Heat Shock Protein Network: the Mode of Action, the Role in Protein Folding and Human Pathologies

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F24%3A00603830" target="_blank" >RIV/61388971:_____/24:00603830 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/00216208:11310/24:10494298

Výsledek na webu

<a href="https://foliabiologica.lf1.cuni.cz/70/3/0152/" target="_blank" >https://foliabiologica.lf1.cuni.cz/70/3/0152/</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.14712/fb2024070030152" target="_blank" >10.14712/fb2024070030152</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Heat Shock Protein Network: the Mode of Action, the Role in Protein Folding and Human Pathologies

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

Heat Shock Protein Network: the Mode of Action, the Role in Protein Folding and Human Pathologies

Popis výsledku anglicky

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.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10606 - Microbiology

Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2024

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Folia Biologica

ISSN

0015-5500

e-ISSN

0015-5500

Svazek periodika

70

Číslo periodika v rámci svazku

3

Stát vydavatele periodika

CZ - Česká republika

Počet stran výsledku

14

Strana od-do

152-165

Kód UT WoS článku

001372840400002

EID výsledku v databázi Scopus

2-s2.0-85212021960