2019
A polymorphism in intron I of the human angiotensinogen gene (hAGT) affects binding by HNF3 and hAGT expression and increases blood pressure in mice
Mopidevi B, Kaw MK, Sivankutty I, Jain S, Perla SK, Kumar A. A polymorphism in intron I of the human angiotensinogen gene (hAGT) affects binding by HNF3 and hAGT expression and increases blood pressure in mice. Journal Of Biological Chemistry 2019, 294: 11829-11839. PMID: 31201268, PMCID: PMC6682742, DOI: 10.1074/jbc.ra119.007715.Peer-Reviewed Original ResearchMeSH KeywordsAngiotensinogenAnimalsBinding SitesBlood PressureCCAAT-Enhancer-Binding Protein-betaChromatinHep G2 CellsHepatocyte Nuclear Factor 3-betaHumansIntronsLinkage DisequilibriumLiverMiceMice, Inbred C57BLMice, TransgenicPolymorphism, Single NucleotideProtein BindingReceptors, GlucocorticoidReninRNA, MessengerConceptsIntron IHap-IITransgenic animalsGenome-wide association studiesHepatocyte nuclear factor 3Reporter gene constructsBlood pressureCCAAT enhancer-binding protein βEnhancer-binding protein βHuman angiotensinogen geneStrong homologyHypoxanthine-guanine phosphoribosyltransferase locusNucleotide sequenceGene constructsTranscription rateHuman renin genePromoter activityAssociation studiesHAGT expressionMain haplotypesGenesProtein βElevated blood pressureTransgenic mouse modelFactor 3
2000
Developmental expression of Pim kinases suggests functions also outside of the hematopoietic system
Eichmann A, Yuan L, Bréant C, Alitalo K, Koskinen P. Developmental expression of Pim kinases suggests functions also outside of the hematopoietic system. Oncogene 2000, 19: 1215-1224. PMID: 10713710, DOI: 10.1038/sj.onc.1203355.Peer-Reviewed Original ResearchMeSH KeywordsAbdomenAmino Acid SequenceAnimalsCloning, MolecularEctodermEmbryo, NonmammalianEmbryonic and Fetal DevelopmentEmbryonic DevelopmentGene Expression Regulation, DevelopmentalHematopoiesisHumansMiceMolecular Sequence DataNervous SystemOrgan SpecificityProtein Serine-Threonine KinasesProto-Oncogene ProteinsProto-Oncogene Proteins c-pim-1QuailRatsTranscription, GeneticConceptsExpression patternsSerine/threonine kinaseDeduced amino acid sequenceDynamic expression patternHematopoietic systemPim-1Amino acid sequencePim family kinasesEarly developmental stagesFunctional redundancyThreonine kinaseFamily kinasesEmbryonic developmentStrong homologyNovel functionAcid sequenceExpression sitesPIM genesAvian embryosDevelopmental expressionDevelopmental stagesPIM familyPIM kinasesCDNAKinase
1996
The role of the human homologue of Drosophila patched in sporadic basal cell carcinomas
Gailani M, Ståhle-Bäckdahl M, Leffell D, Glyn M, Zaphiropoulos P, Undén A, Dean M, Brash D, Bale A, Toftgård R. The role of the human homologue of Drosophila patched in sporadic basal cell carcinomas. Nature Genetics 1996, 14: 78-81. PMID: 8782823, DOI: 10.1038/ng0996-78.Peer-Reviewed Original ResearchConceptsSporadic basal cell carcinomasSingle-strand conformational polymorphismTumor suppressorDrosophila segment polarity geneSegment polarity genesHedgehog target genesPolarity genesDrosophila mutantsStrong homologyHuman homologueTarget genesMutational inactivationMutant transcriptsStrand conformational polymorphismNorthern blotSSCP variantsGenesNegative feedback mechanismSitu hybridizationConformational polymorphismNevoid basal cell carcinoma syndromeSuppressorAllelic lossInactivationMutationsMutations of the Human Homolog of Drosophila patched in the Nevoid Basal Cell Carcinoma Syndrome
Hahn H, Wicking C, Zaphiropoulos P, Gailani M, Shanley S, Chidambaram A, Vorechovsky I, Holmberg E, Unden A, Gillies S, Negus K, Smyth I, Pressman C, Leffell D, Gerrard B, Goldstein A, Dean M, Toftgard R, Chenevix-Trench G, Wainwright B, Bale A. Mutations of the Human Homolog of Drosophila patched in the Nevoid Basal Cell Carcinoma Syndrome. Cell 1996, 85: 841-851. PMID: 8681379, DOI: 10.1016/s0092-8674(00)81268-4.Peer-Reviewed Original ResearchMeSH KeywordsAllelesAnimalsBasal Cell Nevus SyndromeBase SequenceChromosome MappingChromosomes, Human, Pair 9Cloning, MolecularDNA, ComplementaryDrosophilaDrosophila ProteinsExonsFemaleGene DeletionGene ExpressionGenes, Tumor SuppressorHumansIn Vitro TechniquesInsect HormonesIntronsMembrane ProteinsMolecular Sequence DataMutationPedigreeReceptors, Cell SurfaceSequence Homology, Nucleic AcidConceptsDrosophila segment polarity geneSegment polarity genesCertain cell typesDevelopmental abnormalitiesPolarity genesHuman homologStrong homologySporadic basal cell carcinomasHuman sequenceCosmid contigTumor suppressorLoss of heterozygosityCell typesGenesPatched geneChromosome 9q22.3Complete lossFunction contributesNevoid basal cell carcinoma syndromeMutation analysisBasal cell carcinoma syndromeAutosomal dominant disorderNBCCS patientsDrosophilaDominant disorder
1991
Molecular characterization of a protein-tyrosine-phosphatase enriched in striatum.
Lombroso P, Murdoch G, Lerner M. Molecular characterization of a protein-tyrosine-phosphatase enriched in striatum. Proceedings Of The National Academy Of Sciences Of The United States Of America 1991, 88: 7242-7246. PMID: 1714595, PMCID: PMC52270, DOI: 10.1073/pnas.88.16.7242.Peer-Reviewed Original ResearchConceptsDeduced amino acid sequenceAmino acid consensus sequenceAmino acid sequenceApparent molecular massRat striatal cDNA librarySingle geneVitro translationCDNA clonesStrong homologyCDNA libraryCytoplasmic membraneAcid sequenceRNA transcriptsN-terminusMolecular characterizationRNA analysisMolecular massAmino acidsProteinPhosphataseMRNASequenceHomologyGenesTerminus
1990
Regulation of the segmentation gene fushi tarazu has been functionally conserved in Drosophila.
Maier D, Preiss A, Powell J. Regulation of the segmentation gene fushi tarazu has been functionally conserved in Drosophila. The EMBO Journal 1990, 9: 3957-3966. PMID: 2174353, PMCID: PMC552166, DOI: 10.1002/j.1460-2075.1990.tb07616.x.Peer-Reviewed Original ResearchConceptsSegmentation gene fushi tarazuFtz geneFushi tarazuD. melanogasterUpstream elementEvolution of DrosophilaEntire regulatory networksSegmentation genesMillions of yearsRegulatory networksRegulatory elementsStrong homologySpecific enhancersGene productsUpstream regionUnrelated sequencesTransformation experimentsGenesDrosophilaMelanogasterOverall organizationRegulationFTZHomologuesHomology
1987
A new lamin in Xenopus somatic tissues displays strong homology to human lamin A.
Wolin S, Krohne G, Kirschner M. A new lamin in Xenopus somatic tissues displays strong homology to human lamin A. The EMBO Journal 1987, 6: 3809-3818. PMID: 3428277, PMCID: PMC553853, DOI: 10.1002/j.1460-2075.1987.tb02717.x.Peer-Reviewed Original ResearchConceptsHuman lamin ACDNA clonesXenopus laminSomatic tissuesLamin AMajor lamin proteinsCarboxy-terminal domainAdult somatic cellsHuman lamin A.Major laminsDistinct structural classesLamin proteinsNuclear laminaLamin LIIIEmbryonic developmentSomatic cellsSomatic laminsStrong homologyLamin A.Lamin LILaminsMajor polypeptidesGerm cellsProteinClones
1978
Conservation of the primary structure at the 3′ end of 18S rRNA from eucaryotic cells
Hagenbüchle O, Santer M, Steitz J, Mans R. Conservation of the primary structure at the 3′ end of 18S rRNA from eucaryotic cells. Cell 1978, 13: 551-563. PMID: 77738, DOI: 10.1016/0092-8674(78)90328-8.Peer-Reviewed Original ResearchConceptsE. coli 16S rRNAE. coli ribosomesPurine-rich regionDNA sequencing methodsRRNA moleculesEucaryotic speciesStrong homologyCDNA transcriptsCDNA copyPolynucleotidyl transferasesRNA moleculesRRNA sequencesEucaryotic cellsEucaryotic mRNAsExtensive complementarityColi ribosomesRRNAPrimary structureEnzyme ATPSequencing methodsOligonucleotide primersAMV reverse transcriptaseTerminusReverse transcriptaseSequence
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