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”

Changing faces of stress: Impact of heat and arsenite treatment on the composition of stress granules

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F20%3A10414167" target="_blank" >RIV/00216208:11310/20:10414167 - isvavai.cz</a>

  • Result on the web

    <a href="https://verso.is.cuni.cz/pub/verso.fpl?fname=obd_publikace_handle&handle=nusWpzV-fL" target="_blank" >https://verso.is.cuni.cz/pub/verso.fpl?fname=obd_publikace_handle&handle=nusWpzV-fL</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1002/wrna.1596" target="_blank" >10.1002/wrna.1596</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Changing faces of stress: Impact of heat and arsenite treatment on the composition of stress granules

  • Original language description

    Stress granules (SGs), hallmarks of the cellular adaptation to stress, promote survival, conserve cellular energy, and are fully dissolved upon the cessation of stress treatment. Different stresses can initiate the assembly of SGs, but arsenite and heat are the best studied of these stresses. The composition of SGs and posttranslational modifications of SG proteins differ depending on the type and severity of the stress insult, methodology used, cell line, and presence of overexpressed and tagged proteins. A group of 18 proteins showing differential localization to SGs in heat- and arsenite-stressed mammalian cell lines is described. Upon severe and prolonged stress, physiological SGs transform into more solid protein aggregates that are no longer reversible and do not contain mRNA. Similar pathological inclusions are hallmarks of neurodegenerative diseases. SGs induced by heat stress are less dynamic than SGs induced by arsenite and contain a set of unique proteins and linkage-specific polyubiquitinated proteins. The same types of ubiquitin linkages have been found to contribute to the development of neurodegenerative disorders such as Parkinson disease, Alzheimer disease, and amyotrophic lateral sclerosis (ALS). We propose heat stress-induced SGs as a possible model of an intermediate stage along the transition from dynamic, fully reversible arsenite stress-induced SGs toward aberrant SGs, the hallmark of neurodegenerative diseases. Stress- and methodology-specific differences in the compositions of SGs and the transition of SGs to aberrant protein aggregates are discussed. This article is categorized under: RNA in Disease and Development &gt; RNA in Disease RNA Interactions with Proteins and Other Molecules &gt; RNA-Protein Complexes RNA Export and Localization &gt; RNA Localization

  • 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

    10600 - Biological sciences

Result continuities

  • Project

    <a href="/en/project/GA19-13491S" target="_blank" >GA19-13491S: In vitro oocyte culture vs in vivo oocyte development - is their physiology really comparable?</a><br>

  • Continuities

    P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Others

  • Publication year

    2020

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Wiley interdisciplinary reviews. RNA

  • ISSN

    1757-7004

  • e-ISSN

  • Volume of the periodical

    11

  • Issue of the periodical within the volume

    6

  • Country of publishing house

    GB - UNITED KINGDOM

  • Number of pages

    26

  • Pages from-to

    e1596

  • UT code for WoS article

    000529788200001

  • EID of the result in the Scopus database

    2-s2.0-85083838270