All

What are you looking for?

All
Projects
Results
Organizations

Quick search

  • Projects supported by TA ČR
  • Excellent projects
  • Projects with the highest public support
  • Current projects

Smart search

  • That is how I find a specific +word
  • That is how I leave the -word out of the results
  • “That is how I can find the whole phrase”

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

The result's identifiers

  • Result code in 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>

  • Alternative codes found

    RIV/00216208:11310/24:10494298

  • Result on the web

    <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>

Alternative languages

  • Result language

    angličtina

  • Original language name

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

  • Original language description

    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.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    10606 - Microbiology

Result continuities

  • Project

    Result was created during the realization of more than one project. More information in the Projects tab.

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2024

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Folia Biologica

  • ISSN

    0015-5500

  • e-ISSN

    0015-5500

  • Volume of the periodical

    70

  • Issue of the periodical within the volume

    3

  • Country of publishing house

    CZ - CZECH REPUBLIC

  • Number of pages

    14

  • Pages from-to

    152-165

  • UT code for WoS article

    001372840400002

  • EID of the result in the Scopus database

    2-s2.0-85212021960