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Time scale of protein aggregation dictated by liquid‐liquid demixing

https://doi.org/10.1002/prot.10306
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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

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Interaction of explicit solvent with hydrophobic/philic/charged residues of a protein: Residue character vs. conformational context
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Interacting processes in protein coagulation
inferredcites →https://doi.org/10.1002/1097-0282(200107)59:1<51::aid-bip1005>3.0.co;2-8openalex-snapshot
Interaction of processes on different length scales in a bioelastomer capable of performing energy conversion
inferredcites →https://doi.org/10.1002/bip.360251204openalex-snapshot
Sol–sol structural transition of aqueous agarose systems
inferredcites →https://doi.org/10.1002/bip.360260513openalex-snapshot
Order parameters of gels and gelation kinetics of aqueous agarose systems: Relation to the spinodal decomposition of the sol
inferredcites →https://doi.org/10.1002/bip.360310706openalex-snapshot
Time‐Resolved study of network self‐organization from a biopolymeric solution
inferredcites →https://doi.org/10.1002/bip.360330504openalex-snapshot
Self‐assembly of bioelastomeric structures from solutions: Mean‐field critical behavior and Flory–Huggins free energy of interactions
inferredcites →https://doi.org/10.1002/polc.5070390125openalex-snapshot
Light scattering of concentrated polydisperse polymer solutions
inferredcites →https://doi.org/10.1007/bf01441902openalex-snapshot
Experimental studies of the rheological behavior of a demixing biopolymeric sol
inferredcites →https://doi.org/10.1007/s002490050125openalex-snapshot
Physics and biophysics of solvent induced forces: hydrophobic interactions and context-dependent hydration
inferredcites →https://doi.org/10.1016/0009-2614(89)87135-0openalex-snapshot
CO-Solute control of the self-assembly of a biopolymeric supramolecular structure
inferredcites →https://doi.org/10.1016/0009-2614(91)85163-qopenalex-snapshot
Microgel regions in dilute agarose solutions: the notion of non-gelling concentration, and the role of spinodal demixing
inferredcites →https://doi.org/10.1016/0009-2614(96)00322-3openalex-snapshot
Correlated solvent-induced forces on a protein at single residue resolution: relation to conformation, stability, dynamics and function
inferredcites →https://doi.org/10.1016/0021-9614(75)90197-4openalex-snapshot
Phase transitions and critical phenomena
inferredcites →https://doi.org/10.1016/0022-2836(85)90174-3openalex-snapshot
Kinetics of sickle hemoglobin polymerization
inferredcites →https://doi.org/10.1016/0022-2836(85)90175-5openalex-snapshot
Kinetics of sickle hemoglobin polymerization
inferredcites →https://doi.org/10.1016/b978-0-12-309770-5.50014-xopenalex-snapshot
DYNAMICS OF FIRST ORDER PHASE TRANSITIONS
inferredcites →https://doi.org/10.1016/s0006-3495(00)76355-7openalex-snapshot
Nonideality and the Nucleation of Sickle Hemoglobin
inferredcites →https://doi.org/10.1016/s0006-3495(91)82078-1openalex-snapshot
Spinodal lines and Flory-Huggins free-energies for solutions of human hemoglobins HbS and HbA
inferredcites →https://doi.org/10.1016/s0006-3495(97)78044-5openalex-snapshot
Collective properties of hydration: long range and specificity of hydrophobic interactions
inferredcites →https://doi.org/10.1016/s0006-3495(97)78673-9openalex-snapshot
Homogeneous nucleation in sickle hemoglobin: stochastic measurements with a parallel method
inferredcites →https://doi.org/10.1016/s0065-3233(08)60287-9openalex-snapshot
Sickle Cell Hemoglobin Polymerization
inferredcites →https://doi.org/10.1016/s0301-4622(99)00004-6openalex-snapshot
Effects of solvent perturbation on gelation driven by spinodal demixing
inferredcites →https://doi.org/10.1016/s0959-440x(99)00049-4openalex-snapshot
Amyloid fibrillogenesis: themes and variations
inferredcites →https://doi.org/10.1016/s0959-440x(99)00051-2openalex-snapshot
Mammalian prion proteins
inferredcites →https://doi.org/10.1021/ar9702278openalex-snapshot
Nucleation of First-Order Phase Transitions
inferredcites →https://doi.org/10.1021/jp980296jopenalex-snapshot
The Protein−Water Phase Diagram and the Growth of Protein Crystals from Aqueous Solution
inferredcites →https://doi.org/10.1021/ma60075a033openalex-snapshot
Characterization of Polystyrenes of Extremely High Molecular Weights
inferredcites →https://doi.org/10.1023/a:1013146530021openalex-snapshot
The Role of Solvent in Protein Folding and in Aggregation
inferredcites →https://doi.org/10.1038/416507aopenalex-snapshot
Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases
inferredcites →https://doi.org/10.1038/416535aopenalex-snapshot
Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo
inferredcites →https://doi.org/10.1038/416811aopenalex-snapshot
Insights into phase transition kinetics from colloid science
inferredcites →https://doi.org/10.1063/1.1695731openalex-snapshot
Phase Separation by Spinodal Decomposition in Isotropic Systems
inferredcites →https://doi.org/10.1063/1.2914118openalex-snapshot
Scaling Concepts in Polymer Physics
inferredcites →https://doi.org/10.1063/1.3127900openalex-snapshot
Introduction to Phase Transitions and Critical Phenomena
inferredcites →https://doi.org/10.1063/1.474547openalex-snapshot
Liquid–liquid phase separation in supersaturated lysozyme solutions and associated precipitate formation/crystallization
inferredcites →https://doi.org/10.1073/pnas.110000497openalex-snapshot
Control of protein crystal nucleation around the metastable liquid–liquid phase boundary
inferredcites →https://doi.org/10.1073/pnas.84.20.7079openalex-snapshot
Binary liquid phase separation and critical phenomena in a protein/water solution.
inferredcites →https://doi.org/10.1074/jbc.274.36.25945openalex-snapshot
Amyloid β-Protein Fibrillogenesis
inferredcites →https://doi.org/10.1103/physreve.56.r4939openalex-snapshot
Effects of electric charges on hydrophobic forces
inferredcites →https://doi.org/10.1103/physreve.59.2222openalex-snapshot
Multiple interactions between molecular and supramolecular ordering
inferredcites →https://doi.org/10.1103/physreve.62.6799openalex-snapshot
Effects of electric charges on hydrophobic forces. II.
inferredcites →https://doi.org/10.1103/physrevlett.39.474openalex-snapshot
Critical Behavior of a Binary Mixture of Protein and Salt Water
inferredcites →https://doi.org/10.1103/physrevlett.79.4286openalex-snapshot
Fractal Morphogenesis and Interacting Processes in Gelation
inferredcites →https://doi.org/10.1119/1.1986710openalex-snapshot
Introduction to Phase Transitions and Critical Phenomena
inferredcites →https://doi.org/10.1126/science.277.5334.1975openalex-snapshot
Enhancement of Protein Crystal Nucleation by Critical Density Fluctuations
inferredcites →https://doi.org/10.1126/science.7539154openalex-snapshot
The Biophysics of Sickle Cell Hydroxyurea Therapy
inferredcites →https://doi.org/10.1126/science.8446903openalex-snapshot
The Role of Water in Hemoglobin Function and Stability
inferredcites →https://doi.org/10.1142/9789812798763_0016openalex-snapshot
Scaling, Universality and Operator Algebras
inferredcites →https://doi.org/10.1146/annurev.neuro.24.1.519openalex-snapshot
Prion Diseases of Humans and Animals: Their Causes and Molecular Basis
inferredcites →https://doi.org/10.1209/epl/i1997-00289-yopenalex-snapshot
Role of metastable states in phase ordering dynamics
inferredcites →https://doi.org/10.1887/0750303131/b984v1c12openalex-snapshot
Phase transitions and critical phenomena

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

inferred← citeshttps://doi.org/10.2139/ssrn.4803885openalex-extracted
Surface-Catalysed Liquid-Liquid Phase Separation and Amyloid-Like Assembly in Microscale Compartments
inferred← citeshttps://doi.org/10.1002/prot.10648openalex-snapshot
The role of pH on instability and aggregation of sickle hemoglobin solutions
inferred← citeshttps://doi.org/10.1002/prot.20074openalex-snapshot
Irreversible formation of intermediate BSA oligomers requires and induces conformational changes
inferred← citeshttps://doi.org/10.1002/prot.20339openalex-snapshot
Effect of T‐R conformational change on sickle‐cell hemoglobin interactions and aggregation
inferred← citeshttps://doi.org/10.1002/prot.22122openalex-snapshot
Early stages of β2‐microglobulin aggregation and the inhibiting action of αB‐crystallin
inferred← citeshttps://doi.org/10.1007/s00249-007-0137-3openalex-snapshot
Effects of confinement on insulin amyloid fibrils formation
inferred← citeshttps://doi.org/10.1016/b0-12-369401-9/00752-xopenalex-snapshot
Protein Folding and Aggregation
inferred← citeshttps://doi.org/10.1016/b978-0-323-90800-9.00307-3openalex-snapshot
Protein Folding and Aggregation
inferred← citeshttps://doi.org/10.1016/j.abb.2011.01.024openalex-snapshot
Bovine Serum Albumin protofibril-like aggregates formation: Solo but not simple mechanism
inferred← citeshttps://doi.org/10.1016/j.bbapap.2009.09.013openalex-snapshot
Concanavalin A aggregation and toxicity on cell cultures
inferred← citeshttps://doi.org/10.1016/j.chemphys.2013.01.041openalex-snapshot
Prediction of thermodynamic instabilities of protein solutions from simple protein–protein interactions
inferred← citeshttps://doi.org/10.1016/j.febslet.2015.07.006openalex-snapshot
The route to protein aggregate superstructures: Particulates and amyloid‐like spherulites
inferred← citeshttps://doi.org/10.1016/j.jcis.2024.07.135openalex-snapshot
Surface-catalyzed liquid–liquid phase separation and amyloid-like assembly in microscale compartments
inferred← citeshttps://doi.org/10.1016/j.jcrysgro.2004.10.056openalex-snapshot
Lysozyme crystallization rates controlled by anomalous fluctuations
inferred← citeshttps://doi.org/10.1016/s0006-3495(04)74239-3openalex-snapshot
Liquid-Liquid Phase Separation in Hemoglobins: Distinct Aggregation Mechanisms of the β6 Mutants
inferred← citeshttps://doi.org/10.1021/acs.jpca.5b01869openalex-snapshot
Enhanced Hydrate Nucleation Near the Limit of Stability
inferred← citeshttps://doi.org/10.1021/acs.jpcb.0c07575openalex-snapshot
Coarse-Grained Model of Entropy-Driven Demixing
inferred← citeshttps://doi.org/10.1021/acs.jpcc.5b01869openalex-snapshot
Enhanced Hydrate Nucleation near the Limit of Stability
inferred← citeshttps://doi.org/10.1021/acsabm.0c01541openalex-snapshot
Conformational Transitions upon Maturation Rule Surface and pH-Responsiveness of α-Lactalbumin Microparticulates
inferred← citeshttps://doi.org/10.1021/acsomega.0c05638openalex-snapshot
Heparin Accelerates the Protein Aggregation via the Downhill Polymerization Mechanism: Multi-Spectroscopic Studies to Delineate the Implications on Proteinopathies
inferred← citeshttps://doi.org/10.1021/ma025890copenalex-snapshot
Hydrophobic Interaction Model for Upper and Lower Critical Solution Temperatures
inferred← citeshttps://doi.org/10.1038/srep11260openalex-snapshot
Optimization of crystal nucleation close to a metastable fluid-fluid phase transition
inferred← citeshttps://doi.org/10.1039/b717404gopenalex-snapshot
Protein crystallization: universal thermodynamic vs. specific effects of PEG
inferred← citeshttps://doi.org/10.1039/c8sc01479eopenalex-snapshot
Origin of metastable oligomers and their effects on amyloid fibril self-assembly
inferred← citeshttps://doi.org/10.1063/1.2771168openalex-snapshot
Protein phase behavior and crystallization: Effect of glycerol
inferred← citeshttps://doi.org/10.1063/1.4811343openalex-snapshot
Structural fingerprints and their evolution during oligomeric vs. oligomer-free amyloid fibril growth
inferred← citeshttps://doi.org/10.1063/5.0235786openalex-snapshot
Phase changes in sickle hemoglobin self-assembly
inferred← citeshttps://doi.org/10.1073/pnas.0501957102openalex-snapshot
Systematically perturbed folding patterns of amyotrophic lateral sclerosis (ALS)-associated SOD1 mutants
inferred← citeshttps://doi.org/10.1103/physreve.68.011904openalex-snapshot
Thermodynamic instability in supersaturated lysozyme solutions: Effect of salt and role of concentration fluctuations
inferred← citeshttps://doi.org/10.1103/physrevlett.109.095702openalex-snapshot
Homogeneous Crystal Nucleation Near a Metastable Fluid-Fluid Phase Transition
inferred← citeshttps://doi.org/10.1110/ps.03538904openalex-snapshot
Transient formation of nano‐crystalline structures during fibrillation of an Aβ‐like peptide
inferred← citeshttps://doi.org/10.1115/1.3127259openalex-snapshot
Insights Into Crowding Effects on Protein Stability From a Coarse-Grained Model
inferred← citeshttps://doi.org/10.1529/biophysj.104.046482openalex-snapshot
Aggregation of Normal and Sickle Hemoglobin in High Concentration Phosphate Buffer
inferred← citeshttps://doi.org/10.1529/biophysj.104.051250openalex-snapshot
Understanding the Shape of Sickled Red Cells
inferred← citeshttps://doi.org/10.1529/biophysj.105.076497openalex-snapshot
Coarse-Grained Strategy for Modeling Protein Stability in Concentrated Solutions. II: Phase Behavior
inferred← citeshttps://doi.org/10.1529/biophysj.107.110577openalex-snapshot
Protein Aggregation/Crystallization and Minor Structural Changes: Universal versus Specific Aspects
inferred← citeshttps://doi.org/10.3390/biom12050684openalex-snapshot
Randomizing of Oligopeptide Conformations by Nearest Neighbor Interactions between Amino Acid Residues
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