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Description
  • Cyclin-dependent kinases (CDKs) are enzymes controlling the eukaryotic cell cycle. Cell-cycle dependent oscillations in CDK activity are induced by complex mechanisms that include binding to positive regulatory subunits and phosphorylation at positive and negative regulatory sites. Binding to Cyclin A or Cyclin E is required for CDK2 activation. CDK2 obtains full activity by phosphorylation of the T160 residue in the activation segment (T-loop) and it is inhibited by phosphorylation on inhibitory sites at Y15 and/or T14 in the Glycine rich loop (G-loop). CDK2 is inhibited also by interactions with various native protein inhibitors. The primary function of CDK is to catalyze the phosphoryl transfer of the ATP g-phosphate to serine or threonine hydroxyl in the protein target substrate. The adenosine triphosphate is native substrate of CDK2. Human CDK2 contains the classical bi-lobal kinase fold. The ATP binding site is located in the deep cleft between two lobes. The N-terminal domain is composed mainly
  • Cyclin-dependent kinases (CDKs) are enzymes controlling the eukaryotic cell cycle. Cell-cycle dependent oscillations in CDK activity are induced by complex mechanisms that include binding to positive regulatory subunits and phosphorylation at positive and negative regulatory sites. Binding to Cyclin A or Cyclin E is required for CDK2 activation. CDK2 obtains full activity by phosphorylation of the T160 residue in the activation segment (T-loop) and it is inhibited by phosphorylation on inhibitory sites at Y15 and/or T14 in the Glycine rich loop (G-loop). CDK2 is inhibited also by interactions with various native protein inhibitors. The primary function of CDK is to catalyze the phosphoryl transfer of the ATP g-phosphate to serine or threonine hydroxyl in the protein target substrate. The adenosine triphosphate is native substrate of CDK2. Human CDK2 contains the classical bi-lobal kinase fold. The ATP binding site is located in the deep cleft between two lobes. The N-terminal domain is composed mainly (en)
  • Cyclin-dependent kinases (CDKs) are enzymes controlling the eukaryotic cell cycle. Cell-cycle dependent oscillations in CDK activity are induced by complex mechanisms that include binding to positive regulatory subunits and phosphorylation at positive and negative regulatory sites. Binding to Cyclin A or Cyclin E is required for CDK2 activation. CDK2 obtains full activity by phosphorylation of the T160 residue in the activation segment (T-loop) and it is inhibited by phosphorylation on inhibitory sites at Y15 and/or T14 in the Glycine rich loop (G-loop). CDK2 is inhibited also by interactions with various native protein inhibitors. The primary function of CDK is to catalyze the phosphoryl transfer of the ATP g-phosphate to serine or threonine hydroxyl in the protein target substrate. The adenosine triphosphate is native substrate of CDK2. Human CDK2 contains the classical bi-lobal kinase fold. The ATP binding site is located in the deep cleft between two lobes. The N-terminal domain is composed mainly (cs)
Title
  • COMPUTER SIMULATIONS OF CYCLIN-DEPENDENT KINASE-2 NOTES ABOUT INHIBITION
  • COMPUTER SIMULATIONS OF CYCLIN-DEPENDENT KINASE-2 NOTES ABOUT INHIBITION (en)
  • COMPUTER SIMULATIONS OF CYCLIN-DEPENDENT KINASE-2 NOTES ABOUT INHIBITION (cs)
skos:prefLabel
  • COMPUTER SIMULATIONS OF CYCLIN-DEPENDENT KINASE-2 NOTES ABOUT INHIBITION
  • COMPUTER SIMULATIONS OF CYCLIN-DEPENDENT KINASE-2 NOTES ABOUT INHIBITION (en)
  • COMPUTER SIMULATIONS OF CYCLIN-DEPENDENT KINASE-2 NOTES ABOUT INHIBITION (cs)
skos:notation
  • RIV/00216224:14310/03:00009258!RIV08-MSM-14310___
http://linked.open.../vavai/riv/strany
  • 8
http://linked.open...avai/riv/aktivita
http://linked.open...avai/riv/aktivity
  • P(LN00A016)
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
  • 601948
http://linked.open...ai/riv/idVysledku
  • RIV/00216224:14310/03:00009258
http://linked.open...riv/jazykVysledku
http://linked.open.../riv/klicovaSlova
  • molekular dynamics; CDK regulation; cell cycle (en)
http://linked.open.../riv/klicoveSlovo
http://linked.open...ontrolniKodProRIV
  • [025FA618970D]
http://linked.open...v/mistoKonaniAkce
  • Nové Hrady
http://linked.open...i/riv/mistoVydani
  • Praha
http://linked.open...i/riv/nazevZdroje
  • Book of Abstracts
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...iv/tvurceVysledku
  • Koča, Jaroslav
  • Otyepka, Michal
  • Kříž, Zdeněk
  • Bártová, Iveta
http://linked.open...vavai/riv/typAkce
http://linked.open.../riv/zahajeniAkce
number of pages
http://purl.org/ne...btex#hasPublisher
  • Workshop on Modeling Interactions in Biomolecules
http://localhost/t...ganizacniJednotka
  • 14310
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