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Statements

Subject Item
n2:RIV%2F61388971%3A_____%2F13%3A00395482%21RIV14-AV0-61388971
rdf:type
skos:Concept n5:Vysledek
dcterms: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
dcterms:title
Beta-N-Acetylhexosaminidases: group-specific inhibitors wanted Beta-N-Acetylhexosaminidases: group-specific inhibitors wanted
skos:prefLabel
Beta-N-Acetylhexosaminidases: group-specific inhibitors wanted Beta-N-Acetylhexosaminidases: group-specific inhibitors wanted
skos:notation
RIV/61388971:_____/13:00395482!RIV14-AV0-61388971
n5:predkladatel
n6:ico%3A61388971
n3:aktivita
n16:P n16:I
n3:aktivity
I, P(GP13-06818P)
n3:dodaniDat
n7:2014
n3:domaciTvurceVysledku
n21:7072104 n21:5894190
n3:druhVysledku
n10:C
n3:duvernostUdaju
n19:S
n3:entitaPredkladatele
n13:predkladatel
n3:idSjednocenehoVysledku
63132
n3:idVysledku
RIV/61388971:_____/13:00395482
n3:jazykVysledku
n11:eng
n3:klicovaSlova
β-N-Acetylhexosaminidases:; Alzheimer’s disease
n3:klicoveSlovo
n18:%CE%B2-N-Acetylhexosaminidases%3A n18:Alzheimer%E2%80%99s%20disease
n3:kontrolniKodProRIV
[0EFD32BD0729]
n3:mistoVydani
Cambridge
n3:nazevEdiceCisloSvazku
Chemical and Biological Approaches, 39
n3:nazevZdroje
Carbohydrate Chemistry
n3:obor
n8:CE
n3:pocetDomacichTvurcuVysledku
2
n3:pocetStranKnihy
246
n3:pocetTvurcuVysledku
2
n3:projekt
n14:GP13-06818P
n3:rokUplatneniVysledku
n7:2013
n3:tvurceVysledku
Křen, Vladimír Slámová, Kristýna
s:numberOfPages
18
n15:doi
10.1039/9781849737173-00102
n12:hasPublisher
The Royal Society of Chemistry
n17:isbn
978-1-84973-587-2