Neurotransmitter transporters: structure meets function. - sprookjes - yvandenbroek - TriplyDB

Neurotransmitter transporters: structure meets function.

Neurotransmitter transporters: structure meets function.

http://www.wikidata.org/entity/Q38105743

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Spontaneous inward opening of the dopamine transporter is triggered by PIP2-regulated dynamics of the N-terminus 13C NMR detects conformational change in the 100-kD membrane transporter ClC-ec1.Allosteric regulation of γ-secretase activity by a phenylimidazole-type γ-secretase modulator.Functional mechanisms of neurotransmitter transporters regulated by lipid-protein interactions of their terminal loops.Selective effect of cell membrane on synaptic neurotransmission.Role of N-glycosylation in renal betaine transport.SLC1 glutamate transporters The Hill analysis and co-ion-driven transporter kinetics.Evidence for a Revised Ion/Substrate Coupling Stoichiometry of GABA Transporters.Glial Excitatory Amino Acid Transporters and Glucose Incorporation.Threonine 67 is a key component in the coupling of the NSS amino acid transporter KAAT1.Characterisation of the DAACS Family Escherichia coli Glutamate/Aspartate-Proton Symporter GltP Using Computational, Chemical, Biochemical and Biophysical Methods.Substrate-modulated unwinding of transmembrane helices in the NSS transporter LeuT.

P2860

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P2860

Neurotransmitter transporters: structure meets function.

http://www.wikidata.org/entity/Q38105743

description

article científic

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article scientifique

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articol științific

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articolo scientifico

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artigo científico

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artigo científico

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artigo científico

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artikel ilmiah

@id

artikull shkencor

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artículo científico

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name

Neurotransmitter transporters: structure meets function.

@en

type

label

Neurotransmitter transporters: structure meets function.

@en

prefLabel

Neurotransmitter transporters: structure meets function.

@en

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J.STR.2013.03.002

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P1476

Neurotransmitter transporters: structure meets function.

@en

P2093

H Peter Larsson

http://www.w3.org/2001/XMLSchema#string

Paul J Focke

http://www.w3.org/2001/XMLSchema#string

Xiaoyu Wang

http://www.w3.org/2001/XMLSchema#string

P2860

LeuT-desipramine structure reveals how antidepressants block neurotransmitter reuptake

The glutamate-activated anion conductance in excitatory amino acid transporters is gated independently by the individual subunits

Antidepressant specificity of serotonin transporter suggested by three LeuT-SSRI structures

Modeling and dynamics of the inward-facing state of a Na+/Cl- dependent neurotransmitter transporter homologue

Coupling substrate and ion binding to extracellular gate of a sodium-dependent aspartate transporter

Antidepressant binding site in a bacterial homologue of neurotransmitter transporters

A competitive inhibitor traps LeuT in an open-to-out conformation.

Binding of an octylglucoside detergent molecule in the second substrate (S2) site of LeuT establishes an inhibitor-bound conformation

Transport mechanism of a bacterial homologue of glutamate transporters.

Insights into transport mechanism from LeuT engineered to transport tryptophan

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694-705

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scholarly article

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10.1016/J.STR.2013.03.002

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5

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21

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2013-05-01T00:00:00Z

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236690236

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23664361

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neurotransmitter

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3654398

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