2018
Comprehensive functional genomic resource and integrative model for the human brain
Wang D, Liu S, Warrell J, Won H, Shi X, Navarro FCP, Clarke D, Gu M, Emani P, Yang YT, Xu M, Gandal MJ, Lou S, Zhang J, Park JJ, Yan C, Rhie SK, Manakongtreecheep K, Zhou H, Nathan A, Peters M, Mattei E, Fitzgerald D, Brunetti T, Moore J, Jiang Y, Girdhar K, Hoffman GE, Kalayci S, Gümüş ZH, Crawford GE, Roussos P, Akbarian S, Jaffe A, White K, Weng Z, Sestan N, Geschwind D, Knowles J, Gerstein M, Ashley-Koch A, Crawford G, Garrett M, Song L, Safi A, Johnson G, Wray G, Reddy T, Goes F, Zandi P, Bryois J, Jaffe A, Price A, Ivanov N, Collado-Torres L, Hyde T, Burke E, Kleiman J, Tao R, Shin J, Akbarian S, Girdhar K, Jiang Y, Kundakovic M, Brown L, Kassim B, Park R, Wiseman J, Zharovsky E, Jacobov R, Devillers O, Flatow E, Hoffman G, Lipska B, Lewis D, Haroutunian V, Hahn C, Charney A, Dracheva S, Kozlenkov A, Belmont J, DelValle D, Francoeur N, Hadjimichael E, Pinto D, van Bakel H, Roussos P, Fullard J, Bendl J, Hauberg M, Mangravite L, Peters M, Chae Y, Peng J, Niu M, Wang X, Webster M, Beach T, Chen C, Jiang Y, Dai R, Shieh A, Liu C, Grennan K, Xia Y, Vadukapuram R, Wang Y, Fitzgerald D, Cheng L, Brown M, Brown M, Brunetti T, Goodman T, Alsayed M, Gandal M, Geschwind D, Won H, Polioudakis D, Wamsley B, Yin J, Hadzic T, De La Torre Ubieta L, Swarup V, Sanders S, State M, Werling D, An J, Sheppard B, Willsey A, White K, Ray M, Giase G, Kefi A, Mattei E, Purcaro M, Weng Z, Moore J, Pratt H, Huey J, Borrman T, Sullivan P, Giusti-Rodriguez P, Kim Y, Sullivan P, Szatkiewicz J, Rhie S, Armoskus C, Camarena A, Farnham P, Spitsyna V, Witt H, Schreiner S, Evgrafov O, Knowles J, Gerstein M, Liu S, Wang D, Navarro F, Warrell J, Clarke D, Emani P, Gu M, Shi X, Xu M, Yang Y, Kitchen R, Gürsoy G, Zhang J, Carlyle B, Nairn A, Li M, Pochareddy S, Sestan N, Skarica M, Li Z, Sousa A, Santpere G, Choi J, Zhu Y, Gao T, Miller D, Cherskov A, Yang M, Amiri A, Coppola G, Mariani J, Scuderi S, Szekely A, Vaccarino F, Wu F, Weissman S, Roychowdhury T, Abyzov A. Comprehensive functional genomic resource and integrative model for the human brain. Science 2018, 362 PMID: 30545857, PMCID: PMC6413328, DOI: 10.1126/science.aat8464.Peer-Reviewed Original ResearchConceptsQuantitative trait lociCell type proportionsComprehensive functional genomics resourceExpression quantitative trait lociFunctional genomics resourcesSingle-cell expression profilesGene regulatory networksFurther quantitative trait lociPsychENCODE ConsortiumGenomic resourcesComprehensive online resourceRegulatory networksKey genesCross-population variationExpression profilesMolecular mechanismsCell typesGenesAdult brainPolygenic risk scoresStudy variantsChromatinSplicingGenetic riskInterpretable deep learning model
2005
Control of the CFTR channel's gates
Vergani P, Basso C, Mense M, Nairn A, Gadsby D. Control of the CFTR channel's gates. Biochemical Society Transactions 2005, 33: 1003-1007. DOI: 10.1042/bst0331003.Peer-Reviewed Original ResearchChannel gateIon channelsProtein family membersNBD dimer interfaceAnion-selective poreEvolutionary conservationABC proteinsCFTR moleculesForm homodimersTransmembrane domainATP bindingHeterodimer interfaceDimer interfaceMolecular mechanismsTight dimerizationNBDATPSingle-channel recordingsResiduesFamily membersNBD1NBD2Cystic fibrosis patientsMutagenesisHomodimerControl of the CFTR channel's gates.
Vergani P, Basso C, Mense M, Nairn A, Gadsby D. Control of the CFTR channel's gates. Biochemical Society Transactions 2005, 33: 1003-7. PMID: 16246032, PMCID: PMC2728124, DOI: 10.1042/bst20051003.Peer-Reviewed Original ResearchConceptsChannel gateIon channelsProtein family membersNBD dimer interfaceAnion-selective poreEvolutionary conservationABC proteinsCFTR moleculesForm homodimersTransmembrane domainATP bindingHeterodimer interfaceDimer interfaceMolecular mechanismsTight dimerizationNBDATPSingle-channel recordingsResiduesFamily membersNBD1NBD2Cystic fibrosis patientsMutagenesisHomodimer
1999
Protein phosphatase 1 modulation of neostriatal AMPA channels: regulation by DARPP–32 and spinophilin
Yan Z, Hsieh–Wilson L, Feng J, Tomizawa K, Allen P, Fienberg A, Nairn A, Greengard P. Protein phosphatase 1 modulation of neostriatal AMPA channels: regulation by DARPP–32 and spinophilin. Nature Neuroscience 1999, 2: 13-17. PMID: 10195174, DOI: 10.1038/4516.Peer-Reviewed Original ResearchConceptsPP-1Protein phosphatase 1DARPP-32Distinct molecular mechanismsPhosphatase 1Molecular mechanismsAMPA receptor-mediated synaptic transmissionPostsynaptic densityAMPA channelsRegulationSynaptic plasticitySpinophilinNeostriatal neuronsPlasticityPhysiological evidenceGlutamate channelsSynaptic transmissionAMPA receptorsPhosphoproteinProteinMechanismBindingActivityModulationCatalytic activity
1996
Amyloid β Peptide Formation in Cell-free Preparations REGULATION BY PROTEIN KINASE C, CALMODULIN, AND CALCINEURIN*
Desdouits F, Buxbaum J, Desdouits-Magnen J, Nairn A, Greengard P. Amyloid β Peptide Formation in Cell-free Preparations REGULATION BY PROTEIN KINASE C, CALMODULIN, AND CALCINEURIN*. Journal Of Biological Chemistry 1996, 271: 24670-24674. PMID: 8798734, DOI: 10.1074/jbc.271.40.24670.Peer-Reviewed Original ResearchConceptsProtein kinase CAction of PKCCell-free systemIntact cellsKinase CProtein phosphatase calcineurinCell-permeant inhibitorStimulation of PKCSpecific peptide inhibitorPhosphatase calcineurinMolecular mechanismsCalcineurinPeptide inhibitorRegulationShort peptidesCalmodulinCellsBeta peptideInhibitorsPeptide formationPeptidesMajor constituentsPronounced inhibitionCyclosporin ASingle substrate
1994
Role of elongation factor 2 in regulating peptide-chain elongation in the heart
Vary T, Nairn A, Lynch C. Role of elongation factor 2 in regulating peptide-chain elongation in the heart. American Journal Of Physiology 1994, 266: e628-e634. PMID: 7513958, DOI: 10.1152/ajpendo.1994.266.4.e628.Peer-Reviewed Original ResearchConceptsDiabetic ratsEF-2 contentFactor 2Protein synthesisInsulin therapyIncrease of RNADecreased translational efficiencyElongation factor 2RatsDiabetesCardiac muscleImpaired rateDecreased rateProgressive decreaseHeartInhibitionMolecular mechanismsRNA contentPeptide chain elongationH durationTherapyInsulinDecrease
1992
Phosphorylation of elongation factor 2 during Ca2+-mediated secretion from rat parotid acini
Hincke M, Nairn A. Phosphorylation of elongation factor 2 during Ca2+-mediated secretion from rat parotid acini. Biochemical Journal 1992, 282: 877-882. PMID: 1372803, PMCID: PMC1130869, DOI: 10.1042/bj2820877.Peer-Reviewed Original ResearchConceptsElongation factor 2Protein synthesisFactor 2Two-dimensional PAGECalmodulin-dependent phosphorylationRapid phosphorylationParotid acinar cellsMolecular mechanismsRat parotid cellsPhosphorylationPhorbol esterStimulation of secretionProteinParotid cellsAcinar cellsRat parotid aciniParotid aciniSpecific antiseraCellsCa2ImmunoprecipitationExtracellular Ca2SecretionStimulationInhibition
1989
Role of protein phosphorylation in neuronal signal transduction1
Hemmings H, Nairn A, McGuinness T, Huganir R, Greengard P. Role of protein phosphorylation in neuronal signal transduction1. The FASEB Journal 1989, 3: 1583-1592. PMID: 2493406, DOI: 10.1096/fasebj.3.5.2493406.Peer-Reviewed Original ResearchConceptsProtein phosphorylationSubstrate proteinsSignal transductionProtein kinaseMolecular mechanismsProtein phosphatase inhibitorSignal transduction processesPrecise molecular mechanismsAdditional molecular mechanismsSignal transduction1Extracellular signalsPhosphatase inhibitorAdditional phosphoproteinsPhysiological processesTransduction processesNicotinic acetylcholine receptorsPhosphorylationSynaptic transmissionNervous systemSynapsin IExcitable cellsDARPP-32TransductionKinaseNeurotransmitter release