Search results for "carbohydrates"

showing 10 items of 474 documents

N-Glycosyl Amides as Glycosyl Donors in Stereoselective Glycosylation Reactions

2004

Due to their high stability, N-glycosyl amides have so far not been considered as glycosyl donors for glycosylation reactions. Two new procedures for the cleavage of the anomeric amide functionality under mild reaction conditions and further stereoselective in situ conversions of the activated glycosyl donors with alcohols and amines to give β-configured O- and N-glycosides are described in this article.

Reaction conditionsanimal structuresAnomerGlycosylationStereochemistryChemical glycosylationOrganic ChemistryGeneral Medicinemacromolecular substancesCleavage (embryo)Koenigs–Knorr reactionCatalysiscarbohydrates (lipids)chemistry.chemical_compoundchemistryAmidelipids (amino acids peptides and proteins)GlycosylStereoselectivityGlycosyl donorSynthesis
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m6A RNA methylation regulates promoter proximal pausing of RNA Polymerase II

2021

AbstractRNA Polymerase II (RNAP II) pausing is essential to precisely control gene expression and is critical for development of metazoans. Here, we show that the m6A RNA modification regulates promoter-proximal RNAP II pausing. The m6A methyltransferase complex (MTC), with the nuclear reader Ythdc1, are recruited to gene promoters. Depleting the m6A MTC leads to a decrease in RNAP II pause release and in Ser2P occupancy on the gene body, and affects nascent RNA transcription. Tethering Mettl3 to a heterologous gene promoter is sufficient to increase RNAP II pause release, an effect that relies on its m6A catalytic domain. Collectively, our data reveal an important link between RNAP II paus…

Regulation of gene expression0303 health sciencesbiologyRNA methylationChemistryMethyltransferase complex[SDV]Life Sciences [q-bio]030302 biochemistry & molecular biologyHeterologousRNA polymerase IIPromoterCell BiologyCell biology[SDV] Life Sciences [q-bio]enzymes and coenzymes (carbohydrates)03 medical and health sciencesGene expressionbiology.proteinbacteriaMolecular BiologyGeneComputingMilieux_MISCELLANEOUS030304 developmental biology
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DICER and ZRF1 contribute to chromatin decondensation during nucleotide excision repair

2016

Abstract Repair of damaged DNA relies on the recruitment of DNA repair factors in a well orchestrated manner. As a prerequisite, the chromatin needs to be decondensed by chromatin remodelers to allow for binding of repair factors and for DNA repair to occur. Recent studies have implicated members of the SWI/SNF and INO80 families as well as PARP1 in nucleotide excision repair (NER). In this study, we report that the endonuclease DICER is implicated in chromatin decondensation during NER. In response to UV irradiation, DICER is recruited to chromatin in a ZRF1-mediated manner. The H2A–ubiquitin binding protein ZRF1 and DICER together impact on the chromatin conformation via PARP1. Moreover, …

Ribonuclease III0301 basic medicineDNA RepairUltraviolet RaysDNA damageDNA repairgenetic processesPoly (ADP-Ribose) Polymerase-1Genome Integrity Repair and ReplicationBiologyChromatin remodelingCell LineDEAD-box RNA HelicasesHistones03 medical and health scienceschemistry.chemical_compoundUbiquitinCell Line TumorGeneticsAnimalsHumansCaenorhabditis elegansOncogene ProteinsOsteoblastsUbiquitinfungiRNA-Binding ProteinsFibroblastsChromatin Assembly and DisassemblyMolecular biologyChromatinChromatinDNA-Binding Proteinsenzymes and coenzymes (carbohydrates)HEK293 Cells030104 developmental biologychemistrybiology.proteinDNADNA DamageMolecular ChaperonesNucleotide excision repairDicerNucleic Acids Research
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Blockage of cell wall receptors for yeast killer toxin KT28 with antimannoprotein antibodies.

1990

Binding of yeast killer toxin KT28 to its primary cell wall receptor was specifically blocked with polyclonal antimannoprotein antibodies which masked all toxin-binding sites on the surface of sensitive yeast cells. By indirect immunofluorescence, it was shown that KT28 binds to the cell wall mannoprotein and that the toxin resistance of mannoprotein mutants (mnn) of Saccharomyces cerevisiae was due to a lack of killer toxin-binding sites within the yeast cell wall. Structural analysis of acetylated mannoprotein from KT28-resistant mutant strains identified the outer mannotriose side chains as the actual killer toxin-binding domains.

Saccharomyces cerevisiae ProteinsMutantSaccharomyces cerevisiaeFluorescent Antibody TechniqueSaccharomyces cerevisiaeBiologymedicine.disease_causeAntibodiesCell wallCell WallmedicinePharmacology (medical)ReceptorPharmacologyMembrane GlycoproteinsToxinMycotoxinsbiology.organism_classificationYeastKiller Factors YeastCell biologycarbohydrates (lipids)Infectious DiseasesBiochemistryPolyclonal antibodiesbiology.proteinAntibodyResearch Article
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Molecular structure of the cell wall receptor for killer toxin KT28 in Saccharomyces cerevisiae

1988

The adsorption of the yeast killer toxin KT28 to susceptible cells of Saccharomyces cerevisiae was prevented by concanavalin A, which blocks the mannoprotein receptor. Certain mannoprotein mutants of S. cerevisiae that lack definite structures in the mannan of their cell walls were found to be resistant to KT28, whereas the wild-type yeast from which the mutants were derived was susceptible. Isolated mannoprotein from a resistant mutant was unable to adsorb killer toxin. By comparing the resistances of different mannoprotein mutants, information about the molecular structure of the receptor was obtained. At least two mannose residues have to be present in the side chains of the outer chain …

Saccharomyces cerevisiae ProteinsMutantSaccharomyces cerevisiaeMannoseReceptors Cell Surfacechemical and pharmacologic phenomenaSaccharomyces cerevisiaeSpheroplastsMicrobiologyFungal Proteinschemistry.chemical_compoundCell WallConcanavalin AReceptorMolecular BiologyGlycoproteinsMannanMembrane GlycoproteinsbiologyMycotoxinsSpheroplastbiology.organism_classificationKiller Factors YeastYeastcarbohydrates (lipids)BiochemistrychemistryConcanavalin AMutationbiology.proteinAdsorptionResearch ArticleJournal of Bacteriology
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The yeast histone acetyltransferase A2 complex, but not free Gcn5p, binds stably to nucleosomal arrays.

2000

We have investigated the structural basis for the differential catalytic function of the yeast Gcn5p-containing histone acetyltransferase (HAT) A2 complex and free recombinant yeast Gcn5p (rGcn5p). HAT A2 is shown to be a unique complex that contains Gcn5p, Ada2p, and Ada3p, but not proteins specific to other related HAT A complexes, e.g. ADA, SAGA. Nevertheless, HAT A2 produces the same unique polyacetylation pattern of nucleosomal substrates reported previously for ADA and SAGA, demonstrating that proteins specific to the ADA and SAGA complexes do not influence the enzymatic activity of Gcn5p within the HAT A2 complex. To investigate the role of substrate interactions in the differential …

Saccharomyces cerevisiae ProteinsSaccharomyces cerevisiaeBiologyBiochemistrySubstrate SpecificityFungal ProteinsHistonesTetramerAcetyl Coenzyme AAcetyltransferasesparasitic diseasesCentrifugation Density GradientAnimalsMolecular BiologyHistone Acetyltransferaseschemistry.chemical_classificationSubstrate (chemistry)AcetylationCell BiologyHistone acetyltransferaseYeastChromatinRecombinant ProteinsTrypsinizationNucleosomesN-terminusDNA-Binding Proteinsenzymes and coenzymes (carbohydrates)EnzymechemistryBiochemistryAcetylationBiophysicsbiology.proteinChickensProtein KinasesThe Journal of biological chemistry
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Mannoprotein of the yeast cell wall as primary receptor for the killer toxin of Saccharomyces cerevisiae strain 28.

1987

The killer toxin KT 28 of Saccharomyces cerevisiae strain 28 is primarily bound to the mannoprotein of the cell wall of sensitive yeasts. The mannoprotein of S. cerevisiae X 2180 was purified; gel filtration and SDS-PAGE indicated an estimated Mr of 185,000. The ability to bind killer toxin KT 28 increased during purification of the mannoprotein. Removing the protein part of the mannoprotein by enzymic digestion or removing the alkali-labile oligosaccharide chains by beta-elimination did not destroy the ability to bind killer toxin KT 28. However, binding activity was lost when the 1,6-alpha-linkages of the outer carbohydrate backbone were hydrolysed by acetolysis. The separated oligomannos…

Saccharomyces cerevisiae ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiaeBiologymedicine.disease_causeMicrobiologyChromatography AffinityCell wallSepharoseAffinity chromatographyCell WallmedicineReceptorGlycoproteinschemistry.chemical_classificationMembrane GlycoproteinsToxinOligosaccharideMycotoxinsbiology.organism_classificationChromatography Ion ExchangeYeastKiller Factors Yeastcarbohydrates (lipids)chemistryBiochemistryAdsorptionJournal of general microbiology
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Protective effect of adenylate deaminase (from Penicillium lanoso-viride) against acute infections in mice

1996

We examined the effects of the immunomodulator-adenylate deaminase (E.C. 3.5.4.6) from Penicillium lanoso-viride on experimental mice infections. Prophylactic intraperitoneal administration of adenylate deaminase (ADA) increased survival time and numbers of survivors after infection with Salmonella typhimurium, Pseudomonas aeruginosa and influenza A (H3N2) virus. Protection against influenza virus after intranasal ADA application was also observed. The influence of ADA was time and dose dependent. The most pronounced protection was obtained by administration of 3 U ADA/mice 24 h prior to infection. ADA had no antibiotic effect against these bacterial strains. Protective effects of ADA were …

Salmonella typhimuriumcongenital hereditary and neonatal diseases and abnormalitiesSalmonellamedicine.disease_causeVirusAMP DeaminaseMicrobiologyMicechemistry.chemical_compoundOrthomyxoviridae Infectionsimmune system diseasesCyclosporin amedicineAnimalsMacrophagePseudomonas InfectionsPharmacologyMice Inbred ICRSalmonella Infections AnimalbiologyPseudomonas aeruginosaPenicilliumnutritional and metabolic diseaseshemic and immune systemsbiology.organism_classificationenzymes and coenzymes (carbohydrates)chemistryInfluenza A virusAcute DiseaseImmunologyPenicilliumMice Inbred CBAFemaleNasal administrationTrypan blueImmunopharmacology
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An interlaboratory study as useful tool for proficiency testing of chemical oxygen demand measurements using solid substrates and liquid samples with…

2009

In 2008, the first Proficiency Testing Scheme of Chemical Oxygen Demand (1stCOD-PTADG) was conducted to assess the results obtained for different research groups whose field work is mainly anaerobic digestion. This study was performed using four samples, two solid samples as raw materials and two solid samples to prepare high concentration suspended solid solutions. Invitations were sent to a large number of laboratories, mainly to anaerobic digestion research groups. Finally, thirty labs from sixteen countries agreed to participate, but for different reasons four participants could not send any data. In total, twenty-six results were reported to the COD-PT coordinator. This study showed th…

Sample (material)[SDV]Life Sciences [q-bio]Analytical chemistryCarbohydratesSolid substrateSuspended solidsHomogeneity test010501 environmental sciences01 natural sciencesStandard deviationChemistry Techniques AnalyticalAnalytical ChemistryProficiency testingFatsAnaerobic digestionStatisticsProficiency testingPlant OilsSunflower OilAnaerobiosisChenopodium quinoa0105 earth and related environmental sciencesSuspended solidsInterlaboratory studyScience & TechnologySewageChemistryClinical Laboratory Techniques010401 analytical chemistryChemical oxygen demandProteinsReproducibility of ResultsCHEMICAL OXYDEN DEMANDReference StandardsTheoretical oxygen demand0104 chemical sciencesOxygenCHIMIE ANALYTIQUECertified reference materials[SDE]Environmental SciencesChemical oxygen demandRound robin test
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Antigenic cell wall mannoproteins in Candida albicans isolates and in other Candida species.

1991

Polyclonal antibodies (pAbs) and monoclonal antibodies (mAbs), raised against mannoprotein components from Candida albicans ATCC 26555 (serotype A) blastoconidia and mycelial cell walls, were used to investigate antigenic similarities among wall mannoproteins from other C. albicans serotype A and B strains, and from C. tropicalis and C. guilliermondii. Radioactively labelled walls isolated from cells grown at either 28 degrees C or 37 degrees C were digested with a beta-glucanase complex (Zymolyase 20T) to release cell-wall-bound mannoproteins. Numerous molecular species with different electrophoretic mobilities were released from the various isolates. Differences appeared to be related to …

SerotypeAntigenicityAntigens FungalHydrolasesMicrobiologyBlastoconidiumMicrobiologyCell wallFungal ProteinsEpitopesSpecies SpecificityCell WallCandida albicansCandida albicansCandidaMembrane GlycoproteinsMolecular massbiologyImmunochemistryAntibodies MonoclonalMembrane Proteinsbiology.organism_classificationCorpus albicanscarbohydrates (lipids)BiochemistrySolubilityPolyclonal antibodiesbiology.proteinJournal of general microbiology
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