On the public citation graph

Study of amyloid fibrils via atomic force microscopy

https://doi.org/10.1016/j.cocis.2012.08.001

0 signed · 246 inferred · view as graph

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

Is this your work? Sign in with ORCID and put your name on the claims that are yours.

Claim with ORCID

Reference health. See whether every reference in this work resolves to a known work and none has been retracted — and get a dated CiteStamped badge you can embed.

See reference health

What this work says

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

inferredcites →https://doi.org/10.1002/anie.200703133openalex-snapshot

Amyloids: Not Only Pathological Agents but Also Ordered Nanomaterials

inferredcites →https://doi.org/10.1002/anie.201001032openalex-snapshot

Large Mechanical Response of Single Dendronized Polymers Induced by Ionic Strength

inferredcites →https://doi.org/10.1002/anie.201100807openalex-snapshot

Direct Observation of Time‐Resolved Polymorphic States in the Self‐Assembly of End‐Capped Heptapeptides

inferredcites →https://doi.org/10.1002/jmr.1112openalex-snapshot

Structure and assembly–disassembly properties of wild‐type transthyretin amyloid protofibrils observed with atomic force microscopy

inferredcites →https://doi.org/10.1002/jmr.1113openalex-snapshot

Effect of the beta‐sheet‐breaker peptide LPFFD on oriented network of amyloid β25‐35 fibrils

inferredcites →https://doi.org/10.1006/jmbi.2001.5130openalex-snapshot

Micromechanics of isolated sickle cell hemoglobin fibers: bending moduli and persistence lengths 1 1Edited by I. Tinoco

inferredcites →https://doi.org/10.1007/s00249-009-0526-xopenalex-snapshot

Dehydration stability of amyloid fibrils studied by AFM

inferredcites →https://doi.org/10.1007/s11434-010-3201-9openalex-snapshot

Nanomechanics of individual amyloid fibrils using atomic force microscopy

inferredcites →https://doi.org/10.1016/j.bbrc.2007.07.014openalex-snapshot

Atomic force microscopic investigation on the potential early intermediate stages of fibrillogenesis of fibronectin within fibrils

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.2010.02.047openalex-snapshot

Two-Dimensional Nanoscale Structural and Functional Imaging in Individual Collagen Type I Fibrils

inferredcites →https://doi.org/10.1016/j.cocis.2008.02.002openalex-snapshot

Use of AFM in bio-related systems

inferredcites →https://doi.org/10.1016/j.febslet.2009.05.040openalex-snapshot

Methods for structural characterization of prefibrillar intermediates and amyloid fibrils

inferredcites →https://doi.org/10.1016/j.jbiomech.2009.11.026openalex-snapshot

Atomistic simulation of nanomechanical properties of Alzheimer’s Aβ(1–40) amyloid fibrils under compressive and tensile loading

inferredcites →https://doi.org/10.1016/j.jmb.2006.02.007openalex-snapshot

Polymorphism and Ultrastructural Organization of Prion Protein Amyloid Fibrils: An Insight from High Resolution Atomic Force Microscopy

inferredcites →https://doi.org/10.1016/j.nano.2010.08.001openalex-snapshot

Nanoprobing of α-synuclein misfolding and aggregation with atomic force microscopy

inferredcites →https://doi.org/10.1016/j.surfrep.2005.08.003openalex-snapshot

Force measurements with the atomic force microscope: Technique, interpretation and applications

inferredcites →https://doi.org/10.1021/bi200147aopenalex-snapshot

Single-Molecule Atomic Force Microscopy Force Spectroscopy Study of Aβ-40 Interactions

inferredcites →https://doi.org/10.1021/bm101119topenalex-snapshot

Disassembly and Reassembly of Amyloid Fibrils in Water−Ethanol Mixtures

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/bm201005kopenalex-snapshot

Peptide Mixtures Can Self-Assemble into Large Amyloid Fibers of Varying Size and Morphology

inferredcites →https://doi.org/10.1021/bm201314eopenalex-snapshot

Evidence of a Discrete Axial Structure in Unimodal Collagen Fibrils

inferredcites →https://doi.org/10.1021/bm201509bopenalex-snapshot

Shear-Induced Self-Assembly of Native Silk Proteins into Fibrils Studied by Atomic Force Microscopy

inferredcites →https://doi.org/10.1021/ma202157hopenalex-snapshot

Proteins Fibrils from a Polymer Physics Perspective

inferredcites →https://doi.org/10.1021/nn1031998openalex-snapshot

Influence of Hydrophobicity on the Surface-Catalyzed Assembly of the Islet Amyloid Polypeptide

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/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/10.1038/nnano.2012.62openalex-snapshot

Biodegradable nanocomposites of amyloid fibrils and graphene with shape-memory and enzyme-sensing properties

inferredcites →https://doi.org/10.1038/nsmb.1591openalex-snapshot

Converging concepts of protein folding in vitro and in vivo

inferredcites →https://doi.org/10.1039/b914089aopenalex-snapshot

Shear-induced structure and mechanics of β-lactoglobulin amyloid fibrils

inferredcites →https://doi.org/10.1039/c0cc02423fopenalex-snapshot

Direct observation and pH control of reversed supramolecular chirality in insulin fibrils by vibrational circular dichroism

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/c1cc14285bopenalex-snapshot

Co-assembly of human islet amyloid polypeptide (hIAPP)/insulin

inferredcites →https://doi.org/10.1039/c1cp21156kopenalex-snapshot

Structural, morphological, and kinetic studies of β-amyloid peptide aggregation on self-assembled monolayers

inferredcites →https://doi.org/10.1039/c1nr10332fopenalex-snapshot

Assembly of glucagon (proto)fibrils by longitudinal addition of oligomers

inferredcites →https://doi.org/10.1039/c1sm05382eopenalex-snapshot

Adjustable twisting periodic pitch of amyloid fibrils

inferredcites →https://doi.org/10.1039/c2cc16895bopenalex-snapshot

Spontaneous inter-conversion of insulin fibril chirality

inferredcites →https://doi.org/10.1039/c2nr30768eopenalex-snapshot

Measurement of intrinsic properties of amyloid fibrils by the peak force QNM method

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.0604035103openalex-snapshot

Characterization of the nanoscale properties of individual amyloid fibrils

inferredcites →https://doi.org/10.1073/pnas.0704305105openalex-snapshot

Stepwise dynamics of epitaxially growing single amyloid fibrils

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.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/10.1074/jbc.m109.049809openalex-snapshot

Fibril Fragmentation Enhances Amyloid Cytotoxicity

inferredcites →https://doi.org/10.1074/jbc.m110.145318openalex-snapshot

Human Tau Isoforms Assemble into Ribbon-like Fibrils That Display Polymorphic Structure and Stability

inferredcites →https://doi.org/10.1074/jbc.m111.237875openalex-snapshot

Competing Interactions Stabilize Pro- and Anti-aggregant Conformations of Human Tau

inferredcites →https://doi.org/10.1088/0953-8984/24/24/243101openalex-snapshot

Nanomechanical properties of single amyloid fibrils

inferredcites →https://doi.org/10.1088/0957-4484/19/38/384013openalex-snapshot

AFM-based force spectroscopy measurements of mature amyloid fibrils of the peptide glucagon

inferredcites →https://doi.org/10.1103/physrevlett.107.238101openalex-snapshot

Sub-Persistence-Length Complex Scaling Behavior in Lysozyme Amyloid Fibrils

inferredcites →https://doi.org/10.1111/j.1365-2818.2010.03412.xopenalex-snapshot

Real-time enzymatic degradation of human dentin collagen fibrils exposed to exogenous collagenase: an AFM study in situ

inferredcites →https://doi.org/10.1126/science.1150057openalex-snapshot

Role of Intermolecular Forces in Defining Material Properties of Protein Nanofibrils

inferredcites →https://doi.org/10.1146/annurev-biochem-090908-120656openalex-snapshot

Amyloid Structure: Conformational Diversity and Consequences

inferredcites →https://doi.org/10.1146/annurev.biochem.75.101304.123901openalex-snapshot

Protein Misfolding, Functional Amyloid, and Human Disease

inferredcites →https://doi.org/10.1186/1556-276x-6-270openalex-snapshot

Nanomechanical properties of α-synuclein amyloid fibrils: a comparative study by nanoindentation, harmonic force microscopy, and Peakforce QNM

inferredcites →https://doi.org/10.1371/journal.pbio.0060006openalex-snapshot

Conformational Equilibria in Monomeric α-Synuclein at the Single-Molecule Level

inferredcites →https://doi.org/10.1371/journal.pone.0025954openalex-snapshot

Effect of Surfaces on Amyloid Fibril Formation

inferredcites →https://doi.org/10.1529/biophysj.105.077438openalex-snapshot

Amyloid Fibrils of Glucagon Characterized by High-Resolution Atomic Force Microscopy

inferredcites →https://doi.org/10.1529/biophysj.107.127464openalex-snapshot

Concentration Dependence of α-Synuclein Fibril Length Assessed by Quantitative Atomic Force Microscopy and Statistical-Mechanical Theory

inferredcites →https://doi.org/10.1529/biophysj.108.133108openalex-snapshot

Nanomechanical Properties of Human Prion Protein Amyloid as Probed by Force Spectroscopy

What points at this work

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

inferred← citeshttps://doi.org/10.2139/ssrn.4667728openalex-extracted

Comparison of Morphological and Mechanical Properties of Hen Egg White Lysozyme (Hewl) Amyloid Fibrils Incubated Under Acidic and Neutral Environments

inferred← citeshttps://doi.org/10.1002/9781118845363.ch6openalex-snapshot

Structural Properties of Bacterial Inclusion Bodies

inferred← citeshttps://doi.org/10.1002/9781118876015.ch16openalex-snapshot

Functional Amyloid Fibrils

inferred← citeshttps://doi.org/10.1002/adfm.202517899openalex-snapshot

Peptide‐Based Electronics for Neuromorphic Hardware

inferred← citeshttps://doi.org/10.1002/adma.202414658openalex-snapshot

Sustainable Smart Packaging from Protein Nanofibrils

inferred← citeshttps://doi.org/10.1002/ange.201409050openalex-snapshot

Influence of the β‐Sheet Content on the Mechanical Properties of Aggregates during Amyloid Fibrillization

inferred← citeshttps://doi.org/10.1002/ange.201410768openalex-snapshot

Chirality‐Assisted Ring‐Like Aggregation of Aβ(1–40) at Liquid–Solid Interfaces: A Stereoselective Two‐Step Assembly Process

inferred← citeshttps://doi.org/10.1002/ange.202408163openalex-snapshot

Structural Mapping of Protein Aggregates in Live Cells Modeling Huntington's Disease

inferred← citeshttps://doi.org/10.1002/anie.201409050openalex-snapshot

Influence of the β‐Sheet Content on the Mechanical Properties of Aggregates during Amyloid Fibrillization

inferred← citeshttps://doi.org/10.1002/anie.201410768openalex-snapshot

Chirality‐Assisted Ring‐Like Aggregation of Aβ(1–40) at Liquid–Solid Interfaces: A Stereoselective Two‐Step Assembly Process

inferred← citeshttps://doi.org/10.1002/anie.202408163openalex-snapshot

Structural Mapping of Protein Aggregates in Live Cells Modeling Huntington's Disease

inferred← citeshttps://doi.org/10.1002/btpr.1812openalex-snapshot

Protein misfolding and aggregation research: Some thoughts on improving quality and utility

inferred← citeshttps://doi.org/10.1002/ijch.201900083openalex-snapshot

Self‐Assembly in Protein‐Based Bionanomaterials

inferred← citeshttps://doi.org/10.1002/polb.23428openalex-snapshot

Polymer physics inspired approaches for the study of the mechanical properties of amyloid fibrils

inferred← citeshttps://doi.org/10.1002/pro.70066openalex-snapshot

Guide to the structural characterization of protein aggregates and amyloid fibrils by CD spectroscopy

inferred← citeshttps://doi.org/10.1002/pro.70151openalex-snapshot

Experimental methods for studying amyloid cross‐interactions

inferred← citeshttps://doi.org/10.1007/978-1-4939-4029-5_20openalex-snapshot

Applications of AFM in Pharmaceutical Sciences

inferred← citeshttps://doi.org/10.1007/978-1-4939-7811-3_1openalex-snapshot

Methods to Characterize the Nanostructure and Molecular Organization of Amphiphilic Peptide Assemblies

inferred← citeshttps://doi.org/10.1007/978-1-4939-8820-4_5openalex-snapshot

A Multipronged Method for Unveiling Subtle Structural–Functional Defects of Mutant Chaperone Molecules Causing Human Chaperonopathies

inferred← citeshttps://doi.org/10.1007/978-3-031-29360-3_8openalex-snapshot

Characterization of Peptide-Based Nanomaterials

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/10.1007/978-981-13-9791-2_7openalex-snapshot

Protein Microgels from Amyloid Fibril Networks

inferred← citeshttps://doi.org/10.1007/s00223-026-01505-xopenalex-snapshot

Serine-16 Phosphorylation, C-Terminal Truncation, and Ion-Specific Interactions Coordinate Amelogenin Nanoribbon Formation

inferred← citeshttps://doi.org/10.1007/s00249-020-01421-4openalex-snapshot

Measurement of length distribution of beta-lactoglobulin fibrils by multiwavelength analytical ultracentrifugation

inferred← citeshttps://doi.org/10.1007/s12013-024-01293-xopenalex-snapshot

Screening Carbon Nano Materials for Preventing Amyloid Protein Aggregation by Adopting a Facile Method

inferred← citeshttps://doi.org/10.1007/s12274-020-2748-2openalex-snapshot

Effect of metallic nanoparticles on amyloid fibrils and their influence to neural cell toxicity

inferred← citeshttps://doi.org/10.1007/s13361-016-1347-7openalex-snapshot

Human Islet Amyloid Polypeptide N-Terminus Fragment Self-Assembly: Effect of Conserved Disulfide Bond on Aggregation Propensity

inferred← citeshttps://doi.org/10.1007/s42493-018-00009-7openalex-snapshot

Computer Simulation of Protein Materials at Multiple Length Scales: From Single Proteins to Protein Assemblies

inferred← citeshttps://doi.org/10.1007/s44211-022-00185-5openalex-snapshot

J-aggregation of 5, 10, 15, 20-tetraphenyl-21H, 23H-porphinetetrasulfonic acid in a molecular crowding environment simulated using dextran

inferred← citeshttps://doi.org/10.1016/b978-0-08-102850-6.00005-xopenalex-snapshot

Characterization techniques of protein and peptide nanofibers: Self-assembly kinetics

inferred← citeshttps://doi.org/10.1016/b978-0-323-46142-9.00009-8openalex-snapshot

Short peptide self-assembled nanostructures for therapeutics innovative delivery

inferred← citeshttps://doi.org/10.1016/bs.mie.2024.02.013openalex-snapshot

Structural characterization of amyloid aggregates with spatially resolved infrared spectroscopy

inferred← citeshttps://doi.org/10.1016/j.ab.2016.03.015openalex-snapshot

Analysis of the length distribution of amyloid fibrils by centrifugal sedimentation

inferred← citeshttps://doi.org/10.1016/j.abb.2019.02.001openalex-snapshot

Atomic force microscopy for single molecule characterisation of protein aggregation

inferred← citeshttps://doi.org/10.1016/j.abb.2025.110462openalex-snapshot

Fibrillar structures detected by AFM in the cerebrospinal fluid of patients affected by Alzheimer's disease and other neurological conditions

inferred← citeshttps://doi.org/10.1016/j.bbadva.2023.100086openalex-snapshot

Insight into the self-assembly and gel formation of a bioactive peptide derived from bovine casein

inferred← citeshttps://doi.org/10.1016/j.bbamem.2018.04.012openalex-snapshot

Impact of membrane curvature on amyloid aggregation

inferred← citeshttps://doi.org/10.1016/j.bbapap.2022.140767openalex-snapshot

A unifying framework for amyloid-mediated membrane damage: The lipid-chaperone hypothesis

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.bioorg.2026.109539openalex-snapshot

Recent advances in small molecules for amyloid fibril inhibition: chemical strategies and molecular mechanistic insights from lysozyme and insulin models

inferred← citeshttps://doi.org/10.1016/j.bpj.2020.10.045openalex-snapshot

Atomic Force Microscopy Imaging and Nanomechanical Properties of Six Tau Isoform Assemblies

inferred← citeshttps://doi.org/10.1016/j.carbon.2014.01.055openalex-snapshot

Hybrid peptide–carbon nanotube dispersions and hydrogels

inferred← citeshttps://doi.org/10.1016/j.colsurfb.2019.01.033openalex-snapshot

Investigating the effects of amino acid-based surface modification of carbon nanoparticles on the kinetics of insulin amyloid formation

inferred← citeshttps://doi.org/10.1016/j.colsurfb.2024.114185openalex-snapshot

Application of metallic nanoparticles-amyloid protein supramolecular materials in tissue engineering and drug delivery: Recent progress and perspectives

inferred← citeshttps://doi.org/10.1016/j.cpc.2017.01.011openalex-snapshot

FibrilJ: ImageJ plugin for fibrils’ diameter and persistence length determination

inferred← citeshttps://doi.org/10.1016/j.crfs.2026.101577openalex-snapshot

Predicting the compression mechanical properties of muscle from microscale indentation mechanics using multiscale mechanical models

inferred← citeshttps://doi.org/10.1016/j.foodchem.2025.146523openalex-snapshot

Hofmeister and electrostatic modulation of the structure and polymorphism of rice protein fibrils

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.2019.105343openalex-snapshot

In vitro digestion and stability under environmental stresses of ovotransferrin nanofibrils

inferred← citeshttps://doi.org/10.1016/j.foodhyd.2022.107797openalex-snapshot

Epigallocatechin-3-gallate mediated self-assemble behavior and gelling properties of the ovalbumin with heating treatment

inferred← citeshttps://doi.org/10.1016/j.foodhyd.2024.109871openalex-snapshot

Elucidating the modulatory influence of Hofmeister divalent ions on the structural dynamics and rheological properties of soy protein amyloid fibrils

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.2024.110796openalex-snapshot

Amelioration of extremely acidic environment of soy protein amyloid fibrils to enhance gelation performance by dialysis strategy: Effects of pH and ions

inferred← citeshttps://doi.org/10.1016/j.foodhyd.2024.110899openalex-snapshot

Adsorption mechanism of soy protein amyloid fibrils with different morphological structures at the interface of oil-in-water emulsion

inferred← citeshttps://doi.org/10.1016/j.foodhyd.2025.111049openalex-snapshot

β-lactoglobulin amyloid fibrils: Architecture, preparation, characterization, and potential applications

inferred← citeshttps://doi.org/10.1016/j.foodhyd.2025.111740openalex-snapshot

Structural evolution of soy protein amyloid fibrils induced by high-temperature pretreatment

inferred← citeshttps://doi.org/10.1016/j.foodhyd.2025.111979openalex-snapshot

Pulsed electric field facilitated fibrillation of soy protein isolate: preparation, characterization, and functional properties

inferred← citeshttps://doi.org/10.1016/j.foodhyd.2025.112116openalex-snapshot

Exploring the time-regulated fibrillation of chickpea protein isolate: Formation, structural characteristics, and improved functional properties

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.2026.112527openalex-snapshot

Structural transitions and emulsification properties of pH-shift soy protein amyloid fibrils

inferred← citeshttps://doi.org/10.1016/j.foodhyd.2026.112746openalex-snapshot

Bidirectional regulation of gluten amyloid fibril formation by hydrocolloids during boiling

inferred← citeshttps://doi.org/10.1016/j.foodhyd.2026.112839openalex-snapshot

Effects of simulated baking conditions on the formation mechanism of wheat gluten amyloid-like fibrils

inferred← citeshttps://doi.org/10.1016/j.foodhyd.2026.113239openalex-snapshot

Protein nanofibrils as next-generation architectures for Pickering emulsions in food and nutraceuticals

inferred← citeshttps://doi.org/10.1016/j.foodhyd.2026.113416openalex-snapshot

Divalent cation-mediated regulation of the hierarchical structure and rheological properties of ovalbumin fibrils

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.freeradbiomed.2025.11.044openalex-snapshot

Dual glycation and oxidation of tau protein: impact of methylglyoxal and hydrogen peroxide on tau structure and fibril assembly

inferred← citeshttps://doi.org/10.1016/j.ifset.2026.104716openalex-snapshot

Hofmeister anion-dependent amyloid fibrillation enhances gel strength of mung bean (Vigna radiata) protein

inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2015.10.029openalex-snapshot

Generation-dependent effect of PAMAM dendrimers on human insulin fibrillation and thermal stability

inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2022.02.104openalex-snapshot

Progress in infrared spectroscopy as an efficient tool for predicting protein secondary structure

inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2022.12.134openalex-snapshot

The impact of α-synuclein aggregates on blood-brain barrier integrity in the presence of neurovascular unit cells

inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2023.124855openalex-snapshot

Amyloid-like aggregation of recombinant β-lactoglobulin at pH 3.5 and 7.0: Is disulfide bond removal the key to fibrillation?

inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2026.152648openalex-snapshot

Nanoscale insights into the structure and properties of tau protein fibrils revealed by scanning probe microscopy-based approaches: A review

inferred← citeshttps://doi.org/10.1016/j.jmb.2020.11.016openalex-snapshot

ATP Impedes the Inhibitory Effect of Hsp90 on Aβ40 Fibrillation

inferred← citeshttps://doi.org/10.1016/j.jmb.2021.167124openalex-snapshot

On the Structural Diversity and Individuality of Polymorphic Amyloid Protein Assemblies

inferred← citeshttps://doi.org/10.1016/j.jmb.2025.169008openalex-snapshot

How is the Amyloid Fold Built? Polymorphism and the Microscopic Mechanisms of Fibril Assembly

inferred← citeshttps://doi.org/10.1016/j.jmbbm.2021.104776openalex-snapshot

Quantitative nanomechanical properties evaluation of a family of β-sheet peptide fibres using rapid bimodal AFM

inferred← citeshttps://doi.org/10.1016/j.jsb.2017.10.006openalex-snapshot

Sup35NMp morphology evaluation on Au, Si, formvar and mica surfaces using AFM, SEM and TEM

inferred← citeshttps://doi.org/10.1016/j.nantod.2024.102615openalex-snapshot

Food-derived protein fibril-based multiscale structured systems: Construction, potential applications, and future prospects

inferred← citeshttps://doi.org/10.1016/j.neuroscience.2022.02.031openalex-snapshot

Nanoscale Structural Characterization and Impact on Long-term memory of Amyloid-β42 Oligomeric forms in Zebrafish

inferred← citeshttps://doi.org/10.1016/j.pnmrs.2026.101611openalex-snapshot

Application of NMR spectroscopy for studies of self-association and aggregation in protein formulations

inferred← citeshttps://doi.org/10.1016/j.polymer.2019.121626openalex-snapshot

Thermally triggered self-assembly of κ-casein amyloid nanofibrils and their nanomechanical properties

inferred← citeshttps://doi.org/10.1016/j.tibtech.2026.06.012openalex-snapshot

Bacterial spores as a modular platform for the production of amyloids for materials

inferred← citeshttps://doi.org/10.1016/j.xcrp.2025.102430openalex-snapshot

Scanning probe microscopy elucidates gelation and rejuvenation of biomolecular condensates

inferred← citeshttps://doi.org/10.1016/j.xphs.2019.10.006openalex-snapshot

Evaluation of Nanoparticle Tracking Analysis for the Detection of Rod-Shaped Particles and Protein Aggregates

inferred← citeshttps://doi.org/10.1017/s0033583520000086openalex-snapshot

Single-molecule studies of amyloid proteins: from biophysical properties to diagnostic perspectives

inferred← citeshttps://doi.org/10.1017/s143192761900744xopenalex-snapshot

Atomic Force Microscopy Investigation of Influenza A Virus Nuclear Export Protein Aggregation

inferred← citeshttps://doi.org/10.1021/ac503845fopenalex-snapshot

Label-Free Measurement of Amyloid Elongation by Suspended Microchannel Resonators

inferred← citeshttps://doi.org/10.1021/acs.biochem.5b01110openalex-snapshot

Conformational Switching and Nanoscale Assembly of Human Prion Protein into Polymorphic Amyloids via Structurally Labile Oligomers

inferred← citeshttps://doi.org/10.1021/acs.biochem.7b00243openalex-snapshot

Laser-Induced Population Inversion in Rhodamine 6G for Lysozyme Oligomer Detection

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.8b00408openalex-snapshot

Nanomechanics of Pectin-Linked β-Lactoglobulin Nanofibril Bundles

inferred← citeshttps://doi.org/10.1021/acs.jafc.4c12444openalex-snapshot

Investigation of the Differences in Amyloid-Like Fibrils Derived from Wheat Gluten with Varying Structures under Typical Food Processing Conditions

inferred← citeshttps://doi.org/10.1021/acs.jafc.5c12097openalex-snapshot

Nanofilm Formed via Amyloid-Like Protein Aggregation for Interfacial Modification: Prospects in Food, Agricultural, and Beyond

inferred← citeshttps://doi.org/10.1021/acs.jpcb.0c00916openalex-snapshot

Investigation of the Dissociation Mechanism of Single-Walled Carbon Nanotube on Mature Amyloid-β Fibrils at Single Nanotube Level

inferred← citeshttps://doi.org/10.1021/acs.jpcb.3c06925openalex-snapshot

Zn2+ Binding Increases Parallel Structure in the Aβ(16–22) Oligomer by Disrupting Salt Bridge in Antiparallel Structure

inferred← citeshttps://doi.org/10.1021/acs.jpcb.5b07221openalex-snapshot

Preformed Seeds Modulate Native Insulin Aggregation Kinetics

inferred← citeshttps://doi.org/10.1021/acs.jpcb.6b05619openalex-snapshot

Characterization of Salt-Induced Oligomerization of Human β2-Microglobulin at Low pH

inferred← citeshttps://doi.org/10.1021/acs.jpcb.6b09475openalex-snapshot

Human Islet Amyloid Polypeptide Assembly: The Key Role of the 8–20 Fragment

inferred← citeshttps://doi.org/10.1021/acs.jpclett.6c01930openalex-snapshot

Multipathway Aggregation Drives Concentration-Dependent Amyloid Polymorphism and Time-Dependent Morphological Evolution

inferred← citeshttps://doi.org/10.1021/acsami.3c06460openalex-snapshot

Biophysical Properties of the Fibril Structure of the Toxic Conformer of Amyloid-β42: Characterization by Atomic Force Microscopy in Liquid and Molecular Docking

inferred← citeshttps://doi.org/10.1021/acscentsci.7b00115openalex-snapshot

Molecular, Local, and Network-Level Basis for the Enhanced Stiffness of Hydrogel Networks Formed from Coassembled Racemic Peptides: Predictions from Pauling and Corey

inferred← citeshttps://doi.org/10.1021/acsnano.4c00883openalex-snapshot

Hybrid Amyloid–Chitin Nanofibrils for Magnetic and Catalytic Aerogels

inferred← citeshttps://doi.org/10.1021/acsnano.9b09676openalex-snapshot

The Influence of Pathogenic Mutations in α‑Synuclein on Biophysical and Structural Characteristics of Amyloid Fibrils

inferred← citeshttps://doi.org/10.1021/acsomega.3c01606openalex-snapshot

Ambient Temperature Affects Protein Self-Assembly by Interfering with the Interfacial Aggregation Behavior

inferred← citeshttps://doi.org/10.1021/acsomega.5c07595openalex-snapshot

Amyloidogenic Growth Observation of Stem Bromelain via Atomic Force Microscopy

inferred← citeshttps://doi.org/10.1021/acssuschemeng.5c01218openalex-snapshot

Toward Clickable Protein Networks: Orthogonal Amidation of Self-Assembled Lysozyme and Bovine Serum Albumin Nanofibers

inferred← citeshttps://doi.org/10.1021/acssuschemeng.8b00600openalex-snapshot

Enzymatic Hydrolysis in the Green Production of Bacterial Cellulose Nanocrystals

inferred← citeshttps://doi.org/10.1021/bm401646xopenalex-snapshot

Engineered Lysozyme Amyloid Fibril Networks Support Cellular Growth and Spreading

inferred← citeshttps://doi.org/10.1021/jacs.1c02974openalex-snapshot

Multiple-State Monitoring of SOD1 Amyloid Formation at Single-Residue Resolution by Rheo-NMR Spectroscopy

inferred← citeshttps://doi.org/10.1021/jp400009jopenalex-snapshot

Fibrils or Globules? Tuning the Morphology of Peptide Aggregates from Helical Building Blocks

inferred← citeshttps://doi.org/10.1021/la5049369openalex-snapshot

Fibrillar Structures Formed by Covalently Bound, Short, β-Stranded Peptides on Self-Assembled Monolayers

inferred← citeshttps://doi.org/10.1021/nn404886kopenalex-snapshot

Polymorphism Complexity and Handedness Inversion in Serum Albumin Amyloid Fibrils

inferred← citeshttps://doi.org/10.1021/nn504869dopenalex-snapshot

Protein Microgels from Amyloid Fibril Networks

inferred← citeshttps://doi.org/10.1038/ncomms15902openalex-snapshot

Silk micrococoons for protein stabilisation and molecular encapsulation

inferred← citeshttps://doi.org/10.1038/ncomms8831openalex-snapshot

Infrared nanospectroscopy characterization of oligomeric and fibrillar aggregates during amyloid formation

inferred← citeshttps://doi.org/10.1038/s41467-018-06345-4openalex-snapshot

Microfluidic deposition for resolving single-molecule protein architecture and heterogeneity

inferred← citeshttps://doi.org/10.1038/s41467-019-11473-6openalex-snapshot

Shape and fluctuations of frustrated self-assembled nano ribbons

inferred← citeshttps://doi.org/10.1038/s41467-021-26553-9openalex-snapshot

Role of mutations and post-translational modifications in systemic AL amyloidosis studied by cryo-EM

inferred← citeshttps://doi.org/10.1038/s41586-025-09244-zopenalex-snapshot

How short peptides disassemble tau fibrils in Alzheimer’s disease

inferred← citeshttps://doi.org/10.1038/s41598-019-56788-yopenalex-snapshot

Amyloidophilic Molecule Interactions on the Surface of Insulin Fibrils: Cooperative Binding and Fluorescence Quenching

inferred← citeshttps://doi.org/10.1038/s42004-020-00372-3openalex-snapshot

Quantification of amyloid fibril polymorphism by nano-morphometry reveals the individuality of filament assembly

inferred← citeshttps://doi.org/10.1039/9781839161148-00019openalex-snapshot

Characterization of Peptides and Their Assemblies

inferred← citeshttps://doi.org/10.1039/c3fd00083dopenalex-snapshot

Polymorphism in bovine serum albumin fibrils: morphology and statistical analysis

inferred← citeshttps://doi.org/10.1039/c3nr06752aopenalex-snapshot

Chirality effects at each amino acid position on tripeptide self-assembly into hydrogel biomaterials

inferred← citeshttps://doi.org/10.1039/c3sm27244copenalex-snapshot

Lysine functionalised amyloid fibrils: the design and assembly of a TTR1-based peptide

inferred← citeshttps://doi.org/10.1039/c3sm51029hopenalex-snapshot

The effect of pH on the self-assembly of a collagen derived peptide amphiphile

inferred← citeshttps://doi.org/10.1039/c4cp05563bopenalex-snapshot

On the lag phase in amyloid fibril formation

inferred← citeshttps://doi.org/10.1039/c4cs00176aopenalex-snapshot

Quantitative biomolecular imaging by dynamic nanomechanical mapping

inferred← citeshttps://doi.org/10.1039/c4nr05109bopenalex-snapshot

Mechanical properties of amyloid-like fibrils defined by secondary structures

inferred← citeshttps://doi.org/10.1039/c4sm02092hopenalex-snapshot

Stimuli responsive fibrous hydrogels from hierarchical self-assembly of a triblock copolypeptide

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/c5sm01037copenalex-snapshot

Amyloid-like fibrils formed from intrinsically disordered caseins: physicochemical and nanomechanical properties

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/c6nr00863aopenalex-snapshot

AFM-based mechanical characterization of single nanofibres

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/c8cs00115dopenalex-snapshot

Multicomponent peptide assemblies

inferred← citeshttps://doi.org/10.1039/d1nr03190bopenalex-snapshot

Unveiling the interaction of protein fibrils with gold nanoparticles by plasmon enhanced nano-spectroscopy

inferred← citeshttps://doi.org/10.1039/d2an01591aopenalex-snapshot

Novel perspective for protein–drug interaction analysis: atomic force microscope

inferred← citeshttps://doi.org/10.1039/d2cs00756hopenalex-snapshot

Rational design of functional amyloid fibrillar assemblies

inferred← citeshttps://doi.org/10.1039/d3sm00408bopenalex-snapshot

A coarse-grained molecular model of amyloid fibrils systems

inferred← citeshttps://doi.org/10.1039/d4dt00704bopenalex-snapshot

Modulating the aggregation of human prion protein PrP 106–126 by an indole-based cyclometallated palladium complex

inferred← citeshttps://doi.org/10.1039/d4nh00088aopenalex-snapshot

N-Formylation modifies membrane damage associated with PSMα3 interfacial fibrillation

inferred← citeshttps://doi.org/10.1042/bsr20181415openalex-snapshot

Congo Red and amyloids: history and relationship

inferred← citeshttps://doi.org/10.1063/5.0236610openalex-snapshot

The mechanobiology of biomolecular condensates

inferred← citeshttps://doi.org/10.1073/pnas.2112783118openalex-snapshot

Amyloid β 42 fibril structure based on small-angle scattering

inferred← citeshttps://doi.org/10.1080/1061186x.2022.2063297openalex-snapshot

Formulation development of tocopherol polyethylene glycol nanoengineered polyamidoamine dendrimer for neuroprotection and treatment of Alzheimer disease

inferred← citeshttps://doi.org/10.1080/21690707.2015.1056905openalex-snapshot

Collapsed state of polyglutamic acid results in amyloid spherulite formation

inferred← citeshttps://doi.org/10.1088/0034-4885/76/4/046601openalex-snapshot

The self-assembly, aggregation and phase transitions of food protein systems in one, two and three dimensions

inferred← citeshttps://doi.org/10.1088/1674-1056/26/12/128701openalex-snapshot

Anisotropic formation mechanism and nanomechanics for the self-assembly process of cross- β peptides

inferred← citeshttps://doi.org/10.1101/2023.10.09.561223openalex-snapshot

Nanoscale Structural Mapping of Protein Aggregates in Live Cells Modeling Huntington’s Disease

inferred← citeshttps://doi.org/10.1101/2024.01.29.577710openalex-snapshot

Imaging Aβ aggregation by liquid-phase transmission electron microscopy

inferred← citeshttps://doi.org/10.1111/1541-4337.70399openalex-snapshot

Modulation of Food‐Derived Protein Fibrillization: A Comprehensive Review of Regulatory Strategies, Enhanced Functional Properties and Food Applications

inferred← citeshttps://doi.org/10.1111/febs.17215openalex-snapshot

Type I Hsp40s/ DnaJs aggregates exhibit features reminiscent of amyloidogenic structures

inferred← citeshttps://doi.org/10.1111/ijfs.14363openalex-snapshot

A review of current and future food applications of natural hydrocolloids

inferred← citeshttps://doi.org/10.1126/sciadv.aaz6014openalex-snapshot

Complete aggregation pathway of amyloid β (1-40) and (1-42) resolved on an atomically clean interface

inferred← citeshttps://doi.org/10.1134/s0006297924120022openalex-snapshot

Pathogenesis-Associated Bacterial Amyloids: The Network of Interactions

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-food-030216-025753openalex-snapshot

Enzyme-Based Strategies for Structuring Foods for Improved Functionality

inferred← citeshttps://doi.org/10.1155/2016/5873695openalex-snapshot

Nanomechanical Characterization of Amyloid Fibrils Using Single-Molecule Experiments and Computational Simulations

inferred← citeshttps://doi.org/10.1155/2019/8452851openalex-snapshot

Atomic Force Microscopy on Biological Materials Related to Pathological Conditions

inferred← citeshttps://doi.org/10.1177/1934578x241306603openalex-snapshot

The Effects of Naturally Occurring Phenols on Amyloid Fibrils from Insulin in the Liquid Phase Using Atomic Force Microscopy

inferred← citeshttps://doi.org/10.21203/rs.3.rs-2631727/v1openalex-snapshot

Resolving the soluble-to-toxic transformation of amyloidogenic proteins: A method to assess intervention by small-molecules

inferred← citeshttps://doi.org/10.2139/ssrn.5228001openalex-snapshot

Amyloid Fibril Formation of Human Recombinant Insulin Due to the Interfacial Hydrophobicity of Fluorocarbon Polymer Membranes

inferred← citeshttps://doi.org/10.2174/2210681212666220217121830openalex-snapshot

Preparation and Chemical/Physical Characterization of Individual Nanoscaled Fibrils

inferred← citeshttps://doi.org/10.3389/fbioe.2019.00083openalex-snapshot

The Role of Structural Polymorphism in Driving the Mechanical Performance of the Alzheimer's Beta Amyloid Fibrils

inferred← citeshttps://doi.org/10.3389/fmolb.2024.1376411openalex-snapshot

Exploring the Aβ1-42 fibrillogenesis timeline by atomic force microscopy and surface enhanced Raman spectroscopy

inferred← citeshttps://doi.org/10.3390/biom15010040openalex-snapshot

Saponins Effect on Human Insulin Amyloid Aggregation

inferred← citeshttps://doi.org/10.3390/bios14080400openalex-snapshot

Capillary Flow-Based One-Minute Quantification of Amyloid Proteolysis

inferred← citeshttps://doi.org/10.3390/fib11100083openalex-snapshot

Overcoming Challenges and Limitations Regarding the Atomic Force Microscopy Imaging and Mechanical Characterization of Nanofibers

inferred← citeshttps://doi.org/10.3390/foods12030486openalex-snapshot

Cultivation Factors That Affect Amyloid-β Aggregation Inhibitory Activity in Perilla frutescens var. crispa

inferred← citeshttps://doi.org/10.3390/foods13213411openalex-snapshot

Fava Bean Protein Nanofibrils Modulate Cell Membrane Interfaces for Biomolecular Interactions as Unveiled by Atomic Force Microscopy

inferred← citeshttps://doi.org/10.3390/gels12050399openalex-snapshot

Chirality Effect on Physical and Biological Properties of Peptide-Based Hydrogels

inferred← citeshttps://doi.org/10.3390/ijms21124287openalex-snapshot

High-Speed Atomic Force Microscopy Reveals the Structural Dynamics of the Amyloid-β and Amylin Aggregation Pathways

inferred← citeshttps://doi.org/10.3390/ijms21197240openalex-snapshot

Biological Functions of Prokaryotic Amyloids in Interspecies Interactions: Facts and Assumptions

inferred← citeshttps://doi.org/10.3390/ijms22105075openalex-snapshot

Temperature-Dependent Structural Variability of Prion Protein Amyloid Fibrils

inferred← citeshttps://doi.org/10.3390/life13071523openalex-snapshot

Realization of Amyloid-like Aggregation as a Common Cause for Pathogenesis in Diseases

inferred← citeshttps://doi.org/10.3390/mi12121501openalex-snapshot

Micro/Nanopatterned Superhydrophobic Surfaces Fabrication for Biomolecules and Biomaterials Manipulation and Analysis

inferred← citeshttps://doi.org/10.3390/molecules201119658openalex-snapshot

The Phe-Phe Motif for Peptide Self-Assembly in Nanomedicine

inferred← citeshttps://doi.org/10.37349/ebmx.2026.101357openalex-snapshot

Amyloid fibril formation of human recombinant insulin due to the interfacial hydrophobicity of fluorocarbon polymer membranes

inferred← citeshttps://doi.org/10.53846/goediss-4822openalex-snapshot

Label-Free Measurements of Amyloid Formation by Suspended Microchannel Resonators

inferred← citeshttps://doi.org/10.64898/2026.01.13.699108openalex-snapshot

An Aggregation Prone Region (APR) in talin controls talin self-interactions to regulate integrin adhesion complex dynamics

inferred← citeshttps://doi.org/10.64898/2026.05.29.728721openalex-snapshot

Extracellular chaperones modulate AL light chains fibrillar aggregation and contribute to amyloid structural heterogeneity

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.