1999
Mutational Analysis of Cell Cycle Inhibition by Integrin β1C *
Meredith J, Kiosses W, Takada Y, Schwartz M. Mutational Analysis of Cell Cycle Inhibition by Integrin β1C *. Journal Of Biological Chemistry 1999, 274: 8111-8116. PMID: 10075712, DOI: 10.1074/jbc.274.12.8111.Peer-Reviewed Original ResearchMeSH KeywordsAlternative SplicingAmino Acid SequenceAnimalsCells, CulturedDNA Mutational AnalysisDNA ReplicationDose-Response Relationship, DrugHumansIntegrin beta1MiceMice, Inbred C3HMolecular Sequence DataMutagenesis, Site-DirectedReceptors, Interleukin-2Recombinant Fusion ProteinsStructure-Activity RelationshipConceptsCytoplasmic domainGreen fluorescent protein fusion proteinFluorescent protein fusion proteinProtein fusion proteinMembrane-proximal regionCell cycle progressionAnalysis of deletionsHuman interleukin-2 receptorBeta5 cytoplasmic domainsMembrane targetingMouse 10T1/2 cellsGrowth inhibitionCell cycle inhibitionTransmembrane domainLow expression levelsProstate epithelial cellsAcid domainCytoplasmic variantsTac subunitMutational analysisCycle progressionFusion proteinIntact receptorCell line DU145Human endothelial cell line
1995
Molecular Cloning of the Human Homolog of a Striatum-Enriched Phosphatase (STEP) Gene and Chromosomal Mapping of the Human and Murine Loci
Li X, Luna J, Lombroso P, Francke U. Molecular Cloning of the Human Homolog of a Striatum-Enriched Phosphatase (STEP) Gene and Chromosomal Mapping of the Human and Murine Loci. Genomics 1995, 28: 442-449. PMID: 7490079, DOI: 10.1006/geno.1995.1173.Peer-Reviewed Original ResearchConceptsSrc homology domain 3STEP geneTyrosine phosphataseSomatic cell hybrid analysisHuman fetal brain cDNA libraryFetal brain cDNA libraryPhosphatase catalytic domainCell hybrid analysisProtein tyrosine phosphataseAmino acid domainProline-rich regionCandidate disease genesBrain cDNA libraryUsher syndrome type 1CAmino acid levelsChromosomal mappingPhosphatase geneMutant lociHuman homologTrue homologsMolecular cloningCatalytic domainAcid domainMurine locusCDNA library
1992
The Core Protein of Epican, a Heparan Sulfate Proteoglycan on Keratinocytes, Is an Alternative Form of CD44
Kugelman L, Ganguly S, Haggerty J, Weissman S, Milstone L. The Core Protein of Epican, a Heparan Sulfate Proteoglycan on Keratinocytes, Is an Alternative Form of CD44. Journal Of Investigative Dermatology 1992, 99: 887-891. PMID: 1281868, DOI: 10.1111/1523-1747.ep12614896.Peer-Reviewed Original ResearchConceptsHeparan sulfate proteoglycanCore proteinForm of CD44Human keratinocyte cDNA libraryDeduced protein sequenceAmino acid domainProximal extracellular domainKeratinocyte cDNA librarySulfate proteoglycanAcid domainCDNA libraryProtein sequencesGlycosylation sitesProteolysis siteExtracellular domainAdditional domainsAmino acidsProteinEpicanLeukocyte formCD44ProteoglycansDomainMonoclonal antibodiesKeratinocytesThe Core Protein of Epican, a Heparan Sulfate Proteoglycan on Keratinocytes, Is an Alternative Form of CD44
Kugelman L, Ganguly S, Haggerty J, Weissman S, Milstone L. The Core Protein of Epican, a Heparan Sulfate Proteoglycan on Keratinocytes, Is an Alternative Form of CD44. Journal Of Investigative Dermatology 1992, 99: 381-385. DOI: 10.1111/1523-1747.ep12616092.Peer-Reviewed Original ResearchHeparan sulfate proteoglycanCore proteinForm of CD44Human keratinocyte cDNA libraryDeduced protein sequenceAmino acid domainProximal extracellular domainKeratinocyte cDNA librarySulfate proteoglycanAcid domainCDNA libraryProtein sequencesGlycosylation sitesProteolysis siteExtracellular domainAdditional domainsAmmo acidsProteinEpicanLeukocyte formCD44ProteoglycansDomain
This site is protected by hCaptcha and its Privacy Policy and Terms of Service apply