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rdf:type
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Description
| - Je diskutována molekulová dynamika CDK2 se substrátovým peptidem HHASPRK a inhibice fosforylací. (cs)
- The cyclin-dependent kinase-2, CDK2, controls the eukaryotic cell cycle at the G1 -S boundary. CDK2 catalyzes the phosphoryl transfer of the adenosine-5´-triphosphate (ATP) ?-phosphate to serine or threonine hydroxyl in the protein substrate. The CDK2 activity is regulated by complex mechanism including binding to positive regulatorysubunit (Cyclin A or Cyclin E) and phosphorylation at positive regulatory site in the activation segment (T-loop)1. The CDK2 activity is inhibited in several ways, for example, by (de)phosphorylation, interaction with various artificial and natural protein inhibitors2,3, etc. The CDK2 can be also negatively regulated by phosphorylation at Y15 and, to a lesser extent, at T14 residue in the inhibition segment (G-loop)4. Mechanism of the CDK2 inhibition by phosphorylation is known from the kinetics experiments but the structural aspects of inhibition remains unclear. The first attempt to explain the mechanism of inhibition by phosphorylation came from molecular dynamics simul
- The cyclin-dependent kinase-2, CDK2, controls the eukaryotic cell cycle at the G1 -S boundary. CDK2 catalyzes the phosphoryl transfer of the adenosine-5´-triphosphate (ATP) ?-phosphate to serine or threonine hydroxyl in the protein substrate. The CDK2 activity is regulated by complex mechanism including binding to positive regulatorysubunit (Cyclin A or Cyclin E) and phosphorylation at positive regulatory site in the activation segment (T-loop)1. The CDK2 activity is inhibited in several ways, for example, by (de)phosphorylation, interaction with various artificial and natural protein inhibitors2,3, etc. The CDK2 can be also negatively regulated by phosphorylation at Y15 and, to a lesser extent, at T14 residue in the inhibition segment (G-loop)4. Mechanism of the CDK2 inhibition by phosphorylation is known from the kinetics experiments but the structural aspects of inhibition remains unclear. The first attempt to explain the mechanism of inhibition by phosphorylation came from molecular dynamics simul (en)
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Title
| - A molecular dynamics study of the cyclin-dependent kinase-2 (CDK2) with substrate peptide (HHASPRK) inhibition by phosphorylation
- A molecular dynamics study of the cyclin-dependent kinase-2 (CDK2) with substrate peptide (HHASPRK) inhibition by phosphorylation (en)
- Molekulová dynamika CDK2 se substrátovým peptidem HHASPRK, inhibice fosforylací (cs)
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skos:prefLabel
| - A molecular dynamics study of the cyclin-dependent kinase-2 (CDK2) with substrate peptide (HHASPRK) inhibition by phosphorylation
- A molecular dynamics study of the cyclin-dependent kinase-2 (CDK2) with substrate peptide (HHASPRK) inhibition by phosphorylation (en)
- Molekulová dynamika CDK2 se substrátovým peptidem HHASPRK, inhibice fosforylací (cs)
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skos:notation
| - RIV/61989592:15310/04:00002046!RIV/2005/MSM/153105/N
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http://linked.open.../vavai/riv/strany
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http://linked.open...avai/riv/aktivita
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http://linked.open...avai/riv/aktivity
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http://linked.open...iv/cisloPeriodika
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http://linked.open...vai/riv/dodaniDat
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http://linked.open...aciTvurceVysledku
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http://linked.open.../riv/druhVysledku
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http://linked.open...iv/duvernostUdaju
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http://linked.open...titaPredkladatele
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http://linked.open...dnocenehoVysledku
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http://linked.open...ai/riv/idVysledku
| - RIV/61989592:15310/04:00002046
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http://linked.open...riv/jazykVysledku
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http://linked.open.../riv/klicovaSlova
| - cyclic dependent kinase;CDK2;inhibition;phosphorylation (en)
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http://linked.open.../riv/klicoveSlovo
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http://linked.open...odStatuVydavatele
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http://linked.open...ontrolniKodProRIV
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http://linked.open...i/riv/nazevZdroje
| - Acta Universitatis Palackianae Olomucensis, Facultas Rerum Naturalium, Chemica
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http://linked.open...in/vavai/riv/obor
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http://linked.open...ichTvurcuVysledku
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http://linked.open...cetTvurcuVysledku
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http://linked.open...UplatneniVysledku
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http://linked.open...v/svazekPeriodika
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http://linked.open...iv/tvurceVysledku
| - Koča, Jaroslav
- Otyepka, Michal
- Kříž, Zdeněk
- Bártová, Iveta
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http://linked.open...n/vavai/riv/zamer
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issn
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number of pages
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http://localhost/t...ganizacniJednotka
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