Search results for "proteomics."

showing 10 items of 523 documents

What Can Proteomics Tell Us About Platelets?

2014

More than 130 years ago, it was recognized that platelets are key mediators of hemostasis. Nowadays, it is established that platelets participate in additional physiological processes and contribute to the genesis and progression of cardiovascular diseases. Recent data indicate that the platelet proteome, defined as the complete set of expressed proteins, comprises >5000 proteins and is highly similar between different healthy individuals. Owing to their anucleate nature, platelets have limited protein synthesis. By implication, in patients experiencing platelet disorders, platelet (dys)function is almost completely attributable to alterations in protein expression and dynamic difference…

PhysiologyPlatelet disorderblood plateletsproteomeBlood ProteinsDiseaseBiologyProteomicsBioinformaticsbleedingcardiovascular diseasesproteomicsHemostasisImmunologyProteomeAnimalsHumansPlatelethemorrhageTranscriptomeCardiology and Cardiovascular MedicineHomeostasisFunction (biology)Signal TransductionCirculation Research
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TRIC: an automated alignment strategy for reproducible protein quantification in targeted proteomics

2016

Nature Methods, 13 (9)

Pluripotent Stem CellsProteomics0301 basic medicineAnalyteStreptococcus pyogenesSoftware toolQuantitative proteomicsProteomic analysisComputational biologyBiologyProteome informaticsProteomicsBioinformaticsBiochemistryArticleMass Spectrometry03 medical and health sciencesSequence Analysis ProteinProtein methodsHumansProtein PrecursorsHuman Induced Pluripotent Stem CellsMolecular BiologyElectronic Data ProcessingReproducibility of ResultsCell BiologyMass spectrometricTargeted proteomics030104 developmental biologyProteolysissense organsPeptidesSequence AlignmentAlgorithmsSoftwareBiotechnologyNature Methods
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A Approach to Clinical Proteomics Data Quality Control and Import

2011

International audience; Biomedical domain and proteomics in particular are faced with an increasing volume of data. The heterogeneity of data sources implies heterogeneity in the representation and in the content of data. Data may also be incorrect, implicate errors and can compromise the analysis of experiments results. Our approach aims to ensure the initial quality of data during import into an information system dedicated to proteomics. It is based on the joint use of models, which represent the system sources, and ontologies, which are use as mediators between them. The controls, we propose, ensure the validity of values, semantics and data consistency during import process.

Process (engineering)Computer sciencemedia_common.quotation_subject02 engineering and technologyOntology (information science)Proteomicscomputer.software_genreDomain (software engineering)03 medical and health sciences020204 information systems[ INFO.INFO-BI ] Computer Science [cs]/Bioinformatics [q-bio.QM]0202 electrical engineering electronic engineering information engineeringInformation systemQuality (business)[ SDV.BIBS ] Life Sciences [q-bio]/Quantitative Methods [q-bio.QM]030304 developmental biologymedia_common0303 health sciences[INFO.INFO-DB]Computer Science [cs]/Databases [cs.DB][SDV.BIBS]Life Sciences [q-bio]/Quantitative Methods [q-bio.QM]Data science[ INFO.INFO-DB ] Computer Science [cs]/Databases [cs.DB]Data qualityData mining[INFO.INFO-BI]Computer Science [cs]/Bioinformatics [q-bio.QM]computer
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Protein content and lipid profiling of isolated native autophagosomes

2021

AbstractAutophagy is a central eukaryotic catabolic pathway responsible for clearance and recycling of an extensive portfolio of cargoes, which are packed in vesicles, called autophagosomes, and are delivered to lysosomes for degradation. Besides basal autophagy, which constantly degrades cellular material, the pathway is highly responsive to several stress conditions. However, the exact protein content and phospholipid composition of autophagosomes under changing autophagy conditions remain elusive so far. Here, we introduce a FACS-based approach for isolation of native unmanipulated autophagosomes and ensure the quality of the preparations. Employing quantitative proteomics and phospholip…

Protein contentAutophagosomechemistry.chemical_compoundCatabolismChemistryVesicleAutophagyQuantitative proteomicsPhospholipidLipid profilingCell biology
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Identification of metabolic enzymes in renal cell carcinoma utilizing PROTEOMEX analyses

2003

Abstract PROTEOMEX, an approach which combines conventional proteome analysis with serological screening, is a powerful tool to separate proteins and identify immunogenic components in malignant diseases. By applying this approach, we characterized nine metabolic enzymes which were differentially expressed in renal cell carcinoma (RCC) cell lines and compared their expression profiles to that of normal kidney epithelium cells. Four of these proteins, superoxide dismutase (SODC), triosephosphatase isomerase (TPIS), thioredoxin (THIO) and ubiquitin carboxyl-terminal hydrolase (UBL1) were further analysed for both their constitutive and interferon (IFN)-γ inducible protein expression pattern i…

ProteomeBiophysicsBiologyurologic and male genital diseasesProteomicsBiochemistryAnalytical ChemistryInterferon-gammaThioredoxinsDownregulation and upregulationWestern blotTumor Cells CulturedmedicineHumansElectrophoresis Gel Two-DimensionalCarcinoma Renal CellMolecular BiologyKidneymedicine.diagnostic_testSuperoxide DismutaseImmunohistochemistryMolecular biologyKidney NeoplasmsEpitheliumEnzymesmedicine.anatomical_structureCell cultureProteomeThioredoxinSoftwareTriose-Phosphate IsomeraseBiochimica et Biophysica Acta (BBA) - Proteins and Proteomics
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Prediction of a Missing Protein Expression Map in the Context of the Human Proteome Project

2015

Experimental evidence for the entire human proteome has been defined in the Human Proteome Project, and it is publicly available in the neXtProt database. However, there are still human proteins for which reliable experimental evidence does not exist, and the identification of such information has become one of the overriding objectives in the chromosome-centric study of the human proteome. With this aim and considering the complexity of protein detection using shotgun and targeted proteomics, the research community has addressed the integration of transcriptomics and proteomics landscapes. Here, we describe an analytical pipeline that predicts the probability of a missing protein being exp…

ProteomeNeXtProtMicroarrayProtein Array AnalysisProteinsShotgunGeneral ChemistryComputational biologyBiologyBioinformaticsProteomicsBiochemistryTranscriptomeGene expressionHuman proteome projectHumansTranscriptomeGeneJournal of Proteome Research
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Proteome-Wide Characterization of the RNA-Binding Protein RALY-Interactome Using the in Vivo-Biotinylation-Pulldown-Quant (iBioPQ) Approach

2013

RALY is a member of the heterogeneous nuclear ribonucleoproteins, a family of RNA-binding proteins generally involved in many processes of mRNA metabolism. No quantitative proteomic analysis of RALY-containing ribonucleoparticles (RNPs) has been performed so far, and the biological role of RALY remains elusive. Here, we present a workflow for the characterization of RALY's interaction partners, termed iBioPQ, that involves in vivo biotinylation of biotin acceptor peptide (BAP)-fused protein in the presence of the prokaryotic biotin holoenzyme synthetase of BirA so that it can be purified using streptavidin-coated magnetic beads, circumventing the need for specific antibodies and providing e…

ProteomeRecombinant Fusion ProteinsMolecular Sequence DataBiotinRNA-binding proteinBiologyHeterogeneous ribonucleoprotein particleProteomicsPoly(A)-Binding Protein IBiochemistryInteractomeELAV-Like Protein 103 medical and health scienceschemistry.chemical_compound0302 clinical medicineNuclear Matrix-Associated ProteinsBiotinProtein Interaction MappingHumansCarbon-Nitrogen LigasesAmino Acid SequenceProtein Interaction MapsPeptide sequence030304 developmental biology0303 health sciencesEscherichia coli ProteinsHeterogeneous-Nuclear Ribonucleoprotein Group CRNA-Binding ProteinsGeneral ChemistryRepressor ProteinsHEK293 CellsELAV ProteinsGene Expression RegulationBiochemistrychemistryProtein Biosynthesis030220 oncology & carcinogenesisBiotinylationProteomeBiological AssayStreptavidinHeLa CellsProtein BindingJournal of Proteome Research
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Evolution of nacre: biochemistry and proteomics of the shell organic matrix of the cephalopod Nautilus macromphalus.

2009

12 pages; International audience; In mollusks, one of the most widely studied shell textures is nacre, the lustrous aragonitic layer that constitutes the internal components of the shells of several bivalves, a few gastropods, and one cephalopod: the nautilus. Nacre contains a minor organic fraction, which displays a wide range of functions in relation to the biomineralization process. Here, we have biochemically characterized the nacre matrix of the cephalopod Nautilus macromphalus. The acid-soluble matrix contains a mixture of polydisperse and discrete proteins and glycoproteins, which interact with the formation of calcite crystals. In addition, a few bind calcium ions. Furthermore, we h…

ProteomeShell (structure)ProteomicsBiochemistryCalcium Carbonate03 medical and health sciencesPaleontologychemistry.chemical_compoundproteomicsevolutionAnimals14. Life underwaterAmino Acid SequenceNautilus[SDV.IB.BIO]Life Sciences [q-bio]/Bioengineering/BiomaterialsMolecular BiologyChromatography High Pressure Liquid030304 developmental biologyCalciteNautilus macromphalus0303 health sciencesbiology030302 biochemistry & molecular biologyOrganic ChemistryProteinsbiology.organism_classificationbiomineralization[ SDV.IB.BIO ] Life Sciences [q-bio]/Bioengineering/BiomaterialsBiological EvolutionCephalopodCalcium carbonatechemistryChemical engineeringSolubilitySpectrometry Mass Matrix-Assisted Laser Desorption-IonizationMolecular MedicineNautilusNautilus macromphalusSequence AlignmentBiomineralizationmollusk shell nacre
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Differential proteomic analysis highlights metabolic strategies associated with balhimycin production in Amycolatopsis balhimycina chemostat cultivat…

2010

Abstract Background Proteomics was recently used to reveal enzymes whose expression is associated with the production of the glycopeptide antibiotic balhimycin in Amycolatopsis balhimycina batch cultivations. Combining chemostat fermentation technology, where cells proliferate with constant parameters in a highly reproducible steady-state, and differential proteomics, the relationships between physiological status and metabolic pathways during antibiotic producing and non-producing conditions could be highlighted. Results Two minimal defined media, one with low Pi (0.6 mM; LP) and proficient glucose (12 g/l) concentrations and the other one with high Pi (1.8 mM) and limiting (6 g/l; LG) glu…

Proteomemedicine.drug_classlcsh:QR1-502BioengineeringChemostatBiologyGlycopeptide antibioticProteomicsSettore BIO/19 - Microbiologia GeneraleApplied Microbiology and Biotechnologylcsh:Microbiology03 medical and health sciencesBacterial ProteinsVancomycinantibioticActinomycetalesmedicineElectrophoresis Gel Two-DimensionalBalhimycinproteomic030304 developmental biology2. Zero hungerchemistry.chemical_classification0303 health sciences030306 microbiologyResearchFatty AcidsCarbonAnti-Bacterial AgentsMetabolic pathwayglycopeptideEnzymeGlucosechemistryBiochemistryAmycolatopsis balhimycinaProtein BiosynthesisFermentationBiotechnologyMicrobial Cell Factories
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LARGE-SCALE COMPARATIVE PROTEOMICS OF BREAST CANCER SURGICAL TISSUES

2009

Proteomics BREAST CANCERSettore BIO/06 - Anatomia Comparata E Citologia
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