Heat Shock Protein Network: the Mode of Action, the Role in Protein Folding and Human Pathologies
Jazyk angličtina Země Česko Médium print
Typ dokumentu časopisecké články, přehledy
Grantová podpora
22-27695S
Grantová Agentura České Republiky
RVO: 61388971
Akademie Věd České Republiky
PubMed
39644110
DOI
10.14712/fb2024070030152
PII: fb_2024070030152
Knihovny.cz E-zdroje
- Klíčová slova
- HSP, aggregation, cancer, chaperone, neurodegenerative disease, protein folding,
- MeSH
- lidé MeSH
- neurodegenerativní nemoci metabolismus genetika MeSH
- proteiny teplotního šoku * metabolismus genetika MeSH
- sbalování proteinů * MeSH
- zvířata MeSH
- Check Tag
- lidé MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- přehledy MeSH
- Názvy látek
- proteiny teplotního šoku * MeSH
Protein folding is an extremely complicated process, which has been extensively tackled during the last decades. In vivo, a certain molecular machinery is responsible for assisting the correct folding of proteins and maintaining protein homeostasis: the members of this machinery are the heat shock proteins (HSPs), which belong among molecular chaperones. Mutations in HSPs are associated with several inherited diseases, and members of this group were also proved to be involved in neurodegenerative pathologies (e.g., Alzheimer and Parkinson diseases), cancer, viral infections, and antibiotic resistance of bacteria. Therefore, it is critical to understand the principles of HSP functioning and their exact role in human physiology and pathology. This review attempts to briefly describe the main chaperone families and the interplay between individual chaperones, as well as their general and specific functions in the context of cell physiology and human diseases.
BIOCEV Faculty of Science Charles University Prague Czech Republic
BIOCEV Institute of Microbiology Czech Academy of Sciences Prague Czech Republic
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