Inward rectification of the AKT2 channel abolished by voltage-dependent phosphorylation.
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Potassium channels in plant cellsIon channels in plantsOutward Rectification of Voltage-Gated K+ Channels Evolved at Least Twice in Life HistoryProteome-wide survey of phosphorylation patterns affected by nuclear DNA polymorphisms in Arabidopsis thalianaPotassium (K+) gradients serve as a mobile energy source in plant vascular tissues.Heteromerization of Arabidopsis Kv channel alpha-subunits: Data and prospects.Preferential KAT1-KAT2 heteromerization determines inward K+ current properties in Arabidopsis guard cells.Post-transcriptional regulation of GORK channels by superoxide anion contributes to increases in outward-rectifying K⁺ currents.The K (+) battery-regulating Arabidopsis K (+) channel AKT2 is under the control of multiple post-translational stepsCross-family translational genomics of abiotic stress-responsive genes between Arabidopsis and Medicago truncatula.Study of the affinity between the protein kinase PKA and peptide substrates derived from kemptide using molecular dynamics simulations and MM/GBSA.Involvement of the S4-S5 linker and the C-linker domain regions to voltage-gating in plant Shaker channels: comparison with animal HCN and Kv channels.Distinct populations of HCN pacemaker channels produce voltage-dependent and voltage-independent currents.K+ channel activity in plants: genes, regulations and functions.Osmoregulation of leaf motor cells.The role of the C-terminus for functional heteromerization of the plant channel KDC1.The receptor-like pseudokinase MRH1 interacts with the voltage-gated potassium channel AKT2.The role of K(+) channels in uptake and redistribution of potassium in the model plant Arabidopsis thaliana.Constant change: dynamic regulation of membrane transport by calcium signalling networks keeps plants in tune with their environment.Calcium-dependent modulation and plasma membrane targeting of the AKT2 potassium channel by the CBL4/CIPK6 calcium sensor/protein kinase complex.The potassium battery: a mobile energy source for transport processes in plant vascular tissues.The Arabidopsis AtPP2CA Protein Phosphatase Inhibits the GORK K+ Efflux Channel and Exerts a Dominant Suppressive Effect on Phosphomimetic-activating Mutations.Overexpression of GmAKT2 potassium channel enhances resistance to soybean mosaic virus.A unique voltage sensor sensitizes the potassium channel AKT2 to phosphoregulationModulation of the Arabidopsis KAT1 channel by an activator of protein kinase C in Xenopus laevis oocytes.Threonine at position 306 of the KAT1 potassium channel is essential for channel activity and is a target site for ABA-activated SnRK2/OST1/SnRK2.6 protein kinase.Polyamines improve K+/Na+ homeostasis in barley seedlings by regulating root ion channel activities.Identification of regions responsible for the function of the plant K+ channels KAT1 and AKT2 in Saccharomyces cerevisiae and Xenopus laevis oocytes.Distinct roles of the last transmembrane domain in controlling Arabidopsis K+ channel activity.Phosphorylation dynamics of membrane proteins from Arabidopsis roots submitted to salt stress.Increased functional diversity of plant K+ channels by preferential heteromerization of the shaker-like subunits AKT2 and KAT2.The Role of Potassium Channels in Arabidopsis thaliana Long Distance Electrical Signalling: AKT2 Modulates Tissue Excitability While GORK Shapes Action Potentials.
P2860
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P2860
Inward rectification of the AKT2 channel abolished by voltage-dependent phosphorylation.
description
2005 nî lūn-bûn
@nan
2005年の論文
@ja
2005年学术文章
@wuu
2005年学术文章
@zh-cn
2005年学术文章
@zh-hans
2005年学术文章
@zh-my
2005年学术文章
@zh-sg
2005年學術文章
@yue
2005年學術文章
@zh
2005年學術文章
@zh-hant
name
Inward rectification of the AKT2 channel abolished by voltage-dependent phosphorylation.
@en
Inward rectification of the AKT2 channel abolished by voltage-dependent phosphorylation.
@nl
type
label
Inward rectification of the AKT2 channel abolished by voltage-dependent phosphorylation.
@en
Inward rectification of the AKT2 channel abolished by voltage-dependent phosphorylation.
@nl
prefLabel
Inward rectification of the AKT2 channel abolished by voltage-dependent phosphorylation.
@en
Inward rectification of the AKT2 channel abolished by voltage-dependent phosphorylation.
@nl
P2860
P50
P1433
P1476
Inward rectification of the AKT2 channel abolished by voltage-dependent phosphorylation
@en
P2093
Jean-Baptiste Thibaud
P2860
P304
P356
10.1111/J.1365-313X.2005.02566.X
P577
2005-12-01T00:00:00Z