Search results for "Leucine Zippers"

showing 4 items of 4 documents

A novel tumour associated leucine zipper protein targeting to sites of gene transcription and splicing

2002

We describe here the definition and characterization of antigen CT-8/HOM-TES-85 encoded by a previously unknown gene and identified by serological expression screening using antibodies from a seminoma patient. Intriguingly, the leucine zipper region of CT-8/HOM-TES-85 shows an atypical amphipathy with clusters of hydrophobic residues that is exclusively shared by the N-myc proto-oncogene. CT-8/HOM-TES-85 gene is tightly silenced in normal tissues except for testis. However, it is frequently activated in human neoplasms of different types including lung cancer, ovarian cancer, melanoma and glioma. Endogenous as well as heterogeneously expressed CT-8/HOM-TES-85 targets predominantly to the nu…

Cancer ResearchLeucine zipperDNA ComplementaryTranscription GeneticGreen Fluorescent ProteinsImmunoblottingBiologymedicine.disease_causeModels BiologicalProto-Oncogene MasAntigens NeoplasmTranscription (biology)Protein targetingTumor Cells CulturedGeneticsmedicineHumansTissue DistributionAntigensMolecular BiologyGeneLeucine ZippersATF3GenomeReverse Transcriptase Polymerase Chain ReactionAlternative splicingfood and beveragesBlotting NorthernPhenotypeProtein Structure TertiaryDNA-Binding ProteinsAlternative SplicingLuminescent ProteinsPhenotypeMicroscopy FluorescenceModels ChemicalRNA splicingCancer researchOncogene
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Identification and characterization of amphiphysin II as a novel cellular interaction partner of the hepatitis C virus NS5A protein.

2003

The hepatitis C virus (HCV) NS5A protein is highly phosphorylated by cellular protein kinases. To study how NS5A might be integrated in cellular kinase signalling, we isolated phosphoproteins from HuH-7 hepatoma cells that specifically interacted with recombinant NS5A protein. Subsequent mass spectrometry identified the adaptor protein amphiphysin II as a novel interaction partner of NS5A. Mutational analysis revealed that complex formation is primarily mediated by a proline-rich region in the C-terminal part of NS5A, which interacts with the amphiphysin II Src homology 3 domain. Importantly, we could further demonstrate specific co-precipitation and cellular co-localization of endogenous a…

CytoplasmProlinevirusesImmunoblottingNerve Tissue ProteinsHepacivirusBiologyProtein Serine-Threonine KinasesViral Nonstructural ProteinsVirus ReplicationSH3 domainVirologyTumor Cells CulturedHumansRepliconNS5AFluorescent Antibody Technique IndirectSubgenomic mRNALeucine ZippersKinasevirus diseasesSignal transducing adaptor proteinbiochemical phenomena metabolism and nutritionMAP Kinase Kinase KinasesRNA-Dependent RNA PolymeraseVirologyMolecular biologydigestive system diseasesRecombinant ProteinsViral replicationMutationPhosphorylationRepliconProtein BindingThe Journal of general virology
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A stage-specific functional role of the leucine zipper transcription factor c-Maf in lung Th2 cell differentiation.

2004

The transcription factor c-Maf controls IL-4 gene expression in CD4(+) T cells, and its expression is up-regulated in human asthmatic airways after allergen challenge. In the present study, we addressed the role of c-Maf in asthma by studying transgenic (Tg) mice overexpressing c-Maf in CD4(+) T cells under the control of the CD2 promoter. As shown, lung CD4(+) T cells of c-maf-Tg mice produced more IL-5 at the early stage (day 2) of culture in the presence of IL-4 than wild-type control cells. Consistently, c-maf-Tg mice spontaneously showed increased IL-5 expression and eosinophils in the bronchial alveolar lavage fluid (BALF) and activated IL-5 signal transduction via Raf-1 and Ras in lu…

Leucine zipperTransgeneCellular differentiationImmunologyMice TransgenicBiologyMiceTh2 CellsProto-Oncogene ProteinsGene expressionmedicineImmunology and AllergyAnimalsTranscription factorLungLeucine ZippersLungCell Differentiationrespiratory systemMolecular biologyrespiratory tract diseasesDNA-Binding ProteinsEosinophilsmedicine.anatomical_structureProto-Oncogene Proteins c-mafInterleukin-4Signal transductionInterleukin-5Proto-Oncogene Proteins c-mafCell DivisionTranscription FactorsEuropean journal of immunology
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P sequences ofDrosophilla Subobscuralack exon 3 and may encode a 66 kd repressor-like protein

1991

Abstract Several P homologous sequences have been cloned and sequenced from Drosophila subobscura. These sequences are located at the 85DE region of the O chromosome and at least three of them are organized in tandem. We have identified four copies which exhibit strong similarity between them. All of the isolated elements are truncated at the 5' and 3' ends. They have lost the inverted terminal repeats and exon 3, but maintain exons 0, 1 and 2. They are transcribed producing a polyadenylated RNA. The structure of these transcripts suggests that they are able to encode a 66 kd repressor-like protein, but not a functional transposase. We ask about the biological role of a potential repressor …

Transposable elementMolecular Sequence DataRestriction MappingTransposasesRepressorBiologyHomology (biology)P elementExonSequence Homology Nucleic AcidGeneticsAnimalsAmino Acid SequenceCloning MolecularTransposaseRepetitive Sequences Nucleic AcidGeneticsLeucine ZippersBase SequenceNucleic acid sequenceNucleic Acid HybridizationExonsNucleotidyltransferasesMolecular biologyDrosophila subobscuraRepressor ProteinsDNA Transposable ElementsDrosophilaNucleic Acids Research
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