2011
Cytoplasmic Permeation Pathway of Neurotransmitter Transporters
Rudnick G. Cytoplasmic Permeation Pathway of Neurotransmitter Transporters. Biochemistry 2011, 50: 7462-7475. PMID: 21774491, PMCID: PMC3164596, DOI: 10.1021/bi200926b.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCell Membrane PermeabilityCytoplasmHumansLeucineMolecular Sequence DataNeurotransmitter Transport ProteinsProtein ConformationSignal TransductionConceptsCytoplasmic permeation pathwaysBacterial amino acid transporter LeuTNeurotransmitter transportersPermeation pathwayKingdoms of lifeMammalian serotonin transporterHigh-resolution crystal structuresFour-helix bundleRecent high-resolution crystal structureSubsequent crystal structureStructural repeatsLeuT structureProtein familyCommon structural featuresSolute transportersRelated proteinsLarge structural familyCytoplasmic oneConformational changesSubstrate siteFirst structureBiological membranesTransportersLeuTExtracellular pathways
1985
Relative lack of ATP-driven H+ translocase activity in isolated parotid secretory granules.
Arvan P, Rudnick G, Castle J. Relative lack of ATP-driven H+ translocase activity in isolated parotid secretory granules. Journal Of Biological Chemistry 1985, 260: 14945-14952. PMID: 2866180, DOI: 10.1016/s0021-9258(18)95684-x.Peer-Reviewed Original ResearchAcetatesAcetic AcidAdenosine TriphosphateAnimalsCarbonyl Cyanide m-Chlorophenyl HydrazoneCarbonyl Cyanide p-TrifluoromethoxyphenylhydrazoneCell Membrane PermeabilityCytoplasmic GranulesEthylmaleimideHydrogen-Ion ConcentrationHydrolysisMembrane PotentialsMethylaminesParotid GlandProton-Translocating ATPasesRatsSodium Cyanide