2001
Mechanisms for Increased Levels of Phosphorylation of Elongation Factor-2 during Hibernation in Ground Squirrels †
Chen Y, Matsushita M, Nairn A, Damuni Z, Cai D, Frerichs K, Hallenbeck J. Mechanisms for Increased Levels of Phosphorylation of Elongation Factor-2 during Hibernation in Ground Squirrels †. Biochemistry 2001, 40: 11565-11570. PMID: 11560506, DOI: 10.1021/bi010649w.Peer-Reviewed Original ResearchConceptsEukaryotic elongation factor 2EEF-2 phosphorylationElongation factor 2Elongation phaseEEF-2 kinase activityProtein phosphatase 2AGround squirrelsLevel of phosphorylationFactor 2Phosphatase 2ACellular functionsCatalytic subunitUncharacterized mechanismKinase activityInhibitor 2Protein synthesisPhosphorylationPP2AHibernating animalsActive animalsHibernatorsReversible mechanismSevere reductionSquirrelsHibernation
1996
Structure, Regulation, and Function of Calcium/Calmodulin-Dependent Protein Kinase I
Picciotto M, Nastiuk K, Nairn A. Structure, Regulation, and Function of Calcium/Calmodulin-Dependent Protein Kinase I. Advances In Pharmacology 1996, 36: 251-275. PMID: 8783563, DOI: 10.1016/s1054-3589(08)60585-2.Peer-Reviewed Original ResearchConceptsProtein kinaseProtein kinase CMyosin light chain kinaseKinase ICaM kinaseSecond messenger-regulated protein kinasesCalmodulin-dependent protein kinase ICalcium/calmodulin-dependent protein kinase ICAMP-dependent protein kinaseSpecific subcellular locationsMultifunctional protein kinaseTerminal regulatory domainDependent protein kinaseCaM kinase familyClass of enzymesProtein kinase ICaM kinase IAmino acid residuesMyosin P-light chainDomain bindsAutoinhibitory mechanismRegulatory domainKinase familyProtein phosphorylationLight chain kinase
1995
Three-dimensional structure of the catalytic subunit of protein serine/threonine phosphatase-1
Goldberg J, Huang H, Kwon Y, Greengard P, Nairn A, Kuriyan J. Three-dimensional structure of the catalytic subunit of protein serine/threonine phosphatase-1. Nature 1995, 376: 745-753. PMID: 7651533, DOI: 10.1038/376745a0.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBinding SitesCatalysisCrystallography, X-RayDopamine and cAMP-Regulated Phosphoprotein 32Escherichia coliHumansIntracellular Signaling Peptides and ProteinsMetalsMicrocystinsModels, MolecularMolecular Sequence DataNerve Tissue ProteinsNuclear ProteinsPeptides, CyclicPhosphoprotein PhosphatasesPhosphoproteinsProtein ConformationProtein Phosphatase 1ProteinsRabbitsRecombinant ProteinsRNA-Binding ProteinsSequence Homology, Amino AcidConceptsPhosphatase 1Protein serine/threonine phosphatase-1Serine/threonine phosphatase 1Mammalian protein phosphatase 1Protein phosphatase 1Potential binding sitesThree-dimensional structureCatalytic subunitRegulatory sequencesCatalytic domainCarboxy terminusΒ scaffoldBinding sitesActive siteSurface groovesTerminusSubunitsDomainProteinCrystal structureSitesTyrosineMetalloenzymesSequenceToxin