A juxtamembrane mutation in the N terminus of the dopamine transporter induces preference for an inward-facing conformation. - Wikidata - wikimedia - TriplyDB

A juxtamembrane mutation in the N terminus of the dopamine transporter induces preference for an inward-facing conformation.

A juxtamembrane mutation in the N terminus of the dopamine transporter induces preference for an inward-facing conformation.

http://www.wikidata.org/entity/Q39903252

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Mechanisms of dopamine transporter regulation in normal and disease states Monoamine transporters: insights from molecular dynamics simulations Spontaneous inward opening of the dopamine transporter is triggered by PIP2-regulated dynamics of the N-terminus Substrate-dependent proton antiport in neurotransmitter:sodium symporters.Dopamine transporter trafficking: rapid response on demand.De novo mutation in the dopamine transporter gene associates dopamine dysfunction with autism spectrum disorder An N-terminal threonine mutation produces an efflux-favorable, sodium-primed conformation of the human dopamine transporter The N terminus of monoamine transporters is a lever required for the action of amphetamines The substrate-driven transition to an inward-facing conformation in the functional mechanism of the dopamine transporter.Mutation of tyrosine 470 of human dopamine transporter is critical for HIV-1 Tat-induced inhibition of dopamine transport and transporter conformational transitions.Mutations at tyrosine 88, lysine 92 and tyrosine 470 of human dopamine transporter result in an attenuation of HIV-1 Tat-induced inhibition of dopamine transport.Regulation of monoamine transporters: Role of transporter phosphorylation.Palmitoylation controls dopamine transporter kinetics, degradation, and protein kinase C-dependent regulation Mutational analysis of the high-affinity zinc binding site validates a refined human dopamine transporter homology model SLC6 transporters: structure, function, regulation, disease association and therapeutics Computational modeling of the N-terminus of the human dopamine transporter and its interaction with PIP2 -containing membranes.Site-directed mutations near transmembrane domain 1 alter conformation and function of norepinephrine and dopamine transporters Tyrosine phosphorylation of the human serotonin transporter: a role in the transporter stability and function.Molecular basis for the interaction of the mammalian amino acid transporters B0AT1 and B0AT3 with their ancillary protein collectrin Functional mechanisms of neurotransmitter transporters regulated by lipid-protein interactions of their terminal loops.Dopamine transporter phosphorylation site threonine 53 regulates substrate reuptake and amphetamine-stimulated efflux.Monoamine transporter structure, function, dynamics, and drug discovery: a computational perspective.Steric hindrance mutagenesis in the conserved extracellular vestibule impedes allosteric binding of antidepressants to the serotonin transporter Importance of cholesterol in dopamine transporter function.Phosphorylation of dopamine transporter serine 7 modulates cocaine analog binding.The binding sites for benztropines and dopamine in the dopamine transporter overlap.A Markov State-based Quantitative Kinetic Model of Sodium Release from the Dopamine Transporter.Dopamine release mediated by the dopamine transporter, facts and consequences.Tamoxifen and its active metabolites inhibit dopamine transporter function independently of the estrogen receptors.Dopamine Transporter Amino and Carboxyl Termini Synergistically Contribute to Substrate and Inhibitor Affinities.Computational modeling of human dopamine transporter structures, mechanism and its interaction with HIV-1 transactivator of transcription.HIV, Tat and dopamine transmission.An acute, epitope-specific modification in the dopamine transporter associated with methamphetamine-induced neurotoxicity.Molecular Mechanism of Dopamine Transport by Human Dopamine Transporter.Conformational Dynamics on the Extracellular Side of LeuT Controlled by Na+ and K+ Ions and the Protonation State of Glu290 Mutations in the carboxyl-terminal SEC24 binding motif of the serotonin transporter impair folding of the transporter.The role of human dopamine transporter in NeuroAIDS.Structure and Dynamics Study of LeuT Using the Markov State Model and Perturbation Response Scanning Reveals Distinct Ion Induced Conformational States.Quantitative Assessment of the Energetics of Dopamine Translocation by Human Dopamine Transporter.Dopamine transporter phosphorylation site threonine 53 is stimulated by amphetamines and regulates dopamine transport, efflux, and cocaine analog binding.

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P2860

A juxtamembrane mutation in the N terminus of the dopamine transporter induces preference for an inward-facing conformation.

http://www.wikidata.org/entity/Q39903252

description

2008 nî lūn-bûn

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2008年の論文

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2008年学术文章

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name

A juxtamembrane mutation in th ...... an inward-facing conformation.

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A juxtamembrane mutation in th ...... an inward-facing conformation.

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A juxtamembrane mutation in th ...... an inward-facing conformation.

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Molecular Pharmacology

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A juxtamembrane mutation in th ...... an inward-facing conformation

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P2093

Aurelio Galli

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Bipasha Guptaroy

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Erica Bowton

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Francesca Binda

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Margaret E Gnegy

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Minjia Zhang

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P2860

Amphetamine-induced loss of human dopamine transporter activity: an internalization-dependent and cocaine-sensitive mechanism

N-terminal phosphorylation of the dopamine transporter is required for amphetamine-induced efflux

VMD: visual molecular dynamics

Scalable molecular dynamics with NAMD

Comparative protein modelling by satisfaction of spatial restraints

Mechanisms of neurotransmitter release by amphetamines: a review

Regulation of amphetamine-stimulated dopamine efflux by protein kinase C beta

Phosphorylation of threonine residue 276 is required for acute regulation of serotonin transporter by cyclic GMP

Crystal structure of a bacterial homologue of Na+/Cl--dependent neurotransmitter transporters

Molecular dynamics study of gating in the mechanosensitive channel of small conductance MscS

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3

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23679679

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