ArticlePerspectives in medicinal chemistry2007
Chemical chaperone and inhibitor discovery: potential treatments for protein conformational diseases.
Article in Perspectives in medicinal chemistry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 26 citations in OpenAlex.
- A Review of Targeted Therapies for Monogenic Epilepsy Syndromes.Frontiers in neurology · 2022Review
- Cell-penetrating Chaperone Peptide Prevents Protein Aggregation And Protects Against Cell Apoptosis.Advanced biosystems · 2018Article
- 4-phenylbutyrate Mitigates Fluoride-Induced Cytotoxicity in ALC Cells.Frontiers in physiology · 2017Article
- Chaperone-Based Therapies for Disease Modification in Parkinson's Disease.Parkinson's disease · 2017Review
- Effect of osmolytes on the conformation and aggregation of some amyloid peptides: CD spectroscopic data.Data in brief · 2016Article
- Trimethylamine-N-oxide switches from stabilizing nature: A mechanistic outlook through experimental techniques and molecular dynamics simulation.Scientific reports · 2016Article
- Marine fish may be biochemically constrained from inhabiting the deepest ocean depths.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Target- and mechanism-based therapeutics for neurodegenerative diseases: strength in numbers.Journal of medicinal chemistry · 2013Review
- In vivo detection and quantification of chemicals that enhance protein stability.Analytical biochemistry · 2013Article
- 4-phenylbutyric Acid Regulates Collagen Synthesis and Secretion Induced by High Concentrations of Glucose in Human Gingival Fibroblasts.The Korean journal of physiology & pharmacology : official journal of the Korean Physiological Society and the Korean Society of Pharmacology · 2011Article
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein misfolding and aggregation cause a large number of neurodegenerative diseases in humans due to (i) gain of function as observed in Alzheimer's disease, Huntington's disease, Parkinson's disease, and Prion's disease or (ii) loss of function as observed in cystic fibrosis and alpha1-antitrypsin deficiency. These misfolded proteins could either lead to the formation of harmful amyloids that become toxic for the cells or to be recognized and prematurely degraded by the protein quality control system. An increasing number of studies has indicated that some low-molecular-weight compounds named as chemical chaperones can reverse the mislocalization and/or aggregation of proteins associated with human conformational diseases. These small molecules are thought to non-selectively stabilize proteins and facilitate their folding. In this review, we summarize the probable mechanisms of protein conformational diseases in humans and the use of chemical chaperones and inhibitors as potential therapeutic agents against these diseases. Furthermore, recent advanced experimental and theoretical approaches underlying the detailed mechanisms of protein conformational changes and current structure-based drug designs towards protein conformational diseases are also discussed. It is believed that a better understanding of the mechanisms of conformational changes as well as the biological functions of these proteins will lead to the development and design of potential interfering compounds against amyloid formation associated with protein conformational diseases.
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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.