2024
Optimal conditions for carrying out trypsin digestions on complex proteomes: From bulk samples to single cells
Mansuri M, Bathla S, Lam T, Nairn A, Williams K. Optimal conditions for carrying out trypsin digestions on complex proteomes: From bulk samples to single cells. Journal Of Proteomics 2024, 297: 105109. PMID: 38325732, PMCID: PMC10939724, DOI: 10.1016/j.jprot.2024.105109.Peer-Reviewed Original ResearchComplex proteomesProtein cleavage activityOptimal conditionsTrypsin digestion protocolReversed phase HPLC separationMass spectrometry workflowMS-based proteomicsMass spectrometric analysisC-terminal amino acid residuesTrypsin digestionChromatographic separationDigestion protocolAmino acid residuesHPLC separationMS/MS analysisGlobal proteomic analysisSingle cellsSample matrixSpectrometric analysisCleavage specificityGeneration of peptidesAcid residuesDown proteinsProteomic analysisCleavage activity
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