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
1997
Site-directed mutagenesis of amino acid residues of protein phosphatase 1 involved in catalysis and inhibitor binding
Huang H, Horiuchi A, Goldberg J, Greengard P, Nairn A. Site-directed mutagenesis of amino acid residues of protein phosphatase 1 involved in catalysis and inhibitor binding. Proceedings Of The National Academy Of Sciences Of The United States Of America 1997, 94: 3530-3535. PMID: 9108010, PMCID: PMC20473, DOI: 10.1073/pnas.94.8.3530.Peer-Reviewed Original ResearchConceptsProtein phosphatase 1Site-directed mutagenesisActive site residuesOkadaic acidPhosphatase 1Calyculin AMammalian protein phosphatase 1PP-1Site residuesEnzyme activityMutation of residuesAmino acid residuesMechanism of catalysisActive siteInhibitor bindingAcid residuesInhibitory proteinMutationsResiduesMutagenesisDivalent cationsToxinY272Large lossesR221Characterization of the interaction between DARPP-32 and protein phosphatase 1 (PP-1): DARPP-32 peptides antagonize the interaction of PP-1 with binding proteins
Kwon Y, Huang H, Desdouits F, Girault J, Greengard P, Nairn A. Characterization of the interaction between DARPP-32 and protein phosphatase 1 (PP-1): DARPP-32 peptides antagonize the interaction of PP-1 with binding proteins. Proceedings Of The National Academy Of Sciences Of The United States Of America 1997, 94: 3536-3541. PMID: 9108011, PMCID: PMC20474, DOI: 10.1073/pnas.94.8.3536.Peer-Reviewed Original ResearchConceptsPP-1cPP-1C.PP-1DARPP-32Inhibitor 2Protein phosphatase 1Amino acid sequence analysisAmino acid residuesNH2-terminal regionAcid sequence analysisPhosphoinhibitor-1Threonine residuesPhosphatase 1Inhibitor-1Catalytic subunitCalyculin AOkadaic acidInhibitor proteinActive siteAcid residuesSequence analysisProteinEnzyme activityMotifResidues
1995
Phosphorylation of DARPP-32, a Dopamine- and cAMP-regulated Phosphoprotein, by Casein Kinase I in Vitro and in Vivo *
Desdouits F, Cohen D, Nairn A, Greengard P, Girault J. Phosphorylation of DARPP-32, a Dopamine- and cAMP-regulated Phosphoprotein, by Casein Kinase I in Vitro and in Vivo *. Journal Of Biological Chemistry 1995, 270: 8772-8778. PMID: 7721783, DOI: 10.1074/jbc.270.15.8772.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceCasein KinasesCattleCorpus StriatumCyclic AMPDNA PrimersDopamineDopamine and cAMP-Regulated Phosphoprotein 32Electrophoresis, Polyacrylamide GelHumansMolecular Sequence DataMutagenesis, Site-DirectedNerve Tissue ProteinsNeuronsPeptide MappingPhosphoproteinsPhosphorylationProtein KinasesRabbitsRatsSubstantia NigraConceptsCasein kinase IProtein phosphatase 1Kinase ISer-137Phosphatase 1Ser-189DARPP-32CAMP-dependent protein kinasePhosphatase-1 inhibitorStoichiometry of phosphorylationSite-directed mutagenesisSpecific cell populationsProtein kinaseProtein sequencingSeryl residuesAcidic residuesThr-34PhosphorylationPhosphate/Presence of SDSChoroid plexus epithelial cellsResiduesCell populationsElectrophoretic mobilityEpithelial cells
1984
The amino acid sequence of rabbit skeletal muscle calmodulin
Nairn A, Grand R, Perry S. The amino acid sequence of rabbit skeletal muscle calmodulin. FEBS Letters 1984, 167: 215-220. PMID: 6698209, DOI: 10.1016/0014-5793(84)80129-5.Peer-Reviewed Original ResearchConceptsSingle polypeptide chainMyosin light chain kinaseBlocked N terminusRabbit skeletal muscleLight chain kinasePhosphorylase kinaseMammalian calmodulinN-terminusPolypeptide chainResidues 48Chain kinaseAmide assignmentsCalmodulinLow ionic strength bufferKinaseSkeletal muscleIonic strength bufferSequenceN-terminal tripeptideStrength bufferTerminal tripeptideTerminusSubunitsProteinResidues
1979
PHOSPHORYLATION OF THE MYOFIBRILLAR PROTEINS
Perry S, Cole H, Frearson N, Moir A, Nairn A, Solaro R. PHOSPHORYLATION OF THE MYOFIBRILLAR PROTEINS. 1979, 147-159. DOI: 10.1016/b978-0-08-023178-5.50018-5.Peer-Reviewed Original ResearchCyclic AMP-dependent protein kinaseAMP-dependent protein kinaseProtein kinaseSerine 20Covalent phosphateHalf-maximal ATPase activityMyofibrillar proteinsMaximal ATPase activityPhysiological functionsPhosphorylationATPase activityIntracellular ATPKinaseProteinIncorporation of 32pPhosphate groupsInorganic phosphateATPResiduesPhosphate contentPhosphate