ArticleBiophysical journal2011
Distinct hydration properties of wild-type and familial point mutant A53T of α-synuclein associated with Parkinson's disease.
Article in Biophysical journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 38 citations in OpenAlex.
- Water Accelerates in the Hydration Shell of the N- and C-Terminal Domains of α-Synuclein in the Presence of NaCl.The journal of physical chemistry. B · 2026Article
- Direct current stimulation induced reduction in α-synuclein in primary neurons: targeting Parkinson's disease.Brain communications · 2026Article
- General Characterization of Properties of Ordered and Disordered Proteins by Wide-LineACS omega · 2024Article
- Morphometric and Nanomechanical Screening of Peripheral Blood Cells with Atomic Force Microscopy for Label-Free Assessment of Alzheimer's Disease, Parkinson's Disease, and Amyotrophic Lateral Sclerosis.International journal of molecular sciences · 2023Review
- Thermodynamic Signatures of Blood Plasma Proteome in Neurodegenerative Pathologies.International journal of molecular sciences · 2023Article
- Threonine Cavities Are Targetable Motifs That Control Alpha-Synuclein Fibril Growth.ACS chemical neuroscience · 2022Article
- Using Molecular Simulation to Guide Protein Engineering for Biocatalysis in Organic Solvents.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Exploration of Protein Aggregations in Parkinson's Disease Through Computational Approaches and Big Data Analytics.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Article
- Secondary Structures of Proteins: A Comparison of Models and Experimental Results.Journal of proteome research · 2021Article
- WT and A53T α-Synuclein Systems: Melting Diagram and Its New Interpretation.International journal of molecular sciences · 2020Article
- The Melting Diagram of Protein Solutions and Its Thermodynamic Interpretation.International journal of molecular sciences · 2018Article
- Insights into the Molecular Mechanisms of Alzheimer's and Parkinson's Diseases with Molecular Simulations: Understanding the Roles of Artificial and Pathological Missense Mutations in Intrinsically Disordered Proteins Related to Pathology.International journal of molecular sciences · 2018Review
- Wide-line NMR and DSC studies on intrinsically disordered p53 transactivation domain and its helically pre-structured segment.BMB reports · 2016Article
- The hydrophobic temperature dependence of amino acids directly calculated from protein structures.PLoS computational biology · 2015Article
- Fairy "tails": flexibility and function of intrinsically disordered extensions in the photosynthetic world.Frontiers in molecular biosciences · 2015Review
- Comparison of structure determination methods for intrinsically disordered amyloid-β peptides.The journal of physical chemistry. B · 2014Article
- Computational approaches to understanding protein aggregation in neurodegeneration.Journal of molecular cell biology · 2014Review
- Article
- Structures and free energy landscapes of the A53T mutant-type α-synuclein protein and impact of A53T mutation on the structures of the wild-type α-synuclein protein with dynamics.ACS chemical neuroscience · 2013Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The propensity of α-synuclein to form amyloid plays an important role in Parkinson's disease. Three familial mutations, A30P, E46K, and A53T, correlate with Parkinson's disease. Therefore, unraveling the structural effects of these mutations has basic implications in understanding the molecular basis of the disease. Here, we address this issue through comparing details of the hydration of wild-type α-synuclein and its A53T mutant by a combination of wide-line NMR, differential scanning calorimetry, and molecular dynamics simulations. All three approaches suggest a hydrate shell compatible with a largely disordered state of both proteins. Its fine details, however, are different, with the mutant displaying a somewhat higher level of hydration, suggesting a bias to more open structures, favorable for protein-protein interactions leading to amyloid formation. These differences disappear in the amyloid state, suggesting basically the same surface topology, irrespective of the initial monomeric state.
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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.