Search results for "binding"

showing 10 items of 3896 documents

Heat shock protein 27 is involved in SUMO-2/3 modification of heat shock factor 1 and thereby modulates the transcription factor activity

2009

Heat shock protein 27 (HSP27) accumulates in stressed cells and helps them to survive adverse conditions. We have already shown that HSP27 has a function in the ubiquitination process that is modulated by its oligomerization/phosphorylation status. Here, we show that HSP27 is also involved in protein sumoylation, a ubiquitination-related process. HSP27 increases the number of cell proteins modified by small ubiquitin-like modifier (SUMO)-2/3 but this effect shows some selectivity as it neither affects all proteins nor concerns SUMO-1. Moreover, no such alteration in SUMO-2/3 conjugation is achievable by another HSP, such as HSP70. Heat shock factor 1 (HSF1), a transcription factor responsib…

Protein sumoylationTranscriptional ActivationCancer Researchendocrine systemanimal structuresSUMO proteinHSP27 Heat-Shock ProteinsBiologyurologic and male genital diseasesenvironment and public healthSubstrate Specificity03 medical and health sciencesTransactivation0302 clinical medicineHeat Shock Transcription FactorsHeat shock proteinGeneticsAnimalsHumansAnimals Cell Nucleus/metabolism DNA-Binding Proteins/*metabolism HSP27 Heat-Shock Proteins/chemistry/*metabolism Hela Cells Humans Protein Multimerization Protein Structure[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyHSF1Protein Structure QuaternaryMolecular BiologyTranscription factorUbiquitinsHeat-Shock Proteins030304 developmental biologyCell Nucleus0303 health sciencesMolecular biologyHsp70Cell biologyHeat shock factorDNA-Binding ProteinsProtein TransportQuaternary Protein Transport Small Ubiquitin-Related Modifier Proteins/*metabolism Substrate Specificity Transcription Factors/*metabolism Transcriptional Activation Ubiquitins/*metabolism030220 oncology & carcinogenesisembryonic structuresSmall Ubiquitin-Related Modifier ProteinsProtein MultimerizationHeLa CellsMolecular ChaperonesTranscription Factors
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Peroxisomal and mitochondrial status of two murine oligodendrocytic cell lines (158N, 158JP): potential models for the study of peroxisomal disorders…

2009

International audience; In some neurodegenerative disorders (leukodystrophies) characterized by myelin alterations, the defect of peroxisomal functions on myelin-producing cells (oligodendrocytes) are poorly understood. The development of in vitro models is fundamental to understanding the physiopathogenesis of these diseases. We characterized two immortalized murine oligodendrocyte cell lines: a normal (158N) and a jimpy (158JP) cell line mutated for the proteolipid protein PLP/DM20. Fluorescence microscopy, flow cytometry, and western blotting analysis allow to identify major myelin proteins (PLP colocalizing with mitochondria; myelin basic protein), oligodendrocyte (CNPase and myelin oli…

Proteolipid protein 1BiochemistryMiceMyelinMESH : PhenylbutyratesperoxisomeIsomerasesMESH : Myelin Basic ProteinsEnoyl-CoA HydrataseCell Line TransformedUltrasonographybiologyMESH : Gene Expression RegulationMESH : Myelin Proteolipid Protein3-Hydroxyacyl CoA DehydrogenasesMESH : Myelin-Associated GlycoproteinMESH : Cell Line TransformedPeroxisomeMESH : Multienzyme ComplexesMESH : OligodendrogliaMESH : Enoyl-CoA HydrataseCatalaseFlow CytometryMESH : 3-Hydroxyacyl CoA DehydrogenasesPhenylbutyratesmitochondriaMyelin-Associated GlycoproteinOligodendrogliamyelinMESH : Antineoplastic Agentsmedicine.anatomical_structureMESH : Microscopy Electron TransmissionBiochemistryACOX1MESH : MitochondriaMESH : Acyl-CoA Oxidase2'3'-Cyclic-Nucleotide PhosphodiesterasesMESH : IsomerasesOxidation-ReductionMyelin ProteinsMESH : Flow CytometryAntineoplastic AgentsPeroxisomal Bifunctional EnzymeStatistics NonparametricMyelin oligodendrocyte glycoproteinCellular and Molecular NeuroscienceMicroscopy Electron TransmissionMultienzyme ComplexesMESH : CatalaseMESH : MicePeroxisomesmedicineAnimalsMESH : ATP-Binding Cassette TransportersMyelin Proteolipid ProteinMESH : Statistics Nonparametric[ SDV.BBM ] Life Sciences [q-bio]/Biochemistry Molecular BiologyMESH : Oxidation-ReductionMyelin Basic Proteinmurine oligodendrocytesMESH : 2'3'-Cyclic-Nucleotide PhosphodiesterasesPeroxisomal transportOligodendrocyteMyelin basic proteinGene Expression Regulationbiology.proteinATP-Binding Cassette TransportersMyelin-Oligodendrocyte GlycoproteinAcyl-CoA OxidaseMESH : AnimalsMESH : Peroxisomes
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Perturbed interactions of mutant proteolipid protein/DM20 with cholesterol and lipid rafts in oligodendroglia: implications for dysmyelination in spa…

2006

Missense mutations in the humanPLP1gene lead to dysmyelinating diseases with a broad range of clinical severity, ranging from severe Pelizaeus–Merzbacher disease (PMD) to milder spastic paraplegia type 2 (SPG-2). The molecular pathology has been generally attributed to endoplasmic reticulum (ER) retention of misfolded proteolipid protein (PLP) (and its splice isoform DM20) and induction of the unfolded protein response. As opposed to previous studies of heterologous expression systems, we have analyzed PLP/DM20 trafficking in oligodendroglial cells, thereby revealing differences between PMD and SPG-2-associated PLP/DM20 isoforms. PLPA242Vand DM20A242V(jimpy-msdin mice), associated with seve…

Proteolipid protein 1Time FactorsLeupeptinsBlotting WesternGene Expressionchemical and pharmacologic phenomenaNerve Tissue ProteinsBiologyProtein degradationCysteine Proteinase InhibitorsTransfectionMiceMice Neurologic MutantsCricetulusMembrane MicrodomainsMutant proteinimmune system diseasesCricetinaeAnimalsImmunoprecipitationMyelin Proteolipid ProteinLipid raftCells CulturedGeneral NeuroscienceEndoplasmic reticulumCholesterol bindingER retentionArticlesImmunohistochemistryCell biologynervous system diseasesOligodendrogliaProtein TransportCholesterolBiochemistryUnfolded protein responselipids (amino acids peptides and proteins)Mutant ProteinsSubcellular FractionsThe Journal of neuroscience : the official journal of the Society for Neuroscience
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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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Global transcriptional profiling ofCandida albicans cwt1 null mutant

2007

CaCwt1p is a Candida albicans putative transcriptional factor homologue to Rds2p in Saccharomyces cerevisiae. The lack of this protein in S. cerevisiae leads to a pleiotropic resistance to drugs and defects in cell wall architecture that are also detectable in C. albicans. It is also known that CaCwt1p is mainly expressed in the stationary growth phase of this fungus. In order to elucidate the role of CWT1, transcriptome analysis of the mutant strain was performed in exponential and stationary growth phases. A total of 460 genes were found to be up- or downregulated in the mutant strain growing exponentially, and 666 genes presented a misregulation when cwt1 cells reached the stationary pha…

ProteomeSaccharomyces cerevisiaeRibosome biogenesisBioengineeringApplied Microbiology and BiotechnologyBiochemistryFungal ProteinsTranscriptomeCell WallGene Expression Regulation FungalCandida albicansGeneticsPromoter Regions GeneticCandida albicansGeneTranscription factorOligonucleotide Array Sequence AnalysisBinding SitesbiologyCell growthGene Expression Profilingbiology.organism_classificationMolecular biologyProtein BiosynthesisMutationDNA microarrayGlycolysisTranscription FactorsBiotechnologyYeast
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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
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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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Exosomes from metastatic cancer cells transfer amoeboid phenotype to non-metastatic cells and increase endothelial permeability: their emerging role …

2017

AbstractThe goal of this study was to understand if exosomes derived from high-metastatic cells may influence the behavior of less aggressive cancer cells and the properties of the endothelium. We found that metastatic colon cancer cells are able to transfer their amoeboid phenotype to isogenic primary cancer cells through exosomes, and that this morphological transition is associated with the acquisition of a more aggressive behavior. Moreover, exosomes from the metastatic line (SW620Exos) exhibited higher ability to cause endothelial hyperpermeability than exosomes from the non metastatic line (SW480Exos). SWATH-based quantitative proteomic analysis highlighted that SW620Exos are signific…

Proteomics0301 basic medicineRHOAEndotheliummetastatic cancer cellScienceCell PlasticityContext (language use)ExosomesArticlePermeability03 medical and health sciences0302 clinical medicineSettore BIO/13 - Biologia ApplicataCell Line Tumormetastatic cancer cells; Exosomes; tumor heterogeneitytumor heterogeneityHuman Umbilical Vein Endothelial CellsmedicineHumansEndotheliumrho-Associated KinasesMultidisciplinarybiologyQThrombinRPhenotypeMicrovesicles3. Good healthCell biologyEndothelial stem cellExosomePhenotype030104 developmental biologymedicine.anatomical_structureTumor progression030220 oncology & carcinogenesisColonic NeoplasmsCancer cellbiology.proteinMedicinerhoA GTP-Binding ProteinSignal Transduction
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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
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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
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