Search results for " Post-Translational"

showing 8 items of 148 documents

Posttranslational processing of human alpha 2-HS glycoprotein (human fetuin). Evidence for the production of a phosphorylated single-chain form by he…

1994

alpha 2-HS glycoprotein (alpha 2-HS) is a major protein occurring in human blood and calciferous tissues. Due to extensive sequence identity, alpha 2-HS has been grouped with the fetuins, a family of proteins that occur in fetal plasma in high concentrations. Native alpha 2-HS undergoes a series of posttranslational modifications including proteolytic processing, multiple N-glycosylations and O-glycosylations, and sulfation of the carbohydrate side chains. Various two-chain forms of alpha 2-HS have been prepared from human plasma, however, the single-chain precursor has not yet been isolated. Here, we have studied the biosynthesis of alpha 2-HS by a human hepatoma cell line, HepG2. We demon…

chemistry.chemical_classificationCarcinoma HepatocellularGlycosylationLiver NeoplasmsMolecular Sequence DataAlpha (ethology)PeptideBiologyBiochemistryFetuinSerineSulfationchemistryBiochemistryTumor Cells CulturedPhosphorylationHumansAmino Acid Sequencealpha-FetoproteinsPhosphorylationGlycoproteinPeptide sequenceProtein Processing Post-TranslationalEuropean journal of biochemistry
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C-Glycosyl amino acids through hydroboration-cross-coupling of exo-glycals and their application in automated solid-phase synthesis.

2013

O-Glycosylation is one of the most important post-translational modifications of proteins. The attachment of carbohydrates to the peptide backbone influences the conformation as well as the solubility of the conjugates and can even be essential for binding to specific ligands in cell-cell interactions or for active transport over membranes. This makes glycopeptides an interesting class of compounds for medical applications. To enhance the long-term availability of these molecules in vivo, the stabilization of the glycosidic bond between the amino acid residue and the carbohydrate is of interest. The described modular approach affords β-linked C-glycosyl amino acids by a sequence of Petasis …

chemistry.chemical_classificationGlycosylationStereochemistryOrganic ChemistryMucin-1CarbohydratesGlycopeptidesGlycosidic bondGeneral ChemistryCatalysisCoupling reactionGlycopeptideAmino acidHydroborationchemistry.chemical_compoundSolid-phase synthesischemistrySuzuki reactionHumansGlycosylAmino AcidsProtein Processing Post-TranslationalSolid-Phase Synthesis TechniquesChemistry (Weinheim an der Bergstrasse, Germany)
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Inorganic phosphate is a trigger factor for Microbispora sp. ATCC-PTA-5024 growth and NAI-107 production

2014

Background NAI-107, produced by the actinomycete Microbispora sp. ATCC-PTA-5024, is a promising lantibiotic active against Gram-positive bacteria and currently in late preclinical-phase. Lantibiotics (lanthionine-containing antibiotics) are ribosomally synthesized and post-translationally modified peptides (RiPPs), encoded by structural genes as precursor peptides. The biosynthesis of biologically active compounds is developmentally controlled and it depends upon a variety of environmental stimuli and conditions. Inorganic phosphate (Pi) usually negatively regulates biologically-active molecule production in Actinomycetes, while it has been reported to have a positive control on lantibiotic…

food.ingredientPhosphateBioengineeringBiologyApplied Microbiology and BiotechnologyPhosphatesMicrobiologychemistry.chemical_compoundfoodBacteriocinsBiosynthesisPolyphosphateHumansRibosomal Post-translationally modified Peptides (RiPPs)2. Zero hungerPhoP-PhoRResearchStructural geneBiological activityLantibioticsbiology.organism_classificationActinobacteriaRibosomal Post-translationally modified Peptides (RiPPs) Phosphate PhoP-PhoR PolyphosphateChemically defined mediumRegulonchemistryBiochemistryMicrobisporaBacteriaBiotechnology
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OGT and OGA expression in postmenopausal skeletal muscle associates with hormone replacement therapy and muscle cross-sectional area

2013

Protein glycosylation via O-linked N-acetylglucosaminylation (O-GlcNAcylation) is an important post-translational regulatory mechanism mediated by O-GlcNAc transferase (OGT) and responsive to nutrients and stress. OGT attaches an O-GlcNAc moiety to proteins, while O-GlcNAcase (OGA) catalyzes O-GlcNAc removal. In skeletal muscle of experimental animals, prolonged increase in O-GlcNAcylation associates with age and muscle atrophy. Here we examined the effects of hormone replacement therapy (HRT) and power training (PT) on muscle OGT and OGA gene expression in postmenopausal women generally prone to age-related muscle weakness. In addition, the associations of OGT and OGA gene expressions with…

medicine.medical_specialtyAgingGlycosylationTime Factorsmedicine.drug_classPlyometric ExerciseBiologyta3111N-AcetylglucosaminyltransferasesBiochemistryGene Expression Regulation EnzymologicEndocrinologyDownregulation and upregulationInternal medicineGene expressionGeneticsmedicineHumansMuscle StrengthRNA Messengerta315Muscle SkeletalMolecular BiologyFinlandGlyceraldehyde 3-phosphate dehydrogenasePlyometric power trainingEstrogen Replacement Therapyta1182Age FactorsMuscle weaknessSkeletal muscleta3141Cell BiologyMiddle Agedbeta-N-AcetylhexosaminidasesMuscle atrophyPostmenopausePhenotypeTreatment OutcomeEndocrinologymedicine.anatomical_structureEstrogenbiology.proteinFemaleMuscle atrophymedicine.symptomProtein Processing Post-TranslationalMuscle ContractionMuscle contraction
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Ethanol inhibits astroglial cell proliferation by disruption of phospholipase D-mediated signaling.

2002

The activation of phospholipase D (PLD) is a common response to mitogenic stimuli in various cell types. As PLD-mediated signaling is known to be disrupted in the presence of ethanol, we tested whether PLD is involved in the ethanol-induced inhibition of cell proliferation in rat cortical primary astrocytes. Readdition of fetal calf serum (FCS) to serum-deprived astroglial cultures caused a rapid, threefold increase of PLD activity and a strong mitogenic response; both effects were dependent on tyrosine kinases but not on protein kinase C. Ethanol (0.1-2%) suppressed the FCS-induced, PLD-mediated formation of phosphatidic acid (PA) as well as astroglial cell proliferation in a concentration…

medicine.medical_specialtyPlatelet-derived growth factorIndolestert-Butyl Alcoholmedicine.medical_treatmentButanolsBecaplerminPhosphatidic AcidsNerve Tissue ProteinsBiologyBiochemistryCulture Media Serum-FreeCellular and Molecular Neurosciencechemistry.chemical_compound1-ButanolInternal medicineLysophosphatidic acidmedicinePhospholipase DAnimalsPhosphorylationProtein kinase APlatelet-Derived Growth FactorEndothelin-1EthanolPhospholipase DCell growthGrowth factorPhosphatidic acidDNAProto-Oncogene Proteins c-sisProtein-Tyrosine KinasesGenisteinGrowth InhibitorsCell biologyRatsEndocrinologychemistryFetal Alcohol Spectrum DisordersAstrocyteslipids (amino acids peptides and proteins)Signal transductionVanadatesProtein Processing Post-TranslationalCell DivisionSignal TransductionJournal of neurochemistry
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Comprehensive analysis of interacting proteins and genome-wide location studies of the Sas3-dependent NuA3 histone acetyltransferase complex

2014

Highlights • We characterise Sas3p and Gcn5p active HAT complexes in WT and deleted TAP-strains. • We confirm that Pdp3p interacts with NuA3, histones and chromatin regulators. • Pdp3p MS-analysis reveals its phosphorylation, ubiquitination and methylation. • Sas3p can substitute Gcn5p in acetylation of histone H3K14 but not of H3K9. • Genome-wide profiling of Sas3p supports its involvement in transcriptional elongation.

nt nucleotidePTM post-translational modificationNuA3 histone acetyltransferase complexChIP-on-chip chromatin immunoprecipitation with genome-wide location arraysBiologyArticleGeneral Biochemistry Genetics and Molecular BiologyChromatin remodelingHistonesHistone H3NuA3 nucleosomal acetyltransferase of histone H3Histone H1Histone H2APdp3TAP–MS strategyHistone codelcsh:QH301-705.5TAP tandem affinity purificationGeneticsRNAPII RNA polymerase IIHistone acetyltransferaseWCE whole cell extractSAGA Spt-Ada-Gcn acetyltransferaseWT wild-typeChromatinYeastCell biologyChIP-on-chiplcsh:Biology (General)Histone methyltransferasebiology.proteinHAT histone acetyltransferaseTSS transcription start siteFEBS Open Bio
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Protein tyrosine nitration and thiol oxidation by peroxynitrite-strategies to prevent these oxidative modifications.

2013

The reaction product of nitric oxide and superoxide, peroxynitrite, is a potent biological oxidant. The most important oxidative protein modifications described for peroxynitrite are cysteine-thiol oxidation and tyrosine nitration. We have previously demonstrated that intrinsic heme-thiolate (P450)-dependent enzymatic catalysis increases the nitration of tyrosine 430 in prostacyclin synthase and results in loss of activity which contributes to endothelial dysfunction. We here report the sensitive peroxynitrite-dependent nitration of an over-expressed and partially purified human prostacyclin synthase (3.3 μM) with an EC50 value of 5 μM. Microsomal thiols in these preparations effectively co…

thiol oxidationprotein tyrosine nitrationlcsh:Chemistrychemistry.chemical_compoundCytochrome P-450 Enzyme SystemSf9 CellsTyrosinelcsh:QH301-705.5Spectroscopychemistry.chemical_classification0303 health sciencesbiologySuperoxide030302 biochemistry & molecular biologyGeneral MedicineComputer Science ApplicationsIntramolecular OxidoreductasesBiochemistryThiolprostacyclin synthasesuperoxideOxidation-ReductionPeroxynitriteOxidative phosphorylationSpodopteraCatalysisArticleperoxynitriteNitric oxideProstacyclin synthaseInorganic Chemistry03 medical and health sciencesnitric oxideddc:570NitrationPeroxynitrous AcidAnimalsHumansSulfhydryl CompoundsPhysical and Theoretical ChemistryMolecular Biology030304 developmental biologyOrganic Chemistrynitric oxide; superoxide; peroxynitrite; protein tyrosine nitration; thiol oxidation; peroxynitrite scavengers; prostacyclin synthasechemistrylcsh:Biology (General)lcsh:QD1-999biology.proteinTyrosineCattleperoxynitrite scavengersProtein Processing Post-TranslationalInternational journal of molecular sciences
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The Extracellular δ-Domain is Essential for the Formation of CD81 Tetraspanin Webs

2014

AbstractCD81 is a ubiquitously expressed member of the tetraspanin family. It forms large molecular platforms, so-called tetraspanin webs that play physiological roles in a variety of cellular functions and are involved in viral and parasite infections. We have investigated which part of the CD81 molecule is required for the formation of domains in the cell membranes of T-cells and hepatocytes. Surprisingly, we find that large CD81 platforms assemble via the short extracellular δ-domain, independent from a strong primary partner binding and from weak interactions mediated by palmitoylation. The δ-domain is also essential for the platforms to function during viral entry. We propose that, ins…

virusesLipoylationBiophysicschemical and pharmacologic phenomenaPlasma protein bindingBiologyTetraspanin 28Jurkat CellsProtein structurePalmitoylationTetraspaninViral entryExtracellularHumansComputingMilieux_MISCELLANEOUS[PHYS]Physics [physics]MembranesHep G2 Cellsbiochemical phenomena metabolism and nutritionCell biologyProtein Structure TertiaryProtein MultimerizationProtein Processing Post-TranslationalFunction (biology)CD81Protein Binding
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