ArticleInternational journal of Alzheimer's disease2010
Spectroscopic Characterization of Intermolecular Interaction of Amyloid β Promoted on GM1 Micelles.
Article in International journal of Alzheimer's disease, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 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
27 citing papers in PubMed.
- Single-Molecule Kinetic Observation of Antibody Interactions with Growing Amyloid β Fibrils.Journal of the American Chemical Society · 2024Article
- The Double-Layered Structure of Amyloid-β Assemblage on GM1-Containing Membranes Catalytically Promotes Fibrillization.ACS chemical neuroscience · 2023Article
- Molecular mechanisms of amyloid-β peptide fibril and oligomer formation: NMR-based challenges.Biophysics and physicobiology · 2023Article
- Conformational Variability of Amyloid-β and the Morphological Diversity of Its Aggregates.Molecules (Basel, Switzerland) · 2022Review
- Monosialotetrahexosylganglioside Promotes Early Aβ42 Oligomer Formation and Maintenance.ACS chemical neuroscience · 2022Article
- Molecular Dynamics Simulation Studies on the Aggregation of Amyloid-β Peptides and Their Disaggregation by Ultrasonic Wave and Infrared Laser Irradiation.Molecules (Basel, Switzerland) · 2022Review
- Experimental and computational characterization of dynamic biomolecular interaction systems involving glycolipid glycans.Glycoconjugate journal · 2022Review
- Molecular dynamics simulations of amyloid-β peptides in heterogeneous environments.Biophysics and physicobiology · 2022Article
- Combined Effect of Anti-SSEA4 and Anti-Globo H Antibodies on Breast Cancer Cells.ACS chemical biology · 2021Article
- Cold Atmospheric Plasma Modification of Amyloid β.International journal of molecular sciences · 2021Article
- Improved secretion of glycoproteins using an N-glycan-restricted passport sequence tag recognized by cargo receptor.Nature communications · 2020Article
- β-Amyloid aggregation and heterogeneous nucleation.Protein science : a publication of the Protein Society · 2019Review
- Conformational Change of Amyloid-β 40 in Association with Binding to GM1-Glycan Cluster.Scientific reports · 2019Article
- Synchrotron-radiation vacuum-ultraviolet circular dichroism spectroscopy in structural biology: an overview.Biophysics and physicobiology · 2019Review
- Localization and dynamics of the anticarcinogenic curcumin with GMGlycoconjugate journal · 2017Article
- Protein folding, misfolding and aggregation: The importance of two-electron stabilizing interactions.PloS one · 2017Article
- Article
- NMR characterization of HIV-1 reverse transcriptase binding to various non-nucleoside reverse transcriptase inhibitors with different activities.Scientific reports · 2015Article
- GM1 ganglioside and Alzheimer's disease.Glycoconjugate journal · 2015Review
- Structural and dynamic views of GM1 ganglioside.Glycoconjugate journal · 2015Review
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Clusters of GM1 gangliosides act as platforms for conformational transition of monomeric, unstructured amyloid β (Aβ) to its toxic β-structured aggregates. We have previously shown that Aβ(1-40) accommodated on the hydrophobic/hydrophilic interface of lyso-GM1 or GM1 micelles assumes α-helical structures under ganglioside-excess conditions. For better understanding of the mechanisms underlying the α-to-β conformational transition of Aβ on GM1 clusters, we performed spectroscopic characterization of Aβ(1-40) titrated with GM1. It was revealed that the thioflavin T- (ThT-) reactive β-structure is more populated in Aβ(1-40) under conditions where the Aβ(1-40) density on GM1 micelles is high. Under this circumstance, the C-terminal hydrophobic anchor Val(39)-Val(40) shows two distinct conformational states that are reactive with ThT, while such Aβ species were not generated by smaller lyso-GM1 micelles. These findings suggest that GM1 clusters promote specific Aβ-Aβ interactions through their C-termini coupled with formation of the ThT-reactive β-structure depending on sizes and curvatures of the clusters.
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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.