2015
Carboxyl Residues Required for Transport by a Vesicular Monoamine Transporter Homolog from Brevibacillus Brevis (BbMAT)
Vergara-Jaque A, Yaffe D, Shuster Y, Listov D, Meena S, Singh S, Schuldiner S, Forrest L. Carboxyl Residues Required for Transport by a Vesicular Monoamine Transporter Homolog from Brevibacillus Brevis (BbMAT). Biophysical Journal 2015, 108: 462a. DOI: 10.1016/j.bpj.2014.11.2522.Peer-Reviewed Original Research
2014
Functionally Important Carboxyls in a Bacterial Homologue of the Vesicular Monoamine Transporter (VMAT)*
Yaffe D, Vergara-Jaque A, Shuster Y, Listov D, Meena S, Singh SK, Forrest LR, Schuldiner S. Functionally Important Carboxyls in a Bacterial Homologue of the Vesicular Monoamine Transporter (VMAT)*. Journal Of Biological Chemistry 2014, 289: 34229-34240. PMID: 25336661, PMCID: PMC4256354, DOI: 10.1074/jbc.m114.607366.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsArginineBacterial ProteinsBiogenic MonoaminesBrevibacillusCarrier ProteinsDrug Resistance, BacterialEscherichia coliEvolution, MolecularGene ExpressionHistidineModels, MolecularMolecular Sequence DataProtein FoldingRatsRecombinant ProteinsSequence AlignmentStructural Homology, ProteinStructure-Activity RelationshipSubstrate SpecificitySynaptic TransmissionVesicular Monoamine Transport ProteinsConceptsBacterial multidrug transportersMultidrug transporterBacterial homologueVesicular monoamine transporterRat vesicular monoamine transporterMonoamine transportersPreliminary biochemical characterizationMammalian transportersTransmembrane helicesMammalian counterpartsTransmembrane segmentsMammalian organismsEvolutionary aspectsMajor facilitatorBiochemical characterizationImportant carboxylB. brevisHomology modelBiochemical studiesTransportersHomologuesCarboxyl residuesAntibiotic resistanceOrganismsNeurotransporters