Search results for "post-translational"

showing 10 items of 176 documents

Regulation of NOS expression in vascular diseases

2020

Nitric oxide synthases (NOS) are the major sources of nitric oxide (NO), a small bioactive molecule involved in the regulation of many cellular processes. One of the most prominent functions of NO is regulation of vasodilatation and thereby control of blood pressure. Most important for vascular tone is NOS3. Endothelial NOS3-generated NO diffuses into the vascular smooth muscle cells, activates the soluble guanylate cyclase resulting in enhanced cGMP concentrations and smooth muscle cell relaxation. However, more and more evidence exist that also NOS1 and NOS2 contribute to vascular function. We summarize the current knowledge about the regulation of NOS expression in the vasculature by tra…

Vascular smooth muscleNitric Oxide Synthase Type IIINOS1CellNitric Oxide Synthase Type IIBlood PressureVasodilationInflammationNitric Oxide Synthase Type INitric OxideMuscle Smooth VascularNitric oxidechemistry.chemical_compoundmedicineAnimalsHumansProtein IsoformsVascular DiseasesRNA Processing Post-TranscriptionalInflammationRegulation of gene expressionInnate immune systemAtherosclerosisImmunity InnateCell biologyGene Expression Regulation Neoplasticmedicine.anatomical_structurechemistryNitric Oxide Synthasemedicine.symptomProtein Processing Post-TranslationalFrontiers in Bioscience-Landmark
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Membrane topology and post-translational modification of the Saccharomyces cerevisiae essential protein Rot1.

2007

ROT1 is an essential gene that has been related to cell wall biosynthesis, the actin cytoskeleton and protein folding. In order to help to understand its molecular function, we carried out a characterization of the Rot1 protein. It is primarily located at the endoplasmic reticulum-nuclear membrane facing the lumen. Rot1 migrates more slowly than expected, which might suggest post-translational modification. Our results indicate that Rot1 is a protein that is neither GPI-anchored nor O-glycosylated. In contrast, it is N-glycosylated. By a directed mutagenesis of several Asn residues, we identified that the protein is simultaneously glycosylated at N103, N107 and N139. Although the mutation o…

Vesicle-associated membrane protein 8Saccharomyces cerevisiae ProteinsMolecular Sequence DataBioengineeringmacromolecular substancesSaccharomyces cerevisiaeBiologyEndoplasmic ReticulumApplied Microbiology and BiotechnologyBiochemistryProtein structureSEC62Gene Expression Regulation FungalGeneticsAmino Acid SequenceCell MembraneMembrane ProteinsActin cytoskeletonCell biologyTransport proteinProtein Structure TertiaryTransmembrane domainProtein TransportBiochemistryMembrane topologyProtein foldingProtein Processing Post-TranslationalBiotechnologyMolecular ChaperonesYeast (Chichester, England)
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Les histones déacétylases de type 2 (HD2): des régulateurs importants de l'immunité innée chez le tabac

2013

[SDV] Life Sciences [q-bio][SDE] Environmental Sciences[SDV]Life Sciences [q-bio][SDE]Environmental Sciencesnucleuspost-translational modifications[SDV.BV]Life Sciences [q-bio]/Vegetal Biology[SDV.BV] Life Sciences [q-bio]/Vegetal Biologytobacosignal transduction
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Protein S-nitrosylation: specificity and identification strategies in plants

2015

SPE Pôle IPM UB; International audience; The role of nitric oxide (NO) as a major regulator of plant physiological functions has become increasingly evident. To further improve our understanding of its role, within the last few years plant biologists have begun to embrace the exciting opportunity of investigating protein S-nitrosylation, a major reversible NO-dependent post-translational modification (PTM) targeting specific Cys residues and widely studied in animals. Thanks to the development of dedicated proteomic approaches, in particular the use of the biotin switch technique (BST) combined with mass spectrometry, hundreds of plant protein candidates for S-nitrosylation have been identi…

[SDV]Life Sciences [q-bio]Regulatornitric oxide;S-nitrosylation;post-translational modification;plant;signaling;biotin switcht echniqueplantComputational biologyReview ArticleBiologyBioinformaticsNitric Oxidelcsh:Chemistrybiotin switcht echniqueProtein S-nitrosylationpost-translational modifications[SDV.BV]Life Sciences [q-bio]/Vegetal BiologyFunctional studiesGeneral ChemistryS-NitrosylationPlantsS-nitrosylationStructure and functionChemistryBiotin switchpost-translational modificationlcsh:QD1-999Plant protein[SDE]Environmental SciencesBiotin Switch TechniqueIdentification (biology)signalingFrontiers in Chemistry
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Procollagen C-proteinase Enhancer Stimulates Procollagen Processing by Binding to the C-propeptide Region Only*

2011

Background: Procollagen C-proteinase enhancer-1 (PCPE-1) is an extracellular glycoprotein that increases activity of certain zinc metalloproteinases involved in tissue development and repair. Results: PCPE-1 binds uniquely to the C-propeptide region of the procollagen molecule. Conclusion: PCPE-1 enhances proteolysis by binding solely to the procollagen C-propeptides. Significance: These data may lead to future applications in the development of antifibrotic therapies.

animal structuresGlycosylationBiologyBiochemistryBone morphogenetic protein 1Protein Structure SecondaryBone Morphogenetic Protein 103 medical and health scienceschemistry.chemical_compoundMetalloprotease0302 clinical medicineHumansBinding siteEnhancerMolecular Biology030304 developmental biologyCell Line TransformedGlycoproteinschemistry.chemical_classification0303 health sciencesMetalloproteinaseExtracellular Matrix ProteinsBinding Sitesintegumentary systemCell BiologyEnzymatic ProcessingFibrosisExtracellular MatrixProcollagen peptidaseCollagen Type IIIchemistryBiochemistry030220 oncology & carcinogenesisembryonic structuresEnzymologyCollagenGlycoproteinProtein Processing Post-TranslationalTriple helixThe Journal of Biological Chemistry
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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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Post-Translational Regulation of Fas/CD95 in Cell Death and Survival: Role of Nitric Oxide

2010

chemistry.chemical_compoundBiochemistryPalmitoylationChemistryNitrationGeneticsMolecular MedicinePhosphorylationPost-translational regulationFas receptorBiochemistryBiotechnologyNitric oxideForum on Immunopathological Diseases and Therapeutics
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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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