2003
Phosphoinositide Recognition Domains
Lemmon MA. Phosphoinositide Recognition Domains. Traffic 2003, 4: 201-213. PMID: 12694559, DOI: 10.1034/j.1600-0854.2004.00071.x.Peer-Reviewed Original ResearchConceptsPleckstrin homology domainPhox homologyHomology domainEpsin ENTH domainENTH domainMembrane recruitmentFYVE domainBind phosphoinositidesTargeting domainsCellular phosphoinositidesCellular signalingCytoskeletal remodelingLipid bindingIntracellular traffickingStructural basisDistinct functionsExquisite specificityRecognition domainPhosphoinositideSpecificity characteristicsBilayer curvatureSignificant insightsHigh affinityDomainHomology
1999
The T0 Domain of Rabbit KV1.3 Regulates Steady State Channel Protein Level
Segal A, Yao X, Desir G. The T0 Domain of Rabbit KV1.3 Regulates Steady State Channel Protein Level. Biochemical And Biophysical Research Communications 1999, 254: 54-64. PMID: 9920732, DOI: 10.1006/bbrc.1998.9801.Peer-Reviewed Original ResearchConceptsN-terminal regulatory regionVoltage-gated potassium channelsWild-type channelsRegulatory regionsPlasma membraneAmino terminusChannel assemblyChannel proteinsRecognition domainSingle-channel conductanceKv channelsChannel protein levelsProtein levelsProtein densityPotassium channelsOpen probabilityType channelsChannel conductanceKv1.3Fast inactivationDomainMembraneTerminusProteinInactivation
1996
Genetic analysis of functional connectivity between substrate recognition domains ofEscherichia coli glutaminyl-tRNA synthetase
Kitabatake M, Inokuchi H, Ibba M, Hong K, Söll D. Genetic analysis of functional connectivity between substrate recognition domains ofEscherichia coli glutaminyl-tRNA synthetase. Molecular Genetics And Genomics 1996, 252: 717-722. PMID: 8917315, DOI: 10.1007/bf02173978.Peer-Reviewed Original ResearchConceptsGlutaminyl-tRNA synthetaseWild-type enzymeSubstrate discriminationDouble mutantSubstrate recognition domainThree-dimensional structureAnticodon recognitionSubstrate specificityTRNA bindingGenetic analysisAcceptor stemRecognition domainC171Ternary complexExtensive interactionsMutantsPotential involvementG mutationEnzymeHigh KmSynthetaseMutationsActive siteE222GlnR
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