2022
Genome Editing Using CRISPR-Cas9 and Autoimmune Diseases: A Comprehensive Review
Lee M, Shin J, Yang J, Lee K, Cha H, Hong J, Park Y, Choi E, Tizaoui K, Koyanagi A, Jacob L, Park S, Kim J, Smith L. Genome Editing Using CRISPR-Cas9 and Autoimmune Diseases: A Comprehensive Review. International Journal Of Molecular Sciences 2022, 23: 1337. PMID: 35163260, PMCID: PMC8835887, DOI: 10.3390/ijms23031337.Peer-Reviewed Original ResearchConceptsProprotein convertase subtilisin/kexin type 9Systemic lupus erythematosusAutoimmune diseasesInflammatory bowel diseaseLowering low-density lipoprotein cholesterolBlock proprotein convertase subtilisin/kexin type 9Rheumatoid arthritisLow-density lipoprotein cholesterolTreatment of autoimmune diseasesManagement of autoimmune diseasesMultiple sclerosisType 1 diabetes mellitusBody's own tissuesPolymorphisms of multiple genesGene therapyLupus erythematosusLipoprotein cholesterolOrnithine transcarbamylaseHereditary tyrosinemiaRare diseaseType 9Animal modelsCRISPR-Cas9 treatmentBowel diseaseCRISPR-Cas9
2011
Acute treatment of hyperammonemia by continuous renal replacement therapy in a newborn patient with ornithine transcarbamylase deficiency
Kim H, Park J, Park K, Lee J, Eun H, Kim J, Shin J. Acute treatment of hyperammonemia by continuous renal replacement therapy in a newborn patient with ornithine transcarbamylase deficiency. Clinical And Experimental Pediatrics 2011, 54: 425-428. PMID: 22232626, PMCID: PMC3250597, DOI: 10.3345/kjp.2011.54.10.425.Peer-Reviewed Original ResearchContinuous renal replacement therapyOrnithine transcarbamylase deficiencyRenal replacement therapyReplacement therapyContinuous venovenous hemodiafiltrationSerum ammonia levelInborn errors of metabolismAmmonia levelsDays of lifeTreatment of hyperammonemiaOrnithine transcarbamylaseErrors of metabolismNewborn patientsVenovenous hemodiafiltrationTreatment modalitiesAcute treatmentElevated ammonia levelsInherited disorderNo seizureInborn errorsHyperammonemiaNewbornsTherapyUrea cycleTreatment
1988
Mitochondrial Import and Processing of Mutant Human Ornithine Transcarbamylase Precursors in Cultured Cells
Isaya G, Fenton W, Hendrick J, Furtak K, Kalousek F, Rosenberg L. Mitochondrial Import and Processing of Mutant Human Ornithine Transcarbamylase Precursors in Cultured Cells. Molecular And Cellular Biology 1988, 8: 5150-5158. DOI: 10.1128/mcb.8.12.5150-5158.1988.Peer-Reviewed Original ResearchLeader peptideMitochondrial importMutant precursorHeLa cellsAssociated with mitochondriaHuman ornithine transcarbamylaseAmino acid substitutionsOrnithine transcarbamylase precursorIntact HeLa cellsIntramitochondrial locationLack of bindingMutant proteinsMitochondrial matrixAcid substitutionsActive enzymeActive trimerMitochondrial fractionTrypsin protectionAffinity columnFractionation studiesMitochondriaCultured cellsCytosolOrnithine transcarbamylaseMutationsMeiotic expression of human ornithine transcarbamylase in the testes of transgenic mice.
Kelley K, Chamberlain J, Nolan J, Horwich A, Kalousek F, Eisenstadt J, Herrup K, Rosenberg L. Meiotic expression of human ornithine transcarbamylase in the testes of transgenic mice. Molecular And Cellular Biology 1988, 8: 1821-1825. PMID: 2837657, PMCID: PMC363346, DOI: 10.1128/mcb.8.4.1821.Peer-Reviewed Original ResearchConceptsHuman ornithine transcarbamylaseFusion geneBase pairsProtein-coding sequencesMale germ cellsOrnithine transcarbamylaseMeiotic expressionRegulatory sequencesRegulatory regionsTransgenic micePachytene stageMouse metallothioneinTransgenic animalsGerm cellsGenesKilobasesTransgene expressionSequenceExpressionTranscarbamylaseMeiosisTetraploidMeiotic Expression of Human Ornithine Transcarbamylase in the Testes of Transgenic Mice
Kelley K, Chamberlain J, Nolan J, Horwich A, Kalousek F, Eisenstadt J, Herrup K, Rosenberg L. Meiotic Expression of Human Ornithine Transcarbamylase in the Testes of Transgenic Mice. Molecular And Cellular Biology 1988, 8: 1821-1825. DOI: 10.1128/mcb.8.4.1821-1825.1988.Peer-Reviewed Original ResearchHuman ornithine transcarbamylaseFusion geneBase pairsProtein-coding sequencesMale germ cellsOrnithine transcarbamylaseMeiotic expressionRegulatory sequencesRegulatory regionsTransgenic micePachytene stageMouse metallothioneinTransgenic animalsGerm cellsGenesKilobasesTransgene expressionSequenceExpressionTranscarbamylaseMeiosisTetraploid
1985
A leader peptide is sufficient to direct mitochondrial import of a chimeric protein.
Horwich A, Kalousek F, Mellman I, Rosenberg L. A leader peptide is sufficient to direct mitochondrial import of a chimeric protein. The EMBO Journal 1985, 4: 1129-1135. PMID: 3891325, PMCID: PMC554314, DOI: 10.1002/j.1460-2075.1985.tb03750.x.Peer-Reviewed Original ResearchConceptsChimeric precursor proteinsMitochondrial importLeader peptideChimeric precursorsDihydrofolate reductaseMost mitochondrial proteinsPost-translational importMutant CHO cell linesCloned nucleotide sequencePrecursor proteinOrnithine transcarbamylaseCell-free systemCHO cell linesEnzyme dihydrofolate reductaseMitochondrial proteinsMitochondrial localizationRegulatory elementsLeader sequenceNucleotide sequenceStable transformantsAdditional proteinsSelectable markerChimeric proteinLarger precursorIntact cellsExpression of amplified DNA sequences for ornithine transcarbamylase in HeLa cells: arginine residues may be required for mitochondrial import of enzyme precursor.
Horwich A, Fenton W, Firgaira F, Fox J, Kolansky D, Mellman I, Rosenberg L. Expression of amplified DNA sequences for ornithine transcarbamylase in HeLa cells: arginine residues may be required for mitochondrial import of enzyme precursor. Journal Of Cell Biology 1985, 100: 1515-1521. PMID: 3988798, PMCID: PMC2113848, DOI: 10.1083/jcb.100.5.1515.Peer-Reviewed Original ResearchConceptsMitochondrial importOTC precursorsHeLa cellsOrnithine transcarbamylaseArginine residuesMouse dihydrofolate reductaseNH2-terminal leader sequenceRate of importArginine analog canavanineViral regulatory elementsImmunoprecipitation of extractsMitochondrial localizationCDNA sequenceRegulatory elementsLeader sequenceDNA sequencesEnzyme precursorsMitochondrial enzymesCell extractsDihydrofolate reductaseEnzymatic activityBlot analysisNormal precursorsResiduesSubunitsA cDNA clone for the precursor of rat mitochondrial ornithine transcarbamylase: comparison of rat and human leader sequences and conservation of catalytic sites
Kraus J, Hodges P, Williamson C, Horwich A, Kalousek F, Williams K, Rosenberg L. A cDNA clone for the precursor of rat mitochondrial ornithine transcarbamylase: comparison of rat and human leader sequences and conservation of catalytic sites. Nucleic Acids Research 1985, 13: 943-952. PMID: 3839075, PMCID: PMC341044, DOI: 10.1093/nar/13.3.943.Peer-Reviewed Original ResearchConceptsAmino acid sequenceLeader sequenceAcid sequenceBasic residuesAmino-terminal leader sequenceE. coliComplete sequence homologyAmino acid residuesProtein sequence dataOrnithine transcarbamylaseCDNA clonesSequence dataDNA complementaryOrnithine transcarbamylasesSequence homologyEntire proteinHuman enzymeAcid residuesTranscarbamylasesComplementary DNAAmino acidsMessenger RNARat enzymeNucleotidesCatalytic site
1984
Human Ornithine Transcarbamylase Locus Mapped to Band Xp21.1 Near the Duchenne Muscular Dystrophy Locus
Lindgren V, de Martinville B, Horwich A, Rosenberg L, Francke U. Human Ornithine Transcarbamylase Locus Mapped to Band Xp21.1 Near the Duchenne Muscular Dystrophy Locus. Science 1984, 226: 698-700. PMID: 6494904, DOI: 10.1126/science.6494904.Peer-Reviewed Original ResearchConceptsMitochondrial enzyme ornithine transcarbamylaseHuman ornithine transcarbamylase geneSitu hybridization experimentsOrnithine transcarbamylase geneGene mapsX chromosomeHybridization experimentsDuchenne muscular dystrophy locusShort armGenesX chromosome abnormalitiesMuscular dystrophyCell linesOrnithine transcarbamylaseLociChromosome abnormalitiesCarrier detectionChromosomesDuchenne muscular dystrophyXp21.1DNATranscarbamylaseProbeDystrophyOrnithine transcarbamylase deficiencyStructure and Expression of a Complementary DNA for the Nuclear Coded Precursor of Human Mitochondrial Ornithine Transcarbamylase
Horwich A, Fenton W, Williams K, Kalousek F, Kraus J, Doolittle R, Konigsberg W, Rosenberg L. Structure and Expression of a Complementary DNA for the Nuclear Coded Precursor of Human Mitochondrial Ornithine Transcarbamylase. Science 1984, 224: 1068-1074. PMID: 6372096, DOI: 10.1126/science.6372096.Peer-Reviewed Original ResearchConceptsComplementary DNALeader peptideOrnithine transcarbamylaseAmino-terminal leader peptideMost mitochondrial proteinsComplete primary structureHuman ornithine transcarbamylaseFree cytoplasmic ribosomesMitochondrial matrix enzymeCultured HeLa cellsMitochondrial proteinsCytoplasmic ribosomesRegulatory elementsNucleotide sequenceStable transformantsMatrix enzymeAsparagine residuesAcidic residuesLarger precursorMature formPrimary structureProtein occursHeLa cellsEscherichia coliAmino acids
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