ReviewCellular and molecular life sciences : CMLS2017
Expanding role of molecular chaperones in regulating α-synuclein misfolding; implications in Parkinson's disease.
Review in Cellular and molecular life sciences : CMLS, 2017. 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, 30 citations in OpenAlex.
- Aqueous Extract ofInternational journal of molecular sciences · 2025Article
- Alpha-Synuclein Pathophysiology in Neurodegenerative Disorders: A Review Focusing on Molecular Mechanisms and Treatment Advances in Parkinson's Disease.Cellular and molecular neurobiology · 2025Review
- Immunohistochemical Demonstration of the pGlu79 α-Synuclein Fragment in Alzheimer's Disease and Its Tg2576 Mouse Model.Biomolecules · 2022Article
- Could Small Heat Shock Protein HSP27 Be a First-Line Target for Preventing Protein Aggregation in Parkinson's Disease?International journal of molecular sciences · 2021Review
- Flavonoids: Potential Candidates for the Treatment of Neurodegenerative Disorders.Biomedicines · 2021Review
- General Structural and Functional Features of Molecular Chaperones.Advances in experimental medicine and biology · 2021Article
- Fast kinetics of environmentally induced α-synuclein aggregation mediated by structural alteration in NAC region and result in structure dependent cytotoxicity.Scientific reports · 2020Article
- The Down-Regulation of Clusterin Expression Enhances the αSynuclein Aggregation Process.International journal of molecular sciences · 2020Article
- Chaperones and Proteostasis: Role in Parkinson's Disease.Diseases (Basel, Switzerland) · 2020Review
- Iron Redox Chemistry and Implications in the Parkinson's Disease Brain.Oxidative medicine and cellular longevity · 2019Review
- Conformational flexibility within the nascent polypeptide-associated complex enables its interactions with structurally diverse client proteins.The Journal of biological chemistry · 2018Article
- Folding while bound to chaperones.Current opinion in structural biology · 2018Review
- Insights Into ProteinFrontiers in molecular neuroscience · 2018Review
- The Neuroprotective Role of Protein Quality Control in Halting the Development of Alpha-Synuclein Pathology.Frontiers in molecular neuroscience · 2017Review
- Cellular Regulation of Amyloid Formation in Aging and Disease.Frontiers in neuroscience · 2017Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein misfolding under stressful environmental conditions cause several cellular problems owing to the disturbed cellular protein homeostasis, which may further lead to neurological disorders like Parkinson's disease (PD), Alzheimer's disease (AD), Amyloid lateral sclerosis and Huntington disease (HD). The presence of cellular defense mechanisms like molecular chaperones and proteasomal degradation systems prevent protein misfolding and aggregation. Molecular chaperones plays primary role in preventing protein misfolding by mediating proper native folding, unfolding and refolding of the polypeptides along with vast number of cellular functions. In past few years, the understanding of molecular chaperone mechanisms has been expanded enormously although implementation to prevent protein aggregation diseases is still deficient. We in this review evaluated major classes of molecular chaperones and their mechanisms relevant for preventing protein aggregation, specific case of α-synuclein aggregation. We also evaluate the molecular chaperone function as a novel therapeutic approach and the chaperone inhibitors or activators as small molecular drug targets.
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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.