About: Beta-N-Acetylhexosaminidases: group-specific inhibitors wanted

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An Entity of Type : http://linked.opendata.cz/ontology/domain/vavai/Vysledek, within Data Space : linked.opendata.cz associated with source document(s)

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rdf:type	skos:Concept http://linked.opendata.cz/ontology/domain/vavai/Vysledek
Description	Beta-N-Acetylhexosaminidases (GH20) and β-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 order to 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 compounds suitable for specific application Beta-N-Acetylhexosaminidases (GH20) and β-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 order to 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 compounds suitable for specific application (en)
Title	Beta-N-Acetylhexosaminidases: group-specific inhibitors wanted Beta-N-Acetylhexosaminidases: group-specific inhibitors wanted (en)
skos:prefLabel	Beta-N-Acetylhexosaminidases: group-specific inhibitors wanted Beta-N-Acetylhexosaminidases: group-specific inhibitors wanted (en)
skos:notation	RIV/61388971:_____/13:00395482!RIV14-AV0-61388971
http://linked.open...avai/predkladatel	Mikrobiologický ústav AV ČR, v.v.i.
http://linked.open...avai/riv/aktivita	I P
http://linked.open...avai/riv/aktivity	I, P(GP13-06818P)
http://linked.open...vai/riv/dodaniDat	2014
http://linked.open...aciTvurceVysledku	Slámová, Kristýna Křen, Vladimír
http://linked.open.../riv/druhVysledku	C - Kapitola v knize
http://linked.open...iv/duvernostUdaju	S - Úplné a pravdivé údaje nepodléhající ochraně podle zvláštních právních předpisů
http://linked.open...titaPredkladatele	Mikrobiologický ústav AV ČR, v. v. i.
http://linked.open...dnocenehoVysledku	63132
http://linked.open...ai/riv/idVysledku	RIV/61388971:_____/13:00395482
http://linked.open...riv/jazykVysledku	eng - angličtina
http://linked.open.../riv/klicovaSlova	β-N-Acetylhexosaminidases:; Alzheimer’s disease (en)
http://linked.open.../riv/klicoveSlovo	β-N-Acetylhexosaminidases: Alzheimer’s disease
http://linked.open...ontrolniKodProRIV	[0EFD32BD0729]
http://linked.open...i/riv/mistoVydani	Cambridge
http://linked.open...vEdiceCisloSvazku	Chemical and Biological Approaches, 39
http://linked.open...i/riv/nazevZdroje	Carbohydrate Chemistry
http://linked.open...in/vavai/riv/obor	CE
http://linked.open...ichTvurcuVysledku	2 (xsd:int)
http://linked.open...v/pocetStranKnihy	246 (xsd:int)
http://linked.open...cetTvurcuVysledku	2 (xsd:int)
http://linked.open...vavai/riv/projekt	New synthetic approaches using mutant and wild-type beta-N-acetylhexosaminidase from Talaromyces flavus
http://linked.open...UplatneniVysledku	2013
http://linked.open...iv/tvurceVysledku	Křen, Vladimír Slámová, Kristýna
number of pages	18 (xsd:int)
http://bibframe.org/vocab/doi	10.1039/9781849737173-00102
http://purl.org/ne...btex#hasPublisher	The Royal Society of Chemistry
https://schema.org/isbn	978-1-84973-587-2

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