Mutation K448E in the external loop 5 of rat GABA transporter rGAT1 induces pH sensitivity and alters substrate interactions
about
A steered molecular dynamics study of binding and translocation processes in the GABA transporterRole of the conserved glutamine 291 in the rat gamma-aminobutyric acid transporter rGAT-1A novel dominant hyperekplexia mutation Y705C alters trafficking and biochemical properties of the presynaptic glycine transporter GlyT2Turnover rate of the gamma-aminobutyric acid transporter GAT1.Electrophysiological insights into the mechanism of ion-coupled cotransporters.Dictyostelium Nramp1, which is structurally and functionally similar to mammalian DMT1 transporter, mediates phagosomal iron efflux.Electrogenic glutamate transporters in the CNS: molecular mechanism, pre-steady-state kinetics, and their impact on synaptic signaling.An inverse relationship links temperature and substrate apparent affinity in the ion-coupled cotransporters rGAT1 and KAAT1.Inhibitors of the gamma-aminobutyric acid transporter 1 (GAT1) do not reveal a channel mode of conductionCationic interactions at the human dopamine transporter reveal binding conformations for dopamine distinguishable from those for the cocaine analog 2 alpha-carbomethoxy-3 alpha-(4-fluorophenyl)tropane.Structural and functional basis of amino acid specificity in the invertebrate cotransporter KAAT1.Conformational basis for the Li(+)-induced leak current in the rat gamma-aminobutyric acid (GABA) transporter-1.Role of anion-cation interactions on the pre-steady-state currents of the rat Na(+)-Cl(-)-dependent GABA cotransporter rGAT1.The relation between charge movement and transport-associated currents in the rat GABA cotransporter rGAT1.Residues in the extracellular loop 4 are critical for maintaining the conformational equilibrium of the gamma-aminobutyric acid transporter-1.Relations between substrate affinities and charge equilibration rates in the rat GABA cotransporter GAT1.Temperature effects on the presteady-state and transport-associated currents of GABA cotransporter rGAT1.Pre-steady-state and reverse transport currents in the GABA transporter GAT1.Differential effect of pH on sodium binding by the various GABA transporters expressed in Xenopus oocytes.
P2860
Q27300859-1DBB593B-DB21-424B-BF60-8E4364448620Q28569505-C37D5309-7DE6-46AA-A1B3-7F1E978DEBFDQ30450700-5B113C81-90EC-48C1-BB08-7DD2EC6F46B2Q34437561-CEBB77B1-4376-4860-899B-42E4D0AA8D5EQ35689276-0E8A67D6-2CAB-480F-AEB7-86E3F1227A7EQ36091121-3EBCD179-D544-4485-8148-9317889497D4Q36100152-43E4176E-D3A6-4628-89EA-0A47C7DD2A98Q36538249-3708FA48-23D6-419C-97BC-CD06701B4B43Q37394134-BDC6F98B-F4DD-47BA-B701-56AF9D24CF7CQ40724489-044C52B7-4C3B-4F56-B3EC-63A883532A80Q42033840-B73B88AD-FDF2-445E-B3E0-BA5A4737CF3CQ42685690-B949AB05-CA0B-4A03-AF82-0040B64CE811Q44013250-5BEE4C1D-BC44-478D-AA3F-F5DE9B57AA73Q44249825-1FB5FA5C-71BB-47AE-8B5A-C960AFFDFFADQ44452044-BB91FA74-E9F2-4050-A317-BB00D6990232Q45129844-B8BD2846-74D6-4203-B9C4-E64205765DAEQ45711501-AA05A098-B42B-4AF6-B524-C04D13CE1050Q48659100-5EA2E51F-5965-405B-86E9-177304B7E31EQ48851629-8367920E-177F-4E71-A3D8-696A3417886D
P2860
Mutation K448E in the external loop 5 of rat GABA transporter rGAT1 induces pH sensitivity and alters substrate interactions
description
2001 nî lūn-bûn
@nan
2001 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Mutation K448E in the external ...... alters substrate interactions
@ast
Mutation K448E in the external ...... alters substrate interactions
@en
Mutation K448E in the external ...... alters substrate interactions
@nl
type
label
Mutation K448E in the external ...... alters substrate interactions
@ast
Mutation K448E in the external ...... alters substrate interactions
@en
Mutation K448E in the external ...... alters substrate interactions
@nl
prefLabel
Mutation K448E in the external ...... alters substrate interactions
@ast
Mutation K448E in the external ...... alters substrate interactions
@en
Mutation K448E in the external ...... alters substrate interactions
@nl
P2093
P2860
P1476
Mutation K448E in the external ...... alters substrate interactions
@en
P2093
L Bonadiman
R Ghirardelli
S Giovannardi
P2860
P304
P356
10.1111/J.1469-7793.2001.0479C.XD
P407
P50
P577
2001-10-15T00:00:00Z