Antidepressant specificity of serotonin transporter suggested by three LeuT-SSRI structures - Test2 - elhamkhani - TriplyDB

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

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

http://www.wikidata.org/entity/Q24655640

about

X-ray structure of dopamine transporter elucidates antidepressant mechanism Monoamine transporters: insights from molecular dynamics simulations Insights to ligand binding to the monoamine transporters-from homology modeling to LeuBAT and dDAT Designing modulators of monoamine transporters using virtual screening techniques The SLC6 transporters: perspectives on structure, functions, regulation, and models for transporter dysfunction Visualizing functional motions of membrane transporters with molecular dynamics simulations Behavioral, biological, and chemical perspectives on atypical agents targeting the dopamine transporter Nonclassical pharmacology of the dopamine transporter: atypical inhibitors, allosteric modulators, and partial substrates A steered molecular dynamics study of binding and translocation processes in the GABA transporter Modeling and dynamics of the inward-facing state of a Na+/Cl- dependent neurotransmitter transporter homologue Insights into transport mechanism from LeuT engineered to transport tryptophan X-ray structures of LeuT in substrate-free outward-open and apo inward-open states Structural basis for action by diverse antidepressants on biogenic amine transporters The atypical stimulant and nootropic modafinil interacts with the dopamine transporter in a different manner than classical cocaine-like inhibitors Homozygous SLC6A17 mutations cause autosomal-recessive intellectual disability with progressive tremor, speech impairment, and behavioral problems Ligand induced conformational changes of the human serotonin transporter revealed by molecular dynamics simulations Mapping Cholesterol Interaction Sites on Serotonin Transporter through Coarse-Grained Molecular Dynamics From linked open data to molecular interaction: studying selectivity trends for ligands of the human serotonin and dopamine transporter Direct assessment of substrate binding to the Neurotransmitter:Sodium Symporter LeuT by solid state NMR 4-(4-(dimethylamino)phenyl)-1-methylpyridinium (APP+) is a fluorescent substrate for the human serotonin transporter.Insights from molecular dynamics: the binding site of cocaine in the dopamine transporter and permeation pathways of substrates in the leucine and dopamine transporters.Chronic SSRI stimulation of astrocytic 5-HT2B receptors change multiple gene expressions/editings and metabolism of glutamate, glucose and glycogen: a potential paradigm shift.The significance of chirality in drug design and development.High-throughput screening for TLR3-IFN regulatory factor 3 signaling pathway modulators identifies several antipsychotic drugs as TLR inhibitors.Conformational changes in dopamine transporter intracellular regions upon cocaine binding and dopamine translocation The substrate-driven transition to an inward-facing conformation in the functional mechanism of the dopamine transporter.Profiling of a prescription drug library for potential renal drug-drug interactions mediated by the organic cation transporter 2 Discovery of novel selective serotonin reuptake inhibitors through development of a protein-based pharmacophore.In vivo studies of the SERT-selective [18F]FPBM and VMAT2-selective [18F]AV-133 radiotracers in a rat model of Parkinson's disease.Unbiased simulations reveal the inward-facing conformation of the human serotonin transporter and Na(+) ion release.Structure-activity relationships for a novel series of citalopram (1-(3-(dimethylamino)propyl)-1-(4-fluorophenyl)-1,3-dihydroisobenzofuran-5-carbonitrile) analogues at monoamine transporters Ion/substrate-dependent conformational dynamics of a bacterial homolog of neurotransmitter:sodium symporters.Single-molecule dynamics of gating in a neurotransmitter transporter homologue The high-affinity binding site for tricyclic antidepressants resides in the outer vestibule of the serotonin transporter.Pharmaceuticals as neuroendocrine disruptors: lessons learned from fish on Prozac.Discovery of novel-scaffold monoamine transporter ligands via in silico screening with the S1 pocket of the serotonin transporter Structural dynamics of the monoamine transporter homolog LeuT from accelerated conformational sampling and channel analysis Computational and biochemical docking of the irreversible cocaine analog RTI 82 directly demonstrates ligand positioning in the dopamine transporter central substrate-binding site.X-ray structures and mechanism of the human serotonin transporter.SLC6 transporters: structure, function, regulation, disease association and therapeutics

P2860

Q24612997-C6A8C00D-FCD9-46FD-8537-42F820B2ED11 Q26777242-B577180D-4D24-4DCA-90B1-AD5B01C580B6 Q26781554-C7124388-E910-4082-BC64-11913A8C2AC0 Q26781605-A425C4AF-6F69-4BC5-A355-96CA404A0D4C Q26825461-990E04AC-5468-427F-9C01-F841C2BD44DD Q26826746-38208502-95D8-48BA-AEC1-462B511AE48B Q26829749-A32828B8-7977-4290-AD90-B9CD21BA6753 Q26853319-190BE63D-49E5-4774-8D99-E8B8F3F81078 Q27300859-6AF0344E-C0ED-4A94-9AE7-1854762E839A Q27334606-489A7F5C-8C8C-4303-A8B6-8912F1594FCD Q27674534-0269FFE8-DCCE-4DCF-A8EF-D88CBFC5AEE7 Q27676655-D48A9E8D-3A3C-4007-8171-EA82470CDC55 Q27680298-5DF7B8BD-364A-4273-8345-631BCC116B60 Q28477546-7D010FC1-41D5-4E1E-A4CC-4389DFD5FBCD Q28505479-00F413DC-7CEC-4AA2-9F63-EAD02674A75A Q28533835-DBCD2935-B7D3-40CD-8836-3839A1A34543 Q28554731-25A94375-E012-4BAA-902B-68C7A966DDE7 Q28596136-D67C809F-F7D0-4281-8D25-8AFC63C495B9 Q28818343-C63960F9-D597-4195-930A-7657FE52EC4C Q30511824-D1A1BAD6-8550-4CDC-8AC0-7EDE2981B0DE Q30532521-E15B9590-4F23-484D-AA2F-6F7980653BAD Q30906677-878435DB-DF11-46EB-B015-4B0D81DE3398 Q30997748-8B95EB0C-9CCA-4734-9243-AAB9B386CF8F Q33552169-B0D10287-AF5C-4669-8CBF-D134FEEE80C3 Q33758304-4F03E550-22F9-4C5C-A3E0-D22DEE3D9179 Q33813126-D4CEB760-94B3-4B2C-95EA-0E32B809BB31 Q33907033-8730D506-A246-43D9-8C17-2D87485F84BA Q33990707-CF71DC48-4223-4CBB-A60D-2BE79A137C25 Q34018843-03A6E598-89B8-4C99-AAA0-81F51B86E1F4 Q34064167-3BC20FDF-7461-45D8-9449-57F2F9365101 Q34102188-E151EC54-FFD0-44A8-8CC6-6EFB5BCC646C Q34121740-88EC90E0-5C11-4F5A-B0B0-D7922267302B Q34130830-0DB9F254-EBE6-413C-B959-9C555D858A97 Q34137102-77DB358B-16A6-4BE8-A5F3-97F2880A95C5 Q34203601-67D685D6-55DD-4ABF-90B4-14C169539F78 Q34249476-E1B3264A-64AE-432F-9E4B-6D8135D492A2 Q34254774-28603E1E-A2A4-42F9-9FE6-5E3D9BA9BE64 Q34396818-EEDFA011-BC26-4945-9BCA-4B1D51977D55 Q34521033-2865077E-883B-4D4C-AF17-40210083D202 Q34649517-77302CE7-9B09-4201-BF9A-2450A762BBC9

P2860

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

http://www.wikidata.org/entity/Q24655640

description

2009 nî lūn-bûn

@nan

2009 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

2009 թվականի հունիսին հրատարակված գիտական հոդված

@hy

2009年の論文

@ja

2009年論文

@yue

2009年論文

@zh-hant

2009年論文

@zh-hk

2009年論文

@zh-mo

2009年論文

@zh-tw

2009年论文

@wuu

name

Antidepressant specificity of ...... by three LeuT-SSRI structures

@ast

Antidepressant specificity of ...... by three LeuT-SSRI structures

@en

Antidepressant specificity of ...... by three LeuT-SSRI structures

@nl

type

label

Antidepressant specificity of ...... by three LeuT-SSRI structures

@ast

Antidepressant specificity of ...... by three LeuT-SSRI structures

@en

Antidepressant specificity of ...... by three LeuT-SSRI structures

@nl

altLabel

Antidepressant specificity of ...... by three LeuT–SSRI structures

@en

prefLabel

Antidepressant specificity of ...... by three LeuT-SSRI structures

@ast

Antidepressant specificity of ...... by three LeuT-SSRI structures

@en

Antidepressant specificity of ...... by three LeuT-SSRI structures

@nl

P1433

Q24655640-BD5017ED-5E04-4756-8042-DCB49B438B5E

P1476

Q24655640-C60494DF-2833-44E8-B48D-19B2C2B8E4BE

P2093

Q24655640-47BD950C-1961-4B01-946B-B7E1FB038A10

Q24655640-B2F5F46B-2A04-418A-A821-7F5658FA539D

Q24655640-DCA54A56-0B04-4410-91F7-BD6CEA56FABA

Q24655640-E6B6C5CF-DFAB-4663-B163-D383DBACBEDE

P2860

Q24655640-039D529C-4740-463F-B2DD-2938C2FC403E

Q24655640-10FFE9CE-FCC7-46FB-A400-2CA58E62976F

Q24655640-153C7526-1414-42D9-966C-99C813946E07

Q24655640-1AC1D5BA-7E71-4A53-A154-67E1EAE6D0F4

Q24655640-1C56F2BA-C0D9-460C-BD80-96B802BFCC14

Q24655640-1E7EA477-BB9D-4A55-84E2-F7450C435888

Q24655640-2296235E-D04B-4EFB-8369-8083F71380CE

Q24655640-27A8D902-DD24-4AA8-B766-ECD76B39B52F

Q24655640-2A7FE7EA-52E0-4961-A07E-9E148EFDDB09

Q24655640-2FF5A5A9-E92A-4566-B7E2-3B315EA92FD7

P2888

Q24655640-9A72EB68-4C6D-4331-AECF-825D0BCAFA55

P304

Q24655640-24713F05-4E9A-483F-90EE-0245171A241B

P31

Q24655640-A75BE0BD-E2A8-463A-83E8-A1A1F3BBE27A

P3181

Q24655640-F72CDC98-9AD5-475E-AC3C-39480F273B54

P356

Q24655640-4C1C0D63-706C-4050-962C-B62AB92E4F25

P407

Q24655640-F4E3CD7D-3433-461C-9463-A93314E11D4E

P433

Q24655640-890374F7-AB06-4C3C-9BC8-4B6EE9156538

P478

Q24655640-E30027A9-8BF4-4EAD-86A5-F12DED7F8ECC

P50

Q24655640-7FB49F8E-4820-40B5-BB0B-9699FB6781D5

Q24655640-E88339AB-5C55-4058-9156-C1C869E7AB9C

P577

Q24655640-34DB4A5C-BDF5-4000-A809-1B7595DA561B

P5875

Q24655640-C42B21E4-445F-415E-82F7-B50CE759F105

P6179

Q24655640-098203EC-0F3F-415D-ACE5-8D48A4266578

P698

Q24655640-F93559D7-42EF-47E7-A635-AA9682A3FF90

P921

Q24655640-28F606E8-01D3-41D4-A611-5843EDB6B50C

Q24655640-b1c0ce10-b2d5-4b73-a3b8-33d6a8761f09

P932

Q24655640-15F72D5D-D658-4DAA-BD14-BF48EC4B8F39

P3181

P356

P1433

Nature Structural & Molecular Biology

P1476

Antidepressant specificity of ...... by three LeuT-SSRI structures

@en

P2093

Christopher J Law

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

Maarten E A Reith

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

Nathan K Karpowich

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

Zheng Zhou

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

P2860

Plasma membrane monoamine transporters: structure, regulation and function

Population pharmacokinetic modelling of NS2330 (tesofensine) and its major metabolite in patients with Alzheimer's disease

LeuT-desipramine structure reveals how antidepressants block neurotransmitter reuptake

Comparative molecular field analysis using selectivity fields reveals residues in the third transmembrane helix of the serotonin transporter associated with substrate and antagonist recognition

Neurotransmitter transporters and their impact on the development of psychopharmacology

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

Antidepressant binding site in a bacterial homologue of neurotransmitter transporters

Fluorine in pharmaceuticals: looking beyond intuition

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

P2888

P304

652-657

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

P31

scholarly article

P3181

2239179

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

P356

10.1038/NSMB.1602

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

P407

P433

6

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

P478

16

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

P50

P577

2009-05-10T00:00:00Z

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

P5875

24416032

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

P6179

1022615708

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

P698

19430461

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

P921

structural biology

P932

2758934

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