Search results for "recombinant"

showing 10 items of 1150 documents

Influence of hydrophobic matching on association of model transmembrane fragments containing a minimised glycophorin A dimerisation motif

2005

AbstractThe principles that govern the folding and packing of membrane proteins are still not completely understood. In the present work, we have revisited the glycophorin A (GpA) dimerisation motif that mediates transmembrane (TM) helix association, one of the best-suited models of membrane protein oligomerisation. By using artificial polyleucine TM segments we have demonstrated in this study that a pattern of only five amino acids (GVxxGVxxT) promotes specific dimerisation. Further, we have used this minimised GpA motif to assess the influence of hydrophobic matching on the TM helix packing process in detergent micelles and found that this factor modulates helix–helix association and/or d…

Protein FoldingRecombinant Fusion ProteinsAmino Acid MotifsMolecular Sequence DataBiophysicsBiochemistryMicelleHydrophobic mismatchHydrophobic mismatchStructural BiologyLeucineHelix packingGeneticsGlycophorinAnimalsHumansAmino Acid SequenceGlycophorinsMolecular BiologyPolyacrylamide gel electrophoresischemistry.chemical_classificationbiologyChemistryGlycophorin AProteïnes de membranaMembrane ProteinsMembrane protein associationCell BiologyTransmembrane proteinAmino acidTransmembrane domainBiochemistryMembrane proteinMutationTransmembrane helixBiophysicsbiology.proteinPeptidesDimerizationHydrophobic and Hydrophilic Interactions
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BAG3 mediates chaperone-based aggresome-targeting and selective autophagy of misfolded proteins.

2010

Increasing evidence indicates the existence of selective autophagy pathways, but the manner in which substrates are recognized and targeted to the autophagy system is poorly understood. One strategy is transport of a particular substrate to the aggresome, a perinuclear compartment with high autophagic activity. In this paper, we identify a new cellular pathway that uses the specificity of heat-shock protein 70 (Hsp70) to misfolded proteins as the basis for aggresome-targeting and autophagic degradation. This pathway is regulated by the stress-induced co-chaperone Bcl-2-associated athanogene 3 (BAG3), which interacts with the microtubule-motor dynein and selectively directs Hsp70 substrates …

Protein FoldingRecombinant Fusion ProteinsDyneinGreen Fluorescent ProteinsAggrephagyMice TransgenicBAG3BiochemistryMiceJUNQ and IPODChlorocebus aethiopsGeneticsAutophagyAnimalsHumansPoint MutationHSP70 Heat-Shock ProteinsMolecular BiologyAdaptor Proteins Signal TransducingSequence DeletionInclusion BodiesMotor NeuronsbiologySuperoxide DismutaseAutophagyScientific ReportsDyneinsTransport proteinCell biologyProtein TransportAggresomeHEK293 CellsSpinal CordChaperone (protein)COS Cellsbiology.proteinApoptosis Regulatory ProteinsProteasome InhibitorsEMBO reports
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A Membrane-Bound Vertebrate Globin

2011

The family of vertebrate globins includes hemoglobin, myoglobin, and other O(2)-binding proteins of yet unclear functions. Among these, globin X is restricted to fish and amphibians. Zebrafish (Danio rerio) globin X is expressed at low levels in neurons of the central nervous system and appears to be associated with the sensory system. The protein harbors a unique N-terminal extension with putative N-myristoylation and S-palmitoylation sites, suggesting membrane-association. Intracellular localization and transport of globin X was studied in 3T3 cells employing green fluorescence protein fusion constructs. Both myristoylation and palmitoylation sites are required for correct targeting and m…

Protein StructureLipoylationGreen Fluorescent ProteinsMolecular Sequence Datalcsh:MedicineHemeBiochemistryCell membranechemistry.chemical_compoundModel OrganismsPalmitoylationhemic and lymphatic diseasesmedicineAnimalsRespiratory functionAmino Acid SequenceGlobinlcsh:ScienceProtein InteractionsBiologyZebrafishZebrafishMyristoylationHemoproteinsMultidisciplinarySequence Homology Amino Acidbiologylcsh:RCell MembraneMembrane ProteinsProteinsGene Expression Regulation DevelopmentalAnimal Modelsbiology.organism_classificationRecombinant ProteinsGlobinsGlobin foldOxygenmedicine.anatomical_structureBiochemistryMyoglobinchemistryImmunoglobulin GCytochemistrylcsh:QRabbitsResearch ArticleSubcellular FractionsPLoS ONE
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Different protein turnover of interleukin-6-type cytokine signalling components.

1999

Interleukin (IL)-6 and IL-6-type cytokines signal through the gp130/Jak/STAT signal transduction pathway. The key components involved are the signal transducing receptor subunit gp130, the Janus kinases Jak1, Jak2 and Tyk2, STAT1 and STAT3 of the family of signal transducers and activators of transcription, the protein tyrosine phosphatase SHP2 and the suppressors of cytokine signalling SOCS1, SOCS2 and SOCS3. Whereas considerable information has been accumulated concerning the time-course of activation for the individual signalling molecules, data on the availability of the proteins involved in IL-6-type cytokine signal transduction are scarce. Nevertheless, availability of these molecules…

Protein Tyrosine Phosphatase Non-Receptor Type 11Protein tyrosine phosphataseBiologyBiochemistrySuppressor of cytokine signallingAntigens CDCytokine Receptor gp130Membrane GlycoproteinsSuppressor of cytokine signaling 1Interleukin-6Protein Tyrosine Phosphatase Non-Receptor Type 6Intracellular Signaling Peptides and ProteinsJAK-STAT signaling pathwaySignal transducing adaptor proteinSTAT2 Transcription FactorProtein-Tyrosine KinasesGlycoprotein 130Recombinant ProteinsCell biologyDNA-Binding ProteinsSTAT1 Transcription FactorBiochemistryTrans-ActivatorsCytokinesSignal transductionProtein Tyrosine PhosphatasesJanus kinaseHalf-LifeSignal TransductionEuropean journal of biochemistry
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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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Recombinant functional multidomain hemoglobin from the gastropod Biomphalaria glabrata

2011

The extracellular hemoglobin multimer of the planorbid snail Biomphalaria glabrata, intermediate host of the human parasite Schistosoma mansoni, is presumed to be a 1.44 MDa complex of six 240 kDa polypeptide subunits, arranged as three disulfide-bridged dimers. The complete amino acid sequence of two subunit types (BgHb1 and BgHb2), and the partial sequence of a third type (BgHb3) are known. Each subunit encompasses 13 paralogus heme domains, and N-terminally a smaller plug domain responsible for subunit dimerization. We report here the recombinant expression of different functional fragments of BgHb2 in Escherichia coli, and of the complete functional subunits BgHb1 and BgHb2 in insect ce…

Protein subunitClinical BiochemistryCooperativitymedicine.disease_causeBiochemistrylaw.inventionHemoglobinschemistry.chemical_compoundlawGeneticsmedicineAnimalsHumansBiomphalaria glabrataProtein Structure QuaternaryMolecular BiologyEscherichia coliPeptide sequenceHemeBiomphalariabiologySchistosoma mansoniCell Biologybiology.organism_classificationRecombinant ProteinsOxygenProtein SubunitsBiochemistrychemistryRecombinant DNAOxygen bindingIUBMB Life
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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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Differential proteomic analysis of an engineered Streptomyces coelicolor strain reveals metabolic pathways supporting growth on n-hexadecane

2012

The alkB gene, encoding an alkane monooxygenase in the actinomycete Gordonia sp. SoCg, was expressed in the non-alkane-degrading actinomycete Streptomyces coelicolor M145. The resulting engineered strain, M145-AH, can grow on n-hexadecane as sole carbon source. To unravel proteins associated with growth on n-alkanes, proteome of M145-AH after 6, 24, and 48 h of incubation in the Bushnell-Haas (BH) mineral medium containing n-hexadecane as sole carbon source (H condition) and in BH without any carbon source (0 condition) were compared using 2D-differential gel electrophoresis. Proteome analysis revealed significant changes only at 48 h, showing 48 differentially abundant proteins identified …

ProteomicsProteomeAlkBProtein metabolismGene ExpressionStreptomyces coelicolorSettore BIO/19 - Microbiologia GeneraleProteomicsApplied Microbiology and BiotechnologyStreptomyceschemistry.chemical_compoundAlkanesElectrophoresis Gel Two-DimensionalbiologyStreptomyces coelicolorProteomicGeneral MedicineMetabolism2d-dige analysisMembrane transportbiology.organism_classificationCarbonRecombinant ProteinsStreptomycesCulture MediaN-alkane monoxygenaseStreptomyceN-hexadecane utilizationchemistryBiochemistryEngineered strainProteomebiology.protein2D-DIGE analysiCytochrome P-450 CYP4AMetabolic Networks and PathwaysBiotechnologyApplied Microbiology and Biotechnology
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Strategies for the production of difficult-to-express full-length eukaryotic proteins using microbial cell factories : production of human alpha-gala…

2015

This work was supported by ERANET-IB08-007 project from the European Union and its linked national project EUI2008- 03610 to AV. We also appreciate the support from EME2007-08 to NFM from Universitat Autonoma de Barcelona, from Antartide 2010 to MLT and EP, from MIUR Azioni Integrate Italia-Spagna 2010 Prot. IT10LECLM9 to MLT, from MINECO (IT2009-0021) to AV and LT, from AGAUR (2009SGR-108) to AV. AV is also supported by The Biomedical Research Networking Center in Bioengineering, Biomaterials and Nanomedicine (CIBER-BBN, Spain), an initiative funded by the VI National R&D&i Plan 2008-2011, Iniciativa Ingenio 2010, Consolider Program, CIBER Actions and financed by the Instituto de Salud Car…

PseudoalteromonaRecombinant proteinExpression systemsFabry's diseaseHuman alpha-galactosidase AContext (language use)Computational biologyBiologymedicine.disease_causeApplied Microbiology and BiotechnologyMicrobiologyPseudoalteromonas haloplanktisGene expressionEnzyme StabilitymedicineProtein biosynthesisEscherichia coliHumansEscherichia coliGenePseudoalteromonas haloplanktis TAC125Expression systemGeneral Medicinebiology.organism_classificationRecombinant ProteinsPseudoalteromonasMembrane proteinFabry’s diseaseMetabolic Engineeringalpha-GalactosidaseProtein foldingBiotechnologyHuman
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An open-label, prospective phase I/II study evaluating the immunogenicity and safety of a ras peptide vaccine plus GM-CSF in patients with non-small …

2007

Mutations of the ras gene have been reported in 20-40% of NSCLC patients. If present, they are critical for the malignant phenotype of these tumors. Therefore, targeting them by specific vaccination is a promising therapeutic approach. In a clinical trial we screened for ras mutations in patients with NSCLC. Patients with ras-positive tumors were immunized six times intradermally with a mixture of seven peptides representing the most common ras mutations. Objectives of the study were the feasibility, efficacy and safety of the vaccination. In addition, the induction of a specific immune reaction was investigated by DTH tests, and the induction of peptide-specific T cells was tested in ex vi…

Pulmonary and Respiratory MedicineOncologyMaleCancer Researchmedicine.medical_specialtyLung Neoplasmsmedicine.medical_treatmentT-LymphocytesCancer VaccinesImmune systemInternal medicineCarcinoma Non-Small-Cell LungCarcinomaMedicineHumansLung cancerCodonAgedNeoplasm StagingImmunity Cellularbusiness.industryImmunogenicityRas PeptideVaccinationGranulocyte-Macrophage Colony-Stimulating FactorImmunotherapyMiddle Agedmedicine.diseaseCombined Modality TherapyPeptide FragmentsRecombinant ProteinsVaccinationOncologyImmunologyMutationras ProteinsFemaleImmunotherapybusinessEx vivoLung cancer (Amsterdam, Netherlands)
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