2023
A Multi-Omic Mosaic Model of Acetaminophen Induced Alanine Aminotransferase Elevation
Monte A, Vest A, Reisz J, Berninzoni D, Hart C, Dylla L, D’Alessandro A, Heard K, Wood C, Pattee J. A Multi-Omic Mosaic Model of Acetaminophen Induced Alanine Aminotransferase Elevation. Journal Of Medical Toxicology 2023, 19: 255-261. PMID: 37231244, PMCID: PMC10212224, DOI: 10.1007/s13181-023-00951-5.Peer-Reviewed Original ResearchConceptsGenome-wide association studiesTricarboxylic acid cycleMitochondrial energy productionLiver injuryGenomic dataALT elevationIdentification of genesTherapeutic doses of APAPAlanine aminotransferase elevationPredicting liver injuryDose of APAPMaltose metabolismAPAP-induced liver injuryMechanism of injuryAssociation studiesGenetic analysisRandomized controlled trialsAminotransferase elevationGenetic variantsAcid cycleClinical outcomesTherapeutic dosesMultiomics approachGenetic controlAPAP liver injury
2020
Effects of Iron Isomaltoside vs Ferric Carboxymaltose on Hypophosphatemia in Iron-Deficiency Anemia
Wolf M, Rubin J, Achebe M, Econs MJ, Peacock M, Imel EA, Thomsen LL, Carpenter TO, Weber T, Brandenburg V, Zoller H. Effects of Iron Isomaltoside vs Ferric Carboxymaltose on Hypophosphatemia in Iron-Deficiency Anemia. JAMA 2020, 323: 432-443. PMID: 32016310, PMCID: PMC7042864, DOI: 10.1001/jama.2019.22450.Peer-Reviewed Original ResearchConceptsIron deficiency anemiaFerric carboxymaltoseIncidence of hypophosphatemiaIron isomaltosideDay 0Oral ironBone homeostasisCommon adverse drug reactionsFibroblast growth factor 23Trial ABiomarkers of mineralIntravenous iron isomaltosideRisk of hypophosphatemiaPrimary end pointReduced kidney functionGrowth factor 23Adverse drug reactionsIntravenous ironSerum phosphateFactor 23Kidney functionParathyroid hormoneRandomized trialsClinic sitesDrug reactions
2001
The Single Transmembrane Domains of ErbB Receptors Self-associate in Cell Membranes*
Mendrola JM, Berger MB, King MC, Lemmon MA. The Single Transmembrane Domains of ErbB Receptors Self-associate in Cell Membranes*. Journal Of Biological Chemistry 2001, 277: 4704-4712. PMID: 11741943, DOI: 10.1074/jbc.m108681200.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid MotifsAmino Acid SequenceCell MembraneChloramphenicol O-AcetyltransferaseDimerizationDNA Mutational AnalysisErbB ReceptorsEscherichia coliGenetic VectorsGlutamic AcidHumansLigandsMaltoseModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedMutationProtein Structure, TertiaryReceptor Protein-Tyrosine KinasesReceptor, ErbB-2Receptor, ErbB-3Receptor, ErbB-4Recombinant Fusion ProteinsSequence Homology, Amino AcidValineConceptsTM domain interactionsTM domainReceptor tyrosine kinasesEpidermal growth factor receptorGrowth factor receptorDomain interactionsSingle transmembrane alpha-helixReceptor dimersTyrosine kinaseExtracellular domainErbB receptor functionEscherichia coli cell membraneSingle transmembrane domainTransmembrane alpha-helixErbB receptorsCell membraneLimited mutational analysisFactor receptorGlutamic acid mutationTransmembrane domainGxxxG motifDomain dimerMutational analysisAlpha-helixErythropoietin receptor
1993
Folding in vivo of bacterial cytoplasmic proteins: Role of GroEL
Horwich A, Low K, Fenton W, Hirshfield I, Furtak K. Folding in vivo of bacterial cytoplasmic proteins: Role of GroEL. Cell 1993, 74: 909-917. PMID: 8104102, DOI: 10.1016/0092-8674(93)90470-b.Peer-Reviewed Original ResearchMeSH KeywordsATP-Binding Cassette TransportersBacterial ProteinsBacteriophage lambdaCarrier ProteinsChaperonin 60Citrate (si)-SynthaseEscherichia coliEscherichia coli ProteinsHeat-Shock ProteinsKetoglutarate Dehydrogenase ComplexMaltoseMaltose-Binding ProteinsMethionineMonosaccharide Transport ProteinsOperonOrnithine CarbamoyltransferasePlasmidsPolyribonucleotide NucleotidyltransferasePromoter Regions, GeneticProtein BiosynthesisProtein FoldingProtein Sorting SignalsSequence DeletionTemperatureTransduction, GeneticConceptsCytoplasmic proteinsTemperature-sensitive lethal mutationBacterial cytoplasmic proteinsE. coli chaperonin GroELMaltose-binding proteinRole of GroELNative tertiary structureEssential genesChaperonin GroELBacterial cytoplasmMutant cellsLethal mutationsNonpermissive temperatureGenetic informationPolynucleotide phosphorylaseGeneral translationTertiary structureCitrate synthasePathways of transferKetoglutarate dehydrogenaseGeneral roleGroELNative conformationProteinTest proteins
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