2017
Brain Region and Isoform-Specific Phosphorylation Alters Kalirin SH2 Domain Interaction Sites and Calpain Sensitivity
Miller MB, Yan Y, Machida K, Kiraly DD, Levy AD, Wu YI, Lam TT, Abbott T, Koleske AJ, Eipper BA, Mains RE. Brain Region and Isoform-Specific Phosphorylation Alters Kalirin SH2 Domain Interaction Sites and Calpain Sensitivity. ACS Chemical Neuroscience 2017, 8: 1554-1569. PMID: 28418645, PMCID: PMC5517348, DOI: 10.1021/acschemneuro.7b00076.Peer-Reviewed Original ResearchConceptsLong-term potentiationCalpain sensitivityEffects of cocaineRat nucleus accumbensAdult rat nucleus accumbensRho GDP/GTP exchange factorRegion-specific effectsChronic cocaineNucleus accumbensSynaptic functionBrain regionsKALRN geneSpine morphologyPrefrontal cortexKal7CocainePotentiationFunctional significanceCalpainPhosphorylation
2012
Interaction of the Histone mRNA Hairpin with Stem–Loop Binding Protein (SLBP) and Regulation of the SLBP–RNA Complex by Phosphorylation and Proline Isomerization
Zhang M, Lam TT, Tonelli M, Marzluff WF, Thapar R. Interaction of the Histone mRNA Hairpin with Stem–Loop Binding Protein (SLBP) and Regulation of the SLBP–RNA Complex by Phosphorylation and Proline Isomerization. Biochemistry 2012, 51: 3215-3231. PMID: 22439849, PMCID: PMC3328597, DOI: 10.1021/bi2018255.Peer-Reviewed Original ResearchConceptsStem-loop binding proteinStem-loop structureHistone mRNAProline isomerizationThreonine phosphorylationEnd formationC base pairsReplication-dependent histone mRNAsBase pairsBinding proteinPossible structural roleAdjacent prolineHistone proteinsRibonucleoprotein complexesHelix motifMRNA hairpinsMRNA complexesUntranslated regionStructural roleFirst binding sitePhosphorylationProteinComplex dissociationCritical hingeMRNA
2009
Palmitoylation of Nicotinic Acetylcholine Receptors
Alexander JK, Govind AP, Drisdel RC, Blanton MP, Vallejo Y, Lam TT, Green WN. Palmitoylation of Nicotinic Acetylcholine Receptors. Journal Of Molecular Neuroscience 2009, 40: 12-20. PMID: 19693711, PMCID: PMC3523180, DOI: 10.1007/s12031-009-9246-z.Peer-Reviewed Original ResearchMeSH KeywordsAcetylcholineAcylationAlpha7 Nicotinic Acetylcholine ReceptorAnimalsBinding SitesBiological AssayBrainCell LineElectric OrganHumansLigandsLipoylationMass SpectrometryNeuromuscular JunctionProtein Processing, Post-TranslationalProtein SubunitsProtein TransportReceptors, NicotinicSynaptic TransmissionTorpedoConceptsNicotinic acetylcholine receptorsSites of palmitoylationLigand-gated ion channelsDifferent posttranslational modificationsDisulfide bond formationMass spectrometry strategyLigand binding siteLow abundant proteinsAcetylcholine receptorsProtein palmitoylationPosttranslational modificationsSubunit assemblyPalmitoylationAbundant proteinsMuscle-type nAChRsIon channelsLoss of ligandBinding sitesSubunitsSitesReceptorsPhosphorylationTraffickingGlycosylationSensitive assay
2005
Functional visualization of viral molecular motor by hydrogen-deuterium exchange reveals transient states
Lísal J, Lam TT, Kainov DE, Emmett MR, Marshall AG, Tuma R. Functional visualization of viral molecular motor by hydrogen-deuterium exchange reveals transient states. Nature Structural & Molecular Biology 2005, 12: 460-466. PMID: 15834422, DOI: 10.1038/nsmb927.Peer-Reviewed Original Research