Experimental conditions can obscure the second high-affinity site in LeuT.
about
Insights to ligand binding to the monoamine transporters-from homology modeling to LeuBAT and dDATVisualizing functional motions of membrane transporters with molecular dynamics simulationsBehavioral, biological, and chemical perspectives on atypical agents targeting the dopamine transporterNonclassical pharmacology of the dopamine transporter: atypical inhibitors, allosteric modulators, and partial substratesHow LeuT shapes our understanding of the mechanisms of sodium-coupled neurotransmitter transportersSpontaneous inward opening of the dopamine transporter is triggered by PIP2-regulated dynamics of the N-terminusComplete mapping of substrate translocation highlights the role of LeuT N-terminal segment in regulating transport cycleSubstrate binds in the S1 site of the F253A mutant of LeuT, a neurotransmitter sodium symporter homologueStructural evidence for functional lipid interactions in the betaine transporter BetPRole of Annular Lipids in the Functional Properties of Leucine Transporter LeuT ProteomicellesDirect assessment of substrate binding to the Neurotransmitter:Sodium Symporter LeuT by solid state NMRNavigating Membrane Protein Structure, Dynamics, and Energy Landscapes Using Spin Labeling and EPR Spectroscopy.Evaluation of cell-free protein synthesis for the crystallization of membrane proteins--a case study on a member of the glutamate transporter family from Staphylothermus marinus.Discovery of novel-scaffold monoamine transporter ligands via in silico screening with the S1 pocket of the serotonin transporterStructural dynamics of the monoamine transporter homolog LeuT from accelerated conformational sampling and channel analysisIdentification of a second substrate-binding site in solute-sodium symporters.Microseconds simulations reveal a new sodium-binding site and the mechanism of sodium-coupled substrate uptake by LeuTNbIT--a new information theory-based analysis of allosteric mechanisms reveals residues that underlie function in the leucine transporter LeuT.Antagonist-induced conformational changes in dopamine transporter extracellular loop two involve residues in a potential salt bridgeMechanism of the Association between Na+ Binding and Conformations at the Intracellular Gate in Neurotransmitter:Sodium SymportersFunctional mechanisms of neurotransmitter transporters regulated by lipid-protein interactions of their terminal loops.A conformational switch in a partially unwound helix selectively determines the pathway for substrate release from the carnitine/γ-butyrobetaine antiporter CaiTSubstrate-induced unlocking of the inner gate determines the catalytic efficiency of a neurotransmitter:sodium symporter.Steric hindrance mutagenesis in the conserved extracellular vestibule impedes allosteric binding of antidepressants to the serotonin transporterThe styrene-maleic acid copolymer: a versatile tool in membrane researchTwo Na+ Sites Control Conformational Change in a Neurotransmitter Transporter HomologThe cost of living in the membrane: a case study of hydrophobic mismatch for the multi-segment protein LeuT.Chloride binding site of neurotransmitter sodium symporters.Nanopharmacological Force Sensing to Reveal Allosteric Coupling in Transporter Binding SitesCoupled global and local changes direct substrate translocation by neurotransmitter-sodium symporter ortholog LeuT.The membrane protein LeuT in micellar systems: aggregation dynamics and detergent binding to the S2 site.Design and synthesis of 1-(3-(dimethylamino)propyl)-1-(4-fluorophenyl)-1,3-dihydroisobenzofuran-5-carbonitrile (citalopram) analogues as novel probes for the serotonin transporter S1 and S2 binding sites.A Markov State-based Quantitative Kinetic Model of Sodium Release from the Dopamine Transporter.A KcsA/MloK1 chimeric ion channel has lipid-dependent ligand-binding energetics.Neurotransmitter transporters: structure meets function.New design strategies for antidepressant drugs.HCV E2 core structures and mAbs: something is still missing.Impact of disruption of secondary binding site S2 on dopamine transporter function.Conformational dynamics of a neurotransmitter:sodium symporter in a lipid bilayer.Biophysical Approaches to the Study of LeuT, a Prokaryotic Homolog of Neurotransmitter Sodium Symporters.
P2860
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P2860
Experimental conditions can obscure the second high-affinity site in LeuT.
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
2012年论文
@zh
2012年论文
@zh-cn
name
Experimental conditions can obscure the second high-affinity site in LeuT.
@ast
Experimental conditions can obscure the second high-affinity site in LeuT.
@en
type
label
Experimental conditions can obscure the second high-affinity site in LeuT.
@ast
Experimental conditions can obscure the second high-affinity site in LeuT.
@en
prefLabel
Experimental conditions can obscure the second high-affinity site in LeuT.
@ast
Experimental conditions can obscure the second high-affinity site in LeuT.
@en
P2860
P50
P356
P1476
Experimental conditions can obscure the second high-affinity site in LeuT
@en
P2093
Britta Zehnpfennig
Matthias Quick
P2860
P2888
P304
P356
10.1038/NSMB.2197
P577
2012-01-15T00:00:00Z