Proximity of two oppositely oriented reentrant loops in the glutamate transporter GLT-1 identified by paired cysteine mutagenesis.
about
N-linked glycosylation and sequence changes in a critical negative control region of the ASCT1 and ASCT2 neutral amino acid transporters determine their retroviral receptor functionsMembrane topology of human ASBT (SLC10A2) determined by dual label epitope insertion scanning mutagenesis. New evidence for seven transmembrane domainsMechanisms of glutamate transportCoupling substrate and ion binding to extracellular gate of a sodium-dependent aspartate transporterIndividual subunits of the glutamate transporter EAAC1 homotrimer function independently of each otherStructure of a glutamate transporter homologue from Pyrococcus horikoshii.Time-resolved mechanism of extracellular gate opening and substrate binding in a glutamate transporter.Disulfide cross-linking of transport and trimerization domains of a neuronal glutamate transporter restricts the role of the substrate to the gating of the anion conductanceProximity of transmembrane segments 5 and 8 of the glutamate transporter GLT-1 inferred from paired cysteine mutagenesis.The 3-4 loop of an archaeal glutamate transporter homolog experiences ligand-induced structural changes and is essential for transport.The accessibility in the external part of the TM5 of the glutamate transporter EAAT1 is conformationally sensitive during the transport cycle.Minimal structural rearrangement of the cytoplasmic pore during activation of the 5-HT3A receptor.Conformationally sensitive proximity of extracellular loops 2 and 4 of the γ-aminobutyric acid (GABA) transporter GAT-1 inferred from paired cysteine mutagenesisNew views of glutamate transporter structure and function: advances and challenges.Opposite movement of the external gate of a glutamate transporter homolog upon binding cotransported sodium compared with substrateConstraints imposed by the membrane selectively guide the alternating access dynamics of the glutamate transporter GltPh.A Mutation in Transmembrane Domain 7 (TM7) of Excitatory Amino Acid Transporters Disrupts the Substrate-dependent Gating of the Intrinsic Anion Conductance and Drives the Channel into a Constitutively Open State.Transport function of the renal type IIa Na+/P(i) cotransporter is codetermined by residues in two opposing linker regions.Cysteine cross-linking defines the extracellular gate for the Leishmania donovani nucleoside transporter 1.1 (LdNT1.1).The conserved histidine 295 does not contribute to proton cotransport by the glutamate transporter EAAC1.Disulfide Cross-linking of a Multidrug and Toxic Compound Extrusion Transporter Impacts Multidrug Efflux.Glutamate forward and reverse transport: from molecular mechanism to transporter-mediated release after ischemia.TM4 of the glutamate transporter GLT-1 experiences substrate-induced motion during the transport cycleThe equivalent of a thallium binding residue from an archeal homolog controls cation interactions in brain glutamate transporters.Inward-facing conformation of glutamate transporters as revealed by their inverted-topology structural repeats.Identification of the intracellular gate for a member of the equilibrative nucleoside transporter (ENT) family.Toward a new role for plasma membrane sodium-dependent glutamate transporters of astrocytes: maintenance of antioxidant defenses beyond extracellular glutamate clearance.Topological analysis of glucosyltransferase GtrV of Shigella flexneri by a dual reporter system and identification of a unique reentrant loop.Interaction between lysine 102 and aspartate 338 in the insect amino acid cotransporter KAAT1.Structure and allosteric inhibition of excitatory amino acid transporter 1.Substrates and non-transportable analogues induce structural rearrangements at the extracellular entrance of the glial glutamate transporter GLT-1/EAAT2.Substrate-induced rearrangements in glutamate-transporter homologs.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.Arginine 445 controls the coupling between glutamate and cations in the neuronal transporter EAAC-1.The chloride permeation pathway of a glutamate transporter and its proximity to the glutamate translocation pathway.Alternating access and a pore-loop structure in the Na+-citrate transporter CitS of Klebsiella pneumoniae.Cysteine mutagenesis reveals alternate proximity between transmembrane domain 2 and hairpin loop 1 of the glutamate transporter EAAT1.The substrates of the gamma-aminobutyric acid transporter GAT-1 induce structural rearrangements around the interface of transmembrane domains 1 and 6.The substrate specificity of a neuronal glutamate transporter is determined by the nature of the coupling ion.
P2860
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P2860
Proximity of two oppositely oriented reentrant loops in the glutamate transporter GLT-1 identified by paired cysteine mutagenesis.
description
2001 nî lūn-bûn
@nan
2001年の論文
@ja
2001年学术文章
@wuu
2001年学术文章
@zh
2001年学术文章
@zh-cn
2001年学术文章
@zh-hans
2001年学术文章
@zh-my
2001年学术文章
@zh-sg
2001年學術文章
@yue
2001年學術文章
@zh-hant
name
Proximity of two oppositely or ...... y paired cysteine mutagenesis.
@en
Proximity of two oppositely or ...... y paired cysteine mutagenesis.
@nl
type
label
Proximity of two oppositely or ...... y paired cysteine mutagenesis.
@en
Proximity of two oppositely or ...... y paired cysteine mutagenesis.
@nl
prefLabel
Proximity of two oppositely or ...... y paired cysteine mutagenesis.
@en
Proximity of two oppositely or ...... y paired cysteine mutagenesis.
@nl
P2093
P2860
P356
P1476
Proximity of two oppositely or ...... y paired cysteine mutagenesis.
@en
P2093
Annie Bendahan
Baruch I Kanner
Lihi Brocke
Myriam Grunewald
P2860
P304
P356
10.1074/JBC.M107735200
P407
P577
2001-11-27T00:00:00Z