Search results for "glycoprotein"

showing 10 items of 852 documents

Calcium-dependent conformational changes of membrane-bound Ebola fusion peptide drive vesicle fusion

2003

AbstractThe fusogenic subdomain of the Ebola virus envelope glycoprotein is an internal sequence located ca. 20 residues downstream the N-terminus of the glycoprotein transmembrane subunit. Partitioning of the Ebola fusion peptide into membranes containing phosphatidylinositol in the absence of Ca2+ stabilizes an α-helical conformation, and gives rise to vesicle efflux but not vesicle fusion. In the presence of millimolar Ca2+ the membrane-bound peptide adopts an extended β-structure, and induces inter-vesicle mixing of lipids. The peptide conformational polymorphism may be related to the flexibility of the virus–cell intermembrane fusogenic complex.

Vesicle fusionEbola glycoproteinSpectrophotometry InfraredProtein ConformationvirusesBiophysicsPeptideBiologymedicine.disease_causePhosphatidylinositolsBiochemistryMembrane FusionProtein Structure Secondarychemistry.chemical_compoundProtein structureFusion peptideMembranes (Biologia)Structural BiologyGeneticsmedicinePhosphatidylinositolMolecular Biologychemistry.chemical_classificationEbola virusVesicleCircular DichroismLipid bilayer fusionViral fusionWaterMembranes ArtificialCell BiologyEbolavirusLipidsTransmembrane proteinPeptide FragmentsBiochemistrychemistryLiposomesBiophysicsCalciumPèptidsPeptide–lipid interactionViral Fusion Proteins
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Tissue expression of the vesicle protein pantophysin

1999

The cell-type restricted expression of cytoplasmic microvesicle membrane protein isoforms may be a consequence of the functional adaptation of these vesicles to the execution of specialized processes in cells of different specialization. To characterize the expression of the vesicle protein pantophysin, an isoform of the synaptic vesicle proteins synaptophysin and synaptoporin, we have prepared and characterized antibodies useful for the immunological detection of pantophysin in vitro and in situ. Using these reagents, we show by immunoblot analyses that pantophysin expression is not homogeneous but differs significantly between various bovine tissues. Furthermore, these differences are not…

Vesicle-associated membrane protein 8Membrane GlycoproteinsHistologySynaptobrevinMicrovesicleMembrane ProteinsSNAP25Cell BiologySynaptoporinBiologyCytoplasmic GranulesMolecular biologyPathology and Forensic MedicineCell biologyR-SNARE ProteinsVesicle-associated membrane proteinMembrane proteinOrgan SpecificitySynaptophysinbiology.proteinAnimalsProtein IsoformsCattleCarrier ProteinsFluorescent Antibody Technique IndirectCell and Tissue Research
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Sec61alpha and TRAM are Sequentially Adjacent to a Nascent Viral Membrane Protein during its ER Integration

2007

Co-translational integration of a nascent viral membrane protein into the endoplasmic reticulum membrane takes place via the translocon. We have been studying the early stages of the integration of a double-spanning plant viral movement protein to gain insights into how viral membrane proteins are transferred from the hydrophilic interior of the translocon into the hydrophobic environment of the bilayer, where the transmembrane (TM) segments of the viral proteins can diffuse freely. Photocrosslinking experiments reveal that this integration involves the sequential passage of the TM segments past Sec61alpha and translocating chain-associating membrane protein (TRAM). Each TM segment is first…

Virus IntegrationBiologyEndoplasmic ReticulumModels BiologicalViral Matrix ProteinsDogsMembranes (Biologia)Structural BiologyAnimalsRNA MessengerMolecular BiologyVirus IntegrationMembrane GlycoproteinsViral matrix proteinEndoplasmic reticulumProteïnes de membranaMembrane ProteinsViral membraneTransloconTransmembrane proteinCell biologyPlant Viral Movement ProteinsCross-Linking ReagentsMembrane proteinBiochemistrySEC Translocation ChannelsSEC Translocation ChannelsMolecular Chaperones
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Regeneration of the cell wall in protoplasts of Candida albicans. A cytochemical study using wheat germ agglutinin and concanavalin A.

1988

To assess the dynamics of synthesis of the wall by regenerating Candida albicans protoplasts deposition of chitin and mannoproteins were investigated ultrastructurally using wheat germ agglutinin conjugated with either horseradish peroxidase or colloidal gold, and Concanavalin A coupled to ferritin respectively. Freshly prepared protoplasts lacked wheat germ agglutinin receptor sites but after 1-2 h of regeneration, they were detected. After 4-5 h of regeneration, the cell wall showed a discrete structure which was only labelled with wheat germ agglutinin in thin sections. At this stage of regeneration the outermost layer of the wall was labelled with clusters of Concanavalin A-ferritin par…

Wheat Germ AgglutininsChitinBiochemistryMicrobiologyHorseradish peroxidaseCell wallchemistry.chemical_compoundChitinCell WallCandida albicansGeneticsConcanavalin AColloidsCandida albicansMolecular BiologyGlucanGlycoproteinschemistry.chemical_classificationMembrane GlycoproteinsbiologyHistocytochemistryProtoplastsGeneral MedicineProtoplastbiology.organism_classificationWheat germ agglutininMicroscopy ElectronchemistryBiochemistryConcanavalin AFerritinsbiology.proteinGoldArchives of microbiology
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Toward the Identification of Two Glycoproteins Involved in the Stomatal Deregulation of Downy Mildew–Infected Grapevine Leaves

2015

SPE Pôle IPM UB; International audience; Stomata remain abnormally opened and unresponsive to abscisic acid in grapevine leaves infected by downy mildew. This deregulation occurs from 3 days post inoculation and increases concomitantly with leaf colonization by the pathogen. Using epidermal peels, we demonstrated that the active compound involved in this deregulation is located in the apoplast. Biochemical assays showed that the active compound present in the apoplastic fluids isolated from Plasmopara viticola infected grapevine leaves (IAF) is a CysCys bridge-independent, thermostable and glycosylated protein. Fractionation guided assays based on chromatography / stomatal response and prot…

[SDE] Environmental SciencesProteomicsPhysiology[SDV]Life Sciences [q-bio]stomataMolecular Sequence DataPlant EpidermisFungal ProteinsCell wallPlasmoparaPlasmopara viticolachemistry.chemical_compoundCell WallBotany[SDV.BV]Life Sciences [q-bio]/Vegetal Biology[SDV.BV] Life Sciences [q-bio]/Vegetal BiologyComputer SimulationVitisAmino Acid SequencePathogenAbscisic acidPhylogenyproteomicGlycoproteinsPlant DiseasesPlant Proteinsplant-microbe interactionFungal proteinSequence Homology Amino AcidbiologyfungiPlant Stomatafood and beveragesGeneral MedicineChromatography Ion Exchangebiology.organism_classificationApoplast[SDV] Life Sciences [q-bio]Plant LeavesOomycetesBiochemistrychemistryVitis viniferaHost-Pathogen InteractionsPlant Stomata[SDE]Environmental SciencesDowny mildewguard cellAgronomy and Crop ScienceMolecular Plant-Microbe Interactions®
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Population Structure and Comparative Genome Hybridization of European Flor Yeast Reveal a Unique Group of Saccharomyces cerevisiae Strains with Few G…

2014

Wine biological aging is a wine making process used to produce specific beverages in several countries in Europe, including Spain, Italy, France, and Hungary. This process involves the formation of a velum at the surface of the wine. Here, we present the first large scale comparison of all European flor strains involved in this process. We inferred the population structure of these European flor strains from their microsatellite genotype diversity and analyzed their ploidy. We show that almost all of these flor strains belong to the same cluster and are diploid, except for a few Spanish strains. Comparison of the array hybridization profile of six flor strains originating from these four co…

[SDV.SA]Life Sciences [q-bio]/Agricultural scienceslcsh:MedicineArray CGHespagneyeastbrewer sGenomeComputational biologyPloidymicrobial floraGene DuplicationGenotypevinCluster Analysissaccharomyces cerevisiaelcsh:SciencePhylogenySequence DeletionGenetics0303 health sciencesComparative Genomic HybridizationMultidisciplinaryVegetal BiologyMembrane GlycoproteinsEcologyAlcoholic BeveragesMicrobial GeneticshongrieGenomicsBiodiversityAgricultural sciencesoenologieMicrosatellitePloidyGenome FungalgénotypefranceResearch ArticleSaccharomyces cerevisiae ProteinsMolecular Sequence DataFlorflore microbiennevieillissement vinBiologyMicrobiologyMicrobial EcologyBeverages03 medical and health sciencesSaccharomycesGenetic variationGenetics[SDV.BV]Life Sciences [q-bio]/Vegetal BiologyAmino Acid Sequencewinemicrobiologie030304 developmental biologyNutritionComparative genomicsWineEvolutionary BiologyBase SequenceBiology and life sciences030306 microbiologylcsh:ROrganismsFungiGenetic VariationGenome analysisDietitalieGenetic LociBiofilmsGenetic Polymorphismlcsh:QSequence AlignmentSciences agricolesBiologie végétalePopulation GeneticsMicrosatellite Repeats
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Cloning and Targeted Deletion of the Mouse Fetuin Gene

1998

We proposed that the alpha2-Heremans Schmid glycoprotein/fetuin family of serum proteins inhibits unwanted mineralization. To test this hypothesis in animals, we cloned the mouse fetuin gene and generated mice lacking fetuin. The gene consists of seven exons and six introns. The cystatin-like domains D1 and D2 of mouse fetuin are encoded by three exons each, whereas a single terminal exon encodes the carboxyl-terminal domain D3. The promoter structure is well conserved between rat and mouse fetuin genes within the regions shown to bind transcription factors in the rat system. Expression studies demonstrated that mice homozygous for the gene deletion lacked fetuin protein and that mice heter…

alpha-2-HS-GlycoproteinMolecular Sequence DataBiologyBiochemistryMiceEctopic calcificationExonCalcification PhysiologicApatitesmedicineAnimalsCloning MolecularPromoter Regions GeneticMolecular BiologyGeneMice Knockoutchemistry.chemical_classificationBase SequenceIntronBlood ProteinsSequence Analysis DNACell Biologymedicine.diseaseNull alleleMolecular biologyFetuinRatschemistryFemalealpha-FetoproteinsGlycoproteinalpha-2-HS-glycoproteinGene DeletionJournal of Biological Chemistry
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Rat tyrosine kinase inhibitor shows sequence similarity to human α2-HS glycoprotein and bovine fetuin

1991

Human alpha 2-HS glycoprotein and bovine fetuin, abundant proteins of fetal plasma, are structural members of the fetuin family within the cystatin superfamily. They are characterized by the presence of two N-terminally located cystatin-like units and a unique C-terminal sequence segment not present in the other members of the cystatin superfamily. Search for related sequences revealed that the natural inhibitor of the insulin receptor tyrosine kinase [Auberger, Falquerho, Contreres, Pages, Le Cam, Rossi & Le Cam (1989) Cell (Cambridge, Mass.) 58, 631-640] shows sequence similarity to the mammalian fetuins. The sequence identity between rat tyrosine kinase inhibitor, human alpha 2-HS gl…

alpha-2-HS-Glycoproteinmedicine.drug_classMolecular Sequence DataBiochemistryTyrosine-kinase inhibitorReceptor tyrosine kinaseHomology (biology)Protein structureSequence Homology Nucleic AcidmedicineAnimalsHumansAmino Acid SequenceMolecular Biologychemistry.chemical_classificationbiologyBlood ProteinsCell BiologyProtein-Tyrosine KinasesMolecular biologyFetuinRatschemistryBiochemistrybiology.proteinCattlealpha-FetoproteinsGlycoproteinSequence Alignmentalpha-2-HS-glycoproteinResearch ArticleCysteineBiochemical Journal
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Procollagen C-proteinase Enhancer Stimulates Procollagen Processing by Binding to the C-propeptide Region Only*

2011

Background: Procollagen C-proteinase enhancer-1 (PCPE-1) is an extracellular glycoprotein that increases activity of certain zinc metalloproteinases involved in tissue development and repair. Results: PCPE-1 binds uniquely to the C-propeptide region of the procollagen molecule. Conclusion: PCPE-1 enhances proteolysis by binding solely to the procollagen C-propeptides. Significance: These data may lead to future applications in the development of antifibrotic therapies.

animal structuresGlycosylationBiologyBiochemistryBone morphogenetic protein 1Protein Structure SecondaryBone Morphogenetic Protein 103 medical and health scienceschemistry.chemical_compoundMetalloprotease0302 clinical medicineHumansBinding siteEnhancerMolecular Biology030304 developmental biologyCell Line TransformedGlycoproteinschemistry.chemical_classification0303 health sciencesMetalloproteinaseExtracellular Matrix ProteinsBinding Sitesintegumentary systemCell BiologyEnzymatic ProcessingFibrosisExtracellular MatrixProcollagen peptidaseCollagen Type IIIchemistryBiochemistry030220 oncology & carcinogenesisembryonic structuresEnzymologyCollagenGlycoproteinProtein Processing Post-TranslationalTriple helixThe Journal of Biological Chemistry
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Clinical and MRI measures to identify non-acute MOG-antibody disease in adults

2022

Abstract MRI and clinical features of myelin oligodendrocyte glycoprotein (MOG)-antibody disease may overlap with those of other inflammatory demyelinating conditions posing diagnostic challenges, especially in non-acute phases and when serologic testing for MOG antibodies is unavailable or shows uncertain results. We aimed to identify MRI and clinical markers that differentiate non-acute MOG-antibody disease from aquaporin 4 (AQP4)-antibody neuromyelitis optica spectrum disorder and relapsing remitting multiple sclerosis, guiding in the identification of patients with MOG-antibody disease in clinical practice. In this cross-sectional retrospective study, data from 16 MAGNIMS centres were i…

aquaporin 4-antibody positive neuromyelitis optica spectrum disorder; differential diagnosis; imaging; multiple sclerosis; myelin oligodendrocyte glycoprotein antibody-associated diseaseaquaporin 4-antibody positive neuromyelitis optica spectrum disordermyelin oligodendrocyte glycoprotein antibody-associated diseasedifferential diagnosisimagingNeurology (clinical)multiple sclerosis
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