Search results for "Tandem"

showing 10 items of 560 documents

Metaproteomic analysis of atmospheric aerosol samples.

2016

Metaproteomic analysis of air particulate matter provides information about the abundance and properties of bioaerosols in the atmosphere and their influence on climate and public health. We developed and applied efficient methods for the extraction and analysis of proteins from glass fiber filter samples of total, coarse, and fine particulate matter. Size exclusion chromatography was applied to remove matrix components, and sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) was applied for protein fractionation according to molecular size, followed by in-gel digestion and LC-MS/MS analysis of peptides using a hybrid Quadrupole-Orbitrap MS. Maxquant software and the Swiss-…

Proteomics010504 meteorology & atmospheric sciencesSize-exclusion chromatographyIndoor bioaerosolFractionation010501 environmental sciences01 natural sciencesBiochemistryAnalytical ChemistryMatrix (chemical analysis)Fungal ProteinsBacterial ProteinsMetaproteomicsTandem Mass SpectrometryDatabases ProteinChromatography High Pressure Liquid0105 earth and related environmental sciencesPlant ProteinsAerosolsFungal proteinAir PollutantsChromatographyMass spectrometryChemistryAtmosphereProteinsParticulatesAllergensAtmospheric aerosolsAerosolEnvironmental chemistryBioanalytical methodsParticleElectrophoresis Polyacrylamide GelParticulate MatterHPLCResearch PaperAnalytical and bioanalytical chemistry
researchProduct

Fumarate dependent protein composition under aerobic and anaerobic growth conditions in Escherichia coli

2020

Abstract In the absence of sugars, C4-dicarboxylates (C4DC) like fumarate represent important substrates for growth of Escherichia coli. Aerobically, C4DCs are oxidized to CO2 whereas anaerobically, C4DCs are used for fumarate respiration. In order to determine the impact of fumarate under aerobic and anaerobic conditions, proteomes of E. coli W3110 grown aerobically or anaerobically with fumarate and/or the non-C4DC substrate glycerol were comparatively profiled by nanoLC-MS/MS. Membrane enrichment allowed sensitive detection of membrane proteins. A total of 1657 proteins of which 646 and 374 were assigned to the cytosol or membrane, respectively, were covered. Presence of fumarate trigger…

Proteomics0301 basic medicineBiophysicsCatabolite repressionmedicine.disease_causeBiochemistryCarbon utilization03 medical and health sciencesFumaratesTandem Mass SpectrometryEscherichia colimedicineDicarboxylic AcidsAnaerobiosisEscherichia coli030102 biochemistry & molecular biologybiologyChemistryEscherichia coli ProteinsGene Expression Regulation BacterialAerobiosisDNA-Binding ProteinsCitric acid cycle030104 developmental biologyRegulonMembrane proteinBiochemistrycAMP receptor proteinbiology.proteinProtein KinasesAnaerobic exerciseTranscription FactorsJournal of Proteomics
researchProduct

Versatile, sensitive liquid chromatography mass spectrometry – Implementation of 10 μm OT columns suitable for small molecules, peptides and proteins

2016

AbstractWe have designed a versatile and sensitive liquid chromatographic (LC) system, featuring a monolithic trap column and a very narrow (10 μm ID) fused silica open tubular liquid chromatography (OTLC) separation column functionalized with C18-groups, for separating a wide range of molecules (from small metabolites to intact proteins). Compared to today’s capillary/nanoLC approaches, our system provides significantly enhanced sensitivity (up to several orders) with matching or improved separation efficiency, and highly repeatable chromatographic performance. The chemical properties of the trap column and the analytical column were fine-tuned to obtain practical sample loading capacities…

Proteomics0301 basic medicineCapillary actionBreast NeoplasmsExosomesOrbitrapProteomicsMass spectrometrySensitivity and Specificity01 natural sciencesArticlelaw.inventionMice03 medical and health sciencesAxin ProteinTandem Mass SpectrometrylawLiquid chromatography–mass spectrometryAnimalsHumansMoleculeDetection limitMultidisciplinaryChromatographyChemistry010401 analytical chemistryReproducibility of ResultsSmall moleculeHydroxycholesterols0104 chemical sciences030104 developmental biologyFemalePeptidesChromatography LiquidScientific Reports
researchProduct

Toward the Standardization of Mitochondrial Proteomics: The Italian Mitochondrial Human Proteome Project Initiative

2017

The Mitochondrial Human Proteome Project aims at understanding the function of the mitochondrial proteome and its crosstalk with the proteome of other organelles. Being able to choose a suitable and validated enrichment protocol of functional mitochondria, based on the specific needs of the downstream proteomics analysis, would greatly help the researchers in the field. Mitochondrial fractions from ten model cell lines were prepared using three enrichment protocols and analyzed on seven different LC-MS/MS platforms. All data were processed using neXtProt as reference database. The data are available for the Human Proteome Project purposes through the ProteomeXchange Consortium with the iden…

Proteomics0301 basic medicineProteomeStandardizationComputational biologyBiologyMitochondrionProteomicsBioinformaticsBiochemistryenrichment protocol; mitochondria; Mitochondrial Human Proteome Project; standardization;Cell LineMitochondrial Proteins03 medical and health sciences0302 clinical medicineTandem Mass SpectrometryHuman proteome projectHumansProtein Interaction MapsSettore BIO/10 - BIOCHIMICAMitochondrial proteinstandardizationChromatographyLiquidNeXtProtChemistry (all)General Chemistrymitochondria030104 developmental biologyItalyenrichment protocolProteomeReference databaseMitochondrial Human Proteome Projectenrichment protocol; mitochondria; Mitochondrial Human Proteome Project; standardization; Cell Line; Chromatography Liquid; Humans; Italy; Mitochondria; Mitochondrial Proteins; Protein Interaction Maps; Proteome; Proteomics; Tandem Mass Spectrometry; Biochemistry; Chemistry (all)030217 neurology & neurosurgeryChromatography Liquid
researchProduct

Proteomic characterization of the mucosal pellicle formed in vitro on a cellular model of oral epithelium

2020

The oral mucosal pellicle is a thin lubricating layer generated by the binding of saliva proteins on epithelial oral cells. The protein composition of this biological structure has been to date studied by targeted analyses of specific salivary proteins. In order to perform a more exhaustive proteome characterization of pellicles, we used TR146 cells expressing or not the transmembrane mucin MUC1 and generated pellicles by incubation with human saliva and washing to remove unbound proteins. A suitable method was established for the in vitro isolation of the mucosal pellicle by "shaving" it from the cells using trypsin. The extracts, the washing solutions and the saliva used to constitute the…

Proteomics0301 basic medicineSalivaTR146/MUC1 cells[SDV]Life Sciences [q-bio]BiophysicsPluncBiochemistryEpithelium03 medical and health sciencesTandem Mass SpectrometrymedicineHumansDental PellicleSalivary Proteins and PeptidesSalivaproteomicMUC1Mucosal pellicle030102 biochemistry & molecular biologyChemistryMucinTrypsinIn vitroTransmembrane proteinCellular model of oral mucosa030104 developmental biologyBiochemistryProteome[SDV.AEN]Life Sciences [q-bio]/Food and Nutritionmedicine.drugJournal of Proteomics
researchProduct

Comparative Quantitative Analysis of Porcine Optic Nerve Head and Retina Subproteomes

2019

Optic nerve head (ONH) and retina (RET) are the main sites of damage in neurodegenerative optic neuropathies including glaucoma. Up to date, little is known about the molecular interplay between these two adjoining ocular components in terms of proteomics. To close this gap, we investigated ONH and RET protein extracts derived from porcine eyes (n = 12) (Sus scrofa domestica Linnaeus 1758) using semi-quantitative mass spectrometry (MS)-based proteomics comprising bottom-up LC&ndash

Proteomics0301 basic medicineretinaProteomegenetic structuresSus scrofaGlaucomaProteomicslcsh:ChemistrySus scrofa domestica0302 clinical medicineTandem Mass SpectrometryProtein Interaction Mapslcsh:QH301-705.5Spectroscopybiologyoptic nerve headGeneral MedicineComputer Science ApplicationsCell biologymedicine.anatomical_structureProteomeOptic nerveProtein Binding<i>Sus scrofa domestica</i>Optic DiskArticleCatalysisInorganic Chemistry03 medical and health sciencesmedicineMALDI-TOF MSAnimalsHumansPhysical and Theoretical ChemistryEndoplasminMolecular BiologyRetinaClusterinOrganic Chemistrymedicine.diseaseeye diseasesLC-MSglaucomaGene Ontology030104 developmental biologylcsh:Biology (General)lcsh:QD1-999Spectrometry Mass Matrix-Assisted Laser Desorption-Ionizationbiology.proteinsense organsCeruloplasmin030217 neurology & neurosurgeryInternational Journal of Molecular Sciences
researchProduct

Proteomic composition of Nipah virus-like particles

2017

Abstract Virions are often described as virus-only entities with no cellular components with the exception of the lipids in their membranes. However, advances in proteomics are revealing substantial amounts of host proteins in the viral particles. In the case of Nipah virus (NiV), the viral components in the virion have been known for some time. Nonetheless, no information has been obtained regarding the cellular proteins in the viral particles. To address this question, we produced Virus-Like Particles (VLPs) for NiV by expressing the F, G and M proteins in human-derived cells. Next, the proteomic content in these VLPs was analyzed by LC-MS/MS. We identified 67 human proteins including sol…

Proteomics0301 basic medicinevirusesNipah virusHost–pathogen interactionBiophysicsBiologyProteomicsBiochemistryVirusViral Proteins03 medical and health sciencesViral life cycleViral envelopeTandem Mass SpectrometryViral entryHumans030102 biochemistry & molecular biologyNipah VirusVirionVirology030104 developmental biologyCellular componentHost-Pathogen InteractionsChromatography LiquidProtein BindingJournal of Proteomics
researchProduct

Proteomic analysis of Parietaria judaica pollen and allergen profiling by an immunoproteomic approach

2010

Parietaria judaica pollen is a common cause of airway allergic disease in the Mediterranean area. Proteome analysis of mature Parietaria judaica pollen by two-dimensional gel electrophoresis (2-DE) and mass spectrometry has established the first reference proteome map of this weed. Proteins involved in a variety of cellular functions as well as the occurrence of allergens were detected. By using 2-DE and immunoblotting with sera from Parietaria judaica allergic patients we obtained a more detailed characterization of Parietaria judaica allergen profile so to improve our comprehension of the pathogenesis of pollen-induced allergic reaction.

ProteomicsAllergyProteomeCellular functionsBioengineeringmedicine.disease_causeProteomicsApplied Microbiology and BiotechnologyAllergenTandem Mass SpectrometryPollenotorhinolaryngologic diseasesmedicineHumansElectrophoresis Gel Two-DimensionalPlant Proteinsbiologyfood and beveragesGeneral MedicineAntigens PlantImmunoglobulin Ebiology.organism_classificationmedicine.diseaseParietariaImmunologyProteomeParietaria judaicaPollenParietaria judaica pollenallergens Parietaria judaica immunoproteome pollenBiotechnologyChromatography Liquid
researchProduct

Antilisterial peptides from Spanish dry-cured hams: Purification and identification.

2016

The typical Spanish dry-cured ham has a particular sensory quality that makes it a distinctive food, highly appreciated for consumers worldwide. Its particular physicochemical properties, such as high salt content and reduced water activity contribute to their shelf-stability. However, post-processing actions carried out for the commercialization of these products such as slicing may increase the risk of development of pathogenic microorganisms as Listeria monocytogenes. During ripening, muscle proteins are hydrolyzed by muscle peptidases releasing peptides and free amino acids. Some of these peptides have been described to exert biological activities such as antioxidant and ACE-inhibition.…

ProteomicsAntioxidantWater activitySwinemedicine.medical_treatmentAntimicrobial peptidesMicrobial Sensitivity Testsmedicine.disease_causeProteomics01 natural sciencesMicrobiologyPentapeptide repeatMass SpectrometryHydrolysis0404 agricultural biotechnologyDry-cured hamListeria monocytogenesTandem Mass SpectrometryFood PreservedmedicineEthnicityAnimalsHumansAmino Acid Sequence2. Zero hungerMass spectrometryChemistry010401 analytical chemistryRipening04 agricultural and veterinary sciences040401 food scienceListeria monocytogenes0104 chemical sciencesAnti-Bacterial AgentsMeat ProductsBiochemistrySpainAntimicrobial peptidesPeptidomimeticsPeptidesFood ScienceFood microbiology
researchProduct

Identification of Trans-Golgi Network Proteins in Arabidopsis thaliana Root Tissue

2014

Knowledge of protein subcellular localization assists in the elucidation of protein function and understanding of different biological mechanisms that occur at discrete subcellular niches. Organelle-centric proteomics enables localization of thousands of proteins simultaneously. Although such techniques have successfully allowed organelle protein catalogues to be achieved, they rely on the purification or significant enrichment of the organelle of interest, which is not achievable for many organelles. Incomplete separation of organelles leads to false discoveries, with erroneous assignments. Proteomics methods that measure the distribution patterns of specific organelle markers along densit…

ProteomicsArabidopsis thalianaArabidopsisorganelle proteomicsProteomicsPlant RootsBiochemistryArticlesymbols.namesakeArtificial IntelligenceTandem Mass SpectrometryArabidopsisOrganelleArabidopsis thalianaChromatography Reverse-PhaseimmunoisolationbiologyArabidopsis Proteinstrans-Golgi networkGeneral ChemistryGolgi apparatusbiology.organism_classificationSubcellular localizationLOPITCell biologyIsobaric labelingphenoDiscomachine learningsymbolsIdentification (biology)Journal of Proteome Research
researchProduct