P2X5 subunit assembly requires scaffolding by the second transmembrane domain and a conserved aspartate.
about
Molecular and functional properties of P2X receptors--recent progress and persisting challengesTMEM16A(a)/anoctamin-1 shares a homodimeric architecture with CLC chloride channelsPolar residues in the second transmembrane domain of the rat P2X2 receptor that affect spontaneous gating, unitary conductance, and rectificationCrystal structure of the ATP-gated P2X(4) ion channel in the closed stateP2X receptors: dawn of the post-structure era.Gated access to the pore of a P2X receptor: structural implications for closed-open transitions.The second transmembrane domain of P2X7 contributes to dilated pore formationActivation and regulation of purinergic P2X receptor channelsA truncation variant of the cation channel P2RX5 is upregulated during T cell activation.Allosteric modulation of ATP-gated P2X receptor channelsComparative study of the P2X gene family in animals and plants.Voltage- and [ATP]-dependent gating of the P2X(2) ATP receptor channel.Assembly and trafficking of P2X purinergic receptors (Review).Mouse Leydig cells express multiple P2X receptor subunits.Structural and molecular modeling features of P2X receptors.P2 receptors for extracellular nucleotides in the central nervous system: role of P2X7 and P2Y₂ receptor interactions in neuroinflammation.Heteromeric assembly of P2X subunits.Key sites for P2X receptor function and multimerization: overview of mutagenesis studies on a structural basis.Positional editing of transmembrane domains during ion channel assembly.Identification and characterization of a novel variant of the human P2X(7) receptor resulting in gain of function.TRPM7 is a molecular substrate of ATP-evoked P2X7-like currents in tumor cells.Functional relevance of aromatic residues in the first transmembrane domain of P2X receptors.Lack of evidence for direct phosphorylation of recombinantly expressed P2X(2) and P2X (3) receptors by protein kinase C.An intramembrane aromatic network determines pentameric assembly of Cys-loop receptors.Interaction of Purinergic P2X4 and P2X7 Receptor Subunits.
P2860
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P2860
P2X5 subunit assembly requires scaffolding by the second transmembrane domain and a conserved aspartate.
description
2006 nî lūn-bûn
@nan
2006 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
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
name
P2X5 subunit assembly requires ...... ain and a conserved aspartate.
@ast
P2X5 subunit assembly requires ...... ain and a conserved aspartate.
@en
P2X5 subunit assembly requires ...... ain and a conserved aspartate.
@nl
type
label
P2X5 subunit assembly requires ...... ain and a conserved aspartate.
@ast
P2X5 subunit assembly requires ...... ain and a conserved aspartate.
@en
P2X5 subunit assembly requires ...... ain and a conserved aspartate.
@nl
prefLabel
P2X5 subunit assembly requires ...... ain and a conserved aspartate.
@ast
P2X5 subunit assembly requires ...... ain and a conserved aspartate.
@en
P2X5 subunit assembly requires ...... ain and a conserved aspartate.
@nl
P2093
P356
P1476
P2X5 subunit assembly requires ...... ain and a conserved aspartate.
@en
P2093
Günther Schmalzing
Ralf Hausmann
Wiebke Duckwitz
P304
39561-39572
P356
10.1074/JBC.M606113200
P407
P577
2006-09-25T00:00:00Z