ArticleNature chemical biology2010
A causative link between the structure of aberrant protein oligomers and their toxicity.
Article in Nature chemical biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 253 papers, 1 of them a synthesis that pooled it.
What it found
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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
253 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Pooled it
- Structure-Activity Relationship Study of Protoberberine Alkaloids Reveals Molecular Planarity as a Key Determinant of Membrane Interaction and Protection from Misfolded Protein Oligomers.Journal of medicinal chemistry · 2026Article
- Exposure to oligomeric and fibrillar species of amyloid-β induces toxicity and impairs extravillous trophoblast cell function in vitro.Placenta · 2026Article
- Thermodynamic Frontiers in Hemoglobin-Inspired Polymer Science for Diagnosis and Modulation of Neurodegenerative Diseases.Cell biochemistry and function · 2026Review
- Exploring and Targeting the Connection of Iron and Copper Homeostasis to Neurodegenerative Diseases.MedComm · 2026Review
- Transient Interactions of α-Synuclein N- and C-Termini.ACS chemical neuroscience · 2026Article
- Stress-induced alteration of small extracellular vesicles drives amyloid-beta sequestration and exacerbates Alzheimer's disease pathogenesis.Alzheimer's research & therapy · 2026Article
- Detection of protein oligomers with nanopores.Nature reviews. Chemistry · 2025Review
- Molecular Determinants of Protein Pathogenicity at the Single-Aggregate Level.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Detecting and Tracking β-Amyloid Oligomeric Forms and Dynamics In Vitro by a High-Sensitivity Fluorescent-Based Assay.ACS chemical neuroscience · 2024Article
- α-Synuclein oligomers form by secondary nucleation.Nature communications · 2024Article
- Preparation and Characterization of Zn(II)-Stabilized AβACS chemical neuroscience · 2024Article
- Energy Landscapes and Structural Ensembles of Glucagon-like Peptide-1 Monomers.The journal of physical chemistry. B · 2024Article
- Structure of cytotoxic amyloid oligomers generated during disaggregation.Journal of biochemistry · 2024Review
- A Relationship between the Structures and Neurotoxic Effects of Aβ Oligomers Stabilized by Different Metal Ions.ACS chemical neuroscience · 2024Article
- Misfolded protein oligomers: mechanisms of formation, cytotoxic effects, and pharmacological approaches against protein misfolding diseases.Molecular neurodegeneration · 2024Review
- A Cross-Sectional Study of Alzheimer-Related Proteins in Women with Polycystic Ovary Syndrome.International journal of molecular sciences · 2024Article
- Disturbance in the protein landscape of cochlear perilymph in an Alzheimer's disease mouse model.PloS one · 2024Article
- Intermolecular interactions underlie protein/peptide phase separation irrespective of sequence and structure at crowded milieu.Nature communications · 2023Article
- Amyloid Precursor Protein and Alzheimer's Disease.International journal of molecular sciences · 2023Review
193 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
11 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The aberrant assembly of peptides and proteins into fibrillar aggregates proceeds through oligomeric intermediates that are thought to be the primary pathogenic species in many protein deposition diseases. We describe two types of oligomers formed by the HypF-N protein that are morphologically and tinctorially similar, as detected with atomic force microscopy and thioflavin T assays, though one is benign when added to cell cultures whereas the other is toxic. Structural investigation at a residue-specific level using site-directed labeling with pyrene indicated differences in the packing of the hydrophobic interactions between adjacent protein molecules in the oligomers. The lower degree of hydrophobic packing was found to correlate with a higher ability to penetrate the cell membrane and cause an influx of Ca(2+) ions. Our findings suggest that structural flexibility and hydrophobic exposure are primary determinants of the ability of oligomeric assemblies to cause cellular dysfunction and its consequences, such as neurodegeneration.
Indexed as
Identifiers
20081829What OpenQuestion holds
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.