ArticleChemical science2016
Structure and assembly mechanisms of toxic human islet amyloid polypeptide oligomers associated with copper.
Article in Chemical science, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 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.
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Who cites it
9 citing papers in PubMed.
- Antiparallel β-Sheet as a Key Motif of Amyloid-β Inhibitor Designed via Topological Peptide Reprogramming.Angewandte Chemie (International ed. in English) · 2025Article
- Copper binding and protein aggregation: a journey from the brain to the human lens.RSC chemical biology · 2023Article
- Review
- Optimized experimental pre-treatment strategy for temporary inhibition of islet amyloid polypeptide aggregation.Biochemistry and biophysics reports · 2021Article
- Regulation of divalent metal ions to the aggregation and membrane damage of human islet amyloid polypeptide oligomers.RSC advances · 2021Article
- His18 promotes reactive oxidative stress production in copper-ion mediated human islet amyloid polypeptide aggregation.RSC advances · 2020Article
- Cu and Zn coordination to amyloid peptides: From fascinating chemistry to debated pathological relevance.Coordination chemistry reviews · 2018Article
- Regulation of the aggregation behavior of human islet amyloid polypeptide fragment by titanocene complexes.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2017Article
- Molecular interactions of amyloid nanofibrils with biological aggregation modifiers: implications for cytotoxicity mechanisms and biomaterial design.Interface focus · 2017Review
Corrections and comments
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Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Amyloidosis is a clinical disorder implicated with the formation of toxic amyloid aggregates. Despite their pathological significance, it is challenging to define the structural characteristics of amyloid oligomers owing to their metastable nature. Herein, we report structural and mechanistic investigations of human islet amyloid polypeptide (hIAPP) oligomers, found in type II diabetes mellitus, in both the absence and presence of disease-relevant metal ions [
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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.