2025
Human CCR4 deadenylase homolog Angel1 is a Non-Stop mRNA Decay factor.
Nicholson-Shaw T, Dowdle M, Ajaj Y, Perelis M, Fulzele A, Yeo G, Bennett E, Lykke-Andersen J. Human CCR4 deadenylase homolog Angel1 is a Non-Stop mRNA Decay factor. RNA 2025, rna.080399.125. PMID: 40441874, DOI: 10.1261/rna.080399.125.Peer-Reviewed Original ResearchMRNA decayRibosome-associated quality controlAbsence of stop codonsQuality control pathwaysMRNA decay factorsMRNA coding regionNonsense-mediated decayTargets aberrant mRNAsNascent polypeptidesCatalytic residuesPremature polyadenylationReporter mRNAAberrant mRNAsCoding regionStabilization of reporter mRNAsStop codonAngel1Control pathwaysBiochemical activityHuman cellsCodonMRNAPathwayDecayPolyadenylation
2022
Looking lively: emerging principles of pseudokinase signaling
Sheetz JB, Lemmon MA. Looking lively: emerging principles of pseudokinase signaling. Trends In Biochemical Sciences 2022, 47: 875-891. PMID: 35585008, PMCID: PMC9464697, DOI: 10.1016/j.tibs.2022.04.011.Peer-Reviewed Original Research
2018
Flipping ATP to AMPlify Kinase Functions
Sheetz JB, Lemmon MA. Flipping ATP to AMPlify Kinase Functions. Cell 2018, 175: 641-642. PMID: 30340038, PMCID: PMC6421561, DOI: 10.1016/j.cell.2018.10.011.Peer-Reviewed Original Research
2015
Phosphothreonine as a Catalytic Residue in Peptide‐Mediated Asymmetric Transfer Hydrogenations of 8‐Aminoquinolines
Shugrue CR, Miller SJ. Phosphothreonine as a Catalytic Residue in Peptide‐Mediated Asymmetric Transfer Hydrogenations of 8‐Aminoquinolines. Angewandte Chemie International Edition 2015, 54: 11173-11176. PMID: 26246129, PMCID: PMC4628550, DOI: 10.1002/anie.201505898.Peer-Reviewed Original ResearchConceptsTransfer hydrogenationChiral phosphoric acid catalystHydrogen bonding interactionsPhosphoric acid catalystAsymmetric transfer hydrogenationEnantioselective transfer hydrogenationAsymmetric catalystsAcid catalystStrong complexationNMR studiesSubstrate classesCatalystHydrogenationNew classCatalytic residuesPeptidesComplexationEnantioselectivityQuinolinePhosphopeptidesSubstrateResidues
2012
Active site residues critical for flavin binding and 5,6‐dimethylbenzimidazole biosynthesis in the flavin destructase enzyme BluB
Yu T, Mok K, Kennedy K, Valton J, Anderson K, Walker G, Taga M. Active site residues critical for flavin binding and 5,6‐dimethylbenzimidazole biosynthesis in the flavin destructase enzyme BluB. Protein Science 2012, 21: 839-849. PMID: 22528544, PMCID: PMC3403419, DOI: 10.1002/pro.2068.Peer-Reviewed Original ResearchConceptsConserved ResiduesFlavin mononucleotideReduced catalytic functionPurified mutant proteinsBacterium Sinorhizobium melilotiActive site residuesReduced flavin mononucleotideFlavin isoalloxazine ringCatalytic residuesMutant proteinsFlavin bindingDMB synthesisStructure-function relationshipsActive siteEnzyme familyGenetic screeningSite residuesMutant formsLower axial ligandBound flavinCatalytic functionMutantsEnzyme assaysIsoalloxazine ringBluB
2011
Ammonia Channeling in Plasmodium falciparum GMP Synthetase: Investigation by NMR Spectroscopy and Biochemical Assays
Bhat JY, Venkatachala R, Singh K, Gupta K, Sarma SP, Balaram H. Ammonia Channeling in Plasmodium falciparum GMP Synthetase: Investigation by NMR Spectroscopy and Biochemical Assays. Biochemistry 2011, 50: 3346-3356. PMID: 21413787, DOI: 10.1021/bi1017057.Peer-Reviewed Original ResearchConceptsGMP synthetasePlasmodium falciparum GMP synthetaseBiochemical assaysPurine biosynthetic pathwayAmmonia channelingGlutamine amidotransferasesGlutaminase domainMolecular tunnelBiosynthetic pathwayCatalytic residuesGlutaminase siteSeparate active sitesExternal mediumThioester intermediateExternal ammoniaCys-102NMR spectroscopyConcentration of glutamineSynthetaseUncompetitive inhibitorGlutamineActive siteSynthetase siteProton NMR spectroscopyAssaysChloride Regulation of Enzyme Turnover: Application to the Role of Chloride in Photosystem II
Pokhrel R, McConnell IL, Brudvig GW. Chloride Regulation of Enzyme Turnover: Application to the Role of Chloride in Photosystem II. Biochemistry 2011, 50: 2725-2734. PMID: 21366335, DOI: 10.1021/bi2000388.Peer-Reviewed Original ResearchConceptsOxygen-evolving complexPhotosystem IICatalytic residuesChloride-binding siteRecent structural evidenceCyanobacterial photosystem IISalt bridgeEnzyme-substrate complexΑ-amylaseResidue crucialConformational shiftS-state cycleLys residuesCarboxylate residuesEnzyme turnoverChloride regulationResiduesD61Structural evidenceManganese clusterEnzymeBindingD1Potential mechanismsArg
2000
Identification of Two Catalytic Residues in RAG1 that Define a Single Active Site within the RAG1/RAG2 Protein Complex
Fugmann S, Villey I, Ptaszek L, Schatz D. Identification of Two Catalytic Residues in RAG1 that Define a Single Active Site within the RAG1/RAG2 Protein Complex. Molecular Cell 2000, 5: 97-107. PMID: 10678172, DOI: 10.1016/s1097-2765(00)80406-2.Peer-Reviewed Original ResearchConceptsActive siteDivalent metal ionsSingle active siteMetal ionsTransfer reactionsActive site regionProtein complexesBond breakageCatalysisCatalytic functionRegion of RAG1Strand transfer reactionSecondary structure prediction algorithmsAspartic acid residuesCatalytic residuesRAG2 proteinsComplexesStructure prediction algorithmsPossible structural similaritySite regionAcid residuesRetroviral integrasesRAG1Structural similarityIons
1995
Mechanism of Inhibition of HIV-1 Reverse Transcriptase by Nonnucleoside Inhibitors
Spence R, Kati W, Anderson K, Johnson K. Mechanism of Inhibition of HIV-1 Reverse Transcriptase by Nonnucleoside Inhibitors. Science 1995, 267: 988-993. PMID: 7532321, PMCID: PMC7526747, DOI: 10.1126/science.7532321.Peer-Reviewed Original ResearchConceptsActive site catalytic residuesPre-steady-state kinetic analysisNucleotide-induced conformational changesInterfere with nucleotide bindingPre-steady-state burstEnzyme-DNA complexPre-steady-stateReverse transcriptasePresence of saturating concentrationsCatalytic residuesNucleotide bindingNucleoside triphosphatesDNA polymerizationNucleotide analogsHydrophobic pocketMechanism of inhibitionNonnucleoside inhibitorsConformational changesNoncompetitive inhibitorInhibition of HIV-1 reverse transcriptaseKinetic analysisHIV-1 reverse transcriptaseSaturating concentrationsTranscriptaseInhibitors
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