2009
Ligand Effects on Cross-linking Support a Conformational Mechanism for Serotonin Transport*
Tao Z, Zhang YW, Agyiri A, Rudnick G. Ligand Effects on Cross-linking Support a Conformational Mechanism for Serotonin Transport*. Journal Of Biological Chemistry 2009, 284: 33807-33814. PMID: 19837674, PMCID: PMC2797150, DOI: 10.1074/jbc.m109.071977.Peer-Reviewed Original ResearchConceptsN-terminal cyanogen bromide fragmentGamma-aminobutyric acid transporterCyanogen bromide fragmentsTransmembrane 1Cysteine residuesMutagenesis strategyAcid transportersConformational mechanismSerotonin transportCysteineCorresponding positionDisulfide CrossTransportersSynaptic cleftResiduesSame molecule
2007
Interaction between lysine 102 and aspartate 338 in the insect amino acid cotransporter KAAT1
Castagna M, Soragna A, Mari S, Santacroce M, Betté S, Mandela P, Rudnick G, Peres A, Sacchi V. Interaction between lysine 102 and aspartate 338 in the insect amino acid cotransporter KAAT1. American Journal Of Physiology - Cell Physiology 2007, 293: c1286-c1295. PMID: 17626242, DOI: 10.1152/ajpcell.00190.2007.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAmino Acid SubstitutionAmino Acid Transport Systems, NeutralAnimalsAspartic AcidBinding SitesBiological TransportCross-Linking ReagentsCysteineDithiothreitolFemaleInsect ProteinsKineticsLepidopteraLysineModels, MolecularMolecular Sequence DataOocytesPhenanthrolinesPotassiumProtein Structure, TertiarySequence Homology, Amino AcidSodiumTryptophanXenopus laevisConceptsSingle cysteine mutantsNeutral amino acid transporterSite-directed mutagenesisAmino acid transportersTransport-associated currentNSS transportersDouble mutantXenopus laevis oocytesCysteine mutantsWild typeDependent transportLysine 102MutantsSuper familyAcid transportersPermeation pathwayAmino acidsDisulfide bondsLaevis oocytesFunctional evidenceAsp338Leucine uptakeKAAT1Spatial organizationResidues