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Proteins Fibrils from a Polymer Physics Perspective
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Outgoing claims: the papers this work cites, builds on, or argues with.
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Amyloids: Not Only Pathological Agents but Also Ordered Nanomaterials
inferredcites →https://doi.org/10.1002/anie.200805500openalex-snapshot
Helical‐Ribbon Formation by a β‐Amino Acid Modified Amyloid β‐Peptide Fragment
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Nanocelluloses: A New Family of Nature‐Based Materials
inferredcites →https://doi.org/10.1002/anie.201002037openalex-snapshot
Self‐Assembled Organic Nanostructures with Metallic‐Like Stiffness
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Direct Observation of Time‐Resolved Polymorphic States in the Self‐Assembly of End‐Capped Heptapeptides
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Spider Silk and Amyloid Fibrils: A Structural Comparison
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Common core structure of amyloid fibrils by synchrotron X-ray diffraction 1 1Edited by F. E. Cohen
inferredcites →https://doi.org/10.1006/jmbi.2000.3600openalex-snapshot
Chemical dissection and reassembly of amyloid fibrils formed by a peptide fragment of transthyretin11Edited by F. E. Cohen
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Architecture and Polymorphism of Fibrillar Supramolecular Assemblies Produced by in Vitro Aggregation of Human Calcitonin
inferredcites →https://doi.org/10.1007/s100510070127openalex-snapshot
Fibril stability in solutions of twisted -sheet peptides: a new kind of micellization in chiral systems
inferredcites →https://doi.org/10.1016/0378-4371(81)90148-5openalex-snapshot
Liquid-crystalline ordering in the solution of long persistent chains
inferredcites →https://doi.org/10.1016/j.bbapap.2003.12.008openalex-snapshot
Conformational constraints for amyloid fibrillation: the importance of being unfolded
inferredcites →https://doi.org/10.1016/j.bbapap.2005.10.021openalex-snapshot
Probing the pressure–temperature stability of amyloid fibrils provides new insights into their molecular properties
inferredcites →https://doi.org/10.1016/j.biomaterials.2010.11.066openalex-snapshot
Failure of Aβ(1-40) amyloid fibrils under tensile loading
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.bpj.2009.12.4317openalex-snapshot
Alzheimer's Aβ(1-40) Amyloid Fibrils Feature Size-Dependent Mechanical Properties
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β-Lactoglobulin and WPI aggregates: Formation, structure and applications
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Protein aggregation—Pathways and influencing factors
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Atomistic simulation of nanomechanical properties of Alzheimer’s Aβ(1–40) amyloid fibrils under compressive and tensile loading
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Amyloid-mediated synthesis of giant, fluorescent, gold single crystals and their hybrid sandwiched composites driven by liquid crystalline interactions
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Aβ(1-40) Fibril Polymorphism Implies Diverse Interaction Patterns in Amyloid Fibrils
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Biology of Amyloid: Structure, Function, and Regulation
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Functional amyloid – from bacteria to humans
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Ultrastructural Organization of Amyloid Fibrils byAtomic Force Microscopy
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Phase Behavior of Mixtures of Rods (Tobacco Mosaic Virus) and Spheres (Polyethylene Oxide, Bovine Serum Albumin)
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Surface- and Solution-Based Assembly of Amyloid Fibrils for Biomedical and Nanotechnology Applications
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Structural Models of Amyloid‐Like Fibrils
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Novel peptide-based biomaterial scaffolds for tissue engineering
inferredcites →https://doi.org/10.1016/s0268-005x(09)80122-7openalex-snapshot
Fine-stranded and particulate gels of β-lactoglobulin and whey protein at varying pH
inferredcites →https://doi.org/10.1016/s0959-440x(99)00049-4openalex-snapshot
Amyloid fibrillogenesis: themes and variations
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Protein misfolding, evolution and disease
inferredcites →https://doi.org/10.1017/s0033583506004422openalex-snapshot
Are amyloid diseases caused by protein aggregates that mimic bacterial pore-forming toxins?
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The Structural Biology of Protein Aggregation Diseases: Fundamental Questions and Some Answers
inferredcites →https://doi.org/10.1021/bi0485880openalex-snapshot
Stereospecific Amyloid-like Fibril Formation by a Peptide Fragment of β2-Microglobulin
inferredcites →https://doi.org/10.1021/bi100953topenalex-snapshot
Mutations Alter the Geometry and Mechanical Properties of Alzheimer’s Aβ(1−40) Amyloid Fibrils
inferredcites →https://doi.org/10.1021/bi701427qopenalex-snapshot
Peptide Conformation and Supramolecular Organization in Amylin Fibrils: Constraints from Solid-State NMR
inferredcites →https://doi.org/10.1021/bm200216uopenalex-snapshot
General Self-Assembly Mechanism Converting Hydrolyzed Globular Proteins Into Giant Multistranded Amyloid Ribbons
inferredcites →https://doi.org/10.1021/bm2005752openalex-snapshot
Wet-Spinning of Amyloid Protein Nanofibers into Multifunctional High-Performance Biofibers
inferredcites →https://doi.org/10.1021/bm7009224openalex-snapshot
Thermal Dependence of Thermally Induced Protein Spherulite Formation and Growth: Kinetics of β-lactoglobulin and Insulin
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/ja016229bopenalex-snapshot
Preparation and Characterization of Purified Amyloid Fibrils
inferredcites →https://doi.org/10.1021/ja0341642openalex-snapshot
Exploiting Amyloid Fibril Lamination for Nanotube Self-Assembly
inferredcites →https://doi.org/10.1021/ja054721fopenalex-snapshot
Laminated Morphology of Nontwisting β-Sheet Fibrils Constructed via Peptide Self-Assembly
inferredcites →https://doi.org/10.1021/ja0558387openalex-snapshot
Structural Control of Self-Assembled Nanofibers by Artificial β-Sheet Peptides Composed of d - or l -Isomer
inferredcites →https://doi.org/10.1021/ja064455lopenalex-snapshot
The Formation of Nematic Liquid Crystal Phases by Hen Lysozyme Amyloid Fibrils
inferredcites →https://doi.org/10.1021/ja100613wopenalex-snapshot
Direct Observation of Morphological Tranformation from Twisted Ribbons into Helical Ribbons
inferredcites →https://doi.org/10.1021/ja107069fopenalex-snapshot
Unraveling the Mechanism of Nanotube Formation by Chiral Self-Assembly of Amphiphiles
inferredcites →https://doi.org/10.1021/ja710295topenalex-snapshot
De Novo Design of Strand-Swapped β-Hairpin Hydrogels
inferredcites →https://doi.org/10.1021/ja800328yopenalex-snapshot
Chirality of Amyloid Suprastructures
inferredcites →https://doi.org/10.1021/ja8048964openalex-snapshot
Molecular Structure of Self-Assembled Chiral Nanoribbons and Nanotubules Revealed in the Hydrated State
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/jp101374eopenalex-snapshot
Alignment of a Model Amyloid Peptide Fragment in Bulk and at a Solid Surface
inferredcites →https://doi.org/10.1021/jp102744gopenalex-snapshot
Influence of Salt on the Self-Assembly of Two Model Amyloid Heptapeptides
inferredcites →https://doi.org/10.1021/jp111168sopenalex-snapshot
Influence of End-Capping on the Self-Assembly of Model Amyloid Peptide Fragments
inferredcites →https://doi.org/10.1021/jp8078259openalex-snapshot
Factors That Affect the Degree of Twist in β-Sheet Structures: A Molecular Dynamics Simulation Study of a Cross-β Filament of the GNNQQNY Peptide
inferredcites →https://doi.org/10.1021/la035390sopenalex-snapshot
Mesoscopic Properties of Semiflexible Amyloid Fibrils
inferredcites →https://doi.org/10.1021/la101636ropenalex-snapshot
Effects of Charge Double Layer and Colloidal Aggregation on the Isotropic−Nematic Transition of Protein Fibers in Water
inferredcites →https://doi.org/10.1021/la102721mopenalex-snapshot
Interfacial Activity and Interfacial Shear Rheology of Native β-Lactoglobulin Monomers and Their Heat-Induced Fibers
inferredcites →https://doi.org/10.1021/la9021432openalex-snapshot
Liquid Crystalline Phase Behavior of Protein Fibers in Water: Experiments versus Theory
inferredcites →https://doi.org/10.1021/ma00162a020openalex-snapshot
Effect of electrostatic interaction on the liquid crystal phase transition in solutions of rodlike polyelectrolytes
inferredcites →https://doi.org/10.1021/ma981689jopenalex-snapshot
Static and Dynamic Scattering of β-Lactoglobulin Aggregates Formed after Heat-Induced Denaturation at pH 2
inferredcites →https://doi.org/10.1021/nl0505896openalex-snapshot
Self-Assembled Peptide Nanotubes Are Uniquely Rigid Bioinspired Supramolecular Structures
inferredcites →https://doi.org/10.1021/nl0731670openalex-snapshot
Geometric Confinement Governs the Rupture Strength of H-bond Assemblies at a Critical Length Scale
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/nature03109openalex-snapshot
Equilibrium cluster formation in concentrated protein solutions and colloids
inferredcites →https://doi.org/10.1038/nature03521openalex-snapshot
Nonlinear elasticity in biological gels
inferredcites →https://doi.org/10.1038/nature03680openalex-snapshot
Structure of the cross-β spine of amyloid-like fibrils
inferredcites →https://doi.org/10.1038/nature03793openalex-snapshot
Correlation of structural elements and infectivity of the HET-s prion
inferredcites →https://doi.org/10.1038/nbt874openalex-snapshot
Fabrication of novel biomaterials through molecular self-assembly
inferredcites →https://doi.org/10.1038/nchembio.131openalex-snapshot
Amyloid formation by globular proteins under native conditions
inferredcites →https://doi.org/10.1038/nmat1496openalex-snapshot
Understanding foods as soft materials
inferredcites →https://doi.org/10.1038/nmat2704openalex-snapshot
Nanoconfinement controls stiffness, strength and mechanical toughness of β-sheet crystals in silk
inferredcites →https://doi.org/10.1038/nnano.2006.139openalex-snapshot
Controlled patterning of aligned self-assembled peptide nanotubes
inferredcites →https://doi.org/10.1038/nnano.2010.26openalex-snapshot
Nanostructured films from hierarchical self-assembly of amyloidogenic proteins
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/10.1038/nnano.2011.102openalex-snapshot
Nanomechanics of functional and pathological amyloid materials
inferredcites →https://doi.org/10.1039/b605536mopenalex-snapshot
Self-assembled peptide nanostructures: the design of molecular building blocks and their technological utilization
inferredcites →https://doi.org/10.1039/b914089aopenalex-snapshot
Shear-induced structure and mechanics of β-lactoglobulin amyloid fibrils
inferredcites →https://doi.org/10.1039/c0cc05126hopenalex-snapshot
New biocompatible thermo-reversible hydrogels from PNiPAM-decorated amyloid fibrils
inferredcites →https://doi.org/10.1039/c0sm00502aopenalex-snapshot
Snapshots of fibrillation and aggregation kinetics in multistranded amyloid β-lactoglobulin fibrils
inferredcites →https://doi.org/10.1039/c0sm01253jopenalex-snapshot
A supramolecular bottle-brush approach to disassemble amyloid fibrils
inferredcites →https://doi.org/10.1039/c0sm01339kopenalex-snapshot
Templating effects of lyotropic liquid crystals in the encapsulation of amyloid fibrils and their stimuli-responsive magnetic behavior
inferredcites →https://doi.org/10.1039/c1sm05382eopenalex-snapshot
Adjustable twisting periodic pitch of amyloid fibrils
inferredcites →https://doi.org/10.1039/c1sm05602fopenalex-snapshot
Unravelling adsorption and alignment of amyloid fibrils at interfaces by probe particle tracking
inferredcites →https://doi.org/10.1039/c1sm06643aopenalex-snapshot
Inhibiting, promoting, and preserving stability of functional proteinfibrils
inferredcites →https://doi.org/10.1042/bst0370682openalex-snapshot
Protein aggregation: more than just fibrils
inferredcites →https://doi.org/10.1063/1.3589369openalex-snapshot
Single-step direct measurement of amyloid fibrils stiffness by peak force quantitative nanomechanical atomic force microscopy
inferredcites →https://doi.org/10.1073/pnas.0406847102openalex-snapshot
Molecular basis for amyloid fibril formation and stability
inferredcites →https://doi.org/10.1073/pnas.0506723102openalex-snapshot
3D structure of Alzheimer's amyloid-β(1–42) fibrils
inferredcites →https://doi.org/10.1073/pnas.0604035103openalex-snapshot
Characterization of the nanoscale properties of individual amyloid fibrils
inferredcites →https://doi.org/10.1073/pnas.0806270105openalex-snapshot
Molecular structural basis for polymorphism in Alzheimer's β-amyloid fibrils
inferredcites →https://doi.org/10.1073/pnas.0901422106openalex-snapshot
Ultrasonication-dependent production and breakdown lead to minimum-sized amyloid fibrils
inferredcites →https://doi.org/10.1073/pnas.0907821106openalex-snapshot
Measurement of amyloid fibril mass-per-length by tilted-beam transmission electron microscopy
inferredcites →https://doi.org/10.1073/pnas.1008353107openalex-snapshot
Phase behavior of mixtures of human lens proteins Gamma D and Beta B1
inferredcites →https://doi.org/10.1073/pnas.1017658108openalex-snapshot
Shape selection of twist-nematic-elastomer ribbons
inferredcites →https://doi.org/10.1073/pnas.142459399openalex-snapshot
The protofilament structure of insulin amyloid fibrils
inferredcites →https://doi.org/10.1073/pnas.191250198openalex-snapshot
Hierarchical self-assembly of chiral rod-like molecules as a model for peptide β-sheet tapes, ribbons, fibrils, and fibers
inferredcites →https://doi.org/10.1073/pnas.262663499openalex-snapshot
A structural model for Alzheimer's β-amyloid fibrils based on experimental constraints from solid state NMR
inferredcites →https://doi.org/10.1073/pnas.96.7.3590openalex-snapshot
Designing conditions for in vitro formation of amyloid protofilaments and fibrils
inferredcites →https://doi.org/10.1073/pnas.97.12.6728openalex-snapshot
Extensive neurite outgrowth and active synapse formation on self-assembling peptide scaffolds
inferredcites →https://doi.org/10.1074/jbc.r111.227108openalex-snapshot
Structural Insights into Functional and Pathological Amyloid
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Phase transitions in lyotropic colloidal and polymer liquid crystals
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Cryo‐electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing
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Correlation of polymer persistence length with Euler buckling fluctuations
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Isotropic-cholesteric phase transition of filamentous virus suspensions as a function of rod length and charge
inferredcites →https://doi.org/10.1103/physrevlett.101.148103openalex-snapshot
Conformation of Circular DNA in Two Dimensions
inferredcites →https://doi.org/10.1103/physrevlett.107.238101openalex-snapshot
Sub-Persistence-Length Complex Scaling Behavior in Lysozyme Amyloid Fibrils
inferredcites →https://doi.org/10.1103/physrevlett.63.2068openalex-snapshot
Isotropic-nematic phase transition and angular correlations in isotropic suspensions of tobacco mosaic virus
inferredcites →https://doi.org/10.1103/physrevlett.99.198103openalex-snapshot
New Insight into Cataract Formation: Enhanced Stability through Mutual Attraction
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Use of biomolecular templates for the fabrication of metal nanowires
inferredcites →https://doi.org/10.1126/science.1067122openalex-snapshot
Toxic Proteins in Neurodegenerative Disease
inferredcites →https://doi.org/10.1126/science.1067484openalex-snapshot
Role of Escherichia coli Curli Operons in Directing Amyloid Fiber Formation
inferredcites →https://doi.org/10.1126/science.1105850openalex-snapshot
Self-Propagating, Molecular-Level Polymorphism in Alzheimer's ß-Amyloid Fibrils
inferredcites →https://doi.org/10.1126/science.1150057openalex-snapshot
Role of Intermolecular Forces in Defining Material Properties of Protein Nanofibrils
inferredcites →https://doi.org/10.1126/science.1173155openalex-snapshot
Functional Amyloids As Natural Storage of Peptide Hormones in Pituitary Secretory Granules
inferredcites →https://doi.org/10.1126/science.1176009openalex-snapshot
The Extracellular Matrix: Not Just Pretty Fibrils
inferredcites →https://doi.org/10.1126/science.1203874openalex-snapshot
Geometry and Mechanics in the Opening of Chiral Seed Pods
inferredcites →https://doi.org/10.1146/annurev-cellbio-100109-104020openalex-snapshot
Assembly of Fibronectin Extracellular Matrix
inferredcites →https://doi.org/10.1146/annurev-physchem-032210-103539openalex-snapshot
Solid-State NMR Studies of Amyloid Fibril Structure
inferredcites →https://doi.org/10.1146/annurev.biochem.75.101304.123901openalex-snapshot
Protein Misfolding, Functional Amyloid, and Human Disease
inferredcites →https://doi.org/10.1146/annurev.biochem.77.032207.120833openalex-snapshot
Collagen Structure and Stability
inferredcites →https://doi.org/10.1146/annurev.bioeng.4.092801.094202openalex-snapshot
Peptide Aggregation in Neurodegenerative Disease
inferredcites →https://doi.org/10.1146/annurev.micro.60.080805.142106openalex-snapshot
Curli Biogenesis and Function
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P ROTOFIBRILS , P ORES , F IBRILS, AND N EURODEGENERATION : Separating the Responsible Protein Aggregates from The Innocent Bystanders
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Amyloid as a Depot for the Formulation of Long-Acting Drugs
inferredcites →https://doi.org/10.1515/arh-2006-0018openalex-snapshot
Ca2+-Induced Cold-Set Gelation of Whey Protein Isolate Fibrils
inferredcites →https://doi.org/10.1529/biophysj.106.097535openalex-snapshot
The Formation of Fibrils by Intertwining of Filaments: Model and Application to Amyloid Aβ Protein
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Geometric confinement governs the rupture strength of H-bond assemblies at a critical length scale
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
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Evolution of Conformation, Nanomechanics, and Infrared Nanospectroscopy of Single Amyloid Fibrils Converting into Microcrystals
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Charge‐Induced Secondary Structure Transformation of Amyloid‐Derived Dipeptide Assemblies from β‐Sheet to α‐Helix
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Amyloid Polymorphism in the Protein Folding and Aggregation Energy Landscape
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Amyloid Aggregation of Bacillus circulans Xylanase under Native Conditions and its Modulation by β‐Amyloid‐Derived Peptide Fragments
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Thio‐Bromo “Click” Reaction Derived Polymer–Peptide Conjugates for Their Self‐Assembled Fibrillar Nanostructures
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The Past 40 Years of Macromolecular Sciences: Reflections on Challenges in Synthetic Polymer and Material Science
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Polymer physics inspired approaches for the study of the mechanical properties of amyloid fibrils
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A brief overview of amyloids and Alzheimer's disease
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Lipid‐induced polymorphic amyloid fibril formation by α‐synuclein
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Fibril Synthesis From Food Processing By‐Products and Strategies for Structure–Function Stabilization for Food Applications
inferred← citeshttps://doi.org/10.1007/978-1-4939-2205-5_20openalex-snapshot
Insoluble Protein Assemblies Characterized by Fourier Transform Infrared Spectroscopy
inferred← citeshttps://doi.org/10.1007/978-3-030-41464-1_9openalex-snapshot
Nanotechnology in Early Detection and Treatment of Amyloidosis
inferred← citeshttps://doi.org/10.1007/978-3-319-17344-3_6openalex-snapshot
Interactions of Lipid Membranes with Fibrillar Protein Aggregates
inferred← citeshttps://doi.org/10.1007/s11483-026-10172-2openalex-snapshot
Coordination of WPI Amyloid Fibrils/Hydrolysates with Zinc and Copper Ions: A Comparative Study on the Effect of Accompanying Anion
inferred← citeshttps://doi.org/10.1007/s12551-016-0233-7openalex-snapshot
Measurement of amyloid formation by turbidity assay—seeing through the cloud
inferred← citeshttps://doi.org/10.1016/b978-0-08-100596-5.00940-9openalex-snapshot
β-Lactoglobulin: Nomenclature, Structure, and Function
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/b978-0-12-404610-8.00001-3openalex-snapshot
Understanding Food Structures
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/b978-0-443-27648-4.00021-9openalex-snapshot
Functional properties of whey proteins in food formulation
inferred← citeshttps://doi.org/10.1016/bs.apcsb.2014.06.006openalex-snapshot
Stability of Amyloid Oligomers
inferred← citeshttps://doi.org/10.1016/j.actbio.2014.01.019openalex-snapshot
Learning from nature – Novel synthetic biology approaches for biomaterial design
inferred← citeshttps://doi.org/10.1016/j.bbrc.2023.149307openalex-snapshot
Interaction of gallium, indium, and vanadyl curcumin complexes with hen egg-white lysozyme (HEWL): Mechanistic aspects and evaluation of antiamyloidogenic activity
inferred← citeshttps://doi.org/10.1016/j.bbrc.2024.150008openalex-snapshot
Von-Hippel Lindau protein amyloid formation. The role of GST-tag
inferred← citeshttps://doi.org/10.1016/j.biomaterials.2022.121455openalex-snapshot
Structure remodeling of soy protein-derived amyloid fibrils mediated by epigallocatechin-3-gallate
inferred← citeshttps://doi.org/10.1016/j.biomaterials.2022.121600openalex-snapshot
The kinetic mechanism of cations induced protein nanotubes self-assembly and their application as delivery system
inferred← citeshttps://doi.org/10.1016/j.bpc.2022.106830openalex-snapshot
Lipid membrane-mediated assembly of the functional amyloid-forming peptide Somatostatin-14
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.cocis.2013.03.001openalex-snapshot
Controlled food protein aggregation for new functionality
inferred← citeshttps://doi.org/10.1016/j.cocis.2018.08.004openalex-snapshot
Liquid crystalline filamentous biological colloids: Analogies and differences
inferred← citeshttps://doi.org/10.1016/j.colsurfa.2025.137212openalex-snapshot
Improve the bioaccessibility of curcumin encapsulated in Pickering emulsions stabilized by double fibrils
inferred← citeshttps://doi.org/10.1016/j.colsurfb.2014.12.008openalex-snapshot
Oligomers, protofibrils and amyloid fibrils from recombinant human lysozyme (rHL): Fibrillation process and cytotoxicity evaluation for ARPE-19 cell line
inferred← citeshttps://doi.org/10.1016/j.colsurfb.2016.07.024openalex-snapshot
On the adsorption of magnetite nanoparticles on lysozyme amyloid fibrils
inferred← citeshttps://doi.org/10.1016/j.colsurfb.2019.110459openalex-snapshot
High internal phase emulsions stabilized with amyloid fibrils and their polysaccharide complexes for encapsulation and protection of β-carotene
inferred← citeshttps://doi.org/10.1016/j.foodchem.2024.141745openalex-snapshot
Gelling ability and gel structure of soy protein isolate influenced by heating in the presence of various acids
inferred← citeshttps://doi.org/10.1016/j.foodchem.2024.141746openalex-snapshot
Fabrication and characterization of lysozyme fibrils/Zein complexes for resveratrol encapsulation: Improving stability, antioxidant and antibacterial activities
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.2025.147470openalex-snapshot
Preparations, characterizations, assembly behaviors, applications, and perspectives of whey protein amyloid fibrils: A review
inferred← citeshttps://doi.org/10.1016/j.foodchem.2026.150464openalex-snapshot
The self-assembly behavior of ovotransferrin nanospheres driven by hydrophobic interaction and their application in astaxanthin fortified almond milk drink
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2014.01.013openalex-snapshot
Soy proteins: A review on composition, aggregation and emulsification
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2017.11.049openalex-snapshot
Calcium-induced gelation of whey protein aggregates: Kinetics, structure and rheological properties
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2018.02.043openalex-snapshot
Acid-induced gelation of whey protein aggregates: Kinetics, gel structure and rheological properties
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2019.105503openalex-snapshot
Pickering emulsions stabilized by amphiphilic anisotropic nanofibrils of glycated whey proteins
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2021.106764openalex-snapshot
Conformational transition and gelation of κ-carrageenan in electrostatic complexation with β-lactoglobulin aggregates
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2021.106789openalex-snapshot
Modification approaches of plant-based proteins to improve their techno-functionality and use in food products
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2021.107180openalex-snapshot
Preparation and evaluation of a novel high internal phase Pickering emulsion based on whey protein isolate nanofibrils derived by hydrothermal method
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2021.107450openalex-snapshot
Colloidal stability of oil-in-water emulsions prepared from hen egg white submitted to dry and/or wet heating to induce amyloid-like fibril formation
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2022.107827openalex-snapshot
Recent advances of interfacial and rheological property based techno-functionality of food protein amyloid fibrils
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2022.108302openalex-snapshot
The gel mechanism and carrier quality of fibrous and granular whey protein self-assembly
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2023.108754openalex-snapshot
Interfacial properties of protein nanofibrils with different morphology prepared using aqueous solvent with ethanol: Part I. preparation and characterization
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2023.108879openalex-snapshot
Interfacial properties of protein nanofibrils with different morphology prepared using aqueous solvent with ethanol: Part II. Effect of oil phase hydrophobicity
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2023.109146openalex-snapshot
Food-derived protein amyloid-like fibrils: Fibrillation mechanism, structure, and recent advances for the stabilization of emulsions
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2023.109604openalex-snapshot
Production and characterization of amaranth amyloid fibrils from food protein waste
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2024.109906openalex-snapshot
Roles of soybean β-conglycinin subunit fractions in fibril formation and the effects of glycinin on them
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2024.109972openalex-snapshot
Enhancing emulsifying properties of lentil protein fibrils through EGCG mediation and the mechanism study
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2024.110074openalex-snapshot
The formation mechanism of β-lactoglobulin self-assembled gel and its relationship with slow-release properties through stepwise regression models
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2024.110582openalex-snapshot
The self-assembly mechanism of ovotransferrin fibrils induced by subtilisin A and Ca2+ ions and their application in nutrient delivery and texture optimization for liquid food
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2024.110659openalex-snapshot
Bromelain hydrolysis and CaCl2 coordination promote the fibrillation of quinoa protein at pH 7
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2024.110749openalex-snapshot
Recent progress of plant protein-based amyloid-like nanofibrils
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2024.111039openalex-snapshot
Myofibrillar protein aggregate evolution regulates interfacial adsorption behavior to maintain long-term stability of high internal phase Pickering emulsions
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2025.111539openalex-snapshot
Protein fibril morphology regulation: An effective strategy for enhancing hydrogel mechanical properties
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2025.111915openalex-snapshot
Synergistic multifaceted effects of tea saponin concentration on the foaming properties of wheat aqueous phase protein: A next-generation approach to food foam production
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2025.112019openalex-snapshot
Fibrillation mechanism of soybean protein isolate and pea protein isolate composites: Focused on structure and rheological properties
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2025.112389openalex-snapshot
Amyloid fibrils creating a novel platform constructing network nanostructures for co-encapsulation of iron and vitamin D3
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2026.112478openalex-snapshot
Elucidating the fibril formation and degradation process of soy protein: identification of fibril-forming regions and insights into the self-assembly mechanism
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2026.112788openalex-snapshot
Accelerated fibrillation and prolonged fibril length of soy protein isolate: Mechanistic insights using a novel protein-glutaminase from Chryseobacterium sediminis
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2026.113031openalex-snapshot
Unveiling the self-assembly mechanism of moringa (Moringa oleifera Lam.) seed protein amyloid fibrils: A multi-scale study integrating peptidomics and artificial intelligence
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2026.113420openalex-snapshot
Fabrication of bioactive hydrogels stabilized by gluten amyloid fibrils and ε-polylysine: Effects of fibril morphology and blending ratios
inferred← citeshttps://doi.org/10.1016/j.foostr.2013.11.001openalex-snapshot
Biopolymer composites for engineering food structures to control product functionality
inferred← citeshttps://doi.org/10.1016/j.foostr.2026.100501openalex-snapshot
Mesoscopic properties of Antarctic krill protein amyloid fibrils described by soft matter physics
inferred← citeshttps://doi.org/10.1016/j.idairyj.2016.09.011openalex-snapshot
β-Lactoglobulin nanofibrils: The long and the short of it
inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2016.06.052openalex-snapshot
Kinetics of protein fibril formation: Methods and mechanisms
inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2020.01.258openalex-snapshot
Formation and physicochemical properties of amyloid fibrils from soy protein
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.ijbiomac.2023.123206openalex-snapshot
Protein-supported transition metal catalysts: Preparation, catalytic applications, and prospects
inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2025.143100openalex-snapshot
Role of amino groups in the structural assembly of β-lactoglobulin nanofibers
inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2026.150804openalex-snapshot
Glycosylation engineering in protein modification: Mechanistic insights, food applications, and potential health risks
inferred← citeshttps://doi.org/10.1016/j.jcis.2023.01.105openalex-snapshot
Flow-induced alignment of protein nanofibril dispersions
inferred← citeshttps://doi.org/10.1016/j.jff.2022.105110openalex-snapshot
Formation of pea protein amyloid fibrils to stabilize high internal phase emulsions for encapsulation of lutein
inferred← citeshttps://doi.org/10.1016/j.lwt.2024.117045openalex-snapshot
Fabrication of mung bean protein isolate nanofibrils and calcium ions induced hydrogels
inferred← citeshttps://doi.org/10.1016/j.molliq.2019.111675openalex-snapshot
Two-step FRET as a tool for probing the amyloid state of proteins
inferred← citeshttps://doi.org/10.1016/j.progpolymsci.2021.101375openalex-snapshot
Recent advances in 3D printing with protein-based inks
inferred← citeshttps://doi.org/10.1016/j.tifs.2017.07.013openalex-snapshot
Globular plant protein aggregates for stabilization of food foams and emulsions
inferred← citeshttps://doi.org/10.1016/j.tifs.2018.03.013openalex-snapshot
Technological functionality and biological properties of food protein nanofibrils formed by heating at acidic condition
inferred← citeshttps://doi.org/10.1016/j.tifs.2026.106035openalex-snapshot
The combination of food protein amyloid nanofibers and polysaccharides: From molecular interactions to hybrid composites and food applications
inferred← citeshttps://doi.org/10.1016/j.ultsonch.2021.105477openalex-snapshot
Ultrasound-assisted Maillard reaction of ovalbumin/xylose: The enhancement of functional properties and its mechanism
inferred← citeshttps://doi.org/10.1017/s0022029919000876openalex-snapshot
Comparative experiments of electrical conductivity from whey protein concentrates conventional film and nanofibril film
inferred← citeshttps://doi.org/10.1021/acs.biomac.3c00284openalex-snapshot
Ion-Induced Reassembly between Protein Nanotubes and Nanospheres
inferred← citeshttps://doi.org/10.1021/acs.biomac.4c00151openalex-snapshot
Multiscale Simulations of Self-Assembling Peptides: Surface and Core Hydrophobicity Determine Fibril Stability and Amyloid Aggregation
inferred← citeshttps://doi.org/10.1021/acs.biomac.4c01564openalex-snapshot
Upcycling of Livestock Industry Blood Waste into Bioplastics: Plasma Protein-Based Amyloid Fibrils
inferred← citeshttps://doi.org/10.1021/acs.biomac.5b00371openalex-snapshot
Ferric Ions Inhibit the Amyloid Fibrillation of β-Lactoglobulin at High Temperature
inferred← citeshttps://doi.org/10.1021/acs.biomac.6b00539openalex-snapshot
Continuous Paranematic Ordering of Rigid and Semiflexible Amyloid-Fe3O4 Hybrid Fibrils in an External Magnetic Field
inferred← citeshttps://doi.org/10.1021/acs.biomac.9b01466openalex-snapshot
Growth, Polymorphism, and Spatially Controlled Surface Immobilization of Biotinylated Variants of IAPP21–27 Fibrils
inferred← citeshttps://doi.org/10.1021/acs.jafc.0c03757openalex-snapshot
Fabrication of Composite Structures of Lysozyme Fibril–Zein using Antisolvent Precipitation: Effects of Blending and pH Adjustment Sequences
inferred← citeshttps://doi.org/10.1021/acs.jafc.1c04615openalex-snapshot
High Internal Phase Emulsions Stabilized with Polyphenol-Amyloid Fibril Supramolecules for Encapsulation and Protection of Lutein
inferred← citeshttps://doi.org/10.1021/acs.jpcb.5b01160openalex-snapshot
Fragmentation of Amyloid Fibrils Occurs in Preferential Positions Depending on the Environmental Conditions
inferred← citeshttps://doi.org/10.1021/acs.jpcb.5b07821openalex-snapshot
Polymorphism of Two-Dimensional Cyanine Dye J-Aggregates and Its Genesis: Fluorescence Microscopy and Atomic Force Microscopy Study
inferred← citeshttps://doi.org/10.1021/acs.jpcb.6b10624openalex-snapshot
Amyloid Fibril Polymorphism: Almost Identical on the Atomic Level, Mesoscopically Very Different
inferred← citeshttps://doi.org/10.1021/acs.jpclett.6b02088openalex-snapshot
Water Rearrangements upon Disorder-to-Order Amyloid Transition
inferred← citeshttps://doi.org/10.1021/acs.langmuir.6b01993openalex-snapshot
Influence of the Protein Particle Morphology and Partitioning on the Behavior of Particle-Stabilized Water-in-Water Emulsions
inferred← citeshttps://doi.org/10.1021/acs.langmuir.7b00112openalex-snapshot
Genetically-Tunable Mechanical Properties of Bacterial Functional Amyloid Nanofibers
inferred← citeshttps://doi.org/10.1021/acs.macromol.0c01975openalex-snapshot
Side-Chain Length Dependence of Young’s Modulus and Strength in Crystalline Poly(3-alkylthiophene) Nanofibers
inferred← citeshttps://doi.org/10.1021/acs.macromol.5b02158openalex-snapshot
Ionomer Self-Assembly in Dilute Solution Studied by Coarse-Grained Molecular Dynamics
inferred← citeshttps://doi.org/10.1021/acs.nanolett.1c01737openalex-snapshot
Supramolecular Interactions and Morphology of Self-Assembling Peptide Amphiphile Nanostructures
inferred← citeshttps://doi.org/10.1021/acs.nanolett.4c00601openalex-snapshot
Cation Triggered Self-Assembly of α-Lactalbumin Nanotubes
inferred← citeshttps://doi.org/10.1021/acsami.0c01574openalex-snapshot
Nanomechanical Properties and Phase Behavior of Phenylalanine Amyloid Ribbon Assemblies and Amorphous Self-Healing Hydrogels
inferred← citeshttps://doi.org/10.1021/acsmacrolett.9b00866openalex-snapshot
Quantifying the Mechanical Anisotropy in Poly(3-hexylthiophene) Nanofibers
inferred← citeshttps://doi.org/10.1021/acsnano.7b08969openalex-snapshot
Polyphenol-Binding Amyloid Fibrils Self-Assemble into Reversible Hydrogels with Antibacterial Activity
inferred← citeshttps://doi.org/10.1021/acsomega.0c02326openalex-snapshot
Bifunctional Peptide–Polymer Conjugate-Based Fibers via a One-Pot Tandem Disulfide Reduction Coupled to a Thio-Bromo “Click” Reaction
inferred← citeshttps://doi.org/10.1021/acssuschemeng.1c03937openalex-snapshot
Sustainable Bioplastics from Amyloid Fibril-Biodegradable Polymer Blends
inferred← citeshttps://doi.org/10.1021/bm300896ropenalex-snapshot
Formation of β-Lactoglobulin Nanofibrils by Microwave Heating Gives a Peptide Composition Different from Conventional Heating
inferred← citeshttps://doi.org/10.1021/bm301005wopenalex-snapshot
Gelation, Phase Behavior, and Dynamics of β-Lactoglobulin Amyloid Fibrils at Varying Concentrations and Ionic Strengths
inferred← citeshttps://doi.org/10.1021/bm4013259openalex-snapshot
Amyloid-like Fibrils Formed by ε-Poly- l -lysine
inferred← citeshttps://doi.org/10.1021/bm401646xopenalex-snapshot
Engineered Lysozyme Amyloid Fibril Networks Support Cellular Growth and Spreading
inferred← citeshttps://doi.org/10.1021/bm500762uopenalex-snapshot
Electrostatic Stabilization of β-lactoglobulin Fibrils at Increased pH with Cationic Polymers
inferred← citeshttps://doi.org/10.1021/ja507051wopenalex-snapshot
Amino Acid Sequence in Constitutionally Isomeric Tetrapeptide Amphiphiles Dictates Architecture of One-Dimensional Nanostructures
inferred← citeshttps://doi.org/10.1021/jz3019786openalex-snapshot
Nanoscopic Amyloid Pores Formed via Stepwise Protein Assembly
inferred← citeshttps://doi.org/10.1021/la501622topenalex-snapshot
Fibril Aggregates Formed by a Glatiramer-Mimicking Random Copolymer of Amino Acids
inferred← citeshttps://doi.org/10.1021/ma4007768openalex-snapshot
Toward Novel Polymer-Based Materials Inspired in Blood Clotting
inferred← citeshttps://doi.org/10.1021/mz400639yopenalex-snapshot
Directed Growth of Silk Nanofibrils on Graphene and Their Hybrid Nanocomposites
inferred← citeshttps://doi.org/10.1021/nn404886kopenalex-snapshot
Polymorphism Complexity and Handedness Inversion in Serum Albumin Amyloid Fibrils
inferred← citeshttps://doi.org/10.1021/nn406121wopenalex-snapshot
A Clear View of Polymorphism, Twist, and Chirality in Amyloid Fibril Formation
inferred← citeshttps://doi.org/10.1021/nn503530aopenalex-snapshot
Correlation between Nanomechanics and Polymorphic Conformations in Amyloid Fibrils
inferred← citeshttps://doi.org/10.1021/nn505688bopenalex-snapshot
Multiwalled Nanotubes Formed by Catanionic Mixtures of Drug Amphiphiles
inferred← citeshttps://doi.org/10.1038/ncomms8574openalex-snapshot
Supramolecular amplification of amyloid self-assembly by iodination
inferred← citeshttps://doi.org/10.1038/s41467-017-01424-4openalex-snapshot
Competition between crystal and fibril formation in molecular mutations of amyloidogenic peptides
inferred← citeshttps://doi.org/10.1038/s41598-019-45437-zopenalex-snapshot
Self-assembly of plant protein fibrils interacting with superparamagnetic iron oxide nanoparticles
inferred← citeshttps://doi.org/10.1038/s41598-022-06995-xopenalex-snapshot
Electric-field induced modulation of amorphous protein aggregates: polarization, deformation, and reorientation
inferred← citeshttps://doi.org/10.1038/s43016-019-0009-xopenalex-snapshot
Design principles of food gels
inferred← citeshttps://doi.org/10.1038/s44303-025-00108-9openalex-snapshot
Super-resolution imaging with nanopipettes
inferred← citeshttps://doi.org/10.1039/9781788016155-00383openalex-snapshot
Modelling and Computer Simulation Approaches to Understand and Predict Food Structure Development: Structuring by Gelation and Self-association of Biomolecules
inferred← citeshttps://doi.org/10.1039/c2nr30768eopenalex-snapshot
Measurement of intrinsic properties of amyloid fibrils by the peak force QNM method
inferred← citeshttps://doi.org/10.1039/c3fd00083dopenalex-snapshot
Polymorphism in bovine serum albumin fibrils: morphology and statistical analysis
inferred← citeshttps://doi.org/10.1039/c3nr02194gopenalex-snapshot
Towards lysozyme nanotube and 3D hybrid self-assembly
inferred← citeshttps://doi.org/10.1039/c3sc52504jopenalex-snapshot
Tunable mechano-responsive organogels by ring-opening copolymerizations of N-carboxyanhydrides
inferred← citeshttps://doi.org/10.1039/c5nr00555hopenalex-snapshot
A novel form of β-strand assembly observed in Aβ 33–42 adsorbed onto graphene
inferred← citeshttps://doi.org/10.1039/c5sm00183hopenalex-snapshot
FRET evidence for untwisting of amyloid fibrils on the surface of model membranes
inferred← citeshttps://doi.org/10.1039/c5sm00652jopenalex-snapshot
From ribbons to tubules: a computational study of the polymorphism in aggregation of helical filaments
inferred← citeshttps://doi.org/10.1039/c5sm02934aopenalex-snapshot
A hypothetical hierarchical mechanism of the self-assembly of the Escherichia coli RNA polymerase σ 70 subunit
inferred← citeshttps://doi.org/10.1039/c6cs00542jopenalex-snapshot
Self-assembling peptide and protein amyloids: from structure to tailored function in nanotechnology
inferred← citeshttps://doi.org/10.1039/c6lc00690fopenalex-snapshot
Scanning-SAXS of microfluidic flows: nanostructural mapping of soft matter
inferred← citeshttps://doi.org/10.1039/c6ra24031copenalex-snapshot
Quantitative analysis of amyloid polymorphism using height histograms to correct for tip convolution effects in atomic force microscopy imaging
inferred← citeshttps://doi.org/10.1039/c6sm00073hopenalex-snapshot
Controlled self-assembly of biomolecular rods on structured substrates
inferred← citeshttps://doi.org/10.1039/c6tb02683dopenalex-snapshot
Micro- and nanoscale hierarchical structure of core–shell protein microgels
inferred← citeshttps://doi.org/10.1039/c7ra10485eopenalex-snapshot
Precision polymers containing main-chain-amino acids: ADMET polymerization and crystallization
inferred← citeshttps://doi.org/10.1039/c9cp02683eopenalex-snapshot
Modulation of amyloid β peptide aggregation by hydrophilic polymers
inferred← citeshttps://doi.org/10.1039/c9sm00127aopenalex-snapshot
The influence of pH, protein concentration and calcium ratio on the formation and structure of nanotubes from partially hydrolyzed bovine α-lactalbumin
inferred← citeshttps://doi.org/10.1039/c9tc06002bopenalex-snapshot
Towards supramolecular nanostructured materials: control of the self-assembly of ionic bent-core amphiphiles
inferred← citeshttps://doi.org/10.1039/d0sm01761bopenalex-snapshot
Interfacial behaviour of β-lactoglobulin aggregates at the oil–water interface studied using particle tracking and dilatational rheology
inferred← citeshttps://doi.org/10.1039/d1nr01661jopenalex-snapshot
Mechanistic process understanding of the self-assembling behaviour of asymmetric bolaamphiphilic short-peptides and their templating for silica and titania nanomaterials
inferred← citeshttps://doi.org/10.1039/d1ra06878dopenalex-snapshot
Protein nanofibrils and their use as building blocks of sustainable materials
inferred← citeshttps://doi.org/10.1039/d2nr00372dopenalex-snapshot
Acquiring structural and mechanical information of a fibrous network through deep learning
inferred← citeshttps://doi.org/10.1039/d3sm00408bopenalex-snapshot
A coarse-grained molecular model of amyloid fibrils systems
inferred← citeshttps://doi.org/10.1039/d4nr03030copenalex-snapshot
Cell invasive amyloid assemblies from SARS-CoV-2 peptides can form multiple polymorphs with varying neurotoxicity
inferred← citeshttps://doi.org/10.1039/d6sm00177gopenalex-snapshot
A percolation-based theoretical model reveals the structural origin of strain-stiffening in semiflexible fibrous networks
inferred← citeshttps://doi.org/10.1063/1.4745480openalex-snapshot
Self-organization of amphiphilic macromolecules with local helix structure in concentrated solutions
inferred← citeshttps://doi.org/10.1063/1.4928767openalex-snapshot
Accelerated insulin aggregation under alternating current electric fields: Relevance to amyloid kinetics
inferred← citeshttps://doi.org/10.1063/5.0142867openalex-snapshot
Naturally derived colloidal rods in microfluidic flows
inferred← citeshttps://doi.org/10.1074/jbc.m114.571976openalex-snapshot
Self-Assembly of MinE on the Membrane Underlies Formation of the MinE Ring to Sustain Function of the Escherichia coli Min System
inferred← citeshttps://doi.org/10.1080/00222348.2015.1103430openalex-snapshot
Effect of Melanomal Proteins on Sepia Melanin Assembly
inferred← citeshttps://doi.org/10.1080/07391102.2017.1349691openalex-snapshot
Molecular dynamics simulations of lysozyme–lipid systems: probing the early steps of protein aggregation
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/10.1098/rsos.230443openalex-snapshot
Interaction of gallium, indium and vanadyl diacetylcurcumin complexes with lysozyme: mechanistic aspects and evaluation of antiamyloidogenic activity
inferred← citeshttps://doi.org/10.1103/physreve.88.022502openalex-snapshot
Shape and chirality transitions in off-axis twist nematic elastomer ribbons
inferred← citeshttps://doi.org/10.1103/physrevlett.113.268103openalex-snapshot
Universal Behavior in the Mesoscale Properties of Amyloid Fibrils
inferred← citeshttps://doi.org/10.1103/physrevlett.114.078102openalex-snapshot
Universality in the Morphology and Mechanics of Coarsening Amyloid Fibril Networks
inferred← citeshttps://doi.org/10.1103/physrevlett.116.258105openalex-snapshot
Elasticity and Fluctuations of Frustrated Nanoribbons
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/10.1107/s1600577524005290openalex-snapshot
New opportunities for time-resolved imaging using diffraction-limited storage rings
inferred← citeshttps://doi.org/10.1111/1541-4337.12404openalex-snapshot
Rational Design of Amyloid‐Like Fibrillary Structures for Tailoring Food Protein Techno‐Functionality and Their Potential Health Implications
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/10.1111/1750-3841.14509openalex-snapshot
Composite Gels Containing Whey Protein Fibrils and Bacterial Cellulose Microfibrils
inferred← citeshttps://doi.org/10.1111/1750-3841.70509openalex-snapshot
Ovotransferrin Fibrils Formed by Peptides Self‐Assembly Improve the Stability and Antioxidation of Quercetin and Their Application in Quercetin Fortified Soybean Milk
inferred← citeshttps://doi.org/10.1116/1.4996447openalex-snapshot
Quantifying Young's moduli of protein fibrils and particles with bimodal force spectroscopy
inferred← citeshttps://doi.org/10.1116/1.5098332openalex-snapshot
Amyloid-like peptide nanofibrils as scaffolds for tissue engineering: Progress and challenges (Review)
inferred← citeshttps://doi.org/10.1134/s0965545x2106002xopenalex-snapshot
Atomic Force Microscopy of Biopolymers on Graphite Surfaces
inferred← citeshttps://doi.org/10.1142/s1793048015300029openalex-snapshot
Protein Fibrillar Nanopolymers: Molecular-Level Insights into Their Structural, Physical and Mechanical Properties
inferred← citeshttps://doi.org/10.1146/annurev-biophys-083012-130345openalex-snapshot
Nanoconfinement and the Strength of Biopolymers
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