1992
MARCKS is an actin filament crosslinking protein regulated by protein kinase C and calcium–calmodulin
Hartwig J, Thelen M, Resen A, Janmey P, Nairn A, Aderem A. MARCKS is an actin filament crosslinking protein regulated by protein kinase C and calcium–calmodulin. Nature 1992, 356: 618-622. PMID: 1560845, DOI: 10.1038/356618a0.Peer-Reviewed Original ResearchMeSH KeywordsActin CytoskeletonActinsAmino Acid SequenceAnimalsBrainCalciumCalmodulinCattleCross-Linking ReagentsHomeostasisIntracellular Signaling Peptides and ProteinsKineticsMembrane ProteinsMicroscopy, ElectronMolecular Sequence DataMusclesMyristoylated Alanine-Rich C Kinase SubstratePhosphorylationProtein Kinase CProteinsRabbitsTime FactorsConceptsProtein kinase CPlasma membraneCalcium-calmodulinKinase CSignal transduction pathwaysPKC signal transduction pathwayActin filament crosslinking proteinActin cytoskeletonActin assemblyTransduction pathwaysMARCKS proteinFilamentous actinCrosslinking activitySpecific substratesSubstrates bindMARCKSCell morphologyProteinPhosphorylationActinMembraneCytoskeletonCalmodulinCytoplasmBinds
1988
DARPP‐32 and Phosphatase Inhibitor‐1, Two Structurally Related Inhibitors of Protein Phosphatase‐1, Are Both Present in Striatonigral Neurons
Nairn A, Hemmings H, Walaas S, Greengard P. DARPP‐32 and Phosphatase Inhibitor‐1, Two Structurally Related Inhibitors of Protein Phosphatase‐1, Are Both Present in Striatonigral Neurons. Journal Of Neurochemistry 1988, 50: 257-262. PMID: 3335843, DOI: 10.1111/j.1471-4159.1988.tb13258.x.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBasal GangliaCarrier ProteinsCorpus StriatumDopamine and cAMP-Regulated Phosphoprotein 32Electrophoresis, Polyacrylamide GelIntracellular Signaling Peptides and ProteinsKainic AcidMaleMusclesNerve Tissue ProteinsNeuronsPhosphoproteinsPhosphorylationProteinsRatsRats, Inbred StrainsSubstantia NigraConceptsPhosphatase inhibitor-1Protein phosphatase 1Phosphatase 1DARPP-32Inhibitor-1Striatonigral neuronsSubstantia nigraKainic acidStriatonigral fibersBiochemical propertiesRelated inhibitorsSpecific neuronal subpopulationsIpsilateral substantia nigraBovine caudate nucleusSpecific activityStriatal neuronsNeuronal localizationRat neostriatumNeuronal subpopulationsRat brainCaudate nucleusLesioned neostriatumNeostriatumNeuronsInhibitors
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
1980
THE RELATIONSHIP OF THE STRUCTURE TO THE FUNCTION OF CALMODULIN IN THE MYOSIN LIGHT CHAIN KINASE SYSTEM
Nairn A, Grand R, Wall C, Perry S. THE RELATIONSHIP OF THE STRUCTURE TO THE FUNCTION OF CALMODULIN IN THE MYOSIN LIGHT CHAIN KINASE SYSTEM. Annals Of The New York Academy Of Sciences 1980, 356: 413-414. PMID: 6940506, DOI: 10.1111/j.1749-6632.1980.tb29653.x.Peer-Reviewed Original Research
1979
The Role of Calmodulin in the Structure and Regulation of Phosphorylase Kinase from Rabbit Skeletal Muscle
SHENOLIKAR S, COHEN P, COHEN P, NAIRN A, PERRY S. The Role of Calmodulin in the Structure and Regulation of Phosphorylase Kinase from Rabbit Skeletal Muscle. The FEBS Journal 1979, 100: 329-337. PMID: 159817, DOI: 10.1111/j.1432-1033.1979.tb04175.x.Peer-Reviewed Original ResearchThe role of calmodulin in the myosin light-chain kinase system [proceedings].
NAIRN A, PERRY S. The role of calmodulin in the myosin light-chain kinase system [proceedings]. Biochemical Society Transactions 1979, 7: 966-7. PMID: 229046, DOI: 10.1042/bst0070966.Peer-Reviewed Original ResearchCalcium-binding proteins and the regulation of contractile activity.
PERRY S, GRAND R, NAIRN A, VANAMAN T, WALL C. Calcium-binding proteins and the regulation of contractile activity. Biochemical Society Transactions 1979, 7: 619-22. PMID: 383543, DOI: 10.1042/bst0070619.Peer-Reviewed Original ResearchCalmodulin and myosin light-chain kinase of rabbit fast skeletal muscle
Nairn A, Perry S. Calmodulin and myosin light-chain kinase of rabbit fast skeletal muscle. Biochemical Journal 1979, 179: 89-97. PMID: 224861, PMCID: PMC1186598, DOI: 10.1042/bj1790089.Peer-Reviewed Original Research