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Disassembly and Reassembly of Amyloid Fibrils in Water−Ethanol Mixtures
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1002/anie.200703133openalex-snapshot
Amyloids: Not Only Pathological Agents but Also Ordered Nanomaterials
inferredcites →https://doi.org/10.1002/cyto.a.20105openalex-snapshot
Interactive measurement and characterization of DNA molecules by analysis of AFM images
inferredcites →https://doi.org/10.1006/jsbi.2000.4221openalex-snapshot
Review: History of the Amyloid Fibril
inferredcites →https://doi.org/10.1007/s00109-003-0464-5openalex-snapshot
Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution
inferredcites →https://doi.org/10.1016/j.bpj.2009.11.052openalex-snapshot
Detection of Populations of Amyloid-Like Protofibrils with Different Physical Properties
inferredcites →https://doi.org/10.1016/j.jmb.2008.06.043openalex-snapshot
β-Lactoglobulin Assembles into Amyloid through Sequential Aggregated Intermediates
inferredcites →https://doi.org/10.1016/s0021-9258(18)94333-4openalex-snapshot
The Reliability of Molecular Weight Determinations by Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis
inferredcites →https://doi.org/10.1016/s0065-3233(08)60320-4openalex-snapshot
The Structure of Amyloid Fibrils by Electron Microscopy and X-Ray Diffraction
inferredcites →https://doi.org/10.1016/s0958-1669(98)80109-2openalex-snapshot
Refolding of recombinant proteins
inferredcites →https://doi.org/10.1016/s0968-0004(99)01445-0openalex-snapshot
Protein misfolding, evolution and disease
inferredcites →https://doi.org/10.1016/s0968-0896(98)00219-3openalex-snapshot
Alcohol-induced denaturation of β-lactoglobulin: a close correlation to the alcohol-induced α-helix formation of melittin
inferredcites →https://doi.org/10.1016/s1359-0278(97)00023-0openalex-snapshot
Conformational transitions provoked by organic solvents in β-lactoglobulin: can a molten globule like intermediate be induced by the decrease in dielectric constant?
inferredcites →https://doi.org/10.1021/bi027166sopenalex-snapshot
Conformational Behavior and Aggregation of α-Synuclein in Organic Solvents: Modeling the Effects of Membranes
inferredcites →https://doi.org/10.1021/bm049659dopenalex-snapshot
Fibrillar β-Lactoglobulin Gels: Part 1. Fibril Formation and Structure
inferredcites →https://doi.org/10.1021/bm7014224openalex-snapshot
Peptides are Building Blocks of Heat-Induced Fibrillar Protein Aggregates of β-Lactoglobulin Formed at pH 2
inferredcites →https://doi.org/10.1021/bm800502jopenalex-snapshot
Structure of Heat-Induced β-Lactoglobulin Aggregates and their Complexes with Sodium-Dodecyl Sulfate
inferredcites →https://doi.org/10.1021/jf0261396openalex-snapshot
A New Multistep Ca2+-Induced Cold Gelation Process for β-Lactoglobulin
inferredcites →https://doi.org/10.1021/jf060606sopenalex-snapshot
Fibril Assemblies in Aqueous Whey Protein Mixtures
inferredcites →https://doi.org/10.1021/jf801383mopenalex-snapshot
Ethanol Effect on the Structure of β-Lactoglobulin B and Its Ligand Binding
inferredcites →https://doi.org/10.1021/jf9042908openalex-snapshot
Characterization of β-Lactoglobulin Fibrillar Assembly Using Atomic Force Microscopy, Polyacrylamide Gel Electrophoresis, and in Situ Fourier Transform Infrared Spectroscopy
inferredcites →https://doi.org/10.1021/jp064861ropenalex-snapshot
Amyloid Fibril Formation and Other Aggregate Species Formed by Human Serum Albumin Association
inferredcites →https://doi.org/10.1021/la035390sopenalex-snapshot
Mesoscopic Properties of Semiflexible Amyloid Fibrils
inferredcites →https://doi.org/10.1021/la9021432openalex-snapshot
Liquid Crystalline Phase Behavior of Protein Fibers in Water: Experiments versus Theory
inferredcites →https://doi.org/10.1038/1831202a0openalex-snapshot
Electron Microscopic Observations on a Fibrous Component in Amyloid of Diverse Origins
inferredcites →https://doi.org/10.1038/227680a0openalex-snapshot
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
inferredcites →https://doi.org/10.1038/nmat1496openalex-snapshot
Understanding foods as soft materials
inferredcites →https://doi.org/10.1038/nnano.2010.59openalex-snapshot
Understanding amyloid aggregation by statistical analysis of atomic force microscopy images
inferredcites →https://doi.org/10.1039/b502255jopenalex-snapshot
Template-controlled conformational patterns of insulin fibrillar self-assembly reflect history of solvation of the amyloid nuclei
inferredcites →https://doi.org/10.1042/bss0680001openalex-snapshot
Protein folding and its links with human disease
inferredcites →https://doi.org/10.1073/pnas.96.18.9989openalex-snapshot
Amyloid diseases: Abnormal protein aggregation in neurodegeneration
inferredcites →https://doi.org/10.1093/emboj/18.4.815openalex-snapshot
Cryo‐electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing
inferredcites →https://doi.org/10.1110/ps.0217702openalex-snapshot
A kinetic study of β‐lactoglobulin amyloid fibril formation promoted by urea
inferredcites →https://doi.org/10.1110/ps.9.2.369openalex-snapshot
Amyloid protofilament formation of hen egg lysozyme in highly concentrated ethanol solution
inferredcites →https://doi.org/10.1126/science.1150057openalex-snapshot
Role of Intermolecular Forces in Defining Material Properties of Protein Nanofibrils
inferredcites →https://doi.org/10.1146/annurev.biochem.75.101304.123901openalex-snapshot
Protein Misfolding, Functional Amyloid, and Human Disease
inferredcites →https://doi.org/10.1529/biophysj.105.068726openalex-snapshot
Amyloid Fibril Formation Can Proceed from Different Conformations of a Partially Unfolded Protein
inferredcites →https://doi.org/10.3168/jds.s0022-0302(04)73222-1openalex-snapshot
Invited Review: β-Lactoglobulin: Binding Properties, Structure, and Function
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.4667728openalex-extracted
Comparison of Morphological and Mechanical Properties of Hen Egg White Lysozyme (Hewl) Amyloid Fibrils Incubated Under Acidic and Neutral Environments
inferred← citeshttps://doi.org/10.1002/adfm.201502506openalex-snapshot
Motif‐Designed Peptide Nanofibers Decorated with Graphene Quantum Dots for Simultaneous Targeting and Imaging of Tumor Cells
inferred← citeshttps://doi.org/10.1002/admi.201600895openalex-snapshot
Sequence‐Designed Peptide Nanofibers Bridged Conjugation of Graphene Quantum Dots with Graphene Oxide for High Performance Electrochemical Hydrogen Peroxide Biosensor
inferred← citeshttps://doi.org/10.1002/advs.202310314openalex-snapshot
Remediation of Metal Oxide Nanotoxicity with a Functional Amyloid
inferred← citeshttps://doi.org/10.1002/bip.22992openalex-snapshot
Nano‐mechanical characterization of disassembling amyloid fibrils using the P eak F orce QNM method
inferred← citeshttps://doi.org/10.1002/mabi.202200294openalex-snapshot
Photoinduced Amyloid Fibril Degradation for Controlled Cell Patterning
inferred← citeshttps://doi.org/10.1016/b978-0-12-394431-3.00031-6openalex-snapshot
Structural Basis for the Polymorphism of β-Lactoglobulin Amyloid-Like Fibrils
inferred← citeshttps://doi.org/10.1016/b978-0-12-394431-3.00032-8openalex-snapshot
Fibrillation and Polymorphism of Human Serum Albumin
inferred← citeshttps://doi.org/10.1016/b978-0-12-405171-3.00007-6openalex-snapshot
Structure and Stability of Whey Proteins
inferred← citeshttps://doi.org/10.1016/b978-0-12-815251-5.00007-4openalex-snapshot
Structure and stability of whey proteins
inferred← citeshttps://doi.org/10.1016/j.abb.2019.02.001openalex-snapshot
Atomic force microscopy for single molecule characterisation of protein aggregation
inferred← citeshttps://doi.org/10.1016/j.bpj.2015.03.021openalex-snapshot
A Kinetic Study of Ovalbumin Fibril Formation: The Importance of Fragmentation and End-Joining
inferred← citeshttps://doi.org/10.1016/j.cis.2019.05.002openalex-snapshot
Food protein amyloid fibrils: Origin, structure, formation, characterization, applications and health implications
inferred← citeshttps://doi.org/10.1016/j.cis.2025.103596openalex-snapshot
Fibrous protein gels: Nanoscale features governing gelation behavior and gel properties
inferred← citeshttps://doi.org/10.1016/j.cocis.2012.08.001openalex-snapshot
Study of amyloid fibrils via atomic force microscopy
inferred← citeshttps://doi.org/10.1016/j.foodchem.2024.141849openalex-snapshot
Amyloid fibrils for β-carotene delivery – Influence of self-assembled structures on binding and in vitro release behavior
inferred← citeshttps://doi.org/10.1016/j.foodchem.2024.142559openalex-snapshot
Plant-based protein amyloid fibrils: Origins, formation, extraction, applications, and safety
inferred← citeshttps://doi.org/10.1016/j.foodchem.2025.147470openalex-snapshot
Preparations, characterizations, assembly behaviors, applications, and perspectives of whey protein amyloid fibrils: A review
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2020.106573openalex-snapshot
Flexible protein nanofibrils fabricated in aqueous ethanol: Physical characteristics and properties of forming emulsions of conjugated linolenic acid
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2021.107301openalex-snapshot
Engineering amyloid and amyloid-like morphologies of β-lactoglobulin
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2026.113132openalex-snapshot
The influence of ethanol on the self-assembly behavior, structural characteristics and mechanism of whey protein nanofibrils
inferred← citeshttps://doi.org/10.1016/j.foodres.2020.109856openalex-snapshot
The role of amyloid fibrils in the modification of whey protein isolate gels with the form of stranded and particulate microstructures
inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2015.11.055openalex-snapshot
Insight into the co-solvent induced conformational changes and aggregation of bovine β-lactoglobulin
inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2020.11.055openalex-snapshot
WITHDRAWN: Reinforcing the rheological and mechanical properties of WPI nanocomposite hydrogels with birefringence morphologies
inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2022.06.182openalex-snapshot
A new fibrillization mechanism of β-lactoglobulin in glycine solutions
inferred← citeshttps://doi.org/10.1016/j.polymer.2013.02.029openalex-snapshot
Amyloids: From molecular structure to mechanical properties
inferred← citeshttps://doi.org/10.1021/acs.biochem.2c00143openalex-snapshot
Spontaneous Refolding of Amyloid Fibrils from One Polymorph to Another Caused by Changes in Environmental Hydrophobicity
inferred← citeshttps://doi.org/10.1021/acs.biomac.1c01597openalex-snapshot
Lysozyme Amyloid Fibril-Integrated PEG Injectable Hydrogel Adhesive with Improved Antiswelling and Antibacterial Capabilities
inferred← citeshttps://doi.org/10.1021/acs.biomac.2c01142openalex-snapshot
Green Ambient-Dried Aerogels with a Facile pH-Tunable Surface Charge for Adsorption of Cationic and Anionic Contaminants with High Selectivity
inferred← citeshttps://doi.org/10.1021/acs.jpcb.5c04696openalex-snapshot
Transition of Structurally Distinct Amyloids in the Degradation of Protein Materials
inferred← citeshttps://doi.org/10.1021/acs.langmuir.4c00438openalex-snapshot
Controlling Solvent Polarity to Regulate Protein Self-Assembly Morphology and Its Universal Insight for Fibrillation Mechanism
inferred← citeshttps://doi.org/10.1021/acsnano.4c04758openalex-snapshot
Interfacial Protein Fibril Polymorphisms Regulate In Vivo Adipose Expansion for Control of Obesity
inferred← citeshttps://doi.org/10.1021/bm200216uopenalex-snapshot
General Self-Assembly Mechanism Converting Hydrolyzed Globular Proteins Into Giant Multistranded Amyloid Ribbons
inferred← citeshttps://doi.org/10.1021/bm200686ropenalex-snapshot
Complexation of β-Lactoglobulin Fibrils and Sulfated Polysaccharides
inferred← citeshttps://doi.org/10.1021/bm3016994openalex-snapshot
Different Fates of Alzheimer’s Disease Amyloid-β Fibrils Remodeled by Biocompatible Small Molecules
inferred← citeshttps://doi.org/10.1021/bm401646xopenalex-snapshot
Engineered Lysozyme Amyloid Fibril Networks Support Cellular Growth and Spreading
inferred← citeshttps://doi.org/10.1021/ja206513ropenalex-snapshot
Morphology and Persistence Length of Amyloid Fibrils Are Correlated to Peptide Molecular Structure
inferred← citeshttps://doi.org/10.1021/jf300367kopenalex-snapshot
Whey Protein Nanofibrils: The Environment–Morphology–Functionality Relationship in Lyophilization, Rehydration, and Seeding
inferred← citeshttps://doi.org/10.1021/jf403723mopenalex-snapshot
Modulation of the Gelation Efficiency of Fibrillar and Spherical Aggregates by Means of Thiolation
inferred← citeshttps://doi.org/10.1021/nn404886kopenalex-snapshot
Polymorphism Complexity and Handedness Inversion in Serum Albumin Amyloid Fibrils
inferred← citeshttps://doi.org/10.1039/c1sm05382eopenalex-snapshot
Adjustable twisting periodic pitch of amyloid fibrils
inferred← citeshttps://doi.org/10.1039/c1sm06643aopenalex-snapshot
Inhibiting, promoting, and preserving stability of functional proteinfibrils
inferred← citeshttps://doi.org/10.1039/c2fd20031gopenalex-snapshot
Stability of aqueous food grade fibrillar systems against pH change
inferred← citeshttps://doi.org/10.1039/c2sm06762eopenalex-snapshot
Hydration effects on the fibrillation process of a globular protein: the case of human serum albumin
inferred← citeshttps://doi.org/10.1039/c3fd00083dopenalex-snapshot
Polymorphism in bovine serum albumin fibrils: morphology and statistical analysis
inferred← citeshttps://doi.org/10.1039/c4nr04624bopenalex-snapshot
Stability and cytotoxicity of crystallin amyloid nanofibrils
inferred← citeshttps://doi.org/10.1039/c5ra08923aopenalex-snapshot
Modulation of bovine serum albumin fibrillation by ester bonded and conventional gemini surfactants
inferred← citeshttps://doi.org/10.1039/c6nr02665fopenalex-snapshot
The persistence length of adsorbed dendronized polymers
inferred← citeshttps://doi.org/10.1039/c6ra16690copenalex-snapshot
Back to the oligomeric state: pH-induced dissolution of concanavalin A amyloid-like fibrils into non-native oligomers
inferred← citeshttps://doi.org/10.1039/c7ra10981dopenalex-snapshot
On the role of peptide hydrolysis for fibrillation kinetics and amyloid fibril morphology
inferred← citeshttps://doi.org/10.1039/c8cc08432gopenalex-snapshot
Sheet-like and tubular aggregates of protein nanofibril–phosphate hybrids
inferred← citeshttps://doi.org/10.1039/c9cc04139gopenalex-snapshot
Amyloid fibrils from organic solutions of an amphiphilic dipeptide
inferred← citeshttps://doi.org/10.1039/c9sm01826copenalex-snapshot
Creating gradients of amyloid fibrils from the liquid–liquid interface
inferred← citeshttps://doi.org/10.1063/1.4880121openalex-snapshot
Role of filament annealing in the kinetics and thermodynamics of nucleated polymerization
inferred← citeshttps://doi.org/10.1080/0144235x.2016.1239335openalex-snapshot
Scaling and dimensionality in the chemical kinetics of protein filament formation
inferred← citeshttps://doi.org/10.1080/10717544.2016.1242179openalex-snapshot
Formation of multimeric antibodies for self-delivery of active monomers
inferred← citeshttps://doi.org/10.1088/0034-4885/76/4/046601openalex-snapshot
The self-assembly, aggregation and phase transitions of food protein systems in one, two and three dimensions
inferred← citeshttps://doi.org/10.1088/0953-8984/24/24/243101openalex-snapshot
Nanomechanical properties of single amyloid fibrils
inferred← citeshttps://doi.org/10.1088/0953-8984/25/37/373101openalex-snapshot
Modelling amyloid fibril formation kinetics: mechanisms of nucleation and growth
inferred← citeshttps://doi.org/10.1088/1674-1056/25/1/018701openalex-snapshot
Hierarchical processes in β -sheet peptide self-assembly from the microscopic to the mesoscopic level
inferred← citeshttps://doi.org/10.1088/1674-1056/25/12/128704openalex-snapshot
Modulation of intra- and inter-sheet interactions in short peptide self-assembly by acetonitrile in aqueous solution
inferred← citeshttps://doi.org/10.1088/1674-1056/26/12/128701openalex-snapshot
Anisotropic formation mechanism and nanomechanics for the self-assembly process of cross- β peptides
inferred← citeshttps://doi.org/10.1103/physrevlett.107.238101openalex-snapshot
Sub-Persistence-Length Complex Scaling Behavior in Lysozyme Amyloid Fibrils
inferred← citeshttps://doi.org/10.1103/physrevlett.124.118102openalex-snapshot
Interplay between Confinement and Drag Forces Determine the Fate of Amyloid Fibrils
inferred← citeshttps://doi.org/10.1111/1541-4337.12465openalex-snapshot
Conditions Governing Food Protein Amyloid Fibril Formation. Part II: Milk and Legume Proteins
inferred← citeshttps://doi.org/10.1111/1541-4337.13028openalex-snapshot
Nanofibrils of food‐grade proteins: Formation mechanism, delivery systems, and application evaluation
inferred← citeshttps://doi.org/10.1111/1541-4337.70610openalex-snapshot
Protein Nanofibrils as Emerging Biomaterials for Sustainable Food Packaging: Advances, Challenges, and Future Opportunities
inferred← citeshttps://doi.org/10.1122/1.4802051openalex-snapshot
Shear and dilatational linear and nonlinear subphase controlled interfacial rheology of β-lactoglobulin fibrils and their derivatives
inferred← citeshttps://doi.org/10.1140/epjst/e2013-01825-0openalex-snapshot
Protein adsorption and interfacial rheology interfering in dilatational experiment
inferred← citeshttps://doi.org/10.1142/s0217979215300029openalex-snapshot
Kinetic theory of protein filament growth: Self-consistent methods and perturbative techniques
inferred← citeshttps://doi.org/10.18130/v3kq0topenalex-snapshot
Different Fates of Alzheimer's Disease Amyloid-Beta Fibrils Remodeled by Biocompatible Small Molecules
inferred← citeshttps://doi.org/10.18174/179503openalex-snapshot
Formation and properties of whey protein fibrils
inferred← citeshttps://doi.org/10.2139/ssrn.4874530openalex-snapshot
Amyloid Fibrils for Β- Carotene Delivery – Influence of Self-Assembled Structures on Binding and in Vitro Bioaccessibility
inferred← citeshttps://doi.org/10.2174/0929866521666140320104409openalex-snapshot
Effect of Temperature and Solvent on Fibrillation of Human Serum Albumin
inferred← citeshttps://doi.org/10.2174/0929866526666191104145511openalex-snapshot
Solvent Perturbation of Protein Structures - A Review Study with Lectins
inferred← citeshttps://doi.org/10.3168/jds.2026-28607openalex-snapshot
Invited review: Manufacturing whey protein colloidal particles via liquid antisolvent precipitation method—Particle formation mechanism and ingredient functionality aspects
inferred← citeshttps://doi.org/10.3390/ijms232213970openalex-snapshot
Amyloidogenesis: What Do We Know So Far?
inferred← citeshttps://doi.org/10.3390/molecules25030618openalex-snapshot
Human Serum Albumin Aggregation/Fibrillation and its Abilities to Drugs Binding
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