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Identifying the amylome, proteins capable of forming amyloid-like fibrils

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What this work says

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

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Dictionary of protein secondary structure: Pattern recognition of hydrogen‐bonded and geometrical features

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Shape complementarity at protein–protein interfaces

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Common core structure of amyloid fibrils by synchrotron X-ray diffraction 1 1Edited by F. E. Cohen

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“Cross-β” conformation in proteins

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The interpretation of protein structures: Estimation of static accessibility

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How Evolutionary Pressure Against Protein Aggregation Shaped Chaperone Specificity

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Prediction of Aggregation-Prone Regions in Structured Proteins

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Principles of protein folding, misfolding and aggregation

inferredcites →https://doi.org/10.1016/s0014-5793(01)02384-5openalex-snapshot

Amyloid fibril formation by a helical cytochrome

inferredcites →https://doi.org/10.1016/s1359-0278(98)00002-9openalex-snapshot

Protein aggregation: folding aggregates, inclusion bodies and amyloid

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From the globular to the fibrous state: protein structure and structural conversion in amyloid formation

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The Acid-Mediated Denaturation Pathway of Transthyretin Yields a Conformational Intermediate That Can Self-Assemble into Amyloid

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Identical pentapeptides with different backbones

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Human lysozyme gene mutations cause hereditary systemic amyloidosis

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Structure of the cross-β spine of amyloid-like fibrils

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Amyloid-like fibrils of ribonuclease A with three-dimensional domain-swapped and native-like structure

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Atomic structures of amyloid cross-β spines reveal varied steric zippers

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Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins

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Amyloid formation by globular proteins under native conditions

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Molecular mechanisms for protein-encoded inheritance

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The X-ray interpretation of denaturation and the structure of the seed globulins

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αB-crystallin, a small heat-shock protein, prevents the amyloid fibril growth of an amyloid β-peptide and β2-microglobulin

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An amyloid-forming peptide from the yeast prion Sup35 reveals a dehydrated β-sheet structure for amyloid

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The 3D profile method for identifying fibril-forming segments of proteins

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A systematic screen of β 2 -microglobulin and insulin for amyloid-like segments

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A role for destabilizing amino acid replacements in light-chain amyloidosis.

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Native protein sequences are close to optimal for their structures

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Short protein segments can drive a non-fibrillizing protein into the amyloid state

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Atomic structure of the cross‐β spine of islet amyloid polypeptide (amylin)

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Insight into the Structure of Amyloid Fibrils from the Analysis of Globular Proteins

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inferred← citeshttps://doi.org/10.1016/bs.apcsb.2019.10.001openalex-snapshot

Combining molecular dynamics simulations and experimental analyses in protein misfolding

inferred← citeshttps://doi.org/10.1016/bs.ircmb.2016.08.008openalex-snapshot

From the Evolution of Protein Sequences Able to Resist Self-Assembly to the Prediction of Aggregation Propensity

inferred← citeshttps://doi.org/10.1016/bs.ircmb.2016.08.012openalex-snapshot

What Makes a Prion

inferred← citeshttps://doi.org/10.1016/bs.mie.2024.04.004openalex-snapshot

Characterization of self-templating catalytic amyloids

inferred← citeshttps://doi.org/10.1016/bs.pmbts.2024.03.003openalex-snapshot

Morphological features and types of aggregated structures

inferred← citeshttps://doi.org/10.1016/bs.pmbts.2024.03.005openalex-snapshot

Prediction of protein aggregation

inferred← citeshttps://doi.org/10.1016/bs.pmbts.2024.03.010openalex-snapshot

Pathways of amyloid fibril formation and protein aggregation

inferred← citeshttps://doi.org/10.1016/j.abb.2017.03.003openalex-snapshot

Overcoming electrostatic repulsions during amyloid assembly: Effect of pH and interaction with divalent metals using model peptides

inferred← citeshttps://doi.org/10.1016/j.abb.2017.06.007openalex-snapshot

Pressure effects on α-synuclein amyloid fibrils: An experimental investigation on their dissociation and reversible nature

inferred← citeshttps://doi.org/10.1016/j.actbio.2020.07.023openalex-snapshot

Nanoribbon self-assembly and hydrogel formation from an NOctanoyl octapeptide derived from the antiparallel β-Interface of a protein homotetramer

inferred← citeshttps://doi.org/10.1016/j.actbio.2021.05.003openalex-snapshot

Peptide-based supramolecular vaccine systems

inferred← citeshttps://doi.org/10.1016/j.bbamcr.2013.05.007openalex-snapshot

N-terminally truncated forms of human cathepsin F accumulate in aggresome-like inclusions

inferred← citeshttps://doi.org/10.1016/j.bbamem.2013.04.012openalex-snapshot

ATR-FTIR: A “rejuvenated” tool to investigate amyloid proteins

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.2010.04.001openalex-snapshot

Molecular mechanism of Thioflavin-T binding to amyloid fibrils

inferred← citeshttps://doi.org/10.1016/j.bbapap.2012.07.013openalex-snapshot

Kinetic intermediates of amyloid fibrillation studied by hydrogen exchange methods with nuclear magnetic resonance

inferred← citeshttps://doi.org/10.1016/j.bbapap.2013.04.030openalex-snapshot

A radish seed antifungal peptide with a high amyloid fibril-forming propensity

inferred← citeshttps://doi.org/10.1016/j.bbapap.2013.08.013openalex-snapshot

Acceleration of the depolymerization of amyloid β fibrils by ultrasonication

inferred← citeshttps://doi.org/10.1016/j.bbapap.2014.03.001openalex-snapshot

Self-assembly of proteins into a three-dimensional multilayer system: Investigation of the surface of the human fungal pathogen Aspergillus fumigatus

inferred← citeshttps://doi.org/10.1016/j.bbapap.2014.06.006openalex-snapshot

SEVI, the semen enhancer of HIV infection along with fragments from its central region, form amyloid fibrils that are toxic to neuronal cells

inferred← citeshttps://doi.org/10.1016/j.bbapap.2016.10.008openalex-snapshot

Extensive deamidation of RNase A inhibits its oligomerization through 3D domain swapping

inferred← citeshttps://doi.org/10.1016/j.bbapap.2016.12.008openalex-snapshot

Analysis of sheep α-synuclein provides a molecular strategy for the reduction of fibrillation

inferred← citeshttps://doi.org/10.1016/j.bbapap.2018.10.008openalex-snapshot

Exploring the aggregation-prone regions from structural domains of human TDP-43

inferred← citeshttps://doi.org/10.1016/j.bbapap.2019.07.010openalex-snapshot

The molecular lifecycle of amyloid – Mechanism of assembly, mesoscopic organisation, polymorphism, suprastructures, and biological consequences

inferred← citeshttps://doi.org/10.1016/j.bbapap.2022.140854openalex-snapshot

Amyloid fibril formation by αS1- and β-casein implies that fibril formation is a general property of casein proteins

inferred← citeshttps://doi.org/10.1016/j.bbrc.2010.10.062openalex-snapshot

Conformational preferences of non-polar amino acid residues: An additional factor in amyloid formation

inferred← citeshttps://doi.org/10.1016/j.bbrc.2010.11.011openalex-snapshot

Human proteins that specifically bind to 8-oxoguanine-containing RNA and their responses to oxidative stress

inferred← citeshttps://doi.org/10.1016/j.bbrc.2016.12.011openalex-snapshot

Development of a novel catalytic amyloid displaying a metal-dependent ATPase-like activity

inferred← citeshttps://doi.org/10.1016/j.bbrep.2016.10.005openalex-snapshot

Monosialoganglioside-GM1 triggers binding of the amyloid-protein salmon calcitonin to a Langmuir membrane model mimicking the occurrence of lipid-rafts

inferred← citeshttps://doi.org/10.1016/j.biocel.2018.05.012openalex-snapshot

Identification and application of self-binding zipper-like sequences in SARS-CoV spike protein

inferred← citeshttps://doi.org/10.1016/j.biochi.2011.07.005openalex-snapshot

RNase A oligomerization through 3D domain swapping is favoured by a residue located far from the swapping domains

inferred← citeshttps://doi.org/10.1016/j.biochi.2022.02.007openalex-snapshot

Tyrosine 12 of human calcitonin modulates its amyloid formation, membrane binding, and bioactivity

inferred← citeshttps://doi.org/10.1016/j.biochi.2026.01.003openalex-snapshot

Phase separation in regulation of gene expression: current methodological and conceptual approaches

inferred← citeshttps://doi.org/10.1016/j.biomaterials.2015.03.002openalex-snapshot

Self healing hydrogels composed of amyloid nano fibrils for cell culture and stem cell differentiation

inferred← citeshttps://doi.org/10.1016/j.biosystems.2010.09.007openalex-snapshot

Structure and dynamics of the ‘protein folding code’ inferred using Tlusty's topological rate distortion approach

inferred← citeshttps://doi.org/10.1016/j.bpc.2011.08.004openalex-snapshot

Amyloid fibril formation by native and modified bovine β-lactoglobulins proceeds through unfolded form of proteins: A comparative study

inferred← citeshttps://doi.org/10.1016/j.bpc.2013.06.003openalex-snapshot

The amyloid-cell membrane system. The interplay between the biophysical features of oligomers/fibrils and cell membrane defines amyloid toxicity

inferred← citeshttps://doi.org/10.1016/j.bpc.2018.03.004openalex-snapshot

Amyloid fibrillation of an intrinsically disordered plant phloem protein At PP16-1 under acidic condition

inferred← citeshttps://doi.org/10.1016/j.bpc.2020.106507openalex-snapshot

Biophysical processes underlying cross-seeding in amyloid aggregation and implications in amyloid pathology

inferred← citeshttps://doi.org/10.1016/j.bpc.2020.106530openalex-snapshot

Native disulphide-linked dimers facilitate amyloid fibril formation by bovine milk αS2-casein

inferred← citeshttps://doi.org/10.1016/j.bpj.2011.02.060openalex-snapshot

Systematic Examination of Polymorphism in Amyloid Fibrils by Molecular-Dynamics Simulation

inferred← citeshttps://doi.org/10.1016/j.bpj.2013.04.056openalex-snapshot

Differences in β-strand Populations of Monomeric Aβ40 and Aβ42

inferred← citeshttps://doi.org/10.1016/j.bpj.2015.03.021openalex-snapshot

A Kinetic Study of Ovalbumin Fibril Formation: The Importance of Fragmentation and End-Joining

inferred← citeshttps://doi.org/10.1016/j.bpj.2015.03.034openalex-snapshot

Morphology-Dependent HIV-Enhancing Effect of Semen-Derived Enhancer of Viral Infection

inferred← citeshttps://doi.org/10.1016/j.bpj.2019.11.022openalex-snapshot

DNA Facilitates Oligomerization and Prevents Aggregation via DNA Networks

inferred← citeshttps://doi.org/10.1016/j.bpj.2020.05.033openalex-snapshot

The Effect of (−)-Epigallocatechin-3-Gallate on the Amyloid-β Secondary Structure

inferred← citeshttps://doi.org/10.1016/j.bpj.2021.01.032openalex-snapshot

A theoretical study of polymorphism in VQIVYK fibrils

inferred← citeshttps://doi.org/10.1016/j.brainres.2012.01.016openalex-snapshot

The tip of the iceberg: RNA-binding proteins with prion-like domains in neurodegenerative disease

inferred← citeshttps://doi.org/10.1016/j.ccell.2015.12.002openalex-snapshot

A Designed Inhibitor of p53 Aggregation Rescues p53 Tumor Suppression in Ovarian Carcinomas

inferred← citeshttps://doi.org/10.1016/j.cej.2023.146561openalex-snapshot

Fluoride adsorption studies on different amyloid fibrils hybrids: Spectroscopic analysis and molecular docking analysis

inferred← citeshttps://doi.org/10.1016/j.cej.2024.152819openalex-snapshot

Capturer of emerging contaminants: Potentials and perspectives of amyloid protein nanofibrils as the novel adsorbents

inferred← citeshttps://doi.org/10.1016/j.cej.2025.168606openalex-snapshot

Efficient biosynthesis of programable hydrophilic/phobic meta-spidroin dressing

inferred← citeshttps://doi.org/10.1016/j.cell.2010.11.050openalex-snapshot

Amyloid-like Aggregates Sequester Numerous Metastable Proteins with Essential Cellular Functions

inferred← citeshttps://doi.org/10.1016/j.cell.2021.08.013openalex-snapshot

The expanding amyloid family: Structure, stability, function, and pathogenesis

inferred← citeshttps://doi.org/10.1016/j.cell.2023.11.025openalex-snapshot

Structural evolution of fibril polymorphs during amyloid assembly

inferred← citeshttps://doi.org/10.1016/j.celrep.2012.09.036openalex-snapshot

Cellular Strategies for Regulating Functional and Nonfunctional Protein Aggregation

inferred← citeshttps://doi.org/10.1016/j.celrep.2013.09.043openalex-snapshot

Widespread Aggregation and Neurodegenerative Diseases Are Associated with Supersaturated Proteins

inferred← citeshttps://doi.org/10.1016/j.celrep.2018.07.040openalex-snapshot

Stress-Induced Low Complexity RNA Activates Physiological Amyloidogenesis

inferred← citeshttps://doi.org/10.1016/j.celrep.2019.12.080openalex-snapshot

hnRNPDL Phase Separation Is Regulated by Alternative Splicing and Disease-Causing Mutations Accelerate Its Aggregation

inferred← citeshttps://doi.org/10.1016/j.celrep.2020.01.098openalex-snapshot

Entropic Bristles Tune the Seeding Efficiency of Prion-Nucleating Fragments

inferred← citeshttps://doi.org/10.1016/j.chemolab.2015.04.009openalex-snapshot

A quantitative sequence–aggregation relationship predictor applied as identification of self-assembled hexapeptides

inferred← citeshttps://doi.org/10.1016/j.cis.2019.05.002openalex-snapshot

Food protein amyloid fibrils: Origin, structure, formation, characterization, applications and health implications

inferred← citeshttps://doi.org/10.1016/j.cis.2019.102086openalex-snapshot

Adsorption layer formation in dispersions of protein aggregates

inferred← citeshttps://doi.org/10.1016/j.colsurfb.2026.115474openalex-snapshot

CP-31398 restored the functional condensates of R175H p53 by stabilizing the zinc-binding domain and 251–258 segment

inferred← citeshttps://doi.org/10.1016/j.csbj.2021.07.019openalex-snapshot

Cryptic amyloidogenic regions in intrinsically disordered proteins: Function and disease association

inferred← citeshttps://doi.org/10.1016/j.csbj.2025.04.016openalex-snapshot

Three scenarios for amyloid transformation in the context of the funnel model

inferred← citeshttps://doi.org/10.1016/j.csbr.2025.100062openalex-snapshot

Multiple minima problem in protein folding solved appying multi criterial optimisation

inferred← citeshttps://doi.org/10.1016/j.devcel.2016.09.002openalex-snapshot

Adaptation to Stressors by Systemic Protein Amyloidogenesis

inferred← citeshttps://doi.org/10.1016/j.devcel.2024.04.018openalex-snapshot

An evolutionarily conserved mechanism controls reversible amyloids of pyruvate kinase via pH-sensing regions

inferred← citeshttps://doi.org/10.1016/j.eehl.2023.09.003openalex-snapshot

Well-designed protein amyloid nanofibrils composites as versatile and sustainable materials for aquatic environment remediation: A review

inferred← citeshttps://doi.org/10.1016/j.febslet.2010.06.019openalex-snapshot

The amyloid fibrils of the constant domain of immunoglobulin light chain

inferred← citeshttps://doi.org/10.1016/j.febslet.2012.03.019openalex-snapshot

Fibrillogenic propensity of the GroEL apical domain: A Janus‐faced minichaperone

inferred← citeshttps://doi.org/10.1016/j.febslet.2013.09.038openalex-snapshot

Structural and functional relationships of natural and artificial dimeric bovine ribonucleases: New scaffolds for potential antitumor drugs

inferred← citeshttps://doi.org/10.1016/j.febslet.2013.10.049openalex-snapshot

An N‐terminal pro‐atrial natriuretic peptide (NT‐proANP) ‘aggregation‐prone’ segment involved in isolated atrial amyloidosis

inferred← citeshttps://doi.org/10.1016/j.fochx.2026.103604openalex-snapshot

Influences of pH-regulated metal phenolic networks on soy protein hydrolysate nanofibril gels: Microstructure, rheological properties and thermal stability

inferred← citeshttps://doi.org/10.1016/j.foodchem.2023.138351openalex-snapshot

Specific ions effect on aggregation behaviors and structural changes of amyloid fibrils from rice glutelin

inferred← citeshttps://doi.org/10.1016/j.foodchem.2025.144557openalex-snapshot

Formation of tiger nut protein fibrils through self-assembly and different nuclei-induced pathways: Focus on structure and core peptide region

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