Three-dimensional structure of the KChIP1-Kv4.3 T1 complex reveals a cross-shaped octamer
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The stoichiometry and biophysical properties of the Kv4 potassium channel complex with K+ channel-interacting protein (KChIP) subunits are variable, depending on the relative expression levelI SA channel complexes include four subunits each of DPP6 and Kv4.2Mutation of histidine 105 in the T1 domain of the potassium channel Kv2.1 disrupts heteromerization with Kv6.3 and Kv6.4The diversity of calcium sensor proteins in the regulation of neuronal functionA VAMP7/Vti1a SNARE complex distinguishes a non-conventional traffic route to the cell surface used by KChIP1 and Kv4 potassium channelsSpecific effects of KChIP3/calsenilin/DREAM, but not KChIPs 1, 2 and 4, on calcium signalling and regulated secretion in PC12 cellsNeuronal calcium sensor proteins: generating diversity in neuronal Ca2+ signallingQuaternary structures of tumor suppressor p53 and a specific p53 DNA complexCaMKII regulation of cardiac K channelsMolecular structure and target recognition of neuronal calcium sensor proteinsStructural insights into activation of phosphatidylinositol 4-kinase (Pik1) by yeast frequenin (Frq1)X-ray Crystal Structure of a TRPM Assembly Domain Reveals an Antiparallel Four-stranded Coiled-coilStructural Insights into KChIP4a Modulation of Kv4.3 InactivationCharacterisation of the interaction of the C-terminus of the dopamine D2 receptor with neuronal calcium sensor-1S-glutathionylation of an auxiliary subunit confers redox sensitivity to Kv4 channel inactivationX-ray solution scattering (SAXS) combined with crystallography and computation: defining accurate macromolecular structures, conformations and assemblies in solutionThe "Sticky Patch" Model of Crystallization and Modification of Proteins for Enhanced Crystallizability.Characterization of the Photophysical, Thermodynamic, and Structural Properties of the Terbium(III)-DREAM Complex.It's all in the crystals…Mechanism of the modulation of Kv4:KChIP-1 channels by external K+The neurobiologist's guide to structural biology: a primer on why macromolecular structure matters and how to evaluate structural data.Molecular determinants of cardiac transient outward potassium current (I(to)) expression and regulationQuaternary structure of KATP channel SUR2A nucleotide binding domains resolved by synchrotron radiation X-ray scattering.A novel DPP6 isoform (DPP6-E) can account for differences between neuronal and reconstituted A-type K(+) channels.Stapled Voltage-Gated Calcium Channel (CaV) α-Interaction Domain (AID) Peptides Act As Selective Protein-Protein Interaction Inhibitors of CaV FunctionFunctional rescue of Kv4.3 channel tetramerization mutants by KChIP4a.The tetramerization domain potentiates Kv4 channel function by suppressing closed-state inactivation.Molecular structure and target recognition of neuronal calcium sensor proteins.Co-assembly of Kv4 {alpha} subunits with K+ channel-interacting protein 2 stabilizes protein expression and promotes surface retention of channel complexesNeuronal voltage-gated K+ (Kv) channels function in macromolecular complexes.Incorporation of DPP6a and DPP6K variants in ternary Kv4 channel complex reconstitutes properties of A-type K current in rat cerebellar granule cells.Modulation of the voltage-gated potassium channel (Kv4.3) and the auxiliary protein (KChIP3) interactions by the current activator NS5806.K(V)4.3 N-terminal deletion mutant Δ2-39: effects on inactivation and recovery characteristics in both the absence and presence of KChIP2b.Repolarizing cardiac potassium channels: multiple sites and mechanisms for CaMKII-mediated regulation.KChIP-like auxiliary subunits of Kv4 channels regulate excitability of muscle cells and control male turning behavior during mating in Caenorhabditis elegansThe "structurally minimal" isoform KChIP2d modulates recovery of K(v)4.3 N-terminal deletion mutant Δ2-39Different KChIPs compete for heteromultimeric assembly with pore-forming Kv4 subunitsNegative modulation of NMDA receptor channel function by DREAM/calsenilin/KChIP3 provides neuroprotection?Impact of KChIP2 on Cardiac Electrophysiology and the Progression of Heart Failure.Unfolding of a Temperature-Sensitive Domain Controls Voltage-Gated Channel Activation.
P2860
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P2860
Three-dimensional structure of the KChIP1-Kv4.3 T1 complex reveals a cross-shaped octamer
description
2006 nî lūn-bûn
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2006 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի նոյեմբերին 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
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name
Three-dimensional structure of the KChIP1-Kv4.3 T1 complex reveals a cross-shaped octamer
@ast
Three-dimensional structure of the KChIP1-Kv4.3 T1 complex reveals a cross-shaped octamer
@en
Three-dimensional structure of the KChIP1-Kv4.3 T1 complex reveals a cross-shaped octamer
@nl
type
label
Three-dimensional structure of the KChIP1-Kv4.3 T1 complex reveals a cross-shaped octamer
@ast
Three-dimensional structure of the KChIP1-Kv4.3 T1 complex reveals a cross-shaped octamer
@en
Three-dimensional structure of the KChIP1-Kv4.3 T1 complex reveals a cross-shaped octamer
@nl
prefLabel
Three-dimensional structure of the KChIP1-Kv4.3 T1 complex reveals a cross-shaped octamer
@ast
Three-dimensional structure of the KChIP1-Kv4.3 T1 complex reveals a cross-shaped octamer
@en
Three-dimensional structure of the KChIP1-Kv4.3 T1 complex reveals a cross-shaped octamer
@nl
P2093
P2860
P356
P1476
Three-dimensional structure of the KChIP1-Kv4.3 T1 complex reveals a cross-shaped octamer
@en
P2093
Daniel L Minor
Felix Findeisen
Greg L Hura
Marta Pioletti
P2860
P2888
P304
P356
10.1038/NSMB1164
P407
P577
2006-11-01T00:00:00Z
P5875
P6179
1005935925