Cysteine scanning of the surroundings of an alkali-ion binding site of the glutamate transporter GLT-1 reveals a conformationally sensitive residue.
about
Transport mechanism of a glutamate transporter homologue GltPhExcitatory amino acid transporters: roles in glutamatergic neurotransmissionCoupling substrate and ion binding to extracellular gate of a sodium-dependent aspartate transporterRole of the dopamine transporter in the action of psychostimulants, nicotine, and other drugs of abuseA pool of Y2 neuropeptide Y receptors activated by modifiers of membrane sulfhydryl or cholesterol balanceCloned neuropeptide Y (NPY) Y1 and pancreatic polypeptide Y4 receptors expressed in Chinese hamster ovary cells show considerable agonist-driven internalization, in contrast to the NPY Y2 receptor.Disruption of Eaat2b, a glutamate transporter, results in abnormal motor behaviors in developing zebrafish.Structural features of the glutamate transporter familySinorhizobium meliloti dctA mutants with partial ability to transport dicarboxylic acids.Na+ interactions with the neutral amino acid transporter ASCT1.Structural analysis of the extracellular entrance to the serotonin transporter permeation pathway.Identification of the third Na+ site and the sequence of extracellular binding events in the glutamate transporter.The accessibility in the external part of the TM5 of the glutamate transporter EAAT1 is conformationally sensitive during the transport cycle.The structure of glutamate transporters shows channel-like features.Position of the third Na+ site in the aspartate transporter GltPh and the human glutamate transporter, EAAT1.Permeation and gating residues in serotonin transporterTwo serine residues of the glutamate transporter GLT-1 are crucial for coupling the fluxes of sodium and the neurotransmitterDicarboxylate transport by rhizobia.A conserved serine-rich stretch in the glutamate transporter family forms a substrate-sensitive reentrant loop.Dynamics of the extracellular gate and ion-substrate coupling in the glutamate transporter.Glutamate forward and reverse transport: from molecular mechanism to transporter-mediated release after ischemia.Fluorometric measurements of conformational changes in glutamate transporters.The equivalent of a thallium binding residue from an archeal homolog controls cation interactions in brain glutamate transporters.Capturing Functional Motions of Membrane Channels and Transporters with Molecular Dynamics Simulation.Identification of residues lining the translocation pore of human AE1, plasma membrane anion exchange protein.Coupled binding mechanism of three sodium ions and aspartate in the glutamate transporter homologue GltTk.Cysteine-scanning mutagenesis reveals a highly amphipathic, pore-lining membrane-spanning helix in the glutamate transporter GltT.Proximity of two oppositely oriented reentrant loops in the glutamate transporter GLT-1 identified by paired cysteine mutagenesis.Distinct conformational states mediate the transport and anion channel properties of the glutamate transporter EAAT-1.Cysteine-scanning mutagenesis reveals a conformationally sensitive reentrant pore-loop in the glutamate transporter GLT-1.A hydrophobic domain in glutamate transporters forms an extracellular helix associated with the permeation pathway for substrates.Passive water and urea permeability of a human Na(+)-glutamate cotransporter expressed in Xenopus oocytes.Is the glutamate residue Glu-373 the proton acceptor of the excitatory amino acid carrier 1?The chloride permeation pathway of a glutamate transporter and its proximity to the glutamate translocation pathway.Analysis of the quality of crystallographic data and the limitations of structural models.
P2860
Q26747176-894CAAD3-77E7-4040-ADCC-AE627975B22AQ27011208-CAADCCC6-AAAA-46D1-88D0-A66F27C371CAQ27643578-CA7A03BE-38B2-41F0-8356-6E85FCE2EA2EQ28306056-0D6B551A-55B9-4739-BF31-92189330D44DQ28580590-9492B4FF-C3DA-41E8-AAC3-1B7371E11EBEQ31944343-987CF4AB-826A-4B2B-9618-85ABECE7EC3DQ33580893-3ACF6E64-E71F-484E-AFA0-4F97FA0DFA3FQ33652145-B7DEAB0E-2856-41F1-8787-0450A3F06313Q33758157-70532D21-60C7-4E4A-BBB8-C260B970F295Q33792891-FA77F696-9F8A-41D1-B1B6-6BDC8FD505AFQ33832622-43580EC0-13A7-4657-AEC7-C9D24D7E21F9Q34099018-6CFD56D6-7957-4C08-AA0E-A8910E5F35CEQ34146588-DBFAFE79-AFE0-4BD7-B2EA-729E2C2592BEQ34189332-88A0CC86-D71D-4E47-A73D-57C421ED4D6DQ34200400-FDFD78F3-2B28-4453-B3FA-15C5077A56ECQ35000759-BE39C90A-3D72-49F7-8B68-7FB98B2DFEC3Q35010990-5D5701F3-0573-4E24-B825-87A0D1ED175CQ35890758-9E7A03F6-5C86-4D21-ACC1-B1883EB8D1FAQ36742579-3E172926-7228-4EA3-9496-082A669CFDB6Q36838857-C50589AB-D320-4989-A269-335B0445DA1BQ37077117-89A2D679-051F-4B53-9937-352432236ACBQ37095437-38A9EE48-FC0E-4143-83E3-3F4FD63280A9Q37321027-2AA38C98-C499-4D9A-96C6-801E11FB1C6CQ40937985-B6162405-3CF0-4D32-B8B8-451FD0B0AFC2Q40977569-E6770F9A-75A2-4539-96A6-572A2866FED5Q42368299-4E171AAC-B9BE-4428-ADEB-E4F7A4610F84Q43517011-73B7A5D9-6E21-4BA5-9B20-A39EEAE35A39Q43810165-EBF9DF73-EAB8-4A63-B032-B87A5B507879Q43869538-00E4CE7D-EAE5-4557-BFA2-E371E34B387AQ43982363-3D2230AB-76C4-4C8B-BF85-D179F7338B81Q43996674-BDD01AFE-ED06-4138-A150-8C23C8D7D7E8Q44087171-F160D1C3-9600-4250-B527-FC641B538CC6Q44207688-B367A683-AD76-4040-9AB9-1BE38B05FBA7Q44776061-F079E7C8-308C-46C2-BB3B-B7A0D102894CQ47680317-B95D8B2E-CDC2-4360-BDCD-EFE1DD993B8C
P2860
Cysteine scanning of the surroundings of an alkali-ion binding site of the glutamate transporter GLT-1 reveals a conformationally sensitive residue.
description
1998 nî lūn-bûn
@nan
1998年の論文
@ja
1998年学术文章
@wuu
1998年学术文章
@zh
1998年学术文章
@zh-cn
1998年学术文章
@zh-hans
1998年学术文章
@zh-my
1998年学术文章
@zh-sg
1998年學術文章
@yue
1998年學術文章
@zh-hant
name
Cysteine scanning of the surro ...... rmationally sensitive residue.
@en
Cysteine scanning of the surro ...... rmationally sensitive residue.
@nl
type
label
Cysteine scanning of the surro ...... rmationally sensitive residue.
@en
Cysteine scanning of the surro ...... rmationally sensitive residue.
@nl
prefLabel
Cysteine scanning of the surro ...... rmationally sensitive residue.
@en
Cysteine scanning of the surro ...... rmationally sensitive residue.
@nl
P2093
P2860
P356
P1476
Cysteine scanning of the surro ...... rmationally sensitive residue.
@en
P2093
B I Kanner
M Grunewald
M P Kavanaugh
P2860
P304
14231-14237
P356
10.1074/JBC.273.23.14231
P407
P577
1998-06-01T00:00:00Z