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Self-Organization Pathways and Spatial Heterogeneity in Insulin Amyloid Fibril Formation

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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/jcp.1030490415openalex-snapshot

A mechanism for the formation of fibrils from protein molecules

inferredcites →https://doi.org/10.1002/jnr.21135openalex-snapshot

Aβ(25–35) and its C‐ and/or N‐blocked derivatives: Copper driven structural features and neurotoxicity

inferredcites →https://doi.org/10.1007/s00249-007-0137-3openalex-snapshot

Effects of confinement on insulin amyloid fibrils formation

inferredcites →https://doi.org/10.1016/0022-2836(86)90324-4openalex-snapshot

Kinetics of sickle hemoglobin polymerization

inferredcites →https://doi.org/10.1016/j.bbadis.2004.08.004openalex-snapshot

Protein misfolding and aggregation: new examples in medicine and biology of the dark side of the protein world

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.bbrc.2007.01.061openalex-snapshot

Trehalose effects on α-crystallin aggregates

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.2005.09.100openalex-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.jsb.2004.08.002openalex-snapshot

The binding of thioflavin-T to amyloid fibrils: localisation and implications

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/s0076-6879(99)09019-9openalex-snapshot

[17] Analysis of protein aggregation kinetics

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/bi002555copenalex-snapshot

Effect of Environmental Factors on the Kinetics of Insulin Fibril Formation: Elucidation of the Molecular Mechanism

inferredcites →https://doi.org/10.1021/bi0105983openalex-snapshot

Probing the Mechanism of Insulin Fibril Formation with Insulin Mutants

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/ja01107a013openalex-snapshot

Studies of the Nucleation and Growth Reactions of Selected Types of Insulin Fibrils

inferredcites →https://doi.org/10.1021/jp710131uopenalex-snapshot

Secondary Nucleation and Accessible Surface in Insulin Amyloid Fibril Formation

inferredcites →https://doi.org/10.1021/jp805560copenalex-snapshot

Thioflavin T Hydroxylation at Basic pH and Its Effect on Amyloid Fibril Detection

inferredcites →https://doi.org/10.1021/jp805822copenalex-snapshot

Thioflavin T as a Molecular Rotor: Fluorescent Properties of Thioflavin T in Solvents with Different Viscosity

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/10.1073/pnas.96.7.3590openalex-snapshot

Designing conditions for in vitro formation of amyloid protofilaments and fibrils

inferredcites →https://doi.org/10.1074/jbc.m504298200openalex-snapshot

Early Events in the Fibrillation of Monomeric Insulin

inferredcites →https://doi.org/10.1088/0957-4484/14/2/327openalex-snapshot

Dynamic scanning force microscopy investigation of nanostructured spiral-like domains in Langmuir Blodgett monolayers

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.041051205openalex-snapshot

Contribution of the intrinsic disulfide to the assembly mechanism of islet amyloid

inferredcites →https://doi.org/10.1110/ps.041266605openalex-snapshot

The aggregation kinetics of Alzheimer's β‐amyloid peptide is controlled by stochastic nucleation

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/10.1371/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.105.072660openalex-snapshot

Optical Microscopy of Growing Insulin Amyloid Spherulites on Surfaces In Vitro

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.

inferred← citeshttps://doi.org/10.2139/ssrn.4803885openalex-extracted

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

inferred← citeshttps://doi.org/10.1002/prot.24586openalex-snapshot

Kinetics of protein fibrillation controlled by fibril elongation

inferred← citeshttps://doi.org/10.1007/s00396-010-2217-7openalex-snapshot

Probing the internal environment of PVP networks generated by irradiation with different sources

inferred← citeshttps://doi.org/10.1007/s00775-022-01962-3openalex-snapshot

The influence of cations on α-lactalbumin amyloid aggregation

inferred← citeshttps://doi.org/10.1007/s00894-011-1123-3openalex-snapshot

Controlling the aggregation and rate of release in order to improve insulin formulation: molecular dynamics study of full-length insulin amyloid oligomer models

inferred← citeshttps://doi.org/10.1016/b978-0-12-394431-3.00028-6openalex-snapshot

The Formation of Amyloid-Like Superstructures

inferred← citeshttps://doi.org/10.1016/j.abb.2011.01.024openalex-snapshot

Bovine Serum Albumin protofibril-like aggregates formation: Solo but not simple mechanism

inferred← citeshttps://doi.org/10.1016/j.bbadis.2015.10.021openalex-snapshot

D-ribose-glycation of insulin prevents amyloid aggregation and produces cytotoxic adducts

inferred← citeshttps://doi.org/10.1016/j.bej.2012.01.005openalex-snapshot

Calorimetric and spectroscopic studies of the interactions between insulin and (−)-epigallocatechin-3-gallate

inferred← citeshttps://doi.org/10.1016/j.bej.2012.02.002openalex-snapshot

Effect of (−)-epigallocatechin-3-gallate on human insulin fibrillation/aggregation kinetics

inferred← citeshttps://doi.org/10.1016/j.bpc.2013.03.004openalex-snapshot

Characterization of the nucleation process of lysozyme at physiological pH: Primary but not sole process

inferred← citeshttps://doi.org/10.1016/j.bpc.2015.06.006openalex-snapshot

Thioflavin T templates amyloid β(1–40) conformation and aggregation pathway

inferred← citeshttps://doi.org/10.1016/j.bpj.2014.05.030openalex-snapshot

Sulfate Anion Delays the Self-Assembly of Human Insulin by Modifying the Aggregation Pathway

inferred← citeshttps://doi.org/10.1016/j.bpj.2020.11.2280openalex-snapshot

Zinc determines dynamical properties and aggregation kinetics of human insulin

inferred← citeshttps://doi.org/10.1016/j.ces.2012.04.031openalex-snapshot

Time evolution of amyloid fibril length distribution described by a population balance model

inferred← citeshttps://doi.org/10.1016/j.colsurfb.2011.09.018openalex-snapshot

Factors affecting the formation of insulin amyloid spherulites

inferred← citeshttps://doi.org/10.1016/j.ejpb.2022.08.018openalex-snapshot

Morphological integrity of insulin amyloid-like aggregates depends on preparation methods and post-production treatments

inferred← citeshttps://doi.org/10.1016/j.febslet.2015.07.006openalex-snapshot

The route to protein aggregate superstructures: Particulates and amyloid‐like spherulites

inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2020.08.023openalex-snapshot

Dissection of the key steps of amyloid-β peptide 1–40 fibrillogenesis

inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2020.09.104openalex-snapshot

Investigating the effect of sugar-terminated nanoparticles on amyloid fibrillogenesis of β-lactoglobulin

inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2025.141735openalex-snapshot

Probing the effect of the molecular interface of gold nanoparticles on the disassembly of insulin amyloid fibrils

inferred← citeshttps://doi.org/10.1016/j.jcis.2021.09.132openalex-snapshot

Polysorbate 80 controls Morphology, structure and stability of human insulin Amyloid-Like spherulites

inferred← citeshttps://doi.org/10.1016/j.jcis.2024.07.135openalex-snapshot

Surface-catalyzed liquid–liquid phase separation and amyloid-like assembly in microscale compartments

inferred← citeshttps://doi.org/10.1016/j.jmb.2009.10.065openalex-snapshot

Vortex-Induced Formation of Insulin Amyloid Superstructures Probed by Time-Lapse Atomic Force Microscopy and Circular Dichroism Spectroscopy

inferred← citeshttps://doi.org/10.1016/j.jmb.2009.11.012openalex-snapshot

Lability Landscape and Protease Resistance of Human Insulin Amyloid: A New Insight into Its Molecular Properties

inferred← citeshttps://doi.org/10.1016/j.jtice.2022.104360openalex-snapshot

Using Sugar-Derived Nanoparticles to Mitigate Amyloid Fibril Formation of Lysozyme

inferred← citeshttps://doi.org/10.1021/acs.biomac.0c01178openalex-snapshot

Identifying Insulin Fibril Conformational Differences by Thioflavin-T Binding Characteristics

inferred← citeshttps://doi.org/10.1021/acs.jpcb.7b03457openalex-snapshot

Inhibiting the Fibrillation of Serum Albumin Proteins in the Presence of Surface Active Ionic Liquids (SAILs) at Low pH: Spectroscopic and Microscopic Study

inferred← citeshttps://doi.org/10.1021/acs.jpclett.2c03400openalex-snapshot

Heterogeneous and Surface-Catalyzed Amyloid Aggregation Monitored by Spatially Resolved Fluorescence and Single Molecule Microscopy

inferred← citeshttps://doi.org/10.1021/acsomega.7b01776openalex-snapshot

Structural Insight of Amyloidogenic Intermediates of Human Insulin

inferred← citeshttps://doi.org/10.1021/bi101908mopenalex-snapshot

Heterogeneous Amylin Fibril Growth Mechanisms Imaged by Total Internal Reflection Fluorescence Microscopy

inferred← citeshttps://doi.org/10.1021/jp500530hopenalex-snapshot

Solvent Effects on the Dynamics of Amyloidogenic Insulin Revealed by Neutron Spin Echo Spectroscopy

inferred← citeshttps://doi.org/10.1021/jz300082xopenalex-snapshot

Neutron Scattering Reveals Enhanced Protein Dynamics in Concanavalin A Amyloid Fibrils

inferred← citeshttps://doi.org/10.1021/jz401600gopenalex-snapshot

Minimal Model for Self-Catalysis in the Formation of Amyloid-Like Elongated Fibrils

inferred← citeshttps://doi.org/10.1021/jz501570mopenalex-snapshot

α-Casein Inhibits Insulin Amyloid Formation by Preventing the Onset of Secondary Nucleation Processes

inferred← citeshttps://doi.org/10.1038/s42003-022-03810-1openalex-snapshot

Direct observation of heterogeneous formation of amyloid spherulites in real-time by super-resolution microscopy

inferred← citeshttps://doi.org/10.1038/s42003-024-06388-yopenalex-snapshot

Zinc and pH modulate the ability of insulin to inhibit aggregation of islet amyloid polypeptide

inferred← citeshttps://doi.org/10.1039/c0sm00169dopenalex-snapshot

Large-scale polymorphism and auto-catalytic effect in insulin fibrillogenesis

inferred← citeshttps://doi.org/10.1039/c2sm26297eopenalex-snapshot

Sequential dissociation of insulin amyloids probed by high pressure Fourier transform infrared spectroscopy

inferred← citeshttps://doi.org/10.1039/c8cp04838jopenalex-snapshot

Self-inhibition of insulin amyloid-like aggregation

inferred← citeshttps://doi.org/10.1063/1.4819496openalex-snapshot

Protein fibrillation due to elongation and fragmentation of initially appeared fibrils: A simple kinetic model

inferred← citeshttps://doi.org/10.1074/jbc.m113.520874openalex-snapshot

Stepwise Organization of the β-Structure Identifies Key Regions Essential for the Propagation and Cytotoxicity of Insulin Amyloid Fibrils

inferred← citeshttps://doi.org/10.1103/physrevlett.111.108105openalex-snapshot

Electrostatics Controls the Formation of Amyloid Superstructures in Protein Aggregation

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/10.1371/journal.pcbi.1002782openalex-snapshot

Kinetics of Amyloid Aggregation: A Study of the GNNQQNY Prion Sequence

inferred← citeshttps://doi.org/10.21203/rs.3.rs-929517/v1openalex-snapshot

Direct Observation of Anisotropy-Driven Formation of Amyloid Spherulites in Real-time by Super-resolution Microscopy

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/ijms18122551openalex-snapshot

Insights into Insulin Fibril Assembly at Physiological and Acidic pH and Related Amyloid Intrinsic Fluorescence

inferred← citeshttps://doi.org/10.3390/ijms21176169openalex-snapshot

Fluorescence Lifetime and Intensity of Thioflavin T as Reporters of Different Fibrillation Stages: Insights Obtained from Fluorescence Up-Conversion and Particle Size Distribution Measurements

inferred← citeshttps://doi.org/10.3390/life10050060openalex-snapshot

Trehalose Effect on The Aggregation of Model Proteins into Amyloid Fibrils

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/10.70675/b306d45azfd69z4b88z80c0z948cf17c885copenalex-snapshot

Dynamics of pathological aggregates and fibers

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/10.7717/peerj.10918openalex-snapshot

Exploring the occurrence of thioflavin-T-positive insulin amyloid aggregation intermediates

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.