Search results for "PROTEIN KINASE"

showing 10 items of 1188 documents

In silico identification of small molecules as new cdc25 inhibitors through the correlation between chemosensitivity and protein expression pattern

2021

The cell division cycle 25 (Cdc25) protein family plays a crucial role in controlling cell proliferation, making it an excellent target for cancer therapy. In this work, a set of small molecules were identified as Cdc25 modulators by applying a mixed ligand-structure-based approach and taking advantage of the correlation between the chemosensitivity of selected structures and the protein expression pattern of the proposed target. In the first step of the in silico protocol, a set of molecules acting as Cdc25 inhibitors were identified through a new ligand-based protocol and the evaluation of a large database of molecular structures. Subsequently, induced-fit docking (IFD) studies allowed us…

0301 basic medicineHepG2Protein familyCdc25In silicoAntiproliferative activityCell cycleLigandsCatalysisArticleInorganic Chemistrylcsh:Chemistry03 medical and health sciencesCdc250302 clinical medicineCDC2 Protein KinaseDrug DiscoveryHumanscdc25 PhosphatasesComputer SimulationMolecular Targeted TherapyPhysical and Theoretical ChemistryPhosphorylationMolecular Biologylcsh:QH301-705.5DRUDITSpectroscopyBinding SitesbiologyCell growthChemistryOrganic ChemistryGeneral MedicineHep G2 CellsCell cycleAntiproliferative activity; Cdc25; Cell cycle; DRUDIT; HepG2; Molecular dockingLigand (biochemistry)Small moleculeComputer Science Applications030104 developmental biologyBiochemistrylcsh:Biology (General)lcsh:QD1-999Docking (molecular)030220 oncology & carcinogenesisMolecular dockingbiology.proteinDrug Screening Assays Antitumor
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The analysis of estrogen receptor-α positive breast cancer stem-like cells unveils a high expression of the serpin proteinase inhibitor PI-9: Possibl…

2016

Abstract Breast cancer stem cells seem to play important roles in breast tumor recurrence and endocrine therapy resistance, although the underlying mechanisms have not been well established. Moreover, in some tumor systems the immunosurveillance failure against cancer cells has been related to the presence of the granzyme B inhibitor PI-9. This study explored the status of PI-9 in tumorspheres isolated from estrogen receptor-α positive (ERα+) breast cancer MCF7 cells. Studies were performed in tertiary tumorspheres which possess high levels of stemness markers (Nanog, Oct3/4 and Sox2) and self-renewal ability. The exposure to estrogens (17-β estradiol and genistein) increased the number and…

0301 basic medicineHomeobox protein NANOGReceptors CXCR4Cancer Researchmedicine.medical_specialtyEstrogen receptorBreast NeoplasmsBiologyp38 Mitogen-Activated Protein KinasesGranzymes03 medical and health sciences0302 clinical medicineBreast cancerSOX2Internal medicineserpin proteinase inhibitor 9 breast cancer stem-like cells breast cancer estrogen receptorsSettore BIO/10 - BiochimicamedicineHumansSerpinsCell ProliferationEstrogen Receptor alphaCancermedicine.diseaseGenisteinGene Expression Regulation NeoplasticImmunosurveillance030104 developmental biologyEndocrinologyOncology030220 oncology & carcinogenesisCancer cellMCF-7 CellsNeoplastic Stem CellsCancer researchFemaleNeoplasm Recurrence LocalStem cellSignal Transduction
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Dynamic regulatory interaction between cytomegalovirus major tegument protein pp65 and protein kinase pUL97 in intracellular compartments, dense bodi…

2017

Human cytomegalovirus (HCMV) is a ubiquitous pathogen of considerable clinical importance. Understanding the processes that are important for viral replication is essential for the development of therapeutic strategies against HCMV infection. The HCMV-encoded protein kinase pUL97 is an important multifunctional regulator of viral replication. Several viral and cellular proteins are phosphorylated by pUL97. The phosphoprotein pp65 is one important substrate of pUL97. It is the most abundant tegument protein of HCMV virions, mediating the upload of other virion constituents and contributing to particle integrity. Further to that, it interferes with host innate immune defences, thereby enablin…

0301 basic medicineHuman cytomegalovirusvirusesDNA Mutational AnalysisMutantCytomegalovirusBiologyVirus ReplicationViral Matrix ProteinsViral Proteins03 medical and health sciencesViral entryVirologyProtein Interaction MappingViral structural proteinmedicineHumansProtein kinase Avirus diseasesViral tegumentbiochemical phenomena metabolism and nutritionPhosphoproteinsmedicine.diseaseVirologyCell biology030104 developmental biologyViral replicationPhosphoproteinJournal of General Virology
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Synthesis, antitumor activity and CDK1 inhibiton of new thiazole nortopsentin analogues

2017

A new series of thiazole nortopsentin analogues was conveniently synthesized with fair overall yields. The antiproliferative activity of the new derivatives was tested against different human tumor cell lines of the NCI full panel. Four of them showed good antitumor activity with GI(50) values from micro to nanomolar level. The mechanism of the antiproliferative effect of these derivatives, was pro-apoptotic, being associated with externalization of plasma membrane phosphatidylserine and DNA fragmentation. The most active and selective of the new thiazoles confined viable cells in G2/M phase and markedly inhibited in vitro CDK1 activity. (C) 2017 Elsevier Masson SAS.

0301 basic medicineIndolesCell SurvivalStereochemistryMolecular ConformationNortopsentin analogues3-b]pyridinesAntineoplastic AgentsApoptosisMarine alkaloids Nortopsentin analogues Antiproliferative activity Apoptosis CDK1 inhibitors Thiazolyl-1H-pyrrolo[23-b]pyridinesAntiproliferative activity01 natural sciencesStructure-Activity Relationship03 medical and health scienceschemistry.chemical_compoundMarine alkaloidsCDC2 Protein KinaseDrug DiscoveryHumansThiazoleProtein Kinase InhibitorsCell ProliferationPharmacologyCyclin-dependent kinase 1Dose-Response Relationship DrugMarine alkaloids; Nortopsentin analogues; Antiproliferative activity; Apoptosis; CDK1 inhibitors; Thiazolyl-1H-pyrrolo[2; 3-b]pyridines010405 organic chemistryOrganic ChemistryImidazolesGeneral MedicinePhosphatidylserineThiazolyl-1H-pyrrolo[2Settore CHIM/08 - Chimica FarmaceuticaCyclin-Dependent KinasesIn vitro0104 chemical sciencesCDK1 inhibitors030104 developmental biologyMembranechemistryCell cultureApoptosisMCF-7 CellsDNA fragmentationCaco-2 CellsDrug Screening Assays Antitumor
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Feedback Regulation of Syk by Protein Kinase C in Human Platelets

2019

The spleen tyrosine kinase (Syk) is essential for immunoreceptor tyrosine-based activation motif (ITAM)-dependent platelet activation, and it is stimulated by Src-family kinase (SFK)-/Syk-mediated phosphorylation of Y352 (interdomain-B) and Y525/526 (kinase domain). Additional sites for Syk phosphorylation and protein interactions are known but remain elusive. Since Syk S297 phosphorylation (interdomain-B) was detected in platelets, we hypothesized that this phosphorylation site regulates Syk activity via protein kinase C (PKC)-and cyclic adenosine monophosphate (cAMP)-dependent pathways. ADP, the GPVI-agonist convulxin, and the GPIb&alpha

0301 basic medicineIndolesPlatelet AggregationSyk030204 cardiovascular system & hematologyenvironment and public healthMaleimideslcsh:Chemistrychemistry.chemical_compound0302 clinical medicinePhosphorylationlcsh:QH301-705.5SpectroscopyFeedback PhysiologicalKinaseConvulxinhemic and immune systemsGeneral MedicineComputer Science ApplicationsCell biologyAdenosine DiphosphateplateletsPhosphorylationbiological phenomena cell phenomena and immunityBlood Plateletschemical and pharmacologic phenomenaViper Venomsspleen tyrosine kinase (Syk)CatalysisArticleInorganic Chemistryglycoprotein VIglycoprotein Ibα03 medical and health sciencesCrotalid VenomsHumansSyk KinaseCyclic adenosine monophosphateLectins C-TypePlatelet activationPhysical and Theoretical ChemistryMolecular BiologyProtein kinase CPhospholipase C gammaOrganic Chemistryenzymes and coenzymes (carbohydrates)030104 developmental biologyProtein kinase domainchemistrylcsh:Biology (General)lcsh:QD1-999Calciumcyclic adenosine monophosphate (cAMP)protein kinase CInternational Journal of Molecular Sciences
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Cyclin-Dependent Kinase 4 Regulates Adult Neural Stem Cell Proliferation and Differentiation in Response to Insulin

2017

Abstract Insulin is one of the standard components used to culture primary neurospheres. Although it stimulates growth of different types of cells, the effects of insulin on adult neural stem cells (NSCs) have not been well characterized. Here, we reveal that insulin stimulates proliferation, but not survival or self-renewal, of adult NSCs. This effect is mediated by insulin receptor substrate 2 (IRS2) and subsequent activation of the protein kinase B (or Akt), leading to increased activity of the G1-phase cyclin-dependent kinase 4 (Cdk4) and cell cycle progression. Neurospheres isolated from Irs2-deficient mice are reduced in size and fail to expand in culture and this impaired proliferati…

0301 basic medicineInsulin Receptor Substrate ProteinsNeurogenesisCellular differentiationBiologyAdult neurogenesisMice03 medical and health sciencesNeural Stem CellsCyclin-dependent kinaseNeurosphereAnimalsInsulinPhosphorylationNeuritogenesisProtein kinase BCell ProliferationCell CycleG1 PhaseCyclin-dependent kinaseCyclin-Dependent Kinase 4Cell DifferentiationCell BiologyIRS2Neural stem cellCell biology030104 developmental biologyVentricular-subventricular zoneInsulin Receptor Substrate Proteinsbiology.proteinMolecular MedicineNeurospheresbiological phenomena cell phenomena and immunityStem cellDevelopmental BiologyStem Cells
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Cooperation of Secondary Transporters and Sensor Kinases in Transmembrane Signalling

2016

Many membrane-bound sensor kinases require accessory proteins for function. The review describes functional control of membrane-bound sensors by transporters. The C4-dicarboxylate sensor kinase DcuS requires the aerobic or anaerobic C4-dicarboxylate transporters DctA or DcuB, respectively, for function and forms DctA/DcuS or DcuB/DcuS sensor complexes. Free DcuS is in the permanent (ligand independent) ON state. The DctA/DcuS and DcuB/DcuS complexes, on the other hand, control expression in response to C4-dicarboxylates. In DctA/DcuS, helix 8b of DctA and the PASC domain of DcuS are involved in interaction. The stimulus is perceived by the extracytoplasmic sensor domain (PASP) of DcuS. The …

0301 basic medicineKinase030106 microbiologyComplex formationTransporterLimitingBiologymedicine.disease_causeCell biology03 medical and health sciencesTransmembrane signallingBiochemistryProtein kinase domainmedicineEscherichia coli
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A selective inhibitor of the Polo-box domain of Polo-like kinase 1 identified by virtual screening

2018

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0301 basic medicineLK Polo-like kinasePolo-like kinaseCell cycleIC50 50% inhibition concentrationVirtual drug screeningPLK103 medical and health sciences0302 clinical medicineNeoplasmsTargeted chemotherapylcsh:Science (General)MitosisComputingMethodologies_COMPUTERGRAPHICSCDK cyclin-dependent kinasePBD Polo-box domainPyRxNatural productslcsh:R5-920MultidisciplinaryMicroscale thermophoresisKinaseChemistryCell cycleCell biology030104 developmental biology030220 oncology & carcinogenesisCancer cellOriginal ArticleCAMKK2 calcium/calmodulin-dependent protein kinase kinase 2PC Polo-box caplcsh:Medicine (General)Multipolar spindleslcsh:Q1-390Journal of Advanced Research
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PI3K inhibition reduces murine and human liver fibrogenesis in precisioncut liver slices

2019

Background: Liver fibrosis results from continuous inflammation and injury. Despite its high prevalence worldwide, no approved antifibrotic therapies exist. Omipalisib is a selective inhibitor of the PI3K/mTOR pathway that controls nutrient metabolism, growth and proliferation. It has shown antifibrotic properties in vitro. While clinical trials for idiopathic pulmonary fibrosis have been initiated, an in-depth preclinical evaluation is lacking. We evaluated omipalisib's effects on fibrogenesis using the ex vivo model of murine and human precision-cut tissue slices (PCTS).Methods: Murine and human liver and jejunum PCTS were incubated with omipalisib up to 10 mu M for 48 h. PI3K pathway act…

0301 basic medicineLiver CirrhosisMalePrecision-cut tissue slicesPROGRESSIONPharmacologyBILIARYBiochemistryPI3KGSK2126458JejunumMicePhosphatidylinositol 3-Kinases0302 clinical medicineAdenosine TriphosphateFibrosisFIBROSIShealth care economics and organizationsPhosphoinositide-3 Kinase InhibitorsSulfonamidesPyridazinesmedicine.anatomical_structureJejunumTARGET030220 oncology & carcinogenesisToxicityQuinolinesPhosphorylationmedicine.symptomATP Binding Cassette Transporter Subfamily BLiver fibrosisEARLY-ONSETInflammation03 medical and health sciencesmedicineAnimalsHumansOmipalisibProtein kinase BPI3K/AKT/mTOR pathwayPharmacologybusiness.industryCUT LIVERmedicine.diseaseMice Inbred C57BLMODEL030104 developmental biologybusinessMATRIXEx vivoBiochemical Pharmacology
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Loss of cellular FLICE-inhibitory protein promotes acute cholestatic liver injury and inflammation from bile duct ligation.

2017

Cholestatic liver injury results from impaired bile flow or metabolism and promotes hepatic inflammation and fibrogenesis. Toxic bile acids that accumulate in cholestasis induce apoptosis and contribute to early cholestatic liver injury, which is amplified by accompanying inflammation. The aim of the current study was to evaluate the role of the antiapoptotic caspase 8-homolog cellular FLICE-inhibitory (cFLIP) protein during acute cholestatic liver injury. Transgenic mice exhibiting hepatocyte-specific deletion of cFLIP (cFLIP−/−) were used for in vivo and in vitro analysis of cholestatic liver injury using bile duct ligation (BDL) and the addition of bile acids ex vivo. Loss of cFLIP in h…

0301 basic medicineLiver CirrhosisTime FactorsPhysiologyCASP8 and FADD-Like Apoptosis Regulating ProteinInflammationApoptosisp38 Mitogen-Activated Protein KinasesHepatitisBile Acids and Salts03 medical and health sciencesNecrosisCholestasisPhysiology (medical)medicineHepatic Stellate CellsAnimalsASK1Genetic Predisposition to DiseaseLigationCells CulturedTumor Necrosis Factor alpha-Induced Protein 3chemistry.chemical_classificationLiver injuryCommon Bile DuctMice KnockoutReactive oxygen speciesHepatologyBile duct ligationGastroenterologyTranscription Factor RelAmedicine.diseaseOxidative Stress030104 developmental biologyCholedocholithiasisPhenotypechemistryLiverNeutrophil InfiltrationApoptosisFLICE Inhibitory ProteinCancer researchHepatocytesCytokinesmedicine.symptomInflammation MediatorsSignal TransductionAmerican journal of physiology. Gastrointestinal and liver physiology
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