ArticleScientific reports2013
α-helical structures drive early stages of self-assembly of amyloidogenic amyloid polypeptide aggregate formation in membranes.
Article in Scientific reports, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
36 citing papers in PubMed, 104 citations in OpenAlex.
- Modulation of Biological Membranes Using Small-Molecule Compounds to Counter Toxicity Caused by Amyloidogenic Proteins.Membranes · 2024Review
- MAPT mutations associated with familial tauopathies lead to formation of conformationally distinct oligomers that have cross-seeding ability.Protein science : a publication of the Protein Society · 2024Article
- Inhibition of the Early-Stage Cross-Amyloid Aggregation of Amyloid-β and IAPP via EGCG: Insights from Molecular Dynamics Simulations.ACS omega · 2024Article
- Growth kinetics of amyloid-like fibrils: An integrated atomistic simulation and continuum theory approach.PNAS nexus · 2024Article
- Big versus small: The impact of aggregate size in disease.Protein science : a publication of the Protein Society · 2023Review
- Influence of force field choice on the conformational landscape of rat and human islet amyloid polypeptide.Proteins · 2023Article
- Metastable intermediate during hIAPP aggregation catalyzed by membranes as detected with 2D IR spectroscopy.RSC chemical biology · 2022Article
- Monosialotetrahexosylganglioside Promotes Early Aβ42 Oligomer Formation and Maintenance.ACS chemical neuroscience · 2022Article
- Insights into Membrane Curvature Sensing and Membrane Remodeling by Intrinsically Disordered Proteins and Protein Regions.The Journal of membrane biology · 2022Review
- Dual Effects of Presynaptic Membrane Mimetics onFrontiers in cell and developmental biology · 2022Article
- Beta-amyloid pore linked to controlled calcium influx into the cell: A new paradigm for Alzheimer's Disease.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2022Article
- Proteostasis of Islet Amyloid Polypeptide: A Molecular Perspective of Risk Factors and Protective Strategies for Type II Diabetes.Chemical reviews · 2021Review
- Membrane Interactions and Toxicity by Misfolded Protein Oligomers.Frontiers in cell and developmental biology · 2021Review
- Lipid-Chaperone Hypothesis: A Common Molecular Mechanism of Membrane Disruption by Intrinsically Disordered Proteins.ACS chemical neuroscience · 2020Article
- Amyloidogenic Intrinsically Disordered Proteins: New Insights into Their Self-Assembly and Their Interaction with Membranes.Life (Basel, Switzerland) · 2020Review
- Helix Dipole and Membrane Electrostatics Delineate Conformational Transitions in the Self-Assembly of Amyloidogenic Peptides.Langmuir : the ACS journal of surfaces and colloids · 2020Article
- The Amphipathic GM1 Molecule Stabilizes Amyloid Aggregates, Preventing their Cytotoxicity.Biophysical journal · 2020Article
- Article
- The Ionophoric Activity of a Pro-Apoptotic VEGF165 Fragment on HUVEC Cells.International journal of molecular sciences · 2020Article
- Review
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The human islet amyloid polypeptide (hIAPP) is the primary component in the toxic islet amyloid deposits in type-2 diabetes. hIAPP self-assembles to aggregates that permeabilize membranes and constitutes amyloid plaques. Uncovering the mechanisms of amyloid self-assembly is the key to understanding amyloid toxicity and treatment. Although structurally similar, hIAPP's rat counterpart, the rat islet amyloid polypeptide (rIAPP), is non-toxic. It has been a puzzle why these peptides behave so differently. We combined multiscale modelling and theory to explain the drastically different dynamics of hIAPP and rIAPP: The differences stem from electrostatic dipolar interactions. hIAPP forms pentameric aggregates with the hydrophobic residues facing the membrane core and stabilizing water-conducting pores. We give predictions for pore sizes, the number of hIAPP peptides, and aggregate morphology. We show the importance of curvature-induced stress at the early stages of hIAPP assembly and the α-helical structures over β-sheets. This agrees with recent fluorescence spectroscopy experiments.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.