Microseconds simulations reveal a new sodium-binding site and the mechanism of sodium-coupled substrate uptake by LeuT
about
Designing modulators of monoamine transporters using virtual screening techniquesSpontaneous inward opening of the dopamine transporter is triggered by PIP2-regulated dynamics of the N-terminusA conserved leucine occupies the empty substrate site of LeuT in the Na(+)-free return state.Properties of an inward-facing state of LeuT: conformational stability and substrate release.Computational characterization of structural dynamics underlying function in active membrane transporters.Functional mechanisms of neurotransmitter transporters regulated by lipid-protein interactions of their terminal loops.The Environment Shapes the Inner Vestibule of LeuT.Energy landscape of LeuT from molecular simulationsTwo Na+ Sites Control Conformational Change in a Neurotransmitter Transporter HomologNa+ coordination at the Na2 site of the Na+/I- symporter.Molecular Mechanism of Dopamine Transport by Human Dopamine Transporter.Insights into the Modulation of Dopamine Transporter Function by Amphetamine, Orphenadrine, and Cocaine BindingConformational Dynamics on the Extracellular Side of LeuT Controlled by Na+ and K+ Ions and the Protonation State of Glu290Mechanistic studies of the apical sodium-dependent bile acid transporter.Quantitative Assessment of the Energetics of Dopamine Translocation by Human Dopamine Transporter.Allosteric modulation of human dopamine transporter activity under conditions promoting its dimerization.Effect of Dimerization on the Dynamics of Neurotransmitter:Sodium Symporters.Glycine Transporters in Glia Cells: Structural Studies.How structural elements evolving from bacterial to human SLC6 transporters enabled new functional properties.Modification of a Putative Third Sodium Site in the Glycine Transporter GlyT2 Influences the Chloride Dependence of Substrate Transport
P2860
Q26781605-FDAD7BC3-9B99-4DD0-959C-A19EC5C7C051Q27300323-65509F80-DCA6-4252-BC9A-E5442EAB6D09Q27315933-CCF75DCE-1EFD-41EB-BA78-440EB541926EQ35222032-6C8E0D82-523A-48C3-AAB9-7A4B02D78333Q35768037-5DD46F97-C066-4125-BC57-607EB308E296Q35850518-834C7FDE-369B-4DC2-990E-DF9A5D81D6A2Q36189760-9AFF72BA-5C8D-4F82-9400-6AB2ED4C7CE8Q36326990-AE70AA87-DB70-433A-AC52-19BDFD5A2D40Q36466214-32DFAB17-FF00-4185-9AEC-909FA47BE1CDQ37264277-62F66B39-2187-4CC7-9914-0735952C977DQ40415118-BCD5EE2E-FF65-42BF-A994-74AC7CDFD2E1Q40803358-CDA66BDE-4DBA-4DAF-B0B7-2E08FD58B075Q41106799-5ACF9145-3C7B-4D88-A400-8F9B98EEF17EQ41143699-264DC63A-9368-42A5-90F2-AE68EB66C887Q47302876-762D9DF4-5135-40DD-B0C5-F9F6B66D3F83Q47565964-AA7A7F47-0C01-4AF7-8697-CD734580EF53Q47566777-453F218F-93B7-4A61-995E-68084772573AQ47923197-32B4DA28-72E9-471C-A10F-D39B736F603AQ55238977-DAD06082-0BD4-421D-87D4-3492E474360EQ57492430-A9262C08-E84F-4AFF-AFB3-1B613C027E04
P2860
Microseconds simulations reveal a new sodium-binding site and the mechanism of sodium-coupled substrate uptake by LeuT
description
2014 nî lūn-bûn
@nan
2014 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2014 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2014年の論文
@ja
2014年論文
@yue
2014年論文
@zh-hant
2014年論文
@zh-hk
2014年論文
@zh-mo
2014年論文
@zh-tw
2014年论文
@wuu
name
Microseconds simulations revea ...... upled substrate uptake by LeuT
@ast
Microseconds simulations revea ...... upled substrate uptake by LeuT
@en
Microseconds simulations revea ...... upled substrate uptake by LeuT
@nl
type
label
Microseconds simulations revea ...... upled substrate uptake by LeuT
@ast
Microseconds simulations revea ...... upled substrate uptake by LeuT
@en
Microseconds simulations revea ...... upled substrate uptake by LeuT
@nl
prefLabel
Microseconds simulations revea ...... upled substrate uptake by LeuT
@ast
Microseconds simulations revea ...... upled substrate uptake by LeuT
@en
Microseconds simulations revea ...... upled substrate uptake by LeuT
@nl
P2860
P356
P1476
Microseconds simulations revea ...... upled substrate uptake by LeuT
@en
P2093
P2860
P304
P356
10.1074/JBC.M114.617555
P407
P50
P577
2014-11-07T00:00:00Z