Three-dimensional structure of an AMPA receptor without associated stargazin/TARP proteins.
about
Glutamate receptor ion channels: structure, regulation, and functionDomain architecture of a calcium-permeable AMPA receptor in a ligand-free conformation.AMPA receptor/TARP stoichiometry visualized by single-molecule subunit countingGlutamate receptor desensitization is mediated by changes in quaternary structure of the ligand binding domain.Contribution of the global subunit structure and stargazin on the maturation of AMPA receptorsDomain organization and function in GluK2 subtype kainate receptors.Molecular dissection of the interaction between the AMPA receptor and cornichon homolog-3.The biochemistry, ultrastructure, and subunit assembly mechanism of AMPA receptors.Different domains of the AMPA receptor direct stargazin-mediated trafficking and stargazin-mediated modulation of kinetics.Stargazin interaction with alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate (AMPA) receptors is critically dependent on the amino acid at the narrow constriction of the ion channel.Two modes of interaction between the membrane-embedded TARP stargazin's C-terminal domain and the bilayer visualized by electron crystallography.The expanding social network of ionotropic glutamate receptors: TARPs and other transmembrane auxiliary subunits.Emerging structural insights into the function of ionotropic glutamate receptors.A steroid modulatory domain in NR2A collaborates with NR1 exon-5 to control NMDAR modulation by pregnenolone sulfate and protonsPhysiological significance of high- and low-affinity agonist binding to neuronal and recombinant AMPA receptorsRegulation of ionotropic glutamate receptors by their auxiliary subunits.Retour aux sources: defining the structural basis of glutamate receptor activation.Mapping the interaction sites between AMPA receptors and TARPs reveals a role for the receptor N-terminal domain in channel gating.The N-terminal domain modulates α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptor desensitization.Increased accuracy of ligand sensing by receptor diffusion on cell surface.Reconstitution of homomeric GluA2(flop) receptors in supported lipid membranes: functional and structural properties.Differentiation and characterization of excitatory and inhibitory synapses by cryo-electron tomography and correlative microscopy.Activation and desensitization of ionotropic glutamate receptors by selectively triggering pre-existing motions.
P2860
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P2860
Three-dimensional structure of an AMPA receptor without associated stargazin/TARP proteins.
description
2006 nî lūn-bûn
@nan
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
2006年论文
@zh
2006年论文
@zh-cn
name
Three-dimensional structure of ...... iated stargazin/TARP proteins.
@en
type
label
Three-dimensional structure of ...... iated stargazin/TARP proteins.
@en
prefLabel
Three-dimensional structure of ...... iated stargazin/TARP proteins.
@en
P2093
P2860
P356
P1433
P1476
Three-dimensional structure of ...... iated stargazin/TARP proteins.
@en
P2093
Morgan Sheng
Terunaga Nakagawa
Thomas Walz
Yifan Cheng
P2860
P304
P356
10.1515/BC.2006.024
P577
2006-02-01T00:00:00Z