Search results for " Post-Translational"

showing 10 items of 148 documents

α-Secretase Activity of the Disintegrin Metalloprotease ADAM 10: Influences of Domain Structure

2001

Disintegrin metalloproteases from different organisms form the ADAM (a disintegrin and metalloprotease) family. All members display a common domain organization and possess four potential functions: proteolysis, cell adhesion, cell fusion, and cell signaling. Members of the ADAM family are responsible for the proteolytic cleavage of transmembrane proteins and release of their extracellular domain. The proteolytic process is referred to as ectodomain shedding, which is activated by phorbol esters and inhibited by hydroxamic acid-based inhibitors. We have shown that the disintegrin metalloprotease ADAM 10 has both constitutive and regulated alpha-secretase activity. Expression of a dominant n…

Cell signalingDisintegrinsMolecular Sequence DataProtein domainBiologyGeneral Biochemistry Genetics and Molecular BiologyADAM10 ProteinAmyloid beta-Protein PrecursorHistory and Philosophy of ScienceEndopeptidasesDisintegrinAnimalsAspartic Acid EndopeptidasesHumansProtease InhibitorsAmino Acid SequenceCell adhesionMetalloproteinaseGeneral NeuroscienceHEK 293 cellsMembrane ProteinsMetalloendopeptidasesRecombinant ProteinsTransmembrane proteincarbohydrates (lipids)ADAM ProteinsBiochemistryEctodomainbiology.proteinAmyloid Precursor Protein SecretasesProtein Processing Post-TranslationalAnnals of the New York Academy of Sciences
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Subcellular targeting of multiligand-binding protein gC1qR.

1999

Abstract gC1q receptor, a protein originally described as the cell surface receptor for the globular heads of complement factor C1q, has been found to bind human H-kininogen with high affinity and specificity. Therefore, gC1qR has been considered candidate kininogen docking site on the surfaces of platelets, neutrophils and endothelial cells. Recent work demonstrating that gC1qR is an intracellular protein that is tightly associated with mitochondria rather than targeted to the cell surface has challenged this view. To further probe cellular trafficking routes of gC1qR, we overexpressed human gC1qR in a mammalian cell and monitored cell surface exposure of recombinant gC1qR by virtue of its…

CellComplement factor IBiologyLigandsMitochondrial ProteinsCell surface receptormedicineAnimalsHumansBinding siteReceptorPharmacologyBinding SitesMembrane GlycoproteinsBinding proteinComplement C1qBiological TransportTransfectionMolecular biologyCell biologyReceptors Complementmedicine.anatomical_structureHyaluronan ReceptorsCell cultureCOS CellsCarrier ProteinsProtein Processing Post-Translationalcirculatory and respiratory physiologySubcellular FractionsImmunopharmacology
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Chromatin dynamics of the developmentally regulated P. lividus neural alpha tubulin gene

2011

Over 40 years ago, Allfrey and colleagues (1964) suggested that two histone modifications, namely acetylation and methylation, might regulate RNA synthesis. Nowadays it is universally accepted that activation of gene expression strictly depends on enzymatic mechanisms able to dynamically modify chromatin structure. Here, using techniques including DNaseI hypersensitive site analysis, chomatin immunoprecipitation and quantitative PCR analysis, we have analyzed the dynamics of histone post-translation modifications involved in developmentally/spatially controlled activation of the sea urchin PlTalpha2 tubulin gene. We have demonstrated that only when the PlTalpha2 core promoter chromatin is a…

Chromatin ImmunoprecipitationEmbryologyRNA polymerase IISettore BIO/11 - Biologia MolecolareMethylationNervous SystemHistone DeacetylasesHistonesTubulinGene expressionAnimalsParacentrotus lividus chromatin modification epigenetic reprogramming nervous systemPromoter Regions GeneticHistone AcetyltransferasesEpigenomicsHistone DemethylasesbiologyGene Expression Regulation DevelopmentalAcetylationPromoterHistone-Lysine N-MethyltransferaseMolecular biologyChromatinChromatinCell biologyHistoneAcetylationHistone MethyltransferasesParacentrotusbiology.proteinRNA Polymerase IIProtein Processing Post-TranslationalHypersensitive siteDevelopmental Biology
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Substrate determinants for cleavage in cis and in trans by the hepatitis C virus NS3 proteinase

1995

Processing of the hepatitis C virus polyprotein is accomplished by a series of cotranslational and posttranslational cleavages mediated by host cell signalases and two virally encoded proteinases. Of these the NS3 proteinase is essential for processing at the NS3/4A, NS4A/4B, NS4B/5A, and NS5A/5B junctions. Processing between NS3 and NS4A occurs in cis, implying an intramolecular reaction mechanism, whereas cleavage at the other sites can also be mediated in trans. Sequence analysis of the amino termini of mature cleavage products and comparisons of amino acid residues around the scissile bonds of various hepatitis C virus isolates identified amino acid residues which might contribute to su…

Cleavage factorvirusesMolecular Sequence DataImmunologyHepacivirusCleavage and polyadenylation specificity factorViral Nonstructural ProteinsBiologyCleavage (embryo)MicrobiologySubstrate SpecificityScissile bondVirologyHumansAmino Acid SequenceAmino AcidsPeptide sequencechemistry.chemical_classificationNS3Cleavage stimulation factorHydrolysisSerine Endopeptidasesbiochemical phenomena metabolism and nutritionAmino acidchemistryBiochemistryMutagenesisInsect ScienceProtein Processing Post-TranslationalRNA HelicasesHeLa CellsResearch ArticleJournal of Virology
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Post-Translational Regulation of CYP450s Metabolism As Revealed by All-Atoms Simulations of the Aromatase Enzyme.

2019

Phosphorylation by kinases enzymes is a widespread regulatory mechanism able of rapidly altering the function of target proteins. Among these are cytochrome P450s (CYP450), a superfamily of enzymes performing the oxidation of endogenous and exogenous substrates thanks to the electron supply of a redox partner. In spite of its pivotal role, the molecular mechanism by which phosphorylation modulates CYP450s metabolism remains elusive. Here by performing microsecond-long all-atom molecular dynamics simulations, we disclose how phosphorylation regulates estrogen biosynthesis, catalyzed by the Human Aromatase (HA) enzyme. Namely, we unprecedentedly propose that HA phosphorylation at Y361 markedl…

CytochromeFlavin MononucleotideProtein ConformationGeneral Chemical EngineeringFlavin mononucleotide-Oxidative phosphorylationLibrary and Information SciencesMolecular Dynamics Simulation01 natural scienceschemistry.chemical_compoundAromatase0103 physical sciencesPost-translational regulationAromatasePhosphorylationBinding Sites010304 chemical physicsbiologyKinaseGeneral ChemistryMetabolism0104 chemical sciencesComputer Science ApplicationsCell biology010404 medicinal & biomolecular chemistrychemistrySettore CHIM/03 - Chimica Generale E Inorganicabiology.proteinFlavin-Adenine DinucleotidePhosphorylationQuantum TheoryProtein Processing Post-TranslationalNADPJournal of chemical information and modeling
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The La antigen shuttles between the nucleus and the cytoplasm in CV-1 cells

1989

Recently we established a monoclonal antibody against the La-protein (Bachmann et al., Proc. Natl. Acad. Sci. USA, 83, 7770, 1986). The antibody gives a nuclear speckled type staining and, in addition, a perinuclear cytoplasmic staining on cultured cells in immunofluorescence microscopy. After inhibition of RNA synthesis the La-protein is transported into the cytoplasm. After prolonged inhibition it returns into the nucleus forming large growing speckles. The transport into the nucleus apparently depends on glycosylation.

CytoplasmGlycosylationmedicine.drug_classClinical BiochemistryFluorescent Antibody TechniqueMonoclonal antibodyAutoantigensCell Linechemistry.chemical_compoundmedicineAnimalsMolecular BiologyCell NucleusbiologyAutoantibodyAntibodies MonoclonalCell BiologyGeneral MedicineMolecular biologyStainingMolecular Weightmedicine.anatomical_structureRibonucleoproteinschemistryCytoplasmNucleocytoplasmic Transportbiology.proteinAntibodyProtein Processing Post-TranslationalNucleusTranscription FactorsMolecular and Cellular Biochemistry
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Low frequency of cytotoxic liver-infiltrating T lymphocytes specific for endogenous processed surface and core proteins in chronic hepatitis B.

1993

To investigate the role of hepatitis B virus (HBV)-specific CD8+ T cells in chronic hepatitis B, the lytic activity of peripheral blood mononuclear cells (PBMC) and liver-infiltrating T cell clones and cytotoxic T cell (CTL) lines stimulated by recombinant vaccinia virus-infected cells were analyzed. Autologous and allogeneic Epstein-Barr virus-transformed B cells infected with vaccinia vectors (VAC) that contain sequences of the surface (S), secretory core (E), cytoplasmatic core (C) VAC antigen of HBV, or the wild-type (WT) VAC served as target cells. ELISA and immunoblotting showed HBV antigen expression in infected cells. Neither PBMC nor C- or E-VAC-stimulated CTL lines showed specific…

Cytotoxicity ImmunologicHerpesvirus 4 HumanT cellGenes MHC Class IVaccinia virusBiologymedicine.disease_causeHepatitis B AntigensAntigenCell MovementmedicineImmunology and AllergyCytotoxic T cellHumansHepatitis B e AntigensHepatitis ChronicHepatitis B virusHepatitisB-LymphocytesHepatitis B Surface AntigensHepatitis Bmedicine.diseasebiology.organism_classificationCell Transformation ViralHepatitis BVirologyHepatitis B Core AntigensRecombinant ProteinsCTL*Infectious Diseasesmedicine.anatomical_structureHepadnaviridaeLiverProtein Processing Post-TranslationalT-Lymphocytes CytotoxicThe Journal of infectious diseases
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Role of glutathione in cell nucleus

2010

Cells with high proliferation rate have high glutathione levels. This typical feature of cancer cells is viewed usually as a defence mechanism against ionizing radiation or chemotherapy. Efforts have been made in order to decrease cellular glutathione levels in tumours as a necessary pre-treatment for cancer therapy. However, very few reports have considered cellular glutathione as a physiological tool for cells to proliferate and that most of this high glutathione levels were located in the nucleus. The role of nuclear glutathione in cell physiology has become more important in the last years. This review summarizes new findings that point to the nuclear reduced status as an environment th…

DNA RepairDNA repairBiochemistryHistonesProtein Carbonylationchemistry.chemical_compoundHeterochromatinmedicineAnimalsHumansNuclear proteinTelomeraseCell NucleusbiologyCell CycleNuclear ProteinsDNAGeneral MedicineGlutathioneCell cycleGlutathioneChromatinCell biologyHistonemedicine.anatomical_structurechemistryCancer cellbiology.proteinOxidation-ReductionProtein Processing Post-TranslationalNucleusFree Radical Research
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Late activation of stress kinases (SAPK/JNK) by genotoxins requires the DNA repair proteins DNA-PKcs and CSB.

2005

Although genotoxic agents are powerful inducers of stress kinases (SAPK/JNK), the contribution of DNA damage itself to this response is unknown. Therefore, SAPK/JNK activation of cells harboring specific defects in DNA damage-recognition mechanisms was studied. Dual phosphorylation of SAPK/JNK by the genotoxin methyl methanesulfonate (MMS) occurred in two waves. The early response (≤2 h after exposure) was similar in cells knockout for ATM, PARP, p53, and CSB or defective in DNA-PKcscompared with wild-type cells. The late response however (≥4 h), was drastically reduced in DNA-PKcsand Cockayne's syndrome B (CSB)-deficient cells. Similar results were obtained with human cells lacking DNA-PKc…

DNA ReplicationAlkylationDNA RepairDNA damageDNA repairPoly ADP ribose polymeraseDNA-Activated Protein KinaseBiologyModels Biologicalchemistry.chemical_compoundMiceAnimalsHumansPhosphorylationPoly-ADP-Ribose Binding ProteinsMolecular BiologyDNA-PKcsCells CulturedKinaseDNA HelicasesJNK Mitogen-Activated Protein KinasesNuclear ProteinsCell BiologyBase excision repairDNAArticlesMethyl MethanesulfonateMolecular biologyMethyl methanesulfonateDNA-Binding ProteinsEnzyme Activationenzymes and coenzymes (carbohydrates)DNA Repair EnzymeschemistryPhosphorylationProtein Processing Post-TranslationalDNA DamageMutagensSignal TransductionMolecular biology of the cell
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The bacterial cytolethal distending toxin (CDT) triggers a G2 cell cycle checkpoint in mammalian cells without preliminary induction of DNA strand br…

1999

The bacterial cytolethal distending toxin (CDT) was previously shown to arrest the tumor-derived HeLa cell line in the G2-phase of the cell cycle through inactivation of CDK1, a cyclin-dependent kinase whose state of activation determines entry into mitosis. We have analysed the effects induced in HeLa cells by CDT, in comparison to those induced by etoposide, a prototype anti-tumoral agent that triggers a G2 cell cycle checkpoint by inducing DNA damage. Both CDT and etoposide inhibit cell proliferation and induces the formation of enlarged mononucleated cells blocked in G2. In both cases, CDK1 from arrested cells could be re-activated both in vitro by dephosphorylation by recombinant Cdc25…

DNA ReplicationG2 PhaseCancer ResearchCAFFEINECell cycle checkpointCytolethal distending toxinDNA damageRecombinant Fusion Proteins[SDV]Life Sciences [q-bio]Bacterial ToxinsBiologyS Phase03 medical and health sciencesCDC2 Protein KinaseGeneticsHumanscdc25 PhosphatasesCHEK1PhosphorylationMolecular BiologyMitosisEtoposide030304 developmental biology0303 health sciences030306 microbiologyCell growthDNA NeoplasmG2-M DNA damage checkpointCell cycleAntineoplastic Agents PhytogenicNeoplasm Proteins3. Good healthCell biology[SDV] Life Sciences [q-bio]BiochemistryAGENT ANTITUMEURProtein Processing Post-TranslationalCell DivisionDNA DamageHeLa Cells
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