ReviewNeurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics2013
Opportunities and challenges for molecular chaperone modulation to treat protein-conformational brain diseases.
Review in Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 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
9 citing papers in PubMed, 15 citations in OpenAlex.
- Distinct single-nucleus RNA-seq changes among non-neuronal cells in ADNC, LATE-NC, and mixed pathologies.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2026Article
- The role of heat shock proteins in preventing amyloid toxicity.Frontiers in molecular biosciences · 2022Review
- Cryo-EM structure of human mitochondrial HSPD1.iScience · 2021Article
- Proteomic analysis identifies plasma correlates of remote ischemic conditioning in the context of experimental traumatic brain injury.Scientific reports · 2020Article
- Current and future treatment of amyloid diseases.Journal of internal medicine · 2016Review
- Specific chaperones and regulatory domains in control of amyloid formation.The Journal of biological chemistry · 2015Review
- Structural Mechanisms of Mutant Huntingtin Aggregation Suppression by the Synthetic Chaperonin-like CCT5 Complex Explained by Cryoelectron Tomography.The Journal of biological chemistry · 2015Article
- Redox proteomics analysis to decipher the neurobiology of Alzheimer-like neurodegeneration: overlaps in Down's syndrome and Alzheimer's disease brain.The Biochemical journal · 2014Review
- Barcoding heat shock proteins to human diseases: looking beyond the heat shock response.Disease models & mechanisms · 2014Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A common pathological hallmark of protein-conformational brain diseases is the formation of disease-specific protein aggregates. In Alzheimer's disease, these are comprised of amyloid-β and Tau as opposed to α-synuclein in Parkinson's disease and N-terminal fragments of mutant huntingtin in Huntington's disease. Most aggregates also sequester molecular chaperones, a protein family that assists in the folding, refolding, stabilization, and processing of client proteins, including misfolded proteins in brain diseases. Molecular chaperone modulation has achieved remarkable therapeutic effects in some cellular and preclinical animal models of protein-conformational diseases. This has raised hope for chaperone-based strategies to combat these diseases. Here, we review briefly the functional diversity and medical significance of molecular chaperones, their therapeutic potential, and common and specific challenges towards clinical application.
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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.