ArticleACS nano2018
Profiling the Serum Protein Corona of Fibrillar Human Islet Amyloid Polypeptide.
Article in ACS nano, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
17 citing papers in PubMed.
- The protein corona at the nano-bio interface: the need for standardized methodology and opportunities for neurodegenerative disease intervention.RSC advances · 2026Review
- Emerging biophysical origins and pathogenic implications of amyloid oligomers.Nature communications · 2025Review
- Could artificial intelligence revolutionize the development of nanovectors for gene therapy and mRNA vaccines?Nano today · 2022Article
- Anisotropic CdSe Tetrapods in Vortex Flow for Removing Non-Specific Binding and Increasing Protein Capture.Sensors (Basel, Switzerland) · 2022Article
- Simulations of cross-amyloid aggregation of amyloid-β and islet amyloid polypeptide fragments.Biophysical journal · 2022Article
- Engineered nanoparticles enable deep proteomics studies at scale by leveraging tunable nano-bio interactions.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Extracellular protein components of amyloid plaques and their roles in Alzheimer's disease pathology.Molecular neurodegeneration · 2021Review
- The membrane axis of Alzheimer's nanomedicine.Advanced nanobiomed research · 2021Article
- Amyloidosis Inhibition, a New Frontier of the Protein Corona.Nano today · 2020Article
- Half a century of amyloids: past, present and future.Chemical Society reviews · 2020Review
- Cellular Interactions of Liposomes and PISA Nanoparticles during Human Blood Flow in a Microvascular Network.Small (Weinheim an der Bergstrasse, Germany) · 2020Article
- Dissecting the Structural Organization of Multiprotein Amyloid Aggregates Using a Bottom-Up Approach.ACS chemical neuroscience · 2020Article
- Machine learning predicts the functional composition of the protein corona and the cellular recognition of nanoparticles.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Mitigation of Amyloidosis with Nanomaterials.Advanced materials (Deerfield Beach, Fla.) · 2020Review
- Human Plasma Protein Corona of Aβ Amyloid and Its Impact on Islet Amyloid Polypeptide Cross-Seeding.Biomacromolecules · 2020Article
- Differential Roles of Plasma Protein Corona on Immune Cell Association and Cytokine Secretion of Oligomeric and Fibrillar Beta-Amyloid.Biomacromolecules · 2019Article
- Physical and Toxicological Profiles of Human IAPP Amyloids and Plaques.Science bulletin · 2019Article
Corrections and comments
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Authors and funding
11 authors.
Funding
Abstract
Amyloids may be regarded as native nanomaterials that form in the presence of complex protein mixtures. By drawing an analogy with the physicochemical properties of nanoparticles in biological fluids, we hypothesized that amyloids should form a protein corona in vivo that would imbue the underlying amyloid with a modified biological identity. To explore this hypothesis, we characterized the protein corona of human islet amyloid polypeptide (IAPP) fibrils in fetal bovine serum using two complementary methodologies developed herein: quartz crystal microbalance and "centrifugal capture", coupled with nanoliquid chromatography tandem mass spectroscopy. Clear evidence for a significant protein corona was obtained. No trends were identified for amyloid corona proteins based on their physicochemical properties, whereas strong binding with IAPP fibrils occurred for linear proteins or multidomain proteins with structural plasticity. Proteomic analysis identified amyloid-enriched proteins that are known to play significant roles in mediating cellular machinery and processing, potentially leading to pathological outcomes and therapeutic targets.
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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.