ArticleAngewandte Chemie (International ed. in English)2016
Two-Dimensional Crowding Uncovers a Hidden Conformation of α-Synuclein.
Article in Angewandte Chemie (International ed. in English), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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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
15 citing papers in PubMed, 34 citations in OpenAlex.
- RNA chain length and stoichiometry govern surface tension and stability of protein-RNA condensates.iScience · 2022Article
- Crowding-induced morphological changes in synthetic lipid vesicles determined using smFRET.Frontiers in bioengineering and biotechnology · 2022Article
- The structural heterogeneity of α-synuclein is governed by several distinct subpopulations with interconversion times slower than milliseconds.Structure (London, England : 1993) · 2021Article
- Quantifying viscosity and surface tension of multicomponent protein-nucleic acid condensates.Biophysical journal · 2021Article
- Amyloid Oligomers: A Joint Experimental/Computational Perspective on Alzheimer's Disease, Parkinson's Disease, Type II Diabetes, and Amyotrophic Lateral Sclerosis.Chemical reviews · 2021Review
- Single Molecule Characterization of Amyloid Oligomers.Molecules (Basel, Switzerland) · 2021Review
- Sequence-encoded and composition-dependent protein-RNA interactions control multiphasic condensate morphologies.Nature communications · 2021Article
- Keeping α-Synuclein at Bay: A More Active Role of Molecular Chaperones in Preventing Mitochondrial Interactions and Transition to Pathological States?Life (Basel, Switzerland) · 2020Review
- Single-molecule fluorescence studies of intrinsically disordered proteins and liquid phase separation.Biochimica et biophysica acta. Proteins and proteomics · 2019Review
- Divalent cations can control a switch-like behavior in heterotypic and homotypic RNA coacervates.Scientific reports · 2019Article
- Molecular Crowding Tunes Material States of Ribonucleoprotein Condensates.Biomolecules · 2019Article
- Untangling the Conformational Polymorphism of Disordered Proteins Associated With Neurodegeneration at the Single-Molecule Level.Frontiers in molecular neuroscience · 2019Review
- Entropic Control of an Excited Folded-Like Conformation in a Disordered Protein Ensemble.Journal of molecular biology · 2018Article
- Organelle-specific single-molecule imaging of α4β2 nicotinic receptors reveals the effect of nicotine on receptor assembly and cell-surface trafficking.The Journal of biological chemistry · 2017Article
- Making microenvironments: A look into incorporating macromolecular crowding into in vitro experiments, to generate biomimetic microenvironments which are capable of directing cell function for tissue engineering applications.Journal of tissue engineeringArticle
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The intrinsically disordered protein (IDP), α-synuclein (αS), is well-known for phospholipid membrane binding-coupled folding into tunable helical conformers. Here, using single-molecule experiments in conjunction with ensemble assays and a theoretical model, we present a unique case demonstrating that the interaction-folding landscape of αS can be tuned by two-dimensional (2D) crowding through simultaneous binding of a second protein on the bilayer surface. Unexpectedly, the experimental data show a clear deviation from a simple competitive inhibition model, but are consistent with a bimodal inhibition mechanism wherein membrane binding of a second protein (a membrane interacting chaperone, Hsp27, in this case) differentially inhibits two distinct modules of αS-membrane interaction. As a consequence, αS molecules are forced to access a hidden conformational state on the phospholipid bilayer in which only the higher-affinity module remains membrane-bound. Our results demonstrate that macromolecular crowding in two dimensions can play a significant role in shaping the conformational landscape of membrane-binding IDPs with multiple binding modes.
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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.