Search results for "Translational"

showing 10 items of 418 documents

Modification of antigen-encoding RNA increases stability, translational efficacy, and T-cell stimulatory capacity of dendritic cells.

2006

AbstractAdoptive transfer of dendritic cells (DCs) transfected with in vitro–transcribed, RNA-encoding, tumor-associated antigens has recently entered clinical testing as a promising approach for cancer immunotherapy. However, pharmacokinetic exploration of RNA as a potential drug compound and a key aspect of clinical development is still pending. While investigating the impact of different structural modifications of RNA molecules on the kinetics of the encoded protein in DCs, we identified components located 3′ of the coding region that contributed to a higher transcript stability and translational efficiency. With the use of quantitative reverse transcription–polymerase chain reaction (R…

Untranslated regionCD4-Positive T-LymphocytesMaleTranslational efficiencyT cellRNA StabilityImmunologyAntigen presentationBiologyCD8-Positive T-LymphocytesLymphocyte ActivationTransfectionBiochemistryCancer VaccinesImmunotherapy AdoptiveMiceAntigens NeoplasmNeoplasmsmedicineCoding regionAnimalsHumansRNA NeoplasmAntigen-presenting cellCells CulturedAntigen PresentationRNACell BiologyHematologyDendritic cellDendritic CellsVirologyCoculture TechniquesCell biologymedicine.anatomical_structurePoly ABlood
researchProduct

P3‐335: Upstream of N‐ras (UNR) is involved in translational control of ADAM10 protein expression

2008

Background: The amyloid beta peptide (A ) is derived by proteolytic processing of the amyloid precursor protein (APP) by the beta-secretase BACE1 and gamma-secretase. In contrast to this amyloidogenic processing, APP is predominantly cleaved by the alpha-secretase within the A domain and this precludes the formation of A . We and other research groups could show that BACE1 protein expression is regulated by the 5’untranslated region (UTR) of the BACE1 mRNA, however little is known about the regulation of alpha-secretase. Similar to the 5’UTR of BACE1, the 5’UTR of ADAM10 consists of 444 nucleotides with a GC-content of 70% and two upstream open reading frames. We hypothesize that ADAM10, th…

Untranslated regionMessenger RNAbiologyEpidemiologyChemistryHealth PolicyADAM10RNA-binding proteinDNA-binding proteinCell biologyPsychiatry and Mental healthCellular and Molecular NeuroscienceDevelopmental NeuroscienceTranslational regulationAmyloid precursor proteinbiology.proteinNeurology (clinical)Geriatrics and GerontologyBinding siteAlzheimer's & Dementia
researchProduct

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
researchProduct

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)
researchProduct

Biophotonics in veterinary medicine: the first steps toward clinical translation

2019

In this paper, we analyzed the current situation and the potential of biophotonics and biomedical optics in veterinary medicine. Promising optical techniques such as optical coherence tomography, pulse oximeter, and hyperspectral imaging have been clinically translated into human medicine. But even though human and small animal medicine share personalized and state-of-the-art approach, biophotonics remains rarely exploited in the canine and feline medicine. However, there are some biophotonics studies in veterinary oncology which addressed tumor diagnosis (skin and subcutaneous tumors), prognosis (lymphoma), and therapy (clear surgical margins). Visible and near-infrared spectroscopy served…

Veterinary medicineclinical translationaldogs040301 veterinary sciencespulse oximeterAspiration procedureVeterinary oncology01 natural sciences010309 optics0403 veterinary scienceSmall animal0103 physical sciencesOrthopedic problemsHuman medicineMedicineoptical coherence tomographybusiness.industrysmall animalsbiophotonics04 agricultural and veterinary sciences3. Good healthBiophotonicsbiomedical opticsveterinary medicine:NATURAL SCIENCES::Physics::Atomic and molecular physics [Research Subject Categories]business
researchProduct

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
researchProduct

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
researchProduct

Post-translational Modifications in Plant Nuclear Signaling: Novel Insights Into Responses to Environmental Changes

2019

Just imagine a Plant Science professor in front of a classroom full of interested and attentive students. Imagine what their answers to this intriguing question would be: “What are, according to you, the functions ensured by the plant cell nucleus?” It would be very surprising if some of them would answer cell signaling in response to biotic and abiotic stresses or developmental processes. Most of them would probably answer according to a classical point of view: DNA replication or gene expression. Hence it is still admitted in recent publications (see for instance Fedorenko et al., 2010) that molecules smaller than 40 kDa can diffuse freely across the nuclear envelope pores. However, Pauly…

[SDV]Life Sciences [q-bio]SUMO proteinPlant Sciencelcsh:Plant culture03 medical and health sciences0404 agricultural biotechnologynucleus;post-translation modification (PTM);phosphorylation;acetylation;SUMOylationpost-translation modification (PTM)medicine[SDV.BV]Life Sciences [q-bio]/Vegetal Biologylcsh:SB1-1110030304 developmental biologyacetylation0303 health sciencesChemistryphosphorylationnucleus04 agricultural and veterinary sciences040401 food scienceSUMOylationCell biologymedicine.anatomical_structureEditorialAcetylation[SDE]Environmental SciencesPosttranslational modificationPhosphorylationAcetylation ; Nucleus ; Phosphorylation ; Post-translation Modification (ptm) ; SumoylationNucleusFrontiers in Plant Science
researchProduct

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
researchProduct

Editorial: Physiology and Pathophysiology of Heat Shock Protein 60

2020

business.industrypost translational modificationshepatocellular carcinomaacquired chaperonopathieBioinformaticsHsp60Biochemistry Genetics and Molecular Biology (miscellaneous)BiochemistryPathophysiologypost translational modificationlcsh:Biology (General)cardiovascular diseasegenetic chaperonopathieHeat shock proteinPosttranslational modificationMedicineHSP60acquired chaperonopathiesbusinessgenetic chaperonopathieslcsh:QH301-705.5Molecular Biologychaperonotherapy
researchProduct