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Statements

Subject Item
n2:RIV%2F00216224%3A14310%2F04%3A00010531%21RIV08-MSM-14310___
rdf:type
skos:Concept n20:Vysledek
dcterms:description
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 regulatory subunit (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 inhibitors [2,3], 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 dynami MD studie CDK2 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 regulatory subunit (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 inhibitors [2,3], 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 dynami
dcterms:title
MD studie CDK2 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
skos:prefLabel
MD studie CDK2 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
skos:notation
RIV/00216224:14310/04:00010531!RIV08-MSM-14310___
n3:strany
260-261
n3:aktivita
n9:Z
n3:aktivity
Z(MSM 143100005)
n3:dodaniDat
n8:2008
n3:domaciTvurceVysledku
n11:4347374 n11:9309616 n11:5517680
n3:druhVysledku
n15:D
n3:duvernostUdaju
n6:S
n3:entitaPredkladatele
n13:predkladatel
n3:idSjednocenehoVysledku
552987
n3:idVysledku
RIV/00216224:14310/04:00010531
n3:jazykVysledku
n14:eng
n3:klicovaSlova
cell cycle; CDK regulation; phosphorylated tyrosine; threonine
n3:klicoveSlovo
n5:cell%20cycle n5:threonine n5:CDK%20regulation n5:phosphorylated%20tyrosine
n3:kontrolniKodProRIV
[9AD2169C53D8]
n3:mistoKonaniAkce
Olomouc
n3:mistoVydani
Olomouc
n3:nazevZdroje
Acta Univ. Palacki. Olomouc., Fac. Rer. Nat., Chemica 43S
n3:obor
n17:CE
n3:pocetDomacichTvurcuVysledku
3
n3:pocetTvurcuVysledku
4
n3:rokUplatneniVysledku
n8:2004
n3:tvurceVysledku
Otyepka, Michal Koča, Jaroslav Bártová, Iveta Kříž, Zdeněk
n3:typAkce
n10:CST
n3:zahajeniAkce
2004-01-01+01:00
n3:zamer
n19:MSM%20143100005
s:numberOfPages
2
n21:hasPublisher
Univerzita Palackého v Olomouci
n18:isbn
80-244-0353-6
n16:organizacniJednotka
14310