Search results for "binding proteins"

showing 10 items of 911 documents

The germ cell nuclear factor (GCNF)

2005

The germ cell nuclear factor (GCNF), which is also known as RTR (retinoid receptor-related testis-associated receptor) is a member of the nuclear receptor superfamily. As a natural ligand remains to be discovered, GCNF is referred to as an orphan receptor. Owing to GCNF's unique features and its distant relation to any other known nuclear receptor it has been classified as the only member of the subgroup six and designated NR6A1 by the Receptor Nomenclature Committee (Duarte et al., 2002: Nucleic Acids Res 30: 364-368). To date, GCNF has been cloned from distinct vertebrate species, including zebrafish, Xenopus laevis, mouse, rat, and human. Cloning and characterization of the gene, domain …

Germ cell nuclear factorXenopusEmbryonic DevelopmentReceptors Cytoplasmic and NuclearNuclear Receptor Subfamily 6 Group A Member 1GeneticsmedicineAnimalsHumansZebrafishGeneGeneticsOrphan receptorCloningbiologyGene Expression Regulation DevelopmentalCell DifferentiationCell Biologybiology.organism_classificationDNA-Binding ProteinsGerm Cellsmedicine.anatomical_structureNuclear receptorVertebratesGerm cellDevelopmental BiologyMolecular Reproduction and Development
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Role for calnexin and N-linked glycosylation in the assembly and secretion of hepatitis B virus middle envelope protein particles.

1998

ABSTRACT Unlike those of the S and the L envelope proteins, the functional role of the related M protein in the life cycle of the hepatitis B virus (HBV) is less understood. We now demonstrate that a single N glycan, specific for M, is required for efficient secretion of M empty envelope particles. Moreover, this glycan mediates specific association of M with the chaperone calnexin. Conversely, the N glycan, common to all three envelope proteins, is involved neither in calnexin binding nor in subviral particle release. As proper folding and trafficking of M need the assistance of the chaperone, the glycan-dependent association of M with calnexin may thus play a crucial role in the assembly …

GlycanHepatitis B virusGlycosylationGlycosylationCalnexinImmunologyBiologymedicine.disease_causeMicrobiologychemistry.chemical_compoundCytosolN-linked glycosylationViral Envelope ProteinsVirologyCalnexinmedicineAnimalsSecretionPeptide sequenceHepatitis B virusBase SequenceCalcium-Binding ProteinsVirus-Cell Interactionscarbohydrates (lipids)BiochemistrychemistryOligodeoxyribonucleotidesInsect ScienceChaperone (protein)COS Cellsbiology.proteinMutagenesis Site-DirectedJournal of virology
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Genetic rearrangements in the pathogenicity locus of Clostridium difficile strain 8864 – implications for transcription, expression and enzymatic act…

1998

The pathogenicity locus (PaLoc) of Clostridium difficile isolate 8864 was investigated to locate genetic rearrangements that would explain the exceptional pathogenicity of this particular isolate. Two major changes were defined: an insertion of 1.1 kb between the two genes tcdA and tcdE, coding for the enterotoxin and an accessory protein of unknown function, respectively, and a deletion of 5.9 kb encompassing the 3' ends of tcdA and tcdC. Transcription of the tcdA-E genes is severely affected by both rearrangements, explaining the demonstrated complete lack of TcdA polypeptide. We present a model of coordinate, growth-related transcription of the tcdA-E genes that confirms our previous fin…

GlycosylationGlycoside HydrolasesTranscription GeneticBacterial ToxinsMolecular Sequence DataLocus (genetics)Chromosomal translocationEnterotoxinBiologyHomology (biology)law.inventionBacterial ProteinsGTP-Binding ProteinslawTranscription (biology)GeneticsAmino Acid SequenceMolecular BiologyGeneGeneticsClostridioides difficileGene Expression Regulation BacterialMolecular biologyRecombinant ProteinsAntisense RNAGenes BacterialGlucosyltransferasesRecombinant DNASequence AlignmentMolecular and General Genetics MGG
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Suppression of allograft rejection in the sponge Suberites domuncula by FK506 and expression of genes encoding FK506-binding proteins in allografts.

2001

SUMMARY Porifera (sponges) are, evolutionarily, the oldest metazoan phylum. Recent molecular data suggest that these animals possess molecules similar to and homologous with those of the innate and adaptive immune systems of higher Metazoa. Applying the biological system of parabiosis and the technique of differential display of mRNA, two cDNAs encoding putative FK506-binding proteins were isolated. FK506 is successfully used in clinics as a drug to prevent allograft rejection and is toxic to Suberites domuncula cells in vitro at doses above 100ng ml−1. Autograft fusion of transplants from S. domuncula was not affected by FK506. Allograft non-fusion was not affected by FK506 at toxic doses;…

Graft RejectionDNA ComplementaryPhysiologyParabiosisMolecular Sequence DataGene ExpressionSequence HomologyAquatic SciencePolymerase Chain ReactionTacrolimusTacrolimus Binding ProteinsImmune systempolycyclic compoundsHomologous chromosomeAnimalsTransplantation HomologousAmino Acid SequenceCloning MolecularMolecular BiologyGeneEcology Evolution Behavior and SystematicsGene LibraryMessenger RNADifferential displaybiologyAnatomybiology.organism_classificationIn vitroCell biologyPoriferaSuberites domunculaInsect ScienceAnimal Science and ZoologyThe Journal of experimental biology
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Isolation of carcinoembryonic antigen N-terminal domains (N-A1) from soluble aggregates

2011

Abstract Carcinoembryonic antigen (CEA) was identified as a prominent tumor-associated antigen in human colorectal cancer and it is still intensively investigated. However, its physiological role remains unclear. The CEA molecule is composed of seven highly hydrophobic, immunoglobulin-like domains, six of which contain a single disulphide bridge. The production of recombinant protein containing Ig-like domains in bacterial expression systems often results in partial degradation or insolubility due to aggregation hampering the analysis of their native structure and function. Here, we present a new method of expression and purification of CEA N-terminal domains (N-A1) fused to MBP in Escheric…

Guanidinium chlorideCircular dichroismRecombinant Fusion Proteinsmedicine.disease_causeMaltose-Binding Proteinslaw.inventionchemistry.chemical_compoundCarcinoembryonic antigenlawProtein purificationEscherichia colimedicineTEV proteaseHumansDisulfidesEscherichia coliGuanidinebiologyProtein StabilityCircular DichroismFusion proteinCarcinoembryonic AntigenProtein Structure TertiarySolubilitychemistryBiochemistryChromatography GelRecombinant DNAbiology.proteinElectrophoresis Polyacrylamide GelBiotechnologyProtein Expression and Purification
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8-Oxoguanine DNA glycosylase (Ogg1) causes a transcriptional inactivation of damaged DNA in the absence of functional Cockayne syndrome B (Csb) prote…

2008

We have analysed the effect of oxidative guanine lesions on the expression of a transfected reporter gene in mouse embryonic fibroblasts deficient in Cockayne syndrome B protein (Csb) and/or the 8-oxoguanine DNA glycosylase (Ogg1). We used a highly sensitive flow cytometry-based approach and quantitative real-time PCR to measure the changes in gene expression caused by the presence of oxidised guanine residues generated by photosensitisation in the vector DNA. In wild-type cells, small numbers (one or three) of oxidised guanines did not affect gene expression at short times after transfections, whereas progressive reduction of the transgene expression was observed at later time points. Alth…

GuanineGuanineGreen Fluorescent ProteinsGene ExpressionBiologyHost-Cell ReactivationBiochemistryCell LineDNA GlycosylasesMicechemistry.chemical_compoundGenes ReporterGene expressionAnimalsHumansGene SilencingPoly-ADP-Ribose Binding ProteinsMolecular BiologyGeneReporter genePhotosensitizing AgentsReverse Transcriptase Polymerase Chain ReactionDNA HelicasesCell BiologyBase excision repairFlow CytometryMolecular biologyDNA Repair EnzymeschemistryDNA glycosylaseDNADNA DamageDNA Repair
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Mutations in DNA Binding and Transactivation Domains Affect the Dynamics of Parvovirus NS1 Protein

2013

ABSTRACT The multifunctional replication protein of autonomous parvoviruses, NS1, is vital for viral genome replication and for the control of viral protein production. Two DNA-interacting domains of NS1, the N-terminal and helicase domains, are necessary for these functions. In addition, the N and C termini of NS1 are required for activation of viral promoter P38. By comparison with the structural and biochemical data from other parvoviruses, we identified potential DNA-interacting amino acid residues from canine parvovirus NS1. The role of the identified amino acids in NS1 binding dynamics was studied by mutagenesis, fluorescence recovery after photobleaching, and computer simulations. Mu…

HMG-boxParvovirus CaninevirusesImmunologyDNA Mutational AnalysisMutation MissenseNS1 proteiiniViral Nonstructural ProteinsVirus ReplicationMicrobiologyNS1 proteinSingle-stranded binding proteinCell LineSeqA protein domainVirologyAnimalsDNA bindingReplication protein AbiologyTer proteinparvovirusvirus diseasesDNAn sitoutuminen [DNA]biochemical phenomena metabolism and nutritionMolecular biologyCell biologyVirus-Cell InteractionsProtein Structure TertiaryDNA binding siteDNA-Binding ProteinsInsect Sciencebiology.proteinMutant ProteinsViral genome replicationBinding domainProtein Binding
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Genetic manipulation of longevity-related genes as a tool to regulate yeast life span and metabolite production during winemaking

2013

Abstract Background Yeast viability and vitality are essential for different industrial processes where the yeast Saccharomyces cerevisiae is used as a biotechnological tool. Therefore, the decline of yeast biological functions during aging may compromise their successful biotechnological use. Life span is controlled by a variety of molecular mechanisms, many of which are connected to stress tolerance and genomic stability, although the metabolic status of a cell has proven a main factor affecting its longevity. Acetic acid and ethanol accumulation shorten chronological life span (CLS), while glycerol extends it. Results Different age-related gene classes have been modified by deletion or o…

HST3GlycerolSaccharomyces cerevisiae ProteinsTranscription Genetic<it>HST3</it>Saccharomyces cerevisiaeLongevitylcsh:QR1-502SOD2BioengineeringApoptosisWinePUB1Saccharomyces cerevisiaeStressApplied Microbiology and Biotechnologylcsh:MicrobiologyHistone DeacetylasesStress granuleSirtuin 2<it>PUB1</it>Gene expressionChronological agingSirtuinsNADH NADPH OxidoreductasesRNA MessengerEthanol metabolismSilent Information Regulator Proteins Saccharomyces cerevisiaeAcetic AcidbiologyEthanolSuperoxide DismutaseResearchRNA-Binding Proteinsbiology.organism_classificationYeastYeastBiochemistryCaspasesFermentationMutationFermentationHistone deacetylaseGene DeletionBiotechnologyMicrobial Cell Factories
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Detection of oxidative mutagenesis by isoniazid and other hydrazine derivatives in Escherichia coli WP2 tester strain IC203, deficient in OxyR: stron…

1998

Abstract Strain IC203, deficient in the OxyR function, was sensitive to both cytotoxic and mutagenic effects of isoniazid (INH) whereas its parent, WP2 uvrA /pKM101, was resistant to these effects. Four other hydrazine compounds, hydrazine hydrate (HZH), phenylhydrazine (PHZ), hydralazine (HLZ) and nialamide (NLD), were mutagenic in WP2 uvrA /pKM101. Increases in mutagenicity were observed in IC203 for HZH and PHZ but not for HLZ and NLD. Growth inhibition zones by HZH, PHZ and NLD were larger in IC203 than in WP2 uvrA /pKM101. The enhancements in the effects of INH, HZH and PHZ in IC203 with respect to its oxyR + parent are considered to be caused by the production of reactive oxygen speci…

Health Toxicology and Mutagenesismedicine.disease_causechemistry.chemical_compoundSpecies SpecificityEscherichia coliIsoniazidGeneticsmedicineAnimalsEscherichia coliPhenylhydrazinechemistry.chemical_classificationReactive oxygen speciesbiologyMutagenicity TestsEscherichia coli ProteinsMutagenesisbiology.organism_classificationEnterobacteriaceaeRatsDNA-Binding ProteinsRepressor ProteinsLiverBiochemistrychemistryMutagenesisCatalasebiology.proteinbacteriaGrowth inhibitionReactive Oxygen SpeciesOxidation-ReductionCytosineMutagensTranscription FactorsMutation Research/Genetic Toxicology and Environmental Mutagenesis
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The hematopoietic niche: a Drosophila model, at last.

2007

The niche provides a specialised microenvironment necessary for maintenance of stem cells in a non differentiated state. While the hematopoietic stem cell (HSC) niche in vertebrates was the first to be recognized, Drosophila niches supporting germline stem cells were characterised first. Recent evidence for the existence of a niche maintaining hematopoietic precursors in Drosophila opens the way to study in vivo the niche/hematopoietic precursors interactions. The availability of a large collection of cell markers, mutants and sophisticated genetic tools makes Drosophila an attractive model for investigating the cellular and molecular mechanisms that are involved in these interactions.

HemocytesCalcium-Binding ProteinsMembrane ProteinsHematopoietic Stem CellsLarvaModels Animal[SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular BiologyAnimalsDrosophila ProteinsIntercellular Signaling Peptides and Proteins[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyDrosophilaSerrate-Jagged Proteins[ SDV.BBM ] Life Sciences [q-bio]/Biochemistry Molecular BiologyBiomarkersJagged-1 ProteinTranscription FactorsCell cycle (Georgetown, Tex.)
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