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RNase T1 Refolding Assay for Determining Mitochondrial Cyclophilin D Activity: A Novel In Vitro Method Applicable in Drug Research and Discovery

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F62690094%3A18470%2F20%3A50016740" target="_blank" >RIV/62690094:18470/20:50016740 - isvavai.cz</a>

  • Alternative codes found

    RIV/00179906:_____/20:10418150

  • Result on the web

    <a href="https://pubs.acs.org/doi/10.1021/acs.biochem.9b01025?ref=pdf" target="_blank" >https://pubs.acs.org/doi/10.1021/acs.biochem.9b01025?ref=pdf</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1021/acs.biochem.9b01025" target="_blank" >10.1021/acs.biochem.9b01025</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    RNase T1 Refolding Assay for Determining Mitochondrial Cyclophilin D Activity: A Novel In Vitro Method Applicable in Drug Research and Discovery

  • Original language description

    Human cyclophilin D is a mitochondrial peptidyl-prolyl isomerase that plays a role in regulating the opening of the mitochondrial permeability transition pore. It is considered a viable and promising molecular target for the treatment of diseases for which disease development is associated with pore opening, e.g., Alzheimer&apos;s disease or ischemia/reperfusion injury. Currently available and widely used in vitro methods based on Kofron&apos;s assay for determining cyclophilin D activity suffer from serious drawbacks and limitations. In this study, a completely novel approach for an in vitro assay of cyclophilin D activity using RNase T1 refolding is introduced. The method is simple and is more in line with the presumed physiological role of cydophilin D in protein folding than Kofron&apos;s assay, which relies on a peptide substrate. The method is applicable for identifying novel inhibitors of cyclophilin D as potential drugs for the treatment of the diseases mentioned above. Moreover, the description of CypD activity in the in vitro RNase T1 refolding assay reveals new possibilities for investigating the role of cyclophilin D in protein folding in cells and may lead to a better understanding of its pathological and physiological roles.

  • 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/EF18_069%2F0010054" target="_blank" >EF18_069/0010054: IT4Neuro(degeneration)</a><br>

  • Continuities

    P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>S - Specificky vyzkum na vysokych skolach<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

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

    Biochemistry

  • ISSN

    0006-2960

  • e-ISSN

  • Volume of the periodical

    59

  • Issue of the periodical within the volume

    17

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    8

  • Pages from-to

    1680-1687

  • UT code for WoS article

    000530650400010

  • EID of the result in the Scopus database

    2-s2.0-85084270684