AnatomyOrganismsChemicals and DrugsAnalytical, Diagnostic and Therapeutic Techniques and EquipmentPhenomena and ProcessesDisciplines and OccupationsInformation Science
Cyclin-Dependent Kinase Inhibitor p27Cyclin-Dependent Kinase Inhibitor p21Cyclin-Dependent KinasesCyclinsCell Cycle ProteinsCyclin-Dependent Kinase Inhibitor p16Cell CycleTumor Suppressor ProteinsMicrotubule-Associated ProteinsCyclin-Dependent Kinase 2Cyclin D1Cyclin ACyclin ECell ProliferationCyclin-Dependent Kinase 4CDC2-CDC28 KinasesApoptosisCyclin-Dependent Kinase Inhibitor p57Cell Line, TumorProtein Kinase InhibitorsProtein-Serine-Threonine KinasesG1 PhaseCyclin-Dependent Kinase 5Cyclin BCyclin DCDC2 Protein KinaseCyclin-Dependent Kinase Inhibitor ProteinsCyclin CPhosphorylationCyclin D3Retinoblastoma ProteinCyclin-Dependent Kinase 6Cell DivisionEnzyme InhibitorsS PhaseCyclin B1Cyclin-Dependent Kinase Inhibitor p18Tumor Suppressor Protein p53Proto-Oncogene ProteinsTumor Cells, CulturedSignal TransductionCyclin D2Cells, CulturedPhosphatidylinositol 3-KinasesBlotting, WesternE2F1 Transcription FactorCyclin A1Protein KinasesPurinesTransfectionCell LineMitosisCyclin GG2 PhaseTranscription Factor DP1MutationProliferating Cell Nuclear AntigenCyclin-Dependent Kinase Inhibitor p15DNA-Binding ProteinsCyclin G1MAP Kinase Signaling SystemCyclin A2E2F Transcription FactorsRNA, MessengerMolecular Sequence DataCarrier ProteinsNuclear ProteinsAntineoplastic AgentsTranscription FactorsBase SequenceProtein-Tyrosine KinasesCalcium-Calmodulin-Dependent Protein KinasesImmunohistochemistryCyclin-Dependent Kinase Inhibitor p19S-Phase Kinase-Associated Proteinssrc-Family KinasesEnzyme ActivationDown-RegulationGene Expression RegulationProtein BindingProtein Kinase CReverse Transcriptase Polymerase Chain ReactionDNA DamageTranscription, GeneticIntracellular Signaling Peptides and ProteinsAmino Acid Sequencep38 Mitogen-Activated Protein Kinases3T3 CellsMitogen-Activated Protein KinasesMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase KinasesPromoter Regions, GeneticRNA, Small InterferingPyrimidinesMice, KnockoutTime FactorsCyclic AMP-Dependent Protein KinasesGene Expression Regulation, NeoplasticCell NucleusMitogen-Activated Protein Kinase 3

Increased Th17 cells in the tumor microenvironment is mediated by IL-23 via tumor-secreted prostaglandin E2. (57/73)

 (+info)

Myocardin related transcription factors are required for coordinated cell cycle progression. (58/73)

 (+info)

A network of transcription factors operates during early tooth morphogenesis. (59/73)

 (+info)

Cisplatin induces cell cycle arrest and senescence via upregulating P53 and P21 expression in HepG2 cells. (60/73)

OBJECTIVE: Cellular senescence as one of the important steps against tumor is observed in many cancer patients receiving chemotherapy and is related to chemotherapeutic response. To investigate the effect of cisplatin on hepatocellular carcinoma, we treated HepG2 cells exhibiting wild-type TP53 with gradient concentrations of cisplatin. METHODS: The inhibitory effects of cisplatin on human hepatoma HepG2 cells were detected by MTT assay and colony formation test. The changes in cell cycle were analyzed by flow cytometry, and cellular senescence was detected with senescence associated beta-galactosidase (SA beta-gal) staining. The relative mRNA expression levels of TP53, P21 and P19 was estimated using semi-quantitative real-time RT-PCR, and the protein expressions of P53 and P21 were detected using Western blotting. RESULTS: Cisplatin induced irreversible proliferation inhibition and G1 phase arrest of HepG2 cells. Elevated levels of senescence-associated beta-galactosidase was observed in HepG2 cells exposed to low doses of cisplatin. P19 expression immediately increased following cisplatin exposure and reached the maximum level at 48 h, followed then by a rapid decrease to the baseline level, whereas the expressions levels of TP53 and P21 mRNA increased continuously. Western blotting confirmed P53 and P21 expression changes similar to their mRNA expressions during cisplatin-induced cellular senescence in HepG2 cells. CONCLUSION: Our results revealed a functional link between cisplatin and hepatocellular senescence. Cellular senescence induced by cisplatin as a stabile senescent cellular model can be used for further research.  (+info)

Nucleostemin is indispensable for the maintenance and genetic stability of hematopoietic stem cells. (61/73)

 (+info)

Lung tumourigenesis in a conditional Cul4A transgenic mouse model. (62/73)

 (+info)

Isolation and characterization of p19INK4d, a p16-related inhibitor specific to CDK6 and CDK4. (63/73)

Cyclin-dependent kinases 4 and 6 are complexed with many small cellular proteins in vivo. We have isolated cDNA sequences, INK4d, encoding a 19-kDa protein that is associated with CDK6 in several hematopoietic cell lines. p19 shares equal similarity and a common ancestor with other identified inhibitors of the p16/INK4 family. p19 interacts with and inhibits the activity of both CDK4 and CDK6 and exhibits no detectable interaction with the other known CDKs. p19 protein is present in both cell nuclei and cytoplasm. The p19 gene has been mapped to chromosome 19p13.2, and the level of its mRNA expression varies widely between different tissues. In contrast to p21 and p27 whose interaction with CDK subunits is dependent on or stimulated by the cyclin subunit, the interaction of p19 and p18 with CDK6 is hindered by the cyclin protein. Binary cyclin D1-p18/p19 or cyclin D1-CDK6 complexes are highly stable and cannot be dissociated by excess amounts of cyclin D1 or p19/p18 proteins, suggesting that p16 inhibitors and D cyclins may interact with CDKs 4 and 6 in a competing or potentially mutually exclusive manner.  (+info)

NMR structural characterization of the CDK inhibitor p19INK4d. (64/73)

p19INK4d is a 165 amino acid protein that belongs to the INK4 family of CDK4 and CDK6 inhibitors. Assignments of 1H, 15N and 13C resonances have enabled the determination of the secondary structure of the protein which is largely alpha-helical (residues 14-18, 21-29, 54-62, 77-83, 87-95, 110-116, 120-128, 142-148 and 152-160). The protein comprises five 32-amino acid ankyrin-like repeats; each ankyrin repeat contains a helix-beta-turn-helix core. The exception is the second ankyrin repeat, which lacks the first helix. All beta-turns have a central glycine residue flanked by two residues in beta-conformations. There is also a high conservation of Ala at position 8 in the first helix and Leu-Leu(Val) at positions 17-18 of the second helix in all ankyrin repeats of p19. The location of the helix-turn-helix segments found in p19 should be general for all other members of the INK4 family, including, for example, a homologous tumor suppressor p16INK4a. 1H-15N heteronuclear steady-state NOE measurements on p19 indicate that most of the backbone of p19INK4d exists in a well defined structure of limited conformational flexibility on the nano- to picosecond time scale.  (+info)