About: The 14-3-3 Protein Affects the Conformation of the Regulatory Domain of Human Tyrosine Hydroxylase     Goto   Sponge   NotDistinct   Permalink

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Description
  • Tyrosine hydroxylase (TH) catalyzes the first step in the biosynthesis of catecholamines. The main goal of this work was to investigate whether the 14-3-3 protein binding affects the conformation of the regulatory domain of human TH isoform 1 (TH1R). The 14-3-3 protein binding also reduces the sensitivity of phosphorylated TH1R to proteolysis by protecting its N-terminal part (first 33 residues)
  • Tyrosine hydroxylase (TH) catalyzes the first step in the biosynthesis of catecholamines. The main goal of this work was to investigate whether the 14-3-3 protein binding affects the conformation of the regulatory domain of human TH isoform 1 (TH1R). The 14-3-3 protein binding also reduces the sensitivity of phosphorylated TH1R to proteolysis by protecting its N-terminal part (first 33 residues) (en)
  • tyrosinhydroxylasa (TH) katalyzuje první krok v biosyntéze katecholaminů. Hlavním cílem této práce bylo zjistit, zda vazba 14-3-3 proteinu ovlivňuje konformaci regulační domény lidské TH isoformy 1 (TH1R). Vazba 14-3-3 proteinu také reguluje citlivost fosforylovaných TH1R k proteolýze ochranou N-koncového segmentu (prvních 33 zbytků) (cs)
Title
  • The 14-3-3 Protein Affects the Conformation of the Regulatory Domain of Human Tyrosine Hydroxylase
  • The 14-3-3 Protein Affects the Conformation of the Regulatory Domain of Human Tyrosine Hydroxylase (en)
  • 14-3-3 protein ovlivňuje konformaci regulační domény lidské tyrosinhydroxylasy (cs)
skos:prefLabel
  • The 14-3-3 Protein Affects the Conformation of the Regulatory Domain of Human Tyrosine Hydroxylase
  • The 14-3-3 Protein Affects the Conformation of the Regulatory Domain of Human Tyrosine Hydroxylase (en)
  • 14-3-3 protein ovlivňuje konformaci regulační domény lidské tyrosinhydroxylasy (cs)
skos:notation
  • RIV/61388971:_____/08:00315910!RIV09-AV0-61388971
http://linked.open...avai/riv/aktivita
http://linked.open...avai/riv/aktivity
  • P(GA204/06/0565), P(KJB500110601), P(LC554), Z(AV0Z50110509), Z(AV0Z50200510), Z(MSM0021620835), Z(MSM0021620857)
http://linked.open...iv/cisloPeriodika
  • 6
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
  • 407524
http://linked.open...ai/riv/idVysledku
  • RIV/61388971:_____/08:00315910
http://linked.open...riv/jazykVysledku
http://linked.open.../riv/klicovaSlova
  • 14-3-3 protein; tyroxine hydroxylase; fluorescence (en)
http://linked.open.../riv/klicoveSlovo
http://linked.open...odStatuVydavatele
  • US - Spojené státy americké
http://linked.open...ontrolniKodProRIV
  • [C35F8850A239]
http://linked.open...i/riv/nazevZdroje
  • Biochemistry
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
  • 47
http://linked.open...iv/tvurceVysledku
  • Obšil, Tomáš
  • Teisinger, Jan
  • Šulc, Miroslav
  • Bouřa, Evžen
  • Herman, P.
  • Obšilová, Veronika
  • Večeř, J.
  • Šilhán, Jan
  • Nedbálková, Eliška
  • Dyda, F.
http://linked.open...ain/vavai/riv/wos
  • 252940600031
http://linked.open...n/vavai/riv/zamer
issn
  • 0006-2960
number of pages
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