On the public citation graph

Surface-Catalysed Liquid-Liquid Phase Separation and Amyloid-Like Assembly in Microscale Compartments

https://doi.org/10.2139/ssrn.4803885
0 signed · 85 inferred · view as graph

Inferred edges come from two machine sources: sweeps of open repository metadata (mostly SSRN and Zenodo), and a bulk OpenAlex citation snapshot. Every row below is labelled with the one it came from. Neither is a complete citation index — absence here is not evidence of absence.

Is this your work? Sign in with ORCID and put your name on the claims that are yours.
Claim with ORCID
Reference health. See whether every reference in this work resolves to a known work and none has been retracted — and get a dated CiteStamped badge you can embed.
See reference health

What this work says

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

inferredcites →https://doi.org/10.1002/adbi.201900023openalex-extracted
Printing Life‐Inspired Subcellular Scale Compartments with Autonomous Molecularly Crowded Confinement
inferredcites →https://doi.org/10.1002/admi.202000446openalex-extracted
Interfaces Determine the Fate of Seeded α‐Synuclein Aggregation
inferredcites →https://doi.org/10.1002/anie.201713416openalex-extracted
Amyloid Polymorphism in the Protein Folding and Aggregation Energy Landscape
inferredcites →https://doi.org/10.1002/btpr.621openalex-extracted
Crystallization and liquid‐liquid phase separation of monoclonal antibodies and fc‐fusion proteins: Screening results
inferredcites →https://doi.org/10.1002/pro.3674openalex-extracted
β‐Amyloid aggregation and heterogeneous nucleation
inferredcites →https://doi.org/10.1002/prot.10306openalex-extracted
Time scale of protein aggregation dictated by liquid‐liquid demixing
inferredcites →https://doi.org/10.1002/prot.22852openalex-extracted
Universality of protein reentrant condensation in solution induced by multivalent metal ions
inferredcites →https://doi.org/10.1007/978-1-0716-2597-2_20openalex-extracted
Reproducible Formation of Insulin Superstructures: Amyloid-Like Fibrils, Spherulites, and Particulates
inferredcites →https://doi.org/10.1007/s12551-017-0289-zopenalex-extracted
Monomer-dependent secondary nucleation in amyloid formation
inferredcites →https://doi.org/10.1016/bs.apcsb.2019.08.002openalex-extracted
Liquid-liquid phase transitions and amyloid aggregation in proteins related to cancer and neurodegenerative diseases
inferredcites →https://doi.org/10.1016/j.abb.2007.05.015openalex-extracted
Folding versus aggregation: Polypeptide conformations on competing pathways
inferredcites →https://doi.org/10.1016/j.bbapap.2010.04.001openalex-extracted
Molecular mechanism of Thioflavin-T binding to amyloid fibrils
inferredcites →https://doi.org/10.1016/j.bpc.2020.106533openalex-extracted
The role of surfaces on amyloid formation
inferredcites →https://doi.org/10.1016/j.bpj.2022.06.013openalex-extracted
The physics of liquid-to-solid transitions in multi-domain protein condensates
inferredcites →https://doi.org/10.1016/j.cell.2015.09.015openalex-extracted
Phase Separation by Low Complexity Domains Promotes Stress Granule Assembly and Drives Pathological Fibrillization
inferredcites →https://doi.org/10.1016/j.cell.2017.08.048openalex-extracted
Structure of FUS Protein Fibrils and Its Relevance to Self-Assembly and Phase Separation of Low-Complexity Domains
inferredcites →https://doi.org/10.1016/j.cell.2018.12.035openalex-extracted
Considerations and Challenges in Studying Liquid-Liquid Phase Separation and Biomolecular Condensates
inferredcites →https://doi.org/10.1016/j.ces.2012.04.031openalex-extracted
Time evolution of amyloid fibril length distribution described by a population balance model
inferredcites →https://doi.org/10.1016/j.colsurfb.2011.09.018openalex-extracted
Factors affecting the formation of insulin amyloid spherulites
inferredcites →https://doi.org/10.1016/j.febslet.2015.07.006openalex-extracted
The route to protein aggregate superstructures: Particulates and amyloid‐like spherulites
inferredcites →https://doi.org/10.1016/j.jbc.2021.100367openalex-extracted
Liquid–liquid phase separation of full-length prion protein initiates conformational conversion in vitro
inferredcites →https://doi.org/10.1016/j.jcis.2020.03.107openalex-extracted
Probing ensemble polymorphism and single aggregate structural heterogeneity in insulin amyloid self-assembly
inferredcites →https://doi.org/10.1016/j.jcis.2021.09.132openalex-extracted
Polysorbate 80 controls Morphology, structure and stability of human insulin Amyloid-Like spherulites
inferredcites →https://doi.org/10.1016/j.jmb.2006.11.008openalex-extracted
Kinetics of Different Processes in Human Insulin Amyloid Formation
inferredcites →https://doi.org/10.1016/j.jmb.2009.04.042openalex-extracted
Competition between Intramolecular and Intermolecular Interactions in an Amyloid-Forming Protein
inferredcites →https://doi.org/10.1016/j.jmb.2012.02.031openalex-extracted
From Macroscopic Measurements to Microscopic Mechanisms of Protein Aggregation
inferredcites →https://doi.org/10.1016/j.jmb.2018.06.010openalex-extracted
Role of Liquid–Liquid Phase Separation in Assembly of Elastin and Other Extracellular Matrix Proteins
inferredcites →https://doi.org/10.1016/j.jmb.2020.03.004openalex-extracted
Liquid–Liquid Phase Separation and Its Mechanistic Role in Pathological Protein Aggregation
inferredcites →https://doi.org/10.1016/j.susc.2012.03.018openalex-extracted
Attachment limited versus diffusion limited nucleation of organic molecules: Hexaphenyl on sputter-modified mica
inferredcites →https://doi.org/10.1016/s0022-2836(02)01175-0openalex-extracted
Assembly of Amyloid Protofibrils via Critical Oligomers—A Novel Pathway of Amyloid Formation
inferredcites →https://doi.org/10.1021/acs.chemrev.3c00615openalex-extracted
Molecular Crowding: The History and Development of a Scientific Paradigm
inferredcites →https://doi.org/10.1021/acs.jpcb.2c01947openalex-extracted
Gelation Dynamics upon Pressure-Induced Liquid–Liquid Phase Separation in a Water–Lysozyme Solution
inferredcites →https://doi.org/10.1021/acs.jpcb.5b05099openalex-extracted
Molecular Rotors Provide Insights into Microscopic Structural Changes During Protein Aggregation
inferredcites →https://doi.org/10.1021/acs.jpcb.8b01779openalex-extracted
Ethanol Controls the Self-Assembly and Mesoscopic Properties of Human Insulin Amyloid Spherulites
inferredcites →https://doi.org/10.1021/acs.jpclett.0c02567openalex-extracted
Amyloid Aggregation under the Lens of Liquid–Liquid Phase Separation
inferredcites →https://doi.org/10.1021/acs.jpclett.2c03400openalex-extracted
Heterogeneous and Surface-Catalyzed Amyloid Aggregation Monitored by Spatially Resolved Fluorescence and Single Molecule Microscopy
inferredcites →https://doi.org/10.1021/acs.jpclett.7b01720openalex-extracted
Direct Observation of Insulin Association Dynamics with Time-Resolved X-ray Scattering
inferredcites →https://doi.org/10.1021/acsabm.0c01541openalex-extracted
Conformational Transitions upon Maturation Rule Surface and pH-Responsiveness of α-Lactalbumin Microparticulates
inferredcites →https://doi.org/10.1021/acschemneuro.9b00627openalex-extracted
Electrostatically Driven Complex Coacervation and Amyloid Aggregation of Tau Are Independent Processes with Overlapping Conditions
inferredcites →https://doi.org/10.1021/bi00083a004openalex-extracted
Acid stabilization of insulin
inferredcites →https://doi.org/10.1021/bi034879hopenalex-extracted
Aggregation of Bovine Insulin Probed by DSC/PPC Calorimetry and FTIR Spectroscopy
inferredcites →https://doi.org/10.1021/bm7009224openalex-extracted
Thermal Dependence of Thermally Induced Protein Spherulite Formation and Growth: Kinetics of β-lactoglobulin and Insulin
inferredcites →https://doi.org/10.1021/jacs.2c12611openalex-extracted
Liquid-Droplet-Mediated ATP-Triggered Amyloidogenic Pathway of Insulin-Derived Chimeric Peptides: Unraveling the Microscopic and Molecular Processes
inferredcites →https://doi.org/10.1021/jp710131uopenalex-extracted
Secondary Nucleation and Accessible Surface in Insulin Amyloid Fibril Formation
inferredcites →https://doi.org/10.1021/jp810972yopenalex-extracted
Self-Organization Pathways and Spatial Heterogeneity in Insulin Amyloid Fibril Formation
inferredcites →https://doi.org/10.1021/jz501614eopenalex-extracted
Observation of the Early Structural Changes Leading to the Formation of Protein Superstructures
inferredcites →https://doi.org/10.1038/nphys3532openalex-extracted
Polymer physics of intracellular phase transitions
inferredcites →https://doi.org/10.1038/nprot.2006.77openalex-extracted
A detergent-based assay for the detection of promiscuous inhibitors
inferredcites →https://doi.org/10.1038/nrm.2017.7openalex-extracted
Biomolecular condensates: organizers of cellular biochemistry
inferredcites →https://doi.org/10.1038/s41467-017-00480-0openalex-extracted
Liquid–liquid phase separation of the microtubule-binding repeats of the Alzheimer-related protein Tau
inferredcites →https://doi.org/10.1038/s41467-020-16580-3openalex-extracted
Liquid-liquid phase separation induces pathogenic tau conformations in vitro
inferredcites →https://doi.org/10.1038/s41467-021-21181-9openalex-extracted
Reentrant liquid condensate phase of proteins is stabilized by hydrophobic and non-ionic interactions
inferredcites →https://doi.org/10.1038/s41467-021-24727-zopenalex-extracted
A multi-step nucleation process determines the kinetics of prion-like domain phase separation
inferredcites →https://doi.org/10.1038/s41467-021-26532-0openalex-extracted
Sustained enzymatic activity and flow in crowded protein droplets
inferredcites →https://doi.org/10.1038/s41467-022-33545-wopenalex-extracted
Hydrogen-bonds mediate liquid-liquid phase separation of mussel derived adhesive peptides
inferredcites →https://doi.org/10.1038/s41565-020-0731-4openalex-extracted
Biomolecular condensates undergo a generic shear-mediated liquid-to-solid transition
inferredcites →https://doi.org/10.1038/s41570-019-0120-4openalex-extracted
The synergic effect of water and biomolecules in intracellular phase separation
inferredcites →https://doi.org/10.1038/s41583-019-0222-5openalex-extracted
Stress granules and neurodegeneration
inferredcites →https://doi.org/10.1038/s41594-019-0250-xopenalex-extracted
Molecular interactions underlying liquid−liquid phase separation of the FUS low-complexity domain
inferredcites →https://doi.org/10.1038/s41598-017-02237-7openalex-extracted
Thioflavin T fluoresces as excimer in highly concentrated aqueous solutions and as monomer being incorporated in amyloid fibrils
inferredcites →https://doi.org/10.1038/s42003-020-01596-8openalex-extracted
A generic approach to study the kinetics of liquid–liquid phase separation under near-native conditions
inferredcites →https://doi.org/10.1038/s42003-022-03699-wopenalex-extracted
Solution structure of recombinant Pvfp-5β reveals insights into mussel adhesion
inferredcites →https://doi.org/10.1038/s42004-020-0328-8openalex-extracted
Dehydration entropy drives liquid-liquid phase separation by molecular crowding
inferredcites →https://doi.org/10.1039/c1lc20582jopenalex-extracted
Surfactants in droplet-based microfluidics
inferredcites →https://doi.org/10.1039/c6lc01072eopenalex-extracted
Monitoring few molecular binding events in scalable confined aqueous compartments by raster image correlation spectroscopy (CADRICS)
inferredcites →https://doi.org/10.1039/c6sm01837hopenalex-extracted
Kinetics of liquid–liquid phase separation in protein solutions exhibiting LCST phase behavior studied by time-resolved USAXS and VSANS
inferredcites →https://doi.org/10.1039/c7sm01434aopenalex-extracted
Arrested and temporarily arrested states in a protein–polymer mixture studied by USAXS and VSANS
inferredcites →https://doi.org/10.1042/bst0370682openalex-extracted
Protein aggregation: more than just fibrils
inferredcites →https://doi.org/10.1063/5.0125452openalex-extracted
Polymorphic protein phase transitions driven by surface anisotropy
inferredcites →https://doi.org/10.1073/pnas.1218402110openalex-extracted
Proliferation of amyloid-β42 aggregates occurs through a secondary nucleation mechanism
inferredcites →https://doi.org/10.1073/pnas.1916716117openalex-extracted
Liquid–liquid phase separation of type II diabetes-associated IAPP initiates hydrogelation and aggregation
inferredcites →https://doi.org/10.1073/pnas.2109718119openalex-extracted
Adsorption free energy predicts amyloid protein nucleation rates
inferredcites →https://doi.org/10.1074/jbc.ra118.007222openalex-extracted
The role of liquid–liquid phase separation in aggregation of the TDP-43 low-complexity domain
inferredcites →https://doi.org/10.1074/jbc.tm118.001192openalex-extracted
The molecular language of membraneless organelles
inferredcites →https://doi.org/10.1103/physreve.56.r67openalex-extracted
Relation between the phase separation and the crystallization in protein solutions
inferredcites →https://doi.org/10.1103/physreve.59.2222openalex-extracted
Multiple interactions between molecular and supramolecular ordering
inferredcites →https://doi.org/10.1110/ps.9.10.1960openalex-extracted
Formation of insulin amyloid fibrils followed by FTIR simultaneously with CD and electron microscopy
inferredcites →https://doi.org/10.1146/annurev-cellbio-100913-013325openalex-extracted
Liquid-Liquid Phase Separation in Biology
inferredcites →https://doi.org/10.1371/journal.pone.0136602openalex-extracted
pH-Driven Polymorphism of Insulin Amyloid-Like Fibrils
inferredcites →https://doi.org/10.15252/embj.201593517openalex-extracted
Droplet organelles?
inferredcites →https://doi.org/10.1529/biophysj.104.051896openalex-extracted
The Mechanism of Amyloid Spherulite Formation by Bovine Insulin
inferredcites →https://doi.org/10.1529/biophysj.106.094342openalex-extracted
Protein Particulates: Another Generic Form of Protein Aggregation?
inferredcites →https://doi.org/10.1529/biophysj.107.110577openalex-extracted
Protein Aggregation/Crystallization and Minor Structural Changes: Universal versus Specific Aspects
inferredcites →https://doi.org/10.1529/biophysj.107.120154openalex-extracted
The Phasor Approach to Fluorescence Lifetime Imaging Analysis
inferredcites →https://doi.org/10.3390/molecules26247590openalex-extracted
Near-Wall Aggregation of Amyloidogenic Aβ 1-40 Peptide: Direct Observation by the FRET
Editorial review for independent work. ICSAC — the Institute for Complexity Science and Advanced Computing — runs a structured editorial panel for researchers publishing outside journals, and publishes on CiteStamp rails. Submission is free and goes through ORCID: icsacinstitute.org/submit.