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Secondary Nucleation and Accessible Surface in Insulin Amyloid Fibril Formation

https://doi.org/10.1021/jp710131u
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What this work says

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

inferredcites →https://doi.org/10.1007/978-1-4615-7658-7openalex-snapshot
Principles of Fluorescence Spectroscopy
inferredcites →https://doi.org/10.1007/s00249-007-0137-3openalex-snapshot
Effects of confinement on insulin amyloid fibrils formation
inferredcites →https://doi.org/10.1016/0003-2697(89)90046-8openalex-snapshot
Fluorometric determination of amyloid fibrils in vitro using the fluorescent dye, thioflavine T
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(86)90324-4openalex-snapshot
Kinetics of sickle hemoglobin polymerization
inferredcites →https://doi.org/10.1016/j.bpc.2003.09.004openalex-snapshot
Aggregation kinetics of bovine serum albumin studied by FTIR spectroscopy and light scattering
inferredcites →https://doi.org/10.1016/j.bpc.2004.07.042openalex-snapshot
Thermal induced conformational changes involved in the aggregation pathways of beta-lactoglobulin
inferredcites →https://doi.org/10.1016/j.bpc.2006.07.012openalex-snapshot
Amyloid fibrils formation and amorphous aggregation in concanavalin A
inferredcites →https://doi.org/10.1016/j.jmb.2005.06.046openalex-snapshot
Solvational Tuning of the Unfolding, Aggregation and Amyloidogenesis of Insulin
inferredcites →https://doi.org/10.1016/j.jmb.2005.09.100openalex-snapshot
The Changing Face of Glucagon Fibrillation: Structural Polymorphism and Conformational Imprinting
inferredcites →https://doi.org/10.1016/j.jmb.2005.11.075openalex-snapshot
Solvation-assisted Pressure Tuning of Insulin Fibrillation: From Novel Aggregation Pathways to Biotechnological Applications
inferredcites →https://doi.org/10.1016/j.jmb.2006.11.008openalex-snapshot
Kinetics of Different Processes in Human Insulin Amyloid Formation
inferredcites →https://doi.org/10.1016/j.jmb.2006.11.009openalex-snapshot
Absolute Correlation between Lag Time and Growth Rate in the Spontaneous Formation of Several Amyloid-like Aggregates and Fibrils
inferredcites →https://doi.org/10.1016/j.jmb.2007.04.053openalex-snapshot
Cytotoxicity of Insulin within its Self-assembly and Amyloidogenic Pathways
inferredcites →https://doi.org/10.1016/j.jsb.2005.06.006openalex-snapshot
Mechanism of thioflavin T binding to amyloid fibrils
inferredcites →https://doi.org/10.1016/j.jsb.2006.12.010openalex-snapshot
Study on the binding of Thioflavin T to β-sheet-rich and non-β-sheet cavities
inferredcites →https://doi.org/10.1016/j.jsb.2007.06.004openalex-snapshot
Binding mode of Thioflavin T in insulin amyloid fibrils
inferredcites →https://doi.org/10.1016/j.semcdb.2003.12.008openalex-snapshot
Principles of protein folding, misfolding and aggregation
inferredcites →https://doi.org/10.1016/s0006-3495(80)84962-9openalex-snapshot
Kinetic studies on photolysis-induced gelation of sickle cell hemoglobin suggest a new mechanism
inferredcites →https://doi.org/10.1016/s0006-3495(84)84062-xopenalex-snapshot
Kinetics of nucleation-controlled polymerization. A perturbation treatment for use with a secondary pathway
inferredcites →https://doi.org/10.1016/s0022-2836(02)00021-9openalex-snapshot
Insulin at pH 2: Structural Analysis of the Conditions Promoting Insulin Fibre Formation
inferredcites →https://doi.org/10.1016/s0076-6879(99)09020-5openalex-snapshot
[18] Quantification of β-sheet amyloid fibril structures with thioflavin T
inferredcites →https://doi.org/10.1016/s0301-4622(03)00153-4openalex-snapshot
Conformational changes involved in thermal aggregation processes of bovine serum albumin
inferredcites →https://doi.org/10.1021/bi0160462openalex-snapshot
Islet Amyloid: Phase Partitioning and Secondary Nucleation Are Central to the Mechanism of Fibrillogenesis
inferredcites →https://doi.org/10.1021/bi0262698openalex-snapshot
Conformational Prerequisites for α-Lactalbumin Fibrillation
inferredcites →https://doi.org/10.1021/bi050281topenalex-snapshot
Ethanol-Perturbed Amyloidogenic Self-Assembly of Insulin: Looking for Origins of Amyloid Strains
inferredcites →https://doi.org/10.1021/bi6025374openalex-snapshot
Glucagon Amyloid-like Fibril Morphology Is Selected via Morphology-Dependent Growth Inhibition
inferredcites →https://doi.org/10.1021/ja01107a013openalex-snapshot
Studies of the Nucleation and Growth Reactions of Selected Types of Insulin Fibrils
inferredcites →https://doi.org/10.1021/ja01206a030openalex-snapshot
A Fibrous Modification of Insulin. I. The Heat Precipitate of Insulin
inferredcites →https://doi.org/10.1021/ja01206a031openalex-snapshot
The Reactions of Antiserum Homologous to the p-Azophenyltrimethylammonium Group1
inferredcites →https://doi.org/10.1039/b314086eopenalex-snapshot
Hydration and structure—the two sides of the insulin aggregation process
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/bj0530320openalex-snapshot
Partition chromatography of insulin and other proteins
inferredcites →https://doi.org/10.1042/bj0530328openalex-snapshot
The isolation and some chemical properties of viridicatin, a metabolic product of Penicillium viridicatum Westling
inferredcites →https://doi.org/10.1073/pnas.0701250104openalex-snapshot
Nucleation of protein fibrillation by nanoparticles
inferredcites →https://doi.org/10.1073/pnas.0703306104openalex-snapshot
Fiber-dependent amyloid formation as catalysis of an existing reaction pathway
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/10.1093/emboj/cdf573openalex-snapshot
The behaviour of polyamino acids reveals an inverse side chain effect in amyloid structure formation
inferredcites →https://doi.org/10.1098/rsta.2003.1194openalex-snapshot
Protein folding and misfolding: a paradigm of self–assembly and regulation in complex biological systems
inferredcites →https://doi.org/10.1110/ps.03607204openalex-snapshot
Insulin forms amyloid in a strain‐dependent manner: An FT‐IR spectroscopic study
inferredcites →https://doi.org/10.1110/ps.051692305openalex-snapshot
The kinetic behavior of insulin fibrillation is determined by heterogeneous nucleation pathways
inferredcites →https://doi.org/10.1110/ps.9.10.1960openalex-snapshot
Formation of insulin amyloid fibrils followed by FTIR simultaneously with CD and electron microscopy
inferredcites →https://doi.org/10.1371/journal.pbio.0050134openalex-snapshot
A Helical Structural Nucleus Is the Primary Elongating Unit of Insulin Amyloid Fibrils
inferredcites →https://doi.org/10.1529/biophysj.104.048843openalex-snapshot
Amyloidogenic Self-Assembly of Insulin Aggregates Probed by High Resolution Atomic Force Microscopy
inferredcites →https://doi.org/10.1529/biophysj.105.068650openalex-snapshot
Formation Kinetics of Insulin-Based Amyloid Gels and the Effect of Added Metalloporphyrins
inferredcites →https://doi.org/10.1529/biophysj.105.068833openalex-snapshot
Early Events in Insulin Fibrillization Studied by Time-Lapse Atomic Force Microscopy
inferredcites →https://doi.org/10.1529/biophysj.105.070912openalex-snapshot
Sulfates Dramatically Stabilize a Salt-Dependent Type of Glucagon Fibrils
inferredcites →https://doi.org/10.1529/biophysj.105.072660openalex-snapshot
Optical Microscopy of Growing Insulin Amyloid Spherulites on Surfaces In Vitro
inferredcites →https://doi.org/10.1529/biophysj.105.073767openalex-snapshot
The Kinetics of Nucleated Polymerizations at High Concentrations: Amyloid Fibril Formation Near and Above the “Supercritical Concentration”
inferredcites →https://doi.org/10.1529/biophysj.105.077636openalex-snapshot
Kinetics of Insulin Aggregation: Disentanglement of Amyloid Fibrillation from Large-Size Cluster Formation
inferredcites →https://doi.org/10.3109/13506129509031881openalex-snapshot
Thioflavine T interaction with amyloid β-sheet structures
inferredcites →https://doi.org/10.4324/9780203484180openalex-snapshot
Pharmaceutical Formulation Development of Peptides and Proteins

What points at this work

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

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Surface-Catalysed Liquid-Liquid Phase Separation and Amyloid-Like Assembly in Microscale Compartments
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Temperature Control of Sequential Nucleation–Growth Mechanisms in Hierarchical Supramolecular Polymers
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Determination of the Size of the Primary and Secondary Folding Nuclei of Protofibrils from the Concentration Dependence of the Rate and the Lag-Time of Their Formation
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Binding mode of Thioflavin T and other molecular probes in the context of amyloid fibrils—current status
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Monomer-dependent secondary nucleation in amyloid formation
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Concanavalin A aggregation and toxicity on cell cultures
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Molecular mechanism of Thioflavin-T binding to amyloid fibrils
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Off-pathway aggregation can inhibit fibrillation at high protein concentrations
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Solution conditions define morphological homogeneity of α-synuclein fibrils
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Blue autofluorescence in protein aggregates “lighted on” by UV induced oxidation
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Recent advances in small molecules for amyloid fibril inhibition: chemical strategies and molecular mechanistic insights from lysozyme and insulin models
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Oregano polyphenols reduce human insulin amyloid aggregation
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The role of surfaces on amyloid formation
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Kinetics theories to understand the mechanism of aggregation of a protein and to design strategies for its inhibition
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Amyloids, amorphous aggregates and assemblies of peptides – Assessing aggregation
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Enrichment of Amyloidogenesis at an Air-Water Interface
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Sulfate Anion Delays the Self-Assembly of Human Insulin by Modifying the Aggregation Pathway
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Competition between Primary Nucleation and Autocatalysis in Amyloid Fibril Self-Assembly
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Arresting Amyloid with Coulomb’s Law: Acetylation of ALS-Linked SOD1 by Aspirin Impedes Aggregation
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Automated Ex Situ Assays of Amyloid Formation on a Microfluidic Platform
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Insights into the cross-amyloid aggregation of Aβ40 and its N-terminal truncated peptide Aβ11-40 affected by epigallocatechin gallate
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The route to protein aggregate superstructures: Particulates and amyloid‐like spherulites
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Characterization and kinetics of whey protein isolate amyloid fibril aggregates under moderate electric fields
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Cyanidin-3-rutinoside reduces insulin fibrillation and attenuates insulin fibrils-induced oxidative hemolysis of human erythrocytes
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Bifunctional carbon dots for cell imaging and inhibition of human insulin fibrillation in the whole aggregation process
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A tale of two tails: Self-assembling properties of A- and B-chain parts of insulin's highly amyloidogenic H-fragment
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Sensing of insulin fibrillation using alkoxy-bridged binuclear rhenium(I) complexes
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Probing ensemble polymorphism and single aggregate structural heterogeneity in insulin amyloid self-assembly
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Polysorbate 80 controls Morphology, structure and stability of human insulin Amyloid-Like spherulites
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Surface-catalyzed liquid–liquid phase separation and amyloid-like assembly in microscale compartments
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Insulin amyloid morphology is encoded in H-bonds and electrostatics interactions ruling protein phase separation
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Investigating the effect of food additive dye “tartrazine” on BLG fibrillation under in-vitro condition. A biophysical and molecular docking study
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Vortex-Induced Formation of Insulin Amyloid Superstructures Probed by Time-Lapse Atomic Force Microscopy and Circular Dichroism Spectroscopy
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Lability Landscape and Protease Resistance of Human Insulin Amyloid: A New Insight into Its Molecular Properties
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Basic Orange 21: A molecular rotor probe for fluorescence turn-on sensing of amyloid fibrils
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Victoria Blue B acts as a protein isomerization targeting probe for monitoring lysozyme fibrillation
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Secondary nucleation of monomers on fibril surface dominatesα-synuclein aggregation and provides autocatalytic amyloid amplification
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Immunoassays with Protein Misfolding Cycle Amplification: A Platform for Ultrasensitive Detection of Antigen
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Analysis of Protein Aggregation in Neurodegenerative Disease
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PAP(248–286) Conformational Changes during the Lag Phase of Amyloid Fibril Formation
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A Comparison of Three Fluorophores for the Detection of Amyloid Fibers and Prefibrillar Oligomeric Assemblies. ThT (Thioflavin T); ANS (1-Anilinonaphthalene-8-sulfonic Acid); and bisANS (4,4′-Dianilino-1,1′-binaphthyl-5,5′-disulfonic Acid)
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Mechanism of Fibril and Soluble Oligomer Formation in Amyloid Beta and Hen Egg White Lysozyme Proteins
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Sulfobutylether-β-Cyclodextrin for Inhibition and Rupture of Amyloid Fibrils
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Heterogeneous and Surface-Catalyzed Amyloid Aggregation Monitored by Spatially Resolved Fluorescence and Single Molecule Microscopy
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Lipidation Effect on Surface Adsorption and Associated Fibrillation of the Model Protein Insulin
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Modulation of Amyloid Protein Fibrillation by Synthetic Polymers: Recent Advances in the Context of Neurodegenerative Diseases
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Conformational Transitions upon Maturation Rule Surface and pH-Responsiveness of α-Lactalbumin Microparticulates
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Advances in the Study of Cerium Oxide Nanoparticles: New Insights into Antiamyloidogenic Activity
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Two-Dimensional Layered Nanomaterials Steering Self-Assembly of Dodecapeptides with Three Building Blocks
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αS1-Casein-Loaded Proteo-liposomes as Potential Inhibitors in Amyloid Fibrillogenesis: In Vivo Effects on a C. elegans Model of Alzheimer’s Disease
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Stochastic Formation of Fibrillar and Amorphous Superoxide Dismutase Oligomers Linked to Amyotrophic Lateral Sclerosis
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The Properties of α-Synuclein Secondary Nuclei Are Dominated by the Solution Conditions Rather than the Seed Fibril Strain
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Mechanistic Origin of the Combined Effect of Surfaces and Mechanical Agitation on Amyloid Formation
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Human Fibrinogen Inhibits Amyloid Assembly of Most Phenol-Soluble Modulins from Staphylococcus aureus
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Structural Insight of Amyloidogenic Intermediates of Human Insulin
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Cross-Seeding of Fibrils from Two Types of Insulin Induces New Amyloid Strains
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Noncooperative Dimethyl Sulfoxide-Induced Dissection of Insulin Fibrils: Toward Soluble Building Blocks of Amyloid
inferred← citeshttps://doi.org/10.1021/ja405530popenalex-snapshot
Identification of a Common Binding Mode for Imaging Agents to Amyloid Fibrils from Molecular Dynamics Simulations
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Quantification of the Concentration of Aβ42 Propagons during the Lag Phase by an Amyloid Chain Reaction Assay
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Pathway Complexity in Supramolecular Copolymerization and Blocky Star Copolymers by a Hetero-Seeding Effect
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Amyloid Fibrils Formation of Concanavalin A at Basic pH
inferred← citeshttps://doi.org/10.1021/jp309331uopenalex-snapshot
Thioflavin T and Its Photoirradiative Derivatives: Exploring Their Spectroscopic Properties in the Absence and Presence of Amyloid Fibrils
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How to Determine the Size of Folding Nuclei of Protofibrils from the Concentration Dependence of the Rate and Lag-Time of Aggregation. I. Modeling the Amyloid Protofibril Formation
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How to Determine the Size of Folding Nuclei of Protofibrils from the Concentration Dependence of the Rate and Lag-Time of Aggregation. II. Experimental Application for Insulin and LysPro Insulin: Aggregation Morphology, Kinetics, and Sizes of Nuclei
inferred← citeshttps://doi.org/10.1021/jp510980bopenalex-snapshot
Master and Slave Relationship Between Two Types of Self-Propagating Insulin Amyloid Fibrils
inferred← citeshttps://doi.org/10.1021/jp805560copenalex-snapshot
Thioflavin T Hydroxylation at Basic pH and Its Effect on Amyloid Fibril Detection
inferred← citeshttps://doi.org/10.1021/jp810972yopenalex-snapshot
Self-Organization Pathways and Spatial Heterogeneity in Insulin Amyloid Fibril Formation
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Detection of Strongly Bound Thioflavin T Species in Amyloid Fibrils by Ligand-Detected 1H NMR
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Minimal Model for Self-Catalysis in the Formation of Amyloid-Like Elongated Fibrils
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α-Casein Inhibits Insulin Amyloid Formation by Preventing the Onset of Secondary Nucleation Processes
inferred← citeshttps://doi.org/10.1038/ncomms10948openalex-snapshot
Kinetic analysis reveals the diversity of microscopic mechanisms through which molecular chaperones suppress amyloid formation
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Mechanistic and environmental control of the prevalence and lifetime of amyloid oligomers
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Physical determinants of the self-replication of protein fibrils
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Stop-and-go kinetics in amyloid fibrillation
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Spatially constrained disulfide bond shuffling delays insulin aggregation and enhances neurotoxicity
inferred← citeshttps://doi.org/10.1038/s41598-020-61663-2openalex-snapshot
Formation of distinct prion protein amyloid fibrils under identical experimental conditions
inferred← citeshttps://doi.org/10.1038/s41598-020-70982-3openalex-snapshot
Gallic acid oxidation products alter the formation pathway of insulin amyloid fibrils
inferred← citeshttps://doi.org/10.1039/b913510copenalex-snapshot
Formation kinetics and fractal characteristics of regenerated silk fibroin alcogel developed from nanofibrillar network
inferred← citeshttps://doi.org/10.1039/c0sm00169dopenalex-snapshot
Large-scale polymorphism and auto-catalytic effect in insulin fibrillogenesis
inferred← citeshttps://doi.org/10.1039/c3nr33193hopenalex-snapshot
Protein fibrillation and nanoparticle interactions: opportunities and challenges
inferred← citeshttps://doi.org/10.1039/c3ra43259aopenalex-snapshot
A new fluorescent probe for monitoring amyloid fibrillation with high sensitivity and reliability
inferred← citeshttps://doi.org/10.1039/c4cc07911fopenalex-snapshot
Detection of oligomers and fibrils of α-synuclein by AIEgen with strong fluorescence
inferred← citeshttps://doi.org/10.1039/c4cp03072aopenalex-snapshot
Intermediates caught in the act: tracing insulin amyloid fibril formation in time by combined optical spectroscopy, light scattering, mass spectrometry and microscopy
inferred← citeshttps://doi.org/10.1039/c6cc08727bopenalex-snapshot
Detection, inhibition and disintegration of amyloid fibrils: the role of optical probes and macrocyclic receptors
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/c6ra25872gopenalex-snapshot
Sucrose modulates insulin amyloid-like fibril formation: effect on the aggregation mechanism and fibril morphology
inferred← citeshttps://doi.org/10.1039/c8cc02204fopenalex-snapshot
Secondary nucleation in amyloid formation
inferred← citeshttps://doi.org/10.1039/c8cp04838jopenalex-snapshot
Self-inhibition of insulin amyloid-like aggregation
inferred← citeshttps://doi.org/10.1039/c8cp05904gopenalex-snapshot
Sensitivity analysis of the variability of amyloid aggregation profiles
inferred← citeshttps://doi.org/10.1039/d0ma00760aopenalex-snapshot
Review of the current state of protein aggregation inhibition from a materials chemistry perspective: special focus on polymeric materials
inferred← citeshttps://doi.org/10.1039/d1ay01126jopenalex-snapshot
Monitoring the surface tension by the pendant drop technique for detection of insulin fibrillogenesis
inferred← citeshttps://doi.org/10.1042/bst20250489openalex-snapshot
The amplification of α-synuclein amyloid fibrils
inferred← citeshttps://doi.org/10.1063/5.0236947openalex-snapshot
On the reversibility of amyloid fibril formation
inferred← citeshttps://doi.org/10.1063/5.0261115openalex-snapshot
Understanding pathway complexity in assembly mechanisms of hydrophobic peptides in water: Insights from atomistic simulations via event tracking
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/10.1098/rsos.160696openalex-snapshot
Thioflavin T as an amyloid dye: fibril quantification, optimal concentration and effect on aggregation
inferred← citeshttps://doi.org/10.1126/science.1178250openalex-snapshot
An Analytical Solution to the Kinetics of Breakable Filament Assembly
inferred← citeshttps://doi.org/10.1134/s0006297918140122openalex-snapshot
Analysis of Insulin Analogs and the Strategy of Their Further Development
inferred← citeshttps://doi.org/10.1140/epje/i2010-10665-4openalex-snapshot
Tracking the heterogeneous distribution of amyloid spherulites and their population balance with free fibrils
inferred← citeshttps://doi.org/10.1186/s13024-023-00651-2openalex-snapshot
Misfolded protein oligomers: mechanisms of formation, cytotoxic effects, and pharmacological approaches against protein misfolding diseases
inferred← citeshttps://doi.org/10.1186/s13662-024-03819-2openalex-snapshot
Moment dynamics of oligomer formation in protein amyloid aggregation with secondary nucleation
inferred← citeshttps://doi.org/10.1371/journal.pone.0068684openalex-snapshot
Amyloid-Like Fibril Elongation Follows Michaelis-Menten Kinetics
inferred← citeshttps://doi.org/10.1371/journal.pone.0084552openalex-snapshot
Oxidation Enhances Human Serum Albumin Thermal Stability and Changes the Routes of Amyloid Fibril Formation
inferred← citeshttps://doi.org/10.1371/journal.pone.0086320openalex-snapshot
On the Heat Stability of Amyloid-Based Biological Activity: Insights from Thermal Degradation of Insulin Fibrils
inferred← citeshttps://doi.org/10.1371/journal.pone.0149148openalex-snapshot
The Inhibitory Effect of Natural Products on Protein Fibrillation May Be Caused by Degradation Products – A Study Using Aloin and Insulin
inferred← citeshttps://doi.org/10.1515/pac-2018-1017openalex-snapshot
Mechanism of amyloid protein aggregation and the role of inhibitors
inferred← citeshttps://doi.org/10.17795/jjhr-36931openalex-snapshot
Temperature and pH Effects on Insulin Structure: A Molecular Dynamic Approach
inferred← citeshttps://doi.org/10.3168/jds.2021-20895openalex-snapshot
Effect of CaCl2 on 2 heat-induced whey protein concentrate fibrillation pathways: Spontaneous and nuclear induction
inferred← citeshttps://doi.org/10.3389/fmolb.2021.669994openalex-snapshot
Secondary Nucleation and the Conservation of Structural Characteristics of Amyloid Fibril Strains
inferred← citeshttps://doi.org/10.3390/app16167869openalex-snapshot
Time-Resolved Monitoring of β-Lactoglobulin Assembly and Aggregation in Microdroplets
inferred← citeshttps://doi.org/10.3390/biom15010040openalex-snapshot
Saponins Effect on Human Insulin Amyloid Aggregation
inferred← citeshttps://doi.org/10.3390/biom8040108openalex-snapshot
Probing the Occurrence of Soluble Oligomers through Amyloid Aggregation Scaling Laws
inferred← citeshttps://doi.org/10.3390/biophysica2040040openalex-snapshot
A Long Journey into the Investigation of the Structure–Dynamics–Function Paradigm in Proteins through the Activities of the Palermo Biophysics Group
inferred← citeshttps://doi.org/10.3390/ijms12129369openalex-snapshot
Monitoring Insulin Aggregation via Capillary Electrophoresis
inferred← citeshttps://doi.org/10.3390/ijms22041775openalex-snapshot
Lysozyme Fibrils Alter the Mechanism of Insulin Amyloid Aggregation
inferred← citeshttps://doi.org/10.3390/ijms23105421openalex-snapshot
Lysozyme Amyloid Fibril Structural Variability Dependence on Initial Protein Folding State
inferred← citeshttps://doi.org/10.3390/ijms25179406openalex-snapshot
Study of Insulin Aggregation and Fibril Structure under Different Environmental Conditions
inferred← citeshttps://doi.org/10.3390/jmp5020016openalex-snapshot
Exploring the Molecular Pathology of Iatrogenic Amyloidosis
inferred← citeshttps://doi.org/10.3390/life12030448openalex-snapshot
The Possible Role of the Type I Chaperonins in Human Insulin Self-Association
inferred← citeshttps://doi.org/10.3390/molecules25051195openalex-snapshot
Structure and Aggregation Mechanisms in Amyloids
inferred← citeshttps://doi.org/10.37247/pamolscs.1.2020.9openalex-snapshot
Structure and Aggregation Mechanisms in Amyloids
inferred← citeshttps://doi.org/10.3990/1.9789036540247openalex-snapshot
Multifaceted fibrils: self-assembly, polymorphism and functionalization
inferred← citeshttps://doi.org/10.4149/gpb_2013020openalex-snapshot
Polyanion-induced circular dichroism of Thioflavin T
inferred← citeshttps://doi.org/10.4161/pri.22992openalex-snapshot
Amyloidogenic peptides of yeast cell wall glucantransferase Bgl2p as a model for the investigation of its pH-dependent fibril formation
inferred← citeshttps://doi.org/10.5772/63359openalex-snapshot
Kinetics of Amyloid Formation by Different Proteins and Peptides: Polymorphism and Sizes of Folding Nuclei of Fibrils
inferred← citeshttps://doi.org/10.7287/peerj.10918v0.1/reviews/1openalex-snapshot
Peer Review #1 of "Exploring the occurrence of thioflavin-T-positive insulin amyloid aggregation intermediates (v0.1)"
inferred← citeshttps://doi.org/10.7287/peerj.10918v0.1/reviews/2openalex-snapshot
Peer Review #2 of "Exploring the occurrence of thioflavin-T-positive insulin amyloid aggregation intermediates (v0.1)"
inferred← citeshttps://doi.org/10.7287/peerj.12381v0.1/reviews/1openalex-snapshot
Peer Review #1 of "Interplay between epigallocatechin-3-gallate and ionic strength during amyloid aggregation (v0.1)"
inferred← citeshttps://doi.org/10.7287/peerj.12381v0.1/reviews/2openalex-snapshot
Peer Review #2 of "Interplay between epigallocatechin-3-gallate and ionic strength during amyloid aggregation (v0.1)"
inferred← citeshttps://doi.org/10.7287/peerj.12381v0.1/reviews/3openalex-snapshot
Peer Review #3 of "Interplay between epigallocatechin-3-gallate and ionic strength during amyloid aggregation (v0.1)"
inferred← citeshttps://doi.org/10.7287/peerj.12381v0.2/reviews/1openalex-snapshot
Peer Review #1 of "Interplay between epigallocatechin-3-gallate and ionic strength during amyloid aggregation (v0.2)"
inferred← citeshttps://doi.org/10.7287/peerj.12381v0.2/reviews/3openalex-snapshot
Peer Review #3 of "Interplay between epigallocatechin-3-gallate and ionic strength during amyloid aggregation (v0.2)"
inferred← citeshttps://doi.org/10.7287/peerj.14137v0.1/reviews/1openalex-snapshot
Peer Review #1 of "Rapid restructurization of conformationally-distinct alpha-synuclein amyloid fibrils at an elevated temperature (v0.1)"
inferred← citeshttps://doi.org/10.7287/peerj.14137v0.1/reviews/2openalex-snapshot
Peer Review #2 of "Rapid restructurization of conformationally-distinct alpha-synuclein amyloid fibrils at an elevated temperature (v0.1)"
inferred← citeshttps://doi.org/10.7287/peerj.7554v0.1/reviews/1openalex-snapshot
Peer Review #1 of "Exploring the potential of deep-blue autofluorescence for monitoring amyloid fibril formation and dissociation (v0.1)"
inferred← citeshttps://doi.org/10.7287/peerj.7554v0.1/reviews/2openalex-snapshot
Peer Review #2 of "Exploring the potential of deep-blue autofluorescence for monitoring amyloid fibril formation and dissociation (v0.1)"
inferred← citeshttps://doi.org/10.7287/peerj.7554v0.2/reviews/1openalex-snapshot
Peer Review #1 of "Exploring the potential of deep-blue autofluorescence for monitoring amyloid fibril formation and dissociation (v0.2)"
inferred← citeshttps://doi.org/10.7287/peerj.7554v0.2/reviews/2openalex-snapshot
Peer Review #2 of "Exploring the potential of deep-blue autofluorescence for monitoring amyloid fibril formation and dissociation (v0.2)"
inferred← citeshttps://doi.org/10.7287/peerj.8208v0.1/reviews/1openalex-snapshot
Peer Review #1 of "Concentration-dependent polymorphism of insulin amyloid fibrils (v0.1)"
inferred← citeshttps://doi.org/10.7287/peerj.8208v0.1/reviews/2openalex-snapshot
Peer Review #2 of "Concentration-dependent polymorphism of insulin amyloid fibrils (v0.1)"
inferred← citeshttps://doi.org/10.7287/peerj.8208v0.1/reviews/3openalex-snapshot
Peer Review #3 of "Concentration-dependent polymorphism of insulin amyloid fibrils (v0.1)"
inferred← citeshttps://doi.org/10.7554/elife.59776openalex-snapshot
Cross-talk between individual phenol-soluble modulins in Staphylococcus aureus biofilm enables rapid and efficient amyloid formation
inferred← citeshttps://doi.org/10.7717/peerj.10918openalex-snapshot
Exploring the occurrence of thioflavin-T-positive insulin amyloid aggregation intermediates
inferred← citeshttps://doi.org/10.7717/peerj.12381openalex-snapshot
Interplay between epigallocatechin-3-gallate and ionic strength during amyloid aggregation
inferred← citeshttps://doi.org/10.7717/peerj.14137openalex-snapshot
Rapid restructurization of conformationally-distinct alpha-synuclein amyloid fibrils at an elevated temperature
inferred← citeshttps://doi.org/10.7717/peerj.7554openalex-snapshot
Exploring the potential of deep-blue autofluorescence for monitoring amyloid fibril formation and dissociation
inferred← citeshttps://doi.org/10.7717/peerj.8208openalex-snapshot
Concentration-dependent polymorphism of insulin amyloid fibrils
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.