2000
Cellular Mechanisms Regulating Protein Phosphatase-1 A KEY FUNCTIONAL INTERACTION BETWEEN INHIBITOR-2 AND THE TYPE 1 PROTEIN PHOSPHATASE CATALYTIC SUBUNIT*
Frederick D, Huang H, Yang J, Helps N, Cohen P, Nairn A, DePaoli-Roach A, Tatchell K, Connor J, Shenolikar S. Cellular Mechanisms Regulating Protein Phosphatase-1 A KEY FUNCTIONAL INTERACTION BETWEEN INHIBITOR-2 AND THE TYPE 1 PROTEIN PHOSPHATASE CATALYTIC SUBUNIT*. Journal Of Biological Chemistry 2000, 275: 18670-18675. PMID: 10748125, DOI: 10.1074/jbc.m909312199.Peer-Reviewed Original ResearchConceptsPP1 catalytic subunitCatalytic subunitType 1 protein phosphatase catalytic subunitAmino acidsProtein phosphatase catalytic subunitN-terminusProtein serine/threonineN-terminal 35 amino acidsInhibitor 2Phosphatase catalytic subunitTwo-hybrid analysisNovel regulatory interactionsProtein phosphatase 1Serine/threoninePull-down assaysSite-directed mutagenesisN-terminal sequencePP1 mutantsKey functional interactionsPP1 inhibitorPP1 enzymesPP1 inhibitionPhosphatase 1Regulatory interactionsSaccharomyces cerevisiae
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