2025
Structural basis for human NKCC1 inhibition by loop diuretic drugs
Zhao Y, Vidossich P, Forbush B, Ma J, Rinehart J, De Vivo M, Cao E. Structural basis for human NKCC1 inhibition by loop diuretic drugs. The EMBO Journal 2025, 44: 1540-1562. PMID: 39875725, PMCID: PMC11876703, DOI: 10.1038/s44318-025-00368-6.Peer-Reviewed Original ResearchConceptsLoop diureticsNa+-K+-Cl- cotransporterRenal salt reabsorptionEpithelial ion transportTreatment of edemaNKCC1 activityNKCC1 inhibitionChloride secretionSalt reabsorptionNKCC1Loop diuretic drugWNK kinasesDiuretic drugsBumetanideFurosemideHypertonic stressDiureticsIon transportTorsemideMolecular mechanismsCarboxyl groupsInhibitionCo-structureIons exitCells
2024
A Supramolecular Biosensor for Rapid and High-Throughput Quantification of a Disease-Associated Niacin Metabolite
Ueno M, Sugiyama H, Li F, Nishimura T, Arakawa H, Chen X, Cheng X, Takeuchi S, Takeshita Y, Takamura T, Miyagi S, Toyama T, Soga T, Masuo Y, Kato Y, Nakamura H, Tsujiguchi H, Hara A, Tajima A, Noguchi-Shinohara M, Ono K, Kurayoshi K, Kobayashi M, Tadokoro Y, Kasahara A, Shoulkamy M, Maeda K, Ogoshi T, Hirao A. A Supramolecular Biosensor for Rapid and High-Throughput Quantification of a Disease-Associated Niacin Metabolite. Analytical Chemistry 2024, 96: 14499-14507. PMID: 39183562, DOI: 10.1021/acs.analchem.4c02653.Peer-Reviewed Original ResearchHost-guest complexesPhotoinduced electron transferBiological samplesHigh-throughput quantificationSupramolecular hostsElectron transferSulfonate groupsFluorescence quenchingHigh-throughput screeningCarboxyl groupsHuman urineDetection limitMass spectrometryBinding affinityBiosensorNNMT inhibitorsPillar[6]areneDirect additionSupramolecularSulfonateHuman cancer cells in vivoCarboxylQuantificationSpectrometryMetabolitesA salt bridge of the C‐terminal carboxyl group regulates PHPT1 substrate affinity and catalytic activity
Zavala E, Dansereau S, Burke M, Lipchock J, Maschietto F, Batista V, Loria J. A salt bridge of the C‐terminal carboxyl group regulates PHPT1 substrate affinity and catalytic activity. Protein Science 2024, 33: e5009. PMID: 38747379, PMCID: PMC11094782, DOI: 10.1002/pro.5009.Peer-Reviewed Original ResearchConceptsCatalytic activityPhenylphosphonic acidAnalysis of molecular dynamics trajectoriesNMR chemical shiftsSalt bridgesMolecular dynamics trajectoriesC-terminal carboxyl groupChemical shiftsCombination of solution NMRMolecular dynamicsGuanidinium moietyCarboxyl groupsPara-nitrophenylphosphateSolution NMRActive site inhibitorsHistidine phosphataseActive siteElectrostatic interactionsDynamics trajectoriesEnzymatic functionC-terminusGlycine residuesSubstrate affinityBiochemical experimentsBinding affinityStructure, Self-Assembly, and Phase Behavior of Neuroactive N‑Acyl GABAs: Doxorubicin Encapsulation in NPGABA/DPPC Liposomes and Release Studies
Chinapaka R, Sivaramakrishna D, Choudhury S, Manasa K, Cheppali S, Swamy M. Structure, Self-Assembly, and Phase Behavior of Neuroactive N‑Acyl GABAs: Doxorubicin Encapsulation in NPGABA/DPPC Liposomes and Release Studies. Langmuir 2024, 40: 7883-7895. PMID: 38587263, DOI: 10.1021/acs.langmuir.3c03615.Peer-Reviewed Original ResearchConceptsHydrogen bondsSelf-AssemblyPowder X-ray diffraction studiesX-ray diffraction studiesOdd-even alternationN-acyl amino acidsDifferential scanning calorimetric studiesPhase behaviorAmide moietyAdjacent moleculesPhysiologically relevant pH.Molecular packingDiffraction studiesStable unilamellar vesiclesCrystal structureChain compoundsDimeric structureCarboxyl groupsHomologous seriesSupramolecular organizationThermotropic phase behaviorEquimolar mixtureRelevant pH.Calorimetric studiesChain length
1991
Isolation From Commercial Aurintricarboxylic Acid of the Most Effective Polymeric Inhibitors of von Willebrand Factor Interaction With Platelet Glycoprotein Ib. Comparison With Other Polyanionic and Polyaromatic Polymers
Weinstein M, Vosburgh E, Phillips M, Turner N, Chute-Rose L, Moake J. Isolation From Commercial Aurintricarboxylic Acid of the Most Effective Polymeric Inhibitors of von Willebrand Factor Interaction With Platelet Glycoprotein Ib. Comparison With Other Polyanionic and Polyaromatic Polymers. Blood 1991, 78: 2291-2298. PMID: 1932745, DOI: 10.1182/blood.v78.9.2291.2291.Peer-Reviewed Original ResearchConceptsPolyaromatic polymersCommercial aurintricarboxylic acidMolecular weight 200Aromatic polymersPolyanionic polymersPolymeric inhibitorsCarboxyl groupsPolymersExclusion chromatographyLarge polymersWeight 200Heterogeneous mixtureAggregationAurintricarboxylic acidVWF-mediated aggregationVWF-mediated platelet aggregationAcidPolyanionicSolutionChromatographyIsolation from commercial aurintricarboxylic acid of the most effective polymeric inhibitors of von Willebrand factor interaction with platelet glycoprotein Ib. Comparison with other polyanionic and polyaromatic polymers
Weinstein M, Vosburgh E, Phillips M, Turner N, Chute-Rose L, Moake J. Isolation from commercial aurintricarboxylic acid of the most effective polymeric inhibitors of von Willebrand factor interaction with platelet glycoprotein Ib. Comparison with other polyanionic and polyaromatic polymers. Blood 1991, 78: 2291-2298. DOI: 10.1182/blood.v78.9.2291.bloodjournal7892291.Peer-Reviewed Original ResearchPolyaromatic polymersCommercial aurintricarboxylic acidMolecular weight 200Aromatic polymersPolyanionic polymersPolymeric inhibitorsCarboxyl groupsPolymersExclusion chromatographyLarge polymersWeight 200Heterogeneous mixtureAggregationAurintricarboxylic acidVWF-mediated aggregationVWF-mediated platelet aggregationAcidSolutionChromatography
1990
Purification of the glutamyl-tRNA reductase from Chlamydomonas reinhardtii involved in delta-aminolevulinic acid formation during chlorophyll biosynthesis.
Chen M, Jahn D, O'Neill G, Söll D. Purification of the glutamyl-tRNA reductase from Chlamydomonas reinhardtii involved in delta-aminolevulinic acid formation during chlorophyll biosynthesis. Journal Of Biological Chemistry 1990, 265: 4058-4063. PMID: 2303495, DOI: 10.1016/s0021-9258(19)39702-9.Peer-Reviewed Original ResearchConceptsGlu-tRNA reductaseGlutamyl-tRNA reductaseGlu-tRNAChlamydomonas reinhardtiiTRNA-dependent transformationChloroplasts of plantsDelta-aminolevulinic acid formationApparent molecular massChlorophyll biosynthesisGlutamyl-tRNAHomologous tRNAsSecond enzymeActive enzymeMolecular massNondenaturing conditionsDifferent chromatographic separationsCertain bacteriaReductaseDelta-aminolevulinic acidReinhardtiiPorphyrin biosynthesisBiosynthesisStable complexesChromatographic separationCarboxyl groups
1980
Chemical modification reduces the conductance of sodium channels in nerve
Sigworth F, Spalding B. Chemical modification reduces the conductance of sodium channels in nerve. Nature 1980, 283: 293-295. PMID: 6965422, DOI: 10.1038/283293a0.Peer-Reviewed Original ResearchConceptsChemical modificationTrimethyloxonium ionSuch chemical modificationsCarboxyl groupsNegative chargeSuch reagentsTMO treatmentPermeability propertiesReagentsLinear instantaneous current-voltage relationshipSmaller single-channel conductancePropertiesPotent poisonNormal KdIonsModificationSaxitoxinCharge
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