ArticleProceedings of the National Academy of Sciences of the United States of America2011
Islet amyloid polypeptide demonstrates a persistent capacity to disrupt membrane integrity.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.
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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
67 citing papers in PubMed, 136 citations in OpenAlex.
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- A human antibody against pathologic IAPP aggregates protects beta cells in type 2 diabetes models.Nature communications · 2023Article
- Fibril elongation by human islet amyloid polypeptide is the main event linking aggregation to membrane damage.BBA advances · 2023Article
- pH- and concentration-dependent supramolecular assembly of a fungal defensin plectasin variant into helical non-amyloid fibrils.Nature communications · 2022Article
- Mechanistic Kinetic Model Reveals How Amyloidogenic Hydrophobic Patches Facilitate the Amyloid-β Fibril Elongation.ACS chemical neuroscience · 2022Article
- Direct Observation of β-Barrel Intermediates in the Self-Assembly of Toxic SOD1Journal of chemical information and modeling · 2021Article
- Effect of the air-water interface on the conformation of amyloid beta.Biointerphases · 2020Article
- Rapid Formation of Peptide/Lipid Coaggregates by the Amyloidogenic Seminal Peptide PAPBiophysical journal · 2020Article
- Medin Oligomer Membrane Pore Formation: A Potential Mechanism of Vascular Dysfunction.Biophysical journal · 2020Article
- Article
- γ-AApeptides-based Small Molecule Ligands That Disaggregate Human Islet Amyloid Polypeptide.Scientific reports · 2020Article
- Functional Reciprocity of Amyloids and Antimicrobial Peptides: Rethinking the Role of Supramolecular Assembly in Host Defense, Immune Activation, and Inflammation.Frontiers in immunology · 2020Review
- Revealing a Dual Role of Ganglioside Lipids in the Aggregation of Membrane-Associated Islet Amyloid Polypeptide.The Journal of membrane biology · 2019Article
- Impact of semen-derived amyloid (SEVI) on sperm viability and motility: its implication in male reproductive fitness.European biophysics journal : EBJ · 2019Article
- β-Amyloid aggregation and heterogeneous nucleation.Protein science : a publication of the Protein Society · 2019Review
- Conformational switching within dynamic oligomers underpins toxic gain-of-function by diabetes-associated amyloid.Nature communications · 2018Article
- Sterol Structure Strongly Modulates Membrane-Islet Amyloid Polypeptide Interactions.Biochemistry · 2018Article
- Dynamic membrane interactions of antibacterial and antifungal biomolecules, and amyloid peptides, revealed by solid-state NMR spectroscopy.Biochimica et biophysica acta. General subjects · 2018Review
- Spontaneous Lipid Nanodisc Fomation by Amphiphilic Polymethacrylate Copolymers.Journal of the American Chemical Society · 2017Article
- Implications of peptide assemblies in amyloid diseases.Chemical Society reviews · 2017Review
7 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Amyloid fiber formation is correlated with pathology in many diseases, including Alzheimer's, Parkinson's, and type II diabetes. Although β-sheet-rich fibrillar protein deposits define this class of disorder, increasing evidence points toward small oligomeric species as being responsible for cell dysfunction and death. The molecular mechanism by which this occurs is unknown, but likely involves the interaction of these species with biological membranes, with a subsequent loss of integrity. Here, we investigate islet amyloid polypeptide, which is implicated in the loss of insulin-secreting cells in type II diabetics. We report the discovery of oligomeric species that arise through stochastic nucleation on membranes and result in disruption of the lipid bilayer. These species are stable, result in all-or-none leakage, and represent a definable protein/lipid phase that equilibrates over time. We characterize the reaction pathway of assembly through the use of an experimental design that includes both ensemble and single-particle evaluations. Complexity in the reaction pathway could not be satisfied using a two-state description of membrane-bound monomer and oligomeric species. We therefore put forward a three-state kinetic framework, one of which we conjecture represents a non-amyloid, non-β-sheet intermediate previously shown to be a candidate therapeutic target.
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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.