2024
Absence of the dolichol synthesis gene DHRSX leads to N-glycosylation defects in Lec5 and Lec9 Chinese hamster ovary cells
Kentache T, Althoff C, Caligiore F, Souche E, Schulz C, Graff J, Pieters E, Stanley P, Contessa J, Van Schaftingen E, Matthijs G, Foulquier F, Bommer G, Wilson M. Absence of the dolichol synthesis gene DHRSX leads to N-glycosylation defects in Lec5 and Lec9 Chinese hamster ovary cells. Journal Of Biological Chemistry 2024, 300: 107875. PMID: 39395802, PMCID: PMC11607601, DOI: 10.1016/j.jbc.2024.107875.Peer-Reviewed Original ResearchLec9 cellsChinese hamster ovaryDolichol synthesisGlycosylation-deficient Chinese hamster ovaryLong-read whole-genome sequencingCell linesN-glycosylation machineryN-glycan synthesisN-glycosylation defectChinese hamster ovary cellsGenomic regionsDHRSXLec9Hamster ovary cellsGlycosylation defectsHuman enzymeMolecular causesSynthesis defectsDolicholSRD5A3Hamster ovaryLevels of dolicholOvary cellsPolyprenolsKinetic properties
2014
Structural studies provide clues for analog design of specific inhibitors of Cryptosporidium hominis thymidylate synthase–dihydrofolate reductase
Kumar VP, Cisneros JA, Frey KM, Castellanos-Gonzalez A, Wang Y, Gangjee A, White AC, Jorgensen WL, Anderson KS. Structural studies provide clues for analog design of specific inhibitors of Cryptosporidium hominis thymidylate synthase–dihydrofolate reductase. Bioorganic & Medicinal Chemistry Letters 2014, 24: 4158-4161. PMID: 25127103, PMCID: PMC4427026, DOI: 10.1016/j.bmcl.2014.07.049.Peer-Reviewed Original ResearchConceptsCompound 1Crystal structureActive siteCryptosporidium hominisSpecific inhibitorHydrogen-bonding interactionsDHFR active siteFolate biosynthesis pathwaySynthase-dihydrofolate reductaseTS active siteLead compound 1Van der WaalsDihydrofolate reductase enzymeBiosynthesis pathwayBond interactionsEssential enzymeHuman enzymeInhibitor methotrexateNovel seriesDer WaalsDrug targetsProtein residuesSubstrate analoguesStructural studiesReductase enzyme
2008
Novel non-active site inhibitor of Cryptosporidium hominis TS-DHFR identified by a virtual screen
Martucci WE, Udier-Blagovic M, Atreya C, Babatunde O, Vargo MA, Jorgensen WL, Anderson KS. Novel non-active site inhibitor of Cryptosporidium hominis TS-DHFR identified by a virtual screen. Bioorganic & Medicinal Chemistry Letters 2008, 19: 418-423. PMID: 19059777, PMCID: PMC2651159, DOI: 10.1016/j.bmcl.2008.11.054.Peer-Reviewed Original ResearchConceptsThymidylate synthase-dihydrofolate reductaseHuman enzymeNovel allosteric pocketSite inhibitorsSynthase-dihydrofolate reductaseFlavin mononucleotideActive site inhibitorsVirtual screenLinker regionAllosteric pocketInhibitor targetingSpecies specificitySite pocketDrug targetsCryptosporidium hominisNovel inhibitorsEnzymeMicromolar potencySelective inhibitorNoncompetitive inhibitorInhibitorsLead compoundsScreenPocketReductase
2003
Tertiary Structure of Thiopurine Methyltransferase from Pseudomonas syringae, a Bacterial Orthologue of a Polymorphic, Drug-metabolizing Enzyme
Scheuermann TH, Lolis E, Hodsdon ME. Tertiary Structure of Thiopurine Methyltransferase from Pseudomonas syringae, a Bacterial Orthologue of a Polymorphic, Drug-metabolizing Enzyme. Journal Of Molecular Biology 2003, 333: 573-585. PMID: 14556746, DOI: 10.1016/j.jmb.2003.08.039.Peer-Reviewed Original ResearchConceptsTertiary structureBacterial orthologuesPseudomonas syringaeConsensus topologyProteasomal-dependent pathwayEnzymatic activitySAM-dependent methyltransferasesUnstructured N-terminusSequence similarityThree-dimensional structureShares 45Dependent transmethylationProtein sequencesN-terminusHuman enzymePolymorphic proteinsBiochemical studiesS-adenosylmethionineOrthologuesSyringaeMethyltransferaseTissue enzymatic activityThiopurine methyltransferaseIntracellular conversionMultiple insertions
2002
Detection of anti-elongation factor 2 kinase (calmodulin-dependent protein kinase III) antibodies in patients with systemic lupus erythematosus
Arora S, Yang JM, Craft J, Hait W. Detection of anti-elongation factor 2 kinase (calmodulin-dependent protein kinase III) antibodies in patients with systemic lupus erythematosus. Biochemical And Biophysical Research Communications 2002, 293: 1073-1076. PMID: 12051769, DOI: 10.1016/s0006-291x(02)00324-8.Peer-Reviewed Original ResearchConceptsEEF-2KProtein kinaseSerine/threonine protein kinaseCalmodulin-dependent protein kinase IIIElongation factor 2 kinaseEukaryotic protein kinasesProtein translation apparatusProtein kinase IIIC. elegans enzymeThreonine protein kinaseAmino acid sequenceCell surface receptorsIntact enzyme activityTranslation apparatusKinase IIICellular proteinsCell divisionHigh-specificity antibodiesAcid sequenceHuman enzymeStructural domainsKinaseHuman cancersSurface receptorsEnzyme activity
1994
Purification of Human and Rat Kidney Aldose Reductase
Moeckel G, Hallbach J, Guder W. Purification of Human and Rat Kidney Aldose Reductase. Enzyme And Protein 1994, 48: 45-50. PMID: 7787970, DOI: 10.1159/000474968.Peer-Reviewed Original ResearchConceptsPurification of humanAldose reductaseRat kidney papillaRat kidney aldose reductaseSubstrate specificityHuman enzymeAffinity chromatographic procedureBlue SepharoseSDS-PAGESimilar molecular weightReductaseEnzymeMolecular weightSingle bandChromatographic procedureSorbitol formationKinetic constantsKidney papillaHuman kidneyHumansInner medulla
1985
A 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
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