2022
Targeting stem-loop 1 of the SARS-CoV-2 5′ UTR to suppress viral translation and Nsp1 evasion
Vora SM, Fontana P, Mao T, Leger V, Zhang Y, Fu TM, Lieberman J, Gehrke L, Shi M, Wang L, Iwasaki A, Wu H. Targeting stem-loop 1 of the SARS-CoV-2 5′ UTR to suppress viral translation and Nsp1 evasion. Proceedings Of The National Academy Of Sciences Of The United States Of America 2022, 119: e2117198119. PMID: 35149555, PMCID: PMC8892331, DOI: 10.1073/pnas.2117198119.Peer-Reviewed Original ResearchConceptsSARS-CoV-2SARS-CoV-2 nonstructural protein 1Host protein synthesisSARS-CoV-2 5Nonstructural protein 1Viral translationNucleic acid antisenseAntiviral immunityProtein synthesisTherapeutic targetTransgenic miceViral protein synthesisViral replicationDrug resistanceHuman ACE2Infected cellsProtein 1COVID-19Virulence mechanismsNanomolar concentrationsHost translationPathogenic virusesEntry channelSuppressionTranslational suppression
2018
A novel epigenetic modulating agent sensitizes pancreatic cells to a chemotherapy agent
Thakar M, Hu Y, Morreale M, Lerner L, Lin W, Sen R, Cai Y, Karunasena E, Thakar M, Saggi S, Keer H, Ahuja N. A novel epigenetic modulating agent sensitizes pancreatic cells to a chemotherapy agent. PLOS ONE 2018, 13: e0199130. PMID: 29927979, PMCID: PMC6013229, DOI: 10.1371/journal.pone.0199130.Peer-Reviewed Original ResearchConceptsPancreatic ductal adenocarcinomaDNA methyltransferase 1Chemotherapeutic agent irinotecanEpigenetic modulating agentsPDAC cell linesCell viabilityMechanism of actionSystemic chemotherapyCancer mortalityChemotherapy responseDuctal adenocarcinomaChemotherapy agentsEpigenetic sensitizationModulating agentsGuadecitabineAdditional studiesPancreatic cellsSerial concentrationsRest periodCell linesNanomolar concentrationsImproved responseEpigenetic modulatorsSensitizationMethyltransferase 1
2014
Glucocerebrosidase 2 gene deletion rescues type 1 Gaucher disease
Mistry PK, Liu J, Sun L, Chuang WL, Yuen T, Yang R, Lu P, Zhang K, Li J, Keutzer J, Stachnik A, Mennone A, Boyer JL, Jain D, Brady RO, New MI, Zaidi M. Glucocerebrosidase 2 gene deletion rescues type 1 Gaucher disease. Proceedings Of The National Academy Of Sciences Of The United States Of America 2014, 111: 4934-4939. PMID: 24639522, PMCID: PMC3977292, DOI: 10.1073/pnas.1400768111.Peer-Reviewed Original ResearchConceptsType 1 Gaucher's diseaseBone formation defectGaucher diseaseSerum ceramide levelsBone formation rateEnzyme replacement therapyViable therapeutic targetGD1 patientsGBA deficiencyEnhanced elevationTherapeutic targetBone volumeMononuclear phagocytesClinical phenotypeGBA geneConditional deletionBioactive lipidsSphingosine levelsDevelopment of inhibitorsCeramide levelsLysosomal glucocerebrosidasePatientsNanomolar concentrationsDiseaseMice
2013
Molecular Basis of Purinergic Signal Metabolism by Ectonucleotide Pyrophosphatase/Phosphodiesterases 4 and 1 and Implications in Stroke*♦
Albright RA, Ornstein DL, Cao W, Chang WC, Robert D, Tehan M, Hoyer D, Liu L, Stabach P, Yang G, De La Cruz EM, Braddock DT. Molecular Basis of Purinergic Signal Metabolism by Ectonucleotide Pyrophosphatase/Phosphodiesterases 4 and 1 and Implications in Stroke*♦. Journal Of Biological Chemistry 2013, 289: 3294-3306. PMID: 24338010, PMCID: PMC3916532, DOI: 10.1074/jbc.m113.505867.Peer-Reviewed Original ResearchConceptsExtracellular membrane proteinsMembrane proteinsSubstrate specificityMolecular basisHigh-resolution crystal structuresResolution crystal structureComparative structural analysisATP hydrolysisNPP1Brain vascular endotheliumCorresponding regionTerminal phosphateLow nanomolar concentrationsPurinergic signalsPlatelet aggregationProteinATPEnzymeNanomolar concentrationsVascular endotheliumPhosphodiesterases 4Ap3AMetabolismSurface of chondrocytesTissue mineralization
2011
Molecular Structure and Biological Activity of NPP-4, An Endothelial Cell Surface Pyrophosphatase/ Phosphodiesterase That Stimulates Platelet Aggregation and Secretion Via Liberation of ADP Upon Hydrolysis of Diadenosine Triphosphate
Ornstein D, Albright R, Chang W, Robert D, Cao W, De La Cruz E, Braddock D. Molecular Structure and Biological Activity of NPP-4, An Endothelial Cell Surface Pyrophosphatase/ Phosphodiesterase That Stimulates Platelet Aggregation and Secretion Via Liberation of ADP Upon Hydrolysis of Diadenosine Triphosphate. Blood 2011, 118: 701. DOI: 10.1182/blood.v118.21.701.701.Peer-Reviewed Original ResearchHigh-resolution structuresActive site threonineDense granule releaseDiadenosine triphosphateExtracellular spaceNanomolar concentrationsEnzyme familyPlatelet dense granulesMolecular foundationMolecular basisExtracellular enzymesStructural basisPhosphodiesterase enzyme familyGranule releaseEnzymatic mechanismCell surfaceRapid disaggregationEndothelial cell surfaceDense granulesPlatelet aggregationAp3AEnzymatic productBiological activityConcentration-dependent fashionADP
2010
Functional Studies of Plasmodium falciparum Dipeptidyl Aminopeptidase I Using Small Molecule Inhibitors and Active Site Probes
Deu E, Leyva MJ, Albrow VE, Rice MJ, Ellman JA, Bogyo M. Functional Studies of Plasmodium falciparum Dipeptidyl Aminopeptidase I Using Small Molecule Inhibitors and Active Site Probes. Cell Chemical Biology 2010, 17: 808-819. PMID: 20797610, PMCID: PMC2929396, DOI: 10.1016/j.chembiol.2010.06.007.Peer-Reviewed Original ResearchConceptsDipeptidyl aminopeptidasesActivity-based probesSmall molecules resultsNew targetsSmall molecule inhibitorsDipeptidyl aminopeptidase IActive site probesValuable new targetsAminopeptidase IAntimalarial targetImmature trophozoitesMolecule inhibitorsFunctional studiesCovalent inhibitorsParasite growthMalaria parasitesHemoglobin degradationSite probesLow nanomolar concentrationsSpecific inhibitionPlasmodium falciparumNanomolar concentrationsWidespread resistanceInhibitionTarget
2004
On Membrane Motor Activity and Chloride Flux in the Outer Hair Cell: Lessons Learned from the Environmental Toxin Tributyltin
Song L, Seeger A, Santos-Sacchi J. On Membrane Motor Activity and Chloride Flux in the Outer Hair Cell: Lessons Learned from the Environmental Toxin Tributyltin. Biophysical Journal 2004, 88: 2350-2362. PMID: 15596517, PMCID: PMC1305283, DOI: 10.1529/biophysj.104.053579.Peer-Reviewed Original ResearchConceptsLateral membranesCell’s mechanical activityOuter hair cellsMammalian cochlear amplifierHair cellsMembrane motorMarine mammalsIntact outer hair cellsPotent abilityFood chainNonselective conductanceCl(-) homeostasisPrestinNanomolar concentrationsExtracellular Cl- concentrationCl fluxMembraneCellsNew environmental threatsMammalsChloride effectTributyltinEnvironmental threatsHomeostasisNonlinear capacitance
1996
In vitro and in vivo inhibition of glioblastoma and neuroblastoma with MDL101731, a novel ribonucleoside diphosphate reductase inhibitor.
Piepmeier J, Rabidou N, Schold S, Bitonti A, Prakash N, Bush T. In vitro and in vivo inhibition of glioblastoma and neuroblastoma with MDL101731, a novel ribonucleoside diphosphate reductase inhibitor. Cancer Research 1996, 56: 359-61. PMID: 8542592.Peer-Reviewed Original ResearchConceptsMalignant brain tumorsMedian survivalControl animalsAthymic miceBrain tumorsReductase inhibitorsHuman malignant brain tumorsHuman glioblastomaDays of treatmentSK-N-MCConcentration-dependent inhibitionTumor regressionIntracerebral implantsIntracerebral xenograftsXenograft modelGlioblastoma cell linesVivo inhibitionPotent antiproliferative activityNeuroblastomaGlioblastomaSurvivalCell linesXenograftsNanomolar concentrationsTumors
1994
GTP-dependent binding of the antiproliferative agent didemnin to elongation factor 1 alpha.
Crews CM, Collins JL, Lane WS, Snapper ML, Schreiber SL. GTP-dependent binding of the antiproliferative agent didemnin to elongation factor 1 alpha. Journal Of Biological Chemistry 1994, 269: 15411-15414. PMID: 8195179, DOI: 10.1016/s0021-9258(17)40692-2.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsAnti-Infective AgentsCarrier ProteinsCattleChromatography, AffinityDepsipeptidesGuanosine TriphosphateHumansIndicators and ReagentsKineticsMolecular Sequence DataPeptide Elongation Factor 1Peptide Elongation FactorsPeptides, CyclicProtein Synthesis InhibitorsSequence Homology, Amino AcidConceptsEF-1 alphaPotential antineoplastic drugElongation factor 1 alphaDidemnin BProtein synthesisAntiproliferative activityG1 cell cycle progressionGTP-dependent bindingFactor 1 alphaClinical trialsCell cycle progressionImmunosuppressive activityAntineoplastic drugsPeptide sequence analysisElongation factorMode of actionUndefined mechanismPresence of GTPGTPase activityCycle progressionNanomolar concentrationsSequence analysisAlphaMarine natural productsIntracellular targets
1984
2,3,7,8-Tetrachlorodibenzo-p-dioxin Induces Hyperplasia in Confluent Cultures of Human Keratinocytes
Milstone L, LaVigne J. 2,3,7,8-Tetrachlorodibenzo-p-dioxin Induces Hyperplasia in Confluent Cultures of Human Keratinocytes. Journal Of Investigative Dermatology 1984, 82: 532-534. PMID: 6210328, DOI: 10.1111/1523-1747.ep12261149.Peer-Reviewed Original Research
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