2015
Three Myosins Contribute Uniquely to the Assembly and Constriction of the Fission Yeast Cytokinetic Contractile Ring
Laplante C, Berro J, Karatekin E, Hernandez-Leyva A, Lee R, Pollard TD. Three Myosins Contribute Uniquely to the Assembly and Constriction of the Fission Yeast Cytokinetic Contractile Ring. Current Biology 2015, 25: 1955-1965. PMID: 26144970, PMCID: PMC4526439, DOI: 10.1016/j.cub.2015.06.018.Peer-Reviewed Original ResearchConceptsContractile ringActin filamentsHeavy chain geneMyosin IIContractile ring assemblyFission yeast cellsMyosin heavy chain geneCytokinetic contractile ringConventional myosin IICytokinetic nodesMyo2Myo51Myp2Ring assemblyYeast cellsMyosin functionCytokinesisDeletion mutationsComplete assemblyMyosin VConstriction rateGenesMutationsCellsFilaments
2013
Targeting the Intracellular Environment in Cystic Fibrosis: Restoring Autophagy as a Novel Strategy to Circumvent the CFTR Defect
Villella VR, Esposito S, Bruscia EM, Maiuri MC, Raia V, Kroemer G, Maiuri L. Targeting the Intracellular Environment in Cystic Fibrosis: Restoring Autophagy as a Novel Strategy to Circumvent the CFTR Defect. Frontiers In Pharmacology 2013, 4: 1. PMID: 23346057, PMCID: PMC3549520, DOI: 10.3389/fphar.2013.00001.Peer-Reviewed Original ResearchCF transmembrane conductance regulatorIntracellular environmentMutant CF transmembrane conductance regulatorF508del-CFTR proteinBeclin-1CFTR channel activityTransmembrane conductance regulatorDefective CF transmembrane conductance regulatorDirect gene transferGeneral proteostasisProteostasis regulatorsConformational diseasesDisabled autophagyCFTR mutantsAutophagosome formationPlasma membraneConductance regulatorF508del-CFTRCommon deletion mutationsDeletion mutationsRecent pre-clinical evidenceIntracellular retentionGene transferCFTR defectProteostasis
2009
Regulation of the epidermal growth factor receptor intracellular domain
Choi S, Lemmon M. Regulation of the epidermal growth factor receptor intracellular domain. The FASEB Journal 2009, 23: 883.2-883.2. DOI: 10.1096/fasebj.23.1_supplement.883.2.Peer-Reviewed Original ResearchC-terminal tailTyrosine kinase domainIntracellular domainJuxtamembrane regionJM regionEGFR intracellular domainEpidermal growth factor receptorC-tailEGFR extracellular regionC-tail regionReceptor intracellular domainEffects of mutationsReceptor tyrosine kinasesReceptor-receptor interactionsSmall-angle X-ray scatteringKinase assaysKinase domainGrowth factor receptorExtracellular regionReceptor dimerizationEGFR activationBaculovirus systemIntracellular dimerTyrosine kinaseDeletion mutations
2007
Roles for Drosophila melanogaster Myosin IB in Maintenance of Enterocyte Brush-Border Structure and Resistance to the Bacterial Pathogen Pseudomonas entomophila
Hegan PS, Mermall V, Tilney LG, Mooseker MS. Roles for Drosophila melanogaster Myosin IB in Maintenance of Enterocyte Brush-Border Structure and Resistance to the Bacterial Pathogen Pseudomonas entomophila. Molecular Biology Of The Cell 2007, 18: 4625-4636. PMID: 17855510, PMCID: PMC2043548, DOI: 10.1091/mbc.e07-02-0191.Peer-Reviewed Original ResearchConceptsMutant larvaePseudomonas entomophilaTail domainMyosin IBMidgut epithelial cellsActin filament coreDrosophila genomeApical brush borderMidgut enterocytesBrush borderCytoskeletal defectsLarval gutResponse pathwaysApical localizationMV membraneBrush border structureDeletion mutationsFood uptakeGram-negative bacterial infectionsInnate immune responseMyo1bGut physiologyEntomophilaEpithelial cellsMidgut
2006
Immunohistochemical and mutational analysis of apoptosis‐inducing factor (AIF) in colorectal carcinomas
JEONG E, LEE J, SOUNG Y, NAM S, KIM S, LEE J, YOO N, LEE S. Immunohistochemical and mutational analysis of apoptosis‐inducing factor (AIF) in colorectal carcinomas. Apmis 2006, 114: 867-873. PMID: 17207087, DOI: 10.1111/j.1600-0463.2006.apm_502.x.Peer-Reviewed Original ResearchConceptsApoptosis-inducing factorFunction of apoptosis-inducing factorSingle-strand conformation polymorphismCell death functionApoptosis-inducing factor protein expressionNormal mucosal epithelial cellsMutation analysisApoptosis-inducing factor geneExpression of AIF proteinExpression of apoptosis-inducing factorMalignant colorectal epithelial cellsSomatic mutationsApoptosis-inducing factor expressionCaspase-independent apoptosisHuman cancersCancer cellsEpithelial cellsMucosal epithelial cellsColorectal carcinomaAIF proteinProtein expressionConformation polymorphismDeletion mutationsOxidoreductase activityColorectal epithelial cells
2005
SLC34A3 Mutations in Patients with Hereditary Hypophosphatemic Rickets with Hypercalciuria Predict a Key Role for the Sodium-Phosphate Cotransporter NaPi-IIc in Maintaining Phosphate Homeostasis
Bergwitz C, Roslin NM, Tieder M, Loredo-Osti JC, Bastepe M, Abu-Zahra H, Frappier D, Burkett K, Carpenter TO, Anderson D, Garabédian M, Sermet I, Fujiwara TM, Morgan K, Tenenhouse HS, Jüppner H. SLC34A3 Mutations in Patients with Hereditary Hypophosphatemic Rickets with Hypercalciuria Predict a Key Role for the Sodium-Phosphate Cotransporter NaPi-IIc in Maintaining Phosphate Homeostasis. American Journal Of Human Genetics 2005, 78: 179-192. PMID: 16358214, PMCID: PMC1380228, DOI: 10.1086/499409.Peer-Reviewed Original ResearchConceptsConsanguineous BedouinFirst membrane-spanning domainMembrane-spanning domainsPhosphate homeostasisRenal sodium-phosphate cotransporterNucleotide sequence analysisDihydroxyvitamin D levelsSingle nucleotide deletionHereditary hypophosphatemic ricketsCompound heterozygous missenseSLC34A3 mutationsHomozygous single nucleotide deletionHypophosphatemic ricketsLinkage scanCandidate genesGenomic DNASodium-phosphate cotransporterSequence analysisD levelsHomozygosity mappingDeletion mutationsGenomewide linkage scanKey roleChromosome 9q34Mutations
2001
Atm knock-in mice harboring an in-frame deletion corresponding to the human ATM 7636del9 common mutation exhibit a variant phenotype.
Spring K, Cross S, Li C, Watters D, Ben-Senior L, Waring P, Ahangari F, Lu SL, Chen P, Misko I, Paterson C, Kay G, Smorodinsky NI, Shiloh Y, Lavin MF. Atm knock-in mice harboring an in-frame deletion corresponding to the human ATM 7636del9 common mutation exhibit a variant phenotype. Cancer Research 2001, 61: 4561-8. PMID: 11389091.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsApoptosisAtaxia TelangiectasiaAtaxia Telangiectasia Mutated ProteinsBase SequenceCell Cycle ProteinsCrosses, GeneticDNADNA-Binding ProteinsFemaleHumansLymphomaMaleMiceMice, Inbred C57BLMice, KnockoutMice, Mutant StrainsMutagenesis, Site-DirectedPhenotypeProtein Serine-Threonine KinasesSequence DeletionThymus NeoplasmsTumor Suppressor ProteinsUp-RegulationConceptsAtaxia telangiectasiaFrame deletionDisorder ataxia-telangiectasiaProtein kinase activityCell cycle checkpointsAmino acid residuesSelectable marker cassetteDetectable ATM proteinMutant proteinsATM proteinCycle checkpointsHomologous recombinationKinase activityAcid residuesMarker cassetteCommon deletion mutationsDeletion mutationsDeletion resultsCre-loxPATM geneThymic lymphomasExtensive apoptosisVariant phenotypesDifferent phenotypesFas ligand
1998
A Mutation in α-Catenin Disrupts Adhesion in Clone A Cells Without Perturbing its Actin and β-Catenin Binding Activity
Roe S, Koslov E, Rimm D. A Mutation in α-Catenin Disrupts Adhesion in Clone A Cells Without Perturbing its Actin and β-Catenin Binding Activity. Cell Communication & Adhesion 1998, 5: 283-296. PMID: 9762469, DOI: 10.3109/15419069809040298.Peer-Reviewed Original ResearchMeSH KeywordsActinsalpha Cateninbeta CateninCadherinsCell AdhesionCloning, MolecularColonic NeoplasmsCytoskeletal ProteinsCytoskeletonDesmoplakinsExonsgamma CateninHeLa CellsHumansIntercellular JunctionsMutationOctoxynolPrecipitin TestsProtein BindingRecombinant Fusion ProteinsReverse Transcriptase Polymerase Chain ReactionRNA, MessengerSequence Analysis, DNASolubilityTrans-ActivatorsTransfectionTumor Cells, CulturedConceptsN-terminusE-cadherin-catenin complexBundles F-actinCo-sedimentation assaysCell-cell adhesionFull-length proteinClone A cellsCo-precipitation experimentsInternal deletion mutationsWhole cell lysatesAdhesive complexesMutant proteinsA mutantsMutant bindsHuman colon carcinoma cell lineColon carcinoma cell lineMutant formsLength proteinWild typeCytoplasmic connectionsF-actinAdhesive phenotypeDeletion mutationsCell lysatesCarcinoma cell lines
1997
Evidence for a common sex determination mechanism for pistil abortion in maize and in its wild relative Tripsacum
Li D, Blakey C, Dewald C, Dellaporta S. Evidence for a common sex determination mechanism for pistil abortion in maize and in its wild relative Tripsacum. Proceedings Of The National Academy Of Sciences Of The United States Of America 1997, 94: 4217-4222. PMID: 9108132, PMCID: PMC20608, DOI: 10.1073/pnas.94.8.4217.Peer-Reviewed Original ResearchConceptsStaminate floretsPistil abortionRestriction fragment length polymorphism mappingSex determination mechanismSimilar expression patternsMonophyletic traitUnisexual floretsPolymorphism mappingPistillate floretsDetermination mechanismIntergeneric hybridsTribe AndropogoneaeExpression patternsSubepidermal cellsDeletion mutationsMolecular analysisEastern gamagrassGenesAndropogoneaeFloretsMaizeSimilar roleSpikeletsAllelesTasselseed2Definition of a large region of RAG1 that is important for coimmunoprecipitation of RAG2.
McMahan CJ, Sadofsky MJ, Schatz DG. Definition of a large region of RAG1 that is important for coimmunoprecipitation of RAG2. The Journal Of Immunology 1997, 158: 2202-10. PMID: 9036966, DOI: 10.4049/jimmunol.158.5.2202.Peer-Reviewed Original Research
1987
Isolation and sequence of a cDNA clone for human tyrosinase that maps at the mouse c-albino locus.
Kwon BS, Haq AK, Pomerantz SH, Halaban R. Isolation and sequence of a cDNA clone for human tyrosinase that maps at the mouse c-albino locus. Proceedings Of The National Academy Of Sciences Of The United States Of America 1987, 84: 7473-7477. PMID: 2823263, PMCID: PMC299318, DOI: 10.1073/pnas.84.21.7473.Peer-Reviewed Original ResearchConceptsCDNA clonesMelanocyte cDNA libraryRelated mRNA speciesHuman tyrosinaseAmino acid sequenceSouthern blot analysisStructural geneCDNA libraryNucleotide sequenceMRNA speciesAcid sequenceGlycosylation sitesCDNA insertDeletion mutationsCell typesAmino acidsCopper bindingBlot analysisClonesMalignant melanocytesLociSequenceTyrosinaseApproximate lengthKilobases
1983
Transcription of eukaryotic tRNA genes in vitro. II. Formation of stable complexes.
Schaack J, Sharp S, Dingermann T, Söll D. Transcription of eukaryotic tRNA genes in vitro. II. Formation of stable complexes. Journal Of Biological Chemistry 1983, 258: 2447-2453. PMID: 6549758, DOI: 10.1016/s0021-9258(18)32946-6.Peer-Reviewed Original ResearchConceptsStable transcription complex formationTRNA genesTranscription complex formationStable transcription complexesTranscription complexDrosophila Kc cell extractGene regionD-stemDrosophila tRNAArg geneEukaryotic tRNA genesDrosophila tRNA genesTranscription termination sequenceTRNAArg geneStable complexesComplex formationTranscription experimentsDNA regionsTranscription factorsFactor bindingCell-free extractsTermination sequenceSequence 5T-stemCell extractsDeletion mutations
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