Search results for "mapping"

showing 10 items of 1508 documents

Quantitative Analysis of Prion-Protein Degradation by Constitutive and Immuno-20S Proteasomes Indicates Differences Correlated with Disease Susceptib…

2004

Abstract The main part of cytosolic protein degradation depends on the ubiquitin-proteasome system. Proteasomes degrade their substrates into small peptide fragments, some of which are translocated into the endoplasmatic reticulum and loaded onto MHC class I molecules, which are then transported to the cell surface for inspection by CTL. A reliable prediction of proteasomal cleavages in a given protein for the identification of CTL epitopes would benefit immensely from additional cleavage data for the training of prediction algorithms. To increase the knowledge about proteasomal specificity and to gain more insight into the relation of proteasomal activity and susceptibility to prion diseas…

Proteasome Endopeptidase ComplexPrionsMolecular Sequence DataImmunologyCellProtein degradationPeptide MappingMultienzyme ComplexesMHC class ImedicineAnimalsHumansImmunology and AllergyAmino Acid SequencePeptide sequenceAllelesCell Line TransformedSheepbiologyHydrolysisMolecular biologyPeptide FragmentsRecombinant ProteinsCell biologyCysteine EndopeptidasesKineticsCytosolCTL*medicine.anatomical_structureProteasomeCell culturebiology.proteinDisease SusceptibilityThe Journal of Immunology
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The Role of Low Complexity Regions in Protein Interaction Modes: An Illustration in Huntingtin

2021

Low complexity regions (LCRs) are very frequent in protein sequences, generally having a lower propensity to form structured domains and tending to be much less evolutionarily conserved than globular domains. Their higher abundance in eukaryotes and in species with more cellular types agrees with a growing number of reports on their function in protein interactions regulated by post-translational modifications. LCRs facilitate the increase of regulatory and network complexity required with the emergence of organisms with more complex tissue distribution and development. Although the low conservation and structural flexibility of LCRs complicate their study, evolutionary studies of proteins …

Protein Conformation alpha-Helical0301 basic medicineNetwork complexityHuntingtinintrinsically disordered regionsAmino Acid MotifsComputational biologyBiologyprotein interactionsArticlecompositionally biased regionsCatalysisProtein–protein interactionlcsh:ChemistryEvolution MolecularInorganic ChemistryLow complexity03 medical and health sciencesProtein DomainsProtein Interaction MappingAnimalsHumansp300-CBP Transcription FactorsAmino Acid SequenceProtein Interaction MapsHuntingtinTissue distributionPhysical and Theoretical Chemistrylcsh:QH301-705.5Molecular BiologySpectroscopyHuntingtin Protein030102 biochemistry & molecular biologyOrganic ChemistryNuclear Proteinsp120 GTPase Activating ProteinGeneral MedicineMultiple modesSynapsinslow complexity regionsComputer Science ApplicationshomorepeatsMicroscopy Electron030104 developmental biologylcsh:Biology (General)lcsh:QD1-999Sequence AlignmentFunction (biology)Protein BindingInternational Journal of Molecular Sciences
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Identification of disulphide bonds in the refolding of bovine pancreatic RNase A

1996

Background: Comprehension of the rules that govern the folding process is still far from satisfactory, though it is nevertheless clear that all the information required to define the folding is encoded in the amino acid sequence. In proteins that contain disulphide bonds, folding is associated with disulphide bond formation. Protein species with different numbers of disulphides tend to accumulate during the process; these species can be trapped in a stable form, by quenching any remaining free SH groups, and then characterized in order to identify the disulphide bonds formed. Results The refolding pathway of reduced and denatured RNase A has been studied using mass spectrometric strategies …

Protein FoldingSh groupsRNase P010402 general chemistryPeptide Mapping01 natural sciencesBiochemistryrefolding03 medical and health sciencesRNase AAnimalsDisulfidesES-MSPeptide sequencedisulphide bonds030304 developmental biology0303 health sciencesQuenching (fluorescence)ChemistryFAB-MSRibonuclease Pancreatic0104 chemical sciencesFolding (chemistry)CrystallographyMolecular MedicineCattlePancreatic RNaseDisulphide bondsCysteineFolding and Design
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A vertebrate globin expressed in the brain.

2000

Haemoglobins and myoglobins constitute related protein families that function in oxygen transport and storage in humans and other vertebrates. Here we report the identification of a third globin type in man and mouse. This protein is predominantly expressed in the brain, and therefore we have called it neuroglobin. Mouse neuroglobin is a monomer with a high oxygen affinity (half saturation pressure, P50 approximately 2 torr). Analogous to myoglobin, neuroglobin may increase the availability of oxygen to brain tissue. The human neuroglobin gene (NGB), located on chromosome 14q24, has a unique exon-intron structure. Neuroglobin represents a distinct protein family that diverged early in metaz…

Protein familyRecombinant Fusion ProteinsMolecular Sequence DataNeuroglobinNerve Tissue ProteinsBiologyMiceAnimalsHumansGlobinAmino Acid SequenceCloning MolecularChromosomes Human Pair 14Expressed Sequence TagsMice Inbred BALB CMultidisciplinarySequence Homology Amino AcidGene Expression ProfilingCytoglobinOxygen transportNitric oxide dioxygenaseBrainChromosome MappingExonsMolecular biologyIntronsGlobin foldCell biologyGlobinsRespiratory proteinOxygenNeuroglobinNature
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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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7keto-stigmasterol and 7keto-cholesterol induce differential proteome changes to intestinal epitelial (Caco-2) cells

2015

Abstract Recent studies have expanded the appreciation of the roles of oxysterols triggering inflammatory, immune cytotoxic and apoptotic processes, but have not been considered for proteome analysis. A comparative proteomic study in intestinal epithelial cell cultures incubated (60 μM/24 h) with 7keto-cholesterol or 7keto-stigmasterol was performed. The influence of both compounds was studied following the nLC-TripleTOF analysis. Findings were compared to results for control cultures. In the principal component analysis (PCA) of proteome patterns, two components were extracted accounting for 99.8% of the variance in the protein expression. PCA analysis clearly discriminated between the per…

ProteomeStigmasterolInflammationBiologyToxicologyPeptide MappingImmune systemmedicineHumansRNA MessengerKetocholesterolsTranscription factorPrincipal Component AnalysisCell growthGene Expression ProfilingGeneral MedicineOxidantsCell biologyEnterocytesGene Expression RegulationBiochemistryCell cultureApoptosisProteomeMacrophage migration inhibitory factorCaco-2 Cellsmedicine.symptomFood ScienceFood and Chemical Toxicology
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Sub-cellular proteomic analysis of a Medicago truncatula root microsomal fraction

2004

Since the last decade, Medicago truncatula has emerged as one of the model plants particularly investigated in the field of plant-microbe interactions. Several genetic and molecular approaches including proteomics have been developed to increase knowledge about this plant species. To complement the proteomic data, which have mainly focused on the total root proteins from M. truncatula, we carried out a sub-cellular approach to gain access to the total membrane-associated proteins. Following the setting up of the purification process, microsomal proteins were separated on 2-DE. Ninety-six out of the 440 well-resolved proteins were identified by MALDI-TOF peptide mass fingerprinting. A high p…

Proteomics0106 biological sciencesPlant ScienceFractionationHorticultureBiologyProteomicsPeptide MappingPlant Roots01 natural sciencesBiochemistry03 medical and health sciencesSymbiosisPeptide mass fingerprintingBotanyMedicagoElectrophoresis Gel Two-DimensionalSymbiosisMolecular Biology[SDV.BV.PEP] Life Sciences [q-bio]/Vegetal Biology/Phytopathology and phytopharmacyComputingMilieux_MISCELLANEOUSPlant Proteins030304 developmental biology2. Zero hunger0303 health sciencesfungifood and beveragesGeneral Medicinebiology.organism_classificationMedicago truncatula[SDV.BV.PEP]Life Sciences [q-bio]/Vegetal Biology/Phytopathology and phytopharmacyBiochemistryMicrosomePlant speciesProtein identification010606 plant biology & botanyPhytochemistry
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A proteomic approach to studying plant response to crenate broomrape (Orobanche crenata) in pea (Pisum sativum)

2004

Abstract Crenate broomrape ( Orobanche crenata ) is a parasitic plant that threatens legume production in Mediterranean areas. Pea ( Pisum sativum ) is severely affected, and only moderate levels of genetic resistance have so far been identified. In the present work we selected the most resistant accession available (Ps 624) and compared it with a susceptible (Messire) cultivar. Experiments were performed by using pot and Petri dish bioassays, showing little differences in the percentage of broomrape seed germination induced by both genotypes, but a significant hamper in the number of successfully installed tubercles and their developmental stage in the Ps 624 compared to Messire. The prote…

Proteomics0106 biological sciencesSilver StainingGenotypeParasitic plantNitrogen assimilationGene ExpressionPlant ScienceHorticultureOrobanche crenataPeptide MappingPlant Roots01 natural sciencesBiochemistryFructokinasePisum03 medical and health sciencesSativumGlutamine synthetaseElectrophoresis Gel Two-DimensionalDatabases ProteinMolecular Biology[SDV.BV.PEP] Life Sciences [q-bio]/Vegetal Biology/Phytopathology and phytopharmacyComputingMilieux_MISCELLANEOUSPlant Proteins030304 developmental biologyPathogenesis-related protein2. Zero hunger0303 health sciencesbiologyOrobanchePeasGeneral Medicinebiology.organism_classification[SDV.BV.PEP]Life Sciences [q-bio]/Vegetal Biology/Phytopathology and phytopharmacyBiochemistrySpectrometry Mass Matrix-Assisted Laser Desorption-IonizationElectrophoresis Polyacrylamide Gel010606 plant biology & botany
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Do distantly related parasites rely on the same proximate factors to alter the behaviour of their hosts?

2006

Phylogenetically unrelated parasites often increase the chances of their transmission by inducing similar phenotypic changes in their hosts. However, it is not known whether these convergent strategies rely on the same biochemical precursors. In this paper, we explored such aspects by studying two gammarid species ( Gammarus insensibilis and Gammarus pulex ; Crustacea: Amphipoda: Gammaridae) serving as intermediate hosts in the life cycle of two distantly related parasites: the trematode, Microphallus papillorobustus and the acanthocephalan, Polymorphus minutus . Both these parasite species are known to manipulate the behaviour of their amphipod hosts, bringing them towards the water surfa…

Proteomics0106 biological sciences[SDV]Life Sciences [q-bio]MESH : Host-Parasite InteractionsMESH : Behavior Animal[SDV.BID.SPT]Life Sciences [q-bio]/Biodiversity/Systematics Phylogenetics and taxonomyMESH: Peptide Mapping01 natural sciencesAcanthocephalaMESH : ProteomicsMESH: AmphipodatrematodeMESH: Behavior Animal[ SDV.EE.IEO ] Life Sciences [q-bio]/Ecology environment/SymbiosisMESH: AnimalsElectrophoresis Gel Two-DimensionalMESH: PhylogenyPhylogenyComputingMilieux_MISCELLANEOUSGeneral Environmental Science0303 health sciencesMESH : Peptide MappingBehavior AnimalbiologyEcologyMESH : AcanthocephalaMESH: ProteomicsGeneral MedicineMESH : Amphipodamanipulative parasiteMESH : TrematodaMESH: TrematodaMicrophallusTrematodaTrematodagammaridGeneral Agricultural and Biological SciencesAcanthocephalaResearch Article[ SDV.MP.PAR ] Life Sciences [q-bio]/Microbiology and Parasitology/Parasitologymolecular convergenceAmphipodaZoology[ SDV.BBM.BM ] Life Sciences [q-bio]/Biochemistry Molecular Biology/Molecular biologyMESH: Host-Parasite InteractionsPeptide Mapping010603 evolutionary biologyGeneral Biochemistry Genetics and Molecular BiologyHost-Parasite Interactions03 medical and health sciencesproteomicsPhylogeneticsAnimals[SDV.MP.PAR]Life Sciences [q-bio]/Microbiology and Parasitology/ParasitologyAmphipoda030304 developmental biologyGeneral Immunology and MicrobiologyHost (biology)MESH : Phylogeny[SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry Molecular Biology/Molecular biologyMESH : Electrophoresis Gel Two-DimensionalMESH: AcanthocephalaMESH: Electrophoresis Gel Two-Dimensionalbiology.organism_classificationacanthocephalanGammarus pulexPulexMESH : Animals[ SDV.BID.SPT ] Life Sciences [q-bio]/Biodiversity/Systematics Phylogenetics and taxonomy[SDV.EE.IEO]Life Sciences [q-bio]/Ecology environment/Symbiosis
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An organelle-specific protein landscape identifies novel diseases and molecular mechanisms.

2016

Cellular organelles provide opportunities to relate biological mechanisms to disease. Here we use affinity proteomics, genetics and cell biology to interrogate cilia: poorly understood organelles, where defects cause genetic diseases. Two hundred and seventeen tagged human ciliary proteins create a final landscape of 1,319 proteins, 4,905 interactions and 52 complexes. Reverse tagging, repetition of purifications and statistical analyses, produce a high-resolution network that reveals organelle-specific interactions and complexes not apparent in larger studies, and links vesicle transport, the cytoskeleton, signalling and ubiquitination to ciliary signalling and proteostasis. We observe sub…

Proteomics0301 basic medicineSystems AnalysisDNA Mutational Analysislnfectious Diseases and Global Health Radboud Institute for Molecular Life Sciences [Radboudumc 4]General Physics and AstronomyDatasets as Topicmethods [Chromatography Affinity]ProteomicsSensory disorders Donders Center for Medical Neuroscience [Radboudumc 12]Chromatography AffinityMass SpectrometryProtein Interaction Mappingtherapy [Ciliopathies]genetics [Ciliopathies]methods [Molecular Targeted Therapy]Molecular Targeted TherapyProtein Interaction MapsMultidisciplinaryCiliumChemistry (all)Qabnormalities [Spine]pathology [Ciliopathies]genetics [Muscle Hypotonia]therapy [Muscle Hypotonia]Metabolic Disorders Radboud Institute for Molecular Life Sciences [Radboudumc 6]metabolism [Proteins]isolation & purification [Proteins]physiology [Biological Transport]3. Good healthCell biologyVesicular transport proteinpathology [Dwarfism]metabolism [Cilia]Muscle Hypotoniaddc:500pathology [Muscle Hypotonia]pathology [Spine]genetics [Dwarfism]Rare cancers Radboud Institute for Health Sciences [Radboudumc 9]ScienceDwarfismExocystBiologyArticleGeneral Biochemistry Genetics and Molecular BiologyPhysics and Astronomy (all)03 medical and health sciencesIntraflagellar transportCiliogenesisOrganelleHumansCiliaBiochemistry Genetics and Molecular Biology (all)ProteinsBiological TransportGeneral Chemistrytherapy [Dwarfism]Fibroblastsgenetics [Proteins]CiliopathiesSpinemethods [Protein Interaction Mapping]Renal disorders Radboud Institute for Molecular Life Sciences [Radboudumc 11]030104 developmental biologyProteostasisHEK293 Cellsmethods [Proteomics]
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