Search results for " Glycoproteins"

showing 10 items of 329 documents

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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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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Identification of glucan-mannoprotein complexes in the cell wall of Candida albicans using a monoclonal antibody that reacts with a (1,6)- -glucan ep…

1995

The use of a novel monoclonal antibody (mAb) that reacts with (1,6)-beta-glucan has permitted the study of the different covalent linkages between glucan and mannoproteins in the cell wall of Candida albicans. The mAb JRR1 was originally raised by immunization with Zymolyase extracts from C. albicans cell walls, but it soon became apparent that it reacted with a (1,6)-beta-glucan epitope. By using this antibody, we show the existence of glucan-mannoprotein complexes between the (1,6)-beta-glucan epitope recognized by the antibody and cell wall mannoproteins. The topology of the (1,6)-beta-glucan in the cell wall of C. albicans has also been studied.

beta-Glucansmedicine.drug_classFluorescent Antibody Techniquemacromolecular substancesMonoclonal antibodyBinding CompetitiveMicrobiologyChromatography AffinityEpitopeMicrobiologyFungal ProteinsMannansCell wallEpitopesAntigenCell WallPolysaccharidesCandida albicansmedicineCandida albicansGlucansGlucanchemistry.chemical_classificationMembrane GlycoproteinsbiologyTunicamycinAntibodies Monoclonalbiology.organism_classificationCorpus albicanscarbohydrates (lipids)stomatognathic diseaseschemistrybiology.proteinAntibodyMicrobiology
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Role of glycosylation in the incorporation of intrinsic mannoproteins into cell walls of Saccharomyces cerevisiae.

1989

Cell wall mannoproteins from Saccharomyces cerevisiae are completely or partially incorporated into their final location when N-glycosylation is inhibited by tunicamycin. These include a 90–100 kDa species still containing O-linked oligomannose chains, derived from a N-glycosylated material larger than 120 kDa; and a 30.5 kDa peptide lacking mannose residues, derived from a 33 kDa species. For both species, the growth temperature influences the level of incorporation of the non N-glycosylated molecules. Secretion of the peptides lacking N-linked saccharide chains follows the route defined by sec mutants.

chemistry.chemical_classificationGlycosylationGlycosylationMembrane GlycoproteinsTunicamycinSaccharomyces cerevisiaeMannosePeptideTunicamycinSaccharomyces cerevisiaeBiologybiology.organism_classificationMicrobiologyYeastcarbohydrates (lipids)Cell wallchemistry.chemical_compoundchemistryBiochemistryCell WallGeneticsGlycoproteinMolecular BiologyFEMS microbiology letters
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Sulfated and Non-Sulfated Glycopeptide Recognition Domains of P-Selectin Glycoprotein Ligand 1 and their Binding to P- and E-Selectin

2009

Total synthesis through block glycosylation and selective chemical O-sulfation of tyrosine residues yielded the glycopeptide recognition domain A (X=SO(3) (-)) of the P-selectin glycoprotein ligand 1, in which the terminal sialic acid of the complex hexasaccharide side chain was replaced by (S)-cyclohexyl lactic acid. In binding assays the O-sulfated structure A showed high affinity towards P-selectin, the non-sulfated towards E-selectin.

chemistry.chemical_classificationGlycosylationMembrane GlycoproteinsGlycosylationSulfatesStereochemistryGlycopeptidesGeneral ChemistryLigand (biochemistry)CatalysisGlycopeptideProtein Structure TertiarySialic acidMiceP-Selectinchemistry.chemical_compoundProtein structurechemistryBiochemistryAnimalsHumansP-selectin glycoprotein ligand-1TyrosineE-SelectinGlycoproteinAngewandte Chemie International Edition
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Loss of Contact-Dependent Inhibition of Growth in Chemically Transformed Fibroblasts

1988

The plasma membrane has been recognized as an important regulatory unit of mammalian cells during determination, differentiation, and social behaviour of individual cells within various tissues (1–4). On the molecular level, plasma membrane glycoproteins and glycolipids have been shown to be involved in these processes (1–4). Density-dependent growth of non-transformed cells in vitro has been proposed to be regulated by secreted inhibitory compounds (5–7), by the cell’s shape (8) or by diffusion boundary layers (9). On the other hand, specific cell-cell interactions via cell membrane molecules were found to be of great importance for the contact-dependent inhibition of growth (10–16) and co…

chemistry.chemical_classificationGlycosylationbiologyChemistryGlycoconjugateCellIn vitroCell biologyCell membraneMembrane glycoproteinschemistry.chemical_compoundmedicine.anatomical_structureGlycolipidmedicinebiology.proteinGlycoprotein
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Wall mannoproteins of the yeast and mycelial cells of Candida albicans: nature of the glycosidic bonds and polydispersity of their mannan moieties.

1988

SUMMARY: Zymolyase released between 20 and 25% of the total protein from purified walls of yeast (Y) and mycelial (M) cells of Candida albicans. The material released contained 92% carbohydrate (86% mannose and 6% glucose) and 7:< protein. Over 85% of the carbohydrate was N-glycosidically linked to the protein and the rest (less than 15%) was linked O-glycosidically. Highly polydisperse, high molecular mass mannoproteins, resolved by electrophoresis as four defined bands in Y cells and two bands in M cells, had both types of sugar chains. A 34 kDa species found in both types of cells had a single 2.5 kDa N-glycosidically linked sugar chain and a 3 1.5 kDa protein moiety. Polydispersity in t…

chemistry.chemical_classificationMembrane GlycoproteinsMolecular massbiologyHydrolasesProtoplastsMannoseGlycosidic bondCarbohydratebiology.organism_classificationMicrobiologyMolecular biologyYeastCell wallFungal ProteinsMannanschemistry.chemical_compoundchemistryBiochemistryCell WallCandida albicansChromatography GelGlycosidesCandida albicansMannanJournal of general microbiology
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Structural mannoproteins released by β-elimination fromCandida albicanscell walls

1994

Abstract Mild alkaline solutions (β-elimination), after removing the non-covalently bonded wall materials by hot SDS, released 13% and 26% of remaining wall proteins from mycelial and yeast cells of Candida albicans, respectively. When the β-elimination was carried out after digestion of the walls with chitinase, four-fold more proteinaceous materials were released from mycelium and a similar amount in yeast walls. The solubilized materials were shown to be highly polydisperse, and endo-glycosidase H reduced their polydispersity and molecular masses, revealing different electrophoretic patterns in yeast and mycelial cell walls. The solubilized mycelial proteins carried N-glycosidic sugar ch…

chemistry.chemical_classificationMembrane GlycoproteinsbiologyHydrolasesProtein HydrolysatesChitinasesAntibodies MonoclonalHydrogen-Ion Concentrationbiology.organism_classificationMicrobiologyCorpus albicansYeastCell wallchemistryBiochemistryCell WallCandida albicansChitinaseGeneticsbiology.proteinGlycoside hydrolaseCandida albicansGlycoproteinMolecular BiologyMyceliumFEMS Microbiology Letters
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Membrane oligo- and polysialic acids

2011

AbstractPolysialic acid (polySia) and oligosialic acid (oligoSia) chains are linear polysaccharides composed of sialic acid monomers. The majority of biological poly/oligoSia chains are bound to membranes. There is a large diversity of membrane poly/oligoSia in terms of chain length, occurrence, biological function, and the mode of membrane attachment. Poly/oligoSia can be anchored to a membrane via a phospholipid (polySia in bacteria), a glycosphingolipid (oligoSia in gangliosides), an integral membrane glycoprotein, or a glycoprotein attached to a membrane via glycosylphosphatidylinositol. In eukaryotic cells, the attachment of a poly/oligoSia chain to the membrane anchor is usually throu…

chemistry.chemical_classificationPolysialic acidCell MembranePeripheral membrane proteinBiophysicsBiological membraneCell BiologyBiologyPolysialic acidBiochemistrySurface pHMembrane glycoproteinsBiopolymersMembranechemistryMembrane proteinBiochemistryGangliosideSialic Acidsbiology.proteinCapsular polysaccharideNCAMGlycoproteinIntegral membrane proteinMembrane potentialBiochimica et Biophysica Acta (BBA) - Biomembranes
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