The DOI matches its Crossref record; 133 of the 133 references it cites were found in a registry or an index.
Protein‐misfolding diseases and chaperone‐based therapeutic approaches
Abstract
A large number of neurodegenerative diseases in humans result from protein misfolding and aggregation. Protein misfolding is believed to be the primary cause of Alzheimer's disease, Parkinson's disease, Huntington's disease, Creutzfeldt–Jakob disease, cystic fibrosis, Gaucher's disease and many other degenerative and neurodegenerative disorders. Cellular molecular chaperones, which are ubiquitous, stress‐induced proteins, and newly found chemical and pharmacological chaperones have been found to be effective in preventing misfolding of different disease‐causing proteins, essentially reducing the severity of several neurodegenerative disorders and many other protein‐misfolding diseases. In this review, we discuss the probable mechanisms of several protein‐misfolding diseases in humans, as well as therapeutic approaches for countering them. The role of molecular, chemical and pharmacological chaperones in suppressing the effect of protein misfolding‐induced consequences in humans is explained in detail. Functional aspects of the different types of chaperones suggest their uses as potential therapeutic agents against different types of degenerative diseases, including neurodegenerative disorders.
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Protein structure generation via folding diffusion
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AI-Based Protein Structure Prediction in Drug Discovery: Impacts and Challenges
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Metadata
- Authors
- Chaudhuri, T. K., & Paul, S.
- Venue
- The FEBS Journal
- Publisher
- Wiley
- Published
- 2006-04
- Volume
- 273
- Issue
- 7
- Pages
- 1331-1349
- ISSN
- 1742-464X (ISSN-L)
- 1742-4658
- OpenAlex
- W2111256689
- Cited by
- 419
- References
- 133
- FWCI
- 8.96
- Type
- journal article
- Language
- en
- Open access
- closed
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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