Google Scholar
Zhao, M. et al. Partitioning of small molecules in hydrogen-bonding complex coacervates of poly(acrylic acid) and poly(ethylene glycol) or pluronic block copolymer. Macromolecules 50, 3818–3830 (2017).Article
CAS
Google Scholar
Huang, S. et al. Effect of small molecules on the phase behavior and coacervation of aqueous solutions of poly(diallyldimethylammonium chloride) and poly(sodium 4-styrene sulfonate). J. Colloid Interface Sci. 518, 216–224 (2018).Article
CAS
PubMed
Google Scholar
Lipiński, W. P. et al. Fibrils e merging from droplets: molecular guiding principles behind phase transitions of a short peptide-based condensate studied by solid-state NMR. Chem. Eur. J. 29, e202301159 (2023).Article
PubMed
Google Scholar
Leblanc, S. J., Kulkarni, P. & Weninger, K. R. Single molecule FRET: a powerful tool to study intrinsically disordered proteins. Biomolecules 8, 140 (2018).Article
PubMed
PubMed Central
Google Scholar
Holmstrom, E. D. et al. Accurate transfer efficiencies, distance distributions, and ensembles of unfolded and intrinsically disordered proteins from single-molecule FRET. Methods Enzymol. 611, 287–325 (2018).Article
CAS
PubMed
PubMed Central
Google Scholar
Bordignon, E. & Polyhach, Y. EPR techniques to probe insertion and conformation of spin-labeled proteins in lipid bilayers. Meth. Mol. Biol. 974, 329–355 (2013).Article
CAS
Google Scholar
Maltseva, D. et al. Fibril formation and ordering of disordered FUS LC driven by hydrophobic interactions. Nat. Chem. 15, 1146–1154 (2023).Article
CAS
PubMed
PubMed Central
Google Scholar
Dyson, H. J. & Wright, P. E. Insights into the structure and dynamics of unfolded proteins from nuclear magnetic resonance. Adv. Protein Chem. 62, 311–340 (2002).Article
CAS
PubMed
Google Scholar
Saibil, H. Chaperone machines for protein folding, unfolding and disaggregation. Nat. Rev. Mol. Cell Biol. 14, 630–642 (2013).Article
CAS
PubMed
PubMed Central
Google Scholar
Hatters, D. M., Lindner, R. A., Carver, J. A. & Howlett, G. J. The molecular chaperone, α-crystallin, inhibits amyloid formation by apolipoprotein C-II. J. Biol. Chem. 276, 33755–33761 (2001).Article
CAS
PubMed
Google Scholar
Webster, J. M., Darling, A. L., Uversky, V. N. & Blair, L. J. Small heat shock proteins, big impact on protein aggregation in neurodegenerative disease. Front. Pharmacol. 10, 1047 (2019).Article
CAS
PubMed
PubMed Central
Google Scholar
Bruinsma, I. B. et al. Inhibition of α-synuclein aggregation by small heat shock proteins. Proteins 79, 2956–2967 (2011).Article
CAS
PubMed
Google Scholar
Wentink, A. S. et al. Molecular dissection of amyloid disaggregation by human HSP70. Nature 587, 483–488 (2020).Article
CAS
PubMed
Google Scholar
Li, Y. et al. Hsp70 exhibits a liquid-liquid phase separation ability and chaperones condensed FUS against amyloid aggregation. iScience 25, 104356 (2022).Article
CAS
PubMed
PubMed Central
Google Scholar
Shammas, S. L. et al. Binding of the molecular chaperone αb-crystallin to Aβ amyloid fibrils inhibits fibril elongation. Biophys. J. 101, 1681–1689 (2011).Article
CAS
PubMed
PubMed Central
Google Scholar
Shorter, J. The mammalian disaggregase machinery: Hsp110 synergizes with Hsp70 and Hsp40 to catalyze protein disaggregation and reactivation in a cell-free system. PLoS ONE 6, e26319 (2011).Article
CAS
PubMed
PubMed Central
Google Scholar
Daturpalli, S., Waudby, C. A., Meehan, S. & Jackson, S. E. Hsp90 inhibits α-synuclein aggregation by interacting with soluble oligomers. J. Mol. Biol. 425, 4614–4628 (2013).Article
CAS
PubMed
Google Scholar
Zhang, Z. Y. et al. TRIM11 protects against tauopathies and is down-regulated in Alzheimer’s disease. Science 381, eadd6696 (2023).Article
CAS
PubMed
Google Scholar
Liu, Z. et al. Hsp27 chaperones FUS phase separation under the modulation of stress-induced phosphorylation. Nat. Struct. Mol. Biol. 27, 363–372 (2020).Article
CAS
PubMed
Google Scholar
Gu, J. et al. Hsp40 proteins phase separate to chaperone the assembly and maintenance of membraneless organelles. Proc. Natl Acad. Sci. USA 117, 31123–31133 (2020).Article
CAS
PubMed
PubMed Central
Google Scholar
Hiller, S. Chaperone-bound clients: the importance of being dynamic. Trends Biochem. Sci. 44, 517–527 (2019).Article
CAS
PubMed
Google Scholar
Zbinden, A., Pérez-Berlanga, M., De Rossi, P. & Polymenidou, M. Phase separation and neurodegenerative diseases: a disturbance in the force. Dev. Cell 55, 45–68 (2020).Article
CAS
PubMed
Google Scholar
Mateju, D. et al. An aberrant phase transition of stress granules triggered by misfolded protein and prevented by chaperone function. EMBO J. 36, 1669–1687 (2017).Article
CAS
PubMed
PubMed Central
Google Scholar