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Beta-N-Acetylhexosaminidases: group-specific inhibitors wanted

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F13%3A00395482" target="_blank" >RIV/61388971:_____/13:00395482 - isvavai.cz</a>

  • Result on the web

    <a href="http://dx.doi.org/10.1039/9781849737173-00102" target="_blank" >http://dx.doi.org/10.1039/9781849737173-00102</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1039/9781849737173-00102" target="_blank" >10.1039/9781849737173-00102</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Beta-N-Acetylhexosaminidases: group-specific inhibitors wanted

  • Original language description

    Beta-N-Acetylhexosaminidases (GH20) and ?-N-acetylglucosaminidases (GH84) are two genetically and functionally unrelated classes of glycosidases sharing the substrate-assisted catalytic mechanism and architecture of their active sites. In humans, the deficiency of these enzymes causes severe neurodegenerative disorders (GH20) and Alzheimer?s disease (GH84). For the research of the physiological functions of these enzymes, inhibitors selective for just one of the enzyme families must be employed in orderto avoid the generation of complex phenotypes. The search for highly potent and selective inhibitor sis based on the known common and distinct features of these enzyme groups, profiting from the crystal structures of the enzyme-inhibitor complexes. In this chapter, the most studied inhibitor scaffolds such as NAG-thiazoline, PUGNAc and GlcNAcstatins and their rationally designed analogues are described and discussed, providing an actual survey of the most efficient and selective compoun

  • Czech name

  • Czech description

Classification

  • Type

    C - Chapter in a specialist book

  • CEP classification

    CE - Biochemistry

  • OECD FORD branch

Result continuities

  • Project

    <a href="/en/project/GP13-06818P" target="_blank" >GP13-06818P: New synthetic approaches using mutant and wild-type beta-N-acetylhexosaminidase from Talaromyces flavus</a><br>

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2013

  • Confidentiality

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

Data specific for result type

  • Book/collection name

    Carbohydrate Chemistry

  • ISBN

    978-1-84973-587-2

  • Number of pages of the result

    18

  • Pages from-to

    102-119

  • Number of pages of the book

    246

  • Publisher name

    The Royal Society of Chemistry

  • Place of publication

    Cambridge

  • UT code for WoS chapter