ArticleRSC chemical biology2021
Membrane composition and lipid to protein ratio modulate amyloid kinetics of yeast prion protein.
Article in RSC chemical biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 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.
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Who cites it
7 citing papers in PubMed, 16 citations in OpenAlex.
- Response mechanism of Saccharomyces cerevisiae under benzoic acid stress in ethanol fermentation.Scientific reports · 2024Article
- Zinc and pH modulate the ability of insulin to inhibit aggregation of islet amyloid polypeptide.Communications biology · 2024Article
- The Amyloid Assembly of the Bacterial Hfq Is Lipid-Driven and Lipid-Specific.International journal of molecular sciences · 2024Article
- Lipid oxidation controls peptide self-assembly near membranes through a surface attraction mechanism.Chemical science · 2023Article
- Cholesterol and its reciprocal association with prion infection.Cell and tissue research · 2023Review
- Human J-Domain Protein DnaJB6 Protects Yeast from [Biology · 2022Article
- Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Understanding of prion aggregation in a membrane environment may help to ameliorate neurodegenerative complications caused by the amyloid forms of prions. Here, we investigated the membrane binding-induced aggregation of yeast prion protein Sup35. Using the combination of fluorescence correlation spectroscopy (FCS) at single molecule resolution and other biophysical studies, we establish that lipid composition and lipid/protein ratio are key modulators of the aggregation kinetics of Sup35. In the presence of a zwitterionic membrane (DMPC), Sup35 exhibited novel biphasic aggregation kinetics at lipid/protein ratios ranging between 20 : 1 and 70 : 1 (termed here as the optimum lipid concentration, OLC). In ratios below (low lipid concentration, LLC) and above (ELC, excess lipid concentration) that range, the aggregation was found to be monophasic. In contrast, in the presence of negatively charged membranes, we did not observe any bi-phasic aggregation kinetics in the entire range of protein to lipid ratios. Our results provide a mechanistic description of the role that membrane concentration/composition-modulated aggregation may play in neurodegenerative diseases.
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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.