About: Hydroxamic acids as a novel family of serine racemase inhibitors: Mechanistic analysis reveals different modes of interaction with the pyridoxal-5'-phosphate cofactor     Goto   Sponge   NotDistinct   Permalink

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  • Mammalian serine racemase (SR) is a pyridoxal-5-phosphate (PLP) dependent enzyme responsible for the biosynthesis of the neurotransmitter d-serine, which activates N-methyl-d-aspartate (NMDA) receptors in the CNS. Aberrant regulation of NMDA receptor signaling has been implicated in a variety of neuropathologies, and inhibitors of SR would therefore be a worthwhile tool for further investigation or treatment of such conditions. Here, we identify a series of small aliphatic hydroxamic acids (HAs) that act as potent SR inhibitors and present a detailed analysis of there mechanism of action.
  • Mammalian serine racemase (SR) is a pyridoxal-5-phosphate (PLP) dependent enzyme responsible for the biosynthesis of the neurotransmitter d-serine, which activates N-methyl-d-aspartate (NMDA) receptors in the CNS. Aberrant regulation of NMDA receptor signaling has been implicated in a variety of neuropathologies, and inhibitors of SR would therefore be a worthwhile tool for further investigation or treatment of such conditions. Here, we identify a series of small aliphatic hydroxamic acids (HAs) that act as potent SR inhibitors and present a detailed analysis of there mechanism of action. (en)
Title
  • Hydroxamic acids as a novel family of serine racemase inhibitors: Mechanistic analysis reveals different modes of interaction with the pyridoxal-5'-phosphate cofactor
  • Hydroxamic acids as a novel family of serine racemase inhibitors: Mechanistic analysis reveals different modes of interaction with the pyridoxal-5'-phosphate cofactor (en)
skos:prefLabel
  • Hydroxamic acids as a novel family of serine racemase inhibitors: Mechanistic analysis reveals different modes of interaction with the pyridoxal-5'-phosphate cofactor
  • Hydroxamic acids as a novel family of serine racemase inhibitors: Mechanistic analysis reveals different modes of interaction with the pyridoxal-5'-phosphate cofactor (en)
skos:notation
  • RIV/67985858:_____/09:00330745!RIV10-MSM-67985858
http://linked.open...avai/riv/aktivita
http://linked.open...avai/riv/aktivity
  • P(1M0508), P(IAA400720706), Z(AV0Z40550506), Z(AV0Z40720504)
http://linked.open...iv/cisloPeriodika
  • 19
http://linked.open...vai/riv/dodaniDat
http://linked.open...aciTvurceVysledku
http://linked.open.../riv/druhVysledku
http://linked.open...iv/duvernostUdaju
http://linked.open...titaPredkladatele
http://linked.open...dnocenehoVysledku
  • 318191
http://linked.open...ai/riv/idVysledku
  • RIV/67985858:_____/09:00330745
http://linked.open...riv/jazykVysledku
http://linked.open.../riv/klicovaSlova
  • hydroxamic acids; serine racemase; d-serine; pyridoxal-5'-phosphate (en)
http://linked.open.../riv/klicoveSlovo
http://linked.open...odStatuVydavatele
  • US - Spojené státy americké
http://linked.open...ontrolniKodProRIV
  • [883B178129D3]
http://linked.open...i/riv/nazevZdroje
  • Journal of Medicinal Chemistry
http://linked.open...in/vavai/riv/obor
http://linked.open...ichTvurcuVysledku
http://linked.open...cetTvurcuVysledku
http://linked.open...vavai/riv/projekt
http://linked.open...UplatneniVysledku
http://linked.open...v/svazekPeriodika
  • 52
http://linked.open...iv/tvurceVysledku
  • Cígler, Petr
  • Konvalinka, Jan
  • Schraml, Jan
  • Šanda, Miloslav
  • Hoffman, Hillary Elizabeth
  • Jirásková, Jana
http://linked.open...ain/vavai/riv/wos
  • 000270361600025
http://linked.open...n/vavai/riv/zamer
issn
  • 0022-2623
number of pages
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