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”

TRPM7 N-terminal region forms complexes with calcium binding proteins CaM and S100A1

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F21%3A00549345" target="_blank" >RIV/61388963:_____/21:00549345 - isvavai.cz</a>

  • Alternative codes found

    RIV/00216208:11320/21:10434931 RIV/00216208:11130/21:10434931

  • Result on the web

    <a href="https://doi.org/10.1016/j.heliyon.2021.e08490" target="_blank" >https://doi.org/10.1016/j.heliyon.2021.e08490</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1016/j.heliyon.2021.e08490" target="_blank" >10.1016/j.heliyon.2021.e08490</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    TRPM7 N-terminal region forms complexes with calcium binding proteins CaM and S100A1

  • Original language description

    Transient receptor potential melastatin 7 (TRPM7) represents melastatin TRP channel with two significant functions, cation permeability and kinase activity. TRPM7 is widely expressed among tissues and is therefore involved in a variety of cellular functions representing mainly Mg2+ homeostasis, cellular Ca2+ flickering, and the regulation of DNA transcription by a cleaved kinase domain translocated to the nucleus. TRPM7 participates in several important biological processes in the nervous and cardiovascular systems. Together with the necessary function of the TRPM7 in these tissues and its recently analyzed overall structure, this channel requires further studies leading to the development of potential therapeutic targets. Here we present the first study investigating the N-termini of TRPM7 with binding regions for important intracellular modulators calmodulin (CaM) and calcium-binding protein S1 (S100A1) using in vitro and in silico approaches. Molecular simulations of the discovered complexes reveal their potential binding interfaces with common interaction patterns and the important role of basic residues present in the N-terminal binding region of TRPM.

  • 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

    10608 - Biochemistry and molecular biology

Result continuities

  • Project

    <a href="/en/project/GA19-04099S" target="_blank" >GA19-04099S: Role of nucleophosmin interactome in acute myeloid leukemia with mutated NPM</a><br>

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2021

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Heliyon

  • ISSN

    2405-8440

  • e-ISSN

    2405-8440

  • Volume of the periodical

    7

  • Issue of the periodical within the volume

    12

  • Country of publishing house

    GB - UNITED KINGDOM

  • Number of pages

    7

  • Pages from-to

    e08490

  • UT code for WoS article

    000748925400017

  • EID of the result in the Scopus database

    2-s2.0-85120421898