ArticleFEBS letters2015
High pressure promotes alpha-synuclein aggregation in cultured neuronal cells.
Article in FEBS letters, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 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
4 citing papers in PubMed.
- Regulation of bifunctional proteins in cells: Lessons from the phospholipase Cβ/G protein pathway.Protein science : a publication of the Protein Society · 2020Review
- The role of phospholipase Cβ on the plasma membrane and in the cytosol: How modular domains enable novel functions.Advances in biological regulation · 2019Article
- Nitrosative stress uncovers potent βAmerican journal of physiology. Heart and circulatory physiology · 2018Article
- Structural basis for the dissociation of α-synuclein fibrils triggered by pressure perturbation of the hydrophobic core.Scientific reports · 2016Article
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Authors and funding
2 authors.
Funding
Abstract
α-Synuclein is found in plaques associated with Parkinson's and other neurodegenerative diseases. Changes in α-synuclein oligomerization are thought to give rise to nucleation of neurodegenerative plaques. Here, we investigated the effect of hydrostatic pressure on the aggregation of α-synuclein in cultured neuronal cells. We found that hydrostatic pressure is associated with a transition from monomeric to higher order α-synuclein aggregates. We then tested whether this aggregation is associated with the loss of binding partners, such as phospholipase Cβ. We found that increased pressure reduces the level of PLCβ1 and the amount of α-synuclein/PLCβ1 complexes. These studies suggest that pressure promotes release of α-synuclein from protein partners promoting its oligomerization.
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