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Cathepsin D propeptide: Mechanism and Regulation of its interaction with the catalytic core

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F06%3A00053658" target="_blank" >RIV/61388963:_____/06:00053658 - isvavai.cz</a>

  • Result on the web

  • DOI - Digital Object Identifier

Alternative languages

  • Result language

    angličtina

  • Original language name

    Cathepsin D propeptide: Mechanism and Regulation of its interaction with the catalytic core

  • Original language description

    The propeptide blocks the active site of inactive zymogen of cathepsin D and is cleaved off during maturation. We tested set of peptidic fragments derived from the propeptide and evaluated their inhibitory potency and mode of inhibition against mature cathepsin D using kinetic activity assay. Fragment derived from the propeptide N-terminus displayed major inhibition. We investigated influence of sulfated glycosaminoglycans and propeptide mutations.

  • Czech name

    Propeptid katepsinu D: mechanismus a regulace jakointerakce s katalytickým jádrem

  • Czech description

    Propeptid blokuje aktivní místo inaktivního zymogenu katepsinu D a je vyštěpován během zrání. Testovali jsme sadu peptidových fragmentů odvozených od propeptidu a v kinetickém aktivitním testu se zralým katepsinem D jsme určili jejich inhibiční potenciála mod inhibice. Fragment odvozený od N-konce propeptidu vykazoval největší inhibici. Zkoumali jsme vliv sulfatovaných glykosaminoglykanů a peptidových mutací.

Classification

  • Type

    J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

  • CEP classification

    CE - Biochemistry

  • OECD FORD branch

Result continuities

  • Project

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

  • Continuities

    P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)

Others

  • Publication year

    2006

  • 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

    45

  • Issue of the periodical within the volume

    51

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    9

  • Pages from-to

    15474-15482

  • UT code for WoS article

  • EID of the result in the Scopus database