Search results for "c-Raf"

showing 10 items of 21 documents

Enhanced expression of the proto-oncogenes fos and raf in the rhabdomyosarcoma cell line BA-HAN-1C after differentiation induction with retinoic acid…

1990

BA-HAN-IC is a clonal rat rhabdomyosarcoma cell line consisting of proliferating mononuclear tumor cells, some of which spontaneously fuse to form terminally differentiated post-mitotic myotubes. Exposure of BA-HAN-IC cells to retinoic acid (RA) or N-methylformamide (NMF) resulted in a significant inhibition of proliferation (p less than 0.001) and in cellular differentiation, as evidenced by a significant increase in the creatine kinase (CK) activity (p less than 0.05) and the number of terminally differentiated post-mitotic myotubes (p less than 0.001). Furthermore, between 5% (NMF) and 30% (RA) of the mononuclear tumor cells exhibited ultrastructural features of rhabdomyogenic differenti…

Cancer ResearchCellular differentiationRetinoic acidAntineoplastic AgentsTretinoinBiologychemistry.chemical_compoundTretinoinProto-Oncogene ProteinsGene expressionRhabdomyosarcomamedicineTumor Cells CulturedAnimalsRNA MessengerRNA NeoplasmRhabdomyosarcomaFormamidesmedicine.diseaseMolecular biologyRatsGene Expression Regulation NeoplasticProto-Oncogene Proteins c-rafOncologychemistryCell cultureImmunologybiology.proteinCreatine kinaseGrowth inhibitionProto-Oncogene Proteins c-fosmedicine.drugInternational journal of cancer
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Interaction of Mitogen-activated Protein Kinases with the Kinase Interaction Motif of the Tyrosine Phosphatase PTP-SL Provides Substrate Specificity …

1999

ERK1 and ERK2 associate with the tyrosine phosphatase PTP-SL through a kinase interaction motif (KIM) located in the juxtamembrane region of PTP-SL. A glutathione S-transferase (GST)-PTP-SL fusion protein containing the KIM associated with ERK1 and ERK2 as well as with p38/HOG, but not with the related JNK1 kinase or with protein kinase A or C. Accordingly, ERK2 showed in vitro substrate specificity to phosphorylate GST-PTP-SL in comparison with GST-c-Jun. Furthermore, tyrosine dephosphorylation of ERK2 by the PTP-SLDeltaKIM mutant was impaired. The in vitro association of ERK1/2 with GST-PTP-SL was highly stable; however, low concentrations of nucleotides partially dissociated the ERK1/2.P…

Cytoplasmanimal structuresProtein Kinase C-alphaRecombinant Fusion ProteinsCèl·lulesNerve Tissue ProteinsProtein tyrosine phosphataseMitogen-activated protein kinase kinaseTransfectionenvironment and public healthBiochemistrySH3 domainReceptor tyrosine kinaseMAP2K7Substrate SpecificitySerineAnimalsc-RafAmino Acid SequenceMolecular BiologyProtein Kinase CSequence DeletionMitogen-Activated Protein Kinase 1Binding SitesMitogen-Activated Protein Kinase 3biologyCyclin-dependent kinase 2Intracellular Signaling Peptides and ProteinsJNK Mitogen-Activated Protein KinasesCell BiologyCyclic AMP-Dependent Protein KinasesIsoenzymesenzymes and coenzymes (carbohydrates)KineticsBiochemistryAmino Acid SubstitutionCOS CellsCalcium-Calmodulin-Dependent Protein Kinasesbiology.proteinMutagenesis Site-DirectedCyclin-dependent kinase 9CattleMitogen-Activated Protein KinasesProtein Tyrosine PhosphatasesProteïnes
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Efficient Control of raf Gene Expression by CAP and Two Raf Repressors that Bend DNA in Opposite Directions

1999

The plasmid-borne raf operon of Escherichia coli encodes proteins involved in the uptake and utilisation of the trisaccharide raffinose. The operon is subject to dual regulation; to negative control by the binding of RafR repressor to twin operators, O1 and O2, and to positive control by the cAMP-binding protein, CAP. We have identified the CAP binding site (CBS) as a 22 bp palindromic sequence with incomplete dyad symmetry by deletion analysis, DNasel footprinting and electrophoretic mobility shift assays (EMSA) of CAP-DNA complexes. The CBS is centred 60.5 bp upstream of the transcription start point and partially overlaps O1. In vivo, CAP increases rafA (alpha-galactosidase) gene express…

DNA BacterialCyclic AMP Receptor ProteinOperonMolecular Sequence DataClinical BiochemistryRepressorCooperativityBiologyBiochemistrychemistry.chemical_compoundBacterial ProteinsGene expressionCyclic AMPBinding siteMolecular BiologyDyad symmetryPalindromic sequenceBinding SitesBase SequenceGene Expression Regulation BacterialMolecular biologyProto-Oncogene Proteins c-rafchemistryGenes BacterialNucleic Acid ConformationCarrier ProteinsDNABiological Chemistry
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Geldanamycin and its derivatives as Hsp90 inhibitors

2012

The Hsp90 molecule, one of the most abundant heat shock proteins in mammalian cells, maintains homeostasis and prevents stress-induced cellular damage. Hsp90 is expressed under normal conditions at a level of about 1-2 Percent of total proteins, while its expression increases 2-10 fold in cancer cells. The two main constitutively expressed isoforms of Hsp90 are known as Hsp90-alpha and Hsp90-beta, and their upregulation is associated with tumor progression, invasion and formation of metastases, as well as development of drug resistance. The Hsp90 is a key target for many newly established, potent anticancer agents containing Hsp90 N-terminal ATP binding inhibitors, such as geldanamycin, and…

IndolesLactams MacrocyclicCyclin-Dependent KinaseAntineoplastic AgentsTanespimycinBenzoquinoneModels BiologicalAntineoplastic Agentchemistry.chemical_compoundDownregulation and upregulationTransforming Growth Factor betaCyclin-dependent kinaseHeat shock proteinBenzoquinonespolycyclic compoundsAnimalsHumansHSP90 Heat-Shock ProteinsbiologyAnimalTriazolesGeldanamycinHsp90Cyclin-Dependent KinasesProto-Oncogene Proteins c-rafHSP90 Heat-Shock Proteinsrc-Family KinaseschemistryTumor progressionMutationCancer cellbiology.proteinCancer researchMacrolidesMacrolideTriazoleTumor Suppressor Protein p53Animals; Antineoplastic Agents; Benzoquinones; Cyclin-Dependent Kinases; HSP90 Heat-Shock Proteins; Humans; Lactams Macrocyclic; Macrolides; Models Biological; Mutation; Novobiocin; Proto-Oncogene Proteins c-raf; Transforming Growth Factor beta; Triazoles; Tumor Suppressor Protein p53; src-Family KinasesNovobiocinHumanFrontiers in Bioscience
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β1D Integrin Inhibits Cell Cycle Progression in Normal Myoblasts and Fibroblasts

1998

Integrins are alphabeta heterodimeric transmembrane receptors involved in the regulation of cell growth and differentiation. The beta1 integrin subunit is widely expressed in vivo and is represented by four alternatively spliced cytoplasmic domain isoforms. beta1D is a muscle-specific variant of beta1 integrin and a predominant beta1 isoform in striated muscles. In the present study we showed that expression of the exogenous beta1D integrin in C2C12 myoblasts and NIH 3T3 or REF 52 fibroblasts inhibited cell proliferation. Unlike the case of the common beta1A isoform, adhesion of beta1D-transfected C2C12 myoblasts specifically via the expressed integrin did not activate mitogen-activated pro…

IntegrinsRecombinant Fusion ProteinsMolecular Sequence DataIntegrinSignal transductionTransfectionCell adhesion; Integrins; Signal transduction; Alternative splicing isoforms; Cell proliferation; MyodifferentiationBiochemistryCD49cCell LineCollagen receptorMiceAlternative splicing isoformsCell surface receptorAnimalsAmino Acid SequenceMuscle SkeletalMolecular BiologyCell proliferationMyodifferentiationbiologyCell growthIntegrin beta1Cell CycleCell adhesionCell DifferentiationReceptors Interleukin-2Cell BiologyImmunohistochemistryMolecular biologyCell biologyEnzyme ActivationProto-Oncogene Proteins c-rafAlternative SplicingGenes rasIntegrin alpha MCalcium-Calmodulin-Dependent Protein Kinasesbiology.proteinIntegrin beta 6C2C12Journal of Biological Chemistry
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Quantification of the Raf-C1 Interaction With Solid-Supported Bilayers

2002

By use of the quartz crystal microbalance technique, the interaction of the Raf-Ras binding domain (RafRBD) and the cysteine-rich domain Raf-C1 with lipids was quantified by using solid-supported bilayers immobilized on gold electrodes deposited on 5 MHz quartz plates. Solid-supported lipid bilayers were composed of an initial octanethiol monolayer chemisorbed on gold and a physisorbed phospholipid monolayer varying in its lipid composition as the outermost layer. The integrity of bilayer preparation was monitored by impedance spectroscopy. For binding experiments, a protein construct comprising the RafRBD and Raf-C1 linked to the maltose binding protein and a His tag, termed MBP-Raf-C1, wa…

Lipid BilayersPhospholipidBiosensing TechniquesMicroscopy Atomic ForceBiochemistrychemistry.chemical_compoundMonolayerLipid bilayerMolecular BiologyBilayerOrganic ChemistryUnithiolQuartz crystal microbalanceProtein Structure TertiaryProto-Oncogene Proteins c-rafDissociation constantCrystallographychemistryThermodynamicsMolecular Medicinelipids (amino acids peptides and proteins)AdsorptionGoldDimyristoylphosphatidylcholineProtein adsorptionBinding domainChemBioChem
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Tumor Necrosis Factor (TNF) Receptor 1 Signaling Downstream of TNF Receptor-associated Factor 2

1997

Like other members of the tumor necrosis factor (TNF) receptor family, p55 TNF receptor 1 (TNF-R1) lacks intrinsic signaling capacity and transduces signals by recruiting associating molecules. The TNF-R1 associated death domain protein interacts with the p55 TNF-R1 cytoplasmic domain and recruits the Fas-associated death domain protein (which directly activates the apoptotic proteases), the protein kinase receptor interacting protein, and TNF receptor-associated factor 2 (TRAF2). TRAF2 has previously been demonstrated to activate both transcription factor nuclear factor kappaB (NFkappaB) and the c-Jun N-terminal kinase/stress-activated protein kinase (JNK/SAPK) pathway, which in turn stimu…

MAP kinase kinase kinasebiologyChemistryCyclin-dependent kinase 2Cell BiologyMitogen-activated protein kinase kinaseBiochemistryProtein kinase RMAP2K7Cancer researchbiology.proteinCyclin-dependent kinase 9ASK1c-RafMolecular BiologyJournal of Biological Chemistry
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Synthesis and biological evaluation of cycloalkylidene carboxylic acids as novel effectors of Ras/Raf interaction.

2002

The protooncogenes Ras and Raf play important roles in signal transduction pathways regulated by mitogen-activated protein kinases. Mutations of Ras that arrest the protein in its active state are frequently implicated in tumor formation. We used Ras and Raf proteins in the yeast two-hybrid system to search for natural or synthesized substances capable of modulating Ras/Raf interaction by specifically binding to one of the interacting partners. We found that cycloalkylidene carboxylic acids enhanced Ras/Raf interaction by acting on the cysteine-rich domain of Raf. Several analogues of the active substance 2-cyclohexylidene propanoic acid were synthesized and the importance of the semicyclic…

MAPK/ERK pathwayMagnetic Resonance SpectroscopyCarboxylic acidSaccharomyces cerevisiaeAmino Acid MotifsCarboxylic AcidsAnti-apoptotic Ras signalling cascadeTwo-Hybrid System TechniquesDrug DiscoveryHumansHRASProtein kinase Achemistry.chemical_classificationbiologyChemistryKinasebiology.organism_classificationProtein Structure TertiaryProto-Oncogene Proteins c-rafBiochemistryModels ChemicalMutationMutagenesis Site-Directedras ProteinsMolecular MedicineSignal transductionPlasmidsProtein BindingJournal of medicinal chemistry
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Dimerization of the kinase ARAF promotes MAPK pathway activation and cell migration.

2014

The RAF family of kinases mediates RAS signaling, and RAF inhibitors can be effective for treating tumors with BRAF V600E mutant protein. However, RAF inhibitors paradoxically accelerate metastasis in RAS -mutant tumors and become ineffective in BRAF V600E tumors because of reactivation of downstream mitogen-activated protein kinase (MAPK) signaling. We found that the RAF isoform ARAF has an obligatory role in promoting MAPK activity and cell migration in a cell type–dependent manner. Knocking down ARAF prevented the activation of MAPK kinase 1 (MEK1) and extracellular signal–regulated kinase 1 and 2 (ERK1/2) and decreased the number of protrusions from tumor cell spheroids in three-dimensi…

MAPK/ERK pathwayScaffold proteinModels MolecularNiacinamideProto-Oncogene Proteins B-rafMAP Kinase Signaling SystemBlotting WesternMAP Kinase Kinase 1MAPK cascadeBiologyKSR1BiochemistryBinding CompetitiveProto-Oncogene Proteins A-rafTime-Lapse ImagingMutant proteinCell MovementTumor Cells CulturedHumansNeoplasm InvasivenessRNA Small InterferingProtein kinase AMolecular BiologyAnalysis of VarianceKinasePhenylurea CompoundsCell BiologySorafenibCell biologyEnzyme ActivationProto-Oncogene Proteins c-rafHEK293 CellsIndenesGene Knockdown TechniquesCancer researchPyrazolesElectrophoresis Polyacrylamide GelARAFDimerizationScience signaling
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Studies on protein kinases involved in regulation of nucleocytoplasmic mRNA transport

1988

The rate of energy-dependent nucleoside triphosphatase (NTPase)-mediated nucleocytoplasmic translocation of poly(A)-containing mRNA [poly(A)+mRNA] across the nuclear envelope is thought to be regulated by poly(A)-sensitive phosphorylation and dephosphorylation of nuclear-envelope protein. Studying the phosphorylation-related inhibition of the NTPase, we found that phosphorylation of one polypeptide of rat liver envelopes by endogenous NI- and NII-like protein kinase was particularly sensitive to poly(A). This polypeptide (106 kDa) was also phosphorylated by nuclear-envelope-bound Ca2+-activated and phospholipid-dependent protein kinase (protein kinase C). Activation of kinase C by tumour-pr…

MaleCytoplasmNuclear EnvelopeMitogen-activated protein kinase kinasePhosphatidylinositolsBiochemistryMAP2K7AnimalsRNA Messengerc-RafProtein kinase AMolecular BiologyProtein Kinase CProtein kinase CCell NucleusMembrane GlycoproteinsMAP kinase kinase kinasebiologyCyclin-dependent kinase 2Membrane ProteinsNuclear ProteinsBiological TransportRats Inbred StrainsCell BiologyMolecular biologyRatsNuclear Pore Complex ProteinsMicroscopy ElectronLiverBiochemistrybiology.proteinCyclin-dependent kinase 9PeptidesPoly AResearch ArticleBiochemical Journal
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