Search results for " Basic"

showing 10 items of 10515 documents

Label-free quantitative proteomic profiling of colon cancer cells identifies acetyl-CoA carboxylase alpha as antitumor target of Citrus limon-derived…

2017

Abstract We have previously isolated exosome-like nanoparticles from Citrus-limon juice, able to inhibit in vitro and in vivo tumor cell growth. In order to deeply understand the mechanism underlying nanovesicle effects, we performed a proteomic profile of treated colorectal cancer cells. Among the proteins differentially expressed after nanovesicle treatment, we found a significant downregulation of the Acetyl-CoA Carboxylase 1 (ACACA) and we demonstrated that silencing ACACA in cancer cells leads to a reduction of cell growth. Our study proved that the anti-tumor effects of Citrus-limon nanovesicles is partly mediated by lipid metabolism inhibition, in particular via ACACA downregulation.…

Proteomics0301 basic medicineCitrusBiophysicsBiologyExosomesBiochemistry03 medical and health sciencesDownregulation and upregulationSettore BIO/13 - Biologia ApplicataCell Line TumorHumansGene silencingCell ProliferationLabel-free quantitative proteomic analysisACACAProteomic ProfileProteomic ProfilingCell growthCitrus-limon nanovesicleAcetyl-CoA carboxylaseLipid MetabolismColorectal cancer030104 developmental biologyBiochemistryColonic NeoplasmsCancer cellCancer researchAcetyl-CoA CarboxylaseJournal of Proteomics
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Minimal Information About an Immuno-Peptidomics Experiment (MIAIPE)

2018

Minimal Information about an Immuno-Peptidomics Experiment (MIAIPE) is an initiative of the members of the Human Immuno-Peptidome Project (HIPP), an international program organized by the Human Proteome Organization (HUPO). The aim of the MIAIPE guidelines is to deliver technical guidelines representing the minimal information required to sufficiently support the evaluation and interpretation of immunopeptidomics experiments. The MIAIPE document has been designed to report essential information about sample preparation, mass spectrometric measurement and associated mass spectrometry (MS)-related bioinformatics aspects that are unique to immunopeptidomics and may not be covered by the genera…

Proteomics0301 basic medicineComputer scienceComputational biologyProteomicsBiochemistrySpecimen Handling03 medical and health sciencesStandardisation & GuidelinesHuman proteome projectHumansantigen processing and presentationDatabases ProteinMolecular Biology030102 biochemistry & molecular biologyHistocompatibility Antigens Class IHistocompatibility Antigens Class IIimmunopeptidomicsComputational BiologyMass spectrometricPeptide Fragmentsmajor histocompatibility complex3. Good health030104 developmental biologyComputational Biology/standards; Databases Protein; Histocompatibility Antigens Class I/analysis; Histocompatibility Antigens Class I/immunology; Histocompatibility Antigens Class I/metabolism; Histocompatibility Antigens Class II/analysis; Histocompatibility Antigens Class II/immunology; Histocompatibility Antigens Class II/metabolism; Humans; Peptide Fragments/analysis; Peptide Fragments/immunology; Peptide Fragments/metabolism; Proteomics/standards; Software; Specimen Handling/standards; antigen processing and presentation; immunopeptidomics; major histocompatibility complexSoftwareantigen processing and presentation; immunopeptidomics; major histocompatibility complex
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Optimised lyophilisation-based method for different biomolecule single-extractions from the same rat brain sample: Suitability for RNA and protein ex…

2019

Abstract Background Optimisation of tissue processing procedures in preclinical studies reduces the number of animals used and allows integrated multilevel study in the same sample. Multiple extraction of different biomolecules from the same sample has several limitations. New method Using brain samples from rats subjected to ischemic stroke, we combined lyophilisation of flash-frozen tissue, mechanical pulverisation and cryopreservation in a method to optimise tissue handling and preservation for independent RNA or protein single-extract methods, and subsequent RT-qPCR or Western blot analyses. Results Lyophilisation resulted in 70% tissue weight loss. RNA (OD260/280∼1.8) and protein yield…

Proteomics0301 basic medicineCryopreservationSpecimen Handlinglaw.invention03 medical and health sciences0302 clinical medicinelawReference genesProtein purificationAnimalsFlash freezingMessenger RNAChromatographyChemistryGeneral NeuroscienceBrainTissue ProcessingRNARatsStrokeFreeze Drying030104 developmental biologyRNARNA extraction030217 neurology & neurosurgeryJournal of Neuroscience Methods
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Molecular modularity and asymmetry of the molluscan mantle revealed by a gene expression atlas

2018

15 pages; International audience; Background: Conchiferan molluscs construct a biocalcified shell that likely supported much of their evolutionary success.However, beyond broad proteomic and transcriptomic surveys of molluscan shells and the shell-forming mantle tissue,little is known of the spatial and ontogenetic regulation of shell fabrication. In addition, most efforts have been focused onspecies that deposit nacre, which is at odds with the majority of conchiferan species that fabricate shells using acrossed-lamellar microstructure, sensu lato. Results: By combining proteomic and transcriptomic sequencing with in situhybridization we have identified a suite of gene products associated …

Proteomics0301 basic medicineGlycosylationProteomematrix proteinHealth InformaticsLymnaea stagnalisProteomicsalternative splicing03 medical and health sciencesmolluscAnimal Shells[SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry Molecular Biology/Genomics [q-bio.GN]evolutionAnimalsMantle (mollusc)GeneGenetic Association Studiesmodularitymollusc; biomineralizationRegulation of gene expressionMineralsbiologyPhylumResearchGene Expression ProfilingGene Expression Regulation Developmentalbiomineralizationbiology.organism_classificationComputer Science ApplicationsGene expression profilingEvolvability030104 developmental biologyMolluscashellEvolutionary biologygene expressiontranscriptomeasymmetryGigaScience
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The Abundant Tegument Protein pUL25 of Human Cytomegalovirus Prevents Proteasomal Degradation of pUL26 and Supports Its Suppression of ISGylation

2018

The tegument of human cytomegalovirus (HCMV) virions contains proteins that interfere with both the intrinsic and the innate immunity. One protein with a thus far unknown function is pUL25. The deletion of pUL25 in a viral mutant (Towne-ΔUL25) had no impact on the release of virions and subviral dense bodies or on virion morphogenesis. Proteomic analyses showed few alterations in the overall protein composition of extracellular particles. A surprising result, however, was the almost complete absence of pUL26 in virions and dense bodies of Towne-ΔUL25 and a reduction of the large isoform pUL26-p27 in mutant virus-infected cells. pUL26 had been shown to inhibit protein conjugation with the in…

Proteomics0301 basic medicineIntrinsic immunityHuman cytomegalovirusImmunoprecipitationvirusesImmunologyMutantCytomegalovirusBiologyVirus ReplicationMicrobiologyViral Matrix ProteinsViral Proteins03 medical and health sciencesInterferonVirologymedicineHumansUbiquitinsCells CulturedInnate immune systemvirus diseasesViral tegumentFibroblastsbiochemical phenomena metabolism and nutritionPhosphoproteinsmedicine.diseaseISG15Immunity InnateVirus-Cell InteractionsCell biology030104 developmental biologyInsect ScienceMutationProteolysisCytokinesmedicine.drugJournal of Virology
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Phylointeractomics reconstructs functional evolution of protein binding

2017

Molecular phylogenomics investigates evolutionary relationships based on genomic data. However, despite genomic sequence conservation, changes in protein interactions can occur relatively rapidly and may cause strong functional diversification. To investigate such functional evolution, we here combine phylogenomics with interaction proteomics. We develop this concept by investigating the molecular evolution of the shelterin complex, which protects telomeres, across 16 vertebrate species from zebrafish to humans covering 450 million years of evolution. Our phylointeractomics screen discovers previously unknown telomere-associated proteins and reveals how homologous proteins undergo functiona…

Proteomics0301 basic medicineLineage (evolution)ScienceTelomere-Binding ProteinsGeneral Physics and AstronomyGenomicsBiologyProteomicsArticleGeneral Biochemistry Genetics and Molecular BiologyConserved sequenceEvolution Molecular03 medical and health sciencesPhylogeneticsMolecular evolutionPhylogenomicsAnimalsCells CulturedConserved SequencePhylogenyGeneticsGenomeMultidisciplinaryQComputational BiologyGenomicsSequence Analysis DNAGeneral ChemistryTelomereProtein superfamily030104 developmental biologyEvolutionary biologyVertebratesSequence AlignmentProtein Binding
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Are multi-omics enough?

2016

Multi-omic techniques are often seen as the future of microbiome studies. We argue that recent strategies for simplifying complex omic-derived data will need to be combined with improved cultivation techniques to pave the way towards a more targeted approach for understanding microbial communities.

Proteomics0301 basic medicineMicrobiology (medical)BacteriaGene Expression Profiling030106 microbiologyImmunologyComputational BiologyBiodiversityCell BiologyComputational biologyBiologyProteomicsApplied Microbiology and BiotechnologyMicrobiologyGene expression profiling03 medical and health sciences030104 developmental biologyMetagenomicsGeneticsHumansMulti omicsMetagenomicsMicrobiomeTranscriptome
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Integrated quantitative proteomic and transcriptomic analysis of lung tumor and control tissue: a lung cancer showcase

2015

Proteomics analysis of paired cancer and control tissue can be applied to investigate pathological processes in tumors. Advancements in data-independent acquisition mass spectrometry allow for highly reproducible quantitative analysis of complex proteomic patterns. Optimized sample preparation workflows enable integrative multi-omics studies from the same tissue specimens. We performed ion mobility enhanced, data-independent acquisition MS to characterize the proteome of 21 lung tumor tissues including adenocarcinoma and squamous cell carcinoma (SCC) as compared to control lung tissues of the same patient each. Transcriptomic data were generated for the same specimens. The quantitative prot…

Proteomics0301 basic medicinePathologymedicine.medical_specialtyLung NeoplasmsProteomeSystems biologyProteomicsTranscriptometranscriptomics03 medical and health sciencesBiomarkers TumormedicineHumansLung cancerNeoplasm Stagingmass spectrometryadenocarcinomabusiness.industryGene Expression Profilingproteomics analysisPrognosismedicine.diseaseGene expression profiling030104 developmental biologyOncologyCase-Control StudiesProteomeCarcinoma Squamous CellAdenocarcinomalung tumorsTranscriptomebusinessQuantitative analysis (chemistry)Follow-Up StudiesResearch PaperOncotarget
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Purification and partial characterization of a lectin protein complex, the clathrilectin, from the calcareous sponge Clathrina clathrus

2016

Carbohydrate-binding proteins were purified from the marine calcareous sponge Clathrina clathrus via affinity chromatography on lactose and N-acetyl glucosamine- agarose resins. Proteomic analysis of acrylamide gel separated protein subunits obtained in reducing conditions pointed out several candidates for lectins. Based on amino- acid sequence similarity, two peptides displayed homology with the jack bean lectin Concanavalin A, 
 including a conserved domain shared by proteins in the L-type lectin superfamily. An N-acetyl glucosamine - binding protein complex, named clathrilectin, was further purified via gel filtration chromatography, bioguided with a diagnostic rabbit erythrocyte haemag…

Proteomics0301 basic medicinePhysiologySyconBiochemistry03 medical and health sciencesAffinity chromatographyLectinsAnimalsTrypsinMolecular Biology030102 biochemistry & molecular biologybiologyCalcareous spongeHemagglutinationLectinClathrina clathrusbiology.organism_classificationMolecular biologyCell aggregationPoriferaPorifera ; Clathrina clathrus ; lectin ; N-acetyl-glucosamine ; cell aggregation ; proteomicsSponge030104 developmental biologyBiochemistryConcanavalin AProteolysisbiology.proteinCarbohydrate MetabolismFemaleRabbitsComparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology
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TrpM, a Small Protein Modulating Tryptophan Biosynthesis and Morpho-Physiological Differentiation in Streptomyces coelicolor A3(2).

2016

In the model actinomycete Streptomyces coelicolor A3(2), small open reading frames encoding proteins with unknown functions were identified in several amino acid biosynthetic gene operons, such as SCO2038 (trpX) in the tryptophan trpCXBA locus. In this study, the role of the corresponding protein in tryptophan biosynthesis was investigated by combining phenotypic and molecular analyses. The 2038KO mutant strain was characterized by delayed growth, smaller aerial hyphae and reduced production of spores and actinorhodin antibiotic, with respect to the WT strain. The capability of this mutant to grow on minimal medium was rescued by tryptophan and tryptophan precursor (serine and/or indole) su…

Proteomics0301 basic medicineProtein ExtractionMutantlcsh:MedicineStreptomyces coelicolor A3(2)Settore BIO/19 - Microbiologia GeneraleBiochemistrySerinechemistry.chemical_compoundAromatic Amino AcidsSmall ProteinAntibioticsTRPMMicrobial PhysiologyMedicine and Health SciencesBacterial PhysiologyAmino Acidslcsh:ScienceProtein MetabolismExtraction TechniquesMultidisciplinarybiologyOrganic CompoundsAntimicrobialsStreptomyces coelicolorTryptophanDrugsChemistryBiochemistryPhysical SciencesPhysiological DifferentiationResearch ArticleTryptophan BiosynthesiSmall Protein; Biosynthesis; Morpho-Physiological Differentiation: Streptomyces coelicolorBiosynthesisResearch and Analysis MethodsMicrobiologyStreptomycesActinorhodin03 medical and health sciencesBiosynthesisMicrobial ControlBacterial SporesPharmacology030102 biochemistry & molecular biologyOrganic Chemistrylcsh:RChemical CompoundsTryptophanTrpM; Small Protein; Tryptophan Biosynthesis; Morphological Differentiation; Physiological Differentiation; Streptomyces coelicolor A3(2); ProteomicsBiology and Life SciencesProteinsBacteriologybiology.organism_classificationAmino Acid MetabolismMetabolism030104 developmental biologychemistrylcsh:QMorphological DifferentiationTrpM
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