Is the glutamate residue Glu-373 the proton acceptor of the excitatory amino acid carrier 1?
about
Mechanisms of glutamate transportExcitatory amino acid transporters: roles in glutamatergic neurotransmissionMolecular dynamics simulations of the mammalian glutamate transporter EAAT3Characterization of the transport mechanism and permeant binding profile of the uridine permease Fui1p of Saccharomyces cerevisiae.Individual subunits of the glutamate transporter EAAC1 homotrimer function independently of each otherThe position of an arginine residue influences substrate affinity and K+ coupling in the human glutamate transporter, EAAT1.Neutralization of the aspartic acid residue Asp-367, but not Asp-454, inhibits binding of Na+ to the glutamate-free form and cycling of the glutamate transporter EAAC1.Molecular dynamics simulations elucidate the mechanism of proton transport in the glutamate transporter EAAT3Mechanism of cation binding to the glutamate transporter EAAC1 probed with mutation of the conserved amino acid residue Thr101.New views of glutamate transporter structure and function: advances and challenges.A conserved aspartate residue located at the extracellular end of the binding pocket controls cation interactions in brain glutamate transportersElectrogenic glutamate transporters in the CNS: molecular mechanism, pre-steady-state kinetics, and their impact on synaptic signaling.Charge compensation mechanism of a Na+-coupled, secondary active glutamate transporter.Cooperation of the conserved aspartate 439 and bound amino acid substrate is important for high-affinity Na+ binding to the glutamate transporter EAAC1Computational Studies of Glutamate TransportersProtonation state of a conserved acidic amino acid involved in Na(+) binding to the glutamate transporter EAAC1The conserved histidine 295 does not contribute to proton cotransport by the glutamate transporter EAAC1.Dynamics of the extracellular gate and ion-substrate coupling in the glutamate transporter.Voltage-dependent processes in the electroneutral amino acid exchanger ASCT2Role of the glutamate 185 residue in proton translocation mediated by the proton-coupled folate transporter SLC46A1.Conserved glutamate residues Glu-343 and Glu-519 provide mechanistic insights into cation/nucleoside cotransport by human concentrative nucleoside transporter hCNT3Functional characterization of a Na+-dependent aspartate transporter from Pyrococcus horikoshii.The equivalent of a thallium binding residue from an archeal homolog controls cation interactions in brain glutamate transporters.SLC1 glutamate transportersRegulation of glial glutamate transporters by C-terminal domains.Capturing Functional Motions of Membrane Channels and Transporters with Molecular Dynamics Simulation.Coupling between neurotransmitter translocation and protonation state of a titratable residue during Na ⁺-coupled transport.Yeast nutrient transceptors provide novel insight in the functionality of membrane transporters.Molecular determinants for functional differences between alanine-serine-cysteine transporter 1 and other glutamate transporter family members.Conserved glutamate residues are critically involved in Na+/nucleoside cotransport by human concentrative nucleoside transporter 1 (hCNT1).
P2860
Q26830761-ECC4DDEB-8758-4B59-8568-2FEE73E968FDQ27011208-9FBA4101-B541-44B1-9A18-42E7BBB3DB1FQ27314841-B6BB233B-A180-4C65-A0AC-3EA669B747BDQ27937092-6884CDE3-92D8-4BDB-966F-9729124EA50BQ28569538-F304E81F-AFF5-42CB-A984-2296A0B39B52Q30090226-C76FE49C-1EDF-420A-9BBA-5AC7F6E88695Q33233908-B4BD0611-D3AC-4FA7-82D5-AFA87C9B5801Q33803304-7E7861B9-C630-403C-9255-5A7533D4E324Q33885249-DF29C79F-43BC-47C4-8A75-87D256513E6DQ34865910-2F74CC6E-0323-4280-A868-59EC09353110Q35842139-DBC9B19D-1EAE-48F0-8E37-5380B0BEAB1DQ36100152-0B7E10D1-319E-47D1-BDF9-01B79F68FDC0Q36137442-5D4CCDA5-F179-449E-930A-1200E4D865CBQ36295999-EE0E7F50-6BE9-4773-88C7-4AD85B595B4EQ36409591-B2C8C857-59F3-4055-9B88-49C22790B23BQ36479703-7E40390C-7051-439B-B27F-CA216CC681EFQ36724927-A61F2E1D-7CC6-4200-B017-431485422E49Q36838857-7748A926-6EE8-4121-9FF5-3813A1A3F38CQ36877990-4B1E6BF5-2FAB-49A3-A66A-4FDF6563E460Q37264121-04829868-2FE6-43E1-B72A-6AF206DFE9EAQ37285168-D4561302-7732-4166-8373-DC86D6179BDEQ37285230-DC331694-B656-4A57-BF80-442ED2485066Q37321027-A24E824C-AE68-489D-A155-52B9309B8726Q37495425-00CE276B-C02A-4C68-BD14-CE1C05E680CAQ39628906-E5C092CB-05E0-4209-AD91-3DF372E18EE7Q40937985-AE1625A1-134E-4EA0-BF53-0D74C796AC9AQ41151104-02D658FD-07FC-4A34-B24D-00E8509E8961Q42911386-D661771E-8941-4D4E-AFDE-9B190B4145B7Q43219312-4E0E42EA-4E58-4487-A383-A97763023A60Q48785548-33587AC0-A0D9-40C6-8033-35BA3D8306EA
P2860
Is the glutamate residue Glu-373 the proton acceptor of the excitatory amino acid carrier 1?
description
2002 nî lūn-bûn
@nan
2002年の論文
@ja
2002年学术文章
@wuu
2002年学术文章
@zh
2002年学术文章
@zh-cn
2002年学术文章
@zh-hans
2002年学术文章
@zh-my
2002年学术文章
@zh-sg
2002年學術文章
@yue
2002年學術文章
@zh-hant
name
Is the glutamate residue Glu-3 ...... citatory amino acid carrier 1?
@en
Is the glutamate residue Glu-3 ...... citatory amino acid carrier 1?
@nl
type
label
Is the glutamate residue Glu-3 ...... citatory amino acid carrier 1?
@en
Is the glutamate residue Glu-3 ...... citatory amino acid carrier 1?
@nl
prefLabel
Is the glutamate residue Glu-3 ...... citatory amino acid carrier 1?
@en
Is the glutamate residue Glu-3 ...... citatory amino acid carrier 1?
@nl
P2093
P2860
P356
P1476
Is the glutamate residue Glu-3 ...... citatory amino acid carrier 1?
@en
P2093
Christof Grewer
Natalie Watzke
Thomas Rauen
P2860
P304
P356
10.1074/JBC.M207956200
P407
P577
2002-11-04T00:00:00Z