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the single KCNQ channel in Drosophila (dKCNQ) has similar electrophysiological properties to neuronal KCNQ2 (show KCNQ2 ELISA Kits)/3
Data show that Drosophila KCNQ (dKCNQ) is a slowly activating and slowly-deactivating K(+) current open at sub-threshold potentials that has similar properties to neuronal KCNQ2 (show KCNQ2 ELISA Kits)/3 with some features of the cardiac KCNQ1/KCNE1 (show KCNE1 ELISA Kits).
A maternal contribution of KCNQ protein and/or mRNA is essential for early embryonic development
The enhanced sensitivity of KCNQ1 gain-of-function mutations for HMR (show NR4A1 ELISA Kits)-1556 suggests the possibility of selective therapeutic targeting, and a potential proof of principle for genotype-specific treatment of this heritable arrhythmia.
There were substantial transmural gradients in Cav1.2 (show CACNA1C ELISA Kits), KChIP2 (show KCNIP2 ELISA Kits), ERG (show KCNH2 ELISA Kits), KvLQT1, Kir2.1 (show KCNJ2 ELISA Kits), NCX1 (show SLC8A1 ELISA Kits), SERCA2a (show ATP2A2 ELISA Kits) and RyR2 (show RYR2 ELISA Kits) at the mRNA and, in some cases, protein level-in every case the mRNA or protein was more abundant in the epicardium than the endocardium.
3' Untranslated region SNPs are not acting as genetic modifiers in a large group of LQT1 patients.
This study presents biallelic gene mutations in KCNQ1 in Asian Indian patients with AR JLNS (show KCNE1 ELISA Kits) and RWS. It adds to the scant worldwide literature of mutation studies in AR RWS.
Western blotting analysis combined with these pharmacological data suggest that long-term insulin (show INS ELISA Kits) treatment augments KCNQ1/KCNE1 (show KCNE1 ELISA Kits) currents by increasing KCNE1 (show KCNE1 ELISA Kits) protein expression.
The KCNQ1 gene has been also associated with Dilated cardiomyopathy in patients carrying a genetic variant that provokes a loss of function of potassium cannel or auto-immune deficiency.
KCNQ1/KCNE1 channel does not require phosphatidylinositol-4,5-bisphosphate (PIP2) or phosphatidylinositol-4-phosphate for anterograde trafficking, but is heavily reliant on PIP2 for channel function once at the plasma membrane.
rs8234, in the KCNQ1 3' untranslated region was associated with joint processing speed and white matter impairments in schizophrenia.
DNA methylation (show HELLS ELISA Kits) of KCNQ1 is likely to be on the causal pathway for type 2 diabetes in later life.
GWAS identified two known loci (TCF7L2 (show TCF7L2 ELISA Kits) and KCNQ1) reaching genome-wide significance levels in Hispanic type 2 diabetes patients. Conditional analysis on known index single nucleotide polymorphisms (SNPs) indicated an additional independent signal at KCNQ1, represented by an African ancestry-specific variant, rs1049549.
Kv7.1 and its isoforms are regulated by both PIP2 and polyunsaturated fatty acids and play a variety of important roles in human health and in heart, neural and other diseases. (Review)
Compound mutations of KCNQ1 were found to be the etiology of Jervell and Lange-Nielsen Syndromeof in four patients from three Chinese families.
This study describes one physiological form of KCNQ1, depolarized voltage sensors with a closed pore in the absence of PIP2, and reveals a regulatory interaction between CaM and KCNQ1 that may explain CaM-mediated Long QT Syndrome.
KCNE1 (show KCNE1 ELISA Kits)/KCNQ1 was expressed in Xenopus oocytes with and without beta-catenin (show CTNNB1 ELISA Kits). Confocal microscopy revealed that beta-catenin (show CTNNB1 ELISA Kits) enhanced the KCNE1 (show KCNE1 ELISA Kits)/KCNQ1 protein abundance in the cell membrane.
results indicate that AMPK inhibits KCNQ1 activity by promoting Nedd4-2-dependent channel ubiquitination and retrieval from the plasma membrane.
S1 constrains S4 in the voltage sensor domain of Kv7.1 K+ channels
characterize a new component of the early bioelectrical circuit: the potassium channel (show KCNAB2 ELISA Kits) KCNQ1 and its accessory subunit KCNE1 (show KCNE1 ELISA Kits)
Slow delayed rectifier potassium currents mediated by mutant KCNQ1(Y111C) or KCNQ1(L114P) are paradoxically reduced by serum- and glucocorticoid-inducible kinase 1.
phenylboronic acid (PBA) activates KCNQ1/KCNE1 (show KCNE1 ELISA Kits) complexes
Collectively, the authors propose that Prmt1 (show PRMT1 ELISA Kits)-dependent facilitation of KCNQ-phosphatidylinositol-4,5-bisphosphate interaction underlies the positive regulation of KCNQ activity by arginine methylation, which may serve as a key target for prevention of neuronal hyperexcitability and seizures.
we investigated the effects of KCNQ1 A340E, a loss-of-function mutant. J343 mice bearing KCNQ1 A340E demonstrated a much higher 24-h intake of electrolytes (potassium, sodium, and chloride). KCNQ1, therefore, is suggested to play a central role in electrolyte metabolism. KCNQ1 A340E, with the loss-of-function phenotype, may dysregulate electrolyte homeostasis
The electrophysiological effects of BACE1 (show BACE ELISA Kits) on KCNQ1 reported here were independent of its enzymatic activity.
Loss of methylation at the Kcnq1 imprinted gDMD was strongly associated with trophoblast giant cell (TGC (show TGM2 ELISA Kits)) expansion.
Data show that disruption of potassium voltage-gated channel, KQT-like subfamily Q, member1 (KCNQ1) results in increased expression of cyclin-dependent kinase inhibitor 1C (Cdkn1c (show CDKN1C ELISA Kits)) only when the mutation is on the paternal allele.
S3 mutations in KCNQ1 cause diverse kinetic defects in I(Ks), affecting opening and closing properties, and can account for LQT1 (show ARFGAP1 ELISA Kits) phenotypes.
Characterization of the imprinted Kcnq1 domain which contains a differentially methylated region in intron 11 of Kcnq1.
KCNQ1, KCNE2 (show KCNE2 ELISA Kits), and SMIT1 (show SLC5A3 ELISA Kits) form reciprocally regulating complexes that affect neuronal excitability.
low expression of KCNQ1 expression was significantly associated with poor overall survival.
Which participates in the allelic repression of Kcnq1.
This gene encodes a voltage-gated potassium channel required for repolarization phase of the cardiac action potential. This protein can form heteromultimers with two other potassium channel proteins, KCNE1 and KCNE3. Mutations in this gene are associated with hereditary long QT syndrome 1 (also known as Romano-Ward syndrome), Jervell and Lange-Nielsen syndrome, and familial atrial fibrillation. This gene exhibits tissue-specific imprinting, with preferential expression from the maternal allele in some tissues, and biallelic expression in others. This gene is located in a region of chromosome 11 amongst other imprinted genes that are associated with Beckwith-Wiedemann syndrome (BWS), and itself has been shown to be disrupted by chromosomal rearrangements in patients with BWS. Alternatively spliced transcript variants have been found for this gene.
, KCNQ-type K[+] channel
, potassium voltage-gated channel, KQT-like subfamily, member 1
, potassium channel protein KCNQ1
, potassium voltage-gated channel, subfamily Q, member 1
, voltage gated potassium channel subunit
, potassium voltage-gated channel subfamily KQT member 1
, KvLQT1 voltage-gated delayed rectifier potassium channel
, Potassium voltage-gated channel subfamily KQT member 1
, IKs producing slow voltage-gated potassium channel subunit alpha KvLQT1
, kidney and cardiac voltage dependend K+ channel
, slow delayed rectifier channel subunit
, voltage-gated potassium channel subunit Kv7.1
, potassium channel protein (KvLQT1)
, ventricular voltage-gated K+ channel pore-forming subunit KCNQ1
, KQT-like 1
, Voltage-gated potassium channel subunit Kv7.1
, potassium channel protein
, IKs producing slow voltage-gated potassium channel subunit alpha xKvLQT1