Search results for "Quantitative proteomics"

showing 10 items of 29 documents

Characterization of 150 Wheat Cultivars by LC-MS-Based Label-Free Quantitative Proteomics Unravels Possibilities to Design Wheat Better for Baking Qu…

2021

Wheat (Triticum aestivum ssp. aestivum) contributes to 20% of the human protein supply, delivers essential amino acids and is of fundamental importance for bread and pasta quality. Wheat proteins are also involved in adverse human reactions like celiac disease (CD), wheat allergy (WA) and non-celiac wheat sensitivity (NCWS). Using liquid chromatography-mass spectrometry (LC-MS)-based label-free quantitative (LFQ) proteomics of aqueous flour extracts, we determined 756 proteins across 150 wheat cultivars grown in three environments. However, only 303 proteins were stably expressed across all environments in at least one cultivar and only 89 proteins thereof across all 150 cultivars. This und…

0106 biological sciences0301 basic medicinehealthy nutritionQuantitative proteomicsPlant ScienceBiologyProteomics01 natural sciencesArticle03 medical and health sciencesHuman healthLiquid chromatography–mass spectrometryLC-MS proteomicswheatmedicineCultivarFood scienceEcology Evolution Behavior and SystematicsLabel freeEcologyfungiBotanyfood and beveragesHeritabilitymedicine.disease030104 developmental biologyQK1-989future breedingWheat allergy010606 plant biology & botanyPlants
researchProduct

Quantitative proteomics reveals a dynamic association of proteins to detergent-resistant membranes upon elicitor signaling in tobacco.

2009

International audience; A large body of evidence from the past decade supports the existence, in membrane from animal and yeast cells, of functional microdomains playing important roles in protein sorting, signal transduction, or infection by pathogens. In plants, as previously observed for animal microdomains, detergent-resistant fractions, enriched in sphingolipids and sterols, were isolated from plasma membrane. A characterization of their proteic content revealed their enrichment in proteins involved in signaling and response to biotic and abiotic stress and cell trafficking suggesting that these domains were likely to be involved in such physiological processes. In the present study, w…

0106 biological sciencesProteomicsGTPase-activating proteinQuantitative proteomicsDetergentsPlasma protein bindingBiologymedicine.disease_causeProteomics01 natural sciencesBiochemistryMass SpectrometryAnalytical ChemistryCell membraneFungal Proteins03 medical and health sciencesProtein targetingTobaccomedicine[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyMolecular Biology030304 developmental biologyPlant Proteins0303 health sciencesFungal proteinStaining and LabelingResearchAlgal ProteinsCell MembraneCell biologymedicine.anatomical_structureBiochemistryLuminescent MeasurementsSignal transductionPeptidesReactive Oxygen Species010606 plant biology & botanyProtein BindingSignal TransductionMolecularcellular proteomics : MCP
researchProduct

A multicenter study benchmarks software tools for label-free proteome quantification

2016

The consistent and accurate quantification of proteins by mass spectrometry (MS)-based proteomics depends on the performance of instruments, acquisition methods and data analysis software. In collaboration with the software developers, we evaluated OpenSWATH, SWATH2.0, Skyline, Spectronaut and DIA-Umpire, five of the most widely used software methods for processing data from SWATH-MS (sequential window acquisition of all theoretical fragment ion spectra), a method that uses data-independent acquisition (DIA) for label-free protein quantification. We analyzed high-complexity test datasets from hybrid proteome samples of defined quantitative composition acquired on two different MS instrument…

0301 basic medicineInternationalityProteomeComputer sciencemedia_common.quotation_subjectSoftware toolQuantitative proteomicsBiomedical EngineeringBioengineeringcomputer.software_genreBioinformaticsSensitivity and SpecificityApplied Microbiology and BiotechnologyArticleMass Spectrometry03 medical and health sciencesSoftwareQuality (business)media_commonLabel freeStaining and Labeling030102 biochemistry & molecular biologybusiness.industryReproducibility of ResultsBenchmarkingComputingMethodologies_PATTERNRECOGNITION030104 developmental biologyMulticenter studyProteomeBenchmark (computing)Molecular MedicineData miningbusinesscomputerAlgorithmsSoftwareBiotechnologyNature Biotechnology
researchProduct

Characterization of the porcine seminal plasma proteome comparing ejaculate portions.

2016

Full identification of boar seminal plasma (SP) proteins remains challenging. This study aims to provide an extensive proteomic analysis of boar SP and to generate an accessible database of boar SP-proteome. A SP-pool (33 entire ejaculates/11 boars; 3 ejaculates/boar) was analyzed to characterize the boar SP-proteome. Twenty ejaculates (5 boars, 4 ejaculates/boar) collected in portions (P1: first 10 mL of sperm rich ejaculate fraction (SRF), P2: rest of SRF and P3: post-SRF) were analyzed to evaluate differentially expressed SP-proteins among portions. SP-samples were analyzed using a combination of SEC, 1-D SDS PAGE and NanoLC-ESI-MS/MS followed by functional bioinformatics. The identified…

0301 basic medicineMaleProteomicsendocrine systemBOARProteomeSwineQuantitative proteomicsBiophysicsComputational biologyBioinformatik och systembiologiBiologyBioinformaticsBiochemistry03 medical and health sciencesTandem Mass SpectrometryAnimalsPorcine; Ejaculate; Seminal plasma; ProteomeEjaculationSperm qualityDatabases ProteinLabel freeBioinformatics and Systems Biologyurogenital systemProteomic ProfilingReproductionSeminal Plasma ProteinsComputational BiologySpermSemen Analysis030104 developmental biologyFertilityGene Expression RegulationBiological significanceProteomeElectrophoresis Polyacrylamide GelChromatography LiquidJournal of proteomics
researchProduct

Quantitative Proteomics Reveals Changes Induced by TIMP-3 on Cell Membrane Composition and Novel Metalloprotease Substrates

2021

Ectodomain shedding is a key mechanism of several biological processes, including cell-communication. Disintegrin and metalloproteinases (ADAMs), together with the membrane-type matrix metalloproteinases, play a pivotal role in shedding transmembrane proteins. Aberrant shedding is associated to several pathological conditions, including arthritis. Tissue inhibitor of metalloproteases 3 (TIMP-3), an endogenous inhibitor of ADAMs and matrix metalloproteases (MMPs), has been proven to be beneficial in such diseases. Thus, strategies to increase TIMP-3 bioavailability in the tissue have been sought for development of therapeutics. Nevertheless, high levels of TIMP-3 may lead to mechanism-based …

0301 basic medicineProteomicsADAM15ProteomeCellMatrix metalloproteinaseMass SpectrometryCell membranelcsh:Chemistryanalysis [Proteome]lcsh:QH301-705.5proteomicSpectroscopybiologyChemistrytissue inhibitor of metalloproteases 3 (TIMP-3)General MedicineTransmembrane proteinComputer Science ApplicationsCell biologymedicine.anatomical_structureEctodomainddc:540TIMP3 protein humanmetalloproteinaseectodomain sheddingmetabolism [Tissue Inhibitor of Metalloproteinase-3]Quantitative proteomicsADAM15 protein humanchemistry [Cell Membrane]Catalysismetabolism [Cell Membrane]ArticlemetalloproteinasesInorganic Chemistry03 medical and health sciencestissue inhibitor of metalloproteases 3 (TIMP-3).medicineDisintegrinHumansPhysical and Theoretical ChemistryMolecular BiologyTissue Inhibitor of Metalloproteinase-3030102 biochemistry & molecular biologyOrganic ChemistryCell MembraneMembrane Proteinsmetabolism [Proteome]ADAM Proteins030104 developmental biologyHEK293 Cellslcsh:Biology (General)lcsh:QD1-999metabolism [ADAM Proteins]biology.proteinmetabolism [Membrane Proteins]International Journal of Molecular Sciences
researchProduct

Label-free quantification in ion mobility-enhanced data-independent acquisition proteomics.

2016

Unbiased data-independent acquisition (DIA) strategies have gained increased popularity in the field of quantitative proteomics. The integration of ion mobility separation (IMS) into DIA workflows provides an additional dimension of separation to liquid chromatography-mass spectrometry (LC-MS), and it increases the achievable analytical depth of DIA approaches. Here we provide a detailed protocol for a label-free quantitative proteomics workflow based on ion mobility-enhanced DIA, which synchronizes precursor ion drift times with collision energies to improve precursor fragmentation efficiency. The protocol comprises a detailed description of all major steps including instrument setup, filt…

0301 basic medicineProteomicsTime FactorsProteomeComputer scienceQuantitative proteomicsProteolytic enzymesProteinsProteomicsMass spectrometryGeneral Biochemistry Genetics and Molecular BiologyChemistry Techniques AnalyticalMass Spectrometry03 medical and health sciencesLabel-free quantification030104 developmental biologyProteomeHumansData-independent acquisitionSample preparationBiological systemChromatography LiquidHeLa CellsNature protocols
researchProduct

Variance component analysis to assess protein quantification in biomarker discovery. Application to MALDI-TOF mass spectrometry.

2017

International audience; Controlling the technological variability on an analytical chain is critical for biomarker discovery. The sources of technological variability should be modeled, which calls for specific experimental design, signal processing, and statistical analysis. Furthermore, with unbalanced data, the various components of variability cannot be estimated with the sequential or adjusted sums of squares of usual software programs. We propose a novel approach to variance component analysis with application to the matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) technology and use this approach for protein quantification by a classical signal processing algori…

0301 basic medicineStatistics and ProbabilityMALDI-TOFexperimental designBiometryprotein quantificationQuantitative proteomicsVariance component analysis[ CHIM ] Chemical Sciences01 natural sciencesSignaltechnological variability010104 statistics & probability03 medical and health sciencesstatistical analysis[INFO.INFO-TS]Computer Science [cs]/Signal and Image Processing[CHIM.ANAL]Chemical Sciences/Analytical chemistryComponent (UML)[SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry Molecular Biology/Genomics [q-bio.GN]biomarker discoverysum of squares type0101 mathematicsBiomarker discoverysignal processingMathematicsSignal processingAnalysis of Variance[ PHYS ] Physics [physics]Noise (signal processing)ProteinsGeneral MedicineVariance (accounting)[SDV.BIBS]Life Sciences [q-bio]/Quantitative Methods [q-bio.QM]030104 developmental biologySpectrometry Mass Matrix-Assisted Laser Desorption-IonizationLinear Modelsvariance components[ CHIM.ANAL ] Chemical Sciences/Analytical chemistryStatistics Probability and UncertaintyBiological systemAlgorithmsBiomarkersBiometrical journal. Biometrische Zeitschrift
researchProduct

The developmental proteome of Drosophila melanogaster

2017

Drosophila melanogaster is a widely used genetic model organism in developmental biology. While this model organism has been intensively studied at the RNA level, a comprehensive proteomic study covering the complete life cycle is still missing. Here, we apply label-free quantitative proteomics to explore proteome remodeling across Drosophila’s life cycle, resulting in 7952 proteins, and provide a high temporal-resolved embryogenesis proteome of 5458 proteins. Our proteome data enabled us to monitor isoform-specific expression of 34 genes during development, to identify the pseudogene Cyp9f3Ψ as a protein-coding gene, and to obtain evidence of 268 small proteins. Moreover, the comparison wi…

0301 basic medicinebiologyved/biologyved/biology.organism_classification_rank.speciesQuantitative proteomicsComputational biologyProteomicsbiology.organism_classificationTranscriptome03 medical and health sciences030104 developmental biologyGenetic modelProteomeGeneticsDrosophila melanogasterModel organismGenetics (clinical)Drosophila ProteinGenome Research
researchProduct

Proteomics Reveals the Potential Protective Mechanism of Hydrogen Sulfide on Retinal Ganglion Cells in an Ischemia/Reperfusion Injury Animal Model

2020

Glaucoma is the leading cause of irreversible blindness and is characterized by progressive retinal ganglion cell (RGC) degeneration. Hydrogen sulfide (H2S) is a potent neurotransmitter and has been proven to protect RGCs against glaucomatous injury in vitro and in vivo. This study is to provide an overall insight of H2S&rsquo

0301 basic medicineneuronal apoptosisgenetic structuresQuantitative proteomicshydrogen sulfidePharmaceutical Sciencelcsh:Medicinelcsh:RS1-441PharmacologyProteomicsRetinal ganglionArticlelabel-free mass spectrometrylcsh:Pharmacy and materia medica03 medical and health scienceschemistry.chemical_compound0302 clinical medicinemitochondrial functionIn vivoDrug DiscoverymedicineRetinaChemistrylcsh:RRetinalmedicine.diseaseequipment and supplieseye diseases030104 developmental biologymedicine.anatomical_structureglaucomaRetinal ganglion cellMolecular Medicinesense organsReperfusion injurysignalling pathways030217 neurology & neurosurgeryPharmaceuticals
researchProduct

In-Depth Proteomic Characterization of Classical and Non-Classical Monocyte Subsets

2018

Monocytes are bone marrow-derived leukocytes that are part of the innate immune system. Monocytes are divided into three subsets: classical, intermediate and non-classical, which can be differentiated by their expression of some surface antigens, mainly CD14 and CD16. These cells are key players in the inflammation process underlying the mechanism of many diseases. Thus, the molecular characterization of these cells may provide very useful information for understanding their biology in health and disease. We performed a multicentric proteomic study with pure classical and non-classical populations derived from 12 healthy donors. The robust workflow used provided reproducible results among t…

0301 basic medicinequantitative proteomicsInnate immune systemFunctional analysisMechanism (biology)CD14Clinical BiochemistryQuantitative proteomicslcsh:QR1-502monocytes; protein profiling; quantitative proteomicsDiseaseComputational biologyCD16Biologyprotein profilingBiochemistryArticlelcsh:Microbiology03 medical and health sciences030104 developmental biologyAntigenStructural BiologymonocytesMolecular Biology
researchProduct