Binding order of substrates to the sodium and potassium ion coupled L-glutamic acid transporter from rat brain.
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ASCT-1 is a neutral amino acid exchanger with chloride channel activityExcitatory amino acid transporters: roles in glutamatergic neurotransmissionMolecular dynamics simulations of the mammalian glutamate transporter EAAT3Coupling substrate and ion binding to extracellular gate of a sodium-dependent aspartate transporterDynamic equilibrium between coupled and uncoupled modes of a neuronal glutamate transporterWater transport by the human Na+-coupled glutamate cotransporter expressed in Xenopus oocytesIndividual subunits of the glutamate transporter EAAC1 homotrimer function independently of each otherFunctional roles of high-affinity glutamate transporters in cochlear afferent synaptic transmission in the mouse.Molecular simulations elucidate the substrate translocation pathway in a glutamate transporter.Glutamate translocation of the neuronal glutamate transporter EAAC1 occurs within milliseconds.Early intermediates in the transport cycle of the neuronal excitatory amino acid carrier EAAC1Neutralization 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.Structural features of the glutamate transporter familyDisulfide cross-linking of transport and trimerization domains of a neuronal glutamate transporter restricts the role of the substrate to the gating of the anion conductanceGlutamate transporters in kidney and brain.Mechanism of cation binding to the glutamate transporter EAAC1 probed with mutation of the conserved amino acid residue Thr101.Proximity of transmembrane segments 5 and 8 of the glutamate transporter GLT-1 inferred from paired cysteine mutagenesis.A conserved methionine residue controls the substrate selectivity of a neuronal glutamate transporter.Evidence for a third sodium-binding site in glutamate transporters suggests an ion/substrate coupling model.Opposite movement of the external gate of a glutamate transporter homolog upon binding cotransported sodium compared with substrateTwo serine residues of the glutamate transporter GLT-1 are crucial for coupling the fluxes of sodium and the neurotransmitterConditional deletion of the glutamate transporter GLT-1 reveals that astrocytic GLT-1 protects against fatal epilepsy while neuronal GLT-1 contributes significantly to glutamate uptake into synaptosomesFree energy simulations of ligand binding to the aspartate transporter Glt(Ph).Molecular determinant of ion selectivity of a (Na+ + K+)-coupled rat brain glutamate transporterA conserved aspartate residue located at the extracellular end of the binding pocket controls cation interactions in brain glutamate transportersStructural intermediates in a model of the substrate translocation path of the bacterial glutamate transporter homologue GltPh.Conserved asparagine residue located in binding pocket controls cation selectivity and substrate interactions in neuronal glutamate transporter.Electrogenic 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.Spatial separation of two different pathways accounting for the generation of calcium signals in astrocytes.Cooperation of the conserved aspartate 439 and bound amino acid substrate is important for high-affinity Na+ binding to the glutamate transporter EAAC1Aspartate-444 is essential for productive substrate interactions in a neuronal glutamate transporter.Molecular Determinants of Substrate Specificity in Sodium-coupled Glutamate Transporters.An intermediate state of the gamma-aminobutyric acid transporter GAT1 revealed by simultaneous voltage clamp and fluorescence.Protonation state of a conserved acidic amino acid involved in Na(+) binding to the glutamate transporter EAAC1Cysteine scanning mutagenesis of transmembrane helix 3 of a brain glutamate transporter reveals two conformationally sensitive positionsTwo conformational changes are associated with glutamate translocation by the glutamate transporter EAAC1.The conserved histidine 295 does not contribute to proton cotransport by the glutamate transporter EAAC1.Acute decrease in net glutamate uptake during energy deprivation.Glutamate forward and reverse transport: from molecular mechanism to transporter-mediated release after ischemia.
P2860
Q24319141-A66DEC85-87F0-4C47-81C8-671945D85A27Q27011208-3477A598-07C6-496E-B85D-4EB4743C980DQ27314841-C18B6B59-F381-4AC6-8123-17B9D4F0E789Q27643578-B5F3B340-4979-420D-8500-3C0365489878Q28217171-100857E4-D747-40EF-B9A8-99021C385B7AQ28346060-DBA15757-FB09-43F6-BD77-9729780E10D7Q28569538-FFBF1F6E-186C-4D8F-85E2-BEC52919047AQ30475677-87A1E17E-CCA9-453A-8AA0-5B6069A075DDQ30485857-89414534-CC8F-49B4-A631-B51DF7F32870Q30898028-A8E6C6CC-29C6-4EBB-93FB-1F9A1302BE1FQ30990921-E66A2FDE-D2C1-41CD-92C1-02193B66758BQ33233908-C1F99223-4577-4D35-9284-DC00E1623A6AQ33652145-ACCFE5FC-FCED-4A3D-BECC-73BC8D6016D4Q33676261-3F5C0C25-0F42-4532-B698-4384CF1E4160Q33749196-6A3D82BE-829B-419A-AA8C-031885002FBCQ33885249-9477170F-53FA-4561-AF50-BF4700F7F9C2Q33940888-93979F9C-6EBA-44AD-8FAC-FDBB9290B2C4Q33967358-6C044418-EC05-4551-88DA-430F5AEA2E11Q34068453-D4B9B36D-27A2-487D-BCBB-F3C74D775019Q34985714-87471344-961F-4EDC-A18C-417F53B98923Q35010990-B0671387-3075-434A-B626-948FBA8B52F9Q35236862-2761AF95-E47E-4752-A981-4483260F2824Q35556342-6F7BFF07-1F82-40AC-80E3-6A86F34EF175Q35744207-5ED4BB56-E930-4828-9D83-F7785D0EBCCCQ35842139-06AD4D80-27F2-446B-BA6B-CD7C547856D4Q35952945-2A1F026F-A588-4A3D-8108-D2D7877F4969Q36006874-14B20F7B-F025-4D25-A9A0-90233EA50611Q36100152-3B796B77-84B3-4812-AF94-627E0F1D5C0DQ36137442-7F7A84C3-2E18-4C91-A610-AC64109E2088Q36278392-15B941B3-D91C-438B-A7BE-CD21793957AFQ36295999-567E0805-72F2-4AF8-A8DE-E3C8A80647A1Q36296014-5CA80D93-2F2E-4897-90B4-7278E907C20CQ36323509-4DDC9579-E7D7-40B4-ABEA-CD7E0E10E7B5Q36444945-06CD84C7-F708-4AF5-9772-D97B3F0E6130Q36479703-D6F92C7B-B1FB-456C-9634-6970F5B13E74Q36526395-8CDD4C84-9B7E-4DD1-BE76-F03BC2CE1907Q36724882-C599F916-EE3A-4E05-82BE-03B9EBE4ABB1Q36724927-3C50ACE8-5DCA-480A-A012-0A514C0E6231Q36985138-E168AE6B-45D8-4042-9279-5266DF915D12Q37077117-68478E54-F0C7-41A9-916F-142F4E64337A
P2860
Binding order of substrates to the sodium and potassium ion coupled L-glutamic acid transporter from rat brain.
description
1982 nî lūn-bûn
@nan
1982年の論文
@ja
1982年学术文章
@wuu
1982年学术文章
@zh-cn
1982年学术文章
@zh-hans
1982年学术文章
@zh-my
1982年学术文章
@zh-sg
1982年學術文章
@yue
1982年學術文章
@zh
1982年學術文章
@zh-hant
name
Binding order of substrates to ...... id transporter from rat brain.
@en
Binding order of substrates to ...... id transporter from rat brain.
@nl
type
label
Binding order of substrates to ...... id transporter from rat brain.
@en
Binding order of substrates to ...... id transporter from rat brain.
@nl
prefLabel
Binding order of substrates to ...... id transporter from rat brain.
@en
Binding order of substrates to ...... id transporter from rat brain.
@nl
P356
P1433
P1476
Binding order of substrates to ...... id transporter from rat brain.
@en
P2093
P304
P356
10.1021/BI00267A044
P407
P577
1982-11-01T00:00:00Z