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
2001
Auto‐inhibition of Ca2+/calmodulin‐dependent protein kinase II by its ATP‐binding domain
Lengyel I, Nairn A, McCluskey A, Tóth G, Penke B, Rostas J. Auto‐inhibition of Ca2+/calmodulin‐dependent protein kinase II by its ATP‐binding domain. Journal Of Neurochemistry 2001, 76: 1066-1072. PMID: 11181826, DOI: 10.1046/j.1471-4159.2001.00139.x.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAnimalsBinding SitesCalcium-Calmodulin-Dependent Protein Kinase Type 1Calcium-Calmodulin-Dependent Protein Kinase Type 2Calcium-Calmodulin-Dependent Protein Kinase Type 4Calcium-Calmodulin-Dependent Protein KinasesCyclic AMP-Dependent Protein KinasesDose-Response Relationship, DrugEnzyme ActivationEnzyme InhibitorsPeptide FragmentsPeptidesProtein Structure, TertiaryRatsSubstrate SpecificityConceptsATP-binding domainDependent protein kinase IIProtein kinase IIProtein kinaseCaMPK-IIKinase IICAMP-dependent protein kinaseDependent protein kinaseSubstitution of phenylalaninePhysiological processesKey enzymeAutocamtide-2Position 25Phenylalanine 25Molecular interactionsKinasePeptide fragmentsDependent activityIndependent activityATPEnzymeCrucial roleIntramolecular interactionsDomainInhibition
1994
Regulation of the gating of cystic fibrosis transmembrane conductance regulator C1 channels by phosphorylation and ATP hydrolysis.
Hwang T, Nagel G, Nairn A, Gadsby D. Regulation of the gating of cystic fibrosis transmembrane conductance regulator C1 channels by phosphorylation and ATP hydrolysis. Proceedings Of The National Academy Of Sciences Of The United States Of America 1994, 91: 4698-4702. PMID: 7515176, PMCID: PMC43855, DOI: 10.1073/pnas.91.11.4698.Peer-Reviewed Original ResearchConceptsCFTR channelsATP hydrolysisPresence of ATPDomains of CFTRCystic fibrosis transmembrane conductance regulator (CFTR) Cl(-) channelProtein kinase AATP analogue 5'Kinase AOpen probabilityAMP-PNPPhosphorylationLow open probabilityCl- channelsATPATP actionIntact cardiac myocytesNucleotidesCFTRSecond siteExcised patchesHigh open probabilityCardiac myocytesChannel closingC1 channelsAnalogue 5Coupling of CFTR Cl− channel gating to an ATP hydrolysis cycle
Baukrowitz T, Hwang T, Nairn A, Gadsby D. Coupling of CFTR Cl− channel gating to an ATP hydrolysis cycle. Neuron 1994, 12: 473-482. PMID: 7512348, DOI: 10.1016/0896-6273(94)90206-2.Peer-Reviewed Original ResearchConceptsCystic fibrosis transmembrane conductance regulatorATP hydrolysis cycleHydrolysis cycleCFTR channelsFibrosis transmembrane conductance regulatorProtein kinase ATransmembrane conductance regulatorATP hydrolysisKinase AConductance regulatorNucleoside triphosphatesChannel openingInorganic phosphate analogueATPPhosphate analogueCardiac myocytesInorganic phosphateMean open timeRegulatorHydrolysis productsBeF3Open timeCycleTriphosphateRegulation of CFTR channel gating.
Gadsby D, Hwang T, Baukrowitz T, Nagel G, Horie M, Nairn A. Regulation of CFTR channel gating. The Journal Of Physiological Sciences 1994, 44 Suppl 2: s183-92. PMID: 7752525.Peer-Reviewed Original ResearchConceptsNon-hydrolyzable ATP analog AMP-PNPCystic fibrosis transmembrane conductance regulator (CFTR) Cl(-) channelAMP-PNPCFTR channel gatingProtein kinase A (PKA) phosphorylationATP analogue AMP-PNPAnalogue AMP-PNPCFTR's twoA PhosphorylationATP hydrolysisChannel gatingCl- channelsChannel openingNBDRegulationMultiple sitesPhosphorylationCFTROrthovanadateATPGatingDomain
1992
cGMP-dependent protein kinase regulation of a chloride channel in T84 cells
Lin M, Nairn A, Guggino S. cGMP-dependent protein kinase regulation of a chloride channel in T84 cells. American Journal Of Physiology 1992, 262: c1304-c1312. PMID: 1317106, DOI: 10.1152/ajpcell.1992.262.5.c1304.Peer-Reviewed Original ResearchConceptsProtein kinaseChloride channelsIntestinal epithelial cellsCGMP-dependent protein kinaseProtein kinase regulationApical membraneDependent protein kinaseT84 cellsEpithelial cellsInhibitor of PKGKinase regulationCatalytic subunitCombination of ATPNonhydrolyzable formExcessive fluid secretionIntracellular faceEscherichia coliElevated guanosineSingle-channel recordingsATPKinasePKGLinear current-voltage relationshipCellsChloride secretion
1990
Amiloride analogs induce the phosphorylation of elongation factor-2 in vascular endothelial cells.
Demolle D, Lecomte M, Boutherin-Falson O, Cragoe E, Nairn A, Boeynaems J. Amiloride analogs induce the phosphorylation of elongation factor-2 in vascular endothelial cells. Molecular Pharmacology 1990, 37: 827-32. PMID: 2359404.Peer-Reviewed Original ResearchConceptsElongation factor 2Protein synthesisFactor 2Rabbit reticulocyte lysateCell-free systemBovine aortic endothelial cellsDependent phosphorylationReticulocyte lysateEndothelial cellsAmiloride analoguesPhosphorylationSimilar MrCytosolic pHVascular endothelial cellsProteinAnalogues of amilorideAortic endothelial cellsPotent inhibitorInhibitory effectAntiportCellsEIPAAmilorideATPLysates
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