PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
27176799-0	2016	Macrolide antibiotics exert antileukemic effects by modulating the autophagic flux through inhibition of hERG1 potassium channels.	macrolide antibiotics	0-21	potassium voltage-gated channel subfamily H member 2	Homo sapiens	105-110
26548443-2	2016	We describe two cases where a switch to bisoprolol resulted in worsening of arrhythmia control: A man with LQT2, asymptomatic on propranolol, experienced syncope after switching to bisoprolol 5 mg daily.	Bisoprolol	40-50	potassium voltage-gated channel subfamily H member 2	Homo sapiens	107-111
26548443-2	2016	We describe two cases where a switch to bisoprolol resulted in worsening of arrhythmia control: A man with LQT2, asymptomatic on propranolol, experienced syncope after switching to bisoprolol 5 mg daily.	Propranolol	129-140	potassium voltage-gated channel subfamily H member 2	Homo sapiens	107-111
26271031-0	2016	Estradiol regulates human QT-interval: acceleration of cardiac repolarization by enhanced KCNH2 membrane trafficking.	Estradiol	0-9	potassium voltage-gated channel subfamily H member 2	Homo sapiens	90-95
26271031-12	2016	Estradiol enhanced the physical interaction of KCNH2-channel subunits with heat-shock proteins and augmented ion-channel trafficking to the membrane.	Estradiol	0-9	potassium voltage-gated channel subfamily H member 2	Homo sapiens	47-52
26271031-14	2016	Estradiol acts on KCNH2 channels via enhanced estradiol-receptor-alpha-mediated Hsp90 interaction, augments membrane trafficking and thereby increases repolarizing current.	Estradiol	0-9	potassium voltage-gated channel subfamily H member 2	Homo sapiens	18-23
26481172-0	2016	Differential Response to Risperidone in Schizophrenia Patients by KCNH2 Genotype and Drug Metabolizer Status.	Risperidone	25-36	potassium voltage-gated channel subfamily H member 2	Homo sapiens	66-71
27013874-2	2016	In light of this goal, we report a robust one-step method for the synthesis of dicarboxylic acid-terminated polyethylene glycol (PEG)-gold nanoparticles (AuNPs) and doxorubicin-loaded PEG-AuNPs, and their further antibody targeting (anti-Kv11.1 polyclonal antibody [pAb]).	Dicarboxylic Acids	79-96	potassium voltage-gated channel subfamily H member 2	Homo sapiens	238-244
27013874-2	2016	In light of this goal, we report a robust one-step method for the synthesis of dicarboxylic acid-terminated polyethylene glycol (PEG)-gold nanoparticles (AuNPs) and doxorubicin-loaded PEG-AuNPs, and their further antibody targeting (anti-Kv11.1 polyclonal antibody [pAb]).	Polyethylene Glycols	129-132	potassium voltage-gated channel subfamily H member 2	Homo sapiens	238-244
27013874-2	2016	In light of this goal, we report a robust one-step method for the synthesis of dicarboxylic acid-terminated polyethylene glycol (PEG)-gold nanoparticles (AuNPs) and doxorubicin-loaded PEG-AuNPs, and their further antibody targeting (anti-Kv11.1 polyclonal antibody [pAb]).	Doxorubicin	165-176	potassium voltage-gated channel subfamily H member 2	Homo sapiens	238-244
26481172-7	2016	RESULTS: Risperidone caused greater in vitro block of the alternatively spliced Kv11.1-3.1 isoform than full-length Kv11.1-1A channels, whereas its metabolite paliperidone and other atypical antipsychotics have similar potencies for the two isoforms.	Risperidone	9-20	potassium voltage-gated channel subfamily H member 2	Homo sapiens	80-86
26481172-8	2016	In the CATIE study (N=362), patients with genotypes associated with increased Kv11.1-3.1 expression (N=52) showed a better treatment response to risperidone compared with other drugs, but this association was dependent on metabolism status.	Risperidone	145-156	potassium voltage-gated channel subfamily H member 2	Homo sapiens	78-84
26481172-9	2016	Patients with KCNH2 risk genotypes and slow metabolizer status (approximately 7% of patients) showed marked improvement in symptoms when treated with risperidone compared with patients with fast metabolizer status or without the KCNH2 risk genotypes.	Risperidone	150-161	potassium voltage-gated channel subfamily H member 2	Homo sapiens	14-19
26481172-10	2016	CONCLUSIONS: These data support the hypothesis that Kv11.1 channels play a role in the therapeutic action of antipsychotic drugs, particularly risperidone, and further highlight the promise of optimizing response with genotype-guided therapy for schizophrenia patients.	Risperidone	143-154	potassium voltage-gated channel subfamily H member 2	Homo sapiens	52-58
26068526-6	2016	Electrophysiological studies showed that macrolides prolonging the QT interval inhibit the rapid component of the delayed rectifier K(+) current (IKr) through the block of potassium channels encoded by the human ether-a-go-go-related gene (HERG).	Macrolides	41-51	potassium voltage-gated channel subfamily H member 2	Homo sapiens	240-244
27069917-9	2016	By facilitating expression of channel protein HERG, potassium ions may prevent it from being shunted to procancerous pathways by inducing apoptosis.	Potassium	52-61	potassium voltage-gated channel subfamily H member 2	Homo sapiens	46-50
27069917-11	2016	Thus, our findings suggest that potassium ions could inhibit tumorigenesis through inducing apoptosis of hepatoma cells by upregulating potassium ions transport channel proteins HERG and VDAC1.	Potassium	32-41	potassium voltage-gated channel subfamily H member 2	Homo sapiens	178-182
26649323-0	2016	HERG Protein Plays a Role in Moxifloxacin-Induced Hypoglycemia.	Moxifloxacin	29-41	potassium voltage-gated channel subfamily H member 2	Homo sapiens	0-4
26649323-1	2016	The purpose of this study was to investigate the effect of moxifloxacin on HERG channel protein and glucose metabolism.	Moxifloxacin	59-71	potassium voltage-gated channel subfamily H member 2	Homo sapiens	75-79
26649323-3	2016	The whole-cell patch clamp method was used to examine the effect of moxifloxacin on HERG channel currents.	Moxifloxacin	68-80	potassium voltage-gated channel subfamily H member 2	Homo sapiens	84-88
26649323-6	2016	Moxifloxacin inhibited HERG time-dependent and tail currents in HEK293 cells in a concentration-dependent manner.	Moxifloxacin	0-12	potassium voltage-gated channel subfamily H member 2	Homo sapiens	23-27
26649323-10	2016	Serum glucose levels increased and insulin concentrations decreased in HERG knockout mice when compared to wild-type mice.	Glucose	6-13	potassium voltage-gated channel subfamily H member 2	Homo sapiens	71-75
26649323-11	2016	The moxifloxacin-induced decrease in blood glucose and increase in insulin secretion occurred via the HERG protein; thus, HERG protein plays a role in insulin secretion.	Moxifloxacin	4-16	potassium voltage-gated channel subfamily H member 2	Homo sapiens	102-106
26649323-11	2016	The moxifloxacin-induced decrease in blood glucose and increase in insulin secretion occurred via the HERG protein; thus, HERG protein plays a role in insulin secretion.	Moxifloxacin	4-16	potassium voltage-gated channel subfamily H member 2	Homo sapiens	122-126
26277508-2	2015	METHODS: HEK293 cells were transiently transfected with HERG channel cDNA plasmid pcDNA3.1 via Lipofectamine.	Lipofectamine	95-108	potassium voltage-gated channel subfamily H member 2	Homo sapiens	56-60
26503718-6	2015	Open-state stabilization by PIP2 has been observed in human Erg1, but the proposed site of regulation in the distal C terminus is not conserved among EAG family channels.	Phosphatidylinositol 4,5-Diphosphate	28-32	potassium voltage-gated channel subfamily H member 2	Homo sapiens	60-64
26376488-11	2015	Furthermore, the equine KV11.1 channel was susceptible to pharmacological block with terfenadine.	Terfenadine	85-96	potassium voltage-gated channel subfamily H member 2	Homo sapiens	24-30
25790957-6	2015	Experiments using the KCNH2-pore blocking agent quinidine supported these findings.	Quinidine	48-57	potassium voltage-gated channel subfamily H member 2	Homo sapiens	22-27
25986146-0	2015	Ivabradine prolongs phase 3 of cardiac repolarization and blocks the hERG1 (KCNH2) current over a concentration-range overlapping with that required to block HCN4.	Ivabradine	0-10	potassium voltage-gated channel subfamily H member 2	Homo sapiens	69-74
25986146-0	2015	Ivabradine prolongs phase 3 of cardiac repolarization and blocks the hERG1 (KCNH2) current over a concentration-range overlapping with that required to block HCN4.	Ivabradine	0-10	potassium voltage-gated channel subfamily H member 2	Homo sapiens	76-81
25986146-5	2015	The objective of this study is to assess whether ivabradine blocked the hERG1 current.	Ivabradine	49-59	potassium voltage-gated channel subfamily H member 2	Homo sapiens	72-77
25986146-9	2015	Disruption of C-type inactivation also suppressed block of hERG1 by ivabradine.	Ivabradine	68-78	potassium voltage-gated channel subfamily H member 2	Homo sapiens	59-64
25986146-10	2015	Molecular docking and molecular dynamics simulations indicate that ivabradine may access the inner cavity of the hERG1 via a lipophilic route and has a well-defined binding site in the closed state of the channel.	Ivabradine	67-77	potassium voltage-gated channel subfamily H member 2	Homo sapiens	113-118
25888115-6	2015	Analysis of a panel of mutant hERG1 and rERG2 channels further revealed that seven residues, five in the C-linker and two in the adjacent region of the cyclic nucleotide-binding homology domain, can fully account for the differential sensitivity of hERG1 and rERG2 channels to RPR.	Nucleotides, Cyclic	152-169	potassium voltage-gated channel subfamily H member 2	Homo sapiens	30-35
25888115-6	2015	Analysis of a panel of mutant hERG1 and rERG2 channels further revealed that seven residues, five in the C-linker and two in the adjacent region of the cyclic nucleotide-binding homology domain, can fully account for the differential sensitivity of hERG1 and rERG2 channels to RPR.	Nucleotides, Cyclic	152-169	potassium voltage-gated channel subfamily H member 2	Homo sapiens	249-254
26076856-0	2015	QT interval prolongation in a patient with LQT2 on levetiracetam.	Levetiracetam	51-64	potassium voltage-gated channel subfamily H member 2	Homo sapiens	43-47
25855787-4	2015	Concatenated hERG1 tetramers containing four wild-type subunits exhibited high-affinity block by cisapride, dofetilide, and MK-499, similar to wild-type channels formed from hERG1 monomers.	Cisapride	97-106	potassium voltage-gated channel subfamily H member 2	Homo sapiens	13-18
25855787-4	2015	Concatenated hERG1 tetramers containing four wild-type subunits exhibited high-affinity block by cisapride, dofetilide, and MK-499, similar to wild-type channels formed from hERG1 monomers.	dofetilide	108-118	potassium voltage-gated channel subfamily H member 2	Homo sapiens	13-18
25855787-4	2015	Concatenated hERG1 tetramers containing four wild-type subunits exhibited high-affinity block by cisapride, dofetilide, and MK-499, similar to wild-type channels formed from hERG1 monomers.	L 706000	124-130	potassium voltage-gated channel subfamily H member 2	Homo sapiens	13-18
25800797-6	2015	HEK293 cells stably transfected with KCNH2 (hERG) cDNA were used to examine the effects of hypaconitine on the KCNH2 channel by using the manual patch clamp technique.	hypaconitine	91-103	potassium voltage-gated channel subfamily H member 2	Homo sapiens	111-116
25800797-10	2015	In the in vitro study in HEK293 cells, hypaconitine inhibited the KCNH2 currents in a concentration-dependent manner with an IC50 of 8.1nM.	hypaconitine	39-51	potassium voltage-gated channel subfamily H member 2	Homo sapiens	66-71
25911606-2	2015	This study investigated the propensity of ivabradine to interact with KCNH2-encoded human Ether-a-go-go-Related Gene (hERG) potassium channels, which strongly influence ventricular repolarization and susceptibility to torsades de pointes arrhythmia.	Ivabradine	42-52	potassium voltage-gated channel subfamily H member 2	Homo sapiens	70-75
25967940-9	2015	The best combination of in silico tools for KCNH2 is SIFT and PROVEAN or PROVEAN, SNPs&GO and SIFT.	Adenosine Monophosphate	87-90	potassium voltage-gated channel subfamily H member 2	Homo sapiens	44-49
26937396-3	2015	Changes were identified in the KCNH2 gene and mitochondrial tRNA for cysteine.	Cysteine	69-77	potassium voltage-gated channel subfamily H member 2	Homo sapiens	31-36
25719829-6	2015	ERG1 expression in vivo was determined by optical imaging using Alexa-680-labelled alpha-hERG1-MoAb.	alexa-680	64-73	potassium voltage-gated channel subfamily H member 2	Homo sapiens	89-94
25468537-4	2015	Norsandwicine, 10-methoxypanarine, tueiaoine, and more importantly nukuhivensiums, were shown to significantly induce a reduction of IKr amplitude (HERG current).	norsandwicine	0-13	potassium voltage-gated channel subfamily H member 2	Homo sapiens	148-152
25576780-11	2015	The second AED rescue occurred in a remotely symptomatic 14-year-old boy with high-risk LQT2 (QTc >550 ms) on a beta-blocker who previously declined a prophylactic ICD.	qtc	94-97	potassium voltage-gated channel subfamily H member 2	Homo sapiens	88-92
25296617-4	2015	EXPERIMENTAL APPROACH: The affinity and kinetic parameters of 15 prototypical Kv 11.1 inhibitors were evaluated in a number of [(3) H]-dofetilide binding assays.	[(3) h]-dofetilide	127-145	potassium voltage-gated channel subfamily H member 2	Homo sapiens	78-85
25296617-6	2015	KEY RESULTS: A novel [(3) H]-dofetilide competition association assay was set up and validated, which allowed us to determine the binding kinetics of the Kv 11.1 blockers used in this study.	[(3) h]-dofetilide	21-39	potassium voltage-gated channel subfamily H member 2	Homo sapiens	154-161
25596745-0	2015	Stimulation of hERG1 channel activity promotes a calcium-dependent degradation of cyclin E2, but not cyclin E1, in breast cancer cells.	Calcium	49-56	potassium voltage-gated channel subfamily H member 2	Homo sapiens	15-20
25596745-4	2015	In addition we have also reveal that hERG1 stimulation induces an increase in intracellular calcium that is required for cyclin E2 degradation.	Calcium	92-99	potassium voltage-gated channel subfamily H member 2	Homo sapiens	37-42
25704028-0	2015	Phosphatidylinositol4-phosphate 5-kinase prevents the decrease in the HERG potassium current induced by Gq protein-coupled receptor stimulation.	Potassium	75-84	potassium voltage-gated channel subfamily H member 2	Homo sapiens	70-74
25704028-1	2015	The human ether-a-go-go-related gene (HERG) potassium current (IHERG) has been shown to decrease in amplitude following stimulation with Gq protein-coupled receptors (GqRs), such as alpha1-adrenergic and M1-muscarinic receptors (alpha1R and M1R, respectively), at least partly via the reduction of membrane phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2).	Potassium	44-53	potassium voltage-gated channel subfamily H member 2	Homo sapiens	38-42
25704028-1	2015	The human ether-a-go-go-related gene (HERG) potassium current (IHERG) has been shown to decrease in amplitude following stimulation with Gq protein-coupled receptors (GqRs), such as alpha1-adrenergic and M1-muscarinic receptors (alpha1R and M1R, respectively), at least partly via the reduction of membrane phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2).	Phosphatidylinositol 4,5-Diphosphate	307-344	potassium voltage-gated channel subfamily H member 2	Homo sapiens	38-42
25704028-1	2015	The human ether-a-go-go-related gene (HERG) potassium current (IHERG) has been shown to decrease in amplitude following stimulation with Gq protein-coupled receptors (GqRs), such as alpha1-adrenergic and M1-muscarinic receptors (alpha1R and M1R, respectively), at least partly via the reduction of membrane phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2).	pi(4,5)p2	346-355	potassium voltage-gated channel subfamily H member 2	Homo sapiens	38-42
25704028-2	2015	The present study was designed to investigate the modulation of HERG channels by PI(4,5)P2 and phosphatidylinositol4-phosphate 5-kinase (PI(4)P5-K), a synthetic enzyme of PI(4,5)P2.	pi(4,5)p2	81-90	potassium voltage-gated channel subfamily H member 2	Homo sapiens	64-68
25704028-2	2015	The present study was designed to investigate the modulation of HERG channels by PI(4,5)P2 and phosphatidylinositol4-phosphate 5-kinase (PI(4)P5-K), a synthetic enzyme of PI(4,5)P2.	pi(4,5)p2	171-180	potassium voltage-gated channel subfamily H member 2	Homo sapiens	64-68
25468537-4	2015	Norsandwicine, 10-methoxypanarine, tueiaoine, and more importantly nukuhivensiums, were shown to significantly induce a reduction of IKr amplitude (HERG current).	10-methoxypanarine	15-33	potassium voltage-gated channel subfamily H member 2	Homo sapiens	148-152
25468537-4	2015	Norsandwicine, 10-methoxypanarine, tueiaoine, and more importantly nukuhivensiums, were shown to significantly induce a reduction of IKr amplitude (HERG current).	tueiaoine	35-44	potassium voltage-gated channel subfamily H member 2	Homo sapiens	148-152
25232191-11	2014	Considering the substantial relationship between LQT2 and epilepsy, these findings reveal that NS1643 is a useful compound to elucidate the causal connection of LQT2 and epilepsy.	1,3-bis(2-hydroxy-5-trifluoromethylphenyl)urea	95-101	potassium voltage-gated channel subfamily H member 2	Homo sapiens	49-53
25232191-11	2014	Considering the substantial relationship between LQT2 and epilepsy, these findings reveal that NS1643 is a useful compound to elucidate the causal connection of LQT2 and epilepsy.	1,3-bis(2-hydroxy-5-trifluoromethylphenyl)urea	95-101	potassium voltage-gated channel subfamily H member 2	Homo sapiens	161-165
25974115-4	2015	A novel mutation KCNH2-I560T, when expressed in COS-7 cells, showed a 2.5-fold increase in peak current density, and a positive shift (+14 mV) of the inactivation curve compared with wild type.	carbonyl sulfide	48-51	potassium voltage-gated channel subfamily H member 2	Homo sapiens	17-22
25100024-0	2014	Molecular docking and molecular dynamics studies on the structure-activity relationship of fluoroquinolone for the HERG channel.	Fluoroquinolones	91-106	potassium voltage-gated channel subfamily H member 2	Homo sapiens	115-119
25249569-8	2014	Stimulation of LQT2 cells with beta-adrenergic agonist isoproterenol resulted in prolongation of the plateau of action potentials accompanied by aberrant Ca(2+) releases and EADs, which were abolished by inhibition of Ca(2+)/calmodulin-dependent protein kinase type 2.	Isoproterenol	55-68	potassium voltage-gated channel subfamily H member 2	Homo sapiens	15-19
25100024-1	2014	Fluoroquinolones play an important role in the treatment of serious bacterial infections, but at the same time they could lead to cardiac toxicity due to the blockage of the HERG potassium channel, which even leads to the withdrawal of some fluoroquinolones.	Fluoroquinolones	0-16	potassium voltage-gated channel subfamily H member 2	Homo sapiens	174-178
25100024-1	2014	Fluoroquinolones play an important role in the treatment of serious bacterial infections, but at the same time they could lead to cardiac toxicity due to the blockage of the HERG potassium channel, which even leads to the withdrawal of some fluoroquinolones.	Fluoroquinolones	241-257	potassium voltage-gated channel subfamily H member 2	Homo sapiens	174-178
25128783-0	2014	Upregulation of functional Kv11.1 isoform expression by inhibition of intronic polyadenylation with antisense morpholino oligonucleotides.	Morpholinos	110-137	potassium voltage-gated channel subfamily H member 2	Homo sapiens	27-33
25128783-6	2014	More importantly, blocking these elements by antisense morpholino oligonucleotides shifted the alternative processing of KCNH2 intron 9 from the polyadenylation to the splicing pathway, leading to the predominant production of Kv11.1a and a significant increase in Kv11.1 current.	Morpholinos	55-82	potassium voltage-gated channel subfamily H member 2	Homo sapiens	121-126
25128783-6	2014	More importantly, blocking these elements by antisense morpholino oligonucleotides shifted the alternative processing of KCNH2 intron 9 from the polyadenylation to the splicing pathway, leading to the predominant production of Kv11.1a and a significant increase in Kv11.1 current.	Morpholinos	55-82	potassium voltage-gated channel subfamily H member 2	Homo sapiens	227-233
25257637-7	2014	In LQT1, the risk reduction for first cardiac events was similar among the 4 beta-blockers, but in LQT2, nadolol provided the only significant risk reduction (hazard ratio: 0.40 [0.16 to 0.98]).	Nadolol	105-112	potassium voltage-gated channel subfamily H member 2	Homo sapiens	99-103
25257637-9	2014	CONCLUSIONS: Although the 4 beta-blockers are equally effective in reducing the risk of a first cardiac event in LQTS, their efficacy differed by genotype; nadolol was the only beta-blocker associated with a significant risk reduction in patients with LQT2.	Nadolol	156-163	potassium voltage-gated channel subfamily H member 2	Homo sapiens	252-256
25100024-3	2014	Though there were large amounts of bioactivity data of fluoroquinolones on the blockage of HERG, little structural basis of binding of blockers to the HERG channel was known.	Fluoroquinolones	55-71	potassium voltage-gated channel subfamily H member 2	Homo sapiens	91-95
25100024-4	2014	Here, we combined molecular docking, molecular dynamics simulations, free energy calculations and binding energy decomposition analysis to explore the binding modes of fluoroquinolones in the HERG potassium channel.	Fluoroquinolones	168-184	potassium voltage-gated channel subfamily H member 2	Homo sapiens	192-196
25100024-6	2014	Our results showed that the CH3 group in MX was favorable for the binding to the HERG channel, while Tyr652 and Phe656 were critical for the hydrophobic interaction between fluoroquinolones and the HERG channel.	Fluoroquinolones	173-189	potassium voltage-gated channel subfamily H member 2	Homo sapiens	198-202
24846011-0	2014	Inhibition of HERG potassium channels by domiphen bromide and didecyl dimethylammonium bromide.	domiphen	41-57	potassium voltage-gated channel subfamily H member 2	Homo sapiens	14-18
24846011-0	2014	Inhibition of HERG potassium channels by domiphen bromide and didecyl dimethylammonium bromide.	didecyldimethylammonium	62-94	potassium voltage-gated channel subfamily H member 2	Homo sapiens	14-18
24846011-1	2014	Domiphen bromide and didecyl dimethylammonium bromide were widely used environmental chemicals with potent activity on blockade of human ether-a-go-go related gene (HERG) channels.	domiphen	0-16	potassium voltage-gated channel subfamily H member 2	Homo sapiens	165-169
24846011-1	2014	Domiphen bromide and didecyl dimethylammonium bromide were widely used environmental chemicals with potent activity on blockade of human ether-a-go-go related gene (HERG) channels.	didecyldimethylammonium	21-53	potassium voltage-gated channel subfamily H member 2	Homo sapiens	165-169
24846011-3	2014	The kinetics of block of HERG channels by domiphen bromide and didecyl dimethylammonium bromide was studied in order to characterize the inhibition of HERG currents by these quaternary ammonium compounds (QACs).	domiphen	42-58	potassium voltage-gated channel subfamily H member 2	Homo sapiens	25-29
24846011-3	2014	The kinetics of block of HERG channels by domiphen bromide and didecyl dimethylammonium bromide was studied in order to characterize the inhibition of HERG currents by these quaternary ammonium compounds (QACs).	didecyldimethylammonium	63-95	potassium voltage-gated channel subfamily H member 2	Homo sapiens	25-29
24846011-3	2014	The kinetics of block of HERG channels by domiphen bromide and didecyl dimethylammonium bromide was studied in order to characterize the inhibition of HERG currents by these quaternary ammonium compounds (QACs).	Quaternary Ammonium Compounds	174-203	potassium voltage-gated channel subfamily H member 2	Homo sapiens	25-29
24846011-3	2014	The kinetics of block of HERG channels by domiphen bromide and didecyl dimethylammonium bromide was studied in order to characterize the inhibition of HERG currents by these quaternary ammonium compounds (QACs).	Quaternary Ammonium Compounds	174-203	potassium voltage-gated channel subfamily H member 2	Homo sapiens	151-155
24846011-4	2014	Domiphen bromide and didecyl dimethylammonium bromide inhibited HERG channel currents in a dose-dependent manner with IC50 values of 9nM and 5nM, respectively.	domiphen	0-16	potassium voltage-gated channel subfamily H member 2	Homo sapiens	64-68
24846011-4	2014	Domiphen bromide and didecyl dimethylammonium bromide inhibited HERG channel currents in a dose-dependent manner with IC50 values of 9nM and 5nM, respectively.	didecyldimethylammonium	21-53	potassium voltage-gated channel subfamily H member 2	Homo sapiens	64-68
24846011-5	2014	Block of HERG channel by domiphen bromide and didecyl dimethylammonium bromide was voltage-dependent and use-dependent.	domiphen	25-41	potassium voltage-gated channel subfamily H member 2	Homo sapiens	9-13
24846011-5	2014	Block of HERG channel by domiphen bromide and didecyl dimethylammonium bromide was voltage-dependent and use-dependent.	didecyldimethylammonium	46-78	potassium voltage-gated channel subfamily H member 2	Homo sapiens	9-13
24846011-7	2014	The docking models implied that these two compounds bound to PAS domain of HERG channels and inhibited its function.	Protactinium	61-64	potassium voltage-gated channel subfamily H member 2	Homo sapiens	75-79
24846011-8	2014	Our data demonstrated that domiphen bromide and didecyl dimethylammonium bromide blocked the HERG channel with a preference for the activated channel state.	domiphen	27-43	potassium voltage-gated channel subfamily H member 2	Homo sapiens	93-97
24846011-8	2014	Our data demonstrated that domiphen bromide and didecyl dimethylammonium bromide blocked the HERG channel with a preference for the activated channel state.	didecyldimethylammonium	48-80	potassium voltage-gated channel subfamily H member 2	Homo sapiens	93-97
24464434-0	2014	Roles of PKC Isoforms in PMA-Induced Modulation of the hERG Channel (Kv11.1).	Tetradecanoylphorbol Acetate	25-28	potassium voltage-gated channel subfamily H member 2	Homo sapiens	69-75
25254341-4	2014	In myocytes carrying an LQT2 mutation (HERG-A422T), APs and [Ca(2+)]i transients were prolonged in parallel.	Adenosine Phosphosulfate	52-55	potassium voltage-gated channel subfamily H member 2	Homo sapiens	24-28
25254341-4	2014	In myocytes carrying an LQT2 mutation (HERG-A422T), APs and [Ca(2+)]i transients were prolonged in parallel.	Adenosine Phosphosulfate	52-55	potassium voltage-gated channel subfamily H member 2	Homo sapiens	39-43
24875677-4	2014	In order to evaluate if any polymorphism of potassium channels" genes could explain some of the "idiosyncratic" QT prolongations observed in patients treated with methadone, we tested the association between KCNE1, KCNE2, and KCNH2 polymorphism and the QT interval prolongation in those patients, controlling for other variables associated with a decrease of the repolarizing reserve.	Methadone	163-172	potassium voltage-gated channel subfamily H member 2	Homo sapiens	226-231
24875677-9	2014	CONCLUSION: KCNH2 genotyping may be relevant in the analysis of cumulative risk factors for QT prolongation in patients on methadone maintenance treatment.	Methadone	123-132	potassium voltage-gated channel subfamily H member 2	Homo sapiens	12-17
24638994-4	2014	In human ether-a-go-go-related gene 1 (hERG1) K(+) channels, C-type inactivation is allosterically inhibited by ICA-105574, a substituted benzamide.	isocyanic acid	112-115	potassium voltage-gated channel subfamily H member 2	Homo sapiens	39-44
24630832-2	2014	In experimental systems varying from Drosophila to primary mammalian and human cell lines, celecoxib inhibits many voltage-activated Na(+), Ca(2+), and K(+) channels, including NaV1.5, L- and T-type Ca(2+) channels, KV1.5, KV2.1, KV4.3, KV7.1, KV11.1 (hERG), while stimulating other K(+) channels-KV7.2-5 and, possibly, KV11.1 (hERG) channels under certain conditions.	Celecoxib	91-100	potassium voltage-gated channel subfamily H member 2	Homo sapiens	244-250
24630832-2	2014	In experimental systems varying from Drosophila to primary mammalian and human cell lines, celecoxib inhibits many voltage-activated Na(+), Ca(2+), and K(+) channels, including NaV1.5, L- and T-type Ca(2+) channels, KV1.5, KV2.1, KV4.3, KV7.1, KV11.1 (hERG), while stimulating other K(+) channels-KV7.2-5 and, possibly, KV11.1 (hERG) channels under certain conditions.	Celecoxib	91-100	potassium voltage-gated channel subfamily H member 2	Homo sapiens	320-326
24530480-8	2014	Finally, we used a full-length hERG splicing-competent construct to show that inhibition of downstream intron splicing by antisense morpholino oligonucleotides inhibited NMD and rescued the functional expression of a third LQT2 mutation, Y1078.	Morpholinos	132-159	potassium voltage-gated channel subfamily H member 2	Homo sapiens	223-227
24638994-4	2014	In human ether-a-go-go-related gene 1 (hERG1) K(+) channels, C-type inactivation is allosterically inhibited by ICA-105574, a substituted benzamide.	benzamide	138-147	potassium voltage-gated channel subfamily H member 2	Homo sapiens	39-44
24638994-10	2014	Enhancement of hERG1 channel current magnitude by PD-118057 and attenuated inactivation by ICA-105574 were mediated by cooperative subunit interactions.	2-(4-(2-(3,4-dichlorophenyl)ethyl)phenylamino)benzoic acid	50-59	potassium voltage-gated channel subfamily H member 2	Homo sapiens	15-20
24638994-10	2014	Enhancement of hERG1 channel current magnitude by PD-118057 and attenuated inactivation by ICA-105574 were mediated by cooperative subunit interactions.	isocyanic acid	91-94	potassium voltage-gated channel subfamily H member 2	Homo sapiens	15-20
24516604-4	2014	The small molecule hERG ligand doxazosin induced concentration-dependent apoptosis of human LNT-229 (EC50 = 35 microM) and U87MG (EC50 = 29 microM) GB cells, accompanied by cell cycle arrest in the G0/G1 phase.	Doxazosin	31-40	potassium voltage-gated channel subfamily H member 2	Homo sapiens	19-23
24606761-1	2014	BACKGROUND: The human ether-a-go-go related gene 1 (hERG1), which codes for a potassium ion channel, is a key element in the cardiac delayed rectified potassium current, IKr, and plays an important role in the normal repolarization of the heart"s action potential.	Potassium	78-87	potassium voltage-gated channel subfamily H member 2	Homo sapiens	52-57
24606761-4	2014	METHODS: In this proof-of-principle study, we focus on cisapride, a gastroprokinetic agent withdrawn from the market due to its high hERG1 blocking affinity.	Cisapride	55-64	potassium voltage-gated channel subfamily H member 2	Homo sapiens	133-138
24606930-0	2014	Proline scan of the HERG channel S6 helix reveals the location of the intracellular pore gate.	Proline	0-7	potassium voltage-gated channel subfamily H member 2	Homo sapiens	20-24
24366185-0	2014	Comparison of read-through effects of aminoglycosides and PTC124 on rescuing nonsense mutations of HERG gene associated with long QT syndrome.	Aminoglycosides	38-53	potassium voltage-gated channel subfamily H member 2	Homo sapiens	99-103
24366185-2	2014	The read-through effects of different aminoglycosides and PTC124 on HERG gene have yet to be adequately elucidated.	Aminoglycosides	38-53	potassium voltage-gated channel subfamily H member 2	Homo sapiens	68-72
24366185-13	2014	The above results suggest that aminoglycosides and PTC124 induced different effects on rescue nonsense mutations of the HERG gene.	Aminoglycosides	31-46	potassium voltage-gated channel subfamily H member 2	Homo sapiens	120-124
24366185-13	2014	The above results suggest that aminoglycosides and PTC124 induced different effects on rescue nonsense mutations of the HERG gene.	ataluren	51-57	potassium voltage-gated channel subfamily H member 2	Homo sapiens	120-124
24516604-6	2014	HERG suppression via siRNA-mediated knock down mimicked pro-apoptotic effects of doxazosin.	Doxazosin	81-90	potassium voltage-gated channel subfamily H member 2	Homo sapiens	0-4
24212718-3	2014	Reduced serum glucose blocks the repolarizing K(+) channel HERG, which leads to action potential and QT prolongation and is uniformly associated with risk for torsades de pointes ventricular tachycardia.	Glucose	14-21	potassium voltage-gated channel subfamily H member 2	Homo sapiens	59-63
24475014-4	2014	We employed AP-clamp techniques using physiological action potential waveforms recorded from various regions of canine heart to study HERG function in HEK293 cells and identified several novel aspects of HERG function.	CLAmP	15-20	potassium voltage-gated channel subfamily H member 2	Homo sapiens	204-208
24475014-10	2014	Based on our results, we conclude that the distinct biophysical properties of HERG reported by AP-clamp confer its unique function in cardiac repolarization thereby in antiarrhythmia and arrhythmogenesis.	ap-clamp	95-103	potassium voltage-gated channel subfamily H member 2	Homo sapiens	78-82
25177033-0	2014	Blockade of HERG human K+ channels by the antidepressant drug paroxetine.	Paroxetine	62-72	potassium voltage-gated channel subfamily H member 2	Homo sapiens	12-16
24606761-7	2014	An analysis of the fragment interactions of cisapride at human A2A adenosine receptors and hERG1 central cavities helped us to identify the key chemical groups responsible for the drug activity and hERG1 blockade.	Cisapride	44-53	potassium voltage-gated channel subfamily H member 2	Homo sapiens	91-96
24606761-7	2014	An analysis of the fragment interactions of cisapride at human A2A adenosine receptors and hERG1 central cavities helped us to identify the key chemical groups responsible for the drug activity and hERG1 blockade.	Cisapride	44-53	potassium voltage-gated channel subfamily H member 2	Homo sapiens	198-203
24606761-10	2014	CONCLUSIONS: An interaction decomposition of cisapride and cisapride derivatives allowed for the identification of key active scaffolds and functional groups that may be responsible for the unwanted blockade of hERG1.	Cisapride	45-54	potassium voltage-gated channel subfamily H member 2	Homo sapiens	211-216
24606761-10	2014	CONCLUSIONS: An interaction decomposition of cisapride and cisapride derivatives allowed for the identification of key active scaffolds and functional groups that may be responsible for the unwanted blockade of hERG1.	Cisapride	59-68	potassium voltage-gated channel subfamily H member 2	Homo sapiens	211-216
25366487-0	2014	Effect of terfenadine and pentamidine on the HERG channel and its intracellular trafficking: combined analysis with automated voltage clamp and confocal microscopy.	Terfenadine	10-21	potassium voltage-gated channel subfamily H member 2	Homo sapiens	45-49
25366487-0	2014	Effect of terfenadine and pentamidine on the HERG channel and its intracellular trafficking: combined analysis with automated voltage clamp and confocal microscopy.	Pentamidine	26-37	potassium voltage-gated channel subfamily H member 2	Homo sapiens	45-49
25177033-1	2014	The effects of paroxetine, a selective serotonin reuptake inhibitor, on human ether-a-go-go-related gene (HERG) channels were investigated using the whole-cell patch-clamp technique.	Paroxetine	15-25	potassium voltage-gated channel subfamily H member 2	Homo sapiens	106-110
25177033-3	2014	Paroxetine inhibited the peak tail currents of the HERG channel in a concentration-dependent manner, with an IC50 value of 0.45 microM and a Hill coefficient of 0.85.	Paroxetine	0-10	potassium voltage-gated channel subfamily H member 2	Homo sapiens	51-55
24386440-2	2013	METHODS: We treated neonatal rat ventricular myocytes and HEK293 cells with stable expression of h-ERG with H2O2 for 12 h and 48 h. Expression of miR-17-5p seed miRNAs was quantified by real-time RT-PCR.	Hydrogen Peroxide	108-112	potassium voltage-gated channel subfamily H member 2	Homo sapiens	97-102
24386440-6	2013	RESULTS: H-ERG trafficking was impaired by H2O2 after 48 h treatment, accompanied by reciprocal changes of expression between miR-17-5p seed miRNAs and several chaperones (Hsp70, Hsc70, CANX, and Golga2), with the former upregulated and the latter downregulated.	Hydrogen Peroxide	43-47	potassium voltage-gated channel subfamily H member 2	Homo sapiens	9-14
24386440-8	2013	Application miR-17-5p inhibitor rescued H2O2-induced impairment of h-ERG trafficking.	Hydrogen Peroxide	40-44	potassium voltage-gated channel subfamily H member 2	Homo sapiens	67-72
24386440-9	2013	Upregulation of endogenous by H2O2 or forced miR-17-5p expression either reduced h-ERG current.	Hydrogen Peroxide	30-34	potassium voltage-gated channel subfamily H member 2	Homo sapiens	81-86
24369231-2	2013	METHODS: The plasmids pcDNA3.1-PTPN12-RFP and herg mutant constructed by PCR technique were transfected into HEK293 cells via Lipofectamine 2000, and the cells stably expressing PTPN12 selected with G418 were identified by Western blotting with anti-PTPN12 antibody.	Lipofectamine	126-144	potassium voltage-gated channel subfamily H member 2	Homo sapiens	46-50
25246284-6	2014	COX-2 inhibitor and PGE2 had influence on the HERG current in gastric cancer cells.	Dinoprostone	20-24	potassium voltage-gated channel subfamily H member 2	Homo sapiens	46-50
25246284-7	2014	COX-2 inhibitor reduced the amplitude of HERG current in gastric cancer cells and PGE2 enhanced the amplitude.	Dinoprostone	82-86	potassium voltage-gated channel subfamily H member 2	Homo sapiens	41-45
25246284-8	2014	However, in gastric cancer cells transfected with HERG mutant deleting cAMP-binding domain, both COX-2 inhibitor and PGE2 did not show significant effects on HERG current.	Cyclic AMP	71-75	potassium voltage-gated channel subfamily H member 2	Homo sapiens	50-54
25246284-8	2014	However, in gastric cancer cells transfected with HERG mutant deleting cAMP-binding domain, both COX-2 inhibitor and PGE2 did not show significant effects on HERG current.	Dinoprostone	117-121	potassium voltage-gated channel subfamily H member 2	Homo sapiens	50-54
25246284-9	2014	cAMP agonist enhanced the amplitude of HERG current and cAMP antagonist reduced the amplitude in gastric cancer cells.	Cyclic AMP	0-4	potassium voltage-gated channel subfamily H member 2	Homo sapiens	39-43
25177033-5	2014	The paroxetine-induced inhibition of the HERG channels was voltage-dependent.	Paroxetine	4-14	potassium voltage-gated channel subfamily H member 2	Homo sapiens	41-45
25177033-9	2014	Paroxetine induced a leftward shift in the voltage-dependence of the steady-state activation of the HERG channels.	Paroxetine	0-10	potassium voltage-gated channel subfamily H member 2	Homo sapiens	100-104
25177033-14	2014	These results suggest that paroxetine blocks the HERG channels by binding to these channels in the open and inactivated states.	Paroxetine	27-37	potassium voltage-gated channel subfamily H member 2	Homo sapiens	49-53
24193004-6	2013	We here propose a method for hERG1 gene quantification in colorectal cancer samples in both cryopreserved and formalin-fixed and paraffin-embedded samples.	Formaldehyde	110-118	potassium voltage-gated channel subfamily H member 2	Homo sapiens	29-34
24193004-6	2013	We here propose a method for hERG1 gene quantification in colorectal cancer samples in both cryopreserved and formalin-fixed and paraffin-embedded samples.	Paraffin	129-137	potassium voltage-gated channel subfamily H member 2	Homo sapiens	29-34
24369231-7	2013	CONCLUSION: PTPN12 negatively regulates cardiac HERG channel cerrent possibly by decreasing the phosphorylation level of HERG tyrosine residues.	Tyrosine	126-134	potassium voltage-gated channel subfamily H member 2	Homo sapiens	48-52
24369231-7	2013	CONCLUSION: PTPN12 negatively regulates cardiac HERG channel cerrent possibly by decreasing the phosphorylation level of HERG tyrosine residues.	Tyrosine	126-134	potassium voltage-gated channel subfamily H member 2	Homo sapiens	121-125
24206565-8	2013	Potassium supplementation and sex hormone-based therapy may protect patients with LQT2.	Potassium	0-9	potassium voltage-gated channel subfamily H member 2	Homo sapiens	82-86
23718892-0	2013	Differential effects of the beta-adrenoceptor blockers carvedilol and metoprolol on SQT1- and SQT2-mutant channels.	Carvedilol	55-65	potassium voltage-gated channel subfamily H member 2	Homo sapiens	84-88
23864605-11	2013	These data suggest that pharmacological correction quickly increases the trafficking of LQT2 channels stored in the transitional ER via a Rab11B-dependent pathway, and we conclude that the pharmacological chaperone activity of drugs like ranolazine might have therapeutic potential.	Ranolazine	238-248	potassium voltage-gated channel subfamily H member 2	Homo sapiens	88-92
23718892-0	2013	Differential effects of the beta-adrenoceptor blockers carvedilol and metoprolol on SQT1- and SQT2-mutant channels.	Metoprolol	70-80	potassium voltage-gated channel subfamily H member 2	Homo sapiens	84-88
23718892-7	2013	Carvedilol"s (1 muM) inhibition of the IKr tail was attenuated in N588K-KCNH2 (4.5 +- 3% vs 50.3 +- 4%, WT, P < 0.001) with IC50 values of 2.8 muM (WT) and 25.4 muM (N588K).	Carvedilol	0-10	potassium voltage-gated channel subfamily H member 2	Homo sapiens	72-77
23718892-8	2013	Carvedilol"s IKr end-pulse inhibition, however, was increased in N588K-KCNH2 (10 muM, 60.7 +- 6% vs 36.5 +- 5%, WT, P < 0.01).	Carvedilol	0-10	potassium voltage-gated channel subfamily H member 2	Homo sapiens	71-76
23718892-10	2013	CONCLUSIONS: N588K-KCNH2 and V307L-KCNQ1 mutations decrease carvedilol"s inhibition of the IKs or IKr tail but increase carvedilol"s IKr end-pulse inhibition and metoprolol"s inhibition of tail and end-pulse currents.	Carvedilol	60-70	potassium voltage-gated channel subfamily H member 2	Homo sapiens	19-24
23721480-2	2013	Previous studies have identified the cytosolic PAS (Per/Arnt/Sim) domain as a hotspot for mutations that cause Kv11.1 trafficking defects.	Aminosalicylic Acid	47-50	potassium voltage-gated channel subfamily H member 2	Homo sapiens	111-117
23793622-0	2013	Cholesterol regulates HERG K+ channel activation by increasing phospholipase C beta1 expression.	Cholesterol	0-11	potassium voltage-gated channel subfamily H member 2	Homo sapiens	22-26
23793622-3	2013	Recently, we showed that enrichment of cell membrane with cholesterol inhibits HERG channels by reducing the levels of phosphatidylinositol 4,5-bisphosphate [PtdIns(4,5)P2] due to the activation of phospholipase C (PLC).	Cholesterol	58-69	potassium voltage-gated channel subfamily H member 2	Homo sapiens	79-83
23793622-3	2013	Recently, we showed that enrichment of cell membrane with cholesterol inhibits HERG channels by reducing the levels of phosphatidylinositol 4,5-bisphosphate [PtdIns(4,5)P2] due to the activation of phospholipase C (PLC).	Phosphatidylinositol 4,5-Diphosphate	119-156	potassium voltage-gated channel subfamily H member 2	Homo sapiens	79-83
23793622-3	2013	Recently, we showed that enrichment of cell membrane with cholesterol inhibits HERG channels by reducing the levels of phosphatidylinositol 4,5-bisphosphate [PtdIns(4,5)P2] due to the activation of phospholipase C (PLC).	Phosphatidylinositol 4,5-Diphosphate	158-171	potassium voltage-gated channel subfamily H member 2	Homo sapiens	79-83
23793622-4	2013	In this study, we further explored the effect of cholesterol enrichment on HERG channel kinetics.	Cholesterol	49-60	potassium voltage-gated channel subfamily H member 2	Homo sapiens	75-79
23793622-5	2013	When membrane cholesterol level was mildly increased in human embryonic kidney (HEK) 293 cells expressing HERG channel, the inactivation and deactivation kinetics of HERG current were not affected, but the activation rate was significantly decelerated at all voltages tested.	Cholesterol	14-25	potassium voltage-gated channel subfamily H member 2	Homo sapiens	106-110
23793622-5	2013	When membrane cholesterol level was mildly increased in human embryonic kidney (HEK) 293 cells expressing HERG channel, the inactivation and deactivation kinetics of HERG current were not affected, but the activation rate was significantly decelerated at all voltages tested.	Cholesterol	14-25	potassium voltage-gated channel subfamily H member 2	Homo sapiens	166-170
23793622-7	2013	These results indicate that the effect of cholesterol enrichment on HERG channel is due to the depletion of PtdIns(4,5)P2.	Cholesterol	42-53	potassium voltage-gated channel subfamily H member 2	Homo sapiens	68-72
23793622-7	2013	These results indicate that the effect of cholesterol enrichment on HERG channel is due to the depletion of PtdIns(4,5)P2.	Phosphatidylinositol 4,5-Diphosphate	108-121	potassium voltage-gated channel subfamily H member 2	Homo sapiens	68-72
23793622-9	2013	Since the effects of cholesterol enrichment on HERG channel were prevented by inhibiting transcription or by inhibiting PLCbeta1 expression, we conclude that increased PLCbeta1 expression leads to the deceleration of HERG channel activation rate via downregulation of PtdIns(4,5)P2.	Cholesterol	21-32	potassium voltage-gated channel subfamily H member 2	Homo sapiens	47-51
23840331-3	2013	It is reported that PD-118057 and thapsigargin can rescue LQT2 without hERG channel blockade, but the precise mechanism of action is unknown.	2-(4-(2-(3,4-dichlorophenyl)ethyl)phenylamino)benzoic acid	20-29	potassium voltage-gated channel subfamily H member 2	Homo sapiens	58-62
23840331-3	2013	It is reported that PD-118057 and thapsigargin can rescue LQT2 without hERG channel blockade, but the precise mechanism of action is unknown.	Thapsigargin	34-46	potassium voltage-gated channel subfamily H member 2	Homo sapiens	58-62
23840331-5	2013	OBJECTIVE: IN THIS STUDY, WE INVESTIGATED: (a) the effect of PD-118057 and thapsigargin on the current amplitudes of WT-hERG and WT/E637K-hERG channels; (b) the effect of PD-118057 and thapsigargin on the biophysical properties of WT-hERG and WT/E637K-hERG channels; (c) whether drug treatment can rescue channel processing and trafficking defects of the WT/E637K-hERG mutant.	Thapsigargin	75-87	potassium voltage-gated channel subfamily H member 2	Homo sapiens	138-142
23840331-9	2013	Additionally, thapsigargin shows a similar result as PD-118057 for the WT-hERG channel, but with the exception of attenuating steady-state inactivation.	Thapsigargin	14-26	potassium voltage-gated channel subfamily H member 2	Homo sapiens	74-78
23793622-9	2013	Since the effects of cholesterol enrichment on HERG channel were prevented by inhibiting transcription or by inhibiting PLCbeta1 expression, we conclude that increased PLCbeta1 expression leads to the deceleration of HERG channel activation rate via downregulation of PtdIns(4,5)P2.	Cholesterol	21-32	potassium voltage-gated channel subfamily H member 2	Homo sapiens	217-221
23793622-9	2013	Since the effects of cholesterol enrichment on HERG channel were prevented by inhibiting transcription or by inhibiting PLCbeta1 expression, we conclude that increased PLCbeta1 expression leads to the deceleration of HERG channel activation rate via downregulation of PtdIns(4,5)P2.	Phosphatidylinositol 4,5-Diphosphate	268-281	potassium voltage-gated channel subfamily H member 2	Homo sapiens	47-51
23793622-10	2013	These results confirm a crosstalk between two plasma membrane-enriched lipids, cholesterol and PtdIns(4,5)P2, in the regulation of HERG channels.	Cholesterol	79-90	potassium voltage-gated channel subfamily H member 2	Homo sapiens	131-135
23793622-10	2013	These results confirm a crosstalk between two plasma membrane-enriched lipids, cholesterol and PtdIns(4,5)P2, in the regulation of HERG channels.	Phosphatidylinositol 4,5-Diphosphate	95-108	potassium voltage-gated channel subfamily H member 2	Homo sapiens	131-135
22564166-0	2013	QSAR and pharmacophore analysis of a series of piperidinyl urea derivatives as HERG blockers and H3 antagonists.	piperidinyl urea	47-63	potassium voltage-gated channel subfamily H member 2	Homo sapiens	79-83
23744352-6	2013	Application of the hERG1 activator, the diphenylurea derivative NS1643, inhibits cell proliferation irreversibly.	Carbanilides	40-52	potassium voltage-gated channel subfamily H member 2	Homo sapiens	19-24
23744352-6	2013	Application of the hERG1 activator, the diphenylurea derivative NS1643, inhibits cell proliferation irreversibly.	1,3-bis(2-hydroxy-5-trifluoromethylphenyl)urea	64-70	potassium voltage-gated channel subfamily H member 2	Homo sapiens	19-24
23418776-2	2013	In the present study we analysed, using a site-directed cysteine and disulfide chemistry approach, whether the eag/PAS (Per/Arnt/Sim) and proximal domains at the HERG N-terminus exert a role in controlling the access of the N-terminal flexible tail to its binding site in the channel core for interaction with the gating machinery.	Protactinium	115-118	potassium voltage-gated channel subfamily H member 2	Homo sapiens	162-166
23418776-4	2013	The state-dependent formation of a disulfide bridge between Cys3 and an endogenous cysteine residue at position 723 in the C-terminal C-linker suggests that the N-terminal tail of HERG can also get into close proximity with the C-linker structures located at the bottom of helix S6.	Disulfides	35-44	potassium voltage-gated channel subfamily H member 2	Homo sapiens	180-184
23418776-4	2013	The state-dependent formation of a disulfide bridge between Cys3 and an endogenous cysteine residue at position 723 in the C-terminal C-linker suggests that the N-terminal tail of HERG can also get into close proximity with the C-linker structures located at the bottom of helix S6.	Cysteine	83-91	potassium voltage-gated channel subfamily H member 2	Homo sapiens	180-184
23917377-0	2013	ZC88, a novel 4-amino piperidine analog, inhibits the growth of neuroblastoma cells through blocking hERG potassium channel.	zc88	0-4	potassium voltage-gated channel subfamily H member 2	Homo sapiens	101-105
23917377-0	2013	ZC88, a novel 4-amino piperidine analog, inhibits the growth of neuroblastoma cells through blocking hERG potassium channel.	4-aminopiperidine	14-32	potassium voltage-gated channel subfamily H member 2	Homo sapiens	101-105
23917377-4	2013	The results showed that ZC88 could block hERG1 and hERG1b channels expressed in Xenopus oocytes in a concentration-dependent manner.	zc88	24-28	potassium voltage-gated channel subfamily H member 2	Homo sapiens	41-46
23546015-0	2013	Mechanistic basis for type 2 long QT syndrome caused by KCNH2 mutations that disrupt conserved arginine residues in the voltage sensor.	Arginine	95-103	potassium voltage-gated channel subfamily H member 2	Homo sapiens	56-61
23546015-4	2013	Kv11.1 contains several conserved basic amino acids in the fourth transmembrane segment (S4) of the voltage sensor that are important for normal channel trafficking and gating.	Amino Acids, Basic	34-51	potassium voltage-gated channel subfamily H member 2	Homo sapiens	0-6
23546015-5	2013	This study sought to determine the mechanism(s) by which LQT2 mutations at conserved arginine residues in S4 (R531Q, R531W or R534L) alter Kv11.1 function.	Arginine	85-93	potassium voltage-gated channel subfamily H member 2	Homo sapiens	57-61
23546015-5	2013	This study sought to determine the mechanism(s) by which LQT2 mutations at conserved arginine residues in S4 (R531Q, R531W or R534L) alter Kv11.1 function.	Arginine	85-93	potassium voltage-gated channel subfamily H member 2	Homo sapiens	139-145
23613831-2	2013	Some pathways driven by angiotensin II, nitric oxide and adrenergic receptors blocker are involved in modulating the properties of KCNH2 potassium channels.	Nitric Oxide	40-52	potassium voltage-gated channel subfamily H member 2	Homo sapiens	131-136
23613831-7	2013	RESULTS: There were statistically significant interactions between KCNH2 (1956, C>T) polymorphism and DBP change (P = 0.010), MAP change (P = 0.014) on azelnidipine or nitrendipine therapy patients at the end of 6 weeks.	azelnidipine	155-167	potassium voltage-gated channel subfamily H member 2	Homo sapiens	67-72
23613831-7	2013	RESULTS: There were statistically significant interactions between KCNH2 (1956, C>T) polymorphism and DBP change (P = 0.010), MAP change (P = 0.014) on azelnidipine or nitrendipine therapy patients at the end of 6 weeks.	Nitrendipine	171-183	potassium voltage-gated channel subfamily H member 2	Homo sapiens	67-72
23712551-7	2013	Low pH similarly reduces Mg(2+) sensitivity of Kv10.1, and we found that the pH sensitivity of Kv11.1 was greatly attenuated at 1 mM Ca(2+).	magnesium ion	25-31	potassium voltage-gated channel subfamily H member 2	Homo sapiens	95-101
23917959-6	2013	To generate disease model for LQT2 by iPS cells, we should firstly generate iPS cells from the patient with LQT2 and confirm the genomic mutation in iPS cells.	IPS	38-41	potassium voltage-gated channel subfamily H member 2	Homo sapiens	30-34
23917959-6	2013	To generate disease model for LQT2 by iPS cells, we should firstly generate iPS cells from the patient with LQT2 and confirm the genomic mutation in iPS cells.	IPS	76-79	potassium voltage-gated channel subfamily H member 2	Homo sapiens	30-34
23917959-6	2013	To generate disease model for LQT2 by iPS cells, we should firstly generate iPS cells from the patient with LQT2 and confirm the genomic mutation in iPS cells.	IPS	76-79	potassium voltage-gated channel subfamily H member 2	Homo sapiens	108-112
23917959-6	2013	To generate disease model for LQT2 by iPS cells, we should firstly generate iPS cells from the patient with LQT2 and confirm the genomic mutation in iPS cells.	IPS	76-79	potassium voltage-gated channel subfamily H member 2	Homo sapiens	30-34
23917959-6	2013	To generate disease model for LQT2 by iPS cells, we should firstly generate iPS cells from the patient with LQT2 and confirm the genomic mutation in iPS cells.	IPS	76-79	potassium voltage-gated channel subfamily H member 2	Homo sapiens	108-112
23917959-7	2013	In this study, we showed the successful generation of iPS cells from a patient with KCNH2 G603D mutation.	IPS	54-57	potassium voltage-gated channel subfamily H member 2	Homo sapiens	84-89
23917959-9	2013	We also confirmed that the KCNH2 G603D (G1808A) mutation was taken over in patient specific iPS cells.	IPS	92-95	potassium voltage-gated channel subfamily H member 2	Homo sapiens	27-32
22949429-6	2012	Collectively, when at least 3 of the 4 tools agreed on the pathogenic status of C-terminal nsSNVs located outside the KCNH2/Kv11.1 cyclic nucleotide-binding domain, the topology-specific estimated predictive value improved from 56% to 91%.	Nucleotides, Cyclic	131-148	potassium voltage-gated channel subfamily H member 2	Homo sapiens	124-130
23103450-4	2013	Arsenic trioxide (As(2)O(3)), which is used to treat acute promyelocytic leukemia, can cause LQTS type 2 (LQT2) by reducing the hERG current through the diversion of hERG trafficking to the cytoplasmic membrane.	Arsenic Trioxide	0-16	potassium voltage-gated channel subfamily H member 2	Homo sapiens	93-104
23103450-4	2013	Arsenic trioxide (As(2)O(3)), which is used to treat acute promyelocytic leukemia, can cause LQTS type 2 (LQT2) by reducing the hERG current through the diversion of hERG trafficking to the cytoplasmic membrane.	Arsenic Trioxide	0-16	potassium voltage-gated channel subfamily H member 2	Homo sapiens	106-110
23103450-4	2013	Arsenic trioxide (As(2)O(3)), which is used to treat acute promyelocytic leukemia, can cause LQTS type 2 (LQT2) by reducing the hERG current through the diversion of hERG trafficking to the cytoplasmic membrane.	Arsenic	18-20	potassium voltage-gated channel subfamily H member 2	Homo sapiens	93-104
23103450-4	2013	Arsenic trioxide (As(2)O(3)), which is used to treat acute promyelocytic leukemia, can cause LQTS type 2 (LQT2) by reducing the hERG current through the diversion of hERG trafficking to the cytoplasmic membrane.	Arsenic	18-20	potassium voltage-gated channel subfamily H member 2	Homo sapiens	106-110
23103450-4	2013	Arsenic trioxide (As(2)O(3)), which is used to treat acute promyelocytic leukemia, can cause LQTS type 2 (LQT2) by reducing the hERG current through the diversion of hERG trafficking to the cytoplasmic membrane.	(2)o(3)	20-27	potassium voltage-gated channel subfamily H member 2	Homo sapiens	93-104
23103450-4	2013	Arsenic trioxide (As(2)O(3)), which is used to treat acute promyelocytic leukemia, can cause LQTS type 2 (LQT2) by reducing the hERG current through the diversion of hERG trafficking to the cytoplasmic membrane.	(2)o(3)	20-27	potassium voltage-gated channel subfamily H member 2	Homo sapiens	106-110
23103450-11	2013	Therefore, matrine and oxymatrine may have the potential to cure LQT2 as a potassium channel activator by promoting hERG channel activation and increasing hERG channel expression.	oxymatrine	23-33	potassium voltage-gated channel subfamily H member 2	Homo sapiens	65-69
23672049-12	2013	Liensinine improves protein expression of HERG channe in HERG-HEK cells.	liensinine	0-10	potassium voltage-gated channel subfamily H member 2	Homo sapiens	57-61
23221912-0	2013	Role of the activation gate in determining the extracellular potassium dependency of block of HERG by trapped drugs.	Potassium	61-70	potassium voltage-gated channel subfamily H member 2	Homo sapiens	94-98
23221912-4	2013	Extracellular potassium influences HERG channel inactivation and can alter block of HERG by some drugs.	Potassium	14-23	potassium voltage-gated channel subfamily H member 2	Homo sapiens	35-39
23221912-4	2013	Extracellular potassium influences HERG channel inactivation and can alter block of HERG by some drugs.	Potassium	14-23	potassium voltage-gated channel subfamily H member 2	Homo sapiens	84-88
23221912-6	2013	In this study, we show that block of WT HERG by bepridil and terfenadine, two drugs previously shown to be trapped inside the HERG channel after the channel closes, is insensitive to extracellular potassium over the range of 0 mM to 20 mM.	Bepridil	48-56	potassium voltage-gated channel subfamily H member 2	Homo sapiens	40-44
23221912-6	2013	In this study, we show that block of WT HERG by bepridil and terfenadine, two drugs previously shown to be trapped inside the HERG channel after the channel closes, is insensitive to extracellular potassium over the range of 0 mM to 20 mM.	Bepridil	48-56	potassium voltage-gated channel subfamily H member 2	Homo sapiens	126-130
23221912-6	2013	In this study, we show that block of WT HERG by bepridil and terfenadine, two drugs previously shown to be trapped inside the HERG channel after the channel closes, is insensitive to extracellular potassium over the range of 0 mM to 20 mM.	Terfenadine	61-72	potassium voltage-gated channel subfamily H member 2	Homo sapiens	40-44
23221912-6	2013	In this study, we show that block of WT HERG by bepridil and terfenadine, two drugs previously shown to be trapped inside the HERG channel after the channel closes, is insensitive to extracellular potassium over the range of 0 mM to 20 mM.	Terfenadine	61-72	potassium voltage-gated channel subfamily H member 2	Homo sapiens	126-130
23221912-7	2013	We also show that bepridil block of the HERG mutant D540K, a mutant channel that is unable to trap drugs, is dependent on extracellular potassium, correlates with the permeant ion, and is independent of HERG inactivation.	Bepridil	18-26	potassium voltage-gated channel subfamily H member 2	Homo sapiens	40-44
23221912-7	2013	We also show that bepridil block of the HERG mutant D540K, a mutant channel that is unable to trap drugs, is dependent on extracellular potassium, correlates with the permeant ion, and is independent of HERG inactivation.	Potassium	136-145	potassium voltage-gated channel subfamily H member 2	Homo sapiens	40-44
23221912-8	2013	These results suggest that the lack of extracellular potassium dependency of block of HERG by some drugs may in part be related to the ability of these drugs to be trapped inside the channel after the channel closes.	Potassium	53-62	potassium voltage-gated channel subfamily H member 2	Homo sapiens	86-90
24069049-14	2013	GA significantly inhibited the potassium currents in a dose- and voltage-dependent manner, suggesting that it exerts its antiarrhythmic action through the prolongation of APD and ERP owing to the inhibition of I K (I Kr, I Ks) and HERG K(+) channel.	Glycyrrhetinic Acid	0-2	potassium voltage-gated channel subfamily H member 2	Homo sapiens	231-235
24069049-14	2013	GA significantly inhibited the potassium currents in a dose- and voltage-dependent manner, suggesting that it exerts its antiarrhythmic action through the prolongation of APD and ERP owing to the inhibition of I K (I Kr, I Ks) and HERG K(+) channel.	Potassium	31-40	potassium voltage-gated channel subfamily H member 2	Homo sapiens	231-235
23358696-3	2013	For instance, ion channels such as the voltage-gated sodium channel, L-type calcium channel, Kv2.1, Kv1.5, Kv4.3 and HERG potassium channel were all reported to be inhibited by CXB.	Celecoxib	177-180	potassium voltage-gated channel subfamily H member 2	Homo sapiens	117-121
23672049-0	2013	[Effect of berberine, liensinine and neferine on HERG channel expression].	Berberine	11-20	potassium voltage-gated channel subfamily H member 2	Homo sapiens	49-53
23672049-0	2013	[Effect of berberine, liensinine and neferine on HERG channel expression].	liensinine	22-32	potassium voltage-gated channel subfamily H member 2	Homo sapiens	49-53
23672049-0	2013	[Effect of berberine, liensinine and neferine on HERG channel expression].	neferine	37-45	potassium voltage-gated channel subfamily H member 2	Homo sapiens	49-53
23672049-1	2013	OBJECTIVE: Immunofluorescence and Western blot methods were adopted for qualitative and quantitative detections of the effect of different concentrations of berberine, liensinine and neferine on the expression of stable transfection in HERG potassium channel in HEK-293 cells, as well as the effect of different concentrations of berberine on protein expression of Ikr channel in cardiac muscular tissues, in order to investigate the anti-arrhythmic mechanism of berberine, liensinine and neferine.	Berberine	157-166	potassium voltage-gated channel subfamily H member 2	Homo sapiens	236-240
23672049-1	2013	OBJECTIVE: Immunofluorescence and Western blot methods were adopted for qualitative and quantitative detections of the effect of different concentrations of berberine, liensinine and neferine on the expression of stable transfection in HERG potassium channel in HEK-293 cells, as well as the effect of different concentrations of berberine on protein expression of Ikr channel in cardiac muscular tissues, in order to investigate the anti-arrhythmic mechanism of berberine, liensinine and neferine.	liensinine	168-178	potassium voltage-gated channel subfamily H member 2	Homo sapiens	236-240
23672049-1	2013	OBJECTIVE: Immunofluorescence and Western blot methods were adopted for qualitative and quantitative detections of the effect of different concentrations of berberine, liensinine and neferine on the expression of stable transfection in HERG potassium channel in HEK-293 cells, as well as the effect of different concentrations of berberine on protein expression of Ikr channel in cardiac muscular tissues, in order to investigate the anti-arrhythmic mechanism of berberine, liensinine and neferine.	neferine	183-191	potassium voltage-gated channel subfamily H member 2	Homo sapiens	236-240
23672049-1	2013	OBJECTIVE: Immunofluorescence and Western blot methods were adopted for qualitative and quantitative detections of the effect of different concentrations of berberine, liensinine and neferine on the expression of stable transfection in HERG potassium channel in HEK-293 cells, as well as the effect of different concentrations of berberine on protein expression of Ikr channel in cardiac muscular tissues, in order to investigate the anti-arrhythmic mechanism of berberine, liensinine and neferine.	Berberine	330-339	potassium voltage-gated channel subfamily H member 2	Homo sapiens	236-240
23672049-1	2013	OBJECTIVE: Immunofluorescence and Western blot methods were adopted for qualitative and quantitative detections of the effect of different concentrations of berberine, liensinine and neferine on the expression of stable transfection in HERG potassium channel in HEK-293 cells, as well as the effect of different concentrations of berberine on protein expression of Ikr channel in cardiac muscular tissues, in order to investigate the anti-arrhythmic mechanism of berberine, liensinine and neferine.	Berberine	330-339	potassium voltage-gated channel subfamily H member 2	Homo sapiens	236-240
23672049-1	2013	OBJECTIVE: Immunofluorescence and Western blot methods were adopted for qualitative and quantitative detections of the effect of different concentrations of berberine, liensinine and neferine on the expression of stable transfection in HERG potassium channel in HEK-293 cells, as well as the effect of different concentrations of berberine on protein expression of Ikr channel in cardiac muscular tissues, in order to investigate the anti-arrhythmic mechanism of berberine, liensinine and neferine.	liensinine	474-484	potassium voltage-gated channel subfamily H member 2	Homo sapiens	236-240
23672049-1	2013	OBJECTIVE: Immunofluorescence and Western blot methods were adopted for qualitative and quantitative detections of the effect of different concentrations of berberine, liensinine and neferine on the expression of stable transfection in HERG potassium channel in HEK-293 cells, as well as the effect of different concentrations of berberine on protein expression of Ikr channel in cardiac muscular tissues, in order to investigate the anti-arrhythmic mechanism of berberine, liensinine and neferine.	neferine	489-497	potassium voltage-gated channel subfamily H member 2	Homo sapiens	236-240
23672049-3	2013	Immunofluorescence method as well as confocal laser microscope were used to detect the effect of different concentrations of berberine, liensinine and neferine on protein expression of HERG channel.	Berberine	125-134	potassium voltage-gated channel subfamily H member 2	Homo sapiens	185-189
23672049-3	2013	Immunofluorescence method as well as confocal laser microscope were used to detect the effect of different concentrations of berberine, liensinine and neferine on protein expression of HERG channel.	liensinine	136-146	potassium voltage-gated channel subfamily H member 2	Homo sapiens	185-189
23672049-3	2013	Immunofluorescence method as well as confocal laser microscope were used to detect the effect of different concentrations of berberine, liensinine and neferine on protein expression of HERG channel.	neferine	151-159	potassium voltage-gated channel subfamily H member 2	Homo sapiens	185-189
23672049-4	2013	Western blot method was used to detect the effect of different concentrations of berberine on protein expression of Ikr channel in cardiac muscular tissues as well as the effect of berberine, liensinine and neferine on protein expression of stable transfection in HERG potassium channel in HEK-293 cells.	neferine	207-215	potassium voltage-gated channel subfamily H member 2	Homo sapiens	264-268
23672049-6	2013	Berberine (10, 30 micromol x L(-1)) remarkably inhibited protein expression of HERG channel in HERG-HEK cells (P < 0.01).	Berberine	0-9	potassium voltage-gated channel subfamily H member 2	Homo sapiens	79-83
23672049-6	2013	Berberine (10, 30 micromol x L(-1)) remarkably inhibited protein expression of HERG channel in HERG-HEK cells (P < 0.01).	Berberine	0-9	potassium voltage-gated channel subfamily H member 2	Homo sapiens	95-99
23672049-8	2013	Liensinine (3, 10, 30 micromol x L(-1)) increased protein expression of HERG channel in HERG-HEK cells (P < 0.05).	liensinine	0-10	potassium voltage-gated channel subfamily H member 2	Homo sapiens	72-76
23672049-8	2013	Liensinine (3, 10, 30 micromol x L(-1)) increased protein expression of HERG channel in HERG-HEK cells (P < 0.05).	liensinine	0-10	potassium voltage-gated channel subfamily H member 2	Homo sapiens	88-92
23672049-11	2013	Berberine shows inhibitory effect on protein expressions of in vitro HERG-HEK cells and Ikr channel in rat ventricular tissues.	Berberine	0-9	potassium voltage-gated channel subfamily H member 2	Homo sapiens	69-73
23672049-12	2013	Liensinine improves protein expression of HERG channe in HERG-HEK cells.	liensinine	0-10	potassium voltage-gated channel subfamily H member 2	Homo sapiens	42-46
22989185-1	2012	The human ether-a-go-go related gene 1 (hERG1) K ion channel is a key element for the rapid component of the delayed rectified potassium current in cardiac myocytes.	Potassium	127-136	potassium voltage-gated channel subfamily H member 2	Homo sapiens	40-45
22974355-0	2012	Effect of daurisoline on HERG channel electrophysiological function and protein expression.	daurisoline	10-21	potassium voltage-gated channel subfamily H member 2	Homo sapiens	25-29
22889737-10	2012	The HERG blocker E-4031 decreased migration.	E 4031	17-23	potassium voltage-gated channel subfamily H member 2	Homo sapiens	4-8
22856456-9	2012	Collectively, these data suggest that the AZAs physically block the K(+) conductance pathway of hERG1 channels by occluding the cytoplasmic mouth of the open pore.	Azaserine	42-46	potassium voltage-gated channel subfamily H member 2	Homo sapiens	96-101
22853924-8	2012	Finally, in vivo administration of LY364947, a pharmacological antagonist of TGF-beta signalling, dramatically prevented interstitial fibrosis and LQTS and abolished aberrant expression of TGF-beta1, HERG, and Kir2.1 in ATO-treated guinea pigs.	Ly-364947	35-43	potassium voltage-gated channel subfamily H member 2	Homo sapiens	200-204
23054723-0	2012	Blockade of human HERG K+ channels by rosiglitazone, an antidiabetic drug.	Rosiglitazone	38-51	potassium voltage-gated channel subfamily H member 2	Homo sapiens	18-22
23054723-1	2012	This study examined the effect of rosiglitazone, an oral antidiabetic drug, on human ether-a-gogo-related gene (HERG) channels expressed in human embryonic kidney (HEK293) cells.	Rosiglitazone	34-47	potassium voltage-gated channel subfamily H member 2	Homo sapiens	112-116
23054723-3	2012	Rosiglitazone inhibited HERG channels in a concentration-dependent manner, with an IC50 value of 18.8 muM and a Hill coefficient of 1.0.	Rosiglitazone	0-13	potassium voltage-gated channel subfamily H member 2	Homo sapiens	24-28
23054723-5	2012	The rosiglitazone-induced inhibition of HERG channels was voltagedependent, with a steep increase in inhibition over the voltage range of channel opening.	Rosiglitazone	4-17	potassium voltage-gated channel subfamily H member 2	Homo sapiens	40-44
23054723-8	2012	The present study suggests that rosiglitazone blocks HERG channels by binding to activated and inactivated channels, and rosiglitazone use should thus be carefully monitored in patients with pre-existing QT prolongation.	Rosiglitazone	32-45	potassium voltage-gated channel subfamily H member 2	Homo sapiens	53-57
22161019-0	2012	Imatinib has the potential to exert its antileukemia effects by down-regulating hERG1 K+ channels in chronic myelogenous leukemia.	Imatinib Mesylate	0-8	potassium voltage-gated channel subfamily H member 2	Homo sapiens	80-85
22161019-4	2012	The present study explored a possible regulatory effect of imatinib upon hERG1 K(+) channels as a means to uncover new molecular events involved in the antileukemic activity of this PTK inhibitor in CML.	Imatinib Mesylate	59-67	potassium voltage-gated channel subfamily H member 2	Homo sapiens	73-78
22161019-5	2012	The results demonstrated that hERG1 was highly detected in K562 cells and primary CML cells, and down-regulated by imatinib at mRNA and protein levels.	Imatinib Mesylate	115-123	potassium voltage-gated channel subfamily H member 2	Homo sapiens	30-35
22161019-7	2012	Moreover, these antileukemia effects of imatinib were potentiated by E-4031, a specific hERG1 inhibitor.	Imatinib Mesylate	40-48	potassium voltage-gated channel subfamily H member 2	Homo sapiens	88-93
22161019-7	2012	Moreover, these antileukemia effects of imatinib were potentiated by E-4031, a specific hERG1 inhibitor.	E 4031	69-75	potassium voltage-gated channel subfamily H member 2	Homo sapiens	88-93
22161019-8	2012	Together, these results provide evidence of a novel potential molecular mechanism of antileukemic activities by imatinib which, independent of targeting tyrosine kinase, highlight hERG1 K(+) channels as a therapeutic target for CML treatment.	Imatinib Mesylate	112-120	potassium voltage-gated channel subfamily H member 2	Homo sapiens	180-185
22522181-0	2012	HERG potassium channel regulation by the N-terminal eag domain.	Methyl 2-acetamido-2-deoxy-beta-D-glucopyranoside	52-55	potassium voltage-gated channel subfamily H member 2	Homo sapiens	0-4
22573844-4	2012	In silico docking of the activator 1,3-bis-(2-hydroxy-5-trifluoromethylphenyl)-urea (NS1643) to an S1-S6 transmembrane homology model of hERG1 predicted putative binding sites.	1,3-bis(2-hydroxy-5-trifluoromethylphenyl)urea	35-83	potassium voltage-gated channel subfamily H member 2	Homo sapiens	137-142
22573844-11	2012	The inward conductance elicited by hyperpolarization of D540K hERG1 was abrogated by NS1643 treatment, suggesting that it alters the inward movement of the S4 segment.	1,3-bis(2-hydroxy-5-trifluoromethylphenyl)urea	85-91	potassium voltage-gated channel subfamily H member 2	Homo sapiens	62-67
22292854-10	2012	Importantly, hERG1 K(+) channel inhibitor E-4031 impaired these effects.	E 4031	42-48	potassium voltage-gated channel subfamily H member 2	Homo sapiens	13-18
22100990-0	2012	Transfection by eukaryotic expression vector pcDNA3-HERG inhibits the cultured neonatal rabbit ventricular myocyte hypertrophy induced by phenylephrine.	Phenylephrine	138-151	potassium voltage-gated channel subfamily H member 2	Homo sapiens	52-56
22100990-9	2012	HERG overexpression could accelerate repolarization and shorten APD at 90% repolarization prolonged by phenylephrine and partially inhibit myocyte hypertrophy and calcineurin activation.	Phenylephrine	103-116	potassium voltage-gated channel subfamily H member 2	Homo sapiens	0-4
22100990-11	2012	HERG overexpression could enhance the repolarization and inhibit the calcineurin activation and myocyte hypertrophy induced by phenylephrine.	Phenylephrine	127-140	potassium voltage-gated channel subfamily H member 2	Homo sapiens	0-4
22465688-0	2012	Iloperidone (Fanapt ), a novel atypical antipsychotic, is a potent HERG blocker and delays cardiac ventricular repolarization at clinically relevant concentration.	iloperidone	0-11	potassium voltage-gated channel subfamily H member 2	Homo sapiens	67-71
22460808-3	2012	HERG1 protein expression was evaluated by immunohistochemistry in paraffin-embedded tissue specimens from 133 patients with laryngeal/hypopharyngeal squamous cell carcinomas and 75 patients with laryngeal dysplasia, and correlated with clinical data.	Paraffin	66-74	potassium voltage-gated channel subfamily H member 2	Homo sapiens	0-5
22465688-0	2012	Iloperidone (Fanapt ), a novel atypical antipsychotic, is a potent HERG blocker and delays cardiac ventricular repolarization at clinically relevant concentration.	iloperidone	13-19	potassium voltage-gated channel subfamily H member 2	Homo sapiens	67-71
22465688-3	2012	(1) In vitro level: whole-cell patch-clamp experiments were performed on HERG-transfected HEK293 cells exposed to iloperidone 0.01-1 mumol/L (n = 35 cells, total) to assess drug effect on HERG current.	iloperidone	114-125	potassium voltage-gated channel subfamily H member 2	Homo sapiens	73-77
22465688-10	2012	Iloperidone prolongs the QT interval, the cardiac action potentials and is a potent HERG blocker.	iloperidone	0-11	potassium voltage-gated channel subfamily H member 2	Homo sapiens	84-88
22609834-1	2012	AIM: To compare the effects of two stereoisomeric forms of glycyrrhetinic acid on different components of Na(+) current, HERG and Kv1.5 channel currents.	Glycyrrhetinic Acid	59-78	potassium voltage-gated channel subfamily H member 2	Homo sapiens	121-125
22052944-8	2012	Additionally, LQT2-derived cardiac cells were more sensitive than controls to potentially arrhythmogenic drugs, including sotalol, and demonstrated arrhythmogenic electrical activity.	Sotalol	122-129	potassium voltage-gated channel subfamily H member 2	Homo sapiens	14-18
21920426-0	2012	Inhibitory effects of a bisbenzylisoquinline alkaloid dauricine on HERG potassium channels.	bisbenzylisoquinline alkaloid	24-53	potassium voltage-gated channel subfamily H member 2	Homo sapiens	67-71
21920426-0	2012	Inhibitory effects of a bisbenzylisoquinline alkaloid dauricine on HERG potassium channels.	dauricine	54-63	potassium voltage-gated channel subfamily H member 2	Homo sapiens	67-71
21920426-5	2012	AIM OF THE STUDY: The effects of Dau on HERG channels were investigated.	dauricine	33-36	potassium voltage-gated channel subfamily H member 2	Homo sapiens	40-44
21920426-10	2012	Dau inhibited I(HERG) in the open and inactivated states, but not in the closed states.	dauricine	0-3	potassium voltage-gated channel subfamily H member 2	Homo sapiens	16-20
21920426-12	2012	CONCLUSIONS: Dau inhibits HERG encoded potassium channels and this action might be a molecular mechanism for the previously reported APD prolongation with this drug.	dauricine	13-16	potassium voltage-gated channel subfamily H member 2	Homo sapiens	26-30
22392372-2	2012	Each amino acid residue in the first half of the HERG peptide incorporated deuterons with a higher rate than those in the second half of the peptide, consistent with the nuclear magnetic resonance structure of this peptide, with amino acids 1-10 being a flexible coil, whereas amino acids 11-24 are a stable amphipathic helix.	Deuterium	75-84	potassium voltage-gated channel subfamily H member 2	Homo sapiens	49-53
22381725-4	2012	Many explorations have helped in understanding the physiopathology by showing that opioids, including methadone, cause a blockage of the potassium channels of the gene HERG K+P.	Methadone	102-111	potassium voltage-gated channel subfamily H member 2	Homo sapiens	168-172
22183728-8	2012	These different effects of ISO on LQT1 and LQT2 were verified by optical mapping of the whole heart, suggesting that ISO-induced EADs are genotype specific.	Isoproterenol	27-30	potassium voltage-gated channel subfamily H member 2	Homo sapiens	43-47
22183728-8	2012	These different effects of ISO on LQT1 and LQT2 were verified by optical mapping of the whole heart, suggesting that ISO-induced EADs are genotype specific.	Isoproterenol	117-120	potassium voltage-gated channel subfamily H member 2	Homo sapiens	43-47
22075718-6	2012	Inhibition of HERG currents by acute or sustained application of E-4031, a specific ERG channel blocker, depolarized SW2 cells by 10-15 mV.	E 4031	65-71	potassium voltage-gated channel subfamily H member 2	Homo sapiens	14-18
22075718-8	2012	Blockage of HERG channels by E-4031 for up to 72 h did not affect cell proliferation.	E 4031	29-35	potassium voltage-gated channel subfamily H member 2	Homo sapiens	12-16
21934630-3	2012	The purpose of the present study was to investigate the effects of GFA and GFG on the HERG channel and its structure-function relationship.	guanfu base G	75-78	potassium voltage-gated channel subfamily H member 2	Homo sapiens	86-90
21934630-5	2012	RESULTS: GFA and GFG inhibited HERG channel current in concentration-, voltage-, and time-dependent manners.	guanfu base G	17-20	potassium voltage-gated channel subfamily H member 2	Homo sapiens	31-35
21934630-9	2012	CONCLUSIONS: Both GFA and GFG blocked HERG channel current.	guanfu base G	26-29	potassium voltage-gated channel subfamily H member 2	Homo sapiens	38-42
21951015-9	2012	Lastly, we examined a potential role for hypokalemia as a contributory factor to the patient"s lethal arrhythmia by possible low-potassium-induced degradation of WT HERG and haplo-insufficiency of G816V HERG.	Potassium	129-138	potassium voltage-gated channel subfamily H member 2	Homo sapiens	165-169
21951015-9	2012	Lastly, we examined a potential role for hypokalemia as a contributory factor to the patient"s lethal arrhythmia by possible low-potassium-induced degradation of WT HERG and haplo-insufficiency of G816V HERG.	Potassium	129-138	potassium voltage-gated channel subfamily H member 2	Homo sapiens	203-207
22396785-0	2012	Changes in channel trafficking and protein stability caused by LQT2 mutations in the PAS domain of the HERG channel.	Aminosalicylic Acid	85-88	potassium voltage-gated channel subfamily H member 2	Homo sapiens	63-67
22396785-0	2012	Changes in channel trafficking and protein stability caused by LQT2 mutations in the PAS domain of the HERG channel.	Aminosalicylic Acid	85-88	potassium voltage-gated channel subfamily H member 2	Homo sapiens	103-107
22396785-2	2012	Several LQT2-associated mutations have been mapped to the amino terminal cytoplasmic Per-Arnt-Sim (PAS) domain of the HERG1a channel subunit.	Aminosalicylic Acid	99-102	potassium voltage-gated channel subfamily H member 2	Homo sapiens	8-12
22396785-2	2012	Several LQT2-associated mutations have been mapped to the amino terminal cytoplasmic Per-Arnt-Sim (PAS) domain of the HERG1a channel subunit.	Aminosalicylic Acid	99-102	potassium voltage-gated channel subfamily H member 2	Homo sapiens	118-123
22124116-3	2011	Isolated, PAS-containing hERG1a N-terminal regions (NTRs) directly regulate NTR-deleted hERG1a channels; however, it is unclear whether hERG1b isoforms contain sufficient machinery to support regulation by hERG1a NTRs.	Aminosalicylic Acid	10-13	potassium voltage-gated channel subfamily H member 2	Homo sapiens	25-30
22020779-2	2012	The aim of             this study was to investigate the role of HERG in cisplatin-induced apoptosis             in gastric cancer in vitro and in vivo.	Cisplatin	73-82	potassium voltage-gated channel subfamily H member 2	Homo sapiens	65-69
22020779-7	2012	Our results show that cisplatin increased the expression of             HERG in gastric cancer cells.	Cisplatin	22-31	potassium voltage-gated channel subfamily H member 2	Homo sapiens	72-76
22020779-8	2012	Silencing HERG inhibited the apoptosis induced by             cisplatin both in vitro and in vivo, by attenuating the cisplatin effects on Bcl-2,             Bax and active caspase-3.	Cisplatin	62-71	potassium voltage-gated channel subfamily H member 2	Homo sapiens	10-14
22020779-8	2012	Silencing HERG inhibited the apoptosis induced by             cisplatin both in vitro and in vivo, by attenuating the cisplatin effects on Bcl-2,             Bax and active caspase-3.	Cisplatin	118-127	potassium voltage-gated channel subfamily H member 2	Homo sapiens	10-14
22020779-9	2012	The role of HERG in modulation of cisplatin-induced             apoptosis suggests that HERG may provide a new potential target for cisplatin             chemotherapy in human gastric cancer.	Cisplatin	34-43	potassium voltage-gated channel subfamily H member 2	Homo sapiens	12-16
22020779-9	2012	The role of HERG in modulation of cisplatin-induced             apoptosis suggests that HERG may provide a new potential target for cisplatin             chemotherapy in human gastric cancer.	Cisplatin	34-43	potassium voltage-gated channel subfamily H member 2	Homo sapiens	88-92
22020779-9	2012	The role of HERG in modulation of cisplatin-induced             apoptosis suggests that HERG may provide a new potential target for cisplatin             chemotherapy in human gastric cancer.	Cisplatin	132-141	potassium voltage-gated channel subfamily H member 2	Homo sapiens	12-16
22020779-9	2012	The role of HERG in modulation of cisplatin-induced             apoptosis suggests that HERG may provide a new potential target for cisplatin             chemotherapy in human gastric cancer.	Cisplatin	132-141	potassium voltage-gated channel subfamily H member 2	Homo sapiens	88-92
22124116-3	2011	Isolated, PAS-containing hERG1a N-terminal regions (NTRs) directly regulate NTR-deleted hERG1a channels; however, it is unclear whether hERG1b isoforms contain sufficient machinery to support regulation by hERG1a NTRs.	Aminosalicylic Acid	10-13	potassium voltage-gated channel subfamily H member 2	Homo sapiens	88-93
22124116-3	2011	Isolated, PAS-containing hERG1a N-terminal regions (NTRs) directly regulate NTR-deleted hERG1a channels; however, it is unclear whether hERG1b isoforms contain sufficient machinery to support regulation by hERG1a NTRs.	Aminosalicylic Acid	10-13	potassium voltage-gated channel subfamily H member 2	Homo sapiens	88-93
22124116-10	2011	Our results demonstrate that deactivation is faster in hERG1a/hERG1b channels compared to hERG1a channels because of fewer PAS domains, not because of an inhibitory effect of the unique hERG1b NTR.	Aminosalicylic Acid	123-126	potassium voltage-gated channel subfamily H member 2	Homo sapiens	55-60
22124116-10	2011	Our results demonstrate that deactivation is faster in hERG1a/hERG1b channels compared to hERG1a channels because of fewer PAS domains, not because of an inhibitory effect of the unique hERG1b NTR.	Aminosalicylic Acid	123-126	potassium voltage-gated channel subfamily H member 2	Homo sapiens	62-67
21839071-6	2011	Characteristics of blockage on hHCN channels were consistent with those of amiodarone as "trapped" drugs on human ether-a-go-go-related gene (HERG) channels.	Amiodarone	75-85	potassium voltage-gated channel subfamily H member 2	Homo sapiens	142-146
22003215-10	2011	Similarly, the incidence of AP prolongations in the presence of 3 mumol/L bupivacaine was significantly increased from 6% in control myocytes to 24% in LQT1-like but not in LQT2-like myocytes.	Bupivacaine	74-85	potassium voltage-gated channel subfamily H member 2	Homo sapiens	173-177
21856740-1	2011	Two different mechanisms leading to increased current have been described for the small-molecule human ether-a-go-go-related gene (herg) activator NS1643 [1,3-bis-(2-hydroxy-5-trifluoromethylphenyl)-urea].	1,3-bis(2-hydroxy-5-trifluoromethylphenyl)urea	147-153	potassium voltage-gated channel subfamily H member 2	Homo sapiens	131-135
22396785-3	2012	Here we have characterized the trafficking properties of some LQT2-associated PAS domain mutants and analyzed rescue of the trafficking mutants by low temperature (27 C) or by the pore blocker drug E4031.	Aminosalicylic Acid	78-81	potassium voltage-gated channel subfamily H member 2	Homo sapiens	62-66
22396785-4	2012	We show that the LQT2-associated mutations in the PAS domain of the HERG channel display molecular properties that are distinct from the properties of LQT2-associated mutations in the trans-membrane region.	Aminosalicylic Acid	50-53	potassium voltage-gated channel subfamily H member 2	Homo sapiens	17-21
22396785-4	2012	We show that the LQT2-associated mutations in the PAS domain of the HERG channel display molecular properties that are distinct from the properties of LQT2-associated mutations in the trans-membrane region.	Aminosalicylic Acid	50-53	potassium voltage-gated channel subfamily H member 2	Homo sapiens	68-72
22396785-5	2012	Unlike the latter, many of the tested PAS domain LQT2-associated mutations do not result in trafficking deficiency of the channel.	Aminosalicylic Acid	38-41	potassium voltage-gated channel subfamily H member 2	Homo sapiens	49-53
21856740-1	2011	Two different mechanisms leading to increased current have been described for the small-molecule human ether-a-go-go-related gene (herg) activator NS1643 [1,3-bis-(2-hydroxy-5-trifluoromethylphenyl)-urea].	1,3-bis(2-hydroxy-5-trifluoromethylphenyl)urea	155-203	potassium voltage-gated channel subfamily H member 2	Homo sapiens	131-135
22260022-0	2011	[Lidamycin inhibits the proliferation of HERG K+ channel highly expressing cancer cells and shows synergy with anticancer drugs].	C 1027	1-10	potassium voltage-gated channel subfamily H member 2	Homo sapiens	41-45
22260022-1	2011	This study is to investigate inhibitory effects of lidamycin (LDM) on the proliferation of HERG K+ channel highly expressing cancer cells and its synergy with anticancer drugs.	C 1027	51-60	potassium voltage-gated channel subfamily H member 2	Homo sapiens	91-95
22260022-2	2011	MTT assay was used to examine the inhibitory effects of lidamycin combined with various anticancer drugs on the proliferation of human lung cancer A549 cells, human colon cancer HT-29 cells and herg-stably-transfected A549 cells.	monooxyethylene trimethylolpropane tristearate	0-3	potassium voltage-gated channel subfamily H member 2	Homo sapiens	194-198
22260022-2	2011	MTT assay was used to examine the inhibitory effects of lidamycin combined with various anticancer drugs on the proliferation of human lung cancer A549 cells, human colon cancer HT-29 cells and herg-stably-transfected A549 cells.	C 1027	56-65	potassium voltage-gated channel subfamily H member 2	Homo sapiens	194-198
22260022-6	2011	The efficacy in HT-29 cells with high HERG potassium expression level is less potent than that in A549 cells with low expression level.	Potassium	43-52	potassium voltage-gated channel subfamily H member 2	Homo sapiens	38-42
22260022-13	2011	HERG expression level negatively correlated with inhibitory effect on the proliferation of cancer cells by DOX.	Doxorubicin	107-110	potassium voltage-gated channel subfamily H member 2	Homo sapiens	0-4
21798421-7	2011	The average QTc was 314 +- 23 ms. A mutation in genes related to SQTS was found in 23% of the probands; most of them had a gain of function mutation in HERG (SQTS1).	qtc	12-15	potassium voltage-gated channel subfamily H member 2	Homo sapiens	152-156
22128262-1	2011	The effect of cyclosporin A (CsA), an immunosuppressant, on human ether-a-go-go-related gene (HERG) channel as it is expressed in human embryonic kidney cells was studied using a whole-cell, patch-clamp technique.	Cyclosporine	29-32	potassium voltage-gated channel subfamily H member 2	Homo sapiens	94-98
22128262-2	2011	CsA inhibited the HERG channel in a concentration-dependent manner, with an IC(50) value and a Hill coefficient of 3.17 microM and 0.89, respectively.	Cyclosporine	0-3	potassium voltage-gated channel subfamily H member 2	Homo sapiens	18-22
22128262-4	2011	The CsA-induced inhibition of HERG channels was voltage-dependent, with a steep increase over the voltage range of the channel opening.	Cyclosporine	4-7	potassium voltage-gated channel subfamily H member 2	Homo sapiens	30-34
22128262-6	2011	CsA blocked the HERG channels predominantly in the open and inactivated states rather than in the closed state.	Cyclosporine	0-3	potassium voltage-gated channel subfamily H member 2	Homo sapiens	16-20
22128262-7	2011	Results of the present study suggest that CsA acts directly on the HERG channel as an open-channel blocker, and it acts independently of its effect on calcineurin activity.	Cyclosporine	42-45	potassium voltage-gated channel subfamily H member 2	Homo sapiens	67-71
21743002-4	2011	3-Nitro-n-(4-phenoxyphenyl) benzamide [ICA-105574 (ICA)] has been discovered to activate hERG1 by strong attenuation of pore-type inactivation.	3-nitro-N-(4-phenoxyphenyl)benzamide	0-37	potassium voltage-gated channel subfamily H member 2	Homo sapiens	89-94
21743002-4	2011	3-Nitro-n-(4-phenoxyphenyl) benzamide [ICA-105574 (ICA)] has been discovered to activate hERG1 by strong attenuation of pore-type inactivation.	3-nitro-N-(4-phenoxyphenyl)benzamide	39-49	potassium voltage-gated channel subfamily H member 2	Homo sapiens	89-94
21743002-4	2011	3-Nitro-n-(4-phenoxyphenyl) benzamide [ICA-105574 (ICA)] has been discovered to activate hERG1 by strong attenuation of pore-type inactivation.	isocyanic acid	39-42	potassium voltage-gated channel subfamily H member 2	Homo sapiens	89-94
21743002-5	2011	Here, we used scanning mutagenesis of hERG1 to identify the molecular determinants of ICA action.	isocyanic acid	86-89	potassium voltage-gated channel subfamily H member 2	Homo sapiens	38-43
21743002-8	2011	This was confirmed by showing that the noninactivating mutant hERG1 channel (G628C/S631C) was inhibited by ICA and that the addition of the F557L mutation rendered the channel drug-insensitive.	isocyanic acid	107-110	potassium voltage-gated channel subfamily H member 2	Homo sapiens	62-67
21743002-9	2011	Simulated molecular docking of ICA to homology models of hERG1 corroborated the scanning mutagenesis findings.	isocyanic acid	31-34	potassium voltage-gated channel subfamily H member 2	Homo sapiens	57-62
21743002-10	2011	Together, our findings indicate that ICA is a mixed agonist of hERG1 channels.	isocyanic acid	37-40	potassium voltage-gated channel subfamily H member 2	Homo sapiens	63-68
21449979-8	2011	In contrast, E-4031 was a more potent blocker of hERG 1a compared with 1a/1b channels, as previously reported, as was dofetilide, another high-affinity blocker.	E 4031	13-19	potassium voltage-gated channel subfamily H member 2	Homo sapiens	49-55
20547773-6	2011	The results showed that drugs in group 1 induced greater inhibition of human ether-a-go-go-related gene (HERG) potassium current or the rapid component of the delayed rectifier potassium current (I(kr)), had lower half-maximal inhibitory concentration (IC50) values for inhibition of HERG/I(kr), and induced greater QTc increases in humans.	qtc	316-319	potassium voltage-gated channel subfamily H member 2	Homo sapiens	105-109
21490315-5	2011	We found that treating cells in nocodazole, a microtubule depolymerizing agent, altered the subcellular localization, functional expression, and glycosylation of the LQT2 mutation G601S-hERG differently from wild-type hERG (WT-hERG).	Nocodazole	32-42	potassium voltage-gated channel subfamily H member 2	Homo sapiens	166-170
21497594-10	2011	Thus, we conclude that CVB-D inhibits HERG encoded potassium channels and this action might be a molecular mechanism for the previously reported APD prolongation and QT interval prolongation with this drug.	PVB protocol	23-26	potassium voltage-gated channel subfamily H member 2	Homo sapiens	38-42
21525004-0	2011	Progesterone impairs human ether-a-go-go-related gene (HERG) trafficking by disruption of intracellular cholesterol homeostasis.	Cholesterol	104-115	potassium voltage-gated channel subfamily H member 2	Homo sapiens	55-59
21525004-1	2011	The prolongation of QT intervals in both mothers and fetuses during the later period of pregnancy implies that higher levels of progesterone may regulate the function of the human ether-a-go-go-related gene (HERG) potassium channel, a key ion channel responsible for controlling the length of QT intervals.	Progesterone	128-140	potassium voltage-gated channel subfamily H member 2	Homo sapiens	208-212
21525004-3	2011	Treatment with progesterone for 24 h decreased the abundance of the fully glycosylated form of the HERG channel in rat neonatal cardiac myocytes and HERG-HEK293 cells, a cell line stably expressing HERG channels.	Progesterone	15-27	potassium voltage-gated channel subfamily H member 2	Homo sapiens	99-103
21525004-3	2011	Treatment with progesterone for 24 h decreased the abundance of the fully glycosylated form of the HERG channel in rat neonatal cardiac myocytes and HERG-HEK293 cells, a cell line stably expressing HERG channels.	Progesterone	15-27	potassium voltage-gated channel subfamily H member 2	Homo sapiens	149-153
21525004-3	2011	Treatment with progesterone for 24 h decreased the abundance of the fully glycosylated form of the HERG channel in rat neonatal cardiac myocytes and HERG-HEK293 cells, a cell line stably expressing HERG channels.	Progesterone	15-27	potassium voltage-gated channel subfamily H member 2	Homo sapiens	149-153
21525004-4	2011	Progesterone also concentration-dependently decreased HERG current density, but had no effect on voltage-gated L-type Ca(2+) and K(+) channels.	Progesterone	0-12	potassium voltage-gated channel subfamily H member 2	Homo sapiens	54-58
21525004-5	2011	Immunofluorescence microscopy and Western blot analysis show that progesterone preferentially decreased HERG channel protein abundance in the plasma membrane, induced protein accumulation in the dilated endoplasmic reticulum (ER), and increased the protein expression of C/EBP homologous protein, a hallmark of ER stress.	Progesterone	66-78	potassium voltage-gated channel subfamily H member 2	Homo sapiens	104-108
21525004-6	2011	Application of 2-hydroxypropyl-beta-cyclodextrin (a sterol-binding agent) or overexpression of Rab9 rescued the progesterone-induced HERG trafficking defect and ER stress.	2-Hydroxypropyl-beta-cyclodextrin	15-48	potassium voltage-gated channel subfamily H member 2	Homo sapiens	133-137
21525004-6	2011	Application of 2-hydroxypropyl-beta-cyclodextrin (a sterol-binding agent) or overexpression of Rab9 rescued the progesterone-induced HERG trafficking defect and ER stress.	Sterols	52-58	potassium voltage-gated channel subfamily H member 2	Homo sapiens	133-137
21525004-6	2011	Application of 2-hydroxypropyl-beta-cyclodextrin (a sterol-binding agent) or overexpression of Rab9 rescued the progesterone-induced HERG trafficking defect and ER stress.	Progesterone	112-124	potassium voltage-gated channel subfamily H member 2	Homo sapiens	133-137
21525004-7	2011	Disruption of intracellular cholesterol homeostasis with simvastatin, imipramine, or exogenous application of cholesterol mimicked the effect of progesterone on HERG channel trafficking.	Cholesterol	28-39	potassium voltage-gated channel subfamily H member 2	Homo sapiens	161-165
21525004-7	2011	Disruption of intracellular cholesterol homeostasis with simvastatin, imipramine, or exogenous application of cholesterol mimicked the effect of progesterone on HERG channel trafficking.	Cholesterol	110-121	potassium voltage-gated channel subfamily H member 2	Homo sapiens	161-165
21525004-7	2011	Disruption of intracellular cholesterol homeostasis with simvastatin, imipramine, or exogenous application of cholesterol mimicked the effect of progesterone on HERG channel trafficking.	Progesterone	145-157	potassium voltage-gated channel subfamily H member 2	Homo sapiens	161-165
21536673-3	2011	Only a small percentage of hERG channels containing PAS domain LQT2 mutations (hERG PAS-LQT2) have been characterized in mammalian cells, so the functional effect of these mutations is unclear.	Aminosalicylic Acid	52-55	potassium voltage-gated channel subfamily H member 2	Homo sapiens	63-67
21536673-3	2011	Only a small percentage of hERG channels containing PAS domain LQT2 mutations (hERG PAS-LQT2) have been characterized in mammalian cells, so the functional effect of these mutations is unclear.	Aminosalicylic Acid	52-55	potassium voltage-gated channel subfamily H member 2	Homo sapiens	88-92
21536673-11	2011	Thus, our results reveal a putative "gating face" in the PAS domain where mutations within this region form functional channels with altered gating properties, and we show that NPAS is a general means for rescuing aberrant gating in hERG LQT2 mutant channels and may be a potential biological therapeutic.	Aminosalicylic Acid	57-60	potassium voltage-gated channel subfamily H member 2	Homo sapiens	238-242
21536683-8	2011	Rerouting this inhibitor to the outer mitochondrial membrane diminishes its ability to block cAMP-dependent HERG induction.	Cyclic AMP	93-97	potassium voltage-gated channel subfamily H member 2	Homo sapiens	108-112
21776218-7	2011	Expression of the ion-channel genes CACNA1, KCNH2, KCNQ1 and KCNE1 were down-regulated by 1-muM arsenic.	Arsenic	96-103	potassium voltage-gated channel subfamily H member 2	Homo sapiens	44-49
21394035-7	2011	RESULTS: (1) The estimated concentration at which 50% of the maximal inhibitory effect is observed (IC(50)) for paliperidone on HERG current was 0.5276 mumol/L.	Paliperidone Palmitate	112-124	potassium voltage-gated channel subfamily H member 2	Homo sapiens	128-132
21394035-11	2011	CONCLUSIONS: Paliperidone prolongs the QT interval by blocking HERG current at clinically relevant concentrations and is potentially unsafe.	Paliperidone Palmitate	13-25	potassium voltage-gated channel subfamily H member 2	Homo sapiens	63-67
23717061-0	2011	Differential effects of ginsenoside metabolites on HERG k channel currents.	Ginsenosides	24-35	potassium voltage-gated channel subfamily H member 2	Homo sapiens	51-55
23717061-3	2011	In a previous report we demonstrated that ginsenoside Rg3 regulates HERG K(+) channels by decelerating deactivation.	Ginsenosides	42-53	potassium voltage-gated channel subfamily H member 2	Homo sapiens	68-72
23717061-4	2011	However, little is known about how ginsenoside metabolites regulate HERG K(+) channel activity.	Ginsenosides	35-46	potassium voltage-gated channel subfamily H member 2	Homo sapiens	68-72
23717061-5	2011	In the present study, we examined the effects of ginsenoside metabolites such as compound K (CK), protopanaxadiol (PPD), and protopanaxatriol (PPT) on HERG K(+) channel activity by expressing human alpha subunits in Xenopus oocytes.	Ginsenosides	49-60	potassium voltage-gated channel subfamily H member 2	Homo sapiens	151-155
23717061-5	2011	In the present study, we examined the effects of ginsenoside metabolites such as compound K (CK), protopanaxadiol (PPD), and protopanaxatriol (PPT) on HERG K(+) channel activity by expressing human alpha subunits in Xenopus oocytes.	protopanaxadiol	98-113	potassium voltage-gated channel subfamily H member 2	Homo sapiens	151-155
23717061-5	2011	In the present study, we examined the effects of ginsenoside metabolites such as compound K (CK), protopanaxadiol (PPD), and protopanaxatriol (PPT) on HERG K(+) channel activity by expressing human alpha subunits in Xenopus oocytes.	protopanaxatriol	125-141	potassium voltage-gated channel subfamily H member 2	Homo sapiens	151-155
23717061-5	2011	In the present study, we examined the effects of ginsenoside metabolites such as compound K (CK), protopanaxadiol (PPD), and protopanaxatriol (PPT) on HERG K(+) channel activity by expressing human alpha subunits in Xenopus oocytes.	protopanaxatriol	143-146	potassium voltage-gated channel subfamily H member 2	Homo sapiens	151-155
23717061-10	2011	These results indicate that ginsenoside metabolites exhibit differential regulation on Ideactivating-tail of HERG K(+) channel.	Ginsenosides	28-39	potassium voltage-gated channel subfamily H member 2	Homo sapiens	109-113
21175572-0	2011	Trapping and dissociation of propafenone derivatives in HERG channels.	Propafenone	29-40	potassium voltage-gated channel subfamily H member 2	Homo sapiens	56-60
22977528-0	2011	Arsenic trioxide induces the apoptosis of human breast cancer MCF-7 cells through activation of caspase-3 and inhibition of HERG channels.	Arsenic Trioxide	0-16	potassium voltage-gated channel subfamily H member 2	Homo sapiens	124-128
22977528-8	2011	Taken together, the results indicate that arsenic trioxide induces the apoptosis of human breast cancer MCF-7 cells at least in part through the activation of caspase-3 and the decrease in HERG expression.	Arsenic Trioxide	42-58	potassium voltage-gated channel subfamily H member 2	Homo sapiens	189-193
21496174-0	2011	Patient with syncope and LQTS carrying a mutation in the PAS domain of the hERG1 channel.	Protactinium	57-60	potassium voltage-gated channel subfamily H member 2	Homo sapiens	75-80
21496174-6	2011	Identifying mutations in the PAS domain or other domains of the hERG1 channel and understanding their effect may provide more focused and mutation-specific risk assessment in this population.	Protactinium	29-32	potassium voltage-gated channel subfamily H member 2	Homo sapiens	64-69
21175572-3	2011	A small molecule-like propafenone is efficiently trapped in the closed HERG channel conformation.	Propafenone	22-33	potassium voltage-gated channel subfamily H member 2	Homo sapiens	71-75
21175572-12	2011	CONCLUSION AND IMPLICATIONS: The data show that extending the size of a trapped HERG blocker-like propafenone by adding a bulky side chain may impede channel closure and thereby facilitate drug dissociation at rest.	Propafenone	98-109	potassium voltage-gated channel subfamily H member 2	Homo sapiens	80-84
21367833-5	2011	When LQT2-hiPSC cardiomyocytes were exposed to E4031 (an I(Kr) blocker), arrhythmias developed and these presented as early after depolarizations (EADs) in the action potentials.	E 4031	47-52	potassium voltage-gated channel subfamily H member 2	Homo sapiens	5-9
21367833-6	2011	In contrast to control cardiomyocytes, LQT2-hiPSC cardiomyocytes also developed EADs when challenged with the clinically used stressor, isoprenaline.	Isoproterenol	136-148	potassium voltage-gated channel subfamily H member 2	Homo sapiens	39-43
21109023-9	2011	Moreover, the results obtained demonstrate the importance of the glutamic acid at position 637 for the inactivation process and K(+) selectivity of Kv11.1 channels.	Glutamic Acid	65-78	potassium voltage-gated channel subfamily H member 2	Homo sapiens	148-154
21063774-10	2011	Genetic polymorphism in KCNH2 was associated with effectiveness of domperidone (p=0.041).	Domperidone	67-78	potassium voltage-gated channel subfamily H member 2	Homo sapiens	24-29
21278233-3	2011	Although diverse compounds reduce the hERG current (I(hERG)) by blocking the channel, probucol, a cholesterol-lowering drug that causes LQTS, reduces I(hERG) by decreasing plasma-membrane hERG protein expression.	Probucol	86-94	potassium voltage-gated channel subfamily H member 2	Homo sapiens	51-59
21130771-10	2011	Both quinidine and sotalol may be therapeutic options for patients with the T618I HERG mutation.	Quinidine	5-14	potassium voltage-gated channel subfamily H member 2	Homo sapiens	82-86
21130771-10	2011	Both quinidine and sotalol may be therapeutic options for patients with the T618I HERG mutation.	Sotalol	19-26	potassium voltage-gated channel subfamily H member 2	Homo sapiens	82-86
22156660-3	2011	Fluoroquinolones prolong the QT interval by blocking voltage-gated potassium channels, especially the rapid component of the delayed rectifier potassium current I(Kr), expressed by HERG (the human ether-a-go-go-related gene).	Fluoroquinolones	0-16	potassium voltage-gated channel subfamily H member 2	Homo sapiens	181-185
21063774-13	2011	CONCLUSIONS: Genetic characteristics associated with response to domperidone therapy included polymorphisms in the drug transporter gene ABCB1, the potassium channel KCNH2 gene, and alpha1D--adrenoceptor ADRA1D gene.	Domperidone	65-76	potassium voltage-gated channel subfamily H member 2	Homo sapiens	166-171
20876384-0	2011	Molecular determinants of human ether-a-go-go-related gene 1 (hERG1) K+ channel activation by NS1643.	1,3-bis(2-hydroxy-5-trifluoromethylphenyl)urea	94-100	potassium voltage-gated channel subfamily H member 2	Homo sapiens	62-67
20876384-5	2011	We defined previously the mechanism of action of 1,3-bis-(2-hydroxy-5-trifluoromethyl-phenyl)-urea (NS1643), a compound that increases hERG1 currents by shifting the voltage-dependence of inactivation to more positive potentials.	1,3-bis(2-hydroxy-5-trifluoromethylphenyl)urea	49-98	potassium voltage-gated channel subfamily H member 2	Homo sapiens	135-140
20876384-5	2011	We defined previously the mechanism of action of 1,3-bis-(2-hydroxy-5-trifluoromethyl-phenyl)-urea (NS1643), a compound that increases hERG1 currents by shifting the voltage-dependence of inactivation to more positive potentials.	1,3-bis(2-hydroxy-5-trifluoromethylphenyl)urea	100-106	potassium voltage-gated channel subfamily H member 2	Homo sapiens	135-140
20876384-8	2011	Some of these residues form a cluster and, together with molecular modeling, suggest that NS1643 binds to a pocket near the extracellular ends of the S5/S6 segments of two adjacent hERG1 channel subunits.	1,3-bis(2-hydroxy-5-trifluoromethylphenyl)urea	90-96	potassium voltage-gated channel subfamily H member 2	Homo sapiens	181-186
22039467-0	2011	Inhibition of HERG potassium channels by celecoxib and its mechanism.	Celecoxib	41-50	potassium voltage-gated channel subfamily H member 2	Homo sapiens	14-18
21351488-0	2010	[Chinfloxacin hydrochloride inhibits HERG potassium channel at open state].	chinfloxacin hydrochloride	1-27	potassium voltage-gated channel subfamily H member 2	Homo sapiens	37-41
21351488-1	2010	This study is designed to investigate the effects of chinfloxacin hydrochloride (CFX) on the kinetics of HERG K+ channel.	chinfloxacin hydrochloride	53-79	potassium voltage-gated channel subfamily H member 2	Homo sapiens	105-109
21351488-1	2010	This study is designed to investigate the effects of chinfloxacin hydrochloride (CFX) on the kinetics of HERG K+ channel.	Cefoxitin	81-84	potassium voltage-gated channel subfamily H member 2	Homo sapiens	105-109
20693282-6	2010	We identified an intrinsically weak, noncanonical poly(A) signal, AGUAAA, within intron 9 of hERG1 that modulates the expression of hERG1a and hERG1a(USO).	Poly A	50-57	potassium voltage-gated channel subfamily H member 2	Homo sapiens	93-98
21035456-7	2011	The restoration of functional expression by antisense morpholino oligonucleotides was also observed in LQT2 frameshift mutations.	Morpholinos	54-81	potassium voltage-gated channel subfamily H member 2	Homo sapiens	103-107
21035456-8	2011	Our findings suggest that inhibition of NMD by antisense morpholino oligonucleotides may be a potential therapeutic approach for some LQT2 patients carrying nonsense and frameshift mutations.	Morpholinos	57-84	potassium voltage-gated channel subfamily H member 2	Homo sapiens	134-138
20674746-3	2010	The present study investigated whether raloxifene could affect the cloned hERG channel (I(hERG)) and recombinant human cardiac KCNQ1/KCNE1 channel (I(Ks)) stably expressed in HEK 293 cells using a patch-clamp technique.	Raloxifene Hydrochloride	39-49	potassium voltage-gated channel subfamily H member 2	Homo sapiens	87-95
20693282-8	2010	In contrast, eliminating the intron 9 poly(A) signal or increasing the strength of 5" splice site led to the predominant production of hERG1a and a significant increase in hERG1 current.	Poly A	38-45	potassium voltage-gated channel subfamily H member 2	Homo sapiens	135-140
20601449-5	2010	LQT1-like behavior was pharmacologically induced by chromanol 293B (10 micromol/L) and LQT2-like states by E4031 (10 micromol/L).	E 4031	107-112	potassium voltage-gated channel subfamily H member 2	Homo sapiens	87-91
20535583-1	2010	OBJECTIVE: To observe the effect of matrine on human ether a go-go related gene (HERG) potassium channels expressed in Chinese hamster ovary (CHO) cells and investigate whether HERG channel is a new target of the pharmacological effect of matrine on arrhythmia and tumor METHODS: HERG channel potassium current in CHO cell was recorded using whole-cell patch-clamp technique, and the influence of matrine on the current was explored.	matrine	36-43	potassium voltage-gated channel subfamily H member 2	Homo sapiens	81-85
20535583-2	2010	RESULTS: Matrine inhibited HERG potassium current in a dose-dependent manner, and the 50% inhibitory concentration (IC IC(50)) was 411+-23 mumol/L.	Potassium	32-41	potassium voltage-gated channel subfamily H member 2	Homo sapiens	27-31
20535583-3	2010	Matrine had no significant effect on the activation kinetics, and mainly blocked HERG channels in their closed state.	matrine	0-7	potassium voltage-gated channel subfamily H member 2	Homo sapiens	81-85
21165329-0	2010	Response of i(kr) and HERG currents to the antipsychotics tiapride and sulpiride.	Tiapride Hydrochloride	58-66	potassium voltage-gated channel subfamily H member 2	Homo sapiens	22-26
21165329-0	2010	Response of i(kr) and HERG currents to the antipsychotics tiapride and sulpiride.	Sulpiride	71-80	potassium voltage-gated channel subfamily H member 2	Homo sapiens	22-26
21165329-4	2010	However, our findings did show that tiapride increased the potential for half-maximal activation (V(1/2)) of HERG at 10~300 microM, whereas sulpiride increased the maximum conductance (G(max)) at 3, 10 and 100 microM.	Tiapride Hydrochloride	36-44	potassium voltage-gated channel subfamily H member 2	Homo sapiens	109-113
20734202-1	2010	The goal of the present study was to examine the effects of lobeline, an agonist at nicotinic receptors, on cloned Kv channels, Kv1.5, Kv3.1, Kv4.3, and human ether-a-gogo-related gene (HERG), which are stably expressed in Chinese hamster ovary (CHO) or human embryonic kidney 293 (HEK293) cells.	Lobeline	60-68	potassium voltage-gated channel subfamily H member 2	Homo sapiens	186-190
20734202-10	2010	Lobeline also inhibited Kv3.1, Kv4.3, and HERG in a concentration-dependent manner, with IC(50) values of 21.7, 28.2, and 0.34 muM, respectively.	Lobeline	0-8	potassium voltage-gated channel subfamily H member 2	Homo sapiens	42-46
20601449-9	2010	In LQT1-like myocytes, droperidol (0.6 micromol/L) further prolonged action potentials by 31% + or - 6% (n = 6) but shortened action potentials of LQT2-like myocytes by 11% + or - 2% (n = 8).	Droperidol	23-33	potassium voltage-gated channel subfamily H member 2	Homo sapiens	147-151
20394569-5	2010	In vitro studies demonstrated cardiac electrophysiological effects of domperidone on the rapid component of the cardiac delayed rectifier K(+) current (I(Kr)) through the blockade of channels encoded by the Human Ether-a-go-go Related Gene (HERG).	Domperidone	70-81	potassium voltage-gated channel subfamily H member 2	Homo sapiens	241-245
20547678-0	2010	Cysteine 723 in the C-linker segment confers oxidative inhibition of hERG1 potassium channels.	Cysteine	0-8	potassium voltage-gated channel subfamily H member 2	Homo sapiens	69-74
20547678-3	2010	To investigate the molecular mechanisms of hERG1 channel alteration by ROS, hERG1 and mutants thereof were expressed in HEK293 cells and studied with the whole-cell patch-clamp method.	Reactive Oxygen Species	71-74	potassium voltage-gated channel subfamily H member 2	Homo sapiens	43-48
20662825-0	2010	The action of a novel fluoroquinolone antibiotic agent antofloxacin hydrochloride on human-ether-a-go-go-related gene potassium channel.	Fluoroquinolones	22-37	potassium voltage-gated channel subfamily H member 2	Homo sapiens	85-117
20662825-0	2010	The action of a novel fluoroquinolone antibiotic agent antofloxacin hydrochloride on human-ether-a-go-go-related gene potassium channel.	antofloxacin	55-81	potassium voltage-gated channel subfamily H member 2	Homo sapiens	85-117
20662825-2	2010	In this study, the effects of a novel fluoroquinolone, antofloxacin hydrochloride (AX) on human-ether-a-go-go-related gene (HERG) encoding potassium channels and the biophysical mechanisms of drug action were performed with whole-cell patch-clamp technique in transiently transfected HEK293 cells.	Fluoroquinolones	38-53	potassium voltage-gated channel subfamily H member 2	Homo sapiens	90-122
20662825-2	2010	In this study, the effects of a novel fluoroquinolone, antofloxacin hydrochloride (AX) on human-ether-a-go-go-related gene (HERG) encoding potassium channels and the biophysical mechanisms of drug action were performed with whole-cell patch-clamp technique in transiently transfected HEK293 cells.	Fluoroquinolones	38-53	potassium voltage-gated channel subfamily H member 2	Homo sapiens	124-128
20662825-2	2010	In this study, the effects of a novel fluoroquinolone, antofloxacin hydrochloride (AX) on human-ether-a-go-go-related gene (HERG) encoding potassium channels and the biophysical mechanisms of drug action were performed with whole-cell patch-clamp technique in transiently transfected HEK293 cells.	antofloxacin	55-81	potassium voltage-gated channel subfamily H member 2	Homo sapiens	90-122
20662825-2	2010	In this study, the effects of a novel fluoroquinolone, antofloxacin hydrochloride (AX) on human-ether-a-go-go-related gene (HERG) encoding potassium channels and the biophysical mechanisms of drug action were performed with whole-cell patch-clamp technique in transiently transfected HEK293 cells.	antofloxacin	55-81	potassium voltage-gated channel subfamily H member 2	Homo sapiens	124-128
20662825-2	2010	In this study, the effects of a novel fluoroquinolone, antofloxacin hydrochloride (AX) on human-ether-a-go-go-related gene (HERG) encoding potassium channels and the biophysical mechanisms of drug action were performed with whole-cell patch-clamp technique in transiently transfected HEK293 cells.	antofloxacin	83-85	potassium voltage-gated channel subfamily H member 2	Homo sapiens	90-122
20662825-2	2010	In this study, the effects of a novel fluoroquinolone, antofloxacin hydrochloride (AX) on human-ether-a-go-go-related gene (HERG) encoding potassium channels and the biophysical mechanisms of drug action were performed with whole-cell patch-clamp technique in transiently transfected HEK293 cells.	antofloxacin	83-85	potassium voltage-gated channel subfamily H member 2	Homo sapiens	124-128
20662825-4	2010	In comparison with sparfloxacin (SPX), levofloxacin lactate (LVFX), the potency of AX to inhibit HERG tail currents was the least one, with an IC(50) value of 460.37 microM.	antofloxacin	83-85	potassium voltage-gated channel subfamily H member 2	Homo sapiens	97-101
20463060-4	2010	Stimulation of alpha1A-AR with phenylephrine or direct activation of PKC with phorbol ester increased HERG channel protein abundance and K(+) current density in a time- and dose-dependent manner.	Phenylephrine	31-44	potassium voltage-gated channel subfamily H member 2	Homo sapiens	102-106
20463060-4	2010	Stimulation of alpha1A-AR with phenylephrine or direct activation of PKC with phorbol ester increased HERG channel protein abundance and K(+) current density in a time- and dose-dependent manner.	Phorbol Esters	78-91	potassium voltage-gated channel subfamily H member 2	Homo sapiens	102-106
20463060-6	2010	Phorbol ester and moderate alpha1A-AR stimulation enhanced HERG abundance in a PKC-dependent fashion but with stronger alpha1A-adrenergic stimulation; protein kinase A (PKA)-dependent activity also contributed.	Phorbol Esters	0-13	potassium voltage-gated channel subfamily H member 2	Homo sapiens	59-63
20428834-0	2010	HERG K+ channel related chemosensitivity to sparfloxacin in colon cancer cells.	sparfloxacin	44-56	potassium voltage-gated channel subfamily H member 2	Homo sapiens	0-4
20428834-3	2010	The aim of this study was to investigate the effects of antibacterial agents sparfloxacin (SPFX), a blocker of HERG channel, on HERG K+ channel highly expressing colon cancer cells.	sparfloxacin	77-89	potassium voltage-gated channel subfamily H member 2	Homo sapiens	111-115
20428834-3	2010	The aim of this study was to investigate the effects of antibacterial agents sparfloxacin (SPFX), a blocker of HERG channel, on HERG K+ channel highly expressing colon cancer cells.	sparfloxacin	77-89	potassium voltage-gated channel subfamily H member 2	Homo sapiens	128-132
20428834-3	2010	The aim of this study was to investigate the effects of antibacterial agents sparfloxacin (SPFX), a blocker of HERG channel, on HERG K+ channel highly expressing colon cancer cells.	sparfloxacin	91-95	potassium voltage-gated channel subfamily H member 2	Homo sapiens	111-115
20428834-3	2010	The aim of this study was to investigate the effects of antibacterial agents sparfloxacin (SPFX), a blocker of HERG channel, on HERG K+ channel highly expressing colon cancer cells.	sparfloxacin	91-95	potassium voltage-gated channel subfamily H member 2	Homo sapiens	128-132
20428834-14	2010	Study with herg-transfected HEK293 cells and siRNA-knock down HCT116 cells confirmed that the cell viability inhibition by SPFX was correlated with HERG expression.	sparfloxacin	123-127	potassium voltage-gated channel subfamily H member 2	Homo sapiens	11-15
20428834-14	2010	Study with herg-transfected HEK293 cells and siRNA-knock down HCT116 cells confirmed that the cell viability inhibition by SPFX was correlated with HERG expression.	sparfloxacin	123-127	potassium voltage-gated channel subfamily H member 2	Homo sapiens	148-152
20660661-5	2010	In human ether-a-go-go-related gene type 1 (hERG1) channels, Cd(2+) coordinated by D456 and D460 in S2 and D509 in S3 induces a positive shift in the voltage dependence of activation of ionic currents.	d456	83-87	potassium voltage-gated channel subfamily H member 2	Homo sapiens	44-49
20660661-5	2010	In human ether-a-go-go-related gene type 1 (hERG1) channels, Cd(2+) coordinated by D456 and D460 in S2 and D509 in S3 induces a positive shift in the voltage dependence of activation of ionic currents.	d460	92-96	potassium voltage-gated channel subfamily H member 2	Homo sapiens	44-49
20660661-5	2010	In human ether-a-go-go-related gene type 1 (hERG1) channels, Cd(2+) coordinated by D456 and D460 in S2 and D509 in S3 induces a positive shift in the voltage dependence of activation of ionic currents.	d509	107-111	potassium voltage-gated channel subfamily H member 2	Homo sapiens	44-49
20660661-11	2010	New Markov models of hERG1 channels were developed that describe gating currents as a noncooperative two-phase process of the VSD and can account for changes in these currents caused by extracellular Cd(2+).	Cadmium	200-202	potassium voltage-gated channel subfamily H member 2	Homo sapiens	21-26
20375276-0	2010	Ceramide modulates HERG potassium channel gating by translocation into lipid rafts.	Ceramides	0-8	potassium voltage-gated channel subfamily H member 2	Homo sapiens	19-23
20375276-4	2010	Yet the acute effects of ceramide on HERG potassium channels are not known.	Ceramides	25-33	potassium voltage-gated channel subfamily H member 2	Homo sapiens	37-41
20375276-5	2010	In the present study we examined the effects of cell-permeable C(6)-ceramide on HERG potassium channels stably expressed in HEK-293 cells.	N-caproylsphingosine	63-76	potassium voltage-gated channel subfamily H member 2	Homo sapiens	80-84
20375276-6	2010	C(6)-ceramide (10 microM) reversibly inhibited HERG channel current (I(HERG)) by 36 +/- 5%.	N-caproylsphingosine	0-13	potassium voltage-gated channel subfamily H member 2	Homo sapiens	47-51
20375276-6	2010	C(6)-ceramide (10 microM) reversibly inhibited HERG channel current (I(HERG)) by 36 +/- 5%.	N-caproylsphingosine	0-13	potassium voltage-gated channel subfamily H member 2	Homo sapiens	71-75
20375276-8	2010	Mechanistically, ceramide recruited HERG channels within caveolin-enriched lipid rafts.	Ceramides	17-25	potassium voltage-gated channel subfamily H member 2	Homo sapiens	36-40
20375276-11	2010	Our results provide new insights into the effects of C(6)-ceramide on HERG channels and suggest that C(6)-ceramide can be a promising therapeutic for cancers that overexpress HERG.	N-caproylsphingosine	53-66	potassium voltage-gated channel subfamily H member 2	Homo sapiens	70-74
20375276-11	2010	Our results provide new insights into the effects of C(6)-ceramide on HERG channels and suggest that C(6)-ceramide can be a promising therapeutic for cancers that overexpress HERG.	N-caproylsphingosine	101-114	potassium voltage-gated channel subfamily H member 2	Homo sapiens	70-74
20375276-11	2010	Our results provide new insights into the effects of C(6)-ceramide on HERG channels and suggest that C(6)-ceramide can be a promising therapeutic for cancers that overexpress HERG.	N-caproylsphingosine	101-114	potassium voltage-gated channel subfamily H member 2	Homo sapiens	175-179
20348026-1	2010	BACKGROUND: Mutations in the KCNQ1 and human ether-a-go-go-related gene (HERG) genes cause the long QT syndromes, LQTS1 and LQTS2, due to reductions in the cardiac repolarizing I(Ks) and I(Kr) currents, respectively.	Potassium	179-181	potassium voltage-gated channel subfamily H member 2	Homo sapiens	73-77
20097192-0	2010	The amiodarone derivative KB130015 activates hERG1 potassium channels via a novel mechanism.	Amiodarone	4-14	potassium voltage-gated channel subfamily H member 2	Homo sapiens	45-50
20097192-0	2010	The amiodarone derivative KB130015 activates hERG1 potassium channels via a novel mechanism.	KB 130015	26-34	potassium voltage-gated channel subfamily H member 2	Homo sapiens	45-50
20097192-2	2010	Since they are targets of various drugs with cardiac side effects we tested whether the amiodarone derivative 2-methyl-3-(3,5-diiodo-4-carboxymethoxybenzyl)benzofuran (KB130015) blocks hERG1 channels like its parent compound.	Amiodarone	88-98	potassium voltage-gated channel subfamily H member 2	Homo sapiens	185-190
20097192-2	2010	Since they are targets of various drugs with cardiac side effects we tested whether the amiodarone derivative 2-methyl-3-(3,5-diiodo-4-carboxymethoxybenzyl)benzofuran (KB130015) blocks hERG1 channels like its parent compound.	KB 130015	110-166	potassium voltage-gated channel subfamily H member 2	Homo sapiens	185-190
20097192-2	2010	Since they are targets of various drugs with cardiac side effects we tested whether the amiodarone derivative 2-methyl-3-(3,5-diiodo-4-carboxymethoxybenzyl)benzofuran (KB130015) blocks hERG1 channels like its parent compound.	KB 130015	168-176	potassium voltage-gated channel subfamily H member 2	Homo sapiens	185-190
20097192-6	2010	KB130015 presumably binds to the hERG1 pore from the cytosolic side and functionally competes with hERG1 block by amiodarone, E4031 (N-[4-[[1-[2-(6-methyl-2-pyridinyl)ethyl]-4-piperidinyl] carbonyl] phenyl] methanesulfonamide dihydrochloride), and sertindole.	Amiodarone	114-124	potassium voltage-gated channel subfamily H member 2	Homo sapiens	99-104
20097192-6	2010	KB130015 presumably binds to the hERG1 pore from the cytosolic side and functionally competes with hERG1 block by amiodarone, E4031 (N-[4-[[1-[2-(6-methyl-2-pyridinyl)ethyl]-4-piperidinyl] carbonyl] phenyl] methanesulfonamide dihydrochloride), and sertindole.	E 4031	126-131	potassium voltage-gated channel subfamily H member 2	Homo sapiens	33-38
20097192-6	2010	KB130015 presumably binds to the hERG1 pore from the cytosolic side and functionally competes with hERG1 block by amiodarone, E4031 (N-[4-[[1-[2-(6-methyl-2-pyridinyl)ethyl]-4-piperidinyl] carbonyl] phenyl] methanesulfonamide dihydrochloride), and sertindole.	E 4031	126-131	potassium voltage-gated channel subfamily H member 2	Homo sapiens	99-104
20097192-7	2010	Vice versa, amiodarone attenuates hERG1 activation by KB130015.	Amiodarone	12-22	potassium voltage-gated channel subfamily H member 2	Homo sapiens	34-39
20097192-8	2010	Based on synergic channel activation by mallotoxin and KB130015 we conclude that the hERG1 pore contains at least two sites for activators that are functionally coupled among each other and to the cavity-blocker site.	rottlerin	40-50	potassium voltage-gated channel subfamily H member 2	Homo sapiens	85-90
20097192-9	2010	KB130015 and amiodarone may serve as lead structures for the identification of hERG1 pore-interacting drugs favoring channel activation vs. block.	Amiodarone	13-23	potassium voltage-gated channel subfamily H member 2	Homo sapiens	79-84
20015154-6	2010	Enrichment with cholesterol inhibited HERG currents, while inclusion of PIP2 in the pipette solution blocked the cholesterol effect.	Cholesterol	16-27	potassium voltage-gated channel subfamily H member 2	Homo sapiens	38-42
19817928-2	2010	Vanoxerine is a drug that is free of adverse cardiac events in normal volunteers, yet is a potent blocker of the hERG (hK(v)11.1) cardiac potassium channel.	vanoxerine	0-10	potassium voltage-gated channel subfamily H member 2	Homo sapiens	119-128
19817928-6	2010	RESULTS: We found that vanoxerine was a potent hK(v)11.1 blocker, and at submicromolar concentrations, it blocked Ca and Na currents in a strongly frequency-dependent manner.	vanoxerine	23-33	potassium voltage-gated channel subfamily H member 2	Homo sapiens	47-56
20390067-4	2010	Loss-of-function mutations in KCNH2, the gene encoding the cardiac ion channel that is responsible for the rapidly activating delayed rectifying potassium current, are linked to long-QT syndrome type 2 (LQT-2).	Potassium	145-154	potassium voltage-gated channel subfamily H member 2	Homo sapiens	30-35
20390067-4	2010	Loss-of-function mutations in KCNH2, the gene encoding the cardiac ion channel that is responsible for the rapidly activating delayed rectifying potassium current, are linked to long-QT syndrome type 2 (LQT-2).	Potassium	145-154	potassium voltage-gated channel subfamily H member 2	Homo sapiens	203-208
19765650-5	2010	In these cells blockade of HERG channels with the HERG blockers E 4301 or cisapride attenuated both proliferation and migration of the cells.	Cisapride	74-83	potassium voltage-gated channel subfamily H member 2	Homo sapiens	27-31
19859662-0	2010	Regulation of HERG (KCNH2) potassium channel surface expression by diacylglycerol.	Diglycerides	67-81	potassium voltage-gated channel subfamily H member 2	Homo sapiens	14-18
19859662-0	2010	Regulation of HERG (KCNH2) potassium channel surface expression by diacylglycerol.	Diglycerides	67-81	potassium voltage-gated channel subfamily H member 2	Homo sapiens	20-25
19859662-3	2010	In the present report, using human embryonic kidney cells stably expressing HERG, we show that diacylglycerol potently inhibits the HERG current.	Diglycerides	95-109	potassium voltage-gated channel subfamily H member 2	Homo sapiens	76-80
19859662-3	2010	In the present report, using human embryonic kidney cells stably expressing HERG, we show that diacylglycerol potently inhibits the HERG current.	Diglycerides	95-109	potassium voltage-gated channel subfamily H member 2	Homo sapiens	132-136
19859662-6	2010	Thus, diacylglycerol is an important lipid participating in the regulation of HERG surface expression and function.	Diglycerides	6-20	potassium voltage-gated channel subfamily H member 2	Homo sapiens	78-82
21063089-0	2010	The novel mechanism of oxymatrine affecting HERG currents at different temperatures.	oxymatrine	23-33	potassium voltage-gated channel subfamily H member 2	Homo sapiens	44-48
19765650-5	2010	In these cells blockade of HERG channels with the HERG blockers E 4301 or cisapride attenuated both proliferation and migration of the cells.	Cisapride	74-83	potassium voltage-gated channel subfamily H member 2	Homo sapiens	50-54
19765650-6	2010	Activation of HERG with PD118057 stimulated cell migration.	2-(4-(2-(3,4-dichlorophenyl)ethyl)phenylamino)benzoic acid	24-32	potassium voltage-gated channel subfamily H member 2	Homo sapiens	14-18
20210727-7	2010	Methadone is the opiod most tightly associated with QTc prolongation; with much lesser potency buprenorphine and oxycodone can block HERG channels and depress the IKr current in vitro.Antineoplastic chemotherapy like anthracyclines, alkylating drugs, alkilants and cisplatin are associated with electrocardiographic alterations including prolongation of QT and emesis of different grades.	Buprenorphine	95-108	potassium voltage-gated channel subfamily H member 2	Homo sapiens	133-137
20210727-7	2010	Methadone is the opiod most tightly associated with QTc prolongation; with much lesser potency buprenorphine and oxycodone can block HERG channels and depress the IKr current in vitro.Antineoplastic chemotherapy like anthracyclines, alkylating drugs, alkilants and cisplatin are associated with electrocardiographic alterations including prolongation of QT and emesis of different grades.	Oxycodone	113-122	potassium voltage-gated channel subfamily H member 2	Homo sapiens	133-137
19949665-3	2009	Application of MeOH extract of Lindera erythrocarpa showed a dose-dependent decrease in the amplitudes of the outward currents measured at the end of the pulse (I(HERG)) and the tail currents of HERG (I(tail)).	Methanol	15-19	potassium voltage-gated channel subfamily H member 2	Homo sapiens	163-167
19577877-9	2010	The selective HERG1 inhibitor E-4031 dose-dependently impaired tumor growth in the proliferation assays.	E 4031	30-36	potassium voltage-gated channel subfamily H member 2	Homo sapiens	14-19
19949665-3	2009	Application of MeOH extract of Lindera erythrocarpa showed a dose-dependent decrease in the amplitudes of the outward currents measured at the end of the pulse (I(HERG)) and the tail currents of HERG (I(tail)).	Methanol	15-19	potassium voltage-gated channel subfamily H member 2	Homo sapiens	195-199
19949665-4	2009	When the BuOH fraction and H(2)O fraction of Lindera erythrocarpa were added to the perfusate, both I(HERG) and I(tail) were suppressed, while the hexane fraction, CHCl(3) fraction, and EtOAc fraction did not inhibit either I(HERG) or I(tail).	Butanols	9-13	potassium voltage-gated channel subfamily H member 2	Homo sapiens	102-106
19949665-4	2009	When the BuOH fraction and H(2)O fraction of Lindera erythrocarpa were added to the perfusate, both I(HERG) and I(tail) were suppressed, while the hexane fraction, CHCl(3) fraction, and EtOAc fraction did not inhibit either I(HERG) or I(tail).	Butanols	9-13	potassium voltage-gated channel subfamily H member 2	Homo sapiens	226-230
19892732-0	2009	PD-118057 contacts the pore helix of hERG1 channels to attenuate inactivation and enhance K+ conductance.	2-(4-(2-(3,4-dichlorophenyl)ethyl)phenylamino)benzoic acid	0-9	potassium voltage-gated channel subfamily H member 2	Homo sapiens	37-42
19671703-3	2009	Here we explored cyclic nucleotide binding and modulation of mEAG1 and hERG1 channels with fluorescence and electrophysiology.	Nucleotides, Cyclic	17-34	potassium voltage-gated channel subfamily H member 2	Homo sapiens	71-76
19671703-4	2009	Binding of cyclic nucleotides to the isolated CNBD of mEAG1 and hERG1 channels was examined with two independent fluorescence-based methods: changes in tryptophan fluorescence and fluorescence of an analog of cAMP, 8-NBD-cAMP.	Nucleotides, Cyclic	11-29	potassium voltage-gated channel subfamily H member 2	Homo sapiens	64-69
19671703-6	2009	Our results indicated that cyclic nucleotides do not bind to the isolated CNBD domain of mEAG1 channels and bind with low affinity (K(d) > or = 51 microm) to the isolated CNBD of hERG1 channels.	Nucleotides, Cyclic	27-45	potassium voltage-gated channel subfamily H member 2	Homo sapiens	182-187
19725081-0	2009	Exploring chemical substructures essential for HERG k(+) channel blockade by synthesis and biological evaluation of dofetilide analogues.	dofetilide	116-126	potassium voltage-gated channel subfamily H member 2	Homo sapiens	47-51
19457646-1	2009	Sertindole"s propensity to prolong the QT interval relates to blockade of the KCNH2 (HERG) encoded Ikr potassium channel, but there has been limited detailed data on T-wave morphology changes.	sertindole	0-10	potassium voltage-gated channel subfamily H member 2	Homo sapiens	78-83
19457646-1	2009	Sertindole"s propensity to prolong the QT interval relates to blockade of the KCNH2 (HERG) encoded Ikr potassium channel, but there has been limited detailed data on T-wave morphology changes.	sertindole	0-10	potassium voltage-gated channel subfamily H member 2	Homo sapiens	85-89
19892732-10	2009	Molecular modeling indicates that PD-118057 binds to a hydrophobic pocket formed by L646 of one hERG1 subunit and F619 of an adjacent subunit.	2-(4-(2-(3,4-dichlorophenyl)ethyl)phenylamino)benzoic acid	34-43	potassium voltage-gated channel subfamily H member 2	Homo sapiens	96-101
19892732-10	2009	Molecular modeling indicates that PD-118057 binds to a hydrophobic pocket formed by L646 of one hERG1 subunit and F619 of an adjacent subunit.	4-azaindole	84-88	potassium voltage-gated channel subfamily H member 2	Homo sapiens	96-101
19892732-11	2009	We conclude that direct interaction of PD-118057 with the pore helix attenuates fast P-type inactivation and increases open probability of hERG1 channels.	2-(4-(2-(3,4-dichlorophenyl)ethyl)phenylamino)benzoic acid	39-48	potassium voltage-gated channel subfamily H member 2	Homo sapiens	139-144
18692916-1	2009	In a 34-year-old man showing short QT interval (QTc 329 ms), we identified a novel C-terminal KCNH2 mutation, R1135H.	qtc	48-51	potassium voltage-gated channel subfamily H member 2	Homo sapiens	94-99
19215240-6	2009	A mutant F463L HERG channel was expressed in HEK293 cells using a lipofectamine method.	Lipofectamine	66-79	potassium voltage-gated channel subfamily H member 2	Homo sapiens	15-19
19409379-4	2009	Our results showed that E-4031, a specific hERG1 K(+) channels inhibitor, significantly blocked SDF-1-induced migration of leukemic cell lines, primary acute leukemic cells, leukemic stem cells and HEK293T cells transfected with herg-pEGFP.	E 4031	24-30	potassium voltage-gated channel subfamily H member 2	Homo sapiens	43-48
19424681-0	2009	Blockade of HERG K+ channel by isoquinoline alkaloid neferine in the stable transfected HEK293 cells.	Tubocurarine	31-52	potassium voltage-gated channel subfamily H member 2	Homo sapiens	12-16
19424681-0	2009	Blockade of HERG K+ channel by isoquinoline alkaloid neferine in the stable transfected HEK293 cells.	neferine	53-61	potassium voltage-gated channel subfamily H member 2	Homo sapiens	12-16
19424681-1	2009	We studied the effects of isoquinoline alkaloid neferine (Nef) extracted from the seed embryo of Nelumbo nucifera Gaertn on Human ether-a-go-go-related gene (HERG) channels stably expressed in human embryonic kidney (HEK293) cells using whole-cell patch clamp technique, western blot analysis and immunofluorescence experiment.	Tubocurarine	26-47	potassium voltage-gated channel subfamily H member 2	Homo sapiens	158-162
19424681-1	2009	We studied the effects of isoquinoline alkaloid neferine (Nef) extracted from the seed embryo of Nelumbo nucifera Gaertn on Human ether-a-go-go-related gene (HERG) channels stably expressed in human embryonic kidney (HEK293) cells using whole-cell patch clamp technique, western blot analysis and immunofluorescence experiment.	neferine	48-56	potassium voltage-gated channel subfamily H member 2	Homo sapiens	158-162
19419905-3	2009	OBJECTIVE: We investigated acute alpha(1A)- and cyclic adenosine monophosphate (cAMP)-related beta-adrenergic modulation of I(Kr) in HL-1 cardiomyocytes, wild type (WT)- and 2 LQT2-associated mutant Kv11.1 channels (Y43D- and K595E-Kv11.1) reconstituted in Chinese hamster ovary (CHO) cells.	Cyclic AMP	80-84	potassium voltage-gated channel subfamily H member 2	Homo sapiens	176-180
19617705-0	2009	Extracellular potassium dependency of block of HERG by quinidine and cisapride is primarily determined by the permeant ion and not by inactivation.	Potassium	14-23	potassium voltage-gated channel subfamily H member 2	Homo sapiens	47-51
19617705-0	2009	Extracellular potassium dependency of block of HERG by quinidine and cisapride is primarily determined by the permeant ion and not by inactivation.	Quinidine	55-64	potassium voltage-gated channel subfamily H member 2	Homo sapiens	47-51
19617705-0	2009	Extracellular potassium dependency of block of HERG by quinidine and cisapride is primarily determined by the permeant ion and not by inactivation.	Cisapride	69-78	potassium voltage-gated channel subfamily H member 2	Homo sapiens	47-51
19617705-6	2009	In this study, HERG block by quinidine and cisapride was assessed in extracellular solutions of calcium, potassium, rubidium, cesium and tetraethylammonium (TEA) using two-electrode voltage clamping of Xenopus oocytes.	Quinidine	29-38	potassium voltage-gated channel subfamily H member 2	Homo sapiens	15-19
19617705-6	2009	In this study, HERG block by quinidine and cisapride was assessed in extracellular solutions of calcium, potassium, rubidium, cesium and tetraethylammonium (TEA) using two-electrode voltage clamping of Xenopus oocytes.	Cisapride	43-52	potassium voltage-gated channel subfamily H member 2	Homo sapiens	15-19
19617705-6	2009	In this study, HERG block by quinidine and cisapride was assessed in extracellular solutions of calcium, potassium, rubidium, cesium and tetraethylammonium (TEA) using two-electrode voltage clamping of Xenopus oocytes.	Calcium	96-103	potassium voltage-gated channel subfamily H member 2	Homo sapiens	15-19
19617705-6	2009	In this study, HERG block by quinidine and cisapride was assessed in extracellular solutions of calcium, potassium, rubidium, cesium and tetraethylammonium (TEA) using two-electrode voltage clamping of Xenopus oocytes.	Potassium	105-114	potassium voltage-gated channel subfamily H member 2	Homo sapiens	15-19
19617705-6	2009	In this study, HERG block by quinidine and cisapride was assessed in extracellular solutions of calcium, potassium, rubidium, cesium and tetraethylammonium (TEA) using two-electrode voltage clamping of Xenopus oocytes.	Rubidium	116-124	potassium voltage-gated channel subfamily H member 2	Homo sapiens	15-19
19617705-6	2009	In this study, HERG block by quinidine and cisapride was assessed in extracellular solutions of calcium, potassium, rubidium, cesium and tetraethylammonium (TEA) using two-electrode voltage clamping of Xenopus oocytes.	cesium and tetraethylammonium	126-155	potassium voltage-gated channel subfamily H member 2	Homo sapiens	15-19
19617705-6	2009	In this study, HERG block by quinidine and cisapride was assessed in extracellular solutions of calcium, potassium, rubidium, cesium and tetraethylammonium (TEA) using two-electrode voltage clamping of Xenopus oocytes.	Tetraethylammonium	157-160	potassium voltage-gated channel subfamily H member 2	Homo sapiens	15-19
19617705-7	2009	Consistent with previous reports we show that increases in extracellular potassium reduce HERG block by quinidine and cisapride.	Potassium	73-82	potassium voltage-gated channel subfamily H member 2	Homo sapiens	90-94
19617705-7	2009	Consistent with previous reports we show that increases in extracellular potassium reduce HERG block by quinidine and cisapride.	Quinidine	104-113	potassium voltage-gated channel subfamily H member 2	Homo sapiens	90-94
19617705-7	2009	Consistent with previous reports we show that increases in extracellular potassium reduce HERG block by quinidine and cisapride.	Cisapride	118-127	potassium voltage-gated channel subfamily H member 2	Homo sapiens	90-94
19617705-8	2009	We also show that increasing extracellular rubidium and cesium reduced HERG block by quinidine and cisapride whereas increasing extracellular calcium and extracellular TEA did not alter HERG block by quinidine and cisapride.	Rubidium	43-51	potassium voltage-gated channel subfamily H member 2	Homo sapiens	71-75
19617705-8	2009	We also show that increasing extracellular rubidium and cesium reduced HERG block by quinidine and cisapride whereas increasing extracellular calcium and extracellular TEA did not alter HERG block by quinidine and cisapride.	Cesium	56-62	potassium voltage-gated channel subfamily H member 2	Homo sapiens	71-75
19617705-8	2009	We also show that increasing extracellular rubidium and cesium reduced HERG block by quinidine and cisapride whereas increasing extracellular calcium and extracellular TEA did not alter HERG block by quinidine and cisapride.	Quinidine	85-94	potassium voltage-gated channel subfamily H member 2	Homo sapiens	71-75
19617705-8	2009	We also show that increasing extracellular rubidium and cesium reduced HERG block by quinidine and cisapride whereas increasing extracellular calcium and extracellular TEA did not alter HERG block by quinidine and cisapride.	Cisapride	99-108	potassium voltage-gated channel subfamily H member 2	Homo sapiens	71-75
19617705-9	2009	These results demonstrate that at lower extracellular potassium concentrations, the permeant ion is almost exclusively responsible for the reduction in quinidine and cisapride block of HERG due to increases in extracellular potassium.	Potassium	54-63	potassium voltage-gated channel subfamily H member 2	Homo sapiens	185-189
19617705-9	2009	These results demonstrate that at lower extracellular potassium concentrations, the permeant ion is almost exclusively responsible for the reduction in quinidine and cisapride block of HERG due to increases in extracellular potassium.	Cisapride	166-175	potassium voltage-gated channel subfamily H member 2	Homo sapiens	185-189
19617705-9	2009	These results demonstrate that at lower extracellular potassium concentrations, the permeant ion is almost exclusively responsible for the reduction in quinidine and cisapride block of HERG due to increases in extracellular potassium.	Potassium	224-233	potassium voltage-gated channel subfamily H member 2	Homo sapiens	185-189
19528813-6	2009	The IC50 for quinidine block of IKr in CHO cells transfected with HERG alone was significantly higher than cells transfected with HERG + OCTN1 (0.66 +/- 0.15 microM versus 0.14 +/- 0.06 microM [52% absolute increase in drug block; 95% confidence interval, 0.4-0.64 microM]), and this effect was further potentiated by a common genetic variant of OCTN1, L503F.	Quinidine	13-22	potassium voltage-gated channel subfamily H member 2	Homo sapiens	66-70
19366693-3	2009	One of the identified compounds, gambogic acid (GA), potently (EC(50) < or = 100 nm) inhibited Kir2.1 channels in mammalian cells when applied chronically for 3 h. This potent and slow inhibition was not seen with Kv2.1, HERG or Kir1.1 channels.	gambogic acid	33-46	potassium voltage-gated channel subfamily H member 2	Homo sapiens	224-228
19366693-3	2009	One of the identified compounds, gambogic acid (GA), potently (EC(50) < or = 100 nm) inhibited Kir2.1 channels in mammalian cells when applied chronically for 3 h. This potent and slow inhibition was not seen with Kv2.1, HERG or Kir1.1 channels.	gambogic acid	48-50	potassium voltage-gated channel subfamily H member 2	Homo sapiens	224-228
18998156-6	2009	Gating of erg1 channels kept the voltage response to glutamate brief and at physiological amplitudes.	Glutamic Acid	53-62	potassium voltage-gated channel subfamily H member 2	Homo sapiens	10-14
19406877-0	2009	The evolutionarily conserved residue A653 plays a key role in HERG channel closing.	a653	37-41	potassium voltage-gated channel subfamily H member 2	Homo sapiens	62-66
19406877-3	2009	Here, we assess the functional role of the alanine at position 653 (HERG-A653) that is highly conserved among evolutionarily divergent K(+) channels.	Alanine	43-50	potassium voltage-gated channel subfamily H member 2	Homo sapiens	68-72
19406877-4	2009	HERG-A653 is close to the "glycine hinge" implicated in K(+) channel opening, and is flanked by tyrosine 652 and phenylalanine 656, which contribute to the drug binding site.	Glycine	27-34	potassium voltage-gated channel subfamily H member 2	Homo sapiens	0-4
19406877-4	2009	HERG-A653 is close to the "glycine hinge" implicated in K(+) channel opening, and is flanked by tyrosine 652 and phenylalanine 656, which contribute to the drug binding site.	Tyrosine	96-104	potassium voltage-gated channel subfamily H member 2	Homo sapiens	0-4
19406877-4	2009	HERG-A653 is close to the "glycine hinge" implicated in K(+) channel opening, and is flanked by tyrosine 652 and phenylalanine 656, which contribute to the drug binding site.	Phenylalanine	113-126	potassium voltage-gated channel subfamily H member 2	Homo sapiens	0-4
19406877-10	2009	Our study suggests that A653 plays an important functional role in the outwardly rectifying gating behaviour of HERG, supporting channel closure at membrane potentials negative to the channel activation threshold.	a653	24-28	potassium voltage-gated channel subfamily H member 2	Homo sapiens	112-116
19204737-0	2009	Influence of the G2677T/C3435T haplotype of MDR1 on P-glycoprotein trafficking and ibutilide-induced block of HERG.	ibutilide	83-92	potassium voltage-gated channel subfamily H member 2	Homo sapiens	110-114
19204737-3	2009	We tested the effect of these MDR1 variants on Human Ether-Related A Go-Go (HERG) block by ibutilide in CHO cells 48 h following transient transfection with an IRES-dsRed vector containing MDR1, G2677T MDR1, G2677T/C3435T MDR1 or an empty bicistronic site and an IRES-GFP vector containing HERG (KCNH2).	ibutilide	91-100	potassium voltage-gated channel subfamily H member 2	Homo sapiens	76-80
19204737-3	2009	We tested the effect of these MDR1 variants on Human Ether-Related A Go-Go (HERG) block by ibutilide in CHO cells 48 h following transient transfection with an IRES-dsRed vector containing MDR1, G2677T MDR1, G2677T/C3435T MDR1 or an empty bicistronic site and an IRES-GFP vector containing HERG (KCNH2).	ibutilide	91-100	potassium voltage-gated channel subfamily H member 2	Homo sapiens	290-294
19204737-3	2009	We tested the effect of these MDR1 variants on Human Ether-Related A Go-Go (HERG) block by ibutilide in CHO cells 48 h following transient transfection with an IRES-dsRed vector containing MDR1, G2677T MDR1, G2677T/C3435T MDR1 or an empty bicistronic site and an IRES-GFP vector containing HERG (KCNH2).	CAV protocol	104-107	potassium voltage-gated channel subfamily H member 2	Homo sapiens	76-80
19204737-8	2009	Coculture with fexofenadine(1 microM), an MDR1 substrate known to rescue misfolding in other membrane proteins, restored cell surface expression of MDR1 G2677T/C3435T and restored resistance to block HERG by ibutilide 200 nM (98.5+/-0.98% vs 42.3+/-2.2%, P<0.001).	fexofenadine	15-27	potassium voltage-gated channel subfamily H member 2	Homo sapiens	200-204
19204737-8	2009	Coculture with fexofenadine(1 microM), an MDR1 substrate known to rescue misfolding in other membrane proteins, restored cell surface expression of MDR1 G2677T/C3435T and restored resistance to block HERG by ibutilide 200 nM (98.5+/-0.98% vs 42.3+/-2.2%, P<0.001).	ibutilide	208-217	potassium voltage-gated channel subfamily H member 2	Homo sapiens	200-204
19204737-10	2009	These data identify ibutilide as an MDR1 substrate and further support the concept that variable drug transport function can modulate the action of HERG blockers.	ibutilide	20-29	potassium voltage-gated channel subfamily H member 2	Homo sapiens	148-152
19413965-1	2009	hERG1 is a member of the cyclic nucleotide binding domain family of K(+) channels.	Nucleotides, Cyclic	25-42	potassium voltage-gated channel subfamily H member 2	Homo sapiens	0-5
19413965-3	2009	We reasoned that histidine 562 in hERG1 could play an important structure-function role.	Histidine	17-26	potassium voltage-gated channel subfamily H member 2	Homo sapiens	34-39
19413965-4	2009	To explore this role, we created in silica models of the hERG1 pore domain based on the KvAP crystal structure with Rosetta-membrane modeling and molecular-dynamics simulations.	Silicon Dioxide	36-42	potassium voltage-gated channel subfamily H member 2	Homo sapiens	57-62
19413965-11	2009	In conclusion, interactions between H562 in the S5 helix and amino acids in the pore helix are important determinants of hERG1 potassium channel function, as confirmed by theory and experiment.	7-methylquinazoline-2,4-diamine	36-40	potassium voltage-gated channel subfamily H member 2	Homo sapiens	121-126
19234087-6	2009	Direct PKA phosphorylation of the HERG protein was responsible for the cAMP-induced augmentation.	Cyclic AMP	71-75	potassium voltage-gated channel subfamily H member 2	Homo sapiens	34-38
19413965-0	2009	Interactions of H562 in the S5 helix with T618 and S621 in the pore helix are important determinants of hERG1 potassium channel structure and function.	7-methylquinazoline-2,4-diamine	16-20	potassium voltage-gated channel subfamily H member 2	Homo sapiens	104-109
19234087-9	2009	Acceleration of the HERG protein synthesis rate was the primary factor in the cAMP/PKA effect with lesser effects on protein stability.	Cyclic AMP	78-82	potassium voltage-gated channel subfamily H member 2	Homo sapiens	20-24
19244476-0	2009	State-dependent block of HERG potassium channels by R-roscovitine: implications for cancer therapy.	Roscovitine	52-65	potassium voltage-gated channel subfamily H member 2	Homo sapiens	25-29
19285067-7	2009	Furthermore, PF-01354082 decreased I(HERG) current by only 11% at a concentration of 300 microM, indicating that the compound had greater than 150,000-fold selectivity for the human 5-HT(4d) receptor over hERG channels.	4-((4-((((3-Isopropyl-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)carbonyl)amino)methyl)piperidin-1-yl)methyl)tetrahydro-2H-pyran-4-carboxylic acid	13-24	potassium voltage-gated channel subfamily H member 2	Homo sapiens	37-41
19244476-6	2009	In the present study we show that R-roscovitine blocks HERG potassium current (human embryonic kidney-293 cells stably expressing HERG) at clinically relevant concentrations.	Roscovitine	34-47	potassium voltage-gated channel subfamily H member 2	Homo sapiens	55-59
19244476-6	2009	In the present study we show that R-roscovitine blocks HERG potassium current (human embryonic kidney-293 cells stably expressing HERG) at clinically relevant concentrations.	Roscovitine	34-47	potassium voltage-gated channel subfamily H member 2	Homo sapiens	130-134
19244476-6	2009	In the present study we show that R-roscovitine blocks HERG potassium current (human embryonic kidney-293 cells stably expressing HERG) at clinically relevant concentrations.	Potassium	60-69	potassium voltage-gated channel subfamily H member 2	Homo sapiens	55-59
19244476-8	2009	Kinetic study of wild-type and inactivation mutant HERG channels supported block of activated channels by roscovitine with relatively little effect on either closed or inactivated channels.	Roscovitine	106-117	potassium voltage-gated channel subfamily H member 2	Homo sapiens	51-55
19244476-9	2009	A HERG gating model reproduced all roscovitine effects.	Roscovitine	35-46	potassium voltage-gated channel subfamily H member 2	Homo sapiens	2-6
19324319-0	2009	Aminoglycoside antibiotics restore functional expression of truncated HERG channels produced by nonsense mutations.	Aminoglycosides	0-14	potassium voltage-gated channel subfamily H member 2	Homo sapiens	70-74
19234087-4	2009	Sustained elevation of cAMP by either chlorophenylthiol (CPT)-cAMP or forskolin increased the HERG channel protein abundance two- to fourfold within 24 h, with measurable difference as early as 4 h. The cAMP-induced augmentation was not due to changes in transcription and was specific for HERG compared with other cardiac K(+) channels (Kv1.4, Kv1.5, Kir2.1, and KvLQT1).	Cyclic AMP	23-27	potassium voltage-gated channel subfamily H member 2	Homo sapiens	94-98
19234087-4	2009	Sustained elevation of cAMP by either chlorophenylthiol (CPT)-cAMP or forskolin increased the HERG channel protein abundance two- to fourfold within 24 h, with measurable difference as early as 4 h. The cAMP-induced augmentation was not due to changes in transcription and was specific for HERG compared with other cardiac K(+) channels (Kv1.4, Kv1.5, Kir2.1, and KvLQT1).	Cyclic AMP	23-27	potassium voltage-gated channel subfamily H member 2	Homo sapiens	290-294
19234087-4	2009	Sustained elevation of cAMP by either chlorophenylthiol (CPT)-cAMP or forskolin increased the HERG channel protein abundance two- to fourfold within 24 h, with measurable difference as early as 4 h. The cAMP-induced augmentation was not due to changes in transcription and was specific for HERG compared with other cardiac K(+) channels (Kv1.4, Kv1.5, Kir2.1, and KvLQT1).	chlorophenylthiol	38-55	potassium voltage-gated channel subfamily H member 2	Homo sapiens	94-98
19234087-4	2009	Sustained elevation of cAMP by either chlorophenylthiol (CPT)-cAMP or forskolin increased the HERG channel protein abundance two- to fourfold within 24 h, with measurable difference as early as 4 h. The cAMP-induced augmentation was not due to changes in transcription and was specific for HERG compared with other cardiac K(+) channels (Kv1.4, Kv1.5, Kir2.1, and KvLQT1).	chlorophenylthiol	38-55	potassium voltage-gated channel subfamily H member 2	Homo sapiens	290-294
19234087-4	2009	Sustained elevation of cAMP by either chlorophenylthiol (CPT)-cAMP or forskolin increased the HERG channel protein abundance two- to fourfold within 24 h, with measurable difference as early as 4 h. The cAMP-induced augmentation was not due to changes in transcription and was specific for HERG compared with other cardiac K(+) channels (Kv1.4, Kv1.5, Kir2.1, and KvLQT1).	cpt	57-60	potassium voltage-gated channel subfamily H member 2	Homo sapiens	94-98
19234087-4	2009	Sustained elevation of cAMP by either chlorophenylthiol (CPT)-cAMP or forskolin increased the HERG channel protein abundance two- to fourfold within 24 h, with measurable difference as early as 4 h. The cAMP-induced augmentation was not due to changes in transcription and was specific for HERG compared with other cardiac K(+) channels (Kv1.4, Kv1.5, Kir2.1, and KvLQT1).	cpt	57-60	potassium voltage-gated channel subfamily H member 2	Homo sapiens	290-294
19234087-4	2009	Sustained elevation of cAMP by either chlorophenylthiol (CPT)-cAMP or forskolin increased the HERG channel protein abundance two- to fourfold within 24 h, with measurable difference as early as 4 h. The cAMP-induced augmentation was not due to changes in transcription and was specific for HERG compared with other cardiac K(+) channels (Kv1.4, Kv1.5, Kir2.1, and KvLQT1).	Cyclic AMP	62-66	potassium voltage-gated channel subfamily H member 2	Homo sapiens	94-98
19234087-4	2009	Sustained elevation of cAMP by either chlorophenylthiol (CPT)-cAMP or forskolin increased the HERG channel protein abundance two- to fourfold within 24 h, with measurable difference as early as 4 h. The cAMP-induced augmentation was not due to changes in transcription and was specific for HERG compared with other cardiac K(+) channels (Kv1.4, Kv1.5, Kir2.1, and KvLQT1).	Cyclic AMP	62-66	potassium voltage-gated channel subfamily H member 2	Homo sapiens	290-294
19234087-4	2009	Sustained elevation of cAMP by either chlorophenylthiol (CPT)-cAMP or forskolin increased the HERG channel protein abundance two- to fourfold within 24 h, with measurable difference as early as 4 h. The cAMP-induced augmentation was not due to changes in transcription and was specific for HERG compared with other cardiac K(+) channels (Kv1.4, Kv1.5, Kir2.1, and KvLQT1).	Colforsin	70-79	potassium voltage-gated channel subfamily H member 2	Homo sapiens	94-98
19234087-4	2009	Sustained elevation of cAMP by either chlorophenylthiol (CPT)-cAMP or forskolin increased the HERG channel protein abundance two- to fourfold within 24 h, with measurable difference as early as 4 h. The cAMP-induced augmentation was not due to changes in transcription and was specific for HERG compared with other cardiac K(+) channels (Kv1.4, Kv1.5, Kir2.1, and KvLQT1).	Colforsin	70-79	potassium voltage-gated channel subfamily H member 2	Homo sapiens	290-294
19234087-4	2009	Sustained elevation of cAMP by either chlorophenylthiol (CPT)-cAMP or forskolin increased the HERG channel protein abundance two- to fourfold within 24 h, with measurable difference as early as 4 h. The cAMP-induced augmentation was not due to changes in transcription and was specific for HERG compared with other cardiac K(+) channels (Kv1.4, Kv1.5, Kir2.1, and KvLQT1).	Cyclic AMP	62-66	potassium voltage-gated channel subfamily H member 2	Homo sapiens	94-98
19234087-4	2009	Sustained elevation of cAMP by either chlorophenylthiol (CPT)-cAMP or forskolin increased the HERG channel protein abundance two- to fourfold within 24 h, with measurable difference as early as 4 h. The cAMP-induced augmentation was not due to changes in transcription and was specific for HERG compared with other cardiac K(+) channels (Kv1.4, Kv1.5, Kir2.1, and KvLQT1).	Cyclic AMP	62-66	potassium voltage-gated channel subfamily H member 2	Homo sapiens	290-294
19324319-3	2009	OBJECTIVE: The purpose of this study was to investigate the effect of aminoglycoside antibiotics on the expression of nonsense mutants expected to produce truncated HERG channels.	Aminoglycosides	70-84	potassium voltage-gated channel subfamily H member 2	Homo sapiens	165-169
19374880-0	2009	Pitavastatin suppresses mitogen activated protein kinase-mediated Erg-1 induction in human vascular smooth muscle cells.	pitavastatin	0-12	potassium voltage-gated channel subfamily H member 2	Homo sapiens	66-71
19038263-6	2009	Here we show that I(Kr) recorded in cells co-expressing HERG and ARHGAP6 was decreased by 43% compared to HERG alone.	arhgap6	65-72	potassium voltage-gated channel subfamily H member 2	Homo sapiens	106-110
19038263-7	2009	Biochemical measurements of cell-surface associated HERG revealed that ARHGAP6 reduced membrane expression of HERG by 35%, which correlates well with the reduction in current.	arhgap6	71-78	potassium voltage-gated channel subfamily H member 2	Homo sapiens	52-56
19038263-7	2009	Biochemical measurements of cell-surface associated HERG revealed that ARHGAP6 reduced membrane expression of HERG by 35%, which correlates well with the reduction in current.	arhgap6	71-78	potassium voltage-gated channel subfamily H member 2	Homo sapiens	110-114
19038263-11	2009	We further determined that ARHGAP6 effects are mediated by a consensus SH3 binding domain within the C-terminus of HERG, although stable ARHGAP6-HERG complexes were not observed.	arhgap6	27-34	potassium voltage-gated channel subfamily H member 2	Homo sapiens	115-119
19129680-0	2009	A receptor-independent effect of estrone sulfate on the HERG channel.	estrone sulfate	33-48	potassium voltage-gated channel subfamily H member 2	Homo sapiens	56-60
18984955-7	2009	RESULTS: At concentrations of 0.01, 0.03, 0.1, 1 and 3 mM, r/s-methadone produced a dose-dependent inhibition of HERG by 17 +/- 5, 23 +/- 4, 40 +/- 4, 57 +/- 3, 69 +/- 3 and 80 +/- 1%, respectively.	r/s-methadone	59-72	potassium voltage-gated channel subfamily H member 2	Homo sapiens	113-117
18984955-9	2009	At 0.1, 0.3 and 1 mM, s-methadone reduced HERG current by 50 +/- 4, 76 +/- 5 and 87 +/- 5%, respectively, while r-methadone reduced HERG current by 26 +/- 4, 53 +/- 3 and 77 +/- 3%, respectively.	Methadone	22-33	potassium voltage-gated channel subfamily H member 2	Homo sapiens	42-46
18984955-9	2009	At 0.1, 0.3 and 1 mM, s-methadone reduced HERG current by 50 +/- 4, 76 +/- 5 and 87 +/- 5%, respectively, while r-methadone reduced HERG current by 26 +/- 4, 53 +/- 3 and 77 +/- 3%, respectively.	Methadone	112-123	potassium voltage-gated channel subfamily H member 2	Homo sapiens	132-136
19530746-17	2009	In subjects receiving sotalol, T-wave morphology reached similarity to LQT2, whereas QTcF did not.	Sotalol	22-29	potassium voltage-gated channel subfamily H member 2	Homo sapiens	71-75
19530746-18	2009	CONCLUSION: Distinct ECG patterns in LQT2 carriers effectively quantified repolarization changes induced by sotalol.	Sotalol	108-115	potassium voltage-gated channel subfamily H member 2	Homo sapiens	37-41
18781376-2	2009	Here, we investigated the mechanism of hERG K(+) channel current (I(hERG)) blockade expressed in HEK-293 cells by sibutramine HCl, a serotonin-norepinephrine reuptake inhibitor.	sibutramine	114-129	potassium voltage-gated channel subfamily H member 2	Homo sapiens	39-73
19143746-3	2009	To study whether acehytisine hydrochloride affects HERG channel activity and protein trafficking, we expressed HERG in human embryonic kidney 293 (HEK293) cells and recorded HERG channel currents with a whole-cell patch clamp technique.	acehytisine hydrochloride	17-42	potassium voltage-gated channel subfamily H member 2	Homo sapiens	51-55
19143746-5	2009	We found that acehytisine hydrochloride inhibited HERG step current (I(HERG)) in a concentration-dependent manner.	acehytisine hydrochloride	14-39	potassium voltage-gated channel subfamily H member 2	Homo sapiens	50-54
19143746-5	2009	We found that acehytisine hydrochloride inhibited HERG step current (I(HERG)) in a concentration-dependent manner.	acehytisine hydrochloride	14-39	potassium voltage-gated channel subfamily H member 2	Homo sapiens	71-75
19143746-9	2009	Moreover, the F656C mutation in the S6 domain abolished acehytisine hydrochloride inhibition on the I(HERG) and enhanced the inhibitive effects on the trafficking of the 155 kD band.	acehytisine hydrochloride	56-81	potassium voltage-gated channel subfamily H member 2	Homo sapiens	102-106
19143746-10	2009	Acehytisine hydrochloride interrupted HERG protein trafficking at 1000 and 2500 microM.	acehytisine hydrochloride	0-25	potassium voltage-gated channel subfamily H member 2	Homo sapiens	38-42
19143746-11	2009	Our data showed that acehytisine hydrochloride could inhibit I(HERG), but had no effects on I(tail) until the concentration was above 1000 microM.	acehytisine hydrochloride	21-46	potassium voltage-gated channel subfamily H member 2	Homo sapiens	63-67
19034039-0	2008	Papaverine, a vasodilator, blocks the pore of the HERG channel at submicromolar concentration.	Papaverine	0-10	potassium voltage-gated channel subfamily H member 2	Homo sapiens	50-54
19034039-2	2008	To examine the mechanism for this effect, we herein tested the effects of papaverine on human ether-a-go-go (HERG) K channels expressed in HEK293 cells and Xenopus oocytes.	Papaverine	74-84	potassium voltage-gated channel subfamily H member 2	Homo sapiens	109-113
19034039-3	2008	Our results revealed that papaverine dose-dependently decreased the tail currents of HERG channel expressed in HEK293 cells with the IC50 and the Hill coefficient of 0.58 microM and 0.58, respectively, at +20 mV and 36 degrees C. The IC50 for the papaverine-induced blockade of HERG current in Xenopus oocytes was found to decrease progressively relative to depolarization (38.8, 30.0, and 24.8 microM at -10, +20, and +40 mV, respectively).	Papaverine	26-36	potassium voltage-gated channel subfamily H member 2	Homo sapiens	85-89
19034039-3	2008	Our results revealed that papaverine dose-dependently decreased the tail currents of HERG channel expressed in HEK293 cells with the IC50 and the Hill coefficient of 0.58 microM and 0.58, respectively, at +20 mV and 36 degrees C. The IC50 for the papaverine-induced blockade of HERG current in Xenopus oocytes was found to decrease progressively relative to depolarization (38.8, 30.0, and 24.8 microM at -10, +20, and +40 mV, respectively).	Papaverine	26-36	potassium voltage-gated channel subfamily H member 2	Homo sapiens	278-282
19034039-3	2008	Our results revealed that papaverine dose-dependently decreased the tail currents of HERG channel expressed in HEK293 cells with the IC50 and the Hill coefficient of 0.58 microM and 0.58, respectively, at +20 mV and 36 degrees C. The IC50 for the papaverine-induced blockade of HERG current in Xenopus oocytes was found to decrease progressively relative to depolarization (38.8, 30.0, and 24.8 microM at -10, +20, and +40 mV, respectively).	Papaverine	247-257	potassium voltage-gated channel subfamily H member 2	Homo sapiens	85-89
19034039-4	2008	The papaverine-induced blockade of HERG current was time-dependent; the fractional current was 0.92 +/- 0.03 of the control at the beginning of the pulse, but it declined to 0.18 +/- 0.06 after 6 seconds at a test potential of 0 mV.	Papaverine	4-14	potassium voltage-gated channel subfamily H member 2	Homo sapiens	35-39
19034039-5	2008	These results collectively indicate that papaverine blocks HERG channel in a concentration-, voltage-, and time-dependent manner.	Papaverine	41-51	potassium voltage-gated channel subfamily H member 2	Homo sapiens	59-63
19034039-6	2008	Two S6 domain mutations, Y652A and F656A, partially attenuated (Y652A) or abolished (F656A) the hERG current blockade, suggesting that papaverine blocks HERG channel at the pore of the channel.	Papaverine	135-145	potassium voltage-gated channel subfamily H member 2	Homo sapiens	153-157
19034039-8	2008	Therefore, ventricular arrhythmias induced by papaverine could be resulted from the blockage of the HERG channel at the cardiac myocytes.	Papaverine	46-56	potassium voltage-gated channel subfamily H member 2	Homo sapiens	100-104
19057127-0	2008	Hydroxyzine, a first generation H(1)-receptor antagonist, inhibits human ether-a-go-go-related gene (HERG) current and causes syncope in a patient with the HERG mutation.	Hydroxyzine	0-11	potassium voltage-gated channel subfamily H member 2	Homo sapiens	101-105
19057127-0	2008	Hydroxyzine, a first generation H(1)-receptor antagonist, inhibits human ether-a-go-go-related gene (HERG) current and causes syncope in a patient with the HERG mutation.	Hydroxyzine	0-11	potassium voltage-gated channel subfamily H member 2	Homo sapiens	156-160
19057127-2	2008	In this paper, we will report a case of drug-induced long QT syndrome associated with an H(1)-receptor antagonist, hydroxyzine, in which a mutation was identified in the HERG gene.	Hydroxyzine	115-126	potassium voltage-gated channel subfamily H member 2	Homo sapiens	170-174
19057127-7	2008	Hydroxyzine concentration-dependently inhibited both wild-type (WT) and WT/A614V-HERG K(+) currents.	Hydroxyzine	0-11	potassium voltage-gated channel subfamily H member 2	Homo sapiens	81-85
18781376-2	2009	Here, we investigated the mechanism of hERG K(+) channel current (I(hERG)) blockade expressed in HEK-293 cells by sibutramine HCl, a serotonin-norepinephrine reuptake inhibitor.	Serotonin	133-142	potassium voltage-gated channel subfamily H member 2	Homo sapiens	39-73
18781376-2	2009	Here, we investigated the mechanism of hERG K(+) channel current (I(hERG)) blockade expressed in HEK-293 cells by sibutramine HCl, a serotonin-norepinephrine reuptake inhibitor.	Norepinephrine	143-157	potassium voltage-gated channel subfamily H member 2	Homo sapiens	39-73
18805669-7	2008	Berberine could reduce SDF-1 protein level secreted by BMSCs in the microenvironment but not affect CXCR4 expression on HL-60 cell membrane, and we hypothesized that berberine could inhibit AML cells migration partly by reducing the secreting of SDF-1 by BMSCs and inhibiting HERG1 K(+) channels of leukemic cells.	Berberine	0-9	potassium voltage-gated channel subfamily H member 2	Homo sapiens	276-281
18724381-12	2008	In addition, our findings indicate that amiodarone may warrant further investigation as a potential treatment for SQT1.	Amiodarone	40-50	potassium voltage-gated channel subfamily H member 2	Homo sapiens	114-118
18805669-7	2008	Berberine could reduce SDF-1 protein level secreted by BMSCs in the microenvironment but not affect CXCR4 expression on HL-60 cell membrane, and we hypothesized that berberine could inhibit AML cells migration partly by reducing the secreting of SDF-1 by BMSCs and inhibiting HERG1 K(+) channels of leukemic cells.	Berberine	166-175	potassium voltage-gated channel subfamily H member 2	Homo sapiens	276-281
18599551-3	2008	In a concentration-dependent manner (10(-9) to 10(-6) M for 24 h), 5alpha-dihydrotestosterone (5alpha-DHT) increased HERG protein abundance in HEK293 cells stably expressing HERG in the presence of coexpressed cardiac androgen receptor (AR) variant [N-terminal truncated isoform of AR (AR45)].	Dihydrotestosterone	67-93	potassium voltage-gated channel subfamily H member 2	Homo sapiens	117-121
18599551-3	2008	In a concentration-dependent manner (10(-9) to 10(-6) M for 24 h), 5alpha-dihydrotestosterone (5alpha-DHT) increased HERG protein abundance in HEK293 cells stably expressing HERG in the presence of coexpressed cardiac androgen receptor (AR) variant [N-terminal truncated isoform of AR (AR45)].	Dihydrotestosterone	67-93	potassium voltage-gated channel subfamily H member 2	Homo sapiens	174-178
18599551-3	2008	In a concentration-dependent manner (10(-9) to 10(-6) M for 24 h), 5alpha-dihydrotestosterone (5alpha-DHT) increased HERG protein abundance in HEK293 cells stably expressing HERG in the presence of coexpressed cardiac androgen receptor (AR) variant [N-terminal truncated isoform of AR (AR45)].	Dihydrotestosterone	95-105	potassium voltage-gated channel subfamily H member 2	Homo sapiens	117-121
18599551-3	2008	In a concentration-dependent manner (10(-9) to 10(-6) M for 24 h), 5alpha-dihydrotestosterone (5alpha-DHT) increased HERG protein abundance in HEK293 cells stably expressing HERG in the presence of coexpressed cardiac androgen receptor (AR) variant [N-terminal truncated isoform of AR (AR45)].	Dihydrotestosterone	95-105	potassium voltage-gated channel subfamily H member 2	Homo sapiens	174-178
18599551-6	2008	Proteasome inhibitors, N-acetyl-L-leucyl-L-leucyl-L-norleucinal and MG132 prevented the 5alpha-DHT- dependent enhancement of HERG, as did the lysosome inhibitor, bafilomycin A1.	Cysteine	25-31	potassium voltage-gated channel subfamily H member 2	Homo sapiens	125-129
18599551-6	2008	Proteasome inhibitors, N-acetyl-L-leucyl-L-leucyl-L-norleucinal and MG132 prevented the 5alpha-DHT- dependent enhancement of HERG, as did the lysosome inhibitor, bafilomycin A1.	benzyloxycarbonylleucyl-leucyl-leucine aldehyde	68-73	potassium voltage-gated channel subfamily H member 2	Homo sapiens	125-129
18599551-6	2008	Proteasome inhibitors, N-acetyl-L-leucyl-L-leucyl-L-norleucinal and MG132 prevented the 5alpha-DHT- dependent enhancement of HERG, as did the lysosome inhibitor, bafilomycin A1.	Dihydrotestosterone	95-98	potassium voltage-gated channel subfamily H member 2	Homo sapiens	125-129
18599551-7	2008	Consistently, the cycloheximide-based protein chase study showed that 5alpha-DHT prolonged HERG protein half-life.	Cycloheximide	18-31	potassium voltage-gated channel subfamily H member 2	Homo sapiens	91-95
18599551-7	2008	Consistently, the cycloheximide-based protein chase study showed that 5alpha-DHT prolonged HERG protein half-life.	Dihydrotestosterone	70-80	potassium voltage-gated channel subfamily H member 2	Homo sapiens	91-95
18599551-9	2008	Blockade of ERK1/2 with PD98059 and U0126 prevented the effect of androgen on HERG protein abundance.	2-(2-amino-3-methoxyphenyl)-4H-1-benzopyran-4-one	24-31	potassium voltage-gated channel subfamily H member 2	Homo sapiens	78-82
18599551-9	2008	Blockade of ERK1/2 with PD98059 and U0126 prevented the effect of androgen on HERG protein abundance.	U 0126	36-41	potassium voltage-gated channel subfamily H member 2	Homo sapiens	78-82
18599551-10	2008	Functional studies showed that 5alpha-DHT treatment for 24 h increased HERG K+ current density in Chinese hamster ovary cells cotransfected with cDNAs of AR45 and HERG channels.	Dihydrotestosterone	31-41	potassium voltage-gated channel subfamily H member 2	Homo sapiens	71-75
18599551-10	2008	Functional studies showed that 5alpha-DHT treatment for 24 h increased HERG K+ current density in Chinese hamster ovary cells cotransfected with cDNAs of AR45 and HERG channels.	Dihydrotestosterone	31-41	potassium voltage-gated channel subfamily H member 2	Homo sapiens	163-167
19024448-9	2008	Thus, altough the kinetics properties of HERG channels were complicated, the channels kinetics could be indirectly analyzed through differently designed pulse protocols, which provided the basis for investigation on Alanine-scanning mutagenesis and agent action.	Alanine	216-223	potassium voltage-gated channel subfamily H member 2	Homo sapiens	41-45
18791070-3	2008	Here, we show that the hERG1 polymorphism at codon 897, which is read as a Thr instead of a Lys, creates a phosphorylation site for the Akt protein kinase on the Kv11.1 channel protein.	Threonine	75-78	potassium voltage-gated channel subfamily H member 2	Homo sapiens	23-28
18808722-9	2008	KCNH2 SNP K897T was reported to exert a modifying effect on QTc, but it remains controversial whether it confers a risk or protective effect.	qtc	60-63	potassium voltage-gated channel subfamily H member 2	Homo sapiens	0-5
18713925-1	2008	Inhibition of the HERG channel by droperidol depends on channel gating and involves the S6 residue F656.	Droperidol	34-44	potassium voltage-gated channel subfamily H member 2	Homo sapiens	18-22
18713925-1	2008	Inhibition of the HERG channel by droperidol depends on channel gating and involves the S6 residue F656.	f656	99-103	potassium voltage-gated channel subfamily H member 2	Homo sapiens	18-22
18791070-3	2008	Here, we show that the hERG1 polymorphism at codon 897, which is read as a Thr instead of a Lys, creates a phosphorylation site for the Akt protein kinase on the Kv11.1 channel protein.	Threonine	75-78	potassium voltage-gated channel subfamily H member 2	Homo sapiens	162-168
18791070-3	2008	Here, we show that the hERG1 polymorphism at codon 897, which is read as a Thr instead of a Lys, creates a phosphorylation site for the Akt protein kinase on the Kv11.1 channel protein.	Lysine	92-95	potassium voltage-gated channel subfamily H member 2	Homo sapiens	23-28
18791070-3	2008	Here, we show that the hERG1 polymorphism at codon 897, which is read as a Thr instead of a Lys, creates a phosphorylation site for the Akt protein kinase on the Kv11.1 channel protein.	Lysine	92-95	potassium voltage-gated channel subfamily H member 2	Homo sapiens	162-168
18664324-0	2008	Electropharmacological properties of telmisartan in blocking hKv1.5 and HERG potassium channels expressed on Xenopus laevis oocytes.	Telmisartan	37-48	potassium voltage-gated channel subfamily H member 2	Homo sapiens	72-76
18690396-1	2008	In the present study, we investigated the inhibitory action of ketanserin on wild-type (WT) and Y652 mutant human ether-a-go-go-related gene (HERG) potassium channels expressed in Xenopus oocytes and the effects of changing the channel molecular determinants characteristics on the blockade with and without ketanserin intervention using standard two-microelectrode voltage-clamp techniques.	Ketanserin	63-73	potassium voltage-gated channel subfamily H member 2	Homo sapiens	142-146
18690396-5	2008	The results showed that ketanserin blocked WT HERG currents in voltage- and concentration-dependent manner and showed minimal tonic blockade of HERG current evaluated by the envelope of tails test.	Ketanserin	24-34	potassium voltage-gated channel subfamily H member 2	Homo sapiens	46-50
18690396-10	2008	Ketanserin could also modulate the inactivation of HERG channel, which shifted the voltage-dependence of WT HERG channel inactivation curve from (-51.71+/-2.15) mV to (-80.76+/-14.98) mV (P<0.05, n=4).	Ketanserin	0-10	potassium voltage-gated channel subfamily H member 2	Homo sapiens	108-112
18690396-14	2008	In conclusion, ketanserin blocks WT HERG currents in voltage- and concentration-dependent manner and preferentially blocks open-state HERG channels.	Ketanserin	15-25	potassium voltage-gated channel subfamily H member 2	Homo sapiens	36-40
18690396-14	2008	In conclusion, ketanserin blocks WT HERG currents in voltage- and concentration-dependent manner and preferentially blocks open-state HERG channels.	Ketanserin	15-25	potassium voltage-gated channel subfamily H member 2	Homo sapiens	134-138
18664324-1	2008	AIM: The objectives of this study were to investigate the inhibitory action of telmisartan, a selective angiotensin II type 1 receptor antagonist, on hKv1.5 and human ether-a-go-go-related gene (HERG) channels expressed on Xenopus laevis oocytes.	Telmisartan	79-90	potassium voltage-gated channel subfamily H member 2	Homo sapiens	195-199
18664324-5	2008	However, telmisartan exhibited a low affinity for HERG channels (IC50=24.35+/-5.06 micromol/L); the blockade was voltage- and concentration-dependent.	Telmisartan	9-20	potassium voltage-gated channel subfamily H member 2	Homo sapiens	50-54
18458880-10	2008	HERG inactivation kinetics were significantly altered by mianserin without marked effects on channel activation kinetics.	Mianserin	57-66	potassium voltage-gated channel subfamily H member 2	Homo sapiens	0-4
18349188-0	2008	Inhibition of the HERG channel by droperidol depends on channel gating and involves the S6 residue F656.	Droperidol	34-44	potassium voltage-gated channel subfamily H member 2	Homo sapiens	18-22
18520952-0	2008	Rapid kinetic interactions of ranolazine with HERG K+ current.	Ranolazine	30-40	potassium voltage-gated channel subfamily H member 2	Homo sapiens	46-50
18520952-1	2008	Ranolazine, an anti-ischemic agent, inhibits I Kr [encoded by the human ether-a-go-go-related gene (HERG)] and causes a small QT interval prolongation without any proarrhythmic events.	Ranolazine	0-10	potassium voltage-gated channel subfamily H member 2	Homo sapiens	100-104
18520952-2	2008	The objective of this study was to elucidate the biophysical characteristics of inhibition of HERG K+ current (IHERG) by ranolazine.	Ranolazine	121-131	potassium voltage-gated channel subfamily H member 2	Homo sapiens	94-98
18690396-10	2008	Ketanserin could also modulate the inactivation of HERG channel, which shifted the voltage-dependence of WT HERG channel inactivation curve from (-51.71+/-2.15) mV to (-80.76+/-14.98) mV (P<0.05, n=4).	Ketanserin	0-10	potassium voltage-gated channel subfamily H member 2	Homo sapiens	51-55
18679741-3	2008	The HERG potassium channel, which produces the cardiac rapidly activating delayed rectifying K+ current (I(Kr)), is a target for cAMP/PKA regulation.	Cyclic AMP	129-133	potassium voltage-gated channel subfamily H member 2	Homo sapiens	4-8
18679741-7	2008	The functional consequence of AKAP-IS is a reversal of cAMP-dependent regulation of HERG channel activity.	Cyclic AMP	55-59	potassium voltage-gated channel subfamily H member 2	Homo sapiens	84-88
18679741-11	2008	These results suggest that one or more AKAP(s) targets PKA to HERG channels and may contribute to the acute regulation of I(Kr) by cAMP.	Cyclic AMP	131-135	potassium voltage-gated channel subfamily H member 2	Homo sapiens	62-66
18379053-0	2008	HERG K+ channel blockade by the novel antiviral drug sophocarpine.	sophocarpine	53-65	potassium voltage-gated channel subfamily H member 2	Homo sapiens	0-4
18379053-3	2008	The effects of the novel antiviral drug sophocarpine (SC) were examined on stably expressed HERG channels in human embryonic kidney (HEK293) cells using a whole-cell patch clamp technique, Western blot analysis and immunofluorescence experiments.	sophocarpine	40-52	potassium voltage-gated channel subfamily H member 2	Homo sapiens	92-96
18379053-3	2008	The effects of the novel antiviral drug sophocarpine (SC) were examined on stably expressed HERG channels in human embryonic kidney (HEK293) cells using a whole-cell patch clamp technique, Western blot analysis and immunofluorescence experiments.	sophocarpine	54-56	potassium voltage-gated channel subfamily H member 2	Homo sapiens	92-96
18349188-0	2008	Inhibition of the HERG channel by droperidol depends on channel gating and involves the S6 residue F656.	f656	99-103	potassium voltage-gated channel subfamily H member 2	Homo sapiens	18-22
18349188-5	2008	To determine the mechanism underlying these clinical findings, we investigated the effect of droperidol on human HERG potassium channels.	Droperidol	93-103	potassium voltage-gated channel subfamily H member 2	Homo sapiens	113-117
18349188-7	2008	RESULTS: HERG tail currents following test pulses to 50 mV were inhibited by droperidol with an IC(50) of 77.3 +/- 9.6 nM (n = 8).	Droperidol	77-87	potassium voltage-gated channel subfamily H member 2	Homo sapiens	9-13
18349188-9	2008	Droperidol affected HERG channels mainly in their open and inactivated states.	Droperidol	0-10	potassium voltage-gated channel subfamily H member 2	Homo sapiens	20-24
18349188-13	2008	The potency for block of HERG channels by droperidol was significantly decreased with mutation of Phe-656 to Thr or mutation of Ser-631 to Ala, respectively.	Droperidol	42-52	potassium voltage-gated channel subfamily H member 2	Homo sapiens	25-29
18349188-15	2008	CONCLUSIONS: Droperidol potently inhibits transfected HERG channels and this is the probable mechanism for QT prolongation.	Droperidol	13-23	potassium voltage-gated channel subfamily H member 2	Homo sapiens	54-58
18006430-10	2008	Amiodarone inhibited HERG K+ and late Na+ currents with IC50s of 0.8 +/- 0.1 and 3.0 +/- 0.9 microM, respectively.	Amiodarone	0-10	potassium voltage-gated channel subfamily H member 2	Homo sapiens	21-25
17516459-0	2008	Blockade of HERG K+ channel by an antihistamine drug brompheniramine requires the channel binding within the S6 residue Y652 and F656.	Brompheniramine	53-68	potassium voltage-gated channel subfamily H member 2	Homo sapiens	12-16
17516459-2	2008	This study investigated the molecular mechanisms of voltage-dependent inhibition of human ether-a-go-go-related gene (HERG) delayed rectifier K+ channels expressed in HEK-293 cells by brompheniramine, an antihistamine.	Brompheniramine	184-199	potassium voltage-gated channel subfamily H member 2	Homo sapiens	118-122
17516459-3	2008	Brompheniramine inhibited HERG current in a concentration-dependent manner with the half-maximal inhibitory concentration (IC50) value of 1.7 microm at 0 mV.	Brompheniramine	0-15	potassium voltage-gated channel subfamily H member 2	Homo sapiens	26-30
17516459-4	2008	A block of HERG current by brompheniramine was enhanced by progressive membrane depolarization and showed significantly negative shift in voltage-dependence of channel activation.	Brompheniramine	27-42	potassium voltage-gated channel subfamily H member 2	Homo sapiens	11-15
17516459-5	2008	Inhibition of HERG current by brompheniramine showed time-dependence.	Brompheniramine	30-45	potassium voltage-gated channel subfamily H member 2	Homo sapiens	14-18
17516459-7	2008	These results indicate that brompheniramine mainly inhibited the HERG potassium channel through the residue Y652 and F656 and these residues may be an obligatory determinant in inhibition of HERG current for brompheniramine.	Brompheniramine	28-43	potassium voltage-gated channel subfamily H member 2	Homo sapiens	65-69
17516459-7	2008	These results indicate that brompheniramine mainly inhibited the HERG potassium channel through the residue Y652 and F656 and these residues may be an obligatory determinant in inhibition of HERG current for brompheniramine.	Brompheniramine	28-43	potassium voltage-gated channel subfamily H member 2	Homo sapiens	191-195
17516459-7	2008	These results indicate that brompheniramine mainly inhibited the HERG potassium channel through the residue Y652 and F656 and these residues may be an obligatory determinant in inhibition of HERG current for brompheniramine.	Brompheniramine	208-223	potassium voltage-gated channel subfamily H member 2	Homo sapiens	65-69
17516459-7	2008	These results indicate that brompheniramine mainly inhibited the HERG potassium channel through the residue Y652 and F656 and these residues may be an obligatory determinant in inhibition of HERG current for brompheniramine.	Brompheniramine	208-223	potassium voltage-gated channel subfamily H member 2	Homo sapiens	191-195
18181608-0	2008	Incorporation of the HERG potassium channel in a mercury supported lipid bilayer.	Mercury	49-56	potassium voltage-gated channel subfamily H member 2	Homo sapiens	21-25
18191158-0	2008	Protriptyline block of the human ether-a-go-go-related gene (HERG) K+ channel.	Protriptyline	0-13	potassium voltage-gated channel subfamily H member 2	Homo sapiens	61-65
18191158-2	2008	We studied the effects of protriptyline on human ether-a-go-go-related gene (HERG) channels expressed in Xenopus oocytes and HEK293 cells.	Protriptyline	26-39	potassium voltage-gated channel subfamily H member 2	Homo sapiens	77-81
18191158-3	2008	Protriptyline induced a concentration-dependent decrease in current amplitudes at the end of the voltage steps and HERG tail currents.	Protriptyline	0-13	potassium voltage-gated channel subfamily H member 2	Homo sapiens	115-119
18092154-7	2008	Propiverine blocked in a concentration-dependent manner HERG channels expressed in HEK293 cells, as well as native I(Kr) current in ventricular myocytes of guinea pig (IC50 values: 10 microM and 1.8 microM respectively).	propiverine	0-11	potassium voltage-gated channel subfamily H member 2	Homo sapiens	56-60
18181608-1	2008	The HERG potassium channel was incorporated in a mercury-supported tethered bilayer lipid membrane (tBLM) obtained by anchoring a thiolipid monolayer to the mercury surface and by self-assembling a lipid monolayer on top of it from a lipid film spread on the surface of an electrolyte solution.	Mercury	49-56	potassium voltage-gated channel subfamily H member 2	Homo sapiens	4-8
18181608-1	2008	The HERG potassium channel was incorporated in a mercury-supported tethered bilayer lipid membrane (tBLM) obtained by anchoring a thiolipid monolayer to the mercury surface and by self-assembling a lipid monolayer on top of it from a lipid film spread on the surface of an electrolyte solution.	tblm	100-104	potassium voltage-gated channel subfamily H member 2	Homo sapiens	4-8
18191158-4	2008	The IC(50) for protriptyline block of HERG current in Xenopus oocytes progressively decreased relative to the degree of depolarization, from 142.0 microM at -40 mV to 91.7 microM at 0 mV to 52.9 microM at +40 mV.	Protriptyline	15-28	potassium voltage-gated channel subfamily H member 2	Homo sapiens	38-42
18191158-6	2008	The IC(50) for the protriptyline-induced blockade of HERG currents in HEK293 cells at 36 degrees C was 1.18 microM at +20 mV.	Protriptyline	19-32	potassium voltage-gated channel subfamily H member 2	Homo sapiens	53-57
18191158-8	2008	HERG blockade by protriptyline was use-dependent, exhibiting a more rapid onset and a greater steady-state block at higher frequencies of activation.	Protriptyline	17-30	potassium voltage-gated channel subfamily H member 2	Homo sapiens	0-4
18191158-9	2008	Our findings suggest that inhibition of HERG currents may contribute to the arrhythmogenic side effects of protriptyline.	Protriptyline	107-120	potassium voltage-gated channel subfamily H member 2	Homo sapiens	40-44
18057887-0	2008	Extracellular acidification and hyperkalemia induce changes in HERG inhibition by ibutilide.	ibutilide	82-91	potassium voltage-gated channel subfamily H member 2	Homo sapiens	63-67
18181608-1	2008	The HERG potassium channel was incorporated in a mercury-supported tethered bilayer lipid membrane (tBLM) obtained by anchoring a thiolipid monolayer to the mercury surface and by self-assembling a lipid monolayer on top of it from a lipid film spread on the surface of an electrolyte solution.	thiolipid	130-139	potassium voltage-gated channel subfamily H member 2	Homo sapiens	4-8
18057887-2	2008	Our previous studies have shown that extracellular acidosis and hyperkalemia attenuate the HERG-inhibitory effect of proarrhythmic drugs, e.g. quinidine, but have little impact on the less-proarrhythmic drug amiodarone.	Quinidine	143-152	potassium voltage-gated channel subfamily H member 2	Homo sapiens	91-95
18181608-1	2008	The HERG potassium channel was incorporated in a mercury-supported tethered bilayer lipid membrane (tBLM) obtained by anchoring a thiolipid monolayer to the mercury surface and by self-assembling a lipid monolayer on top of it from a lipid film spread on the surface of an electrolyte solution.	Mercury	157-164	potassium voltage-gated channel subfamily H member 2	Homo sapiens	4-8
18181608-2	2008	HERG was then incorporated in this tBLM from its micellar solution in Triton X-100, thus avoiding the use of vesicles in the preparation of the tBLM and of proteoliposomes in channel incorporation.	tblm	35-39	potassium voltage-gated channel subfamily H member 2	Homo sapiens	0-4
18181608-2	2008	HERG was then incorporated in this tBLM from its micellar solution in Triton X-100, thus avoiding the use of vesicles in the preparation of the tBLM and of proteoliposomes in channel incorporation.	Octoxynol	70-82	potassium voltage-gated channel subfamily H member 2	Homo sapiens	0-4
18181608-2	2008	HERG was then incorporated in this tBLM from its micellar solution in Triton X-100, thus avoiding the use of vesicles in the preparation of the tBLM and of proteoliposomes in channel incorporation.	tblm	144-148	potassium voltage-gated channel subfamily H member 2	Homo sapiens	0-4
19088442-0	2008	A highly conserved alanine in the S6 domain of the hERG1 K+ channel is required for normal gating.	Alanine	19-26	potassium voltage-gated channel subfamily H member 2	Homo sapiens	51-56
19088442-3	2008	In hERG1 channels, we determined the functional consequences of substituting this conserved Ala (Ala653) with other hydrophobic or charged amino acids.	ala	92-95	potassium voltage-gated channel subfamily H member 2	Homo sapiens	3-8
19088442-10	2008	Thus, an Ala at position 653 in hERG1 is required for normal voltage dependence of channel gating and a charged residue in this position prevents channel closure.	ala	9-12	potassium voltage-gated channel subfamily H member 2	Homo sapiens	32-37
18357730-0	2008	[Effect of sophocarpine on HERG K+ channels].	sophocarpine	11-23	potassium voltage-gated channel subfamily H member 2	Homo sapiens	27-31
18357730-2	2008	To investigate the effect of sophocarpine (SC) on HERG channel stably expressing in human embryonic kidney-293 (HEK293) cells, whole-cell patch-clamp technique was used to record HERG current and kinetic curves.	sophocarpine	29-41	potassium voltage-gated channel subfamily H member 2	Homo sapiens	50-54
18357730-2	2008	To investigate the effect of sophocarpine (SC) on HERG channel stably expressing in human embryonic kidney-293 (HEK293) cells, whole-cell patch-clamp technique was used to record HERG current and kinetic curves.	sophocarpine	43-45	potassium voltage-gated channel subfamily H member 2	Homo sapiens	50-54
18074444-3	2007	Using the patch clamp technique on the human ether-a-gogo-related gene (HERG) current, the rank order for blockade of the HERG-current (IC(50)) was: sparfloxacin (44 microM)>telithromycin=moxifloxacin=erythromycin (+/-100 microM).	sparfloxacin	149-161	potassium voltage-gated channel subfamily H member 2	Homo sapiens	72-76
18074444-3	2007	Using the patch clamp technique on the human ether-a-gogo-related gene (HERG) current, the rank order for blockade of the HERG-current (IC(50)) was: sparfloxacin (44 microM)>telithromycin=moxifloxacin=erythromycin (+/-100 microM).	sparfloxacin	149-161	potassium voltage-gated channel subfamily H member 2	Homo sapiens	122-126
18074444-3	2007	Using the patch clamp technique on the human ether-a-gogo-related gene (HERG) current, the rank order for blockade of the HERG-current (IC(50)) was: sparfloxacin (44 microM)>telithromycin=moxifloxacin=erythromycin (+/-100 microM).	telithromycin	177-190	potassium voltage-gated channel subfamily H member 2	Homo sapiens	72-76
18074444-3	2007	Using the patch clamp technique on the human ether-a-gogo-related gene (HERG) current, the rank order for blockade of the HERG-current (IC(50)) was: sparfloxacin (44 microM)>telithromycin=moxifloxacin=erythromycin (+/-100 microM).	telithromycin	177-190	potassium voltage-gated channel subfamily H member 2	Homo sapiens	122-126
18074444-3	2007	Using the patch clamp technique on the human ether-a-gogo-related gene (HERG) current, the rank order for blockade of the HERG-current (IC(50)) was: sparfloxacin (44 microM)>telithromycin=moxifloxacin=erythromycin (+/-100 microM).	Moxifloxacin	191-203	potassium voltage-gated channel subfamily H member 2	Homo sapiens	72-76
18074444-3	2007	Using the patch clamp technique on the human ether-a-gogo-related gene (HERG) current, the rank order for blockade of the HERG-current (IC(50)) was: sparfloxacin (44 microM)>telithromycin=moxifloxacin=erythromycin (+/-100 microM).	Moxifloxacin	191-203	potassium voltage-gated channel subfamily H member 2	Homo sapiens	122-126
18074444-3	2007	Using the patch clamp technique on the human ether-a-gogo-related gene (HERG) current, the rank order for blockade of the HERG-current (IC(50)) was: sparfloxacin (44 microM)>telithromycin=moxifloxacin=erythromycin (+/-100 microM).	Erythromycin	204-216	potassium voltage-gated channel subfamily H member 2	Homo sapiens	72-76
18074444-3	2007	Using the patch clamp technique on the human ether-a-gogo-related gene (HERG) current, the rank order for blockade of the HERG-current (IC(50)) was: sparfloxacin (44 microM)>telithromycin=moxifloxacin=erythromycin (+/-100 microM).	Erythromycin	204-216	potassium voltage-gated channel subfamily H member 2	Homo sapiens	122-126
18074444-10	2007	Additional experiments with grepafloxacin indicate that the rank order to detect grepafloxacin-induced long QT was the wedge preparation>the Purkinje fiber>HERG>the isolated heart, where the isolated heart was unable to detect grepafloxacin-induced APD prolongation.	grepafloxacin	81-94	potassium voltage-gated channel subfamily H member 2	Homo sapiens	162-166
18074444-10	2007	Additional experiments with grepafloxacin indicate that the rank order to detect grepafloxacin-induced long QT was the wedge preparation>the Purkinje fiber>HERG>the isolated heart, where the isolated heart was unable to detect grepafloxacin-induced APD prolongation.	grepafloxacin	81-94	potassium voltage-gated channel subfamily H member 2	Homo sapiens	162-166
17826747-2	2007	The present study found that BAPTA-AM rapidly and reversibly suppressed human ether a-go-go-related gene (hERG or Kv11.1) K(+) current, human Kv1.3 and human Kv1.5 channel currents stably expressed in HEK 293 cells, and the effects were not related to Ca(2+) chelation.	1,2-bis(2-aminophenoxy)ethane N,N,N',N'-tetraacetic acid acetoxymethyl ester	29-37	potassium voltage-gated channel subfamily H member 2	Homo sapiens	114-120
18057881-0	2008	The additive effects of the active component of grapefruit juice (naringenin) and antiarrhythmic drugs on HERG inhibition.	naringenin	66-76	potassium voltage-gated channel subfamily H member 2	Homo sapiens	106-110
18057881-1	2008	BACKGROUND: Grapefruit juice causes significant QT prolongation in healthy volunteers and naringenin has been identified as the most potent human ether-a-go-go-related gene (HERG) channel blocker among several dietary flavonoids.	naringenin	90-100	potassium voltage-gated channel subfamily H member 2	Homo sapiens	174-178
18057881-7	2008	Naringenin blocked HERG current dose dependently with an IC(50) of 173.3 +/- 3.1 microM.	naringenin	0-10	potassium voltage-gated channel subfamily H member 2	Homo sapiens	19-23
18057881-8	2008	Naringenin 100 microM alone inhibited HERG current by 31 +/- 6%, and this inhibitory effect was increased with coadministration of 1 or 10 microM antiarrhythmic drugs.	naringenin	0-10	potassium voltage-gated channel subfamily H member 2	Homo sapiens	38-42
18057881-9	2008	When 100 microM naringenin was added to antiarrhythmic drugs, greater HERG inhibition was demonstrated, compared to the current inhibition caused by antiarrhythmic drugs alone.	naringenin	16-26	potassium voltage-gated channel subfamily H member 2	Homo sapiens	70-74
18057881-11	2008	CONCLUSIONS: There is an additive inhibitory effect on HERG current when naringenin is combined with I(Kr)-blocking antiarrhythmic drugs.	naringenin	73-83	potassium voltage-gated channel subfamily H member 2	Homo sapiens	55-59
18057887-2	2008	Our previous studies have shown that extracellular acidosis and hyperkalemia attenuate the HERG-inhibitory effect of proarrhythmic drugs, e.g. quinidine, but have little impact on the less-proarrhythmic drug amiodarone.	Amiodarone	208-218	potassium voltage-gated channel subfamily H member 2	Homo sapiens	91-95
18057887-5	2008	Our results showed that ibutilide was a potent HERG inhibitor.	ibutilide	24-33	potassium voltage-gated channel subfamily H member 2	Homo sapiens	47-51
18057887-10	2008	CONCLUSION: Extracellular acidosis and hyperkalemia attenuate the HERG-inhibitory effect of ibutilide.	ibutilide	92-101	potassium voltage-gated channel subfamily H member 2	Homo sapiens	66-70
18057887-11	2008	The differences in HERG inhibition between acidic and hyperkalemic regions compared to normal regions in the myocardium may result in heterogeneity in repolarization, which may contribute to the proarrhythmic toxicity of ibutilide.	ibutilide	221-230	potassium voltage-gated channel subfamily H member 2	Homo sapiens	19-23
17711440-0	2007	In vivo effects of mutant HERG K+ channel inhibition by disopyramide in patients with a short QT-1 syndrome: a pilot study.	Disopyramide	56-68	potassium voltage-gated channel subfamily H member 2	Homo sapiens	26-30
17965852-0	2007	Anticholinergic antiparkinson drug orphenadrine inhibits HERG channels: block attenuation by mutations of the pore residues Y652 or F656.	Orphenadrine	35-47	potassium voltage-gated channel subfamily H member 2	Homo sapiens	57-61
17965852-5	2007	Orphenadrine inhibits cloned HERG channels in a concentration dependent manner, yielding an IC(50) of 0.85 microM in HEK cells.	Orphenadrine	0-12	potassium voltage-gated channel subfamily H member 2	Homo sapiens	29-33
17965852-11	2007	In conclusion, we show that the anticholinergic agent orphenadrine is an antagonist at HERG channels.	Orphenadrine	54-66	potassium voltage-gated channel subfamily H member 2	Homo sapiens	87-91
17711440-1	2007	INTRODUCTION: Quinidine has been evaluated in patients with a short QT-1 syndrome caused by an IKr gain-of-function mutation of HERG.	Quinidine	14-23	potassium voltage-gated channel subfamily H member 2	Homo sapiens	128-132
17711440-3	2007	The aim of the present study was to test the in vivo effects of disopyramide in patients with short QT-1 syndrome caused by a N588K mutation in HERG.	Disopyramide	64-76	potassium voltage-gated channel subfamily H member 2	Homo sapiens	144-148
17448117-5	2007	In this article, we demonstrate that ERG1-2 channels are also reversibly inhibited by XE991 in the micromolar range (EC(50) 107 microM for ERG1).	10,10-bis(4-pyridinylmethyl)-9(10H)-anthracenone	86-91	potassium voltage-gated channel subfamily H member 2	Homo sapiens	37-43
17768047-0	2007	Discovery of novel and orally active NR2B-selective N-methyl-D-aspartate (NMDA) antagonists, pyridinol derivatives with reduced HERG binding affinity.	N-Methylaspartate	52-72	potassium voltage-gated channel subfamily H member 2	Homo sapiens	128-132
17768047-0	2007	Discovery of novel and orally active NR2B-selective N-methyl-D-aspartate (NMDA) antagonists, pyridinol derivatives with reduced HERG binding affinity.	N-Methylaspartate	74-78	potassium voltage-gated channel subfamily H member 2	Homo sapiens	128-132
17768047-0	2007	Discovery of novel and orally active NR2B-selective N-methyl-D-aspartate (NMDA) antagonists, pyridinol derivatives with reduced HERG binding affinity.	2-hydroxypyridine	93-102	potassium voltage-gated channel subfamily H member 2	Homo sapiens	128-132
17768047-2	2007	Structure-activity relationship investigation led to N-[cis-4-hydroxy-4-(5-hydroxypyridin-2-yl)cyclohexyl]-3-henylpropanamide as an orally active NR2B-subtype selective N-methyl-D-aspartate (NMDA) receptor antagonist with very weak HERG (human ether-a-go-go related gene) binding (IC(50)> 30 microM).	n-[cis-4-hydroxy-4-(5-hydroxypyridin-2-yl)cyclohexyl	53-105	potassium voltage-gated channel subfamily H member 2	Homo sapiens	232-236
17768047-2	2007	Structure-activity relationship investigation led to N-[cis-4-hydroxy-4-(5-hydroxypyridin-2-yl)cyclohexyl]-3-henylpropanamide as an orally active NR2B-subtype selective N-methyl-D-aspartate (NMDA) receptor antagonist with very weak HERG (human ether-a-go-go related gene) binding (IC(50)> 30 microM).	henylpropanamide	109-125	potassium voltage-gated channel subfamily H member 2	Homo sapiens	232-236
17763876-9	2007	Hydrogen peroxide was shown to increase HERG1a K+ current in heterologous expression systems, which constitutes an apoptotic signal.	Hydrogen Peroxide	0-17	potassium voltage-gated channel subfamily H member 2	Homo sapiens	40-45
17622552-0	2007	Phosphatidylinositol 4,5-bisphosphate interactions with the HERG K(+) channel.	Phosphatidylinositol 4,5-Diphosphate	0-37	potassium voltage-gated channel subfamily H member 2	Homo sapiens	60-64
17622552-6	2007	A recently described pathway for regulation of HERG is through channel interaction with the phospholipid phosphatidylinositol 4,5-bisphosphate (PIP2).	phospholipid phosphatidylinositol 4,5-bisphosphate	92-142	potassium voltage-gated channel subfamily H member 2	Homo sapiens	47-51
17622552-6	2007	A recently described pathway for regulation of HERG is through channel interaction with the phospholipid phosphatidylinositol 4,5-bisphosphate (PIP2).	Phosphatidylinositol 4,5-Diphosphate	144-148	potassium voltage-gated channel subfamily H member 2	Homo sapiens	47-51
17624316-3	2007	Functional consequences of oxidative modification of methionine in human ether a go-go related gene 1 (hERG1), which encodes cardiac I(Kr) channels, are unknown.	Methionine	53-63	potassium voltage-gated channel subfamily H member 2	Homo sapiens	103-108
17171344-5	2007	Screening for SCN5A and HERG candidate genes identified a heterozygous missense mutation 1810G-->A in exon 7 of HERG that leads to the substitution of the amino acid glycine by serine (G604S); this mutation was located in the S5/pore region of the HERG protein and was associated with a malignant phenotype.	Glycine	169-176	potassium voltage-gated channel subfamily H member 2	Homo sapiens	24-28
17171344-5	2007	Screening for SCN5A and HERG candidate genes identified a heterozygous missense mutation 1810G-->A in exon 7 of HERG that leads to the substitution of the amino acid glycine by serine (G604S); this mutation was located in the S5/pore region of the HERG protein and was associated with a malignant phenotype.	Glycine	169-176	potassium voltage-gated channel subfamily H member 2	Homo sapiens	115-119
17171344-5	2007	Screening for SCN5A and HERG candidate genes identified a heterozygous missense mutation 1810G-->A in exon 7 of HERG that leads to the substitution of the amino acid glycine by serine (G604S); this mutation was located in the S5/pore region of the HERG protein and was associated with a malignant phenotype.	Glycine	169-176	potassium voltage-gated channel subfamily H member 2	Homo sapiens	115-119
17171344-5	2007	Screening for SCN5A and HERG candidate genes identified a heterozygous missense mutation 1810G-->A in exon 7 of HERG that leads to the substitution of the amino acid glycine by serine (G604S); this mutation was located in the S5/pore region of the HERG protein and was associated with a malignant phenotype.	Serine	180-186	potassium voltage-gated channel subfamily H member 2	Homo sapiens	24-28
17171344-5	2007	Screening for SCN5A and HERG candidate genes identified a heterozygous missense mutation 1810G-->A in exon 7 of HERG that leads to the substitution of the amino acid glycine by serine (G604S); this mutation was located in the S5/pore region of the HERG protein and was associated with a malignant phenotype.	Serine	180-186	potassium voltage-gated channel subfamily H member 2	Homo sapiens	115-119
17171344-5	2007	Screening for SCN5A and HERG candidate genes identified a heterozygous missense mutation 1810G-->A in exon 7 of HERG that leads to the substitution of the amino acid glycine by serine (G604S); this mutation was located in the S5/pore region of the HERG protein and was associated with a malignant phenotype.	Serine	180-186	potassium voltage-gated channel subfamily H member 2	Homo sapiens	115-119
17092964-5	2007	Experiments in HERG-transfected (HERG: human ether-a-gogo-related gene) HEK293 cells (n = 36) demonstrated concentration-dependent block of the rapid component (I(Kr)) of the delayed rectifier potassium current: tail current was decreased 50% at olanzapine 3.8 microM.	Olanzapine	246-256	potassium voltage-gated channel subfamily H member 2	Homo sapiens	15-19
17092964-5	2007	Experiments in HERG-transfected (HERG: human ether-a-gogo-related gene) HEK293 cells (n = 36) demonstrated concentration-dependent block of the rapid component (I(Kr)) of the delayed rectifier potassium current: tail current was decreased 50% at olanzapine 3.8 microM.	Olanzapine	246-256	potassium voltage-gated channel subfamily H member 2	Homo sapiens	33-37
17560554-0	2007	Inhibition of the HERG potassium channel by the tricyclic antidepressant doxepin.	Doxepin	73-80	potassium voltage-gated channel subfamily H member 2	Homo sapiens	18-22
17560554-2	2007	This study investigated the effects on HERG channels of doxepin, a tricyclic antidepressant linked to QT interval prolongation and cardiac arrhythmia.	Doxepin	56-63	potassium voltage-gated channel subfamily H member 2	Homo sapiens	39-43
17560554-4	2007	Doxepin inhibited I(HERG) with an IC(50) value of 6.5+/-1.4 microM and native I(Kr) with an IC(50) of 4.4+/-0.6 microM.	Doxepin	0-7	potassium voltage-gated channel subfamily H member 2	Homo sapiens	20-24
17560554-8	2007	HERG channel blockade is likely to underpin reported cases of QT interval prolongation with doxepin.	Doxepin	92-99	potassium voltage-gated channel subfamily H member 2	Homo sapiens	0-4
17560554-9	2007	Notably, this study also establishes doxepin as an effective inhibitor of mutant (N588K) HERG channels responsible for variant 1 of the short QT syndrome.	Doxepin	37-44	potassium voltage-gated channel subfamily H member 2	Homo sapiens	89-93
17785939-4	2007	Mitemcinal and its metabolites, GM-577 and GM-625, inhibited the human ether-a-go-go-related gene (HERG) tail current in a concentration-dependent manner with IC(50) values of 20.2, 41.7, and 55.0 microM, respectively.	mitemcinal	0-10	potassium voltage-gated channel subfamily H member 2	Homo sapiens	99-103
17785939-4	2007	Mitemcinal and its metabolites, GM-577 and GM-625, inhibited the human ether-a-go-go-related gene (HERG) tail current in a concentration-dependent manner with IC(50) values of 20.2, 41.7, and 55.0 microM, respectively.	gm-577	32-38	potassium voltage-gated channel subfamily H member 2	Homo sapiens	99-103
17610913-5	2007	The compound NS1643 has earlier been reported as an ERG1 channel activator.	1,3-bis(2-hydroxy-5-trifluoromethylphenyl)urea	13-19	potassium voltage-gated channel subfamily H member 2	Homo sapiens	52-56
17610913-6	2007	We found that NS1643 also activates the ERG2 channel; however, the molecular mechanism of the activation differs between the ERG1 and ERG2 channels.	1,3-bis(2-hydroxy-5-trifluoromethylphenyl)urea	14-20	potassium voltage-gated channel subfamily H member 2	Homo sapiens	125-129
18708743-6	2007	Depletion of membrane cholesterol from HEK293 cells expressing Kv11.1 channels using methyl-beta-cyclodextrin (MbetaCD) caused a positive shift of the voltage dependence of activation and an acceleration of deactivation kinetics of Kv11.1 current (I(Kv11.1)).	Cholesterol	22-33	potassium voltage-gated channel subfamily H member 2	Homo sapiens	63-69
18708743-6	2007	Depletion of membrane cholesterol from HEK293 cells expressing Kv11.1 channels using methyl-beta-cyclodextrin (MbetaCD) caused a positive shift of the voltage dependence of activation and an acceleration of deactivation kinetics of Kv11.1 current (I(Kv11.1)).	Cholesterol	22-33	potassium voltage-gated channel subfamily H member 2	Homo sapiens	232-238
18708743-6	2007	Depletion of membrane cholesterol from HEK293 cells expressing Kv11.1 channels using methyl-beta-cyclodextrin (MbetaCD) caused a positive shift of the voltage dependence of activation and an acceleration of deactivation kinetics of Kv11.1 current (I(Kv11.1)).	Cholesterol	22-33	potassium voltage-gated channel subfamily H member 2	Homo sapiens	232-238
18708743-6	2007	Depletion of membrane cholesterol from HEK293 cells expressing Kv11.1 channels using methyl-beta-cyclodextrin (MbetaCD) caused a positive shift of the voltage dependence of activation and an acceleration of deactivation kinetics of Kv11.1 current (I(Kv11.1)).	methyl-beta-cyclodextrin	85-109	potassium voltage-gated channel subfamily H member 2	Homo sapiens	63-69
18708743-6	2007	Depletion of membrane cholesterol from HEK293 cells expressing Kv11.1 channels using methyl-beta-cyclodextrin (MbetaCD) caused a positive shift of the voltage dependence of activation and an acceleration of deactivation kinetics of Kv11.1 current (I(Kv11.1)).	methyl-beta-cyclodextrin	85-109	potassium voltage-gated channel subfamily H member 2	Homo sapiens	232-238
18708743-6	2007	Depletion of membrane cholesterol from HEK293 cells expressing Kv11.1 channels using methyl-beta-cyclodextrin (MbetaCD) caused a positive shift of the voltage dependence of activation and an acceleration of deactivation kinetics of Kv11.1 current (I(Kv11.1)).	methyl-beta-cyclodextrin	85-109	potassium voltage-gated channel subfamily H member 2	Homo sapiens	232-238
18708743-6	2007	Depletion of membrane cholesterol from HEK293 cells expressing Kv11.1 channels using methyl-beta-cyclodextrin (MbetaCD) caused a positive shift of the voltage dependence of activation and an acceleration of deactivation kinetics of Kv11.1 current (I(Kv11.1)).	methyl-beta-cyclodextrin	111-118	potassium voltage-gated channel subfamily H member 2	Homo sapiens	63-69
18708743-6	2007	Depletion of membrane cholesterol from HEK293 cells expressing Kv11.1 channels using methyl-beta-cyclodextrin (MbetaCD) caused a positive shift of the voltage dependence of activation and an acceleration of deactivation kinetics of Kv11.1 current (I(Kv11.1)).	methyl-beta-cyclodextrin	111-118	potassium voltage-gated channel subfamily H member 2	Homo sapiens	232-238
18708743-6	2007	Depletion of membrane cholesterol from HEK293 cells expressing Kv11.1 channels using methyl-beta-cyclodextrin (MbetaCD) caused a positive shift of the voltage dependence of activation and an acceleration of deactivation kinetics of Kv11.1 current (I(Kv11.1)).	methyl-beta-cyclodextrin	111-118	potassium voltage-gated channel subfamily H member 2	Homo sapiens	232-238
18708743-7	2007	Cholesterol loading of HEK293 cells reduced the steep voltage dependence of I(Kv11.1) activation and accelerated the inactivation kinetics of I(Kv11.1).	Cholesterol	0-11	potassium voltage-gated channel subfamily H member 2	Homo sapiens	78-84
18708743-7	2007	Cholesterol loading of HEK293 cells reduced the steep voltage dependence of I(Kv11.1) activation and accelerated the inactivation kinetics of I(Kv11.1).	Cholesterol	0-11	potassium voltage-gated channel subfamily H member 2	Homo sapiens	144-150
18708743-9	2007	We conclude that Kv11.1 protein localizes in cholesterol and sphingolipid enriched membranes and that membrane cholesterol can modulate I(Kv11.1) and I(Kr).	Cholesterol	45-56	potassium voltage-gated channel subfamily H member 2	Homo sapiens	17-23
18708743-9	2007	We conclude that Kv11.1 protein localizes in cholesterol and sphingolipid enriched membranes and that membrane cholesterol can modulate I(Kv11.1) and I(Kr).	Sphingolipids	61-73	potassium voltage-gated channel subfamily H member 2	Homo sapiens	17-23
18708743-9	2007	We conclude that Kv11.1 protein localizes in cholesterol and sphingolipid enriched membranes and that membrane cholesterol can modulate I(Kv11.1) and I(Kr).	Cholesterol	111-122	potassium voltage-gated channel subfamily H member 2	Homo sapiens	17-23
18708743-9	2007	We conclude that Kv11.1 protein localizes in cholesterol and sphingolipid enriched membranes and that membrane cholesterol can modulate I(Kv11.1) and I(Kr).	Cholesterol	111-122	potassium voltage-gated channel subfamily H member 2	Homo sapiens	138-144
17610913-9	2007	In contrast, for ERG1, NS1643 causes a right-ward shift in the voltage-dependent release from inactivation but does not affect time-constants of deactivation.	1,3-bis(2-hydroxy-5-trifluoromethylphenyl)urea	23-29	potassium voltage-gated channel subfamily H member 2	Homo sapiens	17-21
17610913-10	2007	Because of these differences in the responses of ERG1 and ERG2 to NS1643, NS1643 can be used as a pharmacological tool to address ERG channel function.	1,3-bis(2-hydroxy-5-trifluoromethylphenyl)urea	74-80	potassium voltage-gated channel subfamily H member 2	Homo sapiens	49-53
18708743-0	2007	Kv11.1 (ERG1) K+ channels localize in cholesterol and sphingolipid enriched membranes and are modulated by membrane cholesterol.	Cholesterol	38-49	potassium voltage-gated channel subfamily H member 2	Homo sapiens	0-6
18708743-0	2007	Kv11.1 (ERG1) K+ channels localize in cholesterol and sphingolipid enriched membranes and are modulated by membrane cholesterol.	Cholesterol	38-49	potassium voltage-gated channel subfamily H member 2	Homo sapiens	8-12
18708743-0	2007	Kv11.1 (ERG1) K+ channels localize in cholesterol and sphingolipid enriched membranes and are modulated by membrane cholesterol.	Sphingolipids	54-66	potassium voltage-gated channel subfamily H member 2	Homo sapiens	0-6
18708743-0	2007	Kv11.1 (ERG1) K+ channels localize in cholesterol and sphingolipid enriched membranes and are modulated by membrane cholesterol.	Sphingolipids	54-66	potassium voltage-gated channel subfamily H member 2	Homo sapiens	8-12
18708743-0	2007	Kv11.1 (ERG1) K+ channels localize in cholesterol and sphingolipid enriched membranes and are modulated by membrane cholesterol.	Cholesterol	116-127	potassium voltage-gated channel subfamily H member 2	Homo sapiens	0-6
18708743-0	2007	Kv11.1 (ERG1) K+ channels localize in cholesterol and sphingolipid enriched membranes and are modulated by membrane cholesterol.	Cholesterol	116-127	potassium voltage-gated channel subfamily H member 2	Homo sapiens	8-12
18708743-3	2007	Immunocytochemistry and membrane fractionation using discontinuous sucrose density gradients of adult canine ventricular tissue showed that Kv11.1 channel protein localized to both the cell surface and T-tubular sarcolemma.	Sucrose	67-74	potassium voltage-gated channel subfamily H member 2	Homo sapiens	140-146
18708743-4	2007	Furthermore, density gradient membrane fractionation using detergent (Triton X-100) and non-detergent (OptiPrep) methods from canine ventricular myocytes or HEK293 cells demonstrated that Kv11.1 protein, along with MiRP1 and Kv7.1 (KCNQ1) proteins, localize in cholesterol and sphingolipid enriched membrane fractions.	Cholesterol	261-272	potassium voltage-gated channel subfamily H member 2	Homo sapiens	188-194
18708743-4	2007	Furthermore, density gradient membrane fractionation using detergent (Triton X-100) and non-detergent (OptiPrep) methods from canine ventricular myocytes or HEK293 cells demonstrated that Kv11.1 protein, along with MiRP1 and Kv7.1 (KCNQ1) proteins, localize in cholesterol and sphingolipid enriched membrane fractions.	Sphingolipids	277-289	potassium voltage-gated channel subfamily H member 2	Homo sapiens	188-194
18708743-5	2007	In HEK293 cells, Kv11.1 channels, but not long QT-associated mutant G601S-Kv11.1 channels, also localized to cholesterol and sphingolipid enriched membrane fractions.	Cholesterol	109-120	potassium voltage-gated channel subfamily H member 2	Homo sapiens	17-23
18708743-5	2007	In HEK293 cells, Kv11.1 channels, but not long QT-associated mutant G601S-Kv11.1 channels, also localized to cholesterol and sphingolipid enriched membrane fractions.	Sphingolipids	125-137	potassium voltage-gated channel subfamily H member 2	Homo sapiens	17-23
17460149-10	2007	In HERG-transfected COS-7 cells, SM-21 potentiated the ifenprodil-induced blockade of the HERG current.	SM 21	33-38	potassium voltage-gated channel subfamily H member 2	Homo sapiens	3-7
17460149-10	2007	In HERG-transfected COS-7 cells, SM-21 potentiated the ifenprodil-induced blockade of the HERG current.	SM 21	33-38	potassium voltage-gated channel subfamily H member 2	Homo sapiens	90-94
17460149-10	2007	In HERG-transfected COS-7 cells, SM-21 potentiated the ifenprodil-induced blockade of the HERG current.	ifenprodil	55-65	potassium voltage-gated channel subfamily H member 2	Homo sapiens	3-7
17460149-10	2007	In HERG-transfected COS-7 cells, SM-21 potentiated the ifenprodil-induced blockade of the HERG current.	ifenprodil	55-65	potassium voltage-gated channel subfamily H member 2	Homo sapiens	90-94
17641836-2	2007	The functional role of HERG1 K+ channels in leukemic cell proliferation was measured by MTT assay, and cell cycle and apoptosis were analyzed by flow cytometry.	monooxyethylene trimethylolpropane tristearate	88-91	potassium voltage-gated channel subfamily H member 2	Homo sapiens	23-28
17641836-5	2007	In addition, leukemic cell proliferation was dramatically inhibited by HERG K+ channel special inhibitor E-4031.	E 4031	105-111	potassium voltage-gated channel subfamily H member 2	Homo sapiens	71-75
17448117-5	2007	In this article, we demonstrate that ERG1-2 channels are also reversibly inhibited by XE991 in the micromolar range (EC(50) 107 microM for ERG1).	10,10-bis(4-pyridinylmethyl)-9(10H)-anthracenone	86-91	potassium voltage-gated channel subfamily H member 2	Homo sapiens	37-41
18690032-0	2007	Mutational analysis of block and facilitation of HERG current by a class III anti-arrhythmic agent, nifekalant.	nifekalant	100-110	potassium voltage-gated channel subfamily H member 2	Homo sapiens	49-53
17457128-2	2007	Although droperidol potently inhibits human ether-a-go-go-related gene (HERG) channels, the molecular mode of this interaction is unknown.	Droperidol	9-19	potassium voltage-gated channel subfamily H member 2	Homo sapiens	72-76
17457128-5	2007	METHODS: Molecular mechanisms of HERG current inhibition by droperidol were established using two-electrode voltage clamp recordings of Xenopus laevis oocytes expressing wild-type and mutant channels.	Droperidol	60-70	potassium voltage-gated channel subfamily H member 2	Homo sapiens	33-37
17457128-8	2007	RESULTS: Droperidol inhibited currents through HERG wild-type channels with a concentration of half-maximal inhibition of 0.6-0.9 microM.	Droperidol	9-19	potassium voltage-gated channel subfamily H member 2	Homo sapiens	47-51
17457128-14	2007	CONCLUSIONS: Droperidol is a high-affinity blocker of HERG channels.	Droperidol	13-23	potassium voltage-gated channel subfamily H member 2	Homo sapiens	54-58
18690032-3	2007	Besides block, some chemicals such as the class III anti-arrhythmic agent nifekalant stimulate HERG at low potentials by shifting its activation curve towards hyperpolarizing voltages.	nifekalant	74-84	potassium voltage-gated channel subfamily H member 2	Homo sapiens	95-99
18690032-6	2007	Alanine-scanning mutagenesis was performed in the pore region of HERG.	Alanine	0-7	potassium voltage-gated channel subfamily H member 2	Homo sapiens	65-69
17497253-9	2007	Pharmacological treatment has been studied and it could be demonstrated, that some mutant currents may be insufficiently suppressed by drugs targeted to block the specific current such as, e.g., sotalol or ibutilide in patients with a mutation in the IKr-coding gene KCNH2 (HERG).	Sotalol	195-202	potassium voltage-gated channel subfamily H member 2	Homo sapiens	267-272
17497253-9	2007	Pharmacological treatment has been studied and it could be demonstrated, that some mutant currents may be insufficiently suppressed by drugs targeted to block the specific current such as, e.g., sotalol or ibutilide in patients with a mutation in the IKr-coding gene KCNH2 (HERG).	Sotalol	195-202	potassium voltage-gated channel subfamily H member 2	Homo sapiens	274-278
17497253-9	2007	Pharmacological treatment has been studied and it could be demonstrated, that some mutant currents may be insufficiently suppressed by drugs targeted to block the specific current such as, e.g., sotalol or ibutilide in patients with a mutation in the IKr-coding gene KCNH2 (HERG).	ibutilide	206-215	potassium voltage-gated channel subfamily H member 2	Homo sapiens	267-272
17497253-9	2007	Pharmacological treatment has been studied and it could be demonstrated, that some mutant currents may be insufficiently suppressed by drugs targeted to block the specific current such as, e.g., sotalol or ibutilide in patients with a mutation in the IKr-coding gene KCNH2 (HERG).	ibutilide	206-215	potassium voltage-gated channel subfamily H member 2	Homo sapiens	274-278
17376289-0	2007	Inhibitory effects of coronary vasodilator papaverine on heterologously-expressed HERG currents in Xenopus oocytes.	Papaverine	43-53	potassium voltage-gated channel subfamily H member 2	Homo sapiens	82-86
17376289-1	2007	AIM: To characterize the effects of papaverine on HERG channels expressed in Xenopus oocytes as well as cardiac action potential in rabbit ventricular myocytes.	Papaverine	36-46	potassium voltage-gated channel subfamily H member 2	Homo sapiens	50-54
17376289-6	2007	The blockade of papaverine on HERG currents was not voltage-dependent.	Papaverine	16-26	potassium voltage-gated channel subfamily H member 2	Homo sapiens	30-34
17376289-7	2007	The slope conductance measured as a slope of the fully activated HERG current-voltage curves decreased from 78.03+/-4.25 muS of the control to 56.84+/-5.33, 36.06+/-6.53, and 27.09+/-5.50 microS (n=4) by 30, 100, and 300 micromol/L of papaverine, respectively.	Papaverine	235-245	potassium voltage-gated channel subfamily H member 2	Homo sapiens	65-69
17376289-9	2007	Papaverine blocked HERG channels in the closed, open, and inactivated states.	Papaverine	0-10	potassium voltage-gated channel subfamily H member 2	Homo sapiens	19-23
17376289-10	2007	CONCLUSION: These results showed that papaverine blocked HERG channels in a voltage- and state-independent manner, which may most likely be the major mechanism of papaverine-induced cardiac arrhythmia reported in humans.	Papaverine	38-48	potassium voltage-gated channel subfamily H member 2	Homo sapiens	57-61
17376289-10	2007	CONCLUSION: These results showed that papaverine blocked HERG channels in a voltage- and state-independent manner, which may most likely be the major mechanism of papaverine-induced cardiac arrhythmia reported in humans.	Papaverine	163-173	potassium voltage-gated channel subfamily H member 2	Homo sapiens	57-61
17189275-5	2007	KCR1 and the yeast alpha-1,2-glucosyltransferase ALG10 exhibit sequence homology, and like KCR1, ALG10 diminished HERG block by dofetilide.	dofetilide	128-138	potassium voltage-gated channel subfamily H member 2	Homo sapiens	114-118
17489361-0	2007	Maprotiline block of the human ether-a-go-go-related gene (HERG) K+ channel.	Maprotiline	0-11	potassium voltage-gated channel subfamily H member 2	Homo sapiens	59-63
17489361-2	2007	We studied the effects of maprotiline on human ether-a-go-go-related gene (HERG) channels expressed in Xenopus oocytes and HEK293 cells.	Maprotiline	26-37	potassium voltage-gated channel subfamily H member 2	Homo sapiens	75-79
17489361-3	2007	Maprotiline induced a concentration-dependent decrease in current amplitudes at the end of the voltage steps and tail currents of HERG.	Maprotiline	0-11	potassium voltage-gated channel subfamily H member 2	Homo sapiens	130-134
17489361-5	2007	The IC50 for a maprotiline block of HERG current in Xenopus oocytes did not change according to depolarization; 39.5 +/- 3.2 microM at -40 mV and 43.6 +/- 2.8 microM at +40 mV.	Maprotiline	15-26	potassium voltage-gated channel subfamily H member 2	Homo sapiens	36-40
17489361-6	2007	The block of HERG by maprotiline was examined after treatment of trinitrobenzene sulfonic acid (TNBS), an amino-group reagent that neutralizes the positively charged amino-groups of peptide N-terminal and lysine residues.	Maprotiline	21-32	potassium voltage-gated channel subfamily H member 2	Homo sapiens	13-17
17489361-6	2007	The block of HERG by maprotiline was examined after treatment of trinitrobenzene sulfonic acid (TNBS), an amino-group reagent that neutralizes the positively charged amino-groups of peptide N-terminal and lysine residues.	Trinitrobenzenesulfonic Acid	96-100	potassium voltage-gated channel subfamily H member 2	Homo sapiens	13-17
17489361-6	2007	The block of HERG by maprotiline was examined after treatment of trinitrobenzene sulfonic acid (TNBS), an amino-group reagent that neutralizes the positively charged amino-groups of peptide N-terminal and lysine residues.	Lysine	205-211	potassium voltage-gated channel subfamily H member 2	Homo sapiens	13-17
17489361-8	2007	The IC50 for the maprotiline-induced blockade of HERG currents in HEK293 cells at 36 degrees C was 0.13 microM at +20 mV.	Maprotiline	17-28	potassium voltage-gated channel subfamily H member 2	Homo sapiens	49-53
17489361-9	2007	Our findings suggest that the arrhythmogenic side effects of maprotiline are caused by a blockade of HERG and possibly by a blockade of delayed rectifier K+ channel.	Maprotiline	61-72	potassium voltage-gated channel subfamily H member 2	Homo sapiens	101-105
17189275-8	2007	HERG itself is not the target for KCR1-mediated glycosylation because the dofetilide response of glycosylation-deficient HERG(N598Q) was still modulated by KCR1.	dofetilide	74-84	potassium voltage-gated channel subfamily H member 2	Homo sapiens	0-4
17189275-8	2007	HERG itself is not the target for KCR1-mediated glycosylation because the dofetilide response of glycosylation-deficient HERG(N598Q) was still modulated by KCR1.	dofetilide	74-84	potassium voltage-gated channel subfamily H member 2	Homo sapiens	121-125
17518040-0	2007	[Effects of matrine, oxymatrine and resveratrol on HERG channel expression].	matrine	12-19	potassium voltage-gated channel subfamily H member 2	Homo sapiens	51-55
17325511-1	2007	BACKGROUND: Local anesthetics interact with human ether-a-go-go-related gene (HERG) channels via the aromatic amino acids Y652 and F656 in the S6 region.	Amino Acids, Aromatic	101-121	potassium voltage-gated channel subfamily H member 2	Homo sapiens	78-82
17325511-2	2007	This study aimed to establish whether the residues T623, S624, and V625 residing deeper within the pore are also involved in HERG channel block by bupivacaine.	Bupivacaine	147-158	potassium voltage-gated channel subfamily H member 2	Homo sapiens	125-129
17325511-8	2007	Inhibition of HERG tail currents by bupivacaine (300 microm) was reduced by all mutations (P < 0.001).	Bupivacaine	36-47	potassium voltage-gated channel subfamily H member 2	Homo sapiens	14-18
17325511-11	2007	CONCLUSIONS: The authors" results indicate that not only the aromatic residues Y652 and F656 but also residues residing deeper within the pore and close to the selectivity filter of HERG channels are involved in inhibition of HERG channels by the low-affinity blocker bupivacaine.	Bupivacaine	268-279	potassium voltage-gated channel subfamily H member 2	Homo sapiens	182-186
17325511-11	2007	CONCLUSIONS: The authors" results indicate that not only the aromatic residues Y652 and F656 but also residues residing deeper within the pore and close to the selectivity filter of HERG channels are involved in inhibition of HERG channels by the low-affinity blocker bupivacaine.	Bupivacaine	268-279	potassium voltage-gated channel subfamily H member 2	Homo sapiens	226-230
17109852-3	2007	The acute effects of the novel prokinetic prucalopride were examined on heterologously expressed HERG channels in human embryonic kidney (HEK) 293 cells using the whole-cell patch-clamp technique.	prucalopride	42-54	potassium voltage-gated channel subfamily H member 2	Homo sapiens	97-101
17109852-4	2007	Prucalopride inhibited HERG channels in a concentration-dependent manner with an IC(50) of 4.1 microM.	prucalopride	0-12	potassium voltage-gated channel subfamily H member 2	Homo sapiens	23-27
17109852-8	2007	Though prucalopride blocks HERG channels this is unlikely to be significant at clinically relevant concentrations.	prucalopride	7-19	potassium voltage-gated channel subfamily H member 2	Homo sapiens	27-31
17762170-0	2007	Sphingolipid metabolite ceramide causes metabolic perturbation contributing to HERG K+ channel dysfunction.	Sphingolipids	0-12	potassium voltage-gated channel subfamily H member 2	Homo sapiens	79-83
17762170-0	2007	Sphingolipid metabolite ceramide causes metabolic perturbation contributing to HERG K+ channel dysfunction.	Ceramides	24-32	potassium voltage-gated channel subfamily H member 2	Homo sapiens	79-83
17762170-3	2007	To investigate how ceramide is involved in modulating cardiac repolarization, we performed whole-cell patch-clamp studies on HERG current (I(HERG)), a critical determinant of cardiac repolarization, expressed in HEK293 cells.	Ceramides	19-27	potassium voltage-gated channel subfamily H member 2	Homo sapiens	125-129
17762170-11	2007	The inhibitory effect of C2 on I(HERG) was reversed by antioxidants vitamin E or MnTBAP.	Vitamin E	68-77	potassium voltage-gated channel subfamily H member 2	Homo sapiens	33-37
17762170-13	2007	We conclude that ceramide depresses I(HERG) mainly via ROS overproduction and ceramide-induced I(HERG) impairment may contribute to QT prolongation in prolonged myocardial ischemia, heart failure and diabetic cardiomyopathy.	Ceramides	17-25	potassium voltage-gated channel subfamily H member 2	Homo sapiens	38-42
17762170-13	2007	We conclude that ceramide depresses I(HERG) mainly via ROS overproduction and ceramide-induced I(HERG) impairment may contribute to QT prolongation in prolonged myocardial ischemia, heart failure and diabetic cardiomyopathy.	Reactive Oxygen Species	55-58	potassium voltage-gated channel subfamily H member 2	Homo sapiens	38-42
16938156-0	2007	Inhibition of HERG channels by the local anaesthetic articaine.	Carticaine	53-62	potassium voltage-gated channel subfamily H member 2	Homo sapiens	14-18
16938156-2	2007	Human ether-a-go-go-related gene (HERG) potassium channels constitute potential targets involved in cardiotoxic side-effects of various pharmacological agents including amide local anaesthetics.	Amides	169-174	potassium voltage-gated channel subfamily H member 2	Homo sapiens	34-38
16938156-3	2007	The aim of this study was to determine the sensitivity of HERG channels to the inhibitory action of articaine and to further evaluate the effect of the mutations Y652A and F656A in the putative drug-binding region of HERG on the sensitivity for articaine.	Carticaine	100-109	potassium voltage-gated channel subfamily H member 2	Homo sapiens	58-62
16938156-3	2007	The aim of this study was to determine the sensitivity of HERG channels to the inhibitory action of articaine and to further evaluate the effect of the mutations Y652A and F656A in the putative drug-binding region of HERG on the sensitivity for articaine.	Carticaine	100-109	potassium voltage-gated channel subfamily H member 2	Homo sapiens	217-221
16938156-3	2007	The aim of this study was to determine the sensitivity of HERG channels to the inhibitory action of articaine and to further evaluate the effect of the mutations Y652A and F656A in the putative drug-binding region of HERG on the sensitivity for articaine.	Carticaine	245-254	potassium voltage-gated channel subfamily H member 2	Homo sapiens	217-221
16938156-4	2007	METHODS: We examined the inhibition of wild-type and mutant HERG channels, transiently expressed in Chinese hamster ovary cells by articaine.	Carticaine	131-140	potassium voltage-gated channel subfamily H member 2	Homo sapiens	60-64
16938156-6	2007	RESULTS: Inhibition of HERG wild-type and HERG Y652A channels by articaine was concentration dependent and reversible.	Carticaine	65-74	potassium voltage-gated channel subfamily H member 2	Homo sapiens	23-27
16938156-6	2007	RESULTS: Inhibition of HERG wild-type and HERG Y652A channels by articaine was concentration dependent and reversible.	Carticaine	65-74	potassium voltage-gated channel subfamily H member 2	Homo sapiens	42-46
16960444-9	2007	Amiodarone, azimilide, dofetilide, quinidine and sotalol all produced a dose-dependent inhibition of HERG current.	Amiodarone	0-10	potassium voltage-gated channel subfamily H member 2	Homo sapiens	101-105
16960444-9	2007	Amiodarone, azimilide, dofetilide, quinidine and sotalol all produced a dose-dependent inhibition of HERG current.	azimilide	12-21	potassium voltage-gated channel subfamily H member 2	Homo sapiens	101-105
16960444-9	2007	Amiodarone, azimilide, dofetilide, quinidine and sotalol all produced a dose-dependent inhibition of HERG current.	dofetilide	23-33	potassium voltage-gated channel subfamily H member 2	Homo sapiens	101-105
16960444-9	2007	Amiodarone, azimilide, dofetilide, quinidine and sotalol all produced a dose-dependent inhibition of HERG current.	Quinidine	35-44	potassium voltage-gated channel subfamily H member 2	Homo sapiens	101-105
16960444-9	2007	Amiodarone, azimilide, dofetilide, quinidine and sotalol all produced a dose-dependent inhibition of HERG current.	Sotalol	49-56	potassium voltage-gated channel subfamily H member 2	Homo sapiens	101-105
16960444-12	2007	Raising the extracellular potassium to 10 mmol/l, HERG block by azimilide, dofetilide, quinidine and sotalol was significantly decreased, while the block by amiodarone was unchanged.	Potassium	26-35	potassium voltage-gated channel subfamily H member 2	Homo sapiens	50-54
16960444-12	2007	Raising the extracellular potassium to 10 mmol/l, HERG block by azimilide, dofetilide, quinidine and sotalol was significantly decreased, while the block by amiodarone was unchanged.	azimilide	64-73	potassium voltage-gated channel subfamily H member 2	Homo sapiens	50-54
16960444-12	2007	Raising the extracellular potassium to 10 mmol/l, HERG block by azimilide, dofetilide, quinidine and sotalol was significantly decreased, while the block by amiodarone was unchanged.	dofetilide	75-85	potassium voltage-gated channel subfamily H member 2	Homo sapiens	50-54
16960444-12	2007	Raising the extracellular potassium to 10 mmol/l, HERG block by azimilide, dofetilide, quinidine and sotalol was significantly decreased, while the block by amiodarone was unchanged.	Quinidine	87-96	potassium voltage-gated channel subfamily H member 2	Homo sapiens	50-54
16960444-12	2007	Raising the extracellular potassium to 10 mmol/l, HERG block by azimilide, dofetilide, quinidine and sotalol was significantly decreased, while the block by amiodarone was unchanged.	Sotalol	101-108	potassium voltage-gated channel subfamily H member 2	Homo sapiens	50-54
17408310-14	2007	Cisapride was found to bind the human ether-a-go-go-related gene (HERG) potassium channel, which provides a plausible mechanism for QTc interval prolongation/arrhythmia.	Cisapride	0-9	potassium voltage-gated channel subfamily H member 2	Homo sapiens	66-70
17408310-15	2007	Other QTc interval-prolonging/arrhythmic drugs that also bind to HERG provided an analogy for cisapride causing QTc interval prolongation/arrhythmia via this mechanism.	Cisapride	94-103	potassium voltage-gated channel subfamily H member 2	Homo sapiens	65-69
17518040-0	2007	[Effects of matrine, oxymatrine and resveratrol on HERG channel expression].	oxymatrine	21-31	potassium voltage-gated channel subfamily H member 2	Homo sapiens	51-55
17518040-0	2007	[Effects of matrine, oxymatrine and resveratrol on HERG channel expression].	Resveratrol	36-47	potassium voltage-gated channel subfamily H member 2	Homo sapiens	51-55
17518040-1	2007	Because HERG potassium channel has important effects on both proarrhythmia and antiarrhythmia, we use immunofluorescence and Western blotting methods to detect the expression of HERG channel of HERG-HEK cells in different concentrations of matrine, oxymatrine and resveratrol.	matrine	240-247	potassium voltage-gated channel subfamily H member 2	Homo sapiens	178-182
17518040-1	2007	Because HERG potassium channel has important effects on both proarrhythmia and antiarrhythmia, we use immunofluorescence and Western blotting methods to detect the expression of HERG channel of HERG-HEK cells in different concentrations of matrine, oxymatrine and resveratrol.	matrine	240-247	potassium voltage-gated channel subfamily H member 2	Homo sapiens	178-182
17518040-1	2007	Because HERG potassium channel has important effects on both proarrhythmia and antiarrhythmia, we use immunofluorescence and Western blotting methods to detect the expression of HERG channel of HERG-HEK cells in different concentrations of matrine, oxymatrine and resveratrol.	oxymatrine	249-259	potassium voltage-gated channel subfamily H member 2	Homo sapiens	178-182
17518040-1	2007	Because HERG potassium channel has important effects on both proarrhythmia and antiarrhythmia, we use immunofluorescence and Western blotting methods to detect the expression of HERG channel of HERG-HEK cells in different concentrations of matrine, oxymatrine and resveratrol.	oxymatrine	249-259	potassium voltage-gated channel subfamily H member 2	Homo sapiens	178-182
17518040-1	2007	Because HERG potassium channel has important effects on both proarrhythmia and antiarrhythmia, we use immunofluorescence and Western blotting methods to detect the expression of HERG channel of HERG-HEK cells in different concentrations of matrine, oxymatrine and resveratrol.	Resveratrol	264-275	potassium voltage-gated channel subfamily H member 2	Homo sapiens	178-182
17518040-1	2007	Because HERG potassium channel has important effects on both proarrhythmia and antiarrhythmia, we use immunofluorescence and Western blotting methods to detect the expression of HERG channel of HERG-HEK cells in different concentrations of matrine, oxymatrine and resveratrol.	Resveratrol	264-275	potassium voltage-gated channel subfamily H member 2	Homo sapiens	178-182
17518040-2	2007	The findings showed that both matrine (1 micromol x L(-1) ) and oxymatrine ( 1micromol x L (-1) ) increased HERG channel expression ( n = 5, P < 0.	matrine	30-37	potassium voltage-gated channel subfamily H member 2	Homo sapiens	108-112
17518040-2	2007	The findings showed that both matrine (1 micromol x L(-1) ) and oxymatrine ( 1micromol x L (-1) ) increased HERG channel expression ( n = 5, P < 0.	oxymatrine	64-74	potassium voltage-gated channel subfamily H member 2	Homo sapiens	108-112
17518040-3	2007	05 ) , while matrine (100 micromol x L(-1) ) decreased HERG channel expression ( n = 5, P < 0.	matrine	13-20	potassium voltage-gated channel subfamily H member 2	Homo sapiens	55-59
17518040-5	2007	In conclusion, different concentrations of matrine and oxymatrine affect HERG channel expression, while there is no relationship between resveratrol and HERG channel expression.	oxymatrine	55-65	potassium voltage-gated channel subfamily H member 2	Homo sapiens	73-77
17313833-0	2006	[Erythromycin inhibits the proliferation of HERG K+ channel highly expressing cancer cells and shows synergy with anticancer drugs].	Erythromycin	1-13	potassium voltage-gated channel subfamily H member 2	Homo sapiens	44-48
17054943-3	2006	Using the patch clamp technique on the human ether-a-gogo-related gene (HERG) current, the rank order for blockade of the HERG-current (IC(50)) was: sparfloxacin (44 microM)>telithromycin=moxifloxacin=erythromycin (+/-100 microM).	telithromycin	177-190	potassium voltage-gated channel subfamily H member 2	Homo sapiens	122-126
17054943-3	2006	Using the patch clamp technique on the human ether-a-gogo-related gene (HERG) current, the rank order for blockade of the HERG-current (IC(50)) was: sparfloxacin (44 microM)>telithromycin=moxifloxacin=erythromycin (+/-100 microM).	Moxifloxacin	191-203	potassium voltage-gated channel subfamily H member 2	Homo sapiens	72-76
17054943-3	2006	Using the patch clamp technique on the human ether-a-gogo-related gene (HERG) current, the rank order for blockade of the HERG-current (IC(50)) was: sparfloxacin (44 microM)>telithromycin=moxifloxacin=erythromycin (+/-100 microM).	Moxifloxacin	191-203	potassium voltage-gated channel subfamily H member 2	Homo sapiens	122-126
17054943-3	2006	Using the patch clamp technique on the human ether-a-gogo-related gene (HERG) current, the rank order for blockade of the HERG-current (IC(50)) was: sparfloxacin (44 microM)>telithromycin=moxifloxacin=erythromycin (+/-100 microM).	Erythromycin	204-216	potassium voltage-gated channel subfamily H member 2	Homo sapiens	72-76
17054943-3	2006	Using the patch clamp technique on the human ether-a-gogo-related gene (HERG) current, the rank order for blockade of the HERG-current (IC(50)) was: sparfloxacin (44 microM)>telithromycin=moxifloxacin=erythromycin (+/-100 microM).	Erythromycin	204-216	potassium voltage-gated channel subfamily H member 2	Homo sapiens	122-126
17054943-10	2006	Additional experiments with grepafloxacin indicate that the rank order to detect grepafloxacin-induced long QT was the wedge preparation>the Purkinje fiber>HERG>the isolated heart, where the isolated heart was unable to detect grepafloxacin-induced APD prolongation.	grepafloxacin	81-94	potassium voltage-gated channel subfamily H member 2	Homo sapiens	162-166
17054943-10	2006	Additional experiments with grepafloxacin indicate that the rank order to detect grepafloxacin-induced long QT was the wedge preparation>the Purkinje fiber>HERG>the isolated heart, where the isolated heart was unable to detect grepafloxacin-induced APD prolongation.	grepafloxacin	81-94	potassium voltage-gated channel subfamily H member 2	Homo sapiens	162-166
17313833-1	2006	OBJECTIVE: To investigate the effects of erythromycin on the proliferation of the human ether-a-go-go related gene (HERG) K(+) channel highly expressing cancer cells and its synergy with antitumor chemotherapeutic agents.	Erythromycin	41-53	potassium voltage-gated channel subfamily H member 2	Homo sapiens	116-120
17313833-18	2006	CONCLUSION: Erythromycin inhibits the proliferation and induces the apoptosis of cancer cells with high HERG K(+) channel expression.	Erythromycin	12-24	potassium voltage-gated channel subfamily H member 2	Homo sapiens	104-108
17027138-3	2006	Sparfloxacin blocked HERG currents half-maximally (IC(50) value) at a concentration of 33.2 microM, whereas norfloxacin and lomefloxacin each tested at a concentration of 300 microM inhibited HERG currents only by 2.8+/-3.6% and 12.3+/-4.7%, respectively.	sparfloxacin	0-12	potassium voltage-gated channel subfamily H member 2	Homo sapiens	21-25
17027138-3	2006	Sparfloxacin blocked HERG currents half-maximally (IC(50) value) at a concentration of 33.2 microM, whereas norfloxacin and lomefloxacin each tested at a concentration of 300 microM inhibited HERG currents only by 2.8+/-3.6% and 12.3+/-4.7%, respectively.	Norfloxacin	108-119	potassium voltage-gated channel subfamily H member 2	Homo sapiens	192-196
17027138-3	2006	Sparfloxacin blocked HERG currents half-maximally (IC(50) value) at a concentration of 33.2 microM, whereas norfloxacin and lomefloxacin each tested at a concentration of 300 microM inhibited HERG currents only by 2.8+/-3.6% and 12.3+/-4.7%, respectively.	lomefloxacin	124-136	potassium voltage-gated channel subfamily H member 2	Homo sapiens	192-196
17027138-7	2006	The amino group at position C(5) seems to be primarily responsible for the strong HERG current blocking property of sparfloxacin.	sparfloxacin	116-128	potassium voltage-gated channel subfamily H member 2	Homo sapiens	82-86
16942825-7	2006	Quinidine proved to be efficient in prolonging the QT interval and rendering ventricular tachyarrhythmias non-inducible in patients with a mutation in KCNH2 (HERG).	Quinidine	0-9	potassium voltage-gated channel subfamily H member 2	Homo sapiens	151-156
16949586-3	2006	F468C mutation increased IC(50) for astemizole and imipramine but in contrast to HERG channels, only slightly for dofetilide.	dofetilide	114-124	potassium voltage-gated channel subfamily H member 2	Homo sapiens	81-85
16647228-5	2006	To further investigate the electrophysiological basis of the arrhythmogenic potential of chloroform, we analysed inhibitory effects of chloroform on cloned HERG potassium channels, heterologously expressed in Xenopus oocytes and in Human Embryonic Kidney (HEK 293) cells using the double-electrode voltage-clamp technique and the whole-cell patch-clamp technique, respectively.	Chloroform	135-145	potassium voltage-gated channel subfamily H member 2	Homo sapiens	156-160
16647228-6	2006	In HEK cells, chloroform blocked HERG tail currents with an IC(50) of 4.97mM.	Chloroform	14-24	potassium voltage-gated channel subfamily H member 2	Homo sapiens	33-37
16647228-11	2006	Chloroform dependent block of HERG channels was voltage dependent with a decrease of inhibition at more positive membrane potentials.	Chloroform	0-10	potassium voltage-gated channel subfamily H member 2	Homo sapiens	30-34
16647228-13	2006	In summary, chloroform blocked HERG potassium channels probably in a toxicologically relevant concentration.	Chloroform	12-22	potassium voltage-gated channel subfamily H member 2	Homo sapiens	31-35
17054943-3	2006	Using the patch clamp technique on the human ether-a-gogo-related gene (HERG) current, the rank order for blockade of the HERG-current (IC(50)) was: sparfloxacin (44 microM)>telithromycin=moxifloxacin=erythromycin (+/-100 microM).	sparfloxacin	149-161	potassium voltage-gated channel subfamily H member 2	Homo sapiens	72-76
17054943-3	2006	Using the patch clamp technique on the human ether-a-gogo-related gene (HERG) current, the rank order for blockade of the HERG-current (IC(50)) was: sparfloxacin (44 microM)>telithromycin=moxifloxacin=erythromycin (+/-100 microM).	sparfloxacin	149-161	potassium voltage-gated channel subfamily H member 2	Homo sapiens	122-126
17054943-3	2006	Using the patch clamp technique on the human ether-a-gogo-related gene (HERG) current, the rank order for blockade of the HERG-current (IC(50)) was: sparfloxacin (44 microM)>telithromycin=moxifloxacin=erythromycin (+/-100 microM).	telithromycin	177-190	potassium voltage-gated channel subfamily H member 2	Homo sapiens	72-76
16842817-0	2006	Disopyramide is an effective inhibitor of mutant HERG K+ channels involved in variant 1 short QT syndrome.	Disopyramide	0-12	potassium voltage-gated channel subfamily H member 2	Homo sapiens	49-53
16842817-2	2006	The use of implantable cardioverter defibrillators helps to protect SQTS patients from ventricular fibrillation; however, pharmacological treatments to normalise the QT interval are limited: thus far only quinidine has been found to be effective in a subset of patients, with the SQT1 variant.	Quinidine	205-214	potassium voltage-gated channel subfamily H member 2	Homo sapiens	280-284
16842817-4	2006	We demonstrate here that the N588K-HERG mutation only slightly attenuates I(HERG) blockade by the Class Ia antiarrhythmic drug disopyramide (1.5-fold elevation of IC(50)), compared to quinidine (3.5-fold elevation of IC(50)) and the Class III antiarrhythmic drug E-4031 (11.5-fold elevation of IC(50)).	Disopyramide	127-139	potassium voltage-gated channel subfamily H member 2	Homo sapiens	35-39
16842817-4	2006	We demonstrate here that the N588K-HERG mutation only slightly attenuates I(HERG) blockade by the Class Ia antiarrhythmic drug disopyramide (1.5-fold elevation of IC(50)), compared to quinidine (3.5-fold elevation of IC(50)) and the Class III antiarrhythmic drug E-4031 (11.5-fold elevation of IC(50)).	Disopyramide	127-139	potassium voltage-gated channel subfamily H member 2	Homo sapiens	76-80
16842817-4	2006	We demonstrate here that the N588K-HERG mutation only slightly attenuates I(HERG) blockade by the Class Ia antiarrhythmic drug disopyramide (1.5-fold elevation of IC(50)), compared to quinidine (3.5-fold elevation of IC(50)) and the Class III antiarrhythmic drug E-4031 (11.5-fold elevation of IC(50)).	Quinidine	184-193	potassium voltage-gated channel subfamily H member 2	Homo sapiens	35-39
16842817-4	2006	We demonstrate here that the N588K-HERG mutation only slightly attenuates I(HERG) blockade by the Class Ia antiarrhythmic drug disopyramide (1.5-fold elevation of IC(50)), compared to quinidine (3.5-fold elevation of IC(50)) and the Class III antiarrhythmic drug E-4031 (11.5-fold elevation of IC(50)).	E 4031	263-269	potassium voltage-gated channel subfamily H member 2	Homo sapiens	35-39
16842817-5	2006	Thus, of the drugs studied to date, disopyramide is the one least affected by the SQT1 HERG mutation.	Disopyramide	36-48	potassium voltage-gated channel subfamily H member 2	Homo sapiens	82-86
16842817-5	2006	Thus, of the drugs studied to date, disopyramide is the one least affected by the SQT1 HERG mutation.	Disopyramide	36-48	potassium voltage-gated channel subfamily H member 2	Homo sapiens	87-91
16842817-6	2006	Disopyramide is associated with QT prolongation in normal use and our findings provide a rational basis for its evaluation as a treatment for SQT1.	Disopyramide	0-12	potassium voltage-gated channel subfamily H member 2	Homo sapiens	142-146
16942825-7	2006	Quinidine proved to be efficient in prolonging the QT interval and rendering ventricular tachyarrhythmias non-inducible in patients with a mutation in KCNH2 (HERG).	Quinidine	0-9	potassium voltage-gated channel subfamily H member 2	Homo sapiens	158-162
16686685-4	2006	Class III agents like dofetilide, clofilium, and sotalol, which can all cause a drug-induced form of LQT2, significantly lengthen action potential duration at 50% and 90% repolarization in isolated rabbit Purkinje fibers, and can initiate the formation of early afterdepolarizations, and extra beats.	dofetilide	22-32	potassium voltage-gated channel subfamily H member 2	Homo sapiens	101-105
16647228-0	2006	In vitro modulation of HERG channels by organochlorine solvent trichlormethane as potential explanation for proarrhythmic effects of chloroform.	Hydrocarbons, Chlorinated	40-54	potassium voltage-gated channel subfamily H member 2	Homo sapiens	23-27
16647228-0	2006	In vitro modulation of HERG channels by organochlorine solvent trichlormethane as potential explanation for proarrhythmic effects of chloroform.	Chloroform	63-78	potassium voltage-gated channel subfamily H member 2	Homo sapiens	23-27
16647228-0	2006	In vitro modulation of HERG channels by organochlorine solvent trichlormethane as potential explanation for proarrhythmic effects of chloroform.	Chloroform	133-143	potassium voltage-gated channel subfamily H member 2	Homo sapiens	23-27
16860311-0	2006	Blockade of HERG human K+ channel and IKr of guinea pig cardiomyocytes by prochlorperazine.	Prochlorperazine	74-90	potassium voltage-gated channel subfamily H member 2	Homo sapiens	12-16
16860311-2	2006	We studied the effects of prochlorperazine on human ether-a-go-go-related gene (HERG) channels expressed in Xenopus oocytes and also in the delayed rectifier K+ current of guinea pig cardiomyocytes.	Prochlorperazine	26-42	potassium voltage-gated channel subfamily H member 2	Homo sapiens	80-84
16860311-3	2006	Prochlorperazine induced a concentration-dependent decrease in current amplitudes at the end of the voltage steps and tail currents of HERG.	Prochlorperazine	0-16	potassium voltage-gated channel subfamily H member 2	Homo sapiens	135-139
16860311-4	2006	The IC50 for a prochlorperazine block of HERG current in Xenopus oocytes progressively decreased relative to the degree of depolarization, from 42.1 microM at -40 mV to 37.4 microM at 0 mV to 22.6 microM at +40 mV.	Prochlorperazine	15-31	potassium voltage-gated channel subfamily H member 2	Homo sapiens	41-45
16860311-5	2006	The block of HERG by prochlorperazine was use-dependent, exhibiting a more rapid onset and a greater steady-state block at higher frequencies of activation, while there was partial relief of the block with reduced frequencies.	Prochlorperazine	21-37	potassium voltage-gated channel subfamily H member 2	Homo sapiens	13-17
16860311-7	2006	Our findings suggest that the arrhythmogenic side effects of prochlorperazine are caused by a blockade of HERG and the rapid component of the delayed rectifier K+ current rather than by a blockade of the slow component.	Prochlorperazine	61-77	potassium voltage-gated channel subfamily H member 2	Homo sapiens	106-110
16633353-0	2006	Blockade of HERG human K+ channels and IKr of guinea-pig cardiomyocytes by the antipsychotic drug clozapine.	Clozapine	98-107	potassium voltage-gated channel subfamily H member 2	Homo sapiens	12-16
16633353-2	2006	To investigate the arrhythmogenic side effects of clozapine, we studied the impact of clozapine on human ether-a-go-go-related gene (HERG) channels expressed in Xenopus oocytes and HEK293 cells, and on the delayed rectifier K(+) currents of guinea-pig cardiomyocytes.	Clozapine	86-95	potassium voltage-gated channel subfamily H member 2	Homo sapiens	133-137
16633353-3	2006	Clozapine dose-dependently decreased the amplitudes of the currents at the end of voltage steps, and the tail currents of HERG.	Clozapine	0-9	potassium voltage-gated channel subfamily H member 2	Homo sapiens	122-126
16633353-8	2006	Our findings collectively suggest that blockade of HERG currents and I(Kr), but not I(Ks), may contribute to the arrhythmogenic side effects of clozapine.	Clozapine	144-153	potassium voltage-gated channel subfamily H member 2	Homo sapiens	51-55
16616004-2	2006	Our new model suggests three key interactions such that (1) a protonated nitrogen of the channel blocker forms a hydrogen bond with the carbonyl oxygen of HERG residue T623; (2) an aromatic moiety of the channel blocker makes a pi-pi interaction with the aromatic ring of HERG residue Y652; and (3) a hydrophobic group of the channel blocker forms a hydrophobic interaction with the benzene ring of HERG residue F656.	Nitrogen	73-81	potassium voltage-gated channel subfamily H member 2	Homo sapiens	155-159
16616004-2	2006	Our new model suggests three key interactions such that (1) a protonated nitrogen of the channel blocker forms a hydrogen bond with the carbonyl oxygen of HERG residue T623; (2) an aromatic moiety of the channel blocker makes a pi-pi interaction with the aromatic ring of HERG residue Y652; and (3) a hydrophobic group of the channel blocker forms a hydrophobic interaction with the benzene ring of HERG residue F656.	Nitrogen	73-81	potassium voltage-gated channel subfamily H member 2	Homo sapiens	272-276
16616004-2	2006	Our new model suggests three key interactions such that (1) a protonated nitrogen of the channel blocker forms a hydrogen bond with the carbonyl oxygen of HERG residue T623; (2) an aromatic moiety of the channel blocker makes a pi-pi interaction with the aromatic ring of HERG residue Y652; and (3) a hydrophobic group of the channel blocker forms a hydrophobic interaction with the benzene ring of HERG residue F656.	Nitrogen	73-81	potassium voltage-gated channel subfamily H member 2	Homo sapiens	272-276
16616004-2	2006	Our new model suggests three key interactions such that (1) a protonated nitrogen of the channel blocker forms a hydrogen bond with the carbonyl oxygen of HERG residue T623; (2) an aromatic moiety of the channel blocker makes a pi-pi interaction with the aromatic ring of HERG residue Y652; and (3) a hydrophobic group of the channel blocker forms a hydrophobic interaction with the benzene ring of HERG residue F656.	Hydrogen	113-121	potassium voltage-gated channel subfamily H member 2	Homo sapiens	155-159
16616004-2	2006	Our new model suggests three key interactions such that (1) a protonated nitrogen of the channel blocker forms a hydrogen bond with the carbonyl oxygen of HERG residue T623; (2) an aromatic moiety of the channel blocker makes a pi-pi interaction with the aromatic ring of HERG residue Y652; and (3) a hydrophobic group of the channel blocker forms a hydrophobic interaction with the benzene ring of HERG residue F656.	Hydrogen	113-121	potassium voltage-gated channel subfamily H member 2	Homo sapiens	272-276
16616004-2	2006	Our new model suggests three key interactions such that (1) a protonated nitrogen of the channel blocker forms a hydrogen bond with the carbonyl oxygen of HERG residue T623; (2) an aromatic moiety of the channel blocker makes a pi-pi interaction with the aromatic ring of HERG residue Y652; and (3) a hydrophobic group of the channel blocker forms a hydrophobic interaction with the benzene ring of HERG residue F656.	Hydrogen	113-121	potassium voltage-gated channel subfamily H member 2	Homo sapiens	272-276
16616004-2	2006	Our new model suggests three key interactions such that (1) a protonated nitrogen of the channel blocker forms a hydrogen bond with the carbonyl oxygen of HERG residue T623; (2) an aromatic moiety of the channel blocker makes a pi-pi interaction with the aromatic ring of HERG residue Y652; and (3) a hydrophobic group of the channel blocker forms a hydrophobic interaction with the benzene ring of HERG residue F656.	Oxygen	145-151	potassium voltage-gated channel subfamily H member 2	Homo sapiens	155-159
16616004-2	2006	Our new model suggests three key interactions such that (1) a protonated nitrogen of the channel blocker forms a hydrogen bond with the carbonyl oxygen of HERG residue T623; (2) an aromatic moiety of the channel blocker makes a pi-pi interaction with the aromatic ring of HERG residue Y652; and (3) a hydrophobic group of the channel blocker forms a hydrophobic interaction with the benzene ring of HERG residue F656.	Oxygen	145-151	potassium voltage-gated channel subfamily H member 2	Homo sapiens	272-276
16616004-2	2006	Our new model suggests three key interactions such that (1) a protonated nitrogen of the channel blocker forms a hydrogen bond with the carbonyl oxygen of HERG residue T623; (2) an aromatic moiety of the channel blocker makes a pi-pi interaction with the aromatic ring of HERG residue Y652; and (3) a hydrophobic group of the channel blocker forms a hydrophobic interaction with the benzene ring of HERG residue F656.	Oxygen	145-151	potassium voltage-gated channel subfamily H member 2	Homo sapiens	272-276
16616004-2	2006	Our new model suggests three key interactions such that (1) a protonated nitrogen of the channel blocker forms a hydrogen bond with the carbonyl oxygen of HERG residue T623; (2) an aromatic moiety of the channel blocker makes a pi-pi interaction with the aromatic ring of HERG residue Y652; and (3) a hydrophobic group of the channel blocker forms a hydrophobic interaction with the benzene ring of HERG residue F656.	Benzene	383-390	potassium voltage-gated channel subfamily H member 2	Homo sapiens	155-159
16616004-2	2006	Our new model suggests three key interactions such that (1) a protonated nitrogen of the channel blocker forms a hydrogen bond with the carbonyl oxygen of HERG residue T623; (2) an aromatic moiety of the channel blocker makes a pi-pi interaction with the aromatic ring of HERG residue Y652; and (3) a hydrophobic group of the channel blocker forms a hydrophobic interaction with the benzene ring of HERG residue F656.	Benzene	383-390	potassium voltage-gated channel subfamily H member 2	Homo sapiens	272-276
16616004-2	2006	Our new model suggests three key interactions such that (1) a protonated nitrogen of the channel blocker forms a hydrogen bond with the carbonyl oxygen of HERG residue T623; (2) an aromatic moiety of the channel blocker makes a pi-pi interaction with the aromatic ring of HERG residue Y652; and (3) a hydrophobic group of the channel blocker forms a hydrophobic interaction with the benzene ring of HERG residue F656.	Benzene	383-390	potassium voltage-gated channel subfamily H member 2	Homo sapiens	272-276
16616004-3	2006	The previous model assumes two interactions such that (1) a protonated nitrogen of the channel blocker forms a cation-pi interaction with the aromatic ring of HERG residue Y652; and (2) a hydrophobic group of the channel blocker forms a hydrophobic interaction with the benzene ring of HERG residue F656.	Nitrogen	71-79	potassium voltage-gated channel subfamily H member 2	Homo sapiens	159-163
16616004-3	2006	The previous model assumes two interactions such that (1) a protonated nitrogen of the channel blocker forms a cation-pi interaction with the aromatic ring of HERG residue Y652; and (2) a hydrophobic group of the channel blocker forms a hydrophobic interaction with the benzene ring of HERG residue F656.	Nitrogen	71-79	potassium voltage-gated channel subfamily H member 2	Homo sapiens	286-290
16616004-3	2006	The previous model assumes two interactions such that (1) a protonated nitrogen of the channel blocker forms a cation-pi interaction with the aromatic ring of HERG residue Y652; and (2) a hydrophobic group of the channel blocker forms a hydrophobic interaction with the benzene ring of HERG residue F656.	Benzene	270-277	potassium voltage-gated channel subfamily H member 2	Homo sapiens	159-163
16616004-3	2006	The previous model assumes two interactions such that (1) a protonated nitrogen of the channel blocker forms a cation-pi interaction with the aromatic ring of HERG residue Y652; and (2) a hydrophobic group of the channel blocker forms a hydrophobic interaction with the benzene ring of HERG residue F656.	Benzene	270-277	potassium voltage-gated channel subfamily H member 2	Homo sapiens	286-290
16686685-4	2006	Class III agents like dofetilide, clofilium, and sotalol, which can all cause a drug-induced form of LQT2, significantly lengthen action potential duration at 50% and 90% repolarization in isolated rabbit Purkinje fibers, and can initiate the formation of early afterdepolarizations, and extra beats.	clofilium	34-43	potassium voltage-gated channel subfamily H member 2	Homo sapiens	101-105
16686685-4	2006	Class III agents like dofetilide, clofilium, and sotalol, which can all cause a drug-induced form of LQT2, significantly lengthen action potential duration at 50% and 90% repolarization in isolated rabbit Purkinje fibers, and can initiate the formation of early afterdepolarizations, and extra beats.	Sotalol	49-56	potassium voltage-gated channel subfamily H member 2	Homo sapiens	101-105
16542653-0	2006	Inhibition of the HERG K+ channel by the antifungal drug ketoconazole depends on channel gating and involves the S6 residue F656.	Ketoconazole	57-69	potassium voltage-gated channel subfamily H member 2	Homo sapiens	18-22
16542653-1	2006	The mechanism of human ether-a-go-go-related gene (HERG) K+ channel blockade by the antifungal agent ketoconazole was investigated using patch-clamp recording from mammalian cell lines.	Ketoconazole	101-113	potassium voltage-gated channel subfamily H member 2	Homo sapiens	51-55
16542653-2	2006	Ketoconazole inhibited whole-cell HERG current (IHERG) with a clinically relevant half-maximal inhibitory drug concentration (IC50) value of 1.7 microM.	Ketoconazole	0-12	potassium voltage-gated channel subfamily H member 2	Homo sapiens	34-38
16542653-5	2006	Thus, ketoconazole accesses the HERG channel pore-cavity on channel gating, and the S6 residue F656 is an important determinant of ketoconazole binding.	Ketoconazole	6-18	potassium voltage-gated channel subfamily H member 2	Homo sapiens	32-36
16681037-0	2006	Chemical modification of the human ether-a-go-go-related gene (HERG) K+ current by the amino-group reagent trinitrobenzene sulfonic acid.	Trinitrobenzenesulfonic Acid	107-136	potassium voltage-gated channel subfamily H member 2	Homo sapiens	63-67
16681037-1	2006	We investigated the effects of trinitrobenzene sulfonic acid (TNBS), an amino-group reagent, on the human ether-a-go-go-related gene (HERG) K+ channels expressed in Xenopus oocytes.	Trinitrobenzenesulfonic Acid	31-60	potassium voltage-gated channel subfamily H member 2	Homo sapiens	134-138
16681037-1	2006	We investigated the effects of trinitrobenzene sulfonic acid (TNBS), an amino-group reagent, on the human ether-a-go-go-related gene (HERG) K+ channels expressed in Xenopus oocytes.	Trinitrobenzenesulfonic Acid	62-66	potassium voltage-gated channel subfamily H member 2	Homo sapiens	134-138
16681037-3	2006	External application of TNBS at 10 mM for 5 min irreversibly shifted the curves for currents at the end of the pulse and tail currents of HERG to a more negative potential and decreased the maximal amplitude of the I(tail) curve (I(tail,max)).	Trinitrobenzenesulfonic Acid	24-28	potassium voltage-gated channel subfamily H member 2	Homo sapiens	138-142
16681037-5	2006	TNBS shifted the time constant curves of both activation and deactivation of the HERG current to a more hyperpolarized potential; TNBS"s effect was greater on channel opening than channel closing.	Trinitrobenzenesulfonic Acid	0-4	potassium voltage-gated channel subfamily H member 2	Homo sapiens	81-85
16681037-5	2006	TNBS shifted the time constant curves of both activation and deactivation of the HERG current to a more hyperpolarized potential; TNBS"s effect was greater on channel opening than channel closing.	Trinitrobenzenesulfonic Acid	130-134	potassium voltage-gated channel subfamily H member 2	Homo sapiens	81-85
16474415-3	2006	This study was conducted in order to characterise the inhibition of hERG current (I(hERG)) by moxifloxacin, and to determine the role in drug binding of the S6 aromatic amino-acid residues Tyr652 and Phe656.	Moxifloxacin	94-106	potassium voltage-gated channel subfamily H member 2	Homo sapiens	68-89
16534005-8	2006	The median change in QT interval during low-dose epinephrine infusion was -23 ms in the gene-negative group, 78 ms in LQT1, -4 ms in LQT2, and -58 ms in LQT3.	Epinephrine	49-60	potassium voltage-gated channel subfamily H member 2	Homo sapiens	133-137
16446155-0	2006	Erythromycin block of the HERG K+ channel: accessibility to F656 and Y652.	Erythromycin	0-12	potassium voltage-gated channel subfamily H member 2	Homo sapiens	26-30
16446155-3	2006	Here we used whole-cell patch-clamp recording at 37 degrees C from heterologously expressed HERG channels in a mammalian cell line to show that erythromycin either produces a rapid open-state-dependent HERG channel inhibition, or components of both open-state-dependent and closed-state-dependent inhibition.	Erythromycin	144-156	potassium voltage-gated channel subfamily H member 2	Homo sapiens	92-96
16407206-0	2006	Chronic inhibition of cardiac Kir2.1 and HERG potassium channels by celastrol with dual effects on both ion conductivity and protein trafficking.	celastrol	68-77	potassium voltage-gated channel subfamily H member 2	Homo sapiens	41-45
16506891-0	2006	Evaluation of the rubidium efflux assay for preclinical identification of HERG blockade.	Rubidium	18-26	potassium voltage-gated channel subfamily H member 2	Homo sapiens	74-78
16314852-6	2006	Carvedilol (nonselective), propranolol (nonselective) and ICI 118551 (beta(2)-selective) inhibited HERG current in a concentration-dependent manner (IC(50) 0.51, 3.9 and 9.2 microM, respectively).	Carvedilol	0-10	potassium voltage-gated channel subfamily H member 2	Homo sapiens	99-103
16314852-6	2006	Carvedilol (nonselective), propranolol (nonselective) and ICI 118551 (beta(2)-selective) inhibited HERG current in a concentration-dependent manner (IC(50) 0.51, 3.9 and 9.2 microM, respectively).	Propranolol	27-38	potassium voltage-gated channel subfamily H member 2	Homo sapiens	99-103
16314852-6	2006	Carvedilol (nonselective), propranolol (nonselective) and ICI 118551 (beta(2)-selective) inhibited HERG current in a concentration-dependent manner (IC(50) 0.51, 3.9 and 9.2 microM, respectively).	ICI 118551	58-68	potassium voltage-gated channel subfamily H member 2	Homo sapiens	99-103
16314852-9	2006	Inhibition of HERG current by carvedilol, propranolol and ICI 118551 was partially but significantly attenuated in Y652A and F656C mutant channels.	Carvedilol	30-40	potassium voltage-gated channel subfamily H member 2	Homo sapiens	14-18
16314852-9	2006	Inhibition of HERG current by carvedilol, propranolol and ICI 118551 was partially but significantly attenuated in Y652A and F656C mutant channels.	Propranolol	42-53	potassium voltage-gated channel subfamily H member 2	Homo sapiens	14-18
16278312-5	2006	Since two of the drugs that were ineffective I(HERG) blockers, arsenic trioxide and pentamidine, have been associated with cardiac repolarization delays (QT interval lengthening) and torsades de pointes ventricular arrhythmias in patients, we chose to evaluate them further using the isolated perfused rabbit heart model.	Arsenic Trioxide	63-79	potassium voltage-gated channel subfamily H member 2	Homo sapiens	47-51
16278312-5	2006	Since two of the drugs that were ineffective I(HERG) blockers, arsenic trioxide and pentamidine, have been associated with cardiac repolarization delays (QT interval lengthening) and torsades de pointes ventricular arrhythmias in patients, we chose to evaluate them further using the isolated perfused rabbit heart model.	Pentamidine	84-95	potassium voltage-gated channel subfamily H member 2	Homo sapiens	47-51
16480714-7	2006	The HERG-mediated potassium and the SCN5A-mediated sodium currents, however, were only slightly reduced by estradiol at concentrations of up to 30 microM.	Potassium	18-27	potassium voltage-gated channel subfamily H member 2	Homo sapiens	4-8
16480714-7	2006	The HERG-mediated potassium and the SCN5A-mediated sodium currents, however, were only slightly reduced by estradiol at concentrations of up to 30 microM.	Estradiol	107-116	potassium voltage-gated channel subfamily H member 2	Homo sapiens	4-8
16446155-3	2006	Here we used whole-cell patch-clamp recording at 37 degrees C from heterologously expressed HERG channels in a mammalian cell line to show that erythromycin either produces a rapid open-state-dependent HERG channel inhibition, or components of both open-state-dependent and closed-state-dependent inhibition.	Erythromycin	144-156	potassium voltage-gated channel subfamily H member 2	Homo sapiens	202-206
16446155-4	2006	Alanine-substitution of HERG"s canonical determinants of blockade revealed that Y652 was not important as a molecular determinant of blockade, and that mutation of F656 resulted in only weak attenuation of inhibition.	Alanine	0-7	potassium voltage-gated channel subfamily H member 2	Homo sapiens	24-28
16506891-3	2006	We evaluated the rubidium efflux assay for its ability to determine block of the hERG potassium channel.	Rubidium	17-25	potassium voltage-gated channel subfamily H member 2	Homo sapiens	81-85
16291873-0	2006	Drug binding interactions in the inner cavity of HERG channels: molecular insights from structure-activity relationships of clofilium and ibutilide analogs.	clofilium	124-133	potassium voltage-gated channel subfamily H member 2	Homo sapiens	49-53
16291873-0	2006	Drug binding interactions in the inner cavity of HERG channels: molecular insights from structure-activity relationships of clofilium and ibutilide analogs.	ibutilide	138-147	potassium voltage-gated channel subfamily H member 2	Homo sapiens	49-53
16368812-3	2006	To clarify the mechanisms of anesthetics on HERG channels, we monitored the electrocardiogram and measured QT intervals in the guinea pig in the presence of sevoflurane and propofol.	Propofol	173-181	potassium voltage-gated channel subfamily H member 2	Homo sapiens	44-48
16368812-7	2006	Sevoflurane (1%-4%), in a dose-dependent manner, inhibited the HERG outward tail currents (9.7%-26.6%), whereas steady-state currents were inhibited only at large concentrations.	Sevoflurane	0-11	potassium voltage-gated channel subfamily H member 2	Homo sapiens	63-67
16368812-10	2006	In conclusion, compared with steady-state currents, sevoflurane was more potent in inhibiting the outward tail currents, suggesting that sevoflurane may modulate the HERG channel kinetics in its inactivated state.	Sevoflurane	52-63	potassium voltage-gated channel subfamily H member 2	Homo sapiens	166-170
16368812-10	2006	In conclusion, compared with steady-state currents, sevoflurane was more potent in inhibiting the outward tail currents, suggesting that sevoflurane may modulate the HERG channel kinetics in its inactivated state.	Sevoflurane	137-148	potassium voltage-gated channel subfamily H member 2	Homo sapiens	166-170
16472284-4	2006	DNA samples were genotyped for the nucleotide 2690 A>C variation of the KCNH2 gene, corresponding to the KCNH2 K(lysine)897T(threonine) amino acid polymorphism.	Lysine	116-122	potassium voltage-gated channel subfamily H member 2	Homo sapiens	75-80
16423345-2	2006	Here we investigate the molecular mechanisms of voltage-dependent block of human ether-a-go-go-related gene (HERG) K+ channels expressed in cells HEK-293 and Xenopus oocytes by maprotiline.	Maprotiline	177-188	potassium voltage-gated channel subfamily H member 2	Homo sapiens	109-113
16423345-4	2006	Block of HERG expressed in oocytes by maprotiline was enhanced by progressive membrane depolarization and accompanied by a negative shift in the voltage dependence of channel activation.	Maprotiline	38-49	potassium voltage-gated channel subfamily H member 2	Homo sapiens	9-13
16423345-6	2006	The mutation Y652A inverted the voltage dependence of HERG channel block by maprotiline.	Maprotiline	76-87	potassium voltage-gated channel subfamily H member 2	Homo sapiens	54-58
16611127-9	2006	It has been proposed that phenytoin affects the embryonic heart by inhibition of the human-ether-a-go-go (HERG) potassium channel.	Phenytoin	26-35	potassium voltage-gated channel subfamily H member 2	Homo sapiens	85-104
16611127-9	2006	It has been proposed that phenytoin affects the embryonic heart by inhibition of the human-ether-a-go-go (HERG) potassium channel.	Phenytoin	26-35	potassium voltage-gated channel subfamily H member 2	Homo sapiens	106-110
16424781-0	2006	Block of HERG channels by berberine: mechanisms of voltage- and state-dependence probed with site-directed mutant channels.	Berberine	26-35	potassium voltage-gated channel subfamily H member 2	Homo sapiens	9-13
16423345-0	2006	Inhibition of cardiac HERG potassium channels by antidepressant maprotiline.	Maprotiline	64-75	potassium voltage-gated channel subfamily H member 2	Homo sapiens	22-26
16288909-0	2006	Clemastine, a conventional antihistamine, is a high potency inhibitor of the HERG K+ channel.	Clemastine	0-10	potassium voltage-gated channel subfamily H member 2	Homo sapiens	77-81
16288909-2	2006	This study investigated the effects on HERG channel current (IHERG) of clemastine, a "conventional" antihistamine that has been associated with delayed ventricular repolarization in vitro, but for which no adverse effects on the human QT interval have been reported.	Clemastine	71-81	potassium voltage-gated channel subfamily H member 2	Homo sapiens	39-43
16288909-8	2006	We conclude that clemastine is a high potency inhibitor of IHERG, that this action is contingent upon channel gating and that clemastine interacts with a high affinity drug-binding site in the HERG channel pore cavity.	Clemastine	17-27	potassium voltage-gated channel subfamily H member 2	Homo sapiens	60-64
16288909-9	2006	The disparity between clemastine"s potent IHERG inhibition and a lack of QT-prolongation in normal clinical use underscores the need to interpret HERG IC50 data for novel compounds in the context of information from other safety assays.	Clemastine	22-32	potassium voltage-gated channel subfamily H member 2	Homo sapiens	43-47
16472284-4	2006	DNA samples were genotyped for the nucleotide 2690 A>C variation of the KCNH2 gene, corresponding to the KCNH2 K(lysine)897T(threonine) amino acid polymorphism.	Lysine	116-122	potassium voltage-gated channel subfamily H member 2	Homo sapiens	108-113
16472284-4	2006	DNA samples were genotyped for the nucleotide 2690 A>C variation of the KCNH2 gene, corresponding to the KCNH2 K(lysine)897T(threonine) amino acid polymorphism.	Threonine	128-137	potassium voltage-gated channel subfamily H member 2	Homo sapiens	75-80
16472284-4	2006	DNA samples were genotyped for the nucleotide 2690 A>C variation of the KCNH2 gene, corresponding to the KCNH2 K(lysine)897T(threonine) amino acid polymorphism.	Threonine	128-137	potassium voltage-gated channel subfamily H member 2	Homo sapiens	108-113
16219910-10	2006	The effect could be reverted by application of the specific HERG channel inhibitor 4"-[[1-[2-(6-methyl-2-pyridyl)ethyl]-4-piperidinyl]carbonyl]-methanesulfonanilide (E-4031) at 100 nM.	4"-[[1-[2-(6-methyl-2-pyridyl)ethyl]-4-piperidinyl]carbonyl]-methanesulfonanilide	83-164	potassium voltage-gated channel subfamily H member 2	Homo sapiens	60-64
16219910-10	2006	The effect could be reverted by application of the specific HERG channel inhibitor 4"-[[1-[2-(6-methyl-2-pyridyl)ethyl]-4-piperidinyl]carbonyl]-methanesulfonanilide (E-4031) at 100 nM.	E 4031	166-172	potassium voltage-gated channel subfamily H member 2	Homo sapiens	60-64
16219910-13	2006	In conclusion, HERG channel activation by small molecules such as NS1643 increases the repolarization reserve and presents an interesting new antiarrhythmic approach.	1,3-bis(2-hydroxy-5-trifluoromethylphenyl)urea	66-72	potassium voltage-gated channel subfamily H member 2	Homo sapiens	15-19
16226079-11	2005	Furthermore, in patients with a mutation in HERG (SQT1), quinidine rendered ventricular tachyarrhythmias noninducible and restored the QT interval/heart rate relationship toward a reference range.	Quinidine	57-66	potassium voltage-gated channel subfamily H member 2	Homo sapiens	44-48
15987770-0	2005	{Omega}-3 and {omega}-6 polyunsaturated fatty acids block HERG channels.	{omega}-3 and {omega}-6 polyunsaturated fatty acids	0-51	potassium voltage-gated channel subfamily H member 2	Homo sapiens	58-62
15987770-3	2005	In this study we have analyzed the effects of arachidonic acid (AA, omega-6) and docosahexaenoic acid (DHA, omega-3) on HERG channels stably expressed in Chinese hamster ovary cells by using the whole cell patch-clamp technique.	Arachidonic Acid	46-62	potassium voltage-gated channel subfamily H member 2	Homo sapiens	120-124
15987770-3	2005	In this study we have analyzed the effects of arachidonic acid (AA, omega-6) and docosahexaenoic acid (DHA, omega-3) on HERG channels stably expressed in Chinese hamster ovary cells by using the whole cell patch-clamp technique.	Docosahexaenoic Acids	81-101	potassium voltage-gated channel subfamily H member 2	Homo sapiens	120-124
15987770-3	2005	In this study we have analyzed the effects of arachidonic acid (AA, omega-6) and docosahexaenoic acid (DHA, omega-3) on HERG channels stably expressed in Chinese hamster ovary cells by using the whole cell patch-clamp technique.	Docosahexaenoic Acids	103-106	potassium voltage-gated channel subfamily H member 2	Homo sapiens	120-124
15987770-3	2005	In this study we have analyzed the effects of arachidonic acid (AA, omega-6) and docosahexaenoic acid (DHA, omega-3) on HERG channels stably expressed in Chinese hamster ovary cells by using the whole cell patch-clamp technique.	omega-3	108-115	potassium voltage-gated channel subfamily H member 2	Homo sapiens	120-124
15987770-4	2005	At 10 microM, AA and DHA blocked HERG channels, at the end of 5-s pulses to -10 mV, to a similar extent (37.7 +/- 2.4% vs. 50.2 +/- 8.1%, n = 7-10, P > 0.05).	Docosahexaenoic Acids	21-24	potassium voltage-gated channel subfamily H member 2	Homo sapiens	33-37
15987770-10	2005	Finally, both AA and DHA induced a use-dependent inhibition of HERG channels.	Docosahexaenoic Acids	21-24	potassium voltage-gated channel subfamily H member 2	Homo sapiens	63-67
16309205-3	2005	Microarray analysis and confocal microscopy indicated that there was overexpression of the ether-a-gogo gene (HERG) and the inwardly rectifying potassium channel gene (TWIK) in a human epidermal KB and human liver BEL-7404 carcinoma cell line series selected for cisplatin resistance.	Cisplatin	263-272	potassium voltage-gated channel subfamily H member 2	Homo sapiens	110-114
16309205-5	2005	For these reasons, we conducted cell proliferation studies in the presence of either antibodies directed against the detected K+ channels, omeprazole (a H+ pump inhibitor) or a specific inhibitor of the HERG channel (WAY-123398-A-5).	way-123398-a	217-229	potassium voltage-gated channel subfamily H member 2	Homo sapiens	203-207
16120615-7	2005	Chromosomal integration of ERG1 ERG7 at their loci in erg26-1ts ets1-1 and erg26-1ts and ets2-1 mutants, respectively, results in the loss of accumulation of squalene and squalene epoxide, re-accumulation of 4-carboxysterols and cell inviability at high temperature.	Squalene	158-166	potassium voltage-gated channel subfamily H member 2	Homo sapiens	27-31
16120615-7	2005	Chromosomal integration of ERG1 ERG7 at their loci in erg26-1ts ets1-1 and erg26-1ts and ets2-1 mutants, respectively, results in the loss of accumulation of squalene and squalene epoxide, re-accumulation of 4-carboxysterols and cell inviability at high temperature.	oxidosqualene	171-187	potassium voltage-gated channel subfamily H member 2	Homo sapiens	27-31
16120615-7	2005	Chromosomal integration of ERG1 ERG7 at their loci in erg26-1ts ets1-1 and erg26-1ts and ets2-1 mutants, respectively, results in the loss of accumulation of squalene and squalene epoxide, re-accumulation of 4-carboxysterols and cell inviability at high temperature.	4-carboxysterols	208-224	potassium voltage-gated channel subfamily H member 2	Homo sapiens	27-31
16120615-10	2005	We have mapped mutations within the erg1-1/ets1-1 (G247D) and erg7-1/ets2-1 (D530N, V615E) alleles that suppress the inviability of erg26-1ts at high temperature, and cause accumulation of sterol intermediates and decreased enzymatic activities.	Sterols	189-195	potassium voltage-gated channel subfamily H member 2	Homo sapiens	36-42
16120615-11	2005	Finally using erg1-1 and erg7-1 mutant strains, we demonstrate that the expression of the ERG25/26/27 genes required for zymosterol biosynthesis are coordinately transcriptionally regulated, along with ERG1 and ERG7, in response to blocks in sterol biosynthesis.	zymosterol	121-131	potassium voltage-gated channel subfamily H member 2	Homo sapiens	14-20
16120615-11	2005	Finally using erg1-1 and erg7-1 mutant strains, we demonstrate that the expression of the ERG25/26/27 genes required for zymosterol biosynthesis are coordinately transcriptionally regulated, along with ERG1 and ERG7, in response to blocks in sterol biosynthesis.	zymosterol	121-131	potassium voltage-gated channel subfamily H member 2	Homo sapiens	202-206
16120615-11	2005	Finally using erg1-1 and erg7-1 mutant strains, we demonstrate that the expression of the ERG25/26/27 genes required for zymosterol biosynthesis are coordinately transcriptionally regulated, along with ERG1 and ERG7, in response to blocks in sterol biosynthesis.	Sterols	125-131	potassium voltage-gated channel subfamily H member 2	Homo sapiens	202-206
16220205-1	2005	We studied the effects of Chinese traditional medicine rhynchophylline (Rhy) on human ether-a-go-go related gene (HERG) channel and characterized the electrophysiological properties of Rhy"s pharmacological effect on HERG channel using Xenopus oocytes.	rhyncophylline	55-70	potassium voltage-gated channel subfamily H member 2	Homo sapiens	114-118
16166152-0	2005	Tryptophan scanning mutagenesis of the HERG K+ channel: the S4 domain is loosely packed and likely to be lipid exposed.	Tryptophan	0-10	potassium voltage-gated channel subfamily H member 2	Homo sapiens	39-43
16263765-0	2005	Downregulation of the HERG (KCNH2) K(+) channel by ceramide: evidence for ubiquitin-mediated lysosomal degradation.	Ceramides	51-59	potassium voltage-gated channel subfamily H member 2	Homo sapiens	22-26
16263765-0	2005	Downregulation of the HERG (KCNH2) K(+) channel by ceramide: evidence for ubiquitin-mediated lysosomal degradation.	Ceramides	51-59	potassium voltage-gated channel subfamily H member 2	Homo sapiens	28-33
16263765-5	2005	Here we show, using stable HERG-expressing HEK 293 cells, that ceramide evokes a time-dependent decrease in HERG current which was not attributable to a change in gating properties of the channel.	Ceramides	63-71	potassium voltage-gated channel subfamily H member 2	Homo sapiens	27-31
16263765-5	2005	Here we show, using stable HERG-expressing HEK 293 cells, that ceramide evokes a time-dependent decrease in HERG current which was not attributable to a change in gating properties of the channel.	Ceramides	63-71	potassium voltage-gated channel subfamily H member 2	Homo sapiens	108-112
16263765-6	2005	Surface expression of the HERG channel protein was reduced by ceramide as shown by biotinylation of surface proteins, western blotting and immunocytochemistry.	Ceramides	62-70	potassium voltage-gated channel subfamily H member 2	Homo sapiens	26-30
16263765-7	2005	The rapid decline in HERG protein after ceramide stimulation was due to protein ubiquitylation and its association with lysosomes.	Ceramides	40-48	potassium voltage-gated channel subfamily H member 2	Homo sapiens	21-25
16263765-8	2005	The results demonstrate that the surface expression of HERG is strictly regulated, and that ceramide modifies HERG currents and targets the protein for lysosomal degradation.	Ceramides	92-100	potassium voltage-gated channel subfamily H member 2	Homo sapiens	110-114
16260841-0	2005	Coupled K+-water flux through the HERG potassium channel measured by an osmotic pulse method.	Water	11-16	potassium voltage-gated channel subfamily H member 2	Homo sapiens	34-38
16226079-11	2005	Furthermore, in patients with a mutation in HERG (SQT1), quinidine rendered ventricular tachyarrhythmias noninducible and restored the QT interval/heart rate relationship toward a reference range.	Quinidine	57-66	potassium voltage-gated channel subfamily H member 2	Homo sapiens	50-54
16265869-4	2005	The final result of sequencing showed a missense mutation, affecting codon 568 in exon 7 of the KCNH2 (HERG) gene, leading to a tryptophan-cysteine change in the amino acid chain.	Tryptophan	128-138	potassium voltage-gated channel subfamily H member 2	Homo sapiens	96-101
16265869-4	2005	The final result of sequencing showed a missense mutation, affecting codon 568 in exon 7 of the KCNH2 (HERG) gene, leading to a tryptophan-cysteine change in the amino acid chain.	Tryptophan	128-138	potassium voltage-gated channel subfamily H member 2	Homo sapiens	103-107
16265869-4	2005	The final result of sequencing showed a missense mutation, affecting codon 568 in exon 7 of the KCNH2 (HERG) gene, leading to a tryptophan-cysteine change in the amino acid chain.	Cysteine	139-147	potassium voltage-gated channel subfamily H member 2	Homo sapiens	96-101
16265869-4	2005	The final result of sequencing showed a missense mutation, affecting codon 568 in exon 7 of the KCNH2 (HERG) gene, leading to a tryptophan-cysteine change in the amino acid chain.	Cysteine	139-147	potassium voltage-gated channel subfamily H member 2	Homo sapiens	103-107
15967876-0	2005	Intracellular K+ is required for the inactivation-induced high-affinity binding of cisapride to HERG channels.	Cisapride	83-92	potassium voltage-gated channel subfamily H member 2	Homo sapiens	96-100
15983462-1	2005	BACKGROUND: Human ether-a-go-go-related gene (HERG) potassium channels constitute a potential target involved in cardiotoxic side effects of amino-amide local anesthetics.	hydrazinide	141-152	potassium voltage-gated channel subfamily H member 2	Homo sapiens	46-50
15983462-3	2005	The aim of this study was to determine the effect of the mutations Y652A and F656A in the putative drug binding region of HERG on the inhibition by bupivacaine, ropivacaine, and mepivacaine.	Bupivacaine	148-159	potassium voltage-gated channel subfamily H member 2	Homo sapiens	122-126
16155403-1	2005	The antiarrhythmic clofilium is an efficient blocker of hERG1 potassium channels that are strongly expressed in the heart.	clofilium	19-28	potassium voltage-gated channel subfamily H member 2	Homo sapiens	56-61
16155403-3	2005	Fluoro- clofilium (F-clofilium) was synthesized and its channel-blocking properties were determined for hERG1 and hEAG1 channels expressed in HEK?293 cells and in Xenopus oocytes.	clofilium	0-17	potassium voltage-gated channel subfamily H member 2	Homo sapiens	104-109
16155403-3	2005	Fluoro- clofilium (F-clofilium) was synthesized and its channel-blocking properties were determined for hERG1 and hEAG1 channels expressed in HEK?293 cells and in Xenopus oocytes.	clofilium	19-30	potassium voltage-gated channel subfamily H member 2	Homo sapiens	104-109
16155403-6	2005	Similar results were obtained for hERG1, showing F-clofilium is a potent hERG1 and hEAG1 channel blocker once it has reached the intracellularly accessible target site at the channel.	clofilium	49-60	potassium voltage-gated channel subfamily H member 2	Homo sapiens	34-39
16155403-6	2005	Similar results were obtained for hERG1, showing F-clofilium is a potent hERG1 and hEAG1 channel blocker once it has reached the intracellularly accessible target site at the channel.	clofilium	49-60	potassium voltage-gated channel subfamily H member 2	Homo sapiens	73-78
16011830-1	2005	One variant of the syndrome is linked to missense mutations that lead to a single amino-acid change (N588K; asparagine to lysine) in the S5-Pore linker region of the cardiac HERG K(+) channel.	Asparagine	108-118	potassium voltage-gated channel subfamily H member 2	Homo sapiens	174-178
16011830-1	2005	One variant of the syndrome is linked to missense mutations that lead to a single amino-acid change (N588K; asparagine to lysine) in the S5-Pore linker region of the cardiac HERG K(+) channel.	Lysine	122-128	potassium voltage-gated channel subfamily H member 2	Homo sapiens	174-178
16086867-0	2005	[Correlation of HERG K+ channel protein expression to chemosensitivity of tumor cells to doxorubicin and its modulation by erythromycin].	Doxorubicin	89-100	potassium voltage-gated channel subfamily H member 2	Homo sapiens	16-20
16086867-0	2005	[Correlation of HERG K+ channel protein expression to chemosensitivity of tumor cells to doxorubicin and its modulation by erythromycin].	Erythromycin	123-135	potassium voltage-gated channel subfamily H member 2	Homo sapiens	16-20
16086867-1	2005	BACKGROUND & OBJECTIVE: Previous studies have found that HERG, a kind of K(+) channel protein, is expressed in some cancers, but its expression is weak or lost in normal tissues.	Adenosine Monophosphate	12-15	potassium voltage-gated channel subfamily H member 2	Homo sapiens	61-65
16086867-2	2005	This study was to investigate HERG expression in various cancer cell lines, its correlation with chemosensitivity of cancer cells to doxorubicin, and its biochemical modulation.	Doxorubicin	133-144	potassium voltage-gated channel subfamily H member 2	Homo sapiens	30-34
16086867-8	2005	The 50% inhibitory concentration (IC(50)) of doxorubicin was obviously higher in herg-transfected A549 cells than in parent A549 cells.	Doxorubicin	45-56	potassium voltage-gated channel subfamily H member 2	Homo sapiens	81-85
16086867-11	2005	CONCLUSIONS: HERG expression might negatively correlate with the chemosensitivity of tumor cells to doxorubicin.	Doxorubicin	100-111	potassium voltage-gated channel subfamily H member 2	Homo sapiens	13-17
15812674-0	2005	HERG K+ channel expression-related chemosensitivity in cancer cells and its modulation by erythromycin.	Erythromycin	90-102	potassium voltage-gated channel subfamily H member 2	Homo sapiens	0-4
15812674-2	2005	In the study reported here, we investigated HERG expression in various cancer cell lines, its correlation with chemosensitivity to vincristine, paclitaxel, and hydroxy-camptothecin, and its biochemical modulation.	Vincristine	131-142	potassium voltage-gated channel subfamily H member 2	Homo sapiens	44-48
15812674-2	2005	In the study reported here, we investigated HERG expression in various cancer cell lines, its correlation with chemosensitivity to vincristine, paclitaxel, and hydroxy-camptothecin, and its biochemical modulation.	Paclitaxel	144-154	potassium voltage-gated channel subfamily H member 2	Homo sapiens	44-48
15812674-2	2005	In the study reported here, we investigated HERG expression in various cancer cell lines, its correlation with chemosensitivity to vincristine, paclitaxel, and hydroxy-camptothecin, and its biochemical modulation.	hydroxycamptothecinum	160-180	potassium voltage-gated channel subfamily H member 2	Homo sapiens	44-48
15812674-7	2005	RESULTS: HERG expression levels differed widely between various human cancer cell lines and HT-29 cells expressing high levels of HERG were more sensitive than A549 cells expressing low levels of HERG to vincristine, paclitaxel, and hydroxy-camptothecin.	Vincristine	204-215	potassium voltage-gated channel subfamily H member 2	Homo sapiens	9-13
15812674-7	2005	RESULTS: HERG expression levels differed widely between various human cancer cell lines and HT-29 cells expressing high levels of HERG were more sensitive than A549 cells expressing low levels of HERG to vincristine, paclitaxel, and hydroxy-camptothecin.	Vincristine	204-215	potassium voltage-gated channel subfamily H member 2	Homo sapiens	130-134
15812674-7	2005	RESULTS: HERG expression levels differed widely between various human cancer cell lines and HT-29 cells expressing high levels of HERG were more sensitive than A549 cells expressing low levels of HERG to vincristine, paclitaxel, and hydroxy-camptothecin.	Vincristine	204-215	potassium voltage-gated channel subfamily H member 2	Homo sapiens	130-134
15812674-7	2005	RESULTS: HERG expression levels differed widely between various human cancer cell lines and HT-29 cells expressing high levels of HERG were more sensitive than A549 cells expressing low levels of HERG to vincristine, paclitaxel, and hydroxy-camptothecin.	Paclitaxel	217-227	potassium voltage-gated channel subfamily H member 2	Homo sapiens	9-13
15812674-7	2005	RESULTS: HERG expression levels differed widely between various human cancer cell lines and HT-29 cells expressing high levels of HERG were more sensitive than A549 cells expressing low levels of HERG to vincristine, paclitaxel, and hydroxy-camptothecin.	hydroxycamptothecinum	233-253	potassium voltage-gated channel subfamily H member 2	Homo sapiens	9-13
15812674-7	2005	RESULTS: HERG expression levels differed widely between various human cancer cell lines and HT-29 cells expressing high levels of HERG were more sensitive than A549 cells expressing low levels of HERG to vincristine, paclitaxel, and hydroxy-camptothecin.	hydroxycamptothecinum	233-253	potassium voltage-gated channel subfamily H member 2	Homo sapiens	130-134
15812674-7	2005	RESULTS: HERG expression levels differed widely between various human cancer cell lines and HT-29 cells expressing high levels of HERG were more sensitive than A549 cells expressing low levels of HERG to vincristine, paclitaxel, and hydroxy-camptothecin.	hydroxycamptothecinum	233-253	potassium voltage-gated channel subfamily H member 2	Homo sapiens	130-134
15812674-8	2005	In terms of IC50, the chemosensitivities of herg-transfected A549 cells to vincristine, paclitaxel and hydroxy-camptothecin were significantly increased.	Vincristine	75-86	potassium voltage-gated channel subfamily H member 2	Homo sapiens	44-48
15812674-8	2005	In terms of IC50, the chemosensitivities of herg-transfected A549 cells to vincristine, paclitaxel and hydroxy-camptothecin were significantly increased.	Paclitaxel	88-98	potassium voltage-gated channel subfamily H member 2	Homo sapiens	44-48
15812674-8	2005	In terms of IC50, the chemosensitivities of herg-transfected A549 cells to vincristine, paclitaxel and hydroxy-camptothecin were significantly increased.	hydroxycamptothecinum	103-123	potassium voltage-gated channel subfamily H member 2	Homo sapiens	44-48
15812674-10	2005	Erythromycin, a HERG K+ channel blocker, suppressed the growth of various cancer cells and the potency was correlated with HERG expression levels.	Erythromycin	0-12	potassium voltage-gated channel subfamily H member 2	Homo sapiens	16-20
15812674-10	2005	Erythromycin, a HERG K+ channel blocker, suppressed the growth of various cancer cells and the potency was correlated with HERG expression levels.	Erythromycin	0-12	potassium voltage-gated channel subfamily H member 2	Homo sapiens	123-127
15812674-13	2005	There were synergistic effects between erythromycin and vincristine, paclitaxel, and hydroxy-camptothecin, and chemosensitivity was correlated with HERG expression level.	Erythromycin	39-51	potassium voltage-gated channel subfamily H member 2	Homo sapiens	148-152
15812674-13	2005	There were synergistic effects between erythromycin and vincristine, paclitaxel, and hydroxy-camptothecin, and chemosensitivity was correlated with HERG expression level.	Paclitaxel	69-79	potassium voltage-gated channel subfamily H member 2	Homo sapiens	148-152
15812674-14	2005	CONCLUSIONS: HERG expression levels and chemosensitivity were positively correlated for vincristine, paclitaxel, and hydroxy-camptothecin.	Vincristine	88-99	potassium voltage-gated channel subfamily H member 2	Homo sapiens	13-17
15812674-14	2005	CONCLUSIONS: HERG expression levels and chemosensitivity were positively correlated for vincristine, paclitaxel, and hydroxy-camptothecin.	Paclitaxel	101-111	potassium voltage-gated channel subfamily H member 2	Homo sapiens	13-17
15812674-14	2005	CONCLUSIONS: HERG expression levels and chemosensitivity were positively correlated for vincristine, paclitaxel, and hydroxy-camptothecin.	hydroxycamptothecinum	117-137	potassium voltage-gated channel subfamily H member 2	Homo sapiens	13-17
16051125-6	2005	Under these conditions, erythromycin rapidly blocked I(hERG) even at 22 degrees C. The F656C mutation in the distal S6 of KCNH2 completely abrogated block of I(hERG) measured at 37 degrees C. CONCLUSION: Progressively greater block of hERG and prolongation of APD by erythromycin was observed at temperatures between 36 and 42 degrees C. Temperature-dependent block of I(hERG) is explained by temperature-dependent access of erythromycin to the intracellular binding site at F656.	Erythromycin	24-36	potassium voltage-gated channel subfamily H member 2	Homo sapiens	122-127
16051125-6	2005	Under these conditions, erythromycin rapidly blocked I(hERG) even at 22 degrees C. The F656C mutation in the distal S6 of KCNH2 completely abrogated block of I(hERG) measured at 37 degrees C. CONCLUSION: Progressively greater block of hERG and prolongation of APD by erythromycin was observed at temperatures between 36 and 42 degrees C. Temperature-dependent block of I(hERG) is explained by temperature-dependent access of erythromycin to the intracellular binding site at F656.	Erythromycin	267-279	potassium voltage-gated channel subfamily H member 2	Homo sapiens	122-127
16051125-6	2005	Under these conditions, erythromycin rapidly blocked I(hERG) even at 22 degrees C. The F656C mutation in the distal S6 of KCNH2 completely abrogated block of I(hERG) measured at 37 degrees C. CONCLUSION: Progressively greater block of hERG and prolongation of APD by erythromycin was observed at temperatures between 36 and 42 degrees C. Temperature-dependent block of I(hERG) is explained by temperature-dependent access of erythromycin to the intracellular binding site at F656.	Erythromycin	267-279	potassium voltage-gated channel subfamily H member 2	Homo sapiens	122-127
15983462-3	2005	The aim of this study was to determine the effect of the mutations Y652A and F656A in the putative drug binding region of HERG on the inhibition by bupivacaine, ropivacaine, and mepivacaine.	Ropivacaine	161-172	potassium voltage-gated channel subfamily H member 2	Homo sapiens	122-126
15983462-3	2005	The aim of this study was to determine the effect of the mutations Y652A and F656A in the putative drug binding region of HERG on the inhibition by bupivacaine, ropivacaine, and mepivacaine.	Mepivacaine	178-189	potassium voltage-gated channel subfamily H member 2	Homo sapiens	122-126
15983462-4	2005	METHODS: The authors examined the inhibition of wild-type and mutant HERG channels, transiently expressed in Chinese hamster ovary cells by bupivacaine, ropivacaine, and mepivacaine.	Bupivacaine	140-151	potassium voltage-gated channel subfamily H member 2	Homo sapiens	69-73
15983462-4	2005	METHODS: The authors examined the inhibition of wild-type and mutant HERG channels, transiently expressed in Chinese hamster ovary cells by bupivacaine, ropivacaine, and mepivacaine.	Ropivacaine	153-164	potassium voltage-gated channel subfamily H member 2	Homo sapiens	69-73
15983462-4	2005	METHODS: The authors examined the inhibition of wild-type and mutant HERG channels, transiently expressed in Chinese hamster ovary cells by bupivacaine, ropivacaine, and mepivacaine.	Mepivacaine	170-181	potassium voltage-gated channel subfamily H member 2	Homo sapiens	69-73
15983462-10	2005	The mutations resulted in a change of the stereoselectivity of HERG channel block by ropivacaine.	Ropivacaine	85-96	potassium voltage-gated channel subfamily H member 2	Homo sapiens	63-67
15967876-6	2005	In the present study, we examined the effect of inactivation gating on cisapride block of HERG.	Cisapride	71-80	potassium voltage-gated channel subfamily H member 2	Homo sapiens	90-94
15967876-7	2005	Modulation of HERG inactivation was achieved by either changing extracellular K+ or Cs+ concentrations or by mutations of the channel.	Cesium	84-87	potassium voltage-gated channel subfamily H member 2	Homo sapiens	14-18
15967876-9	2005	Furthermore, cisapride block of the HERG K+ current was not linked with inactivation in the mutant HERG channels F656V and F656M.	Cisapride	13-22	potassium voltage-gated channel subfamily H member 2	Homo sapiens	36-40
15967876-10	2005	Our results suggest that inactivation facilitates cisapride block of HERG channels through affecting the positioning of Phe-656.	Cisapride	50-59	potassium voltage-gated channel subfamily H member 2	Homo sapiens	69-73
15967876-10	2005	Our results suggest that inactivation facilitates cisapride block of HERG channels through affecting the positioning of Phe-656.	Phenylalanine	120-123	potassium voltage-gated channel subfamily H member 2	Homo sapiens	69-73
15961404-1	2005	Mutations of a putative cyclic-nucleotide-binding domain (CNBD) can disrupt the function of the hyperpolarization-activated cyclic-nucleotide-gated channel (HCN2) and the human ether-a-go-go-related gene potassium channel (HERG).	Nucleotides, Cyclic	24-41	potassium voltage-gated channel subfamily H member 2	Homo sapiens	223-227
16076272-11	2005	Pharmacologic treatment has only been investigated in patients with a mutation in KCNH2 (HERG), and it could be demonstrated that the mutant currents may be insufficiently suppressed by drugs that are targeted to block the specific current (e.g., sotalol or ibutilide) in patients with a mutation in the IK(r-)coding gene KCNH2 (HERG).	ibutilide	258-267	potassium voltage-gated channel subfamily H member 2	Homo sapiens	89-93
16041196-4	2005	Since the HERG gene encodes IKr, we studied quinidine"s effect on HERG expressed in Xenopus oocytes by the 2-electrode voltage clamp technique.	Quinidine	44-53	potassium voltage-gated channel subfamily H member 2	Homo sapiens	10-14
16041196-4	2005	Since the HERG gene encodes IKr, we studied quinidine"s effect on HERG expressed in Xenopus oocytes by the 2-electrode voltage clamp technique.	Quinidine	44-53	potassium voltage-gated channel subfamily H member 2	Homo sapiens	66-70
16041196-5	2005	When extracellular K+ was 5 mmol/L, quinidine blocked the HERG current dose dependently, with an IC50 of 6.3 +/- 0.2 micromol/L.	Quinidine	36-45	potassium voltage-gated channel subfamily H member 2	Homo sapiens	58-62
16041196-7	2005	The inhibition of HERG by quinidine was not use dependent.	Quinidine	26-35	potassium voltage-gated channel subfamily H member 2	Homo sapiens	18-22
15842772-0	2005	Modulating effect of ginseng saponins on heterologously expressed HERG currents in Xenopus oocytes.	Saponins	29-37	potassium voltage-gated channel subfamily H member 2	Homo sapiens	66-70
15711590-4	2005	The drug pentamidine, at near therapeutic concentrations that do not cause direct KCNH2 channel block, disrupts normal KCNH2 channel protein processing and maturation to reduce its surface membrane expression.	Pentamidine	9-20	potassium voltage-gated channel subfamily H member 2	Homo sapiens	119-124
15973763-7	2005	The mutation might affect, through deficient splicing, the putative cyclic nucleotide binding domain (CNBD) of the HERG K(+) channel.	Nucleotides, Cyclic	68-85	potassium voltage-gated channel subfamily H member 2	Homo sapiens	115-119
15800067-8	2005	hERG1-transfected cells undergo an activation of hERG currents after beta(1) integrin-mediated adhesion to fibronectin; concomitant with this activation, the focal adhesion kinase associates with the hERG1 protein and becomes tyrosine phosphorylated.	Tyrosine	226-234	potassium voltage-gated channel subfamily H member 2	Homo sapiens	0-5
15800067-9	2005	Using hERG1-specific inhibitors, we show that the tyrosine phosphorylation of focal adhesion kinase is strictly dependent on hERG channel activity.	Tyrosine	50-58	potassium voltage-gated channel subfamily H member 2	Homo sapiens	6-11
16007460-0	2005	Inhibition of cardiac HERG channels by grapefruit flavonoid naringenin: implications for the influence of dietary compounds on cardiac repolarisation.	Flavonoids	50-59	potassium voltage-gated channel subfamily H member 2	Homo sapiens	22-26
16007460-0	2005	Inhibition of cardiac HERG channels by grapefruit flavonoid naringenin: implications for the influence of dietary compounds on cardiac repolarisation.	naringenin	60-70	potassium voltage-gated channel subfamily H member 2	Homo sapiens	22-26
16007460-2	2005	In a previous study, we demonstrated for the first time that flavonoids are inhibitors of cardiac human ether-a-go-go-related gene (HERG) channels.	Flavonoids	61-71	potassium voltage-gated channel subfamily H member 2	Homo sapiens	132-136
16007460-4	2005	HERG blockade by grapefruit flavonoid naringenin is most likely to be the mechanism underlying this effect.	Flavonoids	28-37	potassium voltage-gated channel subfamily H member 2	Homo sapiens	0-4
16007460-4	2005	HERG blockade by grapefruit flavonoid naringenin is most likely to be the mechanism underlying this effect.	naringenin	38-48	potassium voltage-gated channel subfamily H member 2	Homo sapiens	0-4
16007460-5	2005	Therefore, the electrophysiological properties of HERG blockade by naringenin were analysed in detail.	naringenin	67-77	potassium voltage-gated channel subfamily H member 2	Homo sapiens	50-54
16007460-6	2005	HERG potassium currents expressed in Xenopus oocytes were measured with a two-microelectrode voltage clamp.	Potassium	5-14	potassium voltage-gated channel subfamily H member 2	Homo sapiens	0-4
16007460-7	2005	Naringenin blocked HERG potassium channels with an IC50 value of 102.6 microM in Xenopus oocytes.	naringenin	0-10	potassium voltage-gated channel subfamily H member 2	Homo sapiens	19-23
16007460-10	2005	Naringenin binding to HERG required aromatic residue F656 in the putative pore binding site.	naringenin	0-10	potassium voltage-gated channel subfamily H member 2	Homo sapiens	22-26
16007460-15	2005	Naringenin inhibits HERG channels with pharmacological characteristics similar to those of well-known HERG antagonists.	naringenin	0-10	potassium voltage-gated channel subfamily H member 2	Homo sapiens	20-24
16007460-15	2005	Naringenin inhibits HERG channels with pharmacological characteristics similar to those of well-known HERG antagonists.	naringenin	0-10	potassium voltage-gated channel subfamily H member 2	Homo sapiens	102-106
15760896-9	2005	These results suggest that the degradation of LQT2 mutant channels is mediated by the cytosolic proteasome in a process that involves mannose trimming, polyubiquitination, and deglycosylation of mutant channels.	Mannose	134-141	potassium voltage-gated channel subfamily H member 2	Homo sapiens	46-50
15842772-1	2005	AIM: To examine the effects of ginseng saponins on the heterologously expressed human ether-a-go-go related gene (HERG) that encodes the rapid component of the delayed rectifier K+ channel.	Saponins	39-47	potassium voltage-gated channel subfamily H member 2	Homo sapiens	114-118
15842772-4	2005	RESULTS: Crude saponins of Korean red ginseng (GS) induced a minimal increase of the maximal HERG conductance without changes in the voltage-dependent HERG current activation and inactivation curves.	Saponins	15-23	potassium voltage-gated channel subfamily H member 2	Homo sapiens	93-97
15842772-5	2005	GS, however, decelerated HERG current deactivation in a concentration-dependent manner, which was more noticeable with panaxitriol (PT) than panaxidiol (PD).	panaxitriol	119-130	potassium voltage-gated channel subfamily H member 2	Homo sapiens	25-29
15842772-5	2005	GS, however, decelerated HERG current deactivation in a concentration-dependent manner, which was more noticeable with panaxitriol (PT) than panaxidiol (PD).	Platinum	132-134	potassium voltage-gated channel subfamily H member 2	Homo sapiens	25-29
15842772-5	2005	GS, however, decelerated HERG current deactivation in a concentration-dependent manner, which was more noticeable with panaxitriol (PT) than panaxidiol (PD).	panaxidiol	141-151	potassium voltage-gated channel subfamily H member 2	Homo sapiens	25-29
15842772-6	2005	Consistently, ginseng saponins increased the HERG deactivation time constants with the order of potency of Rg1 (a major component of PT)>Rf1>Rb1 (a major component of PD).	Saponins	22-30	potassium voltage-gated channel subfamily H member 2	Homo sapiens	45-49
15842772-9	2005	CONCLUSION: Ginseng saponins enhance HERG currents, which could be in part a possible mechanism of the shortening cardiac action potential of ginseng saponins.	Saponins	20-28	potassium voltage-gated channel subfamily H member 2	Homo sapiens	37-41
15842772-9	2005	CONCLUSION: Ginseng saponins enhance HERG currents, which could be in part a possible mechanism of the shortening cardiac action potential of ginseng saponins.	Saponins	150-158	potassium voltage-gated channel subfamily H member 2	Homo sapiens	37-41
15814090-5	2005	Verapamil was used as an HERG channel blocker that is not associated with TdP.	Verapamil	0-9	potassium voltage-gated channel subfamily H member 2	Homo sapiens	25-29
15722405-2	2005	We studied the effects of trifluoperazine on the human ether-a-go-go-related gene (HERG) channel expressed in Xenopus oocytes and on the delayed rectifier K(+) current of guinea pig cardiomyocytes.	Trifluoperazine	26-41	potassium voltage-gated channel subfamily H member 2	Homo sapiens	83-87
15722405-3	2005	The application of trifluoperazine showed a dose-dependent decrease in current amplitudes at the end of voltage steps and tail currents of HERG.	Trifluoperazine	19-34	potassium voltage-gated channel subfamily H member 2	Homo sapiens	139-143
15722405-4	2005	The IC(50) for a trifluoperazine block of HERG current progressively decreased according to depolarization: IC(50) values at -40, 0, and +40 mV were 21.6, 16.6, and 9.29 microM, respectively.	Trifluoperazine	17-32	potassium voltage-gated channel subfamily H member 2	Homo sapiens	42-46
15722405-6	2005	The block of HERG by trifluoperazine was use-dependent, exhibiting more rapid onset and greater steady-state block at higher frequencies of activation; there was partial relief of the block with decreasing frequency.	Trifluoperazine	21-36	potassium voltage-gated channel subfamily H member 2	Homo sapiens	13-17
15640612-0	2005	Comparison of the effects of metoclopramide and domperidone on HERG channels.	Metoclopramide	29-43	potassium voltage-gated channel subfamily H member 2	Homo sapiens	63-67
15722405-8	2005	Our findings suggest the arrhythmogenic side effect of trifluoperazine is caused by a blockade of HERG and the rapid component of the delayed rectifier K(+) current rather than by the blockade of the slow component.	Trifluoperazine	55-70	potassium voltage-gated channel subfamily H member 2	Homo sapiens	98-102
15640612-0	2005	Comparison of the effects of metoclopramide and domperidone on HERG channels.	Domperidone	48-59	potassium voltage-gated channel subfamily H member 2	Homo sapiens	63-67
15640612-3	2005	The gastroprokinetic agent cisapride is a potent blocker of HERG currents and serious cardiac arrhythmias and deaths from TdP and ventricular fibrillation have been reported in patients taking cisapride.	Cisapride	27-36	potassium voltage-gated channel subfamily H member 2	Homo sapiens	60-64
15640612-3	2005	The gastroprokinetic agent cisapride is a potent blocker of HERG currents and serious cardiac arrhythmias and deaths from TdP and ventricular fibrillation have been reported in patients taking cisapride.	Cisapride	193-202	potassium voltage-gated channel subfamily H member 2	Homo sapiens	60-64
15640612-4	2005	The aim of the present study was to compare the effects of the gastroprokinetic agents domperidone and metoclopramide on HERG channels transiently expressed in human embryonic kidney (HEK 293) cells using the whole-cell configuration of the patch-clamp technique.	Domperidone	87-98	potassium voltage-gated channel subfamily H member 2	Homo sapiens	121-125
15640612-4	2005	The aim of the present study was to compare the effects of the gastroprokinetic agents domperidone and metoclopramide on HERG channels transiently expressed in human embryonic kidney (HEK 293) cells using the whole-cell configuration of the patch-clamp technique.	Metoclopramide	103-117	potassium voltage-gated channel subfamily H member 2	Homo sapiens	121-125
15640612-5	2005	Both domperidone and metoclopramide concentration-dependently blocked HERG currents, and the following values were calculated for IC(50) (the concentrations causing half-maximal inhibition) and n (the Hill coefficient): 57.0 nmol/l and 0.99 for domperidone, 5.4 micromol/l and 0.95 for metoclopramide.	Domperidone	5-16	potassium voltage-gated channel subfamily H member 2	Homo sapiens	70-74
15640612-5	2005	Both domperidone and metoclopramide concentration-dependently blocked HERG currents, and the following values were calculated for IC(50) (the concentrations causing half-maximal inhibition) and n (the Hill coefficient): 57.0 nmol/l and 0.99 for domperidone, 5.4 micromol/l and 0.95 for metoclopramide.	Metoclopramide	21-35	potassium voltage-gated channel subfamily H member 2	Homo sapiens	70-74
15640612-6	2005	The observation that the extent of block of HERG currents by domperidone increased at more positive membrane potentials whereas block of HERG currents by metoclopramide displayed a smaller degree of voltage dependency seems to indicate that domperidone and metoclopramide have distinct binding sites on HERG channels.	Domperidone	61-72	potassium voltage-gated channel subfamily H member 2	Homo sapiens	44-48
15640612-6	2005	The observation that the extent of block of HERG currents by domperidone increased at more positive membrane potentials whereas block of HERG currents by metoclopramide displayed a smaller degree of voltage dependency seems to indicate that domperidone and metoclopramide have distinct binding sites on HERG channels.	Metoclopramide	154-168	potassium voltage-gated channel subfamily H member 2	Homo sapiens	137-141
15640612-6	2005	The observation that the extent of block of HERG currents by domperidone increased at more positive membrane potentials whereas block of HERG currents by metoclopramide displayed a smaller degree of voltage dependency seems to indicate that domperidone and metoclopramide have distinct binding sites on HERG channels.	Metoclopramide	154-168	potassium voltage-gated channel subfamily H member 2	Homo sapiens	137-141
15640612-6	2005	The observation that the extent of block of HERG currents by domperidone increased at more positive membrane potentials whereas block of HERG currents by metoclopramide displayed a smaller degree of voltage dependency seems to indicate that domperidone and metoclopramide have distinct binding sites on HERG channels.	Domperidone	241-252	potassium voltage-gated channel subfamily H member 2	Homo sapiens	137-141
15640612-6	2005	The observation that the extent of block of HERG currents by domperidone increased at more positive membrane potentials whereas block of HERG currents by metoclopramide displayed a smaller degree of voltage dependency seems to indicate that domperidone and metoclopramide have distinct binding sites on HERG channels.	Domperidone	241-252	potassium voltage-gated channel subfamily H member 2	Homo sapiens	137-141
15640612-6	2005	The observation that the extent of block of HERG currents by domperidone increased at more positive membrane potentials whereas block of HERG currents by metoclopramide displayed a smaller degree of voltage dependency seems to indicate that domperidone and metoclopramide have distinct binding sites on HERG channels.	Metoclopramide	257-271	potassium voltage-gated channel subfamily H member 2	Homo sapiens	137-141
15640612-6	2005	The observation that the extent of block of HERG currents by domperidone increased at more positive membrane potentials whereas block of HERG currents by metoclopramide displayed a smaller degree of voltage dependency seems to indicate that domperidone and metoclopramide have distinct binding sites on HERG channels.	Metoclopramide	257-271	potassium voltage-gated channel subfamily H member 2	Homo sapiens	137-141
15640612-7	2005	In conclusion, the potency for block of HERG currents is about 100-fold lower for metoclopramide when compared to domperidone.	Metoclopramide	82-96	potassium voltage-gated channel subfamily H member 2	Homo sapiens	40-44
15640612-7	2005	In conclusion, the potency for block of HERG currents is about 100-fold lower for metoclopramide when compared to domperidone.	Domperidone	114-125	potassium voltage-gated channel subfamily H member 2	Homo sapiens	40-44
15778703-0	2005	Blockade of HERG cardiac K+ current by antifungal drug miconazole.	Miconazole	55-65	potassium voltage-gated channel subfamily H member 2	Homo sapiens	12-16
15778703-5	2005	To determine the mechanism underlying these clinical findings, we investigated the effect of miconazole on human ether-a-go-go-related gene (HERG) K+ channels.	Miconazole	93-103	potassium voltage-gated channel subfamily H member 2	Homo sapiens	141-145
15778703-9	2005	Miconazole inhibited HERG peak tail current in a concentration-dependent manner (0.4-40 microM) with an IC50 of 2.1 microM (n=3-5 cells at each concentration, Hill coefficient 1.2).	Miconazole	0-10	potassium voltage-gated channel subfamily H member 2	Homo sapiens	21-25
15778703-16	2005	The S6 domain mutation, F656C, abolished the inhibitory action of miconazole on HERG current indicating that miconazole preferentially binds to an aromatic amino-acid residue within the pore-S6 region.	Miconazole	66-76	potassium voltage-gated channel subfamily H member 2	Homo sapiens	80-84
15778703-16	2005	The S6 domain mutation, F656C, abolished the inhibitory action of miconazole on HERG current indicating that miconazole preferentially binds to an aromatic amino-acid residue within the pore-S6 region.	Miconazole	109-119	potassium voltage-gated channel subfamily H member 2	Homo sapiens	80-84
15778703-16	2005	The S6 domain mutation, F656C, abolished the inhibitory action of miconazole on HERG current indicating that miconazole preferentially binds to an aromatic amino-acid residue within the pore-S6 region.	Amino Acids, Aromatic	147-166	potassium voltage-gated channel subfamily H member 2	Homo sapiens	80-84
15778703-18	2005	Our findings indicate that miconazole causes HERG channel block by binding to a common drug receptor, and this involves preferential binding to activated channels.	Miconazole	27-37	potassium voltage-gated channel subfamily H member 2	Homo sapiens	45-49
15778703-19	2005	Thus, miconazole prolongs the QT interval by direct inhibition of HERG channels.	Miconazole	6-16	potassium voltage-gated channel subfamily H member 2	Homo sapiens	66-70
16244363-6	2005	Consistent with ATF6 activation, the ER chaperones/calcium-binding proteins Grp78, Grp94, and calreticulin are elevated in I593R HERG-expressing cells.	Calcium	51-58	potassium voltage-gated channel subfamily H member 2	Homo sapiens	129-133
15846098-0	2005	The potent inhibitory effects of cisapride, a specific blocker for human ether-a-go-go-related gene (HERG) channel, on gastric cancer cells.	Cisapride	33-42	potassium voltage-gated channel subfamily H member 2	Homo sapiens	101-105
15846098-2	2005	Human ether-a-go-go-related gene (HERG) encoding one of the components of delayed rectifier potassium currents has been indicated to be involved in tumor cell growth and death.	Potassium	92-101	potassium voltage-gated channel subfamily H member 2	Homo sapiens	34-38
15846098-3	2005	Our aim is to investigate the effects of cisapride, a specific blocker for HERG channel, on human gastric cancer cells.	Cisapride	41-50	potassium voltage-gated channel subfamily H member 2	Homo sapiens	75-79
15846098-8	2005	The proliferation of gastric cancer cells expressing HERG protein was inhibited in a time- and dose-dependent manner when treated with cisapride (P<0.05).	Cisapride	135-144	potassium voltage-gated channel subfamily H member 2	Homo sapiens	53-57
15846098-12	2005	CONCLUSIONS: As HERG channel blocker, cisapride, can inhibit the growth of gastric cancer cells by altering distribution of cell cycle and inducing apoptosis so as to be of potential value in the treatment of gastric cancer.	Cisapride	38-47	potassium voltage-gated channel subfamily H member 2	Homo sapiens	16-20
15821840-5	2005	RESULTS: Quinidine (10 microM) inhibited HERG tail current by 37% +/- 5% at pH7.4.	Quinidine	9-18	potassium voltage-gated channel subfamily H member 2	Homo sapiens	41-45
15821840-7	2005	Dofetilide (0.3 microM) inhibited HERG tail current by 34% +/- 3% and 1% +/- 2% at extracellular pH 7.4 and 6.2, respectively.	dofetilide	0-10	potassium voltage-gated channel subfamily H member 2	Homo sapiens	34-38
15721475-5	2005	Drug-induced QT prolongation is usually caused by block of human ether-a-go-go-related gene (HERG) potassium channels, and we showed that lopinavir, nelfinavir, ritonavir, and saquinavir caused dose-dependent block of HERG channels heterologously expressed in HEK293 cells in vitro.	Lopinavir	138-147	potassium voltage-gated channel subfamily H member 2	Homo sapiens	93-97
15721475-5	2005	Drug-induced QT prolongation is usually caused by block of human ether-a-go-go-related gene (HERG) potassium channels, and we showed that lopinavir, nelfinavir, ritonavir, and saquinavir caused dose-dependent block of HERG channels heterologously expressed in HEK293 cells in vitro.	Lopinavir	138-147	potassium voltage-gated channel subfamily H member 2	Homo sapiens	218-222
15721475-5	2005	Drug-induced QT prolongation is usually caused by block of human ether-a-go-go-related gene (HERG) potassium channels, and we showed that lopinavir, nelfinavir, ritonavir, and saquinavir caused dose-dependent block of HERG channels heterologously expressed in HEK293 cells in vitro.	Nelfinavir	149-159	potassium voltage-gated channel subfamily H member 2	Homo sapiens	93-97
15721475-5	2005	Drug-induced QT prolongation is usually caused by block of human ether-a-go-go-related gene (HERG) potassium channels, and we showed that lopinavir, nelfinavir, ritonavir, and saquinavir caused dose-dependent block of HERG channels heterologously expressed in HEK293 cells in vitro.	Nelfinavir	149-159	potassium voltage-gated channel subfamily H member 2	Homo sapiens	218-222
15721475-5	2005	Drug-induced QT prolongation is usually caused by block of human ether-a-go-go-related gene (HERG) potassium channels, and we showed that lopinavir, nelfinavir, ritonavir, and saquinavir caused dose-dependent block of HERG channels heterologously expressed in HEK293 cells in vitro.	Ritonavir	161-170	potassium voltage-gated channel subfamily H member 2	Homo sapiens	93-97
15721475-5	2005	Drug-induced QT prolongation is usually caused by block of human ether-a-go-go-related gene (HERG) potassium channels, and we showed that lopinavir, nelfinavir, ritonavir, and saquinavir caused dose-dependent block of HERG channels heterologously expressed in HEK293 cells in vitro.	Ritonavir	161-170	potassium voltage-gated channel subfamily H member 2	Homo sapiens	218-222
15721475-5	2005	Drug-induced QT prolongation is usually caused by block of human ether-a-go-go-related gene (HERG) potassium channels, and we showed that lopinavir, nelfinavir, ritonavir, and saquinavir caused dose-dependent block of HERG channels heterologously expressed in HEK293 cells in vitro.	Saquinavir	176-186	potassium voltage-gated channel subfamily H member 2	Homo sapiens	93-97
15721475-5	2005	Drug-induced QT prolongation is usually caused by block of human ether-a-go-go-related gene (HERG) potassium channels, and we showed that lopinavir, nelfinavir, ritonavir, and saquinavir caused dose-dependent block of HERG channels heterologously expressed in HEK293 cells in vitro.	Saquinavir	176-186	potassium voltage-gated channel subfamily H member 2	Homo sapiens	218-222
15821840-8	2005	Azimilide (10 microM) inhibited HERG tail current by 59% +/- 3% and 17% +/- 3% at extracellular pH 7.4 and 6.2.	azimilide	0-9	potassium voltage-gated channel subfamily H member 2	Homo sapiens	32-36
15821840-9	2005	There were significant differences in the HERG inhibition by quinidine, dofetilide, and azimilide between pH 7.4 and pH 6.2 (P < .01).	Quinidine	61-70	potassium voltage-gated channel subfamily H member 2	Homo sapiens	42-46
15821840-9	2005	There were significant differences in the HERG inhibition by quinidine, dofetilide, and azimilide between pH 7.4 and pH 6.2 (P < .01).	dofetilide	72-82	potassium voltage-gated channel subfamily H member 2	Homo sapiens	42-46
15821840-9	2005	There were significant differences in the HERG inhibition by quinidine, dofetilide, and azimilide between pH 7.4 and pH 6.2 (P < .01).	azimilide	88-97	potassium voltage-gated channel subfamily H member 2	Homo sapiens	42-46
15548764-7	2005	RPR260243-modified HERG currents were inhibited by dofetilide (IC50 = 58 nM).	dofetilide	51-61	potassium voltage-gated channel subfamily H member 2	Homo sapiens	19-23
15733182-1	2005	AIMS: To explore effects of epinephrine and phenylephrine on the behavior of right ventricular monophasic action potentials (MAPs) in symptomatic LQT1 and LQT2 patients.	Epinephrine	28-39	potassium voltage-gated channel subfamily H member 2	Homo sapiens	155-159
15733182-1	2005	AIMS: To explore effects of epinephrine and phenylephrine on the behavior of right ventricular monophasic action potentials (MAPs) in symptomatic LQT1 and LQT2 patients.	Phenylephrine	44-57	potassium voltage-gated channel subfamily H member 2	Homo sapiens	155-159
15679475-4	2005	Propranolol caused a concentration-dependent inhibition of HERG current with an IC50 value of 81 microM at -10 mV.	Propranolol	0-11	potassium voltage-gated channel subfamily H member 2	Homo sapiens	59-63
15679475-7	2005	The propranolol analogue ICI118551 ((+/-)-1-[2,3-(dihydro-7-methyl-1H-inden-4-yl)oxy]-3-[(1-methylethyl)amino]-2-butanol hydrochloride) blocked the HERG channel with similar affinity, whereas the beta1-receptor antagonists metoprolol and atenolol showed weak effects.	Propranolol	4-15	potassium voltage-gated channel subfamily H member 2	Homo sapiens	148-152
15679475-7	2005	The propranolol analogue ICI118551 ((+/-)-1-[2,3-(dihydro-7-methyl-1H-inden-4-yl)oxy]-3-[(1-methylethyl)amino]-2-butanol hydrochloride) blocked the HERG channel with similar affinity, whereas the beta1-receptor antagonists metoprolol and atenolol showed weak effects.	ICI 118551	25-34	potassium voltage-gated channel subfamily H member 2	Homo sapiens	148-152
15679475-7	2005	The propranolol analogue ICI118551 ((+/-)-1-[2,3-(dihydro-7-methyl-1H-inden-4-yl)oxy]-3-[(1-methylethyl)amino]-2-butanol hydrochloride) blocked the HERG channel with similar affinity, whereas the beta1-receptor antagonists metoprolol and atenolol showed weak effects.	((+/-)-1-[2,3-(dihydro-7-methyl-1h-inden-4-yl)oxy]-3-[(1-methylethyl)amino]-2-butanol hydrochloride	35-134	potassium voltage-gated channel subfamily H member 2	Homo sapiens	148-152
15500450-0	2005	Compound heterozygosity for mutations Asp611-->Tyr in KCNQ1 and Asp609-->Gly in KCNH2 associated with severe long QT syndrome.	Glycine	79-82	potassium voltage-gated channel subfamily H member 2	Homo sapiens	86-91
15500450-2	2005	We have identified two heterozygous missense mutations in the KCNQ1 and KCNH2 (also known as HERG) genes [Asp611-->Tyr (D611Y) in KCNQ1 and Asp609-->Gly (D609G) in KCNH2] in a 2-year-old boy with LQTS.	Tyrosine	118-121	potassium voltage-gated channel subfamily H member 2	Homo sapiens	72-77
15500450-2	2005	We have identified two heterozygous missense mutations in the KCNQ1 and KCNH2 (also known as HERG) genes [Asp611-->Tyr (D611Y) in KCNQ1 and Asp609-->Gly (D609G) in KCNH2] in a 2-year-old boy with LQTS.	Tyrosine	118-121	potassium voltage-gated channel subfamily H member 2	Homo sapiens	93-97
15500450-2	2005	We have identified two heterozygous missense mutations in the KCNQ1 and KCNH2 (also known as HERG) genes [Asp611-->Tyr (D611Y) in KCNQ1 and Asp609-->Gly (D609G) in KCNH2] in a 2-year-old boy with LQTS.	Tyrosine	118-121	potassium voltage-gated channel subfamily H member 2	Homo sapiens	170-175
15500450-2	2005	We have identified two heterozygous missense mutations in the KCNQ1 and KCNH2 (also known as HERG) genes [Asp611-->Tyr (D611Y) in KCNQ1 and Asp609-->Gly (D609G) in KCNH2] in a 2-year-old boy with LQTS.	Glycine	155-158	potassium voltage-gated channel subfamily H member 2	Homo sapiens	72-77
15500450-2	2005	We have identified two heterozygous missense mutations in the KCNQ1 and KCNH2 (also known as HERG) genes [Asp611-->Tyr (D611Y) in KCNQ1 and Asp609-->Gly (D609G) in KCNH2] in a 2-year-old boy with LQTS.	Glycine	155-158	potassium voltage-gated channel subfamily H member 2	Homo sapiens	93-97
15851286-8	2005	During epinephrine infusion, G1- and G2-T waves were more common in LQT2 than in LQT1 (75% vs 26%, P = .009).	Epinephrine	7-18	potassium voltage-gated channel subfamily H member 2	Homo sapiens	68-72
15851286-10	2005	Epinephrine-precipitated biphasic T waves were observed similarly in all groups: LQT1 (6/30), LQT2 (3/28), and control (4/32).	Epinephrine	0-11	potassium voltage-gated channel subfamily H member 2	Homo sapiens	94-98
15851286-11	2005	During low-dose epinephrine infusion (< or =0.05 microg/kg/min), G1-T waves occurred more frequently in LQT2 (LQT1: 25% vs 3%; control 9%, P = .02).	Epinephrine	16-27	potassium voltage-gated channel subfamily H member 2	Homo sapiens	107-111
15851286-12	2005	Low-dose epinephrine-induced G2-T waves were detected exclusively in LQT2 (18%).	Epinephrine	9-20	potassium voltage-gated channel subfamily H member 2	Homo sapiens	69-73
15851286-16	2005	G2-notched T waves elicited during low-dose epinephrine may unmask some patients with concealed LQT2.	Epinephrine	44-55	potassium voltage-gated channel subfamily H member 2	Homo sapiens	96-100
15608471-6	2005	This data, associated with the finding that methadone is a rather potent inhibitor of HERG potassium channels and that it may induce torsade de pointes in predisposed subjects, supports the recommendation that patients entering methadone treatment (MT) are screened for cardiac risk factors.	Methadone	44-53	potassium voltage-gated channel subfamily H member 2	Homo sapiens	86-90
15670565-1	2005	In a 7-week-old infant who experienced sudden infant death syndrome (SIDS), a novel missense mutation was identified in KCNH2, causing a lysine-to-glutamic acid amino acid substitution at position 101 (K101E).	Lysine	137-143	potassium voltage-gated channel subfamily H member 2	Homo sapiens	120-125
15670565-1	2005	In a 7-week-old infant who experienced sudden infant death syndrome (SIDS), a novel missense mutation was identified in KCNH2, causing a lysine-to-glutamic acid amino acid substitution at position 101 (K101E).	glutamic acid amino acid	147-171	potassium voltage-gated channel subfamily H member 2	Homo sapiens	120-125
15673388-0	2005	Further insights into the effect of quinidine in short QT syndrome caused by a mutation in HERG.	Quinidine	36-45	potassium voltage-gated channel subfamily H member 2	Homo sapiens	91-95
15673388-1	2005	INTRODUCTION: The principal aim of this study was to assess the efficacy of quinidine in suppressing IKr in vitro and in modulating the rate dependence of the QT interval in the "SQT1" form of the short QT syndrome.	Quinidine	76-85	potassium voltage-gated channel subfamily H member 2	Homo sapiens	179-183
15673388-6	2005	Data from heterologous expression of wild-type and mutant HERG genes indicate the mutation causes a 20-fold increase in IC50 of d-sotalol but only a 5.8-fold increase in IC50 of quinidine.	Dexsotalol	128-137	potassium voltage-gated channel subfamily H member 2	Homo sapiens	58-62
15673388-6	2005	Data from heterologous expression of wild-type and mutant HERG genes indicate the mutation causes a 20-fold increase in IC50 of d-sotalol but only a 5.8-fold increase in IC50 of quinidine.	Quinidine	178-187	potassium voltage-gated channel subfamily H member 2	Homo sapiens	58-62
15673388-7	2005	CONCLUSION: Oral quinidine is effective in suppressing the gain of function in IKr responsible for some cases of short QT syndrome with a mutation in HERG and thus restoring normal rate dependence of the QT interval and rendering ventricular tachycardia/ventricular fibrillation noninducible.	Quinidine	17-26	potassium voltage-gated channel subfamily H member 2	Homo sapiens	150-154
15572053-7	2004	Using sucrose gradient centrifugation we showed that wild type HERG and R1014X formed a tetrameric structure, whereas Q725X was expressed as a monomer.	Sucrose	6-13	potassium voltage-gated channel subfamily H member 2	Homo sapiens	63-67
15541373-0	2004	High affinity HERG K(+) channel blockade by the antiarrhythmic agent dronedarone: resistance to mutations of the S6 residues Y652 and F656.	Dronedarone	69-80	potassium voltage-gated channel subfamily H member 2	Homo sapiens	14-18
15541373-2	2004	Two aromatic amino-acid residues (Y652 and F656) on the inner (S6) helices are considered to be key constituents of a high affinity drug binding site within the HERG channel pore cavity.	Amino Acids, Aromatic	4-23	potassium voltage-gated channel subfamily H member 2	Homo sapiens	161-165
15541373-3	2004	Using wild-type (WT) and mutant HERG channels expressed in mammalian cell lines, we have investigated HERG channel current (I(HERG)) blockade at 37+/-1 degrees C by dronedarone (DRONED), a non-iodinated analogue of the Class III antiarrhythmic agent amiodarone (AMIOD).	Dronedarone	165-176	potassium voltage-gated channel subfamily H member 2	Homo sapiens	102-106
15541373-3	2004	Using wild-type (WT) and mutant HERG channels expressed in mammalian cell lines, we have investigated HERG channel current (I(HERG)) blockade at 37+/-1 degrees C by dronedarone (DRONED), a non-iodinated analogue of the Class III antiarrhythmic agent amiodarone (AMIOD).	Dronedarone	165-176	potassium voltage-gated channel subfamily H member 2	Homo sapiens	102-106
15558241-0	2004	Inhibitory effects of AMP 579, a novel cardioprotective adenosine A1/A2A receptor agonist, on native IKr and cloned HERG current.	4-(7-((2-3-chloro-2-thienyl)-1-methyl-propylamino)-3H-imidazo(4,5-b)pyridyl-3-yl)cyclopentane carboxamide	22-29	potassium voltage-gated channel subfamily H member 2	Homo sapiens	116-120
15599107-1	2004	While aldosterone receptor blockers improve survival of patients with congestive heart failure, spironolactone and its derivatives were recently shown to block ether-a-go-go-related gene (HERG) channels and native IKs and IKr currents in guinea pig ventricular myocytes.	Spironolactone	96-110	potassium voltage-gated channel subfamily H member 2	Homo sapiens	188-192
15558241-7	2004	In HEK 293 cells expressing HERG channels, AMP 579 (10 microM) significantly blocked the HERG current at +10 mV by 34.9+/-7.0% (n=4, p<0.05), and the degree of inhibition was comparable with that observed in guinea-pig ventricular myocytes (36.8+/-6.0%, n=4).	Adenosine Monophosphate	43-46	potassium voltage-gated channel subfamily H member 2	Homo sapiens	28-32
15558241-7	2004	In HEK 293 cells expressing HERG channels, AMP 579 (10 microM) significantly blocked the HERG current at +10 mV by 34.9+/-7.0% (n=4, p<0.05), and the degree of inhibition was comparable with that observed in guinea-pig ventricular myocytes (36.8+/-6.0%, n=4).	Adenosine Monophosphate	43-46	potassium voltage-gated channel subfamily H member 2	Homo sapiens	89-93
15558241-10	2004	Thus, AMP 579 inhibits both native I(Kr) and cloned HERG channels with additional inhibitory effect of I(Ca), and such inhibitory effects may at least partially underlie the observed antifibrillatory action of the drug during myocardial ischemia/reperfusion.	Adenosine Monophosphate	6-9	potassium voltage-gated channel subfamily H member 2	Homo sapiens	52-56
15558243-4	2004	Here we show that halofantrine preferentially blocks open and inactivated HERG channels heterologously expressed in Xenopus laevis oocytes.	halofantrine	18-30	potassium voltage-gated channel subfamily H member 2	Homo sapiens	74-78
15599706-0	2004	Class Ia anti-arrhythmic drug ajmaline blocks HERG potassium channels: mode of action.	Ajmaline	30-38	potassium voltage-gated channel subfamily H member 2	Homo sapiens	46-50
15558243-6	2004	As we reported previously for other HERG channel blockers, the potency of halofantrine was reduced by mutation to Ala of aromatic residues (Y652, F656) located in the S6 domain, or a Val (V625) located in the pore helix.	halofantrine	74-86	potassium voltage-gated channel subfamily H member 2	Homo sapiens	36-40
15599706-5	2004	Ajmaline blocked HERG currents with an IC(50) of 1.0 micromol/l in HEK cells and 42.3 micromol/l in Xenopus oocytes.	Ajmaline	0-8	potassium voltage-gated channel subfamily H member 2	Homo sapiens	17-21
15599706-7	2004	In HERG mutant channels Y652A and F656A lacking aromatic residues in the S6 domain, the inhibitory effect of ajmaline was completely abolished.	Ajmaline	109-117	potassium voltage-gated channel subfamily H member 2	Homo sapiens	3-7
15558243-6	2004	As we reported previously for other HERG channel blockers, the potency of halofantrine was reduced by mutation to Ala of aromatic residues (Y652, F656) located in the S6 domain, or a Val (V625) located in the pore helix.	Alanine	114-117	potassium voltage-gated channel subfamily H member 2	Homo sapiens	36-40
15599706-8	2004	Ajmaline induced a small shift in HERG current half-maximal activation voltage towards more negative potentials.	Ajmaline	0-8	potassium voltage-gated channel subfamily H member 2	Homo sapiens	34-38
15558243-12	2004	We conclude that halofantrine requires channels to open before it can gain access to its binding site located in the central cavity of the HERG channel.	halofantrine	17-29	potassium voltage-gated channel subfamily H member 2	Homo sapiens	139-143
15599706-12	2004	Ajmaline blocked HERG channels in the open, but not in the closed states.	Ajmaline	0-8	potassium voltage-gated channel subfamily H member 2	Homo sapiens	17-21
15599706-13	2004	Binding of ajmaline to inactivated HERG channels may also be possible.	Ajmaline	11-19	potassium voltage-gated channel subfamily H member 2	Homo sapiens	35-39
15599706-3	2004	In order to elucidate the molecular basis of these effects, we examined effects of ajmaline on human ether a-go-go related gene HERG potassium channels.	Ajmaline	83-91	potassium voltage-gated channel subfamily H member 2	Homo sapiens	128-132
15599706-14	2004	In inactivation-deficient HERG S620T channels, the sensitivity to ajmaline was markedly reduced.	Ajmaline	66-74	potassium voltage-gated channel subfamily H member 2	Homo sapiens	26-30
15599706-15	2004	The IC(50) of HERG channel blockade in HEK cells lies within the range of unbound therapeutic plasma concentrations of ajmaline.	Ajmaline	119-127	potassium voltage-gated channel subfamily H member 2	Homo sapiens	14-18
15599706-16	2004	Therefore, inhibitory effects on HERG channels may contribute to both the high anti-arrhythmic efficacy of ajmaline and to its pro-arrhythmic potential.	Ajmaline	107-115	potassium voltage-gated channel subfamily H member 2	Homo sapiens	33-37
15322737-0	2004	Inhibition of cardiac HERG potassium channels by the atypical antidepressant trazodone.	Trazodone	77-86	potassium voltage-gated channel subfamily H member 2	Homo sapiens	22-26
15280442-4	2004	Using the patch-clamp technique, we showed that clobutinol dose-dependently inhibited the HERG K(+) current with a half-maximum block concentration of 2.9 microM.	clobutinol	48-58	potassium voltage-gated channel subfamily H member 2	Homo sapiens	90-94
15851169-2	2004	BACKGROUND: A differential response of dynamic QT interval to epinephrine infusion between LQT1, LQT2, and LQT3 syndromes has been reported, indicating the potential diagnostic value of the epinephrine test for genotyping the three forms.	Epinephrine	62-73	potassium voltage-gated channel subfamily H member 2	Homo sapiens	97-101
15851169-2	2004	BACKGROUND: A differential response of dynamic QT interval to epinephrine infusion between LQT1, LQT2, and LQT3 syndromes has been reported, indicating the potential diagnostic value of the epinephrine test for genotyping the three forms.	Epinephrine	190-201	potassium voltage-gated channel subfamily H member 2	Homo sapiens	97-101
15851169-6	2004	RESULTS: The sensitivity (penetrance) by ECG diagnostic criteria was lower in LQT1 (68%) than in LQT2 (83%) or LQT3 (83%) before epinephrine and was improved with steady-state epinephrine in LQT1 (87%) and LQT2 (91%) but not in LQT3 (83%), without the expense of specificity (100%).	Epinephrine	176-187	potassium voltage-gated channel subfamily H member 2	Homo sapiens	206-210
15851169-9	2004	CONCLUSIONS: Epinephrine infusion is a powerful test to predict the genotype of LQT1, LQT2, and LQT3 syndromes as well as to improve the clinical diagnosis of genotype-positive patients, especially those with LQT1 syndrome.	Epinephrine	13-24	potassium voltage-gated channel subfamily H member 2	Homo sapiens	86-90
15280551-7	2004	This clinical result is supported by in vitro studies of HERG dofetilide sensitivity by using coexpression of HERG with wild-type and I447V KCR1 cDNAs.	dofetilide	62-72	potassium voltage-gated channel subfamily H member 2	Homo sapiens	57-61
15280551-7	2004	This clinical result is supported by in vitro studies of HERG dofetilide sensitivity by using coexpression of HERG with wild-type and I447V KCR1 cDNAs.	dofetilide	62-72	potassium voltage-gated channel subfamily H member 2	Homo sapiens	110-114
15072950-2	2004	We previously showed that the HERG N470D mutation expressed as homotetrameric channels causes a protein trafficking defect, and this can be corrected by the HERG channel blocking drug E-4031.	E 4031	184-190	potassium voltage-gated channel subfamily H member 2	Homo sapiens	30-34
15072950-2	2004	We previously showed that the HERG N470D mutation expressed as homotetrameric channels causes a protein trafficking defect, and this can be corrected by the HERG channel blocking drug E-4031.	E 4031	184-190	potassium voltage-gated channel subfamily H member 2	Homo sapiens	157-161
15685300-4	2005	Changing from supine to standing alone caused a significant increase in QTc in the LQT2 group compared with in control subjects (change in QTc of 48+/-38 ms versus 21+/-29 ms, respectively, P=0.02).	qtc	72-75	potassium voltage-gated channel subfamily H member 2	Homo sapiens	83-87
15231497-0	2004	Molecular analysis of PIP2 regulation of HERG and IKr.	Phosphatidylinositol 4,5-Diphosphate	22-26	potassium voltage-gated channel subfamily H member 2	Homo sapiens	41-45
15231497-1	2004	We previously reported that cloned human ether-a-go-go-related gene (HERG) K+ channels are regulated by changes in phosphatidylinositol 4,5-bisphosphate (PIP2) concentration.	Phosphatidylinositol 4,5-Diphosphate	115-152	potassium voltage-gated channel subfamily H member 2	Homo sapiens	69-73
15231497-1	2004	We previously reported that cloned human ether-a-go-go-related gene (HERG) K+ channels are regulated by changes in phosphatidylinositol 4,5-bisphosphate (PIP2) concentration.	Phosphatidylinositol 4,5-Diphosphate	154-158	potassium voltage-gated channel subfamily H member 2	Homo sapiens	69-73
15231497-2	2004	Here we investigated the molecular determinants of PIP2 interactions with HERG channel protein.	Phosphatidylinositol 4,5-Diphosphate	51-55	potassium voltage-gated channel subfamily H member 2	Homo sapiens	74-78
15231497-6	2004	Elevating internal PIP2, however, no longer accelerated the activation kinetics of the mutant HERG.	Phosphatidylinositol 4,5-Diphosphate	19-23	potassium voltage-gated channel subfamily H member 2	Homo sapiens	94-98
15231497-12	2004	These results support a physiological role for PIP2 regulation of the rapidly activating delayed rectifier K+ current during autonomic stimulation and localize a site of interaction to the COOH-terminal tail of the HERG K+ channel.	Phosphatidylinositol 4,5-Diphosphate	47-51	potassium voltage-gated channel subfamily H member 2	Homo sapiens	215-219
15522280-0	2004	Role of a KCNH2 polymorphism (R1047 L) in dofetilide-induced Torsades de Pointes.	dofetilide	42-52	potassium voltage-gated channel subfamily H member 2	Homo sapiens	10-15
15308760-0	2004	The low-potency, voltage-dependent HERG blocker propafenone--molecular determinants and drug trapping.	Propafenone	48-59	potassium voltage-gated channel subfamily H member 2	Homo sapiens	35-39
15308760-1	2004	The molecular determinants of high-affinity human ether-a-go-go-related gene (HERG) potassium channel blockade by methanesulfonanilides include two aromatic residues (Phe656 and Tyr652) on the inner helices (S6) and residues on the pore helices that face into the inner cavity, but determinants for lower-affinity HERG blockers may be different.	methanesulfonanilides	114-135	potassium voltage-gated channel subfamily H member 2	Homo sapiens	78-82
15308760-1	2004	The molecular determinants of high-affinity human ether-a-go-go-related gene (HERG) potassium channel blockade by methanesulfonanilides include two aromatic residues (Phe656 and Tyr652) on the inner helices (S6) and residues on the pore helices that face into the inner cavity, but determinants for lower-affinity HERG blockers may be different.	methanesulfonanilides	114-135	potassium voltage-gated channel subfamily H member 2	Homo sapiens	314-318
15308760-2	2004	In this study, alanine-substituted HERG channel mutants of inner cavity residues were expressed in Xenopus laevis oocytes and were used to characterize the HERG channel binding site of the antiarrhythmic propafenone.	Alanine	15-22	potassium voltage-gated channel subfamily H member 2	Homo sapiens	35-39
15308760-2	2004	In this study, alanine-substituted HERG channel mutants of inner cavity residues were expressed in Xenopus laevis oocytes and were used to characterize the HERG channel binding site of the antiarrhythmic propafenone.	Alanine	15-22	potassium voltage-gated channel subfamily H member 2	Homo sapiens	156-160
15308760-2	2004	In this study, alanine-substituted HERG channel mutants of inner cavity residues were expressed in Xenopus laevis oocytes and were used to characterize the HERG channel binding site of the antiarrhythmic propafenone.	Propafenone	204-215	potassium voltage-gated channel subfamily H member 2	Homo sapiens	35-39
15308760-2	2004	In this study, alanine-substituted HERG channel mutants of inner cavity residues were expressed in Xenopus laevis oocytes and were used to characterize the HERG channel binding site of the antiarrhythmic propafenone.	Propafenone	204-215	potassium voltage-gated channel subfamily H member 2	Homo sapiens	156-160
15308760-3	2004	Propafenone"s blockade of HERG was strongly dependent on residue Phe656 but was insensitive or weakly sensitive to mutation of Tyr652, Thr623, Ser624, Val625, Gly648, or Val659 and did not require functional inactivation.	Propafenone	0-11	potassium voltage-gated channel subfamily H member 2	Homo sapiens	26-30
15308760-4	2004	Homology models of HERG based on KcsA and MthK crystal structures, representing the closed and open forms of the channel, respectively, suggest propafenone is trapped in the inner cavity and is unable to interact exclusively with Phe656 in the closed state (whereas exclusive interactions between propafenone and Phe656 are found in the open-channel model).	Propafenone	144-155	potassium voltage-gated channel subfamily H member 2	Homo sapiens	19-23
15476742-4	2004	We studied the ability of three compounds that inhibit PDE5--sildenafil, tadalafil, and vardenafil--to block the HERG channel.	Sildenafil Citrate	61-71	potassium voltage-gated channel subfamily H member 2	Homo sapiens	113-117
15476742-4	2004	We studied the ability of three compounds that inhibit PDE5--sildenafil, tadalafil, and vardenafil--to block the HERG channel.	Tadalafil	73-82	potassium voltage-gated channel subfamily H member 2	Homo sapiens	113-117
15476742-4	2004	We studied the ability of three compounds that inhibit PDE5--sildenafil, tadalafil, and vardenafil--to block the HERG channel.	Vardenafil Dihydrochloride	88-98	potassium voltage-gated channel subfamily H member 2	Homo sapiens	113-117
15476742-8	2004	Because the maximum soluble concentration of tadalafil (100 microM) produced only a 50.9% inhibition of the HERG current amplitude, the IC50 value for tadalafil could not be determined with the Hill equation.	Tadalafil	45-54	potassium voltage-gated channel subfamily H member 2	Homo sapiens	108-112
15476742-9	2004	Tadalafil had the weakest capacity to block the HERG channel, producing a 50.9% blockade at the maximum soluble concentration (100 microM), compared with 86.2% for vardenafil (100 microM) and 75.2% for sildenafil (100 microM).	Tadalafil	0-9	potassium voltage-gated channel subfamily H member 2	Homo sapiens	48-52
15476742-9	2004	Tadalafil had the weakest capacity to block the HERG channel, producing a 50.9% blockade at the maximum soluble concentration (100 microM), compared with 86.2% for vardenafil (100 microM) and 75.2% for sildenafil (100 microM).	Vardenafil Dihydrochloride	164-174	potassium voltage-gated channel subfamily H member 2	Homo sapiens	48-52
15476742-9	2004	Tadalafil had the weakest capacity to block the HERG channel, producing a 50.9% blockade at the maximum soluble concentration (100 microM), compared with 86.2% for vardenafil (100 microM) and 75.2% for sildenafil (100 microM).	Sildenafil Citrate	202-212	potassium voltage-gated channel subfamily H member 2	Homo sapiens	48-52
15169846-0	2004	Functional interaction between extracellular sodium, potassium and inactivation gating in HERG channels.	Sodium	45-51	potassium voltage-gated channel subfamily H member 2	Homo sapiens	90-94
15169846-0	2004	Functional interaction between extracellular sodium, potassium and inactivation gating in HERG channels.	Potassium	53-62	potassium voltage-gated channel subfamily H member 2	Homo sapiens	90-94
15266014-0	2004	Structural determinants of HERG channel block by clofilium and ibutilide.	clofilium	49-58	potassium voltage-gated channel subfamily H member 2	Homo sapiens	27-31
15266014-0	2004	Structural determinants of HERG channel block by clofilium and ibutilide.	ibutilide	63-72	potassium voltage-gated channel subfamily H member 2	Homo sapiens	27-31
15266014-7	2004	Clofilium, a chlorobenzene derivative, is a potent blocker of HERG channels, but has a remarkably slower time course for recovery from block than ibutilide, a methanesulfonanilide.	clofilium	0-9	potassium voltage-gated channel subfamily H member 2	Homo sapiens	62-66
15266014-9	2004	There is little recovery from clofilium block with D540K HERG channels that permit untrapping at hyperpolarized potentials.	clofilium	30-39	potassium voltage-gated channel subfamily H member 2	Homo sapiens	57-61
15266014-11	2004	However, S624A, located at the base of the pore helix, was the only HERG mutation that enabled rapid recovery from clofilium block.	clofilium	115-124	potassium voltage-gated channel subfamily H member 2	Homo sapiens	68-72
15266014-12	2004	In summary, the pore helix residues are important components of the HERG drug binding site, and may be particularly important for drugs with polar substituents, such as a halogen (e.g., clofilium) or a methanesulfonamide (e.g., ibutilide).	Halogens	171-178	potassium voltage-gated channel subfamily H member 2	Homo sapiens	68-72
15266014-12	2004	In summary, the pore helix residues are important components of the HERG drug binding site, and may be particularly important for drugs with polar substituents, such as a halogen (e.g., clofilium) or a methanesulfonamide (e.g., ibutilide).	clofilium	186-195	potassium voltage-gated channel subfamily H member 2	Homo sapiens	68-72
15266014-12	2004	In summary, the pore helix residues are important components of the HERG drug binding site, and may be particularly important for drugs with polar substituents, such as a halogen (e.g., clofilium) or a methanesulfonamide (e.g., ibutilide).	methanesulfonamide	202-220	potassium voltage-gated channel subfamily H member 2	Homo sapiens	68-72
15266014-12	2004	In summary, the pore helix residues are important components of the HERG drug binding site, and may be particularly important for drugs with polar substituents, such as a halogen (e.g., clofilium) or a methanesulfonamide (e.g., ibutilide).	ibutilide	228-237	potassium voltage-gated channel subfamily H member 2	Homo sapiens	68-72
15322737-4	2004	Therefore, we investigated the effect of trazodone on HERG potassium channels expressed in human embryonic kidney (HEK) cells and in Xenopus oocytes.	Trazodone	41-50	potassium voltage-gated channel subfamily H member 2	Homo sapiens	54-58
15322737-5	2004	Trazodone inhibited HERG currents in a dose-dependent manner with an IC50 of 2.9 microM in HEK cells and 13.2 microM in Xenopus oocytes.	Trazodone	0-9	potassium voltage-gated channel subfamily H member 2	Homo sapiens	20-24
15322737-7	2004	In HERG channel mutants Y652A and F656A lacking aromatic residues in the S6 domain, the affinity of trazodone was reduced profoundly.	Trazodone	100-109	potassium voltage-gated channel subfamily H member 2	Homo sapiens	3-7
15322737-8	2004	Trazodone accelerated inactivation of HERG currents without markedly affecting activation.	Trazodone	0-9	potassium voltage-gated channel subfamily H member 2	Homo sapiens	38-42
15322737-11	2004	Trazodone block of HERG channels was state dependent.	Trazodone	0-9	potassium voltage-gated channel subfamily H member 2	Homo sapiens	19-23
15322737-13	2004	In summary, the atypical antidepressant trazodone blocks cardiac HERG channels at concentrations that are probably relevant in vivo, particularly in overdosage.	Trazodone	40-49	potassium voltage-gated channel subfamily H member 2	Homo sapiens	65-69
15189761-0	2004	Comparison of kinetic properties of quinidine and dofetilide block of HERG channels.	Quinidine	36-45	potassium voltage-gated channel subfamily H member 2	Homo sapiens	70-74
14586519-2	2004	Inward HERG currents were recorded on hyperpolarization in 140 mM external Cs(+) and Rb(+), as well as K(+).	Cesium	75-80	potassium voltage-gated channel subfamily H member 2	Homo sapiens	7-11
14586519-2	2004	Inward HERG currents were recorded on hyperpolarization in 140 mM external Cs(+) and Rb(+), as well as K(+).	Rubidium	85-90	potassium voltage-gated channel subfamily H member 2	Homo sapiens	7-11
15189761-0	2004	Comparison of kinetic properties of quinidine and dofetilide block of HERG channels.	dofetilide	50-60	potassium voltage-gated channel subfamily H member 2	Homo sapiens	70-74
15189761-2	2004	We examined the kinetic properties of quinidine block of HERG channels expressed in Xenopus oocytes in comparison with those of the block by a class III antiarrhythmic dofetilide.	Quinidine	38-47	potassium voltage-gated channel subfamily H member 2	Homo sapiens	57-61
15189761-8	2004	In contrast, dofetilide blocked HERG currents in a voltage- and time-independent manner under the steady state because of very slow unblocking at negative potentials, which also caused frequency-independent block.	dofetilide	13-23	potassium voltage-gated channel subfamily H member 2	Homo sapiens	32-36
14975928-12	2004	All HERG channels had similar sensitivity to block by cisapride.	Cisapride	54-63	potassium voltage-gated channel subfamily H member 2	Homo sapiens	4-8
15148258-0	2004	Inhibition of cardiac HERG currents by the DNA topoisomerase II inhibitor amsacrine: mode of action.	Amsacrine	74-83	potassium voltage-gated channel subfamily H member 2	Homo sapiens	22-26
15148258-3	2004	Since blockade of cardiac human ether-a-go-go-related gene (HERG) potassium currents is an important cause of acquired LQTS, we investigated the acute effects of amsacrine on cloned HERG channels to determine the electrophysiological basis for its proarrhythmic potential.	Potassium	66-75	potassium voltage-gated channel subfamily H member 2	Homo sapiens	60-64
15148258-4	2004	2 HERG channels were heterologously expressed in human HEK 293 cells and Xenopus laevis oocytes, and the respective potassium currents were recorded using patch-clamp and two-microelectrode voltage-clamp electrophysiology.	Potassium	116-125	potassium voltage-gated channel subfamily H member 2	Homo sapiens	2-6
15148258-5	2004	3 Amsacrine blocked HERG currents in HEK 293 cells and Xenopus oocytes in a concentration-dependent manner, with IC50 values of 209.4 nm and 2.0 microm, respectively.	Amsacrine	2-11	potassium voltage-gated channel subfamily H member 2	Homo sapiens	20-24
15148258-8	2004	HERG current block by amsacrine was not frequency dependent.	Amsacrine	22-31	potassium voltage-gated channel subfamily H member 2	Homo sapiens	0-4
15148258-9	2004	5 The S6 domain mutations Y652A and F656A attenuated (Y652A) or abolished (F656A, Y652A/F656A) HERG current blockade, indicating that amsacrine binding requires a common drug receptor within the pore-S6 region.	Amsacrine	134-143	potassium voltage-gated channel subfamily H member 2	Homo sapiens	95-99
15148258-10	2004	6 In conclusion, these data demonstrate that the anticancer drug amsacrine is an antagonist of cloned HERG potassium channels, providing a molecular mechanism for the previously reported QTc interval prolongation during clinical administration of amsacrine.	Amsacrine	65-74	potassium voltage-gated channel subfamily H member 2	Homo sapiens	102-106
15148258-10	2004	6 In conclusion, these data demonstrate that the anticancer drug amsacrine is an antagonist of cloned HERG potassium channels, providing a molecular mechanism for the previously reported QTc interval prolongation during clinical administration of amsacrine.	Amsacrine	247-256	potassium voltage-gated channel subfamily H member 2	Homo sapiens	102-106
14744814-0	2004	Potential mechanisms for the enhancement of HERG K+ channel function by phospholipid metabolites.	Phospholipids	72-84	potassium voltage-gated channel subfamily H member 2	Homo sapiens	44-48
15272206-0	2004	Validation of a [3H]astemizole binding assay in HEK293 cells expressing HERG K+ channels.	Tritium	17-19	potassium voltage-gated channel subfamily H member 2	Homo sapiens	72-76
15071359-0	2004	Block of HERG human K(+) channel and IKr of guinea pig cardiomyocytes by chlorpromazine.	Chlorpromazine	73-87	potassium voltage-gated channel subfamily H member 2	Homo sapiens	9-13
15071359-2	2004	We studied the effects of chlorpromazine on the human ether-a-go-go-related gene (HERG) channel expressed in Xenopus oocytes and on delayed rectifier K current of guinea pig ventricular myocytes.	Chlorpromazine	26-40	potassium voltage-gated channel subfamily H member 2	Homo sapiens	82-86
15071359-3	2004	Application of chlorpromazine showed a dose-dependent decrease in the amplitudes of steady-state currents and tail currents of HERG.	Chlorpromazine	15-29	potassium voltage-gated channel subfamily H member 2	Homo sapiens	127-131
15071359-4	2004	The decrease became more pronounced at increasingly positive potential, suggesting that the blockade of HERG by chlorpromazine is voltage dependent.	Chlorpromazine	112-126	potassium voltage-gated channel subfamily H member 2	Homo sapiens	104-108
15071359-5	2004	IC50 for chlorpromazine block of HERG current was progressively decreased according to depolarization: IC50 values at -30, 0, and +30 mV were 10.5, 8.8, and 4.9 microM, respectively.	Chlorpromazine	9-23	potassium voltage-gated channel subfamily H member 2	Homo sapiens	33-37
15071359-9	2004	Our findings suggest that the arrhythmogenic side effect of chlorpromazine is caused by blockade of HERG and rapid component of delayed rectifier K current rather than by blockade of the slow component.	Chlorpromazine	60-74	potassium voltage-gated channel subfamily H member 2	Homo sapiens	100-104
15272206-0	2004	Validation of a [3H]astemizole binding assay in HEK293 cells expressing HERG K+ channels.	Astemizole	20-30	potassium voltage-gated channel subfamily H member 2	Homo sapiens	72-76
15272206-2	2004	Pharmacological characterization of the [(3)H]astemizole binding assay for HERG K(+) channels was performed using HERG-expressing HEK293 cells.	Astemizole	46-56	potassium voltage-gated channel subfamily H member 2	Homo sapiens	75-79
15272206-2	2004	Pharmacological characterization of the [(3)H]astemizole binding assay for HERG K(+) channels was performed using HERG-expressing HEK293 cells.	Astemizole	46-56	potassium voltage-gated channel subfamily H member 2	Homo sapiens	114-118
15272206-5	2004	Binding affinities for 32 reference compounds (including dofetilide, cisapride, and terfenadine) with diverse structures demonstrated a similar potency rank order for HERG inhibition to that reported in the literature.	dofetilide	57-67	potassium voltage-gated channel subfamily H member 2	Homo sapiens	167-171
15272206-5	2004	Binding affinities for 32 reference compounds (including dofetilide, cisapride, and terfenadine) with diverse structures demonstrated a similar potency rank order for HERG inhibition to that reported in the literature.	Cisapride	69-78	potassium voltage-gated channel subfamily H member 2	Homo sapiens	167-171
15272206-5	2004	Binding affinities for 32 reference compounds (including dofetilide, cisapride, and terfenadine) with diverse structures demonstrated a similar potency rank order for HERG inhibition to that reported in the literature.	Terfenadine	84-95	potassium voltage-gated channel subfamily H member 2	Homo sapiens	167-171
15272206-6	2004	Moreover, the [(3)H]astemizole binding data demonstrated a rank order of affinity that was highly correlated to that of inhibitory potency in the electrophysiological studies for HERG in HEK293 (r(SP) = 0.91, P<0.05).	Tritium	14-19	potassium voltage-gated channel subfamily H member 2	Homo sapiens	179-183
15272206-6	2004	Moreover, the [(3)H]astemizole binding data demonstrated a rank order of affinity that was highly correlated to that of inhibitory potency in the electrophysiological studies for HERG in HEK293 (r(SP) = 0.91, P<0.05).	Astemizole	20-30	potassium voltage-gated channel subfamily H member 2	Homo sapiens	179-183
15272206-7	2004	In conclusion, the [(3)H]astemizole binding assay is rapid and capable of detecting HERG inhibitors.	Astemizole	25-35	potassium voltage-gated channel subfamily H member 2	Homo sapiens	84-88
15120636-0	2004	Potent inhibition of human cardiac potassium (HERG) channels by the anti-estrogen agent clomiphene-without QT interval prolongation.	Clomiphene	88-98	potassium voltage-gated channel subfamily H member 2	Homo sapiens	46-50
15120636-3	2004	We describe here a potent inhibitory effect (IC(50) = 0.18 microM) of clomiphene on HERG ionic current (I(HERG)) recorded from a mammalian cell line expressing HERG channels.	Clomiphene	70-80	potassium voltage-gated channel subfamily H member 2	Homo sapiens	84-88
15120636-3	2004	We describe here a potent inhibitory effect (IC(50) = 0.18 microM) of clomiphene on HERG ionic current (I(HERG)) recorded from a mammalian cell line expressing HERG channels.	Clomiphene	70-80	potassium voltage-gated channel subfamily H member 2	Homo sapiens	106-110
15120636-3	2004	We describe here a potent inhibitory effect (IC(50) = 0.18 microM) of clomiphene on HERG ionic current (I(HERG)) recorded from a mammalian cell line expressing HERG channels.	Clomiphene	70-80	potassium voltage-gated channel subfamily H member 2	Homo sapiens	106-110
15120636-4	2004	Inhibition of I(HERG) by clomiphene showed voltage-dependence and developed quickly following membrane depolarisation, indicating contingency of block on HERG channel gating.	Clomiphene	25-35	potassium voltage-gated channel subfamily H member 2	Homo sapiens	16-20
15120636-4	2004	Inhibition of I(HERG) by clomiphene showed voltage-dependence and developed quickly following membrane depolarisation, indicating contingency of block on HERG channel gating.	Clomiphene	25-35	potassium voltage-gated channel subfamily H member 2	Homo sapiens	154-158
15120636-5	2004	At 100 nM, clomiphene and the related anti-estrogen tamoxifen produced similar levels of I(HERG) blockade (p > 0.05).	Clomiphene	11-21	potassium voltage-gated channel subfamily H member 2	Homo sapiens	91-95
15120636-5	2004	At 100 nM, clomiphene and the related anti-estrogen tamoxifen produced similar levels of I(HERG) blockade (p > 0.05).	Tamoxifen	52-61	potassium voltage-gated channel subfamily H member 2	Homo sapiens	91-95
15120636-7	2004	The disparity between clomiphene"s potent I(HERG) inhibition and its lack of effect on the QT interval underscores the notion that I(HERG) pharmacology may best be used alongside other screening methods when investigating the QT-prolonging tendency and related cardiotoxicity of non-cardiac drugs.	Clomiphene	22-32	potassium voltage-gated channel subfamily H member 2	Homo sapiens	44-48
15120636-7	2004	The disparity between clomiphene"s potent I(HERG) inhibition and its lack of effect on the QT interval underscores the notion that I(HERG) pharmacology may best be used alongside other screening methods when investigating the QT-prolonging tendency and related cardiotoxicity of non-cardiac drugs.	Clomiphene	22-32	potassium voltage-gated channel subfamily H member 2	Homo sapiens	133-137
15125690-2	2004	The ether-a-go-go-related gene, HERG, is a primary target for blockade by many drugs including dofetilide, quinidine and azimilide.	dofetilide	95-105	potassium voltage-gated channel subfamily H member 2	Homo sapiens	32-36
15125690-2	2004	The ether-a-go-go-related gene, HERG, is a primary target for blockade by many drugs including dofetilide, quinidine and azimilide.	Quinidine	107-116	potassium voltage-gated channel subfamily H member 2	Homo sapiens	32-36
15125690-2	2004	The ether-a-go-go-related gene, HERG, is a primary target for blockade by many drugs including dofetilide, quinidine and azimilide.	azimilide	121-130	potassium voltage-gated channel subfamily H member 2	Homo sapiens	32-36
15125690-10	2004	Acidification weakened the inhibitory effects of quinidine and azimilide on HERG channels.	Quinidine	49-58	potassium voltage-gated channel subfamily H member 2	Homo sapiens	76-80
15125690-10	2004	Acidification weakened the inhibitory effects of quinidine and azimilide on HERG channels.	azimilide	63-72	potassium voltage-gated channel subfamily H member 2	Homo sapiens	76-80
15125690-12	2004	Acidification markedly potentiated dofetilide blockade of the HERG channels but weakened the inhibitory effects of quinidine and azimilide.	dofetilide	35-45	potassium voltage-gated channel subfamily H member 2	Homo sapiens	62-66
15168062-0	2004	Block of HERG current expressed in HEK293 cells by the Na+-channel blocker cibenzoline.	cifenline	75-86	potassium voltage-gated channel subfamily H member 2	Homo sapiens	9-13
15168062-1	2004	A Na(+)-channel blocker, cibenzoline, blocks the delayed rectifier potassium current ( I(k)), but its detailed action on the rapidly activating component ( I(kr)) of I(k) encoded by the human ether-a-go-go-related gene ( HERG) has not been clarified.	cifenline	25-36	potassium voltage-gated channel subfamily H member 2	Homo sapiens	221-225
15168062-2	2004	We examined the effects of cibenzoline on stably expressed HERG current in HEK293 cells recorded by the patch-clamp technique of whole-cell configuration.	cifenline	27-38	potassium voltage-gated channel subfamily H member 2	Homo sapiens	59-63
15168062-3	2004	Cibenzoline blocked HERG current expressed in HEK293 cells with IC(50) = 3.7 +/- 0.963 micro M and Hill coefficient = 0.74 +/- 0.12.	cifenline	0-11	potassium voltage-gated channel subfamily H member 2	Homo sapiens	20-24
15168062-9	2004	Cibenzoline blocks the I(kr)-like current reconstituted by HERG clone transfection with an IC(50) value comparable to therapeutic concentrations.	cifenline	0-11	potassium voltage-gated channel subfamily H member 2	Homo sapiens	59-63
15168062-10	2004	Cibenzoline has a preferential affinity, at least, to the open state of the HERG channel with a rapid access to the binding site.	cifenline	0-11	potassium voltage-gated channel subfamily H member 2	Homo sapiens	76-80
15135665-0	2004	Lidoflazine is a high affinity blocker of the HERG K(+)channel.	Lidoflazine	0-11	potassium voltage-gated channel subfamily H member 2	Homo sapiens	46-50
15135665-3	2004	Lidoflazine inhibited potently HERG current (I(HERG)) recorded from HEK 293 cells stably expressing wild-type HERG (IC(50) of approximately 16 nM).	Lidoflazine	0-11	potassium voltage-gated channel subfamily H member 2	Homo sapiens	31-35
15135665-3	2004	Lidoflazine inhibited potently HERG current (I(HERG)) recorded from HEK 293 cells stably expressing wild-type HERG (IC(50) of approximately 16 nM).	Lidoflazine	0-11	potassium voltage-gated channel subfamily H member 2	Homo sapiens	47-51
15135665-3	2004	Lidoflazine inhibited potently HERG current (I(HERG)) recorded from HEK 293 cells stably expressing wild-type HERG (IC(50) of approximately 16 nM).	Lidoflazine	0-11	potassium voltage-gated channel subfamily H member 2	Homo sapiens	47-51
15135665-6	2004	The effect of command voltage on the drug"s action suggested that lidoflazine preferentially inhibits activated/open HERG channels.	Lidoflazine	66-77	potassium voltage-gated channel subfamily H member 2	Homo sapiens	117-121
15135665-8	2004	We conclude: first, that lidoflazine produces high affinity blockade of the alpha subunit of the HERG channel by binding to aromatic amino acid residues within the channel pore and, second, that this is likely to represent the molecular mechanism of QT interval prolongation by this drug.	Lidoflazine	25-36	potassium voltage-gated channel subfamily H member 2	Homo sapiens	97-101
15135665-8	2004	We conclude: first, that lidoflazine produces high affinity blockade of the alpha subunit of the HERG channel by binding to aromatic amino acid residues within the channel pore and, second, that this is likely to represent the molecular mechanism of QT interval prolongation by this drug.	Amino Acids, Aromatic	124-143	potassium voltage-gated channel subfamily H member 2	Homo sapiens	97-101
15102940-4	2004	Clofilium inhibited hEAG1 and hERG1 with the same potency, whereas hEAG2 was about 150-fold less sensitive to this antiarrhythmic agent.	clofilium	0-9	potassium voltage-gated channel subfamily H member 2	Homo sapiens	30-35
15098086-7	2004	To assess the action of the effects of prazosin, doxazosin, and terazosin on HERG currents, we investigated their acute electrophysiological effects on cloned HERG potassium channels heterologously expressed in Xenopus oocytes and HEK 293 cells.Prazosin, doxazosin, and terazosin blocked HERG currents in Xenopus oocytes with IC(50) values of 10.1, 18.2, and 113.2 microM respectively, whereas the IC(50) values for HERG channel inhibition in human HEK 293 cells were 1.57 microM, 585.1 nM, and 17.7 microM.	Terazosin	64-73	potassium voltage-gated channel subfamily H member 2	Homo sapiens	77-81
14711935-4	2004	Using patch-clamp electrophysiology, we found that tolterodine was a potent antagonist of the human ether-a-go-go-related gene (HERG) K(+) channel, displaying an IC(50) value of 17 nM.	Tolterodine Tartrate	51-62	potassium voltage-gated channel subfamily H member 2	Homo sapiens	128-132
14711935-6	2004	Tolterodine block of HERG displayed a positive voltage dependence, suggesting an interaction with an activated state.	Tolterodine Tartrate	0-11	potassium voltage-gated channel subfamily H member 2	Homo sapiens	21-25
14711935-11	2004	Tolterodine seems to be an unusual drug in that it blocks HERG with high affinity, but produces little QT prolongation clinically.	Tolterodine Tartrate	0-11	potassium voltage-gated channel subfamily H member 2	Homo sapiens	58-62
15098086-12	2004	The S6 mutations Y652A and F656A partially attenuated (Y652A) or abolished (F656A) HERG current blockade, indicating that prazosin binds to a common drug receptor within the pore-S6 region.	Prazosin	122-130	potassium voltage-gated channel subfamily H member 2	Homo sapiens	83-87
15098086-13	2004	In conclusion, this study demonstrates that HERG potassium channels are blocked by prazosin, doxazosin, and terazosin.	Prazosin	83-91	potassium voltage-gated channel subfamily H member 2	Homo sapiens	44-48
15098086-13	2004	In conclusion, this study demonstrates that HERG potassium channels are blocked by prazosin, doxazosin, and terazosin.	Doxazosin	93-102	potassium voltage-gated channel subfamily H member 2	Homo sapiens	44-48
15098086-13	2004	In conclusion, this study demonstrates that HERG potassium channels are blocked by prazosin, doxazosin, and terazosin.	Terazosin	108-117	potassium voltage-gated channel subfamily H member 2	Homo sapiens	44-48
14744814-3	2004	Here we studied effects of several lysophospholipids with different lengths of hydrocarbon chains and charged headgroups on HERG K(+) currents (I(HERG)) expressed in HEK293 cells and the potential mechanisms using whole-cell patch-clamp techniques.	Lysophospholipids	35-52	potassium voltage-gated channel subfamily H member 2	Homo sapiens	124-128
14744814-3	2004	Here we studied effects of several lysophospholipids with different lengths of hydrocarbon chains and charged headgroups on HERG K(+) currents (I(HERG)) expressed in HEK293 cells and the potential mechanisms using whole-cell patch-clamp techniques.	Lysophospholipids	35-52	potassium voltage-gated channel subfamily H member 2	Homo sapiens	146-150
14744814-5	2004	Only the lipids with 16 hydrocarbons such as 1-palmitoyl-lysophosphatidylcholine (LPC-16) and 1-palmitoyl-lysophosphatidylglycerol (LPG-16) were found to produce significant enhancement of I(HERG) and negative shifts of HERG activation, although the voltage dependence of the effects was different between LPC-16 and LPG-16 which have differently charged headgroups.	We 201	45-80	potassium voltage-gated channel subfamily H member 2	Homo sapiens	191-195
14744814-5	2004	Only the lipids with 16 hydrocarbons such as 1-palmitoyl-lysophosphatidylcholine (LPC-16) and 1-palmitoyl-lysophosphatidylglycerol (LPG-16) were found to produce significant enhancement of I(HERG) and negative shifts of HERG activation, although the voltage dependence of the effects was different between LPC-16 and LPG-16 which have differently charged headgroups.	We 201	45-80	potassium voltage-gated channel subfamily H member 2	Homo sapiens	220-224
14744814-5	2004	Only the lipids with 16 hydrocarbons such as 1-palmitoyl-lysophosphatidylcholine (LPC-16) and 1-palmitoyl-lysophosphatidylglycerol (LPG-16) were found to produce significant enhancement of I(HERG) and negative shifts of HERG activation, although the voltage dependence of the effects was different between LPC-16 and LPG-16 which have differently charged headgroups.	1-palmitoyl-lysophosphatidylglycerol	94-130	potassium voltage-gated channel subfamily H member 2	Homo sapiens	191-195
14744814-5	2004	Only the lipids with 16 hydrocarbons such as 1-palmitoyl-lysophosphatidylcholine (LPC-16) and 1-palmitoyl-lysophosphatidylglycerol (LPG-16) were found to produce significant enhancement of I(HERG) and negative shifts of HERG activation, although the voltage dependence of the effects was different between LPC-16 and LPG-16 which have differently charged headgroups.	1-palmitoyl-lysophosphatidylglycerol	94-130	potassium voltage-gated channel subfamily H member 2	Homo sapiens	220-224
14744814-6	2004	The lipid with 18 hydrocarbons modestly increased I(HERG).	Hydrocarbons	18-30	potassium voltage-gated channel subfamily H member 2	Homo sapiens	52-56
14744814-14	2004	We conclude that enhancement of HERG function by lysophospholipids is specific to the lipids with 16-hydrocarbon chain structure and the pattern of voltage dependence is determined by the polar headgroups.	Lysophospholipids	49-66	potassium voltage-gated channel subfamily H member 2	Homo sapiens	32-36
15176423-2	2004	Inhibition of HERG potassium currents by class III antiarrhythmic drugs causes lengthening of the cardiac action potential, which produces a beneficial antiarrhythmic effect.	Potassium	19-28	potassium voltage-gated channel subfamily H member 2	Homo sapiens	14-18
14709917-5	2004	Terfenadine 1 microM completely inhibited the human ether a go-go-related gene (HERG) channel current expressed in HEK293 cells in the same experimental solution as in microelectrode experiments.	Terfenadine	0-11	potassium voltage-gated channel subfamily H member 2	Homo sapiens	80-84
14665560-8	2004	RESULTS: The amide local anaesthetics bupivacaine, levobupivacaine and ropivacaine inhibited HERG channels at toxicologically relevant concentrations, with IC(50) values of 20 (SEM 2) micro M (n=29), 10 (1) micro M (n=40) and 20 (2) micro M (n=49), respectively.	Amides	13-18	potassium voltage-gated channel subfamily H member 2	Homo sapiens	93-97
14665560-8	2004	RESULTS: The amide local anaesthetics bupivacaine, levobupivacaine and ropivacaine inhibited HERG channels at toxicologically relevant concentrations, with IC(50) values of 20 (SEM 2) micro M (n=29), 10 (1) micro M (n=40) and 20 (2) micro M (n=49), respectively.	Bupivacaine	38-49	potassium voltage-gated channel subfamily H member 2	Homo sapiens	93-97
14665560-8	2004	RESULTS: The amide local anaesthetics bupivacaine, levobupivacaine and ropivacaine inhibited HERG channels at toxicologically relevant concentrations, with IC(50) values of 20 (SEM 2) micro M (n=29), 10 (1) micro M (n=40) and 20 (2) micro M (n=49), respectively.	Levobupivacaine	51-66	potassium voltage-gated channel subfamily H member 2	Homo sapiens	93-97
14665560-8	2004	RESULTS: The amide local anaesthetics bupivacaine, levobupivacaine and ropivacaine inhibited HERG channels at toxicologically relevant concentrations, with IC(50) values of 20 (SEM 2) micro M (n=29), 10 (1) micro M (n=40) and 20 (2) micro M (n=49), respectively.	Ropivacaine	71-82	potassium voltage-gated channel subfamily H member 2	Homo sapiens	93-97
14665560-13	2004	CONCLUSIONS: Amide local anaesthetics target HERG and HERG/MiRP1 channels with identical potency.	Amides	13-18	potassium voltage-gated channel subfamily H member 2	Homo sapiens	45-49
14665560-13	2004	CONCLUSIONS: Amide local anaesthetics target HERG and HERG/MiRP1 channels with identical potency.	Amides	13-18	potassium voltage-gated channel subfamily H member 2	Homo sapiens	54-58
15107589-0	2004	HERG K channel conductance promotes H2O2-induced apoptosis in HEK293 cells: cellular mechanisms.	Hydrogen Peroxide	36-40	potassium voltage-gated channel subfamily H member 2	Homo sapiens	0-4
15107589-9	2004	HERG expression facilitates DNA fragmentation induced by H(2)O(2) at a concentration-dependent fashion, starting at 200 microM and reaching maximum at 1 mM.	Hydrogen Peroxide	57-65	potassium voltage-gated channel subfamily H member 2	Homo sapiens	0-4
15107589-11	2004	Inhibition of p38 by SB-203580 alleviated DNA-F and PD-98059, which inhibited activation of ERKs, nearly abolished DNA-F. Immunoblotting analysis demonstrated that p38, SAPKs and ERKs MAP kinases were all substantially activated (>10-fold higher) in HERG-expressing cells vs. non-transfected cells.	2-(2-amino-3-methoxyphenyl)-4H-1-benzopyran-4-one	52-60	potassium voltage-gated channel subfamily H member 2	Homo sapiens	253-257
14744814-14	2004	We conclude that enhancement of HERG function by lysophospholipids is specific to the lipids with 16-hydrocarbon chain structure and the pattern of voltage dependence is determined by the polar headgroups.	Hydrocarbons	101-112	potassium voltage-gated channel subfamily H member 2	Homo sapiens	32-36
14646167-4	2003	In conclusion, these evaluation methods demonstrated that ER-118585 could prolong the QT interval via APD prolongation, attributable to the inhibition of the HERG potassium current.	Potassium	163-172	potassium voltage-gated channel subfamily H member 2	Homo sapiens	158-162
15371638-3	2004	Within those segments thought to contribute to the channel pore, HERG possesses several serine residues that are not present in EAG channels.	Serine	88-94	potassium voltage-gated channel subfamily H member 2	Homo sapiens	65-69
15371638-6	2004	As with the other serines, S641 is also involved in maintaining ion selectivity of the HERG channel and alters sensitivity to block by E4031.	Serine	18-25	potassium voltage-gated channel subfamily H member 2	Homo sapiens	87-91
15371638-6	2004	As with the other serines, S641 is also involved in maintaining ion selectivity of the HERG channel and alters sensitivity to block by E4031.	3-Methoxydiphenylamine	27-31	potassium voltage-gated channel subfamily H member 2	Homo sapiens	87-91
15371638-6	2004	As with the other serines, S641 is also involved in maintaining ion selectivity of the HERG channel and alters sensitivity to block by E4031.	E 4031	135-140	potassium voltage-gated channel subfamily H member 2	Homo sapiens	87-91
14734057-2	2004	In this study, we examined the effects of mesoridazine on human ether-a-go-go-related gene (HERG) K+ currents.	Mesoridazine	42-54	potassium voltage-gated channel subfamily H member 2	Homo sapiens	92-96
14734057-4	2004	Mesoridazine blocked HERG currents in a concentration-dependent manner (IC50 550 nM at 0 mV); block increased significantly over the voltage range where HERG activates and saturated at voltages eliciting maximal HERG channel activation.	Mesoridazine	0-12	potassium voltage-gated channel subfamily H member 2	Homo sapiens	21-25
14734057-4	2004	Mesoridazine blocked HERG currents in a concentration-dependent manner (IC50 550 nM at 0 mV); block increased significantly over the voltage range where HERG activates and saturated at voltages eliciting maximal HERG channel activation.	Mesoridazine	0-12	potassium voltage-gated channel subfamily H member 2	Homo sapiens	153-157
14734057-4	2004	Mesoridazine blocked HERG currents in a concentration-dependent manner (IC50 550 nM at 0 mV); block increased significantly over the voltage range where HERG activates and saturated at voltages eliciting maximal HERG channel activation.	Mesoridazine	0-12	potassium voltage-gated channel subfamily H member 2	Homo sapiens	153-157
14734057-5	2004	Tonic block of HERG current by mesoridazine (1.8 microM) was minimal (< 2-4%).	Mesoridazine	31-43	potassium voltage-gated channel subfamily H member 2	Homo sapiens	15-19
14734057-6	2004	The rate of the onset of HERG channel block was rapid and dose dependent (tau = 54 +/- 7 ms at 0 mV and 1.8 microM mesoridazine), but not significantly affected by test potentials ranging from -30 to +30 mV.	Mesoridazine	115-127	potassium voltage-gated channel subfamily H member 2	Homo sapiens	25-29
14734057-10	2004	These findings demonstrate that mesoridazine is a potent and rapid open-channel blocker of HERG channels.	Mesoridazine	32-44	potassium voltage-gated channel subfamily H member 2	Homo sapiens	91-95
14525949-6	2003	Functionally, KCR1 reduces the sensitivity of HERG to classic proarrhythmic HERG blockers (sotalol, quinidine, dofetilide) in both cardiac and noncardiac cell lines.	Sotalol	91-98	potassium voltage-gated channel subfamily H member 2	Homo sapiens	46-50
14525949-6	2003	Functionally, KCR1 reduces the sensitivity of HERG to classic proarrhythmic HERG blockers (sotalol, quinidine, dofetilide) in both cardiac and noncardiac cell lines.	Sotalol	91-98	potassium voltage-gated channel subfamily H member 2	Homo sapiens	76-80
14525949-6	2003	Functionally, KCR1 reduces the sensitivity of HERG to classic proarrhythmic HERG blockers (sotalol, quinidine, dofetilide) in both cardiac and noncardiac cell lines.	Quinidine	100-109	potassium voltage-gated channel subfamily H member 2	Homo sapiens	46-50
14525949-6	2003	Functionally, KCR1 reduces the sensitivity of HERG to classic proarrhythmic HERG blockers (sotalol, quinidine, dofetilide) in both cardiac and noncardiac cell lines.	dofetilide	111-121	potassium voltage-gated channel subfamily H member 2	Homo sapiens	46-50
14525949-6	2003	Functionally, KCR1 reduces the sensitivity of HERG to classic proarrhythmic HERG blockers (sotalol, quinidine, dofetilide) in both cardiac and noncardiac cell lines.	dofetilide	111-121	potassium voltage-gated channel subfamily H member 2	Homo sapiens	76-80
14674677-0	2003	Characterization of the inhibitory effects of erythromycin and clarithromycin on the HERG potassium channel.	Erythromycin	46-58	potassium voltage-gated channel subfamily H member 2	Homo sapiens	85-89
14642687-0	2003	A new oral therapy for long QT syndrome: long-term oral potassium improves repolarization in patients with HERG mutations.	Potassium	56-65	potassium voltage-gated channel subfamily H member 2	Homo sapiens	107-111
14642687-1	2003	OBJECTIVES: We sought to determine whether oral potassium supplementation safely increases serum K(+) and results in sustained improvement of repolarization parameters in long QT syndrome type 2 (LQT2) subjects.	Potassium	48-57	potassium voltage-gated channel subfamily H member 2	Homo sapiens	196-200
14642687-4	2003	We tested the hypothesis that long-term oral potassium supplementation results in a mild, sustainable increase in serum K(+) that improves repolarization abnormalities in subjects with LQT2.	Potassium	45-54	potassium voltage-gated channel subfamily H member 2	Homo sapiens	185-189
14642687-13	2003	CONCLUSIONS: Long-term oral potassium administration increases serum K(+) in patients with LQT2.	Potassium	28-37	potassium voltage-gated channel subfamily H member 2	Homo sapiens	91-95
14674677-0	2003	Characterization of the inhibitory effects of erythromycin and clarithromycin on the HERG potassium channel.	Clarithromycin	63-77	potassium voltage-gated channel subfamily H member 2	Homo sapiens	85-89
14674677-2	2003	The goal of this study was to test the hypothesis that these macrolide antibiotics significantly block the delayed rectifier current (IKr) encoded by HERG (the human ether-a-go-go-related gene) at drug concentrations, temperature and ionic conditions mimicking those occurring in human subjects.	Macrolides	61-70	potassium voltage-gated channel subfamily H member 2	Homo sapiens	150-154
14674677-3	2003	Potassium currents in HEK 293 cells stably transfected with HERG were recorded using a whole cell voltage clamp method.	Potassium	0-9	potassium voltage-gated channel subfamily H member 2	Homo sapiens	60-64
14674677-4	2003	Exposure of cells to erythromycin reduced the HERG encoded potassium current in a concentration dependent manner with an IC50 of 38.9 +/- 1.2 microM and Hill Slope factor of 0.4 +/- 0.1.	Erythromycin	21-33	potassium voltage-gated channel subfamily H member 2	Homo sapiens	46-50
14674677-4	2003	Exposure of cells to erythromycin reduced the HERG encoded potassium current in a concentration dependent manner with an IC50 of 38.9 +/- 1.2 microM and Hill Slope factor of 0.4 +/- 0.1.	Potassium	59-68	potassium voltage-gated channel subfamily H member 2	Homo sapiens	46-50
14674677-7	2003	The results of this study document that both erythromycin and clarithromycin significantly inhibit the HERG potassium current at clinically relevant concentrations.	Erythromycin	45-57	potassium voltage-gated channel subfamily H member 2	Homo sapiens	103-107
14674677-7	2003	The results of this study document that both erythromycin and clarithromycin significantly inhibit the HERG potassium current at clinically relevant concentrations.	Clarithromycin	62-76	potassium voltage-gated channel subfamily H member 2	Homo sapiens	103-107
14674677-7	2003	The results of this study document that both erythromycin and clarithromycin significantly inhibit the HERG potassium current at clinically relevant concentrations.	Potassium	108-117	potassium voltage-gated channel subfamily H member 2	Homo sapiens	103-107
14576514-6	2003	Both drugs blocked activated HERG channels in a biexponential decay fashion, with faster time constants for KCB-328 (3 microM) than for dofetilide (0.3 microM).	dofetilide	136-146	potassium voltage-gated channel subfamily H member 2	Homo sapiens	29-33
14557918-0	2003	Drug binding to aromatic residues in the HERG channel pore cavity as possible explanation for acquired Long QT syndrome by antiparkinsonian drug budipine.	budipine	145-153	potassium voltage-gated channel subfamily H member 2	Homo sapiens	41-45
14557918-6	2003	In Xenopus oocytes, HERG potassium channels were blocked by budipine with an IC(50) of 10.2 microM.	budipine	60-68	potassium voltage-gated channel subfamily H member 2	Homo sapiens	20-24
14557918-8	2003	Budipine blocked HERG channels in the open and inactivated state, but not in the closed states.	budipine	0-8	potassium voltage-gated channel subfamily H member 2	Homo sapiens	17-21
14557918-10	2003	Steady-state inactivation of HERG was also influenced by budipine.	budipine	57-65	potassium voltage-gated channel subfamily H member 2	Homo sapiens	29-33
12902341-5	2003	In this study we show that a synthetic 42-residue peptide corresponding to this linker region of the HERG K+ channel does not have defined structural elements in aqueous solution; however, it displays two well defined helical regions when in the presence of SDS micelles.	Sodium Dodecyl Sulfate	258-261	potassium voltage-gated channel subfamily H member 2	Homo sapiens	101-105
12885765-8	2003	This study reveals a novel role of the COOH terminus in the normal biogenesis of HERG channels and suggests defective trafficking as a common mechanism for abnormal channel function resulting from mutations of critical COOH-terminal residues, including the LQTS mutant HERGN861I.	Carbonic Acid	39-43	potassium voltage-gated channel subfamily H member 2	Homo sapiens	81-85
15326914-3	2003	Tertiary amines which form ammonium ions shielded by two structural fragments of the drug molecule were found to be potent HERG/I(Kr) blockers with IC50 < 1 microM (16 of 19 compounds, 84%).	Amines	9-15	potassium voltage-gated channel subfamily H member 2	Homo sapiens	123-127
15326914-3	2003	Tertiary amines which form ammonium ions shielded by two structural fragments of the drug molecule were found to be potent HERG/I(Kr) blockers with IC50 < 1 microM (16 of 19 compounds, 84%).	Ammonium Compounds	27-35	potassium voltage-gated channel subfamily H member 2	Homo sapiens	123-127
15326914-5	2003	Similarly, 27 of 32 weak HERG blockers ( IC50 > 10 microM) were found to be primary or secondary amines, or neutral or very weakly basic compounds.	Amines	100-106	potassium voltage-gated channel subfamily H member 2	Homo sapiens	25-29
15326914-7	2003	Conformational analysis and modeling of the interaction of the charged fragment of the drugs with acetone, a system that mimics a ketone fragment of HERG/I(Kr) channel, supports preference of the conformation with the shielded charged center for potent HERG/I(Kr) blockers.	Acetone	98-105	potassium voltage-gated channel subfamily H member 2	Homo sapiens	149-153
15326914-7	2003	Conformational analysis and modeling of the interaction of the charged fragment of the drugs with acetone, a system that mimics a ketone fragment of HERG/I(Kr) channel, supports preference of the conformation with the shielded charged center for potent HERG/I(Kr) blockers.	Acetone	98-105	potassium voltage-gated channel subfamily H member 2	Homo sapiens	253-257
15326914-7	2003	Conformational analysis and modeling of the interaction of the charged fragment of the drugs with acetone, a system that mimics a ketone fragment of HERG/I(Kr) channel, supports preference of the conformation with the shielded charged center for potent HERG/I(Kr) blockers.	Ketones	130-136	potassium voltage-gated channel subfamily H member 2	Homo sapiens	149-153
15326914-7	2003	Conformational analysis and modeling of the interaction of the charged fragment of the drugs with acetone, a system that mimics a ketone fragment of HERG/I(Kr) channel, supports preference of the conformation with the shielded charged center for potent HERG/I(Kr) blockers.	Ketones	130-136	potassium voltage-gated channel subfamily H member 2	Homo sapiens	253-257
15326914-9	2003	We suggest that the introduction of a hydroxy group at position 3 relative to a tertiary ammonium charged center, or the introduction of hydroxy, alkoxy or amino groups at position 2 relative to the nitrogen center of an aromatic system, should provide easy access of a water molecule to the proton, thereby facilitating deprotonation and thus leading to a moderate or weak HERG/I(Kr) blockade and a reduced risk of TdP.	Water	270-275	potassium voltage-gated channel subfamily H member 2	Homo sapiens	374-378
14527710-6	2003	methadone causes QTc prolongation in humans; (2) whether methadone and/or chlorobutanol block cardiac HERG potassium currents (IHERG) in vitro.	Methadone	57-66	potassium voltage-gated channel subfamily H member 2	Homo sapiens	102-106
14527710-6	2003	methadone causes QTc prolongation in humans; (2) whether methadone and/or chlorobutanol block cardiac HERG potassium currents (IHERG) in vitro.	Chlorobutanol	74-87	potassium voltage-gated channel subfamily H member 2	Homo sapiens	102-106
14527710-6	2003	methadone causes QTc prolongation in humans; (2) whether methadone and/or chlorobutanol block cardiac HERG potassium currents (IHERG) in vitro.	Potassium	107-116	potassium voltage-gated channel subfamily H member 2	Homo sapiens	102-106
12837749-0	2003	Thapsigargin selectively rescues the trafficking defective LQT2 channels G601S and F805C.	Thapsigargin	0-12	potassium voltage-gated channel subfamily H member 2	Homo sapiens	59-63
12837749-12	2003	This study 1) supports the hypothesis that the LQT2 trafficking defective phenotype can be reversed without blocking the channel; 2) demonstrates pharmacological rescue of a C terminus LQT2 mutation; and 3) shows that thapsigargin can correct trafficking defective phenotypes in more than one channel type and disease (i.e. LQT2 and cystic fibrosis).	Thapsigargin	218-230	potassium voltage-gated channel subfamily H member 2	Homo sapiens	47-51
12837749-12	2003	This study 1) supports the hypothesis that the LQT2 trafficking defective phenotype can be reversed without blocking the channel; 2) demonstrates pharmacological rescue of a C terminus LQT2 mutation; and 3) shows that thapsigargin can correct trafficking defective phenotypes in more than one channel type and disease (i.e. LQT2 and cystic fibrosis).	Thapsigargin	218-230	potassium voltage-gated channel subfamily H member 2	Homo sapiens	185-189
12837749-12	2003	This study 1) supports the hypothesis that the LQT2 trafficking defective phenotype can be reversed without blocking the channel; 2) demonstrates pharmacological rescue of a C terminus LQT2 mutation; and 3) shows that thapsigargin can correct trafficking defective phenotypes in more than one channel type and disease (i.e. LQT2 and cystic fibrosis).	Thapsigargin	218-230	potassium voltage-gated channel subfamily H member 2	Homo sapiens	185-189
14512100-0	2003	Prulifloxacin: in vitro (HERG current) and in vivo (conscious dog) assessment of cardiac risk.	prulifloxacin	0-13	potassium voltage-gated channel subfamily H member 2	Homo sapiens	25-29
14512100-1	2003	Prulifloxacin, a new thiazeto-quinoline derivative with antibiotic properties, was evaluated for cardiac risk both in vitro on the ether-a-go-go-related gene (HERG) K+ channel, and in vivo in the conscious dog monitored by telemetry.	prulifloxacin	0-13	potassium voltage-gated channel subfamily H member 2	Homo sapiens	159-163
14512100-5	2003	In contrast, moxifloxacin blocked HERG current amplitude with an IC50 value of 74.7 microM.	Moxifloxacin	13-25	potassium voltage-gated channel subfamily H member 2	Homo sapiens	34-38
12960687-0	2003	Effects of Na+ channel blocker, pilsicainide, on HERG current expressed in HEK-293 cells.	pilsicainide	32-44	potassium voltage-gated channel subfamily H member 2	Homo sapiens	49-53
14499861-1	2003	OBJECTIVE: To determine whether the amino acid 897 threonine (T) to lysine (K) polymorphism of the KCNH2 (HERG) potassium channel influences channel performance or patient phenotype.	Threonine	51-60	potassium voltage-gated channel subfamily H member 2	Homo sapiens	99-104
14499861-1	2003	OBJECTIVE: To determine whether the amino acid 897 threonine (T) to lysine (K) polymorphism of the KCNH2 (HERG) potassium channel influences channel performance or patient phenotype.	Threonine	51-60	potassium voltage-gated channel subfamily H member 2	Homo sapiens	106-110
14499861-1	2003	OBJECTIVE: To determine whether the amino acid 897 threonine (T) to lysine (K) polymorphism of the KCNH2 (HERG) potassium channel influences channel performance or patient phenotype.	Lysine	68-74	potassium voltage-gated channel subfamily H member 2	Homo sapiens	99-104
14499861-1	2003	OBJECTIVE: To determine whether the amino acid 897 threonine (T) to lysine (K) polymorphism of the KCNH2 (HERG) potassium channel influences channel performance or patient phenotype.	Lysine	68-74	potassium voltage-gated channel subfamily H member 2	Homo sapiens	106-110
12960687-2	2003	We studied effects of pilsicainide on the K+ channel current of the human ether-a-go-go-related gene (HERG) in heterologous expression system.	pilsicainide	22-34	potassium voltage-gated channel subfamily H member 2	Homo sapiens	102-106
12960687-4	2003	RESULTS: Pilsicainide suppressed peak currents of HERG channel during depolarizing pulses and tail currents upon repolarization.	pilsicainide	9-21	potassium voltage-gated channel subfamily H member 2	Homo sapiens	50-54
12960687-5	2003	Pilsicainide blocked HERG current with IC50 = 20.4 microM and Hill coefficient = 0.98.	pilsicainide	0-12	potassium voltage-gated channel subfamily H member 2	Homo sapiens	21-25
12960687-11	2003	CONCLUSIONS: Pilsicainide blocks HERG current with a preferential affinity, at least, to the open state of the channels with a fast access to binding sites.	pilsicainide	13-25	potassium voltage-gated channel subfamily H member 2	Homo sapiens	33-37
12860380-0	2003	Preferential closed channel blockade of HERG potassium currents by chemically synthesised BeKm-1 scorpion toxin.	Potassium	45-54	potassium voltage-gated channel subfamily H member 2	Homo sapiens	40-44
12860380-5	2003	Blockade by BeKm-1 and recombinant ergtoxin, another scorpion toxin known to block HERG, differed in their recovery from HERG current inactivation elicited by strong depolarisation and in their ability to block HERG when the channels were already activated.	(6aR,9R)-N-[(1S,2S,4R,7S)-7-benzyl-2-hydroxy-5,8-dioxo-4-propan-2-yl-3-oxa-6,9-diazatricyclo[7.3.0.02,6]dodecan-4-yl]-7-methyl-6,6a,8,9-tetrahydro-4H-indolo[4,3-fg]quinoline-9-carboxamide;(6aR,9R)-N-[(1S,2S,4R,7S)-2-hydroxy-5,8-dioxo-4,7-di(propan-2-yl)-3-oxa-6,9-diazatricyclo[7.3.0.02,6]dodecan-4-yl]-7-methyl-6,6a,8,9-tetrahydro-4H-indolo[4,3-fg]quinoline-9-carboxamide;(6aR,9R)-N-[(1S,2S,4R,7S)-2-hydroxy-7-(2-methylpropyl)-5,8-dioxo-4-propan-2-yl-3-oxa-6,9-diazatricyclo[7.3.0.02,6]dodecan-4-yl]-7-methyl-6,6a,8,9-tetrahydro-4H-indolo[4,3-fg]quinoline-9-carboxamide	35-43	potassium voltage-gated channel subfamily H member 2	Homo sapiens	83-87
12860380-5	2003	Blockade by BeKm-1 and recombinant ergtoxin, another scorpion toxin known to block HERG, differed in their recovery from HERG current inactivation elicited by strong depolarisation and in their ability to block HERG when the channels were already activated.	(6aR,9R)-N-[(1S,2S,4R,7S)-7-benzyl-2-hydroxy-5,8-dioxo-4-propan-2-yl-3-oxa-6,9-diazatricyclo[7.3.0.02,6]dodecan-4-yl]-7-methyl-6,6a,8,9-tetrahydro-4H-indolo[4,3-fg]quinoline-9-carboxamide;(6aR,9R)-N-[(1S,2S,4R,7S)-2-hydroxy-5,8-dioxo-4,7-di(propan-2-yl)-3-oxa-6,9-diazatricyclo[7.3.0.02,6]dodecan-4-yl]-7-methyl-6,6a,8,9-tetrahydro-4H-indolo[4,3-fg]quinoline-9-carboxamide;(6aR,9R)-N-[(1S,2S,4R,7S)-2-hydroxy-7-(2-methylpropyl)-5,8-dioxo-4-propan-2-yl-3-oxa-6,9-diazatricyclo[7.3.0.02,6]dodecan-4-yl]-7-methyl-6,6a,8,9-tetrahydro-4H-indolo[4,3-fg]quinoline-9-carboxamide	35-43	potassium voltage-gated channel subfamily H member 2	Homo sapiens	121-125
12860380-5	2003	Blockade by BeKm-1 and recombinant ergtoxin, another scorpion toxin known to block HERG, differed in their recovery from HERG current inactivation elicited by strong depolarisation and in their ability to block HERG when the channels were already activated.	(6aR,9R)-N-[(1S,2S,4R,7S)-7-benzyl-2-hydroxy-5,8-dioxo-4-propan-2-yl-3-oxa-6,9-diazatricyclo[7.3.0.02,6]dodecan-4-yl]-7-methyl-6,6a,8,9-tetrahydro-4H-indolo[4,3-fg]quinoline-9-carboxamide;(6aR,9R)-N-[(1S,2S,4R,7S)-2-hydroxy-5,8-dioxo-4,7-di(propan-2-yl)-3-oxa-6,9-diazatricyclo[7.3.0.02,6]dodecan-4-yl]-7-methyl-6,6a,8,9-tetrahydro-4H-indolo[4,3-fg]quinoline-9-carboxamide;(6aR,9R)-N-[(1S,2S,4R,7S)-2-hydroxy-7-(2-methylpropyl)-5,8-dioxo-4-propan-2-yl-3-oxa-6,9-diazatricyclo[7.3.0.02,6]dodecan-4-yl]-7-methyl-6,6a,8,9-tetrahydro-4H-indolo[4,3-fg]quinoline-9-carboxamide	35-43	potassium voltage-gated channel subfamily H member 2	Homo sapiens	121-125
12839860-0	2003	Drug binding to HERG channels: evidence for a "non-aromatic" binding site for fluvoxamine.	Fluvoxamine	78-89	potassium voltage-gated channel subfamily H member 2	Homo sapiens	16-20
12839862-0	2003	Blockade of HERG potassium currents by fluvoxamine: incomplete attenuation by S6 mutations at F656 or Y652.	Potassium	17-26	potassium voltage-gated channel subfamily H member 2	Homo sapiens	12-16
12839862-0	2003	Blockade of HERG potassium currents by fluvoxamine: incomplete attenuation by S6 mutations at F656 or Y652.	Fluvoxamine	39-50	potassium voltage-gated channel subfamily H member 2	Homo sapiens	12-16
12839862-3	2003	The objectives of this study were (i) to identify and characterise any inhibitory action on HERG of the selective-serotonin re-uptake inhibitor fluvoxamine, (ii) to then determine whether fluvoxamine shared the consensus molecular determinants of HERG blockade of those drugs so far tested.	Fluvoxamine	144-155	potassium voltage-gated channel subfamily H member 2	Homo sapiens	92-96
12839862-6	2003	I(HERG) tails, following repolarisation from +20 to -40 mV, were blocked by fluvoxamine with an IC(50) of 3.8 micro M. 3.	Fluvoxamine	76-87	potassium voltage-gated channel subfamily H member 2	Homo sapiens	2-6
12839862-7	2003	Blockade of wild-type HERG was of extremely rapid onset (within 10 ms) and showed voltage dependence, with fluvoxamine also inducing a leftward shift in voltage-dependent activation of I(HERG).	Fluvoxamine	107-118	potassium voltage-gated channel subfamily H member 2	Homo sapiens	22-26
12839862-7	2003	Blockade of wild-type HERG was of extremely rapid onset (within 10 ms) and showed voltage dependence, with fluvoxamine also inducing a leftward shift in voltage-dependent activation of I(HERG).	Fluvoxamine	107-118	potassium voltage-gated channel subfamily H member 2	Homo sapiens	187-191
12839862-11	2003	The S6 mutations, Y652A and F656A, and the pore helix mutant S631A only partially attenuated blockade by fluvoxamine at concentrations causing profound blockade of wild-type HERG.	Fluvoxamine	105-116	potassium voltage-gated channel subfamily H member 2	Homo sapiens	174-178
12804575-0	2003	Characterisation of recombinant HERG K+ channel blockade by the Class Ia antiarrhythmic drug procainamide.	Procainamide	93-105	potassium voltage-gated channel subfamily H member 2	Homo sapiens	32-36
14510655-8	2003	CONCLUSIONS: Phenylephrine-induced bradycardia decreased TDR in symptomatic LQT1 but increased TDR in symptomatic LQT2.	Phenylephrine	13-26	potassium voltage-gated channel subfamily H member 2	Homo sapiens	114-118
12829172-6	2003	RESULTS: Application of the phorbol ester PMA, an unspecific protein kinase activator, shifted the voltage dependence of HERG activation towards more positive potentials.	Phorbol Esters	28-41	potassium voltage-gated channel subfamily H member 2	Homo sapiens	121-125
12827215-0	2003	Inhibition of cloned HERG potassium channels by the antiestrogen tamoxifen.	Tamoxifen	65-74	potassium voltage-gated channel subfamily H member 2	Homo sapiens	21-25
12827215-5	2003	Tamoxifen blocked HERG potassium channels with an IC(50) value of 45.3 microM.	Tamoxifen	0-9	potassium voltage-gated channel subfamily H member 2	Homo sapiens	18-22
12827215-9	2003	This study demonstrates that HERG potassium channels are blocked by the antiestrogenic drug tamoxifen.	Tamoxifen	92-101	potassium voltage-gated channel subfamily H member 2	Homo sapiens	29-33
12775586-5	2003	The specific Hsp90 inhibitor geldanamycin prevents maturation and increases proteasomal degradation of hERG WT, while reducing hERG currents in heterologous expression systems.	geldanamycin	29-41	potassium voltage-gated channel subfamily H member 2	Homo sapiens	103-107
12759137-5	2003	We favour the latter hypothesis, since some fluoroquinolones have recently been shown to block the pore-forming subunit of the cardiac rapid delayed rectifier K(+) current I(Kr) (which is encoded by HERG (human ether-a-go-go-related gene)).	Fluoroquinolones	44-60	potassium voltage-gated channel subfamily H member 2	Homo sapiens	199-203
12740430-0	2003	Inhibition of HERG K+ current and prolongation of the guinea-pig ventricular action potential by 4-aminopyridine.	4-Aminopyridine	97-112	potassium voltage-gated channel subfamily H member 2	Homo sapiens	14-18
12740430-2	2003	We report here inhibition by 4-AP of HERG (the human ether-a-go-go-related gene) K+ channels expressed in a mammalian cell line, at concentrations relevant to those used to study ITO,1.	4-Aminopyridine	29-33	potassium voltage-gated channel subfamily H member 2	Homo sapiens	37-41
12736144-9	2003	Low concentrations of the KCNH2 blockers E-4031 (10(-8) M) and MK-499 (3 x 10(-8) M) increased phasic contractile amplitude and the number of spikes per slow wave.	E 4031	41-47	potassium voltage-gated channel subfamily H member 2	Homo sapiens	26-31
12736144-9	2003	Low concentrations of the KCNH2 blockers E-4031 (10(-8) M) and MK-499 (3 x 10(-8) M) increased phasic contractile amplitude and the number of spikes per slow wave.	L 706000	63-69	potassium voltage-gated channel subfamily H member 2	Homo sapiens	26-31
12788816-0	2003	The antipsychotic drug chlorpromazine inhibits HERG potassium channels.	Chlorpromazine	23-37	potassium voltage-gated channel subfamily H member 2	Homo sapiens	47-51
12788816-5	2003	Blockade of human ether-a-go-go-related gene (HERG) potassium channels, which plays a central role in arrhythmogenesis, has previously been reported to occur with chlorpromazine, but information on the mechanism of block is currently not available.	Chlorpromazine	163-177	potassium voltage-gated channel subfamily H member 2	Homo sapiens	46-50
12788816-8	2003	(3) Chlorpromazine blocked HERG potassium channels with an IC(50) value of 21.6 micro M and a Hill coefficient of 1.11.	Chlorpromazine	4-18	potassium voltage-gated channel subfamily H member 2	Homo sapiens	27-31
12788816-10	2003	(5) Inhibition of HERG channels by chlorpromazine displayed reverse frequency dependence, that is, the amount of block was lower at higher stimulation rates.	Chlorpromazine	35-49	potassium voltage-gated channel subfamily H member 2	Homo sapiens	18-22
12759137-6	2003	Thus, as demonstrated for cardiac HERG channels in previous studies and for pancreatic beta-cell K(ATP) channels in the present study, fluoroquinolones differ markedly in their potencies to inhibit K(+) channel activity.	Fluoroquinolones	135-151	potassium voltage-gated channel subfamily H member 2	Homo sapiens	34-38
12948624-0	2003	Phenytoin and phenobarbital inhibit human HERG potassium channels.	Phenytoin	0-9	potassium voltage-gated channel subfamily H member 2	Homo sapiens	42-46
12948624-0	2003	Phenytoin and phenobarbital inhibit human HERG potassium channels.	Phenobarbital	14-27	potassium voltage-gated channel subfamily H member 2	Homo sapiens	42-46
12948624-4	2003	Tail currents, which are purely related to HERG, were blocked with an IC50 (the concentration when 50% inhibition was obtained compared to control values) of 240 microM for PHT and 3 mM for PB.	Phenobarbital	190-192	potassium voltage-gated channel subfamily H member 2	Homo sapiens	43-47
12626667-0	2003	Modulation of human ether-a-go-go-related K+ (HERG) channel inactivation by Cs+ and K+.	Cesium	76-79	potassium voltage-gated channel subfamily H member 2	Homo sapiens	46-50
12695533-2	2003	Here we investigate the molecular mechanisms of voltage-dependent block of human ether-a-go-go-related gene (HERG) delayed rectifier K(+) channels expressed in Xenopus laevis oocytes by quinidine, an antiarrhythmic drug, and vesnarinone, a cardiotonic drug.	Quinidine	186-195	potassium voltage-gated channel subfamily H member 2	Homo sapiens	109-113
12695533-2	2003	Here we investigate the molecular mechanisms of voltage-dependent block of human ether-a-go-go-related gene (HERG) delayed rectifier K(+) channels expressed in Xenopus laevis oocytes by quinidine, an antiarrhythmic drug, and vesnarinone, a cardiotonic drug.	vesnarinone	225-236	potassium voltage-gated channel subfamily H member 2	Homo sapiens	109-113
12695533-4	2003	Block of HERG by quinidine (and its isomer quinine) was enhanced by progressive membrane depolarization and accompanied by a negative shift in the voltage dependence of channel activation.	Quinidine	17-26	potassium voltage-gated channel subfamily H member 2	Homo sapiens	9-13
12695533-4	2003	Block of HERG by quinidine (and its isomer quinine) was enhanced by progressive membrane depolarization and accompanied by a negative shift in the voltage dependence of channel activation.	Quinine	43-50	potassium voltage-gated channel subfamily H member 2	Homo sapiens	9-13
12695533-5	2003	As reported previously for other HERG blockers (e.g., MK-499, cisapride, terfenadine, chloroquine), the potency of quinidine was reduced >100-fold by the mutation of key aromatic residues (Y652, F656) located in the S6 domain.	Quinidine	115-124	potassium voltage-gated channel subfamily H member 2	Homo sapiens	33-37
12695533-6	2003	Mutations of Y652 eliminated (Y652F) or reversed (Y652A) the voltage dependence of HERG channel block by quinidine and quinine.	Quinidine	105-114	potassium voltage-gated channel subfamily H member 2	Homo sapiens	83-87
12695533-6	2003	Mutations of Y652 eliminated (Y652F) or reversed (Y652A) the voltage dependence of HERG channel block by quinidine and quinine.	Quinine	119-126	potassium voltage-gated channel subfamily H member 2	Homo sapiens	83-87
12695533-8	2003	However, similar changes in the voltage-dependent profile for block of Y652F or Y652A HERG channels were observed with vesnarinone, a cardiotonic drug that is uncharged at physiological pH.	vesnarinone	119-130	potassium voltage-gated channel subfamily H member 2	Homo sapiens	86-90
12775973-4	2003	In human ether-a-go-go (HERG)-transfected Chinese hamster ovary cells (n = 16), risperidone caused concentration-dependent block of the rapid component (I(Kr)) of the delayed rectifier potassium current with an IC(50) for tail block of 261 nM.	Risperidone	80-91	potassium voltage-gated channel subfamily H member 2	Homo sapiens	24-28
12771193-0	2003	Saxitoxin is a gating modifier of HERG K+ channels.	Saxitoxin	0-9	potassium voltage-gated channel subfamily H member 2	Homo sapiens	34-38
12771193-5	2003	STX decreased hERG K+ currents by stabilizing closed channel states visualized as shifts in the voltage dependence of channel opening to more depolarized membrane potentials.	Saxitoxin	0-3	potassium voltage-gated channel subfamily H member 2	Homo sapiens	14-18
12771193-10	2003	The results are consistent with a simple model in which STX binds to the hERG K+ channel at multiple sites and alters the energetics of channel gating by shifting both the voltage-inactivation and voltage-activation processes.	Saxitoxin	56-59	potassium voltage-gated channel subfamily H member 2	Homo sapiens	73-77
12771194-4	2003	Data from the other five functional mutants suggest that D411 can stabilize the HERG channel in the closed state, while D460 and D509 have the opposite effect.	d411	57-61	potassium voltage-gated channel subfamily H member 2	Homo sapiens	80-84
12771194-6	2003	On the other hand, all five aspartates work in a concerted fashion in contributing to the slow deactivation process of the HERG channel.	Aspartic Acid	28-38	potassium voltage-gated channel subfamily H member 2	Homo sapiens	123-127
12771194-7	2003	Accessibility tests of the introduced thiol groups to extracellular MTS reagents indicate that water-filled crevices penetrate deep into the HERG protein core, reaching the cytoplasmic halves of S1 and S2.	Sulfhydryl Compounds	38-43	potassium voltage-gated channel subfamily H member 2	Homo sapiens	141-145
12771194-7	2003	Accessibility tests of the introduced thiol groups to extracellular MTS reagents indicate that water-filled crevices penetrate deep into the HERG protein core, reaching the cytoplasmic halves of S1 and S2.	Water	95-100	potassium voltage-gated channel subfamily H member 2	Homo sapiens	141-145
12690509-2	2003	In this study, we have retrospectively screened specific founder mutations in KCNQ1 (KVLQT1) and KCNH2 (HERG) genes in 165 consecutive bodies found in water in Finland.	Water	151-156	potassium voltage-gated channel subfamily H member 2	Homo sapiens	97-102
12690509-2	2003	In this study, we have retrospectively screened specific founder mutations in KCNQ1 (KVLQT1) and KCNH2 (HERG) genes in 165 consecutive bodies found in water in Finland.	Water	151-156	potassium voltage-gated channel subfamily H member 2	Homo sapiens	104-108
12626667-1	2003	Unlike many other native and cloned K+ channels, human ether-a-go-go-related K+ (HERG) channels show significant Cs+ permeability with a PCs/PK (the permeability of Cs+ relative to that of K+) of 0.36 +/- 0.03 (n = 10).	Cesium	113-116	potassium voltage-gated channel subfamily H member 2	Homo sapiens	81-85
12626667-1	2003	Unlike many other native and cloned K+ channels, human ether-a-go-go-related K+ (HERG) channels show significant Cs+ permeability with a PCs/PK (the permeability of Cs+ relative to that of K+) of 0.36 +/- 0.03 (n = 10).	Cesium	165-168	potassium voltage-gated channel subfamily H member 2	Homo sapiens	81-85
12626667-2	2003	Here, we find that raising the concentration of external Cs+ (Cs+o) dramatically slows HERG channel inactivation without affecting activation.	Cesium	57-60	potassium voltage-gated channel subfamily H member 2	Homo sapiens	87-91
12626667-8	2003	The strong effects of Cs+ on inactivation but not on activation highlight the importance of ion and channel interactions during the onset of inactivation in the HERG channel.	Cesium	22-25	potassium voltage-gated channel subfamily H member 2	Homo sapiens	161-165
12650941-0	2003	Solution structure of CnErg1 (Ergtoxin), a HERG specific scorpion toxin.	(6aR,9R)-N-[(1S,2S,4R,7S)-7-benzyl-2-hydroxy-5,8-dioxo-4-propan-2-yl-3-oxa-6,9-diazatricyclo[7.3.0.02,6]dodecan-4-yl]-7-methyl-6,6a,8,9-tetrahydro-4H-indolo[4,3-fg]quinoline-9-carboxamide;(6aR,9R)-N-[(1S,2S,4R,7S)-2-hydroxy-5,8-dioxo-4,7-di(propan-2-yl)-3-oxa-6,9-diazatricyclo[7.3.0.02,6]dodecan-4-yl]-7-methyl-6,6a,8,9-tetrahydro-4H-indolo[4,3-fg]quinoline-9-carboxamide;(6aR,9R)-N-[(1S,2S,4R,7S)-2-hydroxy-7-(2-methylpropyl)-5,8-dioxo-4-propan-2-yl-3-oxa-6,9-diazatricyclo[7.3.0.02,6]dodecan-4-yl]-7-methyl-6,6a,8,9-tetrahydro-4H-indolo[4,3-fg]quinoline-9-carboxamide	30-38	potassium voltage-gated channel subfamily H member 2	Homo sapiens	43-47
12650941-1	2003	The three-dimensional structure of chemically synthesized CnErg1 (Ergtoxin), which specifically blocks HERG (human ether-a-go-go-related gene) K+ channels, was determined by nuclear magnetic resonance spectroscopy.	(6aR,9R)-N-[(1S,2S,4R,7S)-7-benzyl-2-hydroxy-5,8-dioxo-4-propan-2-yl-3-oxa-6,9-diazatricyclo[7.3.0.02,6]dodecan-4-yl]-7-methyl-6,6a,8,9-tetrahydro-4H-indolo[4,3-fg]quinoline-9-carboxamide;(6aR,9R)-N-[(1S,2S,4R,7S)-2-hydroxy-5,8-dioxo-4,7-di(propan-2-yl)-3-oxa-6,9-diazatricyclo[7.3.0.02,6]dodecan-4-yl]-7-methyl-6,6a,8,9-tetrahydro-4H-indolo[4,3-fg]quinoline-9-carboxamide;(6aR,9R)-N-[(1S,2S,4R,7S)-2-hydroxy-7-(2-methylpropyl)-5,8-dioxo-4-propan-2-yl-3-oxa-6,9-diazatricyclo[7.3.0.02,6]dodecan-4-yl]-7-methyl-6,6a,8,9-tetrahydro-4H-indolo[4,3-fg]quinoline-9-carboxamide	66-74	potassium voltage-gated channel subfamily H member 2	Homo sapiens	103-107
12618228-0	2003	Effects of propafenone and its main metabolite, 5-hydroxypropafenone, on HERG channels.	Propafenone	11-22	potassium voltage-gated channel subfamily H member 2	Homo sapiens	73-77
12531891-4	2003	We found that both hyperglycemia (extracellular glucose concentration [Glu](o) = 10 or 20 mm) and hypoglycemia ([Glu](o) = 2.5, 1, or 0 mm) impaired HERG function by reducing HERG current (I(HERG)) density, as compared with normoglycemia ([Glu](o) = 5 mm).	Glutamic Acid	71-74	potassium voltage-gated channel subfamily H member 2	Homo sapiens	149-153
12531891-4	2003	We found that both hyperglycemia (extracellular glucose concentration [Glu](o) = 10 or 20 mm) and hypoglycemia ([Glu](o) = 2.5, 1, or 0 mm) impaired HERG function by reducing HERG current (I(HERG)) density, as compared with normoglycemia ([Glu](o) = 5 mm).	Glutamic Acid	113-116	potassium voltage-gated channel subfamily H member 2	Homo sapiens	149-153
12531891-4	2003	We found that both hyperglycemia (extracellular glucose concentration [Glu](o) = 10 or 20 mm) and hypoglycemia ([Glu](o) = 2.5, 1, or 0 mm) impaired HERG function by reducing HERG current (I(HERG)) density, as compared with normoglycemia ([Glu](o) = 5 mm).	Glutamic Acid	113-116	potassium voltage-gated channel subfamily H member 2	Homo sapiens	149-153
12531891-9	2003	We conclude that ATP, derived from either glycolysis or oxidative phosphorylation, is critical for normal HERG function; depression of I(HERG) in hypoglycemia results from underproduction of ATP and in hyperglycemia from overproduction of reactive oxygen species.	Adenosine Triphosphate	17-20	potassium voltage-gated channel subfamily H member 2	Homo sapiens	106-110
12531891-9	2003	We conclude that ATP, derived from either glycolysis or oxidative phosphorylation, is critical for normal HERG function; depression of I(HERG) in hypoglycemia results from underproduction of ATP and in hyperglycemia from overproduction of reactive oxygen species.	Adenosine Triphosphate	17-20	potassium voltage-gated channel subfamily H member 2	Homo sapiens	137-141
12531891-9	2003	We conclude that ATP, derived from either glycolysis or oxidative phosphorylation, is critical for normal HERG function; depression of I(HERG) in hypoglycemia results from underproduction of ATP and in hyperglycemia from overproduction of reactive oxygen species.	Adenosine Triphosphate	191-194	potassium voltage-gated channel subfamily H member 2	Homo sapiens	137-141
12531891-9	2003	We conclude that ATP, derived from either glycolysis or oxidative phosphorylation, is critical for normal HERG function; depression of I(HERG) in hypoglycemia results from underproduction of ATP and in hyperglycemia from overproduction of reactive oxygen species.	Reactive Oxygen Species	239-262	potassium voltage-gated channel subfamily H member 2	Homo sapiens	137-141
12531891-3	2003	Here we studied modulation of human ether-a-go-go-related gene (HERG) K(+) channel, the major molecular component of delayed rectifier K(+) current responsible for cardiac repolarization, by glucose in HEK293 cells using whole-cell patch clamp techniques.	Glucose	191-198	potassium voltage-gated channel subfamily H member 2	Homo sapiens	64-68
12531891-4	2003	We found that both hyperglycemia (extracellular glucose concentration [Glu](o) = 10 or 20 mm) and hypoglycemia ([Glu](o) = 2.5, 1, or 0 mm) impaired HERG function by reducing HERG current (I(HERG)) density, as compared with normoglycemia ([Glu](o) = 5 mm).	Glucose	48-55	potassium voltage-gated channel subfamily H member 2	Homo sapiens	149-153
12593854-4	2003	The bulk of repolarization, including the after-hyperpolarization, was sustained by the human eag related (HERG) potassium current (I(HERG)) that also governs V(REST) in 21S cells.	Potassium	113-122	potassium voltage-gated channel subfamily H member 2	Homo sapiens	107-111
12593854-4	2003	The bulk of repolarization, including the after-hyperpolarization, was sustained by the human eag related (HERG) potassium current (I(HERG)) that also governs V(REST) in 21S cells.	Potassium	113-122	potassium voltage-gated channel subfamily H member 2	Homo sapiens	134-138
12618228-0	2003	Effects of propafenone and its main metabolite, 5-hydroxypropafenone, on HERG channels.	5-hydroxypropafenone	48-68	potassium voltage-gated channel subfamily H member 2	Homo sapiens	73-77
12618228-3	2003	In the present study we have analysed the effects of propafenone and 5-hydroxypropafenone on HERG current.	Propafenone	53-64	potassium voltage-gated channel subfamily H member 2	Homo sapiens	93-97
12618228-3	2003	In the present study we have analysed the effects of propafenone and 5-hydroxypropafenone on HERG current.	5-hydroxypropafenone	69-89	potassium voltage-gated channel subfamily H member 2	Homo sapiens	93-97
12618228-9	2003	Propafenone, but not 5-hydroxypropafenone, inhibited to a higher extent HERG current at the end of 5-s depolarizing pulses to 0 mV than after promoting the transition of HERG channels from the inactivated to the opened state.	Propafenone	0-11	potassium voltage-gated channel subfamily H member 2	Homo sapiens	72-76
12618228-9	2003	Propafenone, but not 5-hydroxypropafenone, inhibited to a higher extent HERG current at the end of 5-s depolarizing pulses to 0 mV than after promoting the transition of HERG channels from the inactivated to the opened state.	Propafenone	0-11	potassium voltage-gated channel subfamily H member 2	Homo sapiens	170-174
12618228-10	2003	CONCLUSIONS: These results indicate that propafenone and its main active metabolite, 5-hydroxypropafenone, block HERG channels to a similar extent by binding predominantly to the open state of the channel.	Propafenone	41-52	potassium voltage-gated channel subfamily H member 2	Homo sapiens	113-117
12618228-10	2003	CONCLUSIONS: These results indicate that propafenone and its main active metabolite, 5-hydroxypropafenone, block HERG channels to a similar extent by binding predominantly to the open state of the channel.	5-hydroxypropafenone	85-105	potassium voltage-gated channel subfamily H member 2	Homo sapiens	113-117
12689355-0	2003	Interaction between tetraethylammonium and permeant cations at the inactivation gate of the HERG potassium channel.	Tetraethylammonium	20-38	potassium voltage-gated channel subfamily H member 2	Homo sapiens	92-96
12591761-2	2003	In this study, the effects of SP and its metabolite, canrenoic acid (CA), on human ether-a-go-go-related gene (HERG) currents were analyzed.	Spironolactone	30-32	potassium voltage-gated channel subfamily H member 2	Homo sapiens	111-115
12591761-2	2003	In this study, the effects of SP and its metabolite, canrenoic acid (CA), on human ether-a-go-go-related gene (HERG) currents were analyzed.	Canrenoic Acid	53-67	potassium voltage-gated channel subfamily H member 2	Homo sapiens	111-115
12591761-4	2003	SP decreased HERG currents in a concentration-dependent manner (IC50=23.0+/-1.5 micromol/L) and shifted the midpoint of the activation curve to more negative potentials (Vh=-13.1+/-3.4 versus -18.9+/-3.6 mV, P<0.05) without modifying the activation and deactivation kinetics.	Spironolactone	0-2	potassium voltage-gated channel subfamily H member 2	Homo sapiens	13-17
12591761-11	2003	CONCLUSIONS: At concentrations reached after administration of therapeutic doses of SP, CA blocked the HERG channels by binding to both the closed and open states of the channel.	Spironolactone	84-86	potassium voltage-gated channel subfamily H member 2	Homo sapiens	103-107
12689355-1	2003	The fast inactivation of the human ether-a-go-go related gene product (HERG) channel is a form of C-type inactivation and is decelerated by external tetraethylammonium (TEA) and potassium.	Tetraethylammonium	149-167	potassium voltage-gated channel subfamily H member 2	Homo sapiens	71-75
12689355-1	2003	The fast inactivation of the human ether-a-go-go related gene product (HERG) channel is a form of C-type inactivation and is decelerated by external tetraethylammonium (TEA) and potassium.	Tetraethylammonium	169-172	potassium voltage-gated channel subfamily H member 2	Homo sapiens	71-75
12689355-1	2003	The fast inactivation of the human ether-a-go-go related gene product (HERG) channel is a form of C-type inactivation and is decelerated by external tetraethylammonium (TEA) and potassium.	Potassium	178-187	potassium voltage-gated channel subfamily H member 2	Homo sapiens	71-75
12634931-3	2003	The antiarrhythmic agent E-4031, a specific blocker of erg channels, served to isolate HERG currents as the drug-sensitive currents.	E 4031	25-31	potassium voltage-gated channel subfamily H member 2	Homo sapiens	87-91
12538844-2	2003	Irbesartan exhibited a low affinity for HERG and KvLQT1+minK channels (IC(50) = 193.0 +/- 49.8 and 314.6 +/- 85.4 microM, respectively).	Irbesartan	0-10	potassium voltage-gated channel subfamily H member 2	Homo sapiens	40-44
12538844-10	2003	Molecular modeling was used to define energy-minimized dockings of irbesartan to hKv1.5 and HERG channels.	Irbesartan	67-77	potassium voltage-gated channel subfamily H member 2	Homo sapiens	92-96
12427763-6	2003	Sequence alignment against HERG showed a substitution of alanine for valine in the S4 domain.	Alanine	57-64	potassium voltage-gated channel subfamily H member 2	Homo sapiens	27-31
12427763-6	2003	Sequence alignment against HERG showed a substitution of alanine for valine in the S4 domain.	Valine	69-75	potassium voltage-gated channel subfamily H member 2	Homo sapiens	27-31
12427763-10	2003	Site-directed mutagenesis of alanine to valine in the S4 region of erg1-sm converted many of the properties to that of the cardiac HERG, including shifts in the voltage dependence of activation and slowing of deactivation.	Alanine	29-36	potassium voltage-gated channel subfamily H member 2	Homo sapiens	67-71
12427763-10	2003	Site-directed mutagenesis of alanine to valine in the S4 region of erg1-sm converted many of the properties to that of the cardiac HERG, including shifts in the voltage dependence of activation and slowing of deactivation.	Alanine	29-36	potassium voltage-gated channel subfamily H member 2	Homo sapiens	131-135
12427763-10	2003	Site-directed mutagenesis of alanine to valine in the S4 region of erg1-sm converted many of the properties to that of the cardiac HERG, including shifts in the voltage dependence of activation and slowing of deactivation.	Valine	40-46	potassium voltage-gated channel subfamily H member 2	Homo sapiens	67-71
12427763-10	2003	Site-directed mutagenesis of alanine to valine in the S4 region of erg1-sm converted many of the properties to that of the cardiac HERG, including shifts in the voltage dependence of activation and slowing of deactivation.	Valine	40-46	potassium voltage-gated channel subfamily H member 2	Homo sapiens	131-135
12524137-0	2003	Ethanol differently affects stress protein and HERG K+ channel expression in SH-SY5Y cells.	Ethanol	0-7	potassium voltage-gated channel subfamily H member 2	Homo sapiens	47-51
12524137-4	2003	The GRP and human-ether-a-gogo-related gene (HERG) K(+)-channel expression were monitored in short- and long-term ethanol incubation experiments using the human neuroblastoma cell line SH-SY5Y.	Ethanol	114-121	potassium voltage-gated channel subfamily H member 2	Homo sapiens	45-49
12522086-0	2003	Inhibition of hEAG1 and hERG1 potassium channels by clofilium and its tertiary analogue LY97241.	clofilium	52-61	potassium voltage-gated channel subfamily H member 2	Homo sapiens	24-29
12522086-0	2003	Inhibition of hEAG1 and hERG1 potassium channels by clofilium and its tertiary analogue LY97241.	LY 97241	88-95	potassium voltage-gated channel subfamily H member 2	Homo sapiens	24-29
12522086-2	2003	2 In the whole-cell mode of mammalian cells, LY97241 was shown to be a potent inhibitor of both hEAG1 and hERG1 channels (IC(50) of 4.9 and 2.2 nM, respectively).	LY 97241	45-52	potassium voltage-gated channel subfamily H member 2	Homo sapiens	106-111
12361947-8	2002	Tyrosine phosphorylation of ERG-1 was decreased by transfection with SHP-1 wt and increased by SHP-1 Cys --> Ser.	Tyrosine	0-8	potassium voltage-gated channel subfamily H member 2	Homo sapiens	28-33
12527373-2	2003	Wortmannin (a phosphoinositide 3-kinase (PI3K) inhibitor) caused approximately 30% reduction of HERG current (I(HERG)) stably expressed in HEK293 cells.	Wortmannin	0-10	potassium voltage-gated channel subfamily H member 2	Homo sapiens	96-100
12527373-2	2003	Wortmannin (a phosphoinositide 3-kinase (PI3K) inhibitor) caused approximately 30% reduction of HERG current (I(HERG)) stably expressed in HEK293 cells.	Wortmannin	0-10	potassium voltage-gated channel subfamily H member 2	Homo sapiens	112-116
12528876-9	2003	CONCLUSIONS: Beat-to-beat nonalternating T-wave lability occurs in LQT1, LQT2, and LQT3 patients during catecholamine provocation and is associated with a history of prior cardiac events.	Catecholamines	104-117	potassium voltage-gated channel subfamily H member 2	Homo sapiens	73-77
12361947-8	2002	Tyrosine phosphorylation of ERG-1 was decreased by transfection with SHP-1 wt and increased by SHP-1 Cys --> Ser.	Cysteine	101-104	potassium voltage-gated channel subfamily H member 2	Homo sapiens	28-33
12361947-8	2002	Tyrosine phosphorylation of ERG-1 was decreased by transfection with SHP-1 wt and increased by SHP-1 Cys --> Ser.	Serine	112-115	potassium voltage-gated channel subfamily H member 2	Homo sapiens	28-33
12460639-2	2002	We examined the detailed electrophysiological effects of nifekalant on human-ether-a-go-go-related gene (HERG) channels expressed in Xenopus oocytes.	nifekalant	57-67	potassium voltage-gated channel subfamily H member 2	Homo sapiens	71-103
12460639-2	2002	We examined the detailed electrophysiological effects of nifekalant on human-ether-a-go-go-related gene (HERG) channels expressed in Xenopus oocytes.	nifekalant	57-67	potassium voltage-gated channel subfamily H member 2	Homo sapiens	105-109
12460639-3	2002	Nifekalant inhibited the HERG current in a concentration-dependent manner with an IC(50) value of 7.9 microM although the drug did not inhibit the minK current in Xenopus oocytes, suggesting selective inhibition of the rapid component of the delayed rectifier K(+) current (I(Kr)) in cardiomyocytes.	nifekalant	0-10	potassium voltage-gated channel subfamily H member 2	Homo sapiens	25-29
12460639-4	2002	Nifekalant showed a higher binding affinity for the open state than for the inactive state of HERG channels.	nifekalant	0-10	potassium voltage-gated channel subfamily H member 2	Homo sapiens	94-98
12460639-5	2002	Nifekalant inhibited HERG channels in a frequency-dependent manner.	nifekalant	0-10	potassium voltage-gated channel subfamily H member 2	Homo sapiens	21-25
12460639-7	2002	Nifekalant modified the voltage dependence and kinetics of HERG channel gating.	nifekalant	0-10	potassium voltage-gated channel subfamily H member 2	Homo sapiens	59-63
12460639-8	2002	Thus, nifekalant inhibits HERG channels in a voltage-dependent and frequency-dependent manner, and the inhibitory effect may underlie the clinical efficacy of the drug against ventricular tachyarrhythmias.	nifekalant	6-16	potassium voltage-gated channel subfamily H member 2	Homo sapiens	26-30
12411421-3	2002	The antihistamine terfenadine blocks HERG channels, and can cause QT prolongation and torsades de pointes, whereas its carboxylate fexofenadine lacks HERG blocking activity.	antihistamine terfenadine	4-29	potassium voltage-gated channel subfamily H member 2	Homo sapiens	37-41
12354768-0	2002	A novel mutation (T65P) in the PAS domain of the human potassium channel HERG results in the long QT syndrome by trafficking deficiency.	Aminosalicylic Acid	31-34	potassium voltage-gated channel subfamily H member 2	Homo sapiens	73-77
12354768-4	2002	We describe the identification and characterization of a novel missense mutation T65P in the PAS (Per-Arnt-Sim) domain of HERG, resulting in defective trafficking of the protein to the cell membrane.	Aminosalicylic Acid	93-96	potassium voltage-gated channel subfamily H member 2	Homo sapiens	122-126
12354768-8	2002	This study is the first to relate a PAS domain mutation in HERG to a trafficking deficiency at body temperature, apart from effects on channel deactivation.	Aminosalicylic Acid	36-39	potassium voltage-gated channel subfamily H member 2	Homo sapiens	59-63
12388652-2	2002	Our results show that LAAM, methadone, fentanyl, and buprenorphine were effective inhibitors of I(HERG), with IC(50) values in the 1 to 10 microM range.	Methadyl Acetate	22-26	potassium voltage-gated channel subfamily H member 2	Homo sapiens	98-102
12388652-2	2002	Our results show that LAAM, methadone, fentanyl, and buprenorphine were effective inhibitors of I(HERG), with IC(50) values in the 1 to 10 microM range.	Methadone	28-37	potassium voltage-gated channel subfamily H member 2	Homo sapiens	98-102
12388652-2	2002	Our results show that LAAM, methadone, fentanyl, and buprenorphine were effective inhibitors of I(HERG), with IC(50) values in the 1 to 10 microM range.	Fentanyl	39-47	potassium voltage-gated channel subfamily H member 2	Homo sapiens	98-102
12388652-2	2002	Our results show that LAAM, methadone, fentanyl, and buprenorphine were effective inhibitors of I(HERG), with IC(50) values in the 1 to 10 microM range.	Buprenorphine	53-66	potassium voltage-gated channel subfamily H member 2	Homo sapiens	98-102
12388652-4	2002	Compared with the reported maximal plasma concentration (C(max)) after administration of therapeutic doses of these drugs, the ratio of IC(50)/C(max) was highest for codeine and morphine (>455 and >400, respectively), thereby indicating that these drugs have the widest margin of safety (of the compounds tested) with respect to blockade of I(HERG).	Codeine	166-173	potassium voltage-gated channel subfamily H member 2	Homo sapiens	349-353
12388652-4	2002	Compared with the reported maximal plasma concentration (C(max)) after administration of therapeutic doses of these drugs, the ratio of IC(50)/C(max) was highest for codeine and morphine (>455 and >400, respectively), thereby indicating that these drugs have the widest margin of safety (of the compounds tested) with respect to blockade of I(HERG).	Morphine	178-186	potassium voltage-gated channel subfamily H member 2	Homo sapiens	349-353
12388652-6	2002	Further investigation showed that methadone block of I(HERG) was rapid, with steady-state inhibition achieved within 1 s when applied at its IC(50) concentration (10 microM) for I(HERG) block.	Methadone	34-43	potassium voltage-gated channel subfamily H member 2	Homo sapiens	55-59
12388652-6	2002	Further investigation showed that methadone block of I(HERG) was rapid, with steady-state inhibition achieved within 1 s when applied at its IC(50) concentration (10 microM) for I(HERG) block.	Methadone	34-43	potassium voltage-gated channel subfamily H member 2	Homo sapiens	180-184
12388652-9	2002	These results demonstrate that LAAM and methadone can block I(HERG) in transfected cells at clinically relevant concentrations, thereby providing a plausible mechanism for the adverse cardiac effects observed in some patients receiving LAAM or methadone.	Methadyl Acetate	31-35	potassium voltage-gated channel subfamily H member 2	Homo sapiens	62-66
12388652-9	2002	These results demonstrate that LAAM and methadone can block I(HERG) in transfected cells at clinically relevant concentrations, thereby providing a plausible mechanism for the adverse cardiac effects observed in some patients receiving LAAM or methadone.	Methadone	40-49	potassium voltage-gated channel subfamily H member 2	Homo sapiens	62-66
12388652-9	2002	These results demonstrate that LAAM and methadone can block I(HERG) in transfected cells at clinically relevant concentrations, thereby providing a plausible mechanism for the adverse cardiac effects observed in some patients receiving LAAM or methadone.	Methadyl Acetate	236-240	potassium voltage-gated channel subfamily H member 2	Homo sapiens	62-66
12388652-9	2002	These results demonstrate that LAAM and methadone can block I(HERG) in transfected cells at clinically relevant concentrations, thereby providing a plausible mechanism for the adverse cardiac effects observed in some patients receiving LAAM or methadone.	Methadone	244-253	potassium voltage-gated channel subfamily H member 2	Homo sapiens	62-66
12359267-0	2002	Fenamate-induced enhancement of heterologously expressed HERG currents in Xenopus oocytes.	Fenamates	0-8	potassium voltage-gated channel subfamily H member 2	Homo sapiens	57-61
12359267-3	2002	In this study, we examined the effects of the non-steroidal anti-inflammatory agents, flufenamic acid and niflumic acid, on heterologously expressed HERG channels in oocytes.	Flufenamic Acid	86-101	potassium voltage-gated channel subfamily H member 2	Homo sapiens	149-153
12359267-3	2002	In this study, we examined the effects of the non-steroidal anti-inflammatory agents, flufenamic acid and niflumic acid, on heterologously expressed HERG channels in oocytes.	Niflumic Acid	106-119	potassium voltage-gated channel subfamily H member 2	Homo sapiens	149-153
12359267-7	2002	Fenamates accelerated the activation rate of HERG channels and decelerated their deactivation.	Fenamates	0-9	potassium voltage-gated channel subfamily H member 2	Homo sapiens	45-49
12359267-11	2002	The effects of the fenamates were blocked by the HERG channel blocker, E-4031 and were also not observed in water-injected oocytes.	Fenamates	19-28	potassium voltage-gated channel subfamily H member 2	Homo sapiens	49-53
12359267-11	2002	The effects of the fenamates were blocked by the HERG channel blocker, E-4031 and were also not observed in water-injected oocytes.	E 4031	71-77	potassium voltage-gated channel subfamily H member 2	Homo sapiens	49-53
12359267-12	2002	Our data suggest that fenamates enhance HERG currents and affect the action potential duration in the heart.	Fenamates	22-31	potassium voltage-gated channel subfamily H member 2	Homo sapiens	40-44
12411421-5	2002	In the present study the ability of fexofenadine to block the K897T HERG channel variant was investigated.	fexofenadine	36-48	potassium voltage-gated channel subfamily H member 2	Homo sapiens	68-72
12431311-7	2002	In this review article, sympathetic stimulation with isoproterenol or epinephrine infusion is demonstrated to modulate differentially these repolarization indices in the ECG as well as the action potentials of the three cells between the LQT1, LQT2, and LQT3 syndromes both experimentally and clinically, explaining the differences in the sensitivity of genotypes of congenital LQTS to sympathetic stimulation.	Isoproterenol	53-66	potassium voltage-gated channel subfamily H member 2	Homo sapiens	244-248
12431311-7	2002	In this review article, sympathetic stimulation with isoproterenol or epinephrine infusion is demonstrated to modulate differentially these repolarization indices in the ECG as well as the action potentials of the three cells between the LQT1, LQT2, and LQT3 syndromes both experimentally and clinically, explaining the differences in the sensitivity of genotypes of congenital LQTS to sympathetic stimulation.	Epinephrine	70-81	potassium voltage-gated channel subfamily H member 2	Homo sapiens	244-248
12176106-7	2002	We found that sertindole, pimozide and thioridazine displayed little (<10-fold) or no selectivity for dopamine D(2) or 5-HT(2A) receptors relative to their HERG channel affinities.	Thioridazine	39-51	potassium voltage-gated channel subfamily H member 2	Homo sapiens	159-163
12176129-0	2002	The anti-malarial drug halofantrine and its metabolite N-desbutylhalofantrine block HERG potassium channels.	halofantrine	23-35	potassium voltage-gated channel subfamily H member 2	Homo sapiens	84-88
12176129-0	2002	The anti-malarial drug halofantrine and its metabolite N-desbutylhalofantrine block HERG potassium channels.	1,3-dichloro-6-trifluoromethyl-9-phenanthryl-3-(n-butyl)aminopropanol	55-77	potassium voltage-gated channel subfamily H member 2	Homo sapiens	84-88
12176129-3	2002	METHODS: We studied the effects of halofantrine (0.1-1000 nM) and its major metabolite N-desbutylhalofantrine (3-1000 nM) on wild type HERG K(+) channels stably expressed in HEK 293 cells, using the whole cell patch-clamp recording technique.	1,3-dichloro-6-trifluoromethyl-9-phenanthryl-3-(n-butyl)aminopropanol	87-109	potassium voltage-gated channel subfamily H member 2	Homo sapiens	135-139
12176129-4	2002	RESULTS: Halofantrine and N-desbutylhalofantrine blocked HERG K(+) channels in a concentration-dependent manner with a half-maximal inhibitory concentration of 21.6 nM (n=31 cells) and 71.7 nM (n=18 cells), respectively.	halofantrine	9-21	potassium voltage-gated channel subfamily H member 2	Homo sapiens	57-61
12176129-4	2002	RESULTS: Halofantrine and N-desbutylhalofantrine blocked HERG K(+) channels in a concentration-dependent manner with a half-maximal inhibitory concentration of 21.6 nM (n=31 cells) and 71.7 nM (n=18 cells), respectively.	1,3-dichloro-6-trifluoromethyl-9-phenanthryl-3-(n-butyl)aminopropanol	26-48	potassium voltage-gated channel subfamily H member 2	Homo sapiens	57-61
12176129-7	2002	Using a ventricular action potential voltage clamp protocol, halofantrine and N-desbutylhalofantrine block of HERG current was greatest during phases 2 and 3 of the action potential waveform.	1,3-dichloro-6-trifluoromethyl-9-phenanthryl-3-(n-butyl)aminopropanol	78-100	potassium voltage-gated channel subfamily H member 2	Homo sapiens	110-114
12176129-8	2002	CONCLUSION: We conclude that both halofantrine and N-desbutylhalofantrine cause high affinity block of HERG K(+) channels.	halofantrine	34-46	potassium voltage-gated channel subfamily H member 2	Homo sapiens	103-107
12176129-8	2002	CONCLUSION: We conclude that both halofantrine and N-desbutylhalofantrine cause high affinity block of HERG K(+) channels.	1,3-dichloro-6-trifluoromethyl-9-phenanthryl-3-(n-butyl)aminopropanol	51-73	potassium voltage-gated channel subfamily H member 2	Homo sapiens	103-107
12176106-9	2002	Of the other drugs tested (ziprasidone, quetiapine, risperidone and olanzapine), olanzapine displayed the greatest selectivity for dopamine D(2) and 5-HT(2A) receptor binding (100-1000-fold) compared to its HERG channel IC(50).	Olanzapine	81-91	potassium voltage-gated channel subfamily H member 2	Homo sapiens	207-211
12176106-9	2002	Of the other drugs tested (ziprasidone, quetiapine, risperidone and olanzapine), olanzapine displayed the greatest selectivity for dopamine D(2) and 5-HT(2A) receptor binding (100-1000-fold) compared to its HERG channel IC(50).	dopamine d	131-141	potassium voltage-gated channel subfamily H member 2	Homo sapiens	207-211
12357160-0	2002	Kinetic modulation of HERG potassium channels by the volatile anesthetic halothane.	Halothane	73-82	potassium voltage-gated channel subfamily H member 2	Homo sapiens	22-26
12357160-2	2002	General anesthetics, like halothane, can prolong Q-T interval, suggesting that they act on myocellular repolarization, possibly involving HERG channels.	Halothane	26-35	potassium voltage-gated channel subfamily H member 2	Homo sapiens	138-142
12357160-3	2002	Evidence for direct modulation of HERG channels by halothane is still lacking.	Halothane	51-60	potassium voltage-gated channel subfamily H member 2	Homo sapiens	34-38
12357160-4	2002	To gain insight on HERG channel modulation by halothane the authors recorded macroscopic currents expressed in Xenopus oocytes and conducted non-stationary noise analysis to evaluate single channel parameters modified by the anesthetic.	Halothane	46-55	potassium voltage-gated channel subfamily H member 2	Homo sapiens	19-23
12357160-12	2002	CONCLUSIONS: Halothane inhibits HERG currents expressed in oocytes in a concentration-dependent manner.	Halothane	13-22	potassium voltage-gated channel subfamily H member 2	Homo sapiens	32-36
12357160-14	2002	The authors" results demonstrate that halothane decreased HERG currents by modulating kinetic properties of HERG channels, decreasing their open probability.	Halothane	38-47	potassium voltage-gated channel subfamily H member 2	Homo sapiens	58-62
12357160-14	2002	The authors" results demonstrate that halothane decreased HERG currents by modulating kinetic properties of HERG channels, decreasing their open probability.	Halothane	38-47	potassium voltage-gated channel subfamily H member 2	Homo sapiens	108-112
12356854-0	2002	Extracellular sodium interacts with the HERG channel at an outer pore site.	Sodium	14-20	potassium voltage-gated channel subfamily H member 2	Homo sapiens	40-44
12208728-4	2002	Here, we show that HERG conductance markedly promotes H2O2-induced apoptosis of various tumor cells, whereas HERG expression facilitates the tumor cell proliferation caused by tumor necrosis factor (TNF) ligand (TNF-alpha).	Hydrogen Peroxide	54-58	potassium voltage-gated channel subfamily H member 2	Homo sapiens	19-23
12065733-0	2002	Blockade of human cardiac potassium channel human ether-a-go-go-related gene (HERG) by macrolide antibiotics.	macrolide antibiotics	87-108	potassium voltage-gated channel subfamily H member 2	Homo sapiens	78-82
12021266-4	2002	Streptavidin selection of biotin-labeled surface proteins showed good expression of wild-type and HERG(Delta159) at the cell surface and low expression of HERG(Delta147-LGL) and HERG(Delta147).	Biotin	26-32	potassium voltage-gated channel subfamily H member 2	Homo sapiens	98-102
12021266-4	2002	Streptavidin selection of biotin-labeled surface proteins showed good expression of wild-type and HERG(Delta159) at the cell surface and low expression of HERG(Delta147-LGL) and HERG(Delta147).	Biotin	26-32	potassium voltage-gated channel subfamily H member 2	Homo sapiens	168-172
12021266-4	2002	Streptavidin selection of biotin-labeled surface proteins showed good expression of wild-type and HERG(Delta159) at the cell surface and low expression of HERG(Delta147-LGL) and HERG(Delta147).	Biotin	26-32	potassium voltage-gated channel subfamily H member 2	Homo sapiens	155-159
12142119-5	2002	Deoxyribonucleic acid samples were genotyped for the nucleotide 2690A>C variation of the HERG gene, corresponding to the HERG K(lysine)897T(threonine) amino acid polymorphism.	Lysine	131-137	potassium voltage-gated channel subfamily H member 2	Homo sapiens	92-96
12142119-5	2002	Deoxyribonucleic acid samples were genotyped for the nucleotide 2690A>C variation of the HERG gene, corresponding to the HERG K(lysine)897T(threonine) amino acid polymorphism.	Lysine	131-137	potassium voltage-gated channel subfamily H member 2	Homo sapiens	124-128
12142119-5	2002	Deoxyribonucleic acid samples were genotyped for the nucleotide 2690A>C variation of the HERG gene, corresponding to the HERG K(lysine)897T(threonine) amino acid polymorphism.	Threonine	143-152	potassium voltage-gated channel subfamily H member 2	Homo sapiens	92-96
12142119-5	2002	Deoxyribonucleic acid samples were genotyped for the nucleotide 2690A>C variation of the HERG gene, corresponding to the HERG K(lysine)897T(threonine) amino acid polymorphism.	Threonine	143-152	potassium voltage-gated channel subfamily H member 2	Homo sapiens	124-128
12142125-9	2002	Nicorandil caused greater shortening of ARI and greater attenuation of transmural ARI dispersion in the LQT2 model than in the LQT3 model.	Nicorandil	0-10	potassium voltage-gated channel subfamily H member 2	Homo sapiens	104-108
12142125-10	2002	After treatment with nicorandil, a single VTA was induced in the LQT2 model by LSS, whereas in the LQT3 model, VTA remained inducible by BRADY in four experiments and LSS in one experiment.	Nicorandil	21-31	potassium voltage-gated channel subfamily H member 2	Homo sapiens	65-69
12142125-12	2002	Nicorandil attenuated the heterogeneity of ventricular repolarization and suppressed the induction of VTA in the LQT2 model, but had a limited therapeutic effect in the LQT3 model.	Nicorandil	0-10	potassium voltage-gated channel subfamily H member 2	Homo sapiens	113-117
12063283-6	2002	Cardiac action potential duration was prolonged by antagonists of either ERG1 (MK-499, cisapride) or KCNQ1/KCNE1 (chromanol 293B).	L 706000	79-85	potassium voltage-gated channel subfamily H member 2	Homo sapiens	73-77
12086981-0	2002	Inhibition of the current of heterologously expressed HERG potassium channels by flecainide and comparison with quinidine, propafenone and lignocaine.	Flecainide	81-91	potassium voltage-gated channel subfamily H member 2	Homo sapiens	54-58
12086981-3	2002	In this study, we investigated the effects of the Class Ic antiarrhythmic agent flecainide (FLEC) on ionic current (I(HERG)) mediated by cloned HERG channels at 37 degrees C. We also compared the inhibitory potency of FLEC with other Class I agents: quinidine (QUIN, Class Ia); lignocaine (LIG, Class Ib) and propafenone (PROPAF, Class Ic).	Flecainide	80-90	potassium voltage-gated channel subfamily H member 2	Homo sapiens	118-122
12086981-3	2002	In this study, we investigated the effects of the Class Ic antiarrhythmic agent flecainide (FLEC) on ionic current (I(HERG)) mediated by cloned HERG channels at 37 degrees C. We also compared the inhibitory potency of FLEC with other Class I agents: quinidine (QUIN, Class Ia); lignocaine (LIG, Class Ib) and propafenone (PROPAF, Class Ic).	Flecainide	80-90	potassium voltage-gated channel subfamily H member 2	Homo sapiens	144-148
12086981-3	2002	In this study, we investigated the effects of the Class Ic antiarrhythmic agent flecainide (FLEC) on ionic current (I(HERG)) mediated by cloned HERG channels at 37 degrees C. We also compared the inhibitory potency of FLEC with other Class I agents: quinidine (QUIN, Class Ia); lignocaine (LIG, Class Ib) and propafenone (PROPAF, Class Ic).	Flecainide	92-96	potassium voltage-gated channel subfamily H member 2	Homo sapiens	118-122
12086981-3	2002	In this study, we investigated the effects of the Class Ic antiarrhythmic agent flecainide (FLEC) on ionic current (I(HERG)) mediated by cloned HERG channels at 37 degrees C. We also compared the inhibitory potency of FLEC with other Class I agents: quinidine (QUIN, Class Ia); lignocaine (LIG, Class Ib) and propafenone (PROPAF, Class Ic).	Flecainide	92-96	potassium voltage-gated channel subfamily H member 2	Homo sapiens	144-148
12086981-15	2002	Under similar recording conditions QUIN inhibited I(HERG) with an IC(50) of 0.41+/-0.04 microM and PROPAF inhibited I(HERG) with an IC(50) of 0.44+/-0.07 microM.	Quinidine	35-39	potassium voltage-gated channel subfamily H member 2	Homo sapiens	52-56
12086981-21	2002	The rank potency as HERG blockers of the Class I drugs tested in this study was QUIN=PROPAF>FLEC>>LIG.	Quinidine	80-84	potassium voltage-gated channel subfamily H member 2	Homo sapiens	20-24
12065733-2	2002	To clarify the underlying ionic mechanisms, we examined the effects of six macrolides on the human ether-a-go-go-related gene (HERG)-encoded potassium current stably expressed in human embryonic kidney-293 cells.	Potassium	141-150	potassium voltage-gated channel subfamily H member 2	Homo sapiens	127-131
12065733-6	2002	Mechanistic studies showed that inhibition of HERG current by clarithromycin did not require activation of the channel and was both voltage- and time-dependent.	Clarithromycin	62-76	potassium voltage-gated channel subfamily H member 2	Homo sapiens	46-50
12070109-5	2002	We tested terfenadine carboxylate (fexofenadine) and terfenadine, structurally similar drugs with markedly different affinities for HERG block, for rescue of trafficking-defective LQT2 mutations.	fexofenadine	10-33	potassium voltage-gated channel subfamily H member 2	Homo sapiens	180-184
12084597-6	2002	RESULTS: Propranolol in the absence of epinephrine significantly prolonged the mean cQT(p) value but not the mean cQT(e) value, thus decreasing the mean cT(p-e) value in both LQT1 and LQT2 patients; the differences with propranolol were significantly larger in LQT1 than in LQT2 (p < 0.05).	Propranolol	9-20	potassium voltage-gated channel subfamily H member 2	Homo sapiens	184-188
11960982-2	2002	Here we investigate the voltage-dependent block of wild-type and mutant human ether-a-go-go related gene (HERG) K(+) channels by the antimalarial compound chloroquine.	Chloroquine	155-166	potassium voltage-gated channel subfamily H member 2	Homo sapiens	106-110
11960982-5	2002	Chloroquine also slowed the apparent rate of HERG deactivation, reflecting the inability of drug-bound channels to close.	Chloroquine	0-11	potassium voltage-gated channel subfamily H member 2	Homo sapiens	45-49
11960982-6	2002	Mutation to alanine of aromatic residues (Tyr-652 or Phe-656) located in the S6 domain of HERG greatly reduced the potency of channel block by chloroquine (IC(50) > 1 mm at 0 mV).	Alanine	12-19	potassium voltage-gated channel subfamily H member 2	Homo sapiens	90-94
11960982-6	2002	Mutation to alanine of aromatic residues (Tyr-652 or Phe-656) located in the S6 domain of HERG greatly reduced the potency of channel block by chloroquine (IC(50) > 1 mm at 0 mV).	Tyrosine	42-45	potassium voltage-gated channel subfamily H member 2	Homo sapiens	90-94
11960982-6	2002	Mutation to alanine of aromatic residues (Tyr-652 or Phe-656) located in the S6 domain of HERG greatly reduced the potency of channel block by chloroquine (IC(50) > 1 mm at 0 mV).	Phenylalanine	53-56	potassium voltage-gated channel subfamily H member 2	Homo sapiens	90-94
11960982-6	2002	Mutation to alanine of aromatic residues (Tyr-652 or Phe-656) located in the S6 domain of HERG greatly reduced the potency of channel block by chloroquine (IC(50) > 1 mm at 0 mV).	Chloroquine	143-154	potassium voltage-gated channel subfamily H member 2	Homo sapiens	90-94
11960982-9	2002	HERG channel block was voltage-independent when the hydroxyl group of Tyr-652 was removed by mutating the residue to Phe.	Tyrosine	70-73	potassium voltage-gated channel subfamily H member 2	Homo sapiens	0-4
11960982-9	2002	HERG channel block was voltage-independent when the hydroxyl group of Tyr-652 was removed by mutating the residue to Phe.	Phenylalanine	117-120	potassium voltage-gated channel subfamily H member 2	Homo sapiens	0-4
11960982-10	2002	Together these findings indicate a critical role for Tyr-652 in voltage-dependent block of HERG channels.	Tyrosine	53-56	potassium voltage-gated channel subfamily H member 2	Homo sapiens	91-95
11960982-11	2002	Molecular modeling was used to define energy-minimized dockings of chloroquine to the central cavity of HERG.	Chloroquine	67-78	potassium voltage-gated channel subfamily H member 2	Homo sapiens	104-108
11960982-12	2002	Our experimental findings and modeling suggest that chloroquine preferentially blocks open HERG channels by cation-pi and pi-stacking interactions with Tyr-652 and Phe-656 of multiple subunits.	Chloroquine	52-63	potassium voltage-gated channel subfamily H member 2	Homo sapiens	91-95
11893742-7	2002	The selective HERG channel blocker, E-4031, reduced proliferation of CEM, U937, and K562 cells, and this appears to be the first direct evidence of a functional role for the HERG current in cancer cells.	E 4031	36-42	potassium voltage-gated channel subfamily H member 2	Homo sapiens	14-18
11960982-12	2002	Our experimental findings and modeling suggest that chloroquine preferentially blocks open HERG channels by cation-pi and pi-stacking interactions with Tyr-652 and Phe-656 of multiple subunits.	Tyrosine	152-155	potassium voltage-gated channel subfamily H member 2	Homo sapiens	91-95
11960982-12	2002	Our experimental findings and modeling suggest that chloroquine preferentially blocks open HERG channels by cation-pi and pi-stacking interactions with Tyr-652 and Phe-656 of multiple subunits.	Phenylalanine	164-167	potassium voltage-gated channel subfamily H member 2	Homo sapiens	91-95
12029369-7	2002	It also demonstrates that both proximal and eag/PAS domains in the amino terminus contribute to set the gating characteristics of HERG channels.	Protactinium	48-51	potassium voltage-gated channel subfamily H member 2	Homo sapiens	130-134
12069453-7	2002	Epinephrine also prolonged the QTc dramatically (502+/-23 to 620+/-39 ms; P<0.0005, +24%) at peak of epinephrine in LQT2 patients, but this shortened to baseline levels at steady state (531+/-25 ms; P=ns vs baseline, +6%).	Epinephrine	0-11	potassium voltage-gated channel subfamily H member 2	Homo sapiens	119-123
12069453-7	2002	Epinephrine also prolonged the QTc dramatically (502+/-23 to 620+/-39 ms; P<0.0005, +24%) at peak of epinephrine in LQT2 patients, but this shortened to baseline levels at steady state (531+/-25 ms; P=ns vs baseline, +6%).	Epinephrine	104-115	potassium voltage-gated channel subfamily H member 2	Homo sapiens	119-123
11864984-2	2002	Potential insight into the coupling mechanism was provided by our previous finding that mutation to Lys of a single residue (Asp(540)) located in the S4-S5 linker endowed HERG (human ether-a-go-go-related gene) K(+) channels with the unusual ability to open in response to membrane depolarization and hyperpolarization in a voltage-dependent manner.	Lysine	100-103	potassium voltage-gated channel subfamily H member 2	Homo sapiens	171-175
11864984-2	2002	Potential insight into the coupling mechanism was provided by our previous finding that mutation to Lys of a single residue (Asp(540)) located in the S4-S5 linker endowed HERG (human ether-a-go-go-related gene) K(+) channels with the unusual ability to open in response to membrane depolarization and hyperpolarization in a voltage-dependent manner.	Aspartic Acid	125-128	potassium voltage-gated channel subfamily H member 2	Homo sapiens	171-175
11864984-4	2002	Therefore, we mutated six residues located in this region of S6 (Ile(662)-Tyr(667)) to Ala in D540K HERG channels.	Isoleucine	65-68	potassium voltage-gated channel subfamily H member 2	Homo sapiens	100-104
11864984-5	2002	Mutation of Arg(665), but not the other five residues, prevented hyperpolarization-dependent reopening of D540K HERG channels.	Arginine	12-15	potassium voltage-gated channel subfamily H member 2	Homo sapiens	112-116
11864984-8	2002	Together these findings suggest that a single residue (Arg(665)) in the S6 domain interacts with Lys(540) by electrostatic repulsion to couple voltage sensing to hyperpolarization-dependent opening of D540K HERG K(+) channels.	Arginine	55-58	potassium voltage-gated channel subfamily H member 2	Homo sapiens	207-211
11864984-8	2002	Together these findings suggest that a single residue (Arg(665)) in the S6 domain interacts with Lys(540) by electrostatic repulsion to couple voltage sensing to hyperpolarization-dependent opening of D540K HERG K(+) channels.	Lysine	97-100	potassium voltage-gated channel subfamily H member 2	Homo sapiens	207-211
11893742-7	2002	The selective HERG channel blocker, E-4031, reduced proliferation of CEM, U937, and K562 cells, and this appears to be the first direct evidence of a functional role for the HERG current in cancer cells.	E 4031	36-42	potassium voltage-gated channel subfamily H member 2	Homo sapiens	174-178
12133532-4	2002	RESULTS: Elevation of the intracellular cAMP-concentration by incubation with the adenylate cyclase activator, forskolin (10 micromol/L), and the broad range phosphodiesterase inhibitor, IBMX (100 micromol/L), caused a HERG tail current reduction of 83.2%.	Cyclic AMP	40-44	potassium voltage-gated channel subfamily H member 2	Homo sapiens	219-223
11864985-2	2002	We apply cysteine-scanning mutagenesis to the S5-P and P-S6 linkers of HERG and examine the resulting changes in ErgTx potency.	Cysteine	9-17	potassium voltage-gated channel subfamily H member 2	Homo sapiens	71-75
12133532-9	2002	The coupling between the repolarizing cardiac HERG potassium current and the protein kinase A system could contribute to arrhythmogenesis under pathophysiological conditions.	Potassium	51-60	potassium voltage-gated channel subfamily H member 2	Homo sapiens	46-50
12062363-3	2002	Therefore, we investigated the role of a glutamic acid at the vicinity of the pore in HERG channels by mutating it to a lysine.	Glutamic Acid	41-54	potassium voltage-gated channel subfamily H member 2	Homo sapiens	86-90
11834728-4	2002	In this first report of regulation by tyrosine phosphorylation we show that MLS-9 cells express transcripts for r-erg1 (rat homologue of HERG) and r-erg2, and an immunoreactive doublet was identified using an anti-HERG antibody.	Tyrosine	38-46	potassium voltage-gated channel subfamily H member 2	Homo sapiens	137-141
11834728-4	2002	In this first report of regulation by tyrosine phosphorylation we show that MLS-9 cells express transcripts for r-erg1 (rat homologue of HERG) and r-erg2, and an immunoreactive doublet was identified using an anti-HERG antibody.	Tyrosine	38-46	potassium voltage-gated channel subfamily H member 2	Homo sapiens	214-218
11953308-3	2002	Stress stimulates beta-adrenergic receptors, leading to cAMP elevations that can regulate HERG K+ channels both directly and via phosphorylation by cAMP-dependent protein kinase (PKA).	Cyclic AMP	56-60	potassium voltage-gated channel subfamily H member 2	Homo sapiens	90-94
11953308-4	2002	We show that HERG associates with 14-3-3epsilon to potentiate cAMP/PKA effects upon HERG.	Cyclic AMP	62-66	potassium voltage-gated channel subfamily H member 2	Homo sapiens	13-17
11953308-4	2002	We show that HERG associates with 14-3-3epsilon to potentiate cAMP/PKA effects upon HERG.	Cyclic AMP	62-66	potassium voltage-gated channel subfamily H member 2	Homo sapiens	84-88
11927665-7	2002	There were major discrepancies between the sensitivity to quinidine, E-4031 and dofetilide of I(HERG) in Xenopus oocytes compared to I(Kr), which were not substantially affected by coexpression with MiRP1.	dofetilide	80-90	potassium voltage-gated channel subfamily H member 2	Homo sapiens	94-101
11756457-1	2002	The K(+) channels encoded by the human Ether-a-gogo Related Gene-1 (hERG1) are crucially involved in controlling heart and brain excitability and are selectively influenced by reactive oxygen species (ROS).	Reactive Oxygen Species	176-199	potassium voltage-gated channel subfamily H member 2	Homo sapiens	68-73
11756457-1	2002	The K(+) channels encoded by the human Ether-a-gogo Related Gene-1 (hERG1) are crucially involved in controlling heart and brain excitability and are selectively influenced by reactive oxygen species (ROS).	Reactive Oxygen Species	201-204	potassium voltage-gated channel subfamily H member 2	Homo sapiens	68-73
11756457-2	2002	To localize the molecular regions involved in ROS-induced modulation of hERG1, segmental exchanges between the ROS-sensitive hERG1 and the ROS-insensitive bovine ether-a-gogo gene (bEAG) K(+) channels were generated, and the sensitivity of these chimeric channels to ROS was studied with the two-microelectrode voltage-clamp technique upon their expression in Xenopus oocytes.	Reactive Oxygen Species	46-49	potassium voltage-gated channel subfamily H member 2	Homo sapiens	72-77
11756457-2	2002	To localize the molecular regions involved in ROS-induced modulation of hERG1, segmental exchanges between the ROS-sensitive hERG1 and the ROS-insensitive bovine ether-a-gogo gene (bEAG) K(+) channels were generated, and the sensitivity of these chimeric channels to ROS was studied with the two-microelectrode voltage-clamp technique upon their expression in Xenopus oocytes.	Reactive Oxygen Species	111-114	potassium voltage-gated channel subfamily H member 2	Homo sapiens	125-130
11756457-2	2002	To localize the molecular regions involved in ROS-induced modulation of hERG1, segmental exchanges between the ROS-sensitive hERG1 and the ROS-insensitive bovine ether-a-gogo gene (bEAG) K(+) channels were generated, and the sensitivity of these chimeric channels to ROS was studied with the two-microelectrode voltage-clamp technique upon their expression in Xenopus oocytes.	Reactive Oxygen Species	111-114	potassium voltage-gated channel subfamily H member 2	Homo sapiens	125-130
11756457-2	2002	To localize the molecular regions involved in ROS-induced modulation of hERG1, segmental exchanges between the ROS-sensitive hERG1 and the ROS-insensitive bovine ether-a-gogo gene (bEAG) K(+) channels were generated, and the sensitivity of these chimeric channels to ROS was studied with the two-microelectrode voltage-clamp technique upon their expression in Xenopus oocytes.	Reactive Oxygen Species	111-114	potassium voltage-gated channel subfamily H member 2	Homo sapiens	125-130
11756457-3	2002	Substitution of the S(5)-S(6) linker of hERG1 with the corresponding bEAG region removed channel sensitivity to ROS, whereas the reverse chimeric exchange introduced ROS sensitivity into bEAG.	Reactive Oxygen Species	112-115	potassium voltage-gated channel subfamily H member 2	Homo sapiens	40-45
11756457-4	2002	Mutation of each of the two hERG1 histidines at positions 578 and 587 within the S(5)-S(6) linker generated K(+) channels insensitive to modulation by ROS.	Histidine	34-44	potassium voltage-gated channel subfamily H member 2	Homo sapiens	28-33
11756457-5	2002	In addition, the two iron chelators desferrioxamine (1 mm) and o-phenanthroline (0.2 mm) significantly inhibited hERG1 outward K(+) currents and prevented hERG1 inhibition induced by the ROS-scavenging enzyme catalase (1000 units/ml).	Iron	21-25	potassium voltage-gated channel subfamily H member 2	Homo sapiens	113-118
11756457-5	2002	In addition, the two iron chelators desferrioxamine (1 mm) and o-phenanthroline (0.2 mm) significantly inhibited hERG1 outward K(+) currents and prevented hERG1 inhibition induced by the ROS-scavenging enzyme catalase (1000 units/ml).	Iron	21-25	potassium voltage-gated channel subfamily H member 2	Homo sapiens	155-160
11756457-5	2002	In addition, the two iron chelators desferrioxamine (1 mm) and o-phenanthroline (0.2 mm) significantly inhibited hERG1 outward K(+) currents and prevented hERG1 inhibition induced by the ROS-scavenging enzyme catalase (1000 units/ml).	Deferoxamine	36-51	potassium voltage-gated channel subfamily H member 2	Homo sapiens	113-118
11756457-5	2002	In addition, the two iron chelators desferrioxamine (1 mm) and o-phenanthroline (0.2 mm) significantly inhibited hERG1 outward K(+) currents and prevented hERG1 inhibition induced by the ROS-scavenging enzyme catalase (1000 units/ml).	Deferoxamine	36-51	potassium voltage-gated channel subfamily H member 2	Homo sapiens	155-160
11756457-5	2002	In addition, the two iron chelators desferrioxamine (1 mm) and o-phenanthroline (0.2 mm) significantly inhibited hERG1 outward K(+) currents and prevented hERG1 inhibition induced by the ROS-scavenging enzyme catalase (1000 units/ml).	1,10-phenanthroline	63-79	potassium voltage-gated channel subfamily H member 2	Homo sapiens	113-118
11756457-5	2002	In addition, the two iron chelators desferrioxamine (1 mm) and o-phenanthroline (0.2 mm) significantly inhibited hERG1 outward K(+) currents and prevented hERG1 inhibition induced by the ROS-scavenging enzyme catalase (1000 units/ml).	1,10-phenanthroline	63-79	potassium voltage-gated channel subfamily H member 2	Homo sapiens	155-160
11756457-5	2002	In addition, the two iron chelators desferrioxamine (1 mm) and o-phenanthroline (0.2 mm) significantly inhibited hERG1 outward K(+) currents and prevented hERG1 inhibition induced by the ROS-scavenging enzyme catalase (1000 units/ml).	Reactive Oxygen Species	187-190	potassium voltage-gated channel subfamily H member 2	Homo sapiens	113-118
11756457-5	2002	In addition, the two iron chelators desferrioxamine (1 mm) and o-phenanthroline (0.2 mm) significantly inhibited hERG1 outward K(+) currents and prevented hERG1 inhibition induced by the ROS-scavenging enzyme catalase (1000 units/ml).	Reactive Oxygen Species	187-190	potassium voltage-gated channel subfamily H member 2	Homo sapiens	155-160
11756457-6	2002	Finally, the hERG1-inhibitory effect exerted by the iron chelators was prevented by the hERG1 H578D/H587Y double mutation.	Iron	52-56	potassium voltage-gated channel subfamily H member 2	Homo sapiens	13-18
11756457-6	2002	Finally, the hERG1-inhibitory effect exerted by the iron chelators was prevented by the hERG1 H578D/H587Y double mutation.	Iron	52-56	potassium voltage-gated channel subfamily H member 2	Homo sapiens	88-93
11756457-7	2002	Collectively, the results obtained suggest that histidines at positions 578 and 587 in the S(5)-S(6) linker region of hERG1 K(+) channels are crucial players in ROS-induced modulation of hERG1 K(+) channels.	Histidine	48-58	potassium voltage-gated channel subfamily H member 2	Homo sapiens	118-123
11756457-7	2002	Collectively, the results obtained suggest that histidines at positions 578 and 587 in the S(5)-S(6) linker region of hERG1 K(+) channels are crucial players in ROS-induced modulation of hERG1 K(+) channels.	Histidine	48-58	potassium voltage-gated channel subfamily H member 2	Homo sapiens	187-192
11756457-7	2002	Collectively, the results obtained suggest that histidines at positions 578 and 587 in the S(5)-S(6) linker region of hERG1 K(+) channels are crucial players in ROS-induced modulation of hERG1 K(+) channels.	Reactive Oxygen Species	161-164	potassium voltage-gated channel subfamily H member 2	Homo sapiens	118-123
11756457-7	2002	Collectively, the results obtained suggest that histidines at positions 578 and 587 in the S(5)-S(6) linker region of hERG1 K(+) channels are crucial players in ROS-induced modulation of hERG1 K(+) channels.	Reactive Oxygen Species	161-164	potassium voltage-gated channel subfamily H member 2	Homo sapiens	187-192
12645305-29	2002	TRH modifies the current kinetics of human HERG potassium channel co-expressed in Xenopus oocytes with the TRH receptor, whose activity is modulated via the protein kinase C pathway linked to a G protein-coupled receptor and is regulated by changes in the PIP2 concentration in the membrane.	Phosphatidylinositol 4,5-Diphosphate	256-260	potassium voltage-gated channel subfamily H member 2	Homo sapiens	43-47
11852052-0	2002	Inhibitory actions of the selective serotonin re-uptake inhibitor citalopram on HERG and ventricular L-type calcium currents.	Serotonin	36-45	potassium voltage-gated channel subfamily H member 2	Homo sapiens	80-84
11852052-0	2002	Inhibitory actions of the selective serotonin re-uptake inhibitor citalopram on HERG and ventricular L-type calcium currents.	Citalopram	66-76	potassium voltage-gated channel subfamily H member 2	Homo sapiens	80-84
11852052-1	2002	Using whole-cell patch clamp recording of heterologous HERG-mediated currents in transfected mammalian cells, we observed that the selective serotonin re-uptake inhibitor citalopram blocks HERG with an IC(50) of 3.97 microM.	Serotonin	141-150	potassium voltage-gated channel subfamily H member 2	Homo sapiens	55-59
11852052-1	2002	Using whole-cell patch clamp recording of heterologous HERG-mediated currents in transfected mammalian cells, we observed that the selective serotonin re-uptake inhibitor citalopram blocks HERG with an IC(50) of 3.97 microM.	Serotonin	141-150	potassium voltage-gated channel subfamily H member 2	Homo sapiens	189-193
11852052-1	2002	Using whole-cell patch clamp recording of heterologous HERG-mediated currents in transfected mammalian cells, we observed that the selective serotonin re-uptake inhibitor citalopram blocks HERG with an IC(50) of 3.97 microM.	Citalopram	171-181	potassium voltage-gated channel subfamily H member 2	Homo sapiens	55-59
11852052-1	2002	Using whole-cell patch clamp recording of heterologous HERG-mediated currents in transfected mammalian cells, we observed that the selective serotonin re-uptake inhibitor citalopram blocks HERG with an IC(50) of 3.97 microM.	Citalopram	171-181	potassium voltage-gated channel subfamily H member 2	Homo sapiens	189-193
11852052-6	2002	The effects of citalopram on both calcium current amplitude and the I(Ca,L) "window" may help to explain citalopram"s good cardiac safety profile, given its propensity to block HERG at excessive dosages.	Citalopram	15-25	potassium voltage-gated channel subfamily H member 2	Homo sapiens	177-181
11852052-6	2002	The effects of citalopram on both calcium current amplitude and the I(Ca,L) "window" may help to explain citalopram"s good cardiac safety profile, given its propensity to block HERG at excessive dosages.	Citalopram	105-115	potassium voltage-gated channel subfamily H member 2	Homo sapiens	177-181
11805215-0	2002	The antidepressant drug fluoxetine is an inhibitor of human ether-a-go-go-related gene (HERG) potassium channels.	Fluoxetine	24-34	potassium voltage-gated channel subfamily H member 2	Homo sapiens	88-92
11805215-5	2002	We found that fluoxetine blocked HERG channels with an IC(50) value of 3.1 microM.	Fluoxetine	14-24	potassium voltage-gated channel subfamily H member 2	Homo sapiens	33-37
11805215-9	2002	This is the first study demonstrating that HERG potassium channels are blocked by the selective serotonin reuptake inhibitor fluoxetine.	Fluoxetine	125-135	potassium voltage-gated channel subfamily H member 2	Homo sapiens	43-47
11755529-1	2002	We show here that ergtoxin (ErgTx) is a bona fide, specific blocker of the human ether-a-go-go-related gene (HERG) channels.	(6aR,9R)-N-[(1S,2S,4R,7S)-7-benzyl-2-hydroxy-5,8-dioxo-4-propan-2-yl-3-oxa-6,9-diazatricyclo[7.3.0.02,6]dodecan-4-yl]-7-methyl-6,6a,8,9-tetrahydro-4H-indolo[4,3-fg]quinoline-9-carboxamide;(6aR,9R)-N-[(1S,2S,4R,7S)-2-hydroxy-5,8-dioxo-4,7-di(propan-2-yl)-3-oxa-6,9-diazatricyclo[7.3.0.02,6]dodecan-4-yl]-7-methyl-6,6a,8,9-tetrahydro-4H-indolo[4,3-fg]quinoline-9-carboxamide;(6aR,9R)-N-[(1S,2S,4R,7S)-2-hydroxy-7-(2-methylpropyl)-5,8-dioxo-4-propan-2-yl-3-oxa-6,9-diazatricyclo[7.3.0.02,6]dodecan-4-yl]-7-methyl-6,6a,8,9-tetrahydro-4H-indolo[4,3-fg]quinoline-9-carboxamide	18-26	potassium voltage-gated channel subfamily H member 2	Homo sapiens	109-113
11755529-4	2002	From the P-region point mutants of HERG channel assays, only the mutant N598Q shows about 25% decrement of the ErgTx inhibitory effect.	n598q	72-77	potassium voltage-gated channel subfamily H member 2	Homo sapiens	35-39
11744013-0	2002	Inhibition of HERG potassium channels by cocaethylene: a metabolite of cocaine and ethanol.	cocaethylene	41-53	potassium voltage-gated channel subfamily H member 2	Homo sapiens	14-18
11744013-0	2002	Inhibition of HERG potassium channels by cocaethylene: a metabolite of cocaine and ethanol.	Cocaine	71-78	potassium voltage-gated channel subfamily H member 2	Homo sapiens	14-18
11744013-0	2002	Inhibition of HERG potassium channels by cocaethylene: a metabolite of cocaine and ethanol.	Ethanol	83-90	potassium voltage-gated channel subfamily H member 2	Homo sapiens	14-18
11744013-3	2002	RESULTS: The cocaethylene inhibition of HERG is concentration-dependent with an IC(50) of 4.0 microM.	cocaethylene	13-25	potassium voltage-gated channel subfamily H member 2	Homo sapiens	40-44
11744013-7	2002	CONCLUSIONS: Cocaethylene inhibits HERG by binding to the activated or open channels and by modulating the kinetics of inactivation.	cocaethylene	13-25	potassium voltage-gated channel subfamily H member 2	Homo sapiens	35-39
11926362-1	2002	In this paper, we describe an assay using radioactive rubidium (86Rb) efflux to screen functional human ether-a go-go-related gene (HERG) K+ channels in a high-throughput screening (HTS) format.	Rubidium	54-62	potassium voltage-gated channel subfamily H member 2	Homo sapiens	132-136
11926362-1	2002	In this paper, we describe an assay using radioactive rubidium (86Rb) efflux to screen functional human ether-a go-go-related gene (HERG) K+ channels in a high-throughput screening (HTS) format.	Rubidium-86	64-68	potassium voltage-gated channel subfamily H member 2	Homo sapiens	132-136
11926362-5	2002	Our results provide some explanations for the variances of the assay results and offer some guidelines for using the Rb efflux assay to evaluate compound interactions with HERG K+ channels in the pharmaceutical industry.	Rubidium	117-119	potassium voltage-gated channel subfamily H member 2	Homo sapiens	172-176
11994029-9	2002	Verapamil is a notable example of a false positive: it blocks human ether-a-go-go-related (HERG) K(+) channels, but is reported to have little potential to trigger torsade de pointes.	Verapamil	0-9	potassium voltage-gated channel subfamily H member 2	Homo sapiens	91-95
11862331-3	2002	In oocytes using the two electrode voltage clamp technique potassium currents of hminK-, HERG- and Kir2.2-expressing oocytes were inhibited by pentobarbital with IC50 values of 0.20, 1.58 and 0.54 mM, respectively.	Potassium	59-68	potassium voltage-gated channel subfamily H member 2	Homo sapiens	89-93
11862331-3	2002	In oocytes using the two electrode voltage clamp technique potassium currents of hminK-, HERG- and Kir2.2-expressing oocytes were inhibited by pentobarbital with IC50 values of 0.20, 1.58 and 0.54 mM, respectively.	Pentobarbital	143-156	potassium voltage-gated channel subfamily H member 2	Homo sapiens	89-93
11862331-5	2002	Pentobarbital-induced HERG inhibition was not dependent on voltage but influenced the deactivation kinetics and shifted half-maximal activation to more negative voltages.	Pentobarbital	0-13	potassium voltage-gated channel subfamily H member 2	Homo sapiens	22-26
11714889-3	2001	Cisapride is a potent blocker of human ether-a-gogo (HERG) K(+) channels and prolongs the cardiac action potential in a reverse use dependence manner.	Cisapride	0-9	potassium voltage-gated channel subfamily H member 2	Homo sapiens	53-57
11739282-0	2001	HERG K(+) channel activity is regulated by changes in phosphatidyl inositol 4,5-bisphosphate.	Phosphatidylinositol 4,5-Diphosphate	54-92	potassium voltage-gated channel subfamily H member 2	Homo sapiens	0-4
11739282-3	2001	We sought to investigate whether PIP2 changes could alter HERG K(+) channel activity in a manner similar to that seen with inward rectifier channels.	Phosphatidylinositol 4,5-Diphosphate	33-37	potassium voltage-gated channel subfamily H member 2	Homo sapiens	58-62
11739282-7	2001	PIP2 significantly attenuated the run-down of HERG channel activity that we normally observe after patch excision, suggesting that channel run-down is due, in part, to membrane depletion of PIP2.	Phosphatidylinositol 4,5-Diphosphate	0-4	potassium voltage-gated channel subfamily H member 2	Homo sapiens	46-50
11739282-7	2001	PIP2 significantly attenuated the run-down of HERG channel activity that we normally observe after patch excision, suggesting that channel run-down is due, in part, to membrane depletion of PIP2.	Phosphatidylinositol 4,5-Diphosphate	190-194	potassium voltage-gated channel subfamily H member 2	Homo sapiens	46-50
11739282-9	2001	The physiological relevance of PIP2-HERG interactions is supported by our finding that phenylephrine reduced the K(+) current density in cells coexpressing alpha1A-receptor and HERG.	Phosphatidylinositol 4,5-Diphosphate	31-35	potassium voltage-gated channel subfamily H member 2	Homo sapiens	36-40
11739282-9	2001	The physiological relevance of PIP2-HERG interactions is supported by our finding that phenylephrine reduced the K(+) current density in cells coexpressing alpha1A-receptor and HERG.	Phosphatidylinositol 4,5-Diphosphate	31-35	potassium voltage-gated channel subfamily H member 2	Homo sapiens	177-181
11739282-9	2001	The physiological relevance of PIP2-HERG interactions is supported by our finding that phenylephrine reduced the K(+) current density in cells coexpressing alpha1A-receptor and HERG.	Phenylephrine	87-100	potassium voltage-gated channel subfamily H member 2	Homo sapiens	36-40
11739282-9	2001	The physiological relevance of PIP2-HERG interactions is supported by our finding that phenylephrine reduced the K(+) current density in cells coexpressing alpha1A-receptor and HERG.	Phenylephrine	87-100	potassium voltage-gated channel subfamily H member 2	Homo sapiens	177-181
11739282-11	2001	Thus, dynamic regulation of HERG K(+) channels may be achieved via receptor-mediated changes in PIP2 concentrations.	Phosphatidylinositol 4,5-Diphosphate	96-100	potassium voltage-gated channel subfamily H member 2	Homo sapiens	28-32
11723241-2	2001	HERG/I(Kr) channels are blocked selectively by class III antiarrhythmic methanesulfonanilide drugs such as dofetilide.	dofetilide	107-117	potassium voltage-gated channel subfamily H member 2	Homo sapiens	0-4
11723241-12	2001	We conclude that high affinity methanesulfonanilide binding to HERG channels is strongly dependent on C-type inactivation.	N-Phenylmethanesulfonamide	31-51	potassium voltage-gated channel subfamily H member 2	Homo sapiens	63-67
11723012-0	2001	Phospholipid metabolite 1-palmitoyl-lysophosphatidylcholine enhances human ether-a-go-go-related gene (HERG) K(+) channel function.	Phospholipids	0-12	potassium voltage-gated channel subfamily H member 2	Homo sapiens	103-107
11723012-0	2001	Phospholipid metabolite 1-palmitoyl-lysophosphatidylcholine enhances human ether-a-go-go-related gene (HERG) K(+) channel function.	We 201	24-59	potassium voltage-gated channel subfamily H member 2	Homo sapiens	103-107
11736694-8	2001	E-4031, a blocker of a novel inwardly rectifying K+ channel, i.e. the human ether-a-go-go-related gene (HERG) K+ channel, significantly increased contraction amplitude.	E 4031	0-6	potassium voltage-gated channel subfamily H member 2	Homo sapiens	104-108
11802537-5	2001	Genotyping revealed a novel nonsense mutation, R744X (C to T transition in codon 744), in the KCNH2 potassium channel gene, resulting in truncation of the putative cyclic nucleotide-binding domain and C-terminal region of the HERG K(+)-channel in all affected family members.	Nucleotides, Cyclic	164-181	potassium voltage-gated channel subfamily H member 2	Homo sapiens	94-99
11802537-5	2001	Genotyping revealed a novel nonsense mutation, R744X (C to T transition in codon 744), in the KCNH2 potassium channel gene, resulting in truncation of the putative cyclic nucleotide-binding domain and C-terminal region of the HERG K(+)-channel in all affected family members.	Nucleotides, Cyclic	164-181	potassium voltage-gated channel subfamily H member 2	Homo sapiens	226-230
11698075-0	2001	[3H]dofetilide binding to HERG transfected membranes: a potential high throughput preclinical screen.	Tritium	1-3	potassium voltage-gated channel subfamily H member 2	Homo sapiens	26-30
11698075-0	2001	[3H]dofetilide binding to HERG transfected membranes: a potential high throughput preclinical screen.	dofetilide	4-14	potassium voltage-gated channel subfamily H member 2	Homo sapiens	26-30
11698075-1	2001	The pharmacological characteristics of [3H]dofetilide binding were examined in membranes prepared from human embryonic kidney (HEK293) cells stably expressing human ether-a-go-go related gene (HERG) K+ channels.	dofetilide	43-53	potassium voltage-gated channel subfamily H member 2	Homo sapiens	193-197
11698075-4	2001	These data indicate that a [3H]dofetilide binding assay using HERG membranes may help identify compounds that prolong the QT interval.	[3h]dofetilide	27-41	potassium voltage-gated channel subfamily H member 2	Homo sapiens	62-66
11561083-0	2001	Effects of cocaine and its major metabolites on the HERG-encoded potassium channel.	Cocaine	11-18	potassium voltage-gated channel subfamily H member 2	Homo sapiens	52-56
11561083-3	2001	Cocaine blocked HERG-encoded potassium channels with an IC50 of 4.4 +/- 1.1 microM (22 degrees C).	Cocaine	0-7	potassium voltage-gated channel subfamily H member 2	Homo sapiens	16-20
11561083-4	2001	Cocaethylene (a metabolite formed in the presence of ethanol) had a significantly lower IC50 of 1.2 +/- 1.1 microM (P < 0.0001), and cocaine"s primary pyrolysis metabolite methylecgonidine blocked HERG with a higher IC50 of 171.7 +/- 1.2 microM.	cocaethylene	0-12	potassium voltage-gated channel subfamily H member 2	Homo sapiens	200-204
11561083-4	2001	Cocaethylene (a metabolite formed in the presence of ethanol) had a significantly lower IC50 of 1.2 +/- 1.1 microM (P < 0.0001), and cocaine"s primary pyrolysis metabolite methylecgonidine blocked HERG with a higher IC50 of 171.7 +/- 1.2 microM.	Ethanol	53-60	potassium voltage-gated channel subfamily H member 2	Homo sapiens	200-204
11511086-1	2001	The antipsychotic drugs sertindole and pimozide are known to prolong the QT interval on the electrocardiogram via a high affinity block of the cardiac K(+) channel known as HERG (human ether-a-go-go-related gene; erg1).	sertindole	24-34	potassium voltage-gated channel subfamily H member 2	Homo sapiens	173-177
11511086-1	2001	The antipsychotic drugs sertindole and pimozide are known to prolong the QT interval on the electrocardiogram via a high affinity block of the cardiac K(+) channel known as HERG (human ether-a-go-go-related gene; erg1).	sertindole	24-34	potassium voltage-gated channel subfamily H member 2	Homo sapiens	213-217
11511086-1	2001	The antipsychotic drugs sertindole and pimozide are known to prolong the QT interval on the electrocardiogram via a high affinity block of the cardiac K(+) channel known as HERG (human ether-a-go-go-related gene; erg1).	Pimozide	39-47	potassium voltage-gated channel subfamily H member 2	Homo sapiens	173-177
11511086-1	2001	The antipsychotic drugs sertindole and pimozide are known to prolong the QT interval on the electrocardiogram via a high affinity block of the cardiac K(+) channel known as HERG (human ether-a-go-go-related gene; erg1).	Pimozide	39-47	potassium voltage-gated channel subfamily H member 2	Homo sapiens	213-217
11669488-4	2001	Mercury (10 microM) inhibited the K+-channels ROMK and HERG, the phosphate transporter NaPi-3, the amino acid transporter rBAT, the cation transporter OCT-2, and the osmolyte transporter BGT.	Mercury	0-7	potassium voltage-gated channel subfamily H member 2	Homo sapiens	55-59
11455010-0	2001	Open channel block of HERG K(+) channels by vesnarinone.	vesnarinone	44-55	potassium voltage-gated channel subfamily H member 2	Homo sapiens	22-26
11455010-2	2001	To elucidate the mechanisms, we studied the effects of vesnarinone on HERG, the cloned human I(Kr) channel, heterologously expressed in Xenopus laevis oocytes.	vesnarinone	55-66	potassium voltage-gated channel subfamily H member 2	Homo sapiens	70-74
11455010-3	2001	Vesnarinone caused a concentration-dependent inhibition of HERG currents with an IC(50) value of 17.7 +/- 2.5 microM at 0 mV (n = 6).	vesnarinone	0-11	potassium voltage-gated channel subfamily H member 2	Homo sapiens	59-63
11455010-8	2001	Vesnarinone produced similar effects on inactivation-removed mutant (G628C/S631C) HERG channels.	vesnarinone	0-11	potassium voltage-gated channel subfamily H member 2	Homo sapiens	82-86
11455010-10	2001	Amino acids important for the binding of vesnarinone were identified using alanine-scanning mutagenesis of residues believed to line the inner cavity of the HERG channel.	vesnarinone	41-52	potassium voltage-gated channel subfamily H member 2	Homo sapiens	157-161
11455010-10	2001	Amino acids important for the binding of vesnarinone were identified using alanine-scanning mutagenesis of residues believed to line the inner cavity of the HERG channel.	Alanine	75-82	potassium voltage-gated channel subfamily H member 2	Homo sapiens	157-161
11455010-13	2001	In conclusion, vesnarinone preferentially blocks open HERG channels, with little effect on channels in the rested or inactivated state.	vesnarinone	15-26	potassium voltage-gated channel subfamily H member 2	Homo sapiens	54-58
11377395-0	2001	Testosterone-mediated modulation of HERG blockade by proarrhythmic agents.	Testosterone	0-12	potassium voltage-gated channel subfamily H member 2	Homo sapiens	36-40
11377395-2	2001	Men are known to be at a lower risk for drug-induced TdP than women suggesting a role of sex steroid hormones, androgens and estrogens, in modulation of drug sensitivity of cardiac K(+) channels, particularly those encoded by HERG.	Steroids	93-100	potassium voltage-gated channel subfamily H member 2	Homo sapiens	226-230
11306689-0	2001	Cocaine blocks HERG, but not KvLQT1+minK, potassium channels.	Cocaine	0-7	potassium voltage-gated channel subfamily H member 2	Homo sapiens	15-19
11306689-2	2001	We investigated the effect of cocaine on the human K(+) channels HERG and KvLQT1+minK that encode native rapidly (I(Kr)) and slowly (I(Ks)) activating delayed rectifier K(+) channels in the heart.	Cocaine	30-37	potassium voltage-gated channel subfamily H member 2	Homo sapiens	65-69
11306689-10	2001	Using N-methyl-cocaine, a permanently charged, membrane-impermeable cocaine analog, block of HERG channels rapidly developed when the drug was applied intracellularly through the patch pipette, suggesting that the cocaine binding site on the HERG protein is located on a cytoplasmic accessible domain.	n-methyl-cocaine	6-22	potassium voltage-gated channel subfamily H member 2	Homo sapiens	93-97
11306689-10	2001	Using N-methyl-cocaine, a permanently charged, membrane-impermeable cocaine analog, block of HERG channels rapidly developed when the drug was applied intracellularly through the patch pipette, suggesting that the cocaine binding site on the HERG protein is located on a cytoplasmic accessible domain.	n-methyl-cocaine	6-22	potassium voltage-gated channel subfamily H member 2	Homo sapiens	242-246
11306689-10	2001	Using N-methyl-cocaine, a permanently charged, membrane-impermeable cocaine analog, block of HERG channels rapidly developed when the drug was applied intracellularly through the patch pipette, suggesting that the cocaine binding site on the HERG protein is located on a cytoplasmic accessible domain.	Cocaine	15-22	potassium voltage-gated channel subfamily H member 2	Homo sapiens	93-97
11306689-10	2001	Using N-methyl-cocaine, a permanently charged, membrane-impermeable cocaine analog, block of HERG channels rapidly developed when the drug was applied intracellularly through the patch pipette, suggesting that the cocaine binding site on the HERG protein is located on a cytoplasmic accessible domain.	Cocaine	15-22	potassium voltage-gated channel subfamily H member 2	Homo sapiens	242-246
11306689-10	2001	Using N-methyl-cocaine, a permanently charged, membrane-impermeable cocaine analog, block of HERG channels rapidly developed when the drug was applied intracellularly through the patch pipette, suggesting that the cocaine binding site on the HERG protein is located on a cytoplasmic accessible domain.	Cocaine	68-75	potassium voltage-gated channel subfamily H member 2	Homo sapiens	93-97
11306689-10	2001	Using N-methyl-cocaine, a permanently charged, membrane-impermeable cocaine analog, block of HERG channels rapidly developed when the drug was applied intracellularly through the patch pipette, suggesting that the cocaine binding site on the HERG protein is located on a cytoplasmic accessible domain.	Cocaine	68-75	potassium voltage-gated channel subfamily H member 2	Homo sapiens	242-246
11306689-11	2001	These results indicate that cocaine suppresses HERG, but not KvLQT1+minK, channels by preferentially blocking activated channels, that it unblocks upon repolarization, and does so with unique ultrarapid kinetics.	Cocaine	28-35	potassium voltage-gated channel subfamily H member 2	Homo sapiens	47-51
11306689-12	2001	Because the cocaine concentration range we studied is achieved in humans, HERG block may provide an additional mechanism for cocaine-induced arrhythmias and sudden death.	Cocaine	12-19	potassium voltage-gated channel subfamily H member 2	Homo sapiens	74-78
11306689-12	2001	Because the cocaine concentration range we studied is achieved in humans, HERG block may provide an additional mechanism for cocaine-induced arrhythmias and sudden death.	Cocaine	125-132	potassium voltage-gated channel subfamily H member 2	Homo sapiens	74-78
11693770-8	2001	The epinephrine-induced increases in the mean QTc-e and Tcp-e were larger in LQT1 than in LQT2, and were more pronounced when the averaged data were obtained from 24-leads than from 87-leads.	Epinephrine	4-15	potassium voltage-gated channel subfamily H member 2	Homo sapiens	90-94
11693770-10	2001	The increase in the QTc-eD was larger in LQT1 than in LQT2 patients.	qtc-ed	20-26	potassium voltage-gated channel subfamily H member 2	Homo sapiens	54-58
11166283-0	2001	[3H]dofetilide binding in SHSY5Y and HEK293 cells expressing a HERG-like K+ channel?	Tritium	1-3	potassium voltage-gated channel subfamily H member 2	Homo sapiens	63-67
11166283-0	2001	[3H]dofetilide binding in SHSY5Y and HEK293 cells expressing a HERG-like K+ channel?	dofetilide	4-14	potassium voltage-gated channel subfamily H member 2	Homo sapiens	63-67
11166283-4	2001	Electrophysiological studies showed that SHSY5Y cells contained a HERG-like K+ current blocked by application of dofetilide to either side of the membrane.	dofetilide	113-123	potassium voltage-gated channel subfamily H member 2	Homo sapiens	66-70
11166283-7	2001	That [3H]dofetilide is specific for I(Kr)/HERG may be questionable, as HEK293 and CHO-K1 cells contain no such functional K+ current.	[3h]dofetilide	5-19	potassium voltage-gated channel subfamily H member 2	Homo sapiens	42-46
11741516-7	2001	Berberine blocked the HERG channels potently with an IC50 value of approximately 75 micromol/L.	Berberine	0-9	potassium voltage-gated channel subfamily H member 2	Homo sapiens	22-26
11741516-9	2001	CONCLUSION: Berberine prolonged APD and possessed blocking effect on IK1, IK, and HERG channel expressed in Xenopus oocytes.	Berberine	12-21	potassium voltage-gated channel subfamily H member 2	Homo sapiens	82-86
11741516-10	2001	The antiarrhythmic mechanism of berberine is related to its inhibitory effects on IK1, IK, and HERG channel.	Berberine	32-41	potassium voltage-gated channel subfamily H member 2	Homo sapiens	95-99
11164846-0	2001	Antiarrhythmic drug carvedilol inhibits HERG potassium channels.	Carvedilol	20-30	potassium voltage-gated channel subfamily H member 2	Homo sapiens	40-44
11164846-6	2001	RESULTS: Carvedilol at a concentration of 10 microM blocked HERG potassium tail currents by 47%.	Carvedilol	9-19	potassium voltage-gated channel subfamily H member 2	Homo sapiens	60-64
11164846-6	2001	RESULTS: Carvedilol at a concentration of 10 microM blocked HERG potassium tail currents by 47%.	Potassium	65-74	potassium voltage-gated channel subfamily H member 2	Homo sapiens	60-64
11164846-9	2001	CONCLUSION: This is the first study demonstrating that carvedilol blocks HERG potassium channels.	Carvedilol	55-65	potassium voltage-gated channel subfamily H member 2	Homo sapiens	73-77
11160646-10	2001	These results suggest that 1) bupivacaine and IQB-9302 block the open state of hKv1.5, Kv2.1, Kv4.3, and HERG channels; and 2) small differences at the N-substituent of these drugs do not affect the drug-induced block of Kv2.1, Kv4.3, or HERG, but specifically modify block of hKv1.5 channels.	IQB 9302	46-54	potassium voltage-gated channel subfamily H member 2	Homo sapiens	105-109
11160646-10	2001	These results suggest that 1) bupivacaine and IQB-9302 block the open state of hKv1.5, Kv2.1, Kv4.3, and HERG channels; and 2) small differences at the N-substituent of these drugs do not affect the drug-induced block of Kv2.1, Kv4.3, or HERG, but specifically modify block of hKv1.5 channels.	IQB 9302	46-54	potassium voltage-gated channel subfamily H member 2	Homo sapiens	238-242
11160863-3	2001	In this study, cocaine was found to be an inhibitor of HERG channels that underlie the rapidly activating component of I(K).	Cocaine	15-22	potassium voltage-gated channel subfamily H member 2	Homo sapiens	55-59
11046096-7	2000	IC(50) values for block of the HERG cardiac K(+) channel measured 3.73, 0.81, 5.95, and 12.1 microM for granisetron, ondansetron, dolasetron, and MDL 74,156, respectively.	Ondansetron	117-128	potassium voltage-gated channel subfamily H member 2	Homo sapiens	31-35
11046096-7	2000	IC(50) values for block of the HERG cardiac K(+) channel measured 3.73, 0.81, 5.95, and 12.1 microM for granisetron, ondansetron, dolasetron, and MDL 74,156, respectively.	dolasetron	130-140	potassium voltage-gated channel subfamily H member 2	Homo sapiens	31-35
11046096-8	2000	Ondansetron (3 microM) also slowed decay of HERG tail currents.	Ondansetron	0-11	potassium voltage-gated channel subfamily H member 2	Homo sapiens	44-48
11046096-12	2000	The submicromolar affinity of ondansetron for the HERG K(+) channel likely underlies the prolongation of cardiac repolarization reported for this drug.	Ondansetron	30-41	potassium voltage-gated channel subfamily H member 2	Homo sapiens	50-54
11040340-0	2000	Effects of fluoroquinolones on HERG currents.	Fluoroquinolones	11-27	potassium voltage-gated channel subfamily H member 2	Homo sapiens	31-35
11040340-1	2000	We have investigated the effects of four fluoroquinolones on the human ether-a-go-go-related gene (HERG) mediated K(+) currents to evaluate their potential to induce QT-prolongation.	Fluoroquinolones	41-57	potassium voltage-gated channel subfamily H member 2	Homo sapiens	99-103
11040340-3	2000	Bath application of sparfloxacin, moxifloxacin and grepafloxacin produced an inhibition of HERG outward currents at -40 mV with EC(50) of 13.5+/-0.8, 41.	sparfloxacin	20-32	potassium voltage-gated channel subfamily H member 2	Homo sapiens	91-95
11040340-3	2000	Bath application of sparfloxacin, moxifloxacin and grepafloxacin produced an inhibition of HERG outward currents at -40 mV with EC(50) of 13.5+/-0.8, 41.	Moxifloxacin	34-46	potassium voltage-gated channel subfamily H member 2	Homo sapiens	91-95
11040340-3	2000	Bath application of sparfloxacin, moxifloxacin and grepafloxacin produced an inhibition of HERG outward currents at -40 mV with EC(50) of 13.5+/-0.8, 41.	grepafloxacin	51-64	potassium voltage-gated channel subfamily H member 2	Homo sapiens	91-95
11009462-9	2000	However, trafficking could not be restored by chemical chaperones or E-4031, a specific blocker of HERG channels.	E 4031	69-75	potassium voltage-gated channel subfamily H member 2	Homo sapiens	99-103
10866950-2	2000	Selective deletion of the HERG-specific sequence (HERG Delta138-373) located between the conserved initial amino terminus (the eag or PAS domain) and the first transmembrane helix accelerates channel activation and shifts its voltage dependence to hyperpolarized values.	Methyl 2-acetamido-2-deoxy-beta-D-glucopyranoside	127-130	potassium voltage-gated channel subfamily H member 2	Homo sapiens	26-30
10866950-2	2000	Selective deletion of the HERG-specific sequence (HERG Delta138-373) located between the conserved initial amino terminus (the eag or PAS domain) and the first transmembrane helix accelerates channel activation and shifts its voltage dependence to hyperpolarized values.	Methyl 2-acetamido-2-deoxy-beta-D-glucopyranoside	127-130	potassium voltage-gated channel subfamily H member 2	Homo sapiens	50-54
10866950-2	2000	Selective deletion of the HERG-specific sequence (HERG Delta138-373) located between the conserved initial amino terminus (the eag or PAS domain) and the first transmembrane helix accelerates channel activation and shifts its voltage dependence to hyperpolarized values.	Protactinium	134-137	potassium voltage-gated channel subfamily H member 2	Homo sapiens	26-30
10866950-2	2000	Selective deletion of the HERG-specific sequence (HERG Delta138-373) located between the conserved initial amino terminus (the eag or PAS domain) and the first transmembrane helix accelerates channel activation and shifts its voltage dependence to hyperpolarized values.	Protactinium	134-137	potassium voltage-gated channel subfamily H member 2	Homo sapiens	50-54
10871331-3	2000	HERG channel current was inhibited by vesnarinone in a concentration-dependent manner, whereas KvLQT1/minK current was hardly affected by the drug.	vesnarinone	38-49	potassium voltage-gated channel subfamily H member 2	Homo sapiens	0-4
10871331-4	2000	The inhibition of HERG current by vesnarinone became more prominent and faster as the membrane potential was more depolarized.	vesnarinone	34-45	potassium voltage-gated channel subfamily H member 2	Homo sapiens	18-22
10871331-8	2000	Therefore, the effect of vesnarinone on the HERG-K(+) current could be adequately described by a simple kinetic model of drug-channel interaction.	vesnarinone	25-36	potassium voltage-gated channel subfamily H member 2	Homo sapiens	44-48
10898527-0	2000	Altered gating of HERG potassium channels by cobalt and lanthanum.	Cobalt	45-51	potassium voltage-gated channel subfamily H member 2	Homo sapiens	18-22
10898527-0	2000	Altered gating of HERG potassium channels by cobalt and lanthanum.	Lanthanum	56-65	potassium voltage-gated channel subfamily H member 2	Homo sapiens	18-22
10898527-4	2000	Previous studies have reported that IKr of myocytes, and HERG channels heterologously expressed in Xenopus oocytes, are reduced by external Co2+ and La3+.	Cobalt(2+)	140-144	potassium voltage-gated channel subfamily H member 2	Homo sapiens	57-61
10898527-4	2000	Previous studies have reported that IKr of myocytes, and HERG channels heterologously expressed in Xenopus oocytes, are reduced by external Co2+ and La3+.	lanthanum(3+)	149-153	potassium voltage-gated channel subfamily H member 2	Homo sapiens	57-61
10898527-5	2000	We have reinvestigated the "blocking" effect of Co2+ and La3+ on HERG channels expressed in Xenopus oocytes.	Cobalt(2+)	48-52	potassium voltage-gated channel subfamily H member 2	Homo sapiens	65-69
10898527-5	2000	We have reinvestigated the "blocking" effect of Co2+ and La3+ on HERG channels expressed in Xenopus oocytes.	lanthanum(3+)	57-61	potassium voltage-gated channel subfamily H member 2	Homo sapiens	65-69
10898527-9	2000	Co2+ and La3+ accelerated the rate of deactivation, decreased the rate of current activation, and shifted the half-point of the HERG channel activation curve by +53 and +65 mV, respectively.	Cobalt(2+)	0-4	potassium voltage-gated channel subfamily H member 2	Homo sapiens	128-132
10898527-9	2000	Co2+ and La3+ accelerated the rate of deactivation, decreased the rate of current activation, and shifted the half-point of the HERG channel activation curve by +53 and +65 mV, respectively.	lanthanum(3+)	9-13	potassium voltage-gated channel subfamily H member 2	Homo sapiens	128-132
10828461-1	2000	The S631C mutation in human ether-a-go-go-related gene (HERG) channels has previously been reported to disrupt C-type inactivation and ion-selectivity when Cys-631 is in the oxidized state.	Cysteine	156-159	potassium voltage-gated channel subfamily H member 2	Homo sapiens	56-60
10828461-3	2000	We demonstrate that HERGS631C in its reduced state is fully blocked by 1 microM astemizole, terfenadine and dofetilide, similar to wild-type HERG channels.	Astemizole	80-90	potassium voltage-gated channel subfamily H member 2	Homo sapiens	20-24
10828461-3	2000	We demonstrate that HERGS631C in its reduced state is fully blocked by 1 microM astemizole, terfenadine and dofetilide, similar to wild-type HERG channels.	Terfenadine	92-103	potassium voltage-gated channel subfamily H member 2	Homo sapiens	20-24
10828461-3	2000	We demonstrate that HERGS631C in its reduced state is fully blocked by 1 microM astemizole, terfenadine and dofetilide, similar to wild-type HERG channels.	dofetilide	108-118	potassium voltage-gated channel subfamily H member 2	Homo sapiens	20-24
11723241-2	2001	HERG/I(Kr) channels are blocked selectively by class III antiarrhythmic methanesulfonanilide drugs such as dofetilide.	N-Phenylmethanesulfonamide	72-92	potassium voltage-gated channel subfamily H member 2	Homo sapiens	0-4
11602243-1	2001	We did the experiments to search for amino acids that affect quinidine binding to the HERG channel, and have identified an amino acid whose change by mutation affects the binding of various drugs.	Quinidine	61-70	potassium voltage-gated channel subfamily H member 2	Homo sapiens	86-90
11561083-6	2001	Blockade of HERG by cocaine, cocaethylene, and methylecgonidine increased significantly over the voltage range where HERG activates, but became constant at voltages where HERG activation was maximal, indicating that all three drugs block open channels, but by a mechanism that is not highly sensitive to voltage per se.	Cocaine	20-27	potassium voltage-gated channel subfamily H member 2	Homo sapiens	12-16
11561083-6	2001	Blockade of HERG by cocaine, cocaethylene, and methylecgonidine increased significantly over the voltage range where HERG activates, but became constant at voltages where HERG activation was maximal, indicating that all three drugs block open channels, but by a mechanism that is not highly sensitive to voltage per se.	cocaethylene	29-41	potassium voltage-gated channel subfamily H member 2	Homo sapiens	12-16
11561083-6	2001	Blockade of HERG by cocaine, cocaethylene, and methylecgonidine increased significantly over the voltage range where HERG activates, but became constant at voltages where HERG activation was maximal, indicating that all three drugs block open channels, but by a mechanism that is not highly sensitive to voltage per se.	anhydroecgonine methyl ester	47-63	potassium voltage-gated channel subfamily H member 2	Homo sapiens	12-16
11561083-6	2001	Blockade of HERG by cocaine, cocaethylene, and methylecgonidine increased significantly over the voltage range where HERG activates, but became constant at voltages where HERG activation was maximal, indicating that all three drugs block open channels, but by a mechanism that is not highly sensitive to voltage per se.	anhydroecgonine methyl ester	47-63	potassium voltage-gated channel subfamily H member 2	Homo sapiens	117-121
11561083-6	2001	Blockade of HERG by cocaine, cocaethylene, and methylecgonidine increased significantly over the voltage range where HERG activates, but became constant at voltages where HERG activation was maximal, indicating that all three drugs block open channels, but by a mechanism that is not highly sensitive to voltage per se.	anhydroecgonine methyl ester	47-63	potassium voltage-gated channel subfamily H member 2	Homo sapiens	117-121
11561083-8	2001	We conclude that cocaethylene is slightly more potent than cocaine as a blocker of HERG, whereas methylecgonidine has much lower potency, and both benzoylecgonine and ecgonine methyl ester are essentially inactive at clinically relevant concentrations.	cocaethylene	17-29	potassium voltage-gated channel subfamily H member 2	Homo sapiens	83-87
11561083-8	2001	We conclude that cocaethylene is slightly more potent than cocaine as a blocker of HERG, whereas methylecgonidine has much lower potency, and both benzoylecgonine and ecgonine methyl ester are essentially inactive at clinically relevant concentrations.	Cocaine	59-66	potassium voltage-gated channel subfamily H member 2	Homo sapiens	83-87
11561091-0	2001	Interactions of the antimalarial drug mefloquine with the human cardiac potassium channels KvLQT1/minK and HERG.	Mefloquine	38-48	potassium voltage-gated channel subfamily H member 2	Homo sapiens	107-111
11561091-3	2001	Mefloquine can prolong cardiac repolarization, especially when coadministered with halofantrine, an antagonist of the human ether-a-go-go-related gene (HERG) cardiac K+ channel.	Mefloquine	0-10	potassium voltage-gated channel subfamily H member 2	Homo sapiens	152-156
11561091-3	2001	Mefloquine can prolong cardiac repolarization, especially when coadministered with halofantrine, an antagonist of the human ether-a-go-go-related gene (HERG) cardiac K+ channel.	halofantrine	83-95	potassium voltage-gated channel subfamily H member 2	Homo sapiens	152-156
11561091-8	2001	HERG channel currents were about 6-fold less sensitive to block by mefloquine (IC50 = 5.6 microM).	Mefloquine	67-77	potassium voltage-gated channel subfamily H member 2	Homo sapiens	0-4
11561091-12	2001	Inhibition by mefloquine of KvLQT1/minK in the human heart may in part explain the synergistic prolongation of QT interval observed when this drug is coadministered with the HERG antagonist halofantrine.	Mefloquine	14-24	potassium voltage-gated channel subfamily H member 2	Homo sapiens	174-178
11561091-12	2001	Inhibition by mefloquine of KvLQT1/minK in the human heart may in part explain the synergistic prolongation of QT interval observed when this drug is coadministered with the HERG antagonist halofantrine.	halofantrine	190-202	potassium voltage-gated channel subfamily H member 2	Homo sapiens	174-178
11468227-5	2001	Interestingly, six mutations were found in the region of the gene coding for the Per-Arnt-Sim (PAS) and PAS-S1 regions of the HERG protein, stressing the need to examine the entire gene when screening for mutations.	Aminosalicylic Acid	95-98	potassium voltage-gated channel subfamily H member 2	Homo sapiens	126-130
11377395-3	2001	Here by using neuroleptic agents haloperidol, pimozide, and fluspirilene, all of which can induce TdP, and a steroid hormone-sensitive system Xenopus oocytes for HERG channels expression we show that testosterone is able to reduce HERG-blocking potency of neuroleptics.	Pimozide	46-54	potassium voltage-gated channel subfamily H member 2	Homo sapiens	162-166
11377395-3	2001	Here by using neuroleptic agents haloperidol, pimozide, and fluspirilene, all of which can induce TdP, and a steroid hormone-sensitive system Xenopus oocytes for HERG channels expression we show that testosterone is able to reduce HERG-blocking potency of neuroleptics.	Fluspirilene	60-72	potassium voltage-gated channel subfamily H member 2	Homo sapiens	162-166
11377395-3	2001	Here by using neuroleptic agents haloperidol, pimozide, and fluspirilene, all of which can induce TdP, and a steroid hormone-sensitive system Xenopus oocytes for HERG channels expression we show that testosterone is able to reduce HERG-blocking potency of neuroleptics.	Steroids	109-124	potassium voltage-gated channel subfamily H member 2	Homo sapiens	162-166
11377395-3	2001	Here by using neuroleptic agents haloperidol, pimozide, and fluspirilene, all of which can induce TdP, and a steroid hormone-sensitive system Xenopus oocytes for HERG channels expression we show that testosterone is able to reduce HERG-blocking potency of neuroleptics.	Steroids	109-124	potassium voltage-gated channel subfamily H member 2	Homo sapiens	231-235
11377395-3	2001	Here by using neuroleptic agents haloperidol, pimozide, and fluspirilene, all of which can induce TdP, and a steroid hormone-sensitive system Xenopus oocytes for HERG channels expression we show that testosterone is able to reduce HERG-blocking potency of neuroleptics.	Testosterone	200-212	potassium voltage-gated channel subfamily H member 2	Homo sapiens	162-166
11377395-3	2001	Here by using neuroleptic agents haloperidol, pimozide, and fluspirilene, all of which can induce TdP, and a steroid hormone-sensitive system Xenopus oocytes for HERG channels expression we show that testosterone is able to reduce HERG-blocking potency of neuroleptics.	Testosterone	200-212	potassium voltage-gated channel subfamily H member 2	Homo sapiens	231-235
11377395-4	2001	Haloperidol, pimozide, and fluspirilene inhibited HERG current with IC(50) of 1.36, 1.74, and 2.34 microM, and maximal block of 73%, 76% and 65%, respectively.	Haloperidol	0-11	potassium voltage-gated channel subfamily H member 2	Homo sapiens	50-54
11377395-4	2001	Haloperidol, pimozide, and fluspirilene inhibited HERG current with IC(50) of 1.36, 1.74, and 2.34 microM, and maximal block of 73%, 76% and 65%, respectively.	Pimozide	13-21	potassium voltage-gated channel subfamily H member 2	Homo sapiens	50-54
11377395-4	2001	Haloperidol, pimozide, and fluspirilene inhibited HERG current with IC(50) of 1.36, 1.74, and 2.34 microM, and maximal block of 73%, 76% and 65%, respectively.	Fluspirilene	27-39	potassium voltage-gated channel subfamily H member 2	Homo sapiens	50-54
11377395-6	2001	Pretreatment of HERG-expressing oocytes with 1 microM testosterone increased the IC(50) values to 2.73, 2.08, and 5.04 microM, reduced the maximal block to 65%, 59%, and 64%, and strongly diminished voltage-dependence of the blockade.	Testosterone	54-66	potassium voltage-gated channel subfamily H member 2	Homo sapiens	16-20
11377395-7	2001	Testosterone treatment per se produced about a 35% reduction of HERG current compared with untreated oocytes.	Testosterone	0-12	potassium voltage-gated channel subfamily H member 2	Homo sapiens	64-68
11404399-3	2001	Human ether-a-go-go-related gene (HERG) K(+) channels are unusually sensitive to external calcium concentration ([Ca(2+)](o)).	Calcium	90-97	potassium voltage-gated channel subfamily H member 2	Homo sapiens	34-38
11404399-5	2001	The HERG-calcium concentration-response relationship spans the physiological range for [Ca(2+)](o).	Calcium	9-16	potassium voltage-gated channel subfamily H member 2	Homo sapiens	4-8
11278781-0	2001	Analysis of the cyclic nucleotide binding domain of the HERG potassium channel and interactions with KCNE2.	Nucleotides, Cyclic	16-33	potassium voltage-gated channel subfamily H member 2	Homo sapiens	56-60
11278781-1	2001	Mutations in the cyclic nucleotide binding domain (CNBD) of the human ether-a-go-go-related gene (HERG) K+ channel are associated with LQT2, a form of hereditary Long QT syndrome (LQTS).	Nucleotides, Cyclic	17-34	potassium voltage-gated channel subfamily H member 2	Homo sapiens	98-102
11278781-1	2001	Mutations in the cyclic nucleotide binding domain (CNBD) of the human ether-a-go-go-related gene (HERG) K+ channel are associated with LQT2, a form of hereditary Long QT syndrome (LQTS).	Nucleotides, Cyclic	17-34	potassium voltage-gated channel subfamily H member 2	Homo sapiens	135-139
11278781-2	2001	Elevation of cAMP can modulate HERG K+ channels both by direct binding and indirect regulation through protein kinase A.	Cyclic AMP	13-17	potassium voltage-gated channel subfamily H member 2	Homo sapiens	31-35
11278781-3	2001	To assess the physiological significance of cAMP binding to HERG, we introduced mutations to disrupt the cyclic nucleotide binding domain.	Cyclic AMP	44-48	potassium voltage-gated channel subfamily H member 2	Homo sapiens	60-64
11259532-0	2001	Hydrogen peroxide modifies the kinetics of HERG channel expressed in a mammalian cell line.	Hydrogen Peroxide	0-17	potassium voltage-gated channel subfamily H member 2	Homo sapiens	43-47
11259532-3	2001	As these effects could involve the modulation of repolarizing currents, we assessed effects of H2O2 on HERG (which encodes the cardiac potassium channel I(Kr)) expressed in Chinese hamster ovary cells.	Hydrogen Peroxide	95-99	potassium voltage-gated channel subfamily H member 2	Homo sapiens	103-107
11259532-5	2001	HERG activation and deactivation were accelerated when cells were superfused with 30 microM, 100 microM, or 1 mM H2O2.	Hydrogen Peroxide	113-117	potassium voltage-gated channel subfamily H member 2	Homo sapiens	0-4
11259532-9	2001	This indicates that H2O2 diffuses intracellularly before acting on HERG and that its effects on activation but not deactivation are mediated by the superoxide anion.	Hydrogen Peroxide	20-24	potassium voltage-gated channel subfamily H member 2	Homo sapiens	67-71
11238279-7	2001	HERG current in oocytes was reduced by amiodarone (IC(50)=38 micromol/L), whereas KvLQT1/minK current was unaffected by 300 micromol/L amiodarone.	Amiodarone	39-49	potassium voltage-gated channel subfamily H member 2	Homo sapiens	0-4
11741516-0	2001	Inhibitory effects of berberine on IK1, IK, and HERG channels of cardiac myocytes.	Berberine	22-31	potassium voltage-gated channel subfamily H member 2	Homo sapiens	48-52
11160646-9	2001	Bupivacaine and IQB-9302 induced a similar degree of block of HERG channels and induced a steep voltage-dependent decrease of the relative current.	Bupivacaine	0-11	potassium voltage-gated channel subfamily H member 2	Homo sapiens	62-66
11160646-9	2001	Bupivacaine and IQB-9302 induced a similar degree of block of HERG channels and induced a steep voltage-dependent decrease of the relative current.	IQB 9302	16-24	potassium voltage-gated channel subfamily H member 2	Homo sapiens	62-66
11160646-10	2001	These results suggest that 1) bupivacaine and IQB-9302 block the open state of hKv1.5, Kv2.1, Kv4.3, and HERG channels; and 2) small differences at the N-substituent of these drugs do not affect the drug-induced block of Kv2.1, Kv4.3, or HERG, but specifically modify block of hKv1.5 channels.	Bupivacaine	30-41	potassium voltage-gated channel subfamily H member 2	Homo sapiens	105-109
11160646-10	2001	These results suggest that 1) bupivacaine and IQB-9302 block the open state of hKv1.5, Kv2.1, Kv4.3, and HERG channels; and 2) small differences at the N-substituent of these drugs do not affect the drug-induced block of Kv2.1, Kv4.3, or HERG, but specifically modify block of hKv1.5 channels.	Bupivacaine	30-41	potassium voltage-gated channel subfamily H member 2	Homo sapiens	238-242
11125032-0	2001	Interactions of a series of fluoroquinolone antibacterial drugs with the human cardiac K+ channel HERG.	Fluoroquinolones	28-43	potassium voltage-gated channel subfamily H member 2	Homo sapiens	98-102
11125032-7	2001	Block of HERG by sparfloxacin displayed a positive voltage dependence.	sparfloxacin	17-29	potassium voltage-gated channel subfamily H member 2	Homo sapiens	9-13
11125032-9	2001	These results provide a mechanism for the QT prolongation observed clinically with administration of sparfloxacin and certain other fluoroquinolones because free plasma levels of these drugs after therapeutic doses approximate those concentrations that inhibit HERG channel current.	sparfloxacin	101-113	potassium voltage-gated channel subfamily H member 2	Homo sapiens	261-265
11125032-9	2001	These results provide a mechanism for the QT prolongation observed clinically with administration of sparfloxacin and certain other fluoroquinolones because free plasma levels of these drugs after therapeutic doses approximate those concentrations that inhibit HERG channel current.	Fluoroquinolones	132-148	potassium voltage-gated channel subfamily H member 2	Homo sapiens	261-265
11125032-10	2001	In the cases of levofloxacin, ciprofloxacin, and ofloxacin, inhibition of HERG occurs at concentrations much greater than those observed clinically.	Levofloxacin	16-28	potassium voltage-gated channel subfamily H member 2	Homo sapiens	74-78
11125032-10	2001	In the cases of levofloxacin, ciprofloxacin, and ofloxacin, inhibition of HERG occurs at concentrations much greater than those observed clinically.	Ciprofloxacin	30-43	potassium voltage-gated channel subfamily H member 2	Homo sapiens	74-78
11125032-10	2001	In the cases of levofloxacin, ciprofloxacin, and ofloxacin, inhibition of HERG occurs at concentrations much greater than those observed clinically.	Ofloxacin	19-28	potassium voltage-gated channel subfamily H member 2	Homo sapiens	74-78
11125032-12	2001	HERG channel affinity should be an important criterion for the development of newer fluoroquinolones.	Fluoroquinolones	84-100	potassium voltage-gated channel subfamily H member 2	Homo sapiens	0-4
11575008-9	2001	On the other hand terfenadine and astemizole effectively blocked HERG K+ channels with nanomolar affinities (330 and 480 nmol/L, respectively), whereas loratadine was about 300-fold less potent.	Terfenadine	18-29	potassium voltage-gated channel subfamily H member 2	Homo sapiens	65-69
11575008-9	2001	On the other hand terfenadine and astemizole effectively blocked HERG K+ channels with nanomolar affinities (330 and 480 nmol/L, respectively), whereas loratadine was about 300-fold less potent.	Astemizole	34-44	potassium voltage-gated channel subfamily H member 2	Homo sapiens	65-69
11090546-0	2000	Probing the interaction between inactivation gating and Dd-sotalol block of HERG.	Fumigant 93	56-58	potassium voltage-gated channel subfamily H member 2	Homo sapiens	76-80
11090546-0	2000	Probing the interaction between inactivation gating and Dd-sotalol block of HERG.	Sotalol	59-66	potassium voltage-gated channel subfamily H member 2	Homo sapiens	76-80
11090546-1	2000	Potassium channels encoded by HERG underlie I:(Kr), a sensitive target for most class III antiarrhythmic drugs, including methanesulfonanilides such as Dd-sotalol.	methanesulfonanilides	122-143	potassium voltage-gated channel subfamily H member 2	Homo sapiens	30-34
11090546-1	2000	Potassium channels encoded by HERG underlie I:(Kr), a sensitive target for most class III antiarrhythmic drugs, including methanesulfonanilides such as Dd-sotalol.	dd-sotalol	152-162	potassium voltage-gated channel subfamily H member 2	Homo sapiens	30-34
11090546-5	2000	In the present study, we identify a definitive role for inactivation gating in Dd-sotalol block of HERG, using interventions complementary to mutagenesis.	Fumigant 93	79-81	potassium voltage-gated channel subfamily H member 2	Homo sapiens	99-103
11090546-5	2000	In the present study, we identify a definitive role for inactivation gating in Dd-sotalol block of HERG, using interventions complementary to mutagenesis.	Sotalol	82-89	potassium voltage-gated channel subfamily H member 2	Homo sapiens	99-103
11090546-7	2000	In normal extracellular solutions, block of HERG current by 300 micromol/L Dd-sotalol reached 80% after a 10-minute period of repetitive depolarization to +20 mV.	dd-sotalol	75-85	potassium voltage-gated channel subfamily H member 2	Homo sapiens	44-48
11090546-8	2000	Maneuvers that impeded steady-state inactivation also reduced Dd-sotalol block of HERG: 100 micromol/L Cd(2+) reduced steady-state block to 55% at +20 mV (P:<0.05); removing extracellular Na(+) reduced block to 44% (P:<0.05).	dd-sotalol	62-72	potassium voltage-gated channel subfamily H member 2	Homo sapiens	82-86
11082114-0	2000	Inhibition of HERG1 K(+) channels by the novel second-generation antihistamine mizolastine.	antihistamine mizolastine	65-90	potassium voltage-gated channel subfamily H member 2	Homo sapiens	14-19
11082114-5	2000	In the present study, the potential blocking ability of the novel second-generation H(1) receptor antagonist mizolastine of the HERG1 K(+) channels heterologously expressed in Xenopus oocytes and in HEK 293 cells or constitutively present in SH-SY5Y human neuroblastoma cells has been examined and compared to that of astemizole.	mizolastine	109-120	potassium voltage-gated channel subfamily H member 2	Homo sapiens	128-133
11082114-5	2000	In the present study, the potential blocking ability of the novel second-generation H(1) receptor antagonist mizolastine of the HERG1 K(+) channels heterologously expressed in Xenopus oocytes and in HEK 293 cells or constitutively present in SH-SY5Y human neuroblastoma cells has been examined and compared to that of astemizole.	Astemizole	318-328	potassium voltage-gated channel subfamily H member 2	Homo sapiens	128-133
11082114-7	2000	Mizolastine blocked HERG1 K(+) channels expressed in Xenopus oocytes with an estimated IC(50) of 3.4 microM.	mizolastine	0-11	potassium voltage-gated channel subfamily H member 2	Homo sapiens	20-25
11082114-10	2000	In human embryonic kidney 293 cells (HEK 293 cells) stably transfected with HERG1 cDNA, extracellular application of mizolastine exerted a dose-related inhibitory action on I(HERG1), with an IC(50) of 350+/-76 nM.	mizolastine	117-128	potassium voltage-gated channel subfamily H member 2	Homo sapiens	76-81
11082114-10	2000	In human embryonic kidney 293 cells (HEK 293 cells) stably transfected with HERG1 cDNA, extracellular application of mizolastine exerted a dose-related inhibitory action on I(HERG1), with an IC(50) of 350+/-76 nM.	mizolastine	117-128	potassium voltage-gated channel subfamily H member 2	Homo sapiens	175-180
11082114-11	2000	Furthermore, mizolastine dose-dependently inhibited HERG1 K(+) channels constitutively expressed in SH-SY5Y human neuroblastoma clonal cells.	mizolastine	13-24	potassium voltage-gated channel subfamily H member 2	Homo sapiens	52-57
11082114-13	2000	The results of the present study suggest that the novel second-generation H(1) receptor antagonist mizolastine, in concentrations higher than those achieved in vivo during standard therapy, is able to block in some degree both constitutively and heterologously expressed HERG1 K(+) channels, and confirm the heterogeneity of molecules belonging to this therapeutical class with respect to their HERG1-inhibitory action.	mizolastine	99-110	potassium voltage-gated channel subfamily H member 2	Homo sapiens	271-276
11082114-13	2000	The results of the present study suggest that the novel second-generation H(1) receptor antagonist mizolastine, in concentrations higher than those achieved in vivo during standard therapy, is able to block in some degree both constitutively and heterologously expressed HERG1 K(+) channels, and confirm the heterogeneity of molecules belonging to this therapeutical class with respect to their HERG1-inhibitory action.	mizolastine	99-110	potassium voltage-gated channel subfamily H member 2	Homo sapiens	395-400
11033107-0	2000	Comparative effects of azimilide and ambasilide on the human ether-a-go-go-related gene (HERG) potassium channel.	azimilide	23-32	potassium voltage-gated channel subfamily H member 2	Homo sapiens	89-93
11033107-0	2000	Comparative effects of azimilide and ambasilide on the human ether-a-go-go-related gene (HERG) potassium channel.	ambasilide	37-47	potassium voltage-gated channel subfamily H member 2	Homo sapiens	89-93
11033107-1	2000	OBJECTIVE: To evaluate the effects of azimilide and ambasilide on the biophysical properties of the human-ether-a-go-go-related (HERG) channel.	azimilide	38-47	potassium voltage-gated channel subfamily H member 2	Homo sapiens	100-127
11033107-1	2000	OBJECTIVE: To evaluate the effects of azimilide and ambasilide on the biophysical properties of the human-ether-a-go-go-related (HERG) channel.	azimilide	38-47	potassium voltage-gated channel subfamily H member 2	Homo sapiens	129-133
11033107-1	2000	OBJECTIVE: To evaluate the effects of azimilide and ambasilide on the biophysical properties of the human-ether-a-go-go-related (HERG) channel.	ambasilide	52-62	potassium voltage-gated channel subfamily H member 2	Homo sapiens	100-127
11033107-1	2000	OBJECTIVE: To evaluate the effects of azimilide and ambasilide on the biophysical properties of the human-ether-a-go-go-related (HERG) channel.	ambasilide	52-62	potassium voltage-gated channel subfamily H member 2	Homo sapiens	129-133
11033107-7	2000	By comparison, ambasilide inhibited HERG channels with lower potency (IC(50) 3.6 microM), in a voltage- and time-dependent but frequency-independent manner (0.03-1 Hz).	ambasilide	15-25	potassium voltage-gated channel subfamily H member 2	Homo sapiens	36-40
11033107-10	2000	CONCLUSIONS: Inhibition of HERG channels by azimilide and ambasilide exhibits a similar time and voltage-dependence.	azimilide	44-53	potassium voltage-gated channel subfamily H member 2	Homo sapiens	27-31
11033107-10	2000	CONCLUSIONS: Inhibition of HERG channels by azimilide and ambasilide exhibits a similar time and voltage-dependence.	ambasilide	58-68	potassium voltage-gated channel subfamily H member 2	Homo sapiens	27-31
10931813-4	2000	Isoproterenol (50 to 100 nmol/L) was used to mimic an increase in beta-adrenergic tone, d-sotalol (100 micromol/L) to block I(Kr) (LQT2 model), and ATX-II (20 nmol/L) to augment late I(Na) (LQT3 model).	Isoproterenol	0-13	potassium voltage-gated channel subfamily H member 2	Homo sapiens	131-135
10931813-7	2000	High concentrations (10 to 20 micromol/L) completely reversed the effects of 293B+/-isoproterenol and those of d-sotalol to increase APD(90) and TDR and to induce TdP in LQT1 and LQT2 models.	Isoproterenol	84-97	potassium voltage-gated channel subfamily H member 2	Homo sapiens	179-183
10931813-7	2000	High concentrations (10 to 20 micromol/L) completely reversed the effects of 293B+/-isoproterenol and those of d-sotalol to increase APD(90) and TDR and to induce TdP in LQT1 and LQT2 models.	Dexsotalol	111-120	potassium voltage-gated channel subfamily H member 2	Homo sapiens	179-183
10952689-0	2000	Inhibition of HERG potassium channels by the antimalarial agent halofantrine.	halofantrine	64-76	potassium voltage-gated channel subfamily H member 2	Homo sapiens	14-18
10952689-4	2000	We examined the effects of halofantrine on HERG potassium channels stably expressed in Chinese hamster ovary (CHO-K1) cells.	halofantrine	27-39	potassium voltage-gated channel subfamily H member 2	Homo sapiens	43-47
10952689-5	2000	Halofantrine blocked HERG tail currents elicited on repolarization to -60 mV from +30 mV with an IC(50) of 196.9 nM.	halofantrine	0-12	potassium voltage-gated channel subfamily H member 2	Homo sapiens	21-25
10952689-10	2000	We conclude that HERG channel inhibition by halofantrine is the likely underlying cellular mechanism for QT prolongation.	halofantrine	44-56	potassium voltage-gated channel subfamily H member 2	Homo sapiens	17-21
10896755-0	2000	State-dependent barium block of wild-type and inactivation-deficient HERG channels in Xenopus oocytes.	Barium	16-22	potassium voltage-gated channel subfamily H member 2	Homo sapiens	69-73
10896755-1	2000	The effects of Ba2+ on current resulting from the heterologous expression of the human ether-a-go-go related gene (HERG) (IHERG) was studied with two-electrode voltage clamp techniques in Xenopus oocytes.	N-methyl-valyl-amiclenomycin	15-19	potassium voltage-gated channel subfamily H member 2	Homo sapiens	115-119
11714889-4	2001	We compared the effects of four different 5-HT4 receptor agonists (cisapride, prucalopride, renzapride and mosapride) on cloned HERG channels with the objective to evaluate and compare their proarrhythmic potential.	Cisapride	67-76	potassium voltage-gated channel subfamily H member 2	Homo sapiens	128-132
11714889-4	2001	We compared the effects of four different 5-HT4 receptor agonists (cisapride, prucalopride, renzapride and mosapride) on cloned HERG channels with the objective to evaluate and compare their proarrhythmic potential.	prucalopride	78-90	potassium voltage-gated channel subfamily H member 2	Homo sapiens	128-132
11714889-4	2001	We compared the effects of four different 5-HT4 receptor agonists (cisapride, prucalopride, renzapride and mosapride) on cloned HERG channels with the objective to evaluate and compare their proarrhythmic potential.	renzapride	92-102	potassium voltage-gated channel subfamily H member 2	Homo sapiens	128-132
11714889-7	2001	Cisapride inhibited the HERG channels in a concentration-dependent manner with an IC(50) of 2.4 10(-7) M. The IC(50) value for prucalopride to block HERG (5.7 10(-6) M) was 20-fold higher than that of cisapride.	Cisapride	0-9	potassium voltage-gated channel subfamily H member 2	Homo sapiens	24-28
11714889-7	2001	Cisapride inhibited the HERG channels in a concentration-dependent manner with an IC(50) of 2.4 10(-7) M. The IC(50) value for prucalopride to block HERG (5.7 10(-6) M) was 20-fold higher than that of cisapride.	Cisapride	0-9	potassium voltage-gated channel subfamily H member 2	Homo sapiens	149-153
11714889-7	2001	Cisapride inhibited the HERG channels in a concentration-dependent manner with an IC(50) of 2.4 10(-7) M. The IC(50) value for prucalopride to block HERG (5.7 10(-6) M) was 20-fold higher than that of cisapride.	prucalopride	127-139	potassium voltage-gated channel subfamily H member 2	Homo sapiens	24-28
11714889-7	2001	Cisapride inhibited the HERG channels in a concentration-dependent manner with an IC(50) of 2.4 10(-7) M. The IC(50) value for prucalopride to block HERG (5.7 10(-6) M) was 20-fold higher than that of cisapride.	prucalopride	127-139	potassium voltage-gated channel subfamily H member 2	Homo sapiens	149-153
11714889-7	2001	Cisapride inhibited the HERG channels in a concentration-dependent manner with an IC(50) of 2.4 10(-7) M. The IC(50) value for prucalopride to block HERG (5.7 10(-6) M) was 20-fold higher than that of cisapride.	Cisapride	201-210	potassium voltage-gated channel subfamily H member 2	Homo sapiens	24-28
11714889-12	2001	We conclude that the rank order of potency of 5-HT4 agonists to block HERG is cisapride > renzapride > prucalopride > mosapride.	Cisapride	78-87	potassium voltage-gated channel subfamily H member 2	Homo sapiens	70-74
11714889-12	2001	We conclude that the rank order of potency of 5-HT4 agonists to block HERG is cisapride > renzapride > prucalopride > mosapride.	renzapride	93-103	potassium voltage-gated channel subfamily H member 2	Homo sapiens	70-74
11714889-12	2001	We conclude that the rank order of potency of 5-HT4 agonists to block HERG is cisapride > renzapride > prucalopride > mosapride.	prucalopride	109-121	potassium voltage-gated channel subfamily H member 2	Homo sapiens	70-74
11714889-12	2001	We conclude that the rank order of potency of 5-HT4 agonists to block HERG is cisapride > renzapride > prucalopride > mosapride.	mosapride	127-136	potassium voltage-gated channel subfamily H member 2	Homo sapiens	70-74
10720411-1	2000	The N629D mutation, adjacent to the GFG signature sequence of the HERG1 A K(+) channel, causes long-QT syndrome (LQTS).	guanfu base G	36-39	potassium voltage-gated channel subfamily H member 2	Homo sapiens	66-71
10742304-0	2000	Blockade of the HERG human cardiac K(+) channel by the antidepressant drug amitriptyline.	Amitriptyline	75-88	potassium voltage-gated channel subfamily H member 2	Homo sapiens	16-20
10742304-3	2000	We studied the effects of amitriptyline on the human ether-a-go-go-related gene (HERG) channel expressed in Xenopus oocytes and on the rapidly activating delayed rectifier K(+) current (I(Kr)) in rat atrial myocytes.	Amitriptyline	26-39	potassium voltage-gated channel subfamily H member 2	Homo sapiens	81-85
10742304-5	2000	The amplitudes of steady-state currents and tail currents of HERG were decreased by amitriptyline dose-dependently.	Amitriptyline	84-97	potassium voltage-gated channel subfamily H member 2	Homo sapiens	61-65
10742304-6	2000	The decrease became more pronounced at more positive potential, suggesting that the block of HERG by amitriptyline is voltage dependent.	Amitriptyline	101-114	potassium voltage-gated channel subfamily H member 2	Homo sapiens	93-97
10742304-7	2000	IC(50) for amitriptyline block of HERG current was progressively decreased according to depolarization: IC(50) values at -30, -10, +10 and +30 mV were 23.0, 8.71, 5.96 and 4.66 microM, respectively.	Amitriptyline	11-24	potassium voltage-gated channel subfamily H member 2	Homo sapiens	34-38
10742304-9	2000	Block of HERG by amitriptyline was use dependent: exhibiting a much faster block at higher activation frequency.	Amitriptyline	17-30	potassium voltage-gated channel subfamily H member 2	Homo sapiens	9-13
10742304-14	2000	78 microM in 4 mM [K(+)](o), suggesting that the affinity of amitriptyline on HERG was decreased by external K(+).	Amitriptyline	61-74	potassium voltage-gated channel subfamily H member 2	Homo sapiens	78-82
10742304-19	2000	In summary, the data suggest that the block of HERG currents may contribute to arrhythmogenic side effects of amitriptyline.	Amitriptyline	110-123	potassium voltage-gated channel subfamily H member 2	Homo sapiens	47-51
10762666-0	2000	High affinity blockade of the HERG cardiac K(+) channel by the neuroleptic pimozide.	Pimozide	75-83	potassium voltage-gated channel subfamily H member 2	Homo sapiens	30-34
10762666-3	2000	To elucidate the mechanism behind these clinical findings, we examined the effects of pimozide on the cloned human cardiac K(+) channels HERG (human ether-a-go-go-related gene; rapid component of delayed rectifier), Kv1.5 (ultra-rapid delayed rectifier) and KvLQT1/minK (slow component of delayed rectifier).	Pimozide	86-94	potassium voltage-gated channel subfamily H member 2	Homo sapiens	137-141
10762666-4	2000	Using patch clamp electrophysiology, we found that pimozide was a potent inhibitor of HERG displaying an IC(50) value of 18 nM.	Pimozide	51-59	potassium voltage-gated channel subfamily H member 2	Homo sapiens	86-90
10762666-6	2000	We conclude that pimozide is a specific, high affinity antagonist of HERG, and that this interaction leads to prolongation of cardiac repolarization.	Pimozide	17-25	potassium voltage-gated channel subfamily H member 2	Homo sapiens	69-73
10716483-8	2000	In LQT2 isoproterenol initially prolonged, then abbreviated, the APD90 of M but always abbreviated EPI, thus transiently increasing TDR and the incidence of TdP.	Isoproterenol	8-21	potassium voltage-gated channel subfamily H member 2	Homo sapiens	3-7
10735633-2	2000	The syndrome was associated with a novel KCNH2 missense mutation, G572R, causing the substitution of a glycine residue at position 572, at the end of the S5 transmembrane segment of the HERG K(+)-channel, with an arginine residue.	Glycine	103-110	potassium voltage-gated channel subfamily H member 2	Homo sapiens	41-46
10712445-0	2000	HERG-Like potassium current regulates the resting membrane potential in glomus cells of the rabbit carotid body.	Potassium	10-19	potassium voltage-gated channel subfamily H member 2	Homo sapiens	0-4
10712445-7	2000	The HERG-like current was blocked by dofetilide (DOF) in a concentration-dependent manner (IC(50) = 13 +/- 4 nM, mean +/- SE) and high concentrations of Ba(2+) (1 and 10 mM).	dofetilide	37-47	potassium voltage-gated channel subfamily H member 2	Homo sapiens	4-8
10712445-7	2000	The HERG-like current was blocked by dofetilide (DOF) in a concentration-dependent manner (IC(50) = 13 +/- 4 nM, mean +/- SE) and high concentrations of Ba(2+) (1 and 10 mM).	dofetilide	49-52	potassium voltage-gated channel subfamily H member 2	Homo sapiens	4-8
10712445-7	2000	The HERG-like current was blocked by dofetilide (DOF) in a concentration-dependent manner (IC(50) = 13 +/- 4 nM, mean +/- SE) and high concentrations of Ba(2+) (1 and 10 mM).	N-methyl-valyl-amiclenomycin	153-159	potassium voltage-gated channel subfamily H member 2	Homo sapiens	4-8
10735633-2	2000	The syndrome was associated with a novel KCNH2 missense mutation, G572R, causing the substitution of a glycine residue at position 572, at the end of the S5 transmembrane segment of the HERG K(+)-channel, with an arginine residue.	Glycine	103-110	potassium voltage-gated channel subfamily H member 2	Homo sapiens	186-190
10735633-2	2000	The syndrome was associated with a novel KCNH2 missense mutation, G572R, causing the substitution of a glycine residue at position 572, at the end of the S5 transmembrane segment of the HERG K(+)-channel, with an arginine residue.	Arginine	213-221	potassium voltage-gated channel subfamily H member 2	Homo sapiens	41-46
10735633-2	2000	The syndrome was associated with a novel KCNH2 missense mutation, G572R, causing the substitution of a glycine residue at position 572, at the end of the S5 transmembrane segment of the HERG K(+)-channel, with an arginine residue.	Arginine	213-221	potassium voltage-gated channel subfamily H member 2	Homo sapiens	186-190
10860024-3	2000	HERG is blocked by bepridil (EC50 = 0.55 microM), verapamil (EC50 = 0.83 microM) and mibefradil (EC50 = 1.43 microM), whereas nitrendipine and diltiazem have negligible effects.	Bepridil	19-27	potassium voltage-gated channel subfamily H member 2	Homo sapiens	0-4
10604956-10	2000	However, both drugs potently blocked HERG current amplitude, with a mean IC(50) of 173 nM for loratadine and 204 nM for terfenadine (pacing rate, 0.1 Hz).	Loratadine	94-104	potassium voltage-gated channel subfamily H member 2	Homo sapiens	37-41
10604956-10	2000	However, both drugs potently blocked HERG current amplitude, with a mean IC(50) of 173 nM for loratadine and 204 nM for terfenadine (pacing rate, 0.1 Hz).	Terfenadine	120-131	potassium voltage-gated channel subfamily H member 2	Homo sapiens	37-41
10860024-3	2000	HERG is blocked by bepridil (EC50 = 0.55 microM), verapamil (EC50 = 0.83 microM) and mibefradil (EC50 = 1.43 microM), whereas nitrendipine and diltiazem have negligible effects.	Verapamil	50-59	potassium voltage-gated channel subfamily H member 2	Homo sapiens	0-4
10860024-3	2000	HERG is blocked by bepridil (EC50 = 0.55 microM), verapamil (EC50 = 0.83 microM) and mibefradil (EC50 = 1.43 microM), whereas nitrendipine and diltiazem have negligible effects.	Mibefradil	85-95	potassium voltage-gated channel subfamily H member 2	Homo sapiens	0-4
10860024-3	2000	HERG is blocked by bepridil (EC50 = 0.55 microM), verapamil (EC50 = 0.83 microM) and mibefradil (EC50 = 1.43 microM), whereas nitrendipine and diltiazem have negligible effects.	Diltiazem	143-152	potassium voltage-gated channel subfamily H member 2	Homo sapiens	0-4
10545354-1	1999	We have studied the functional effects of extracellular Cd(2+) on human ether-a-go-go-related gene (HERG) encoded K(+) channels.	Cadmium	56-58	potassium voltage-gated channel subfamily H member 2	Homo sapiens	100-104
10600781-3	1999	The HERG K(+) channel blockers E-4031 (1 microM), cisapride (1 microM), and La(3+) (100 microM) strongly inhibited these currents as did millimolar concentrations of Ba(2+).	E 4031	31-37	potassium voltage-gated channel subfamily H member 2	Homo sapiens	4-8
10600781-3	1999	The HERG K(+) channel blockers E-4031 (1 microM), cisapride (1 microM), and La(3+) (100 microM) strongly inhibited these currents as did millimolar concentrations of Ba(2+).	Cisapride	50-59	potassium voltage-gated channel subfamily H member 2	Homo sapiens	4-8
10600781-3	1999	The HERG K(+) channel blockers E-4031 (1 microM), cisapride (1 microM), and La(3+) (100 microM) strongly inhibited these currents as did millimolar concentrations of Ba(2+).	lanthanum(3+)	76-82	potassium voltage-gated channel subfamily H member 2	Homo sapiens	4-8
10600781-3	1999	The HERG K(+) channel blockers E-4031 (1 microM), cisapride (1 microM), and La(3+) (100 microM) strongly inhibited these currents as did millimolar concentrations of Ba(2+).	Barium	166-168	potassium voltage-gated channel subfamily H member 2	Homo sapiens	4-8
10636190-9	1999	Finally, HERG K+ current elicited in HEK293 cells expressing high levels of HERG protein was decreased 50% by droperidol 32.2 nmol/L.	Droperidol	110-120	potassium voltage-gated channel subfamily H member 2	Homo sapiens	9-13
10636190-9	1999	Finally, HERG K+ current elicited in HEK293 cells expressing high levels of HERG protein was decreased 50% by droperidol 32.2 nmol/L.	Droperidol	110-120	potassium voltage-gated channel subfamily H member 2	Homo sapiens	76-80
10570058-0	1999	Modulation of the K(+) channels encoded by the human ether-a-gogo-related gene-1 (hERG1) by nitric oxide.	Nitric Oxide	92-104	potassium voltage-gated channel subfamily H member 2	Homo sapiens	82-87
10570058-1	1999	The inhibition of nitric oxide synthase by N-nitro-L-arginine methyl ester (0.03-3 mM) dose-dependently reduced nitric oxide (NO(*)) levels and enhanced the outward currents carried by human ether-a-gogo-related gene-1 (hERG1) K(+) channels expressed in Xenopus laevis oocytes, whereas the increase in NO(*) levels achieved by exposure to L-arginine (0.03-10 mM) inhibited these currents.	Nitric Oxide	18-30	potassium voltage-gated channel subfamily H member 2	Homo sapiens	220-225
10570058-1	1999	The inhibition of nitric oxide synthase by N-nitro-L-arginine methyl ester (0.03-3 mM) dose-dependently reduced nitric oxide (NO(*)) levels and enhanced the outward currents carried by human ether-a-gogo-related gene-1 (hERG1) K(+) channels expressed in Xenopus laevis oocytes, whereas the increase in NO(*) levels achieved by exposure to L-arginine (0.03-10 mM) inhibited these currents.	n-nitro-l-arginine methyl ester	43-74	potassium voltage-gated channel subfamily H member 2	Homo sapiens	220-225
10570058-1	1999	The inhibition of nitric oxide synthase by N-nitro-L-arginine methyl ester (0.03-3 mM) dose-dependently reduced nitric oxide (NO(*)) levels and enhanced the outward currents carried by human ether-a-gogo-related gene-1 (hERG1) K(+) channels expressed in Xenopus laevis oocytes, whereas the increase in NO(*) levels achieved by exposure to L-arginine (0.03-10 mM) inhibited these currents.	Arginine	51-61	potassium voltage-gated channel subfamily H member 2	Homo sapiens	220-225
10570058-4	1999	The inhibitory effect of NO(*) donors on hERG1 K(+) channels was prevented by the NO(*) scavengers 2-phenyl-4,4,5,5-tetramethylimidazoline-1-oxyl 3-oxide and hemoglobin.	2-phenyl-4,4,5,5-tetramethylimidazoline-1-oxyl-3-oxide	99-153	potassium voltage-gated channel subfamily H member 2	Homo sapiens	41-46
10570058-6	1999	Both L-arginine (10 mM) and NOC-18 (0.3 mM) counteracted the stimulatory effect on hERG1 outward currents induced by the radical oxygen species-generating system FeSO(4) (25 microM)/ascorbic acid (50 microM; Fe/Asc).	Arginine	5-15	potassium voltage-gated channel subfamily H member 2	Homo sapiens	83-88
10570058-6	1999	Both L-arginine (10 mM) and NOC-18 (0.3 mM) counteracted the stimulatory effect on hERG1 outward currents induced by the radical oxygen species-generating system FeSO(4) (25 microM)/ascorbic acid (50 microM; Fe/Asc).	NOC 18	28-34	potassium voltage-gated channel subfamily H member 2	Homo sapiens	83-88
10570058-6	1999	Both L-arginine (10 mM) and NOC-18 (0.3 mM) counteracted the stimulatory effect on hERG1 outward currents induced by the radical oxygen species-generating system FeSO(4) (25 microM)/ascorbic acid (50 microM; Fe/Asc).	Oxygen	129-135	potassium voltage-gated channel subfamily H member 2	Homo sapiens	83-88
10570058-6	1999	Both L-arginine (10 mM) and NOC-18 (0.3 mM) counteracted the stimulatory effect on hERG1 outward currents induced by the radical oxygen species-generating system FeSO(4) (25 microM)/ascorbic acid (50 microM; Fe/Asc).	fesoterodine	162-166	potassium voltage-gated channel subfamily H member 2	Homo sapiens	83-88
10570058-6	1999	Both L-arginine (10 mM) and NOC-18 (0.3 mM) counteracted the stimulatory effect on hERG1 outward currents induced by the radical oxygen species-generating system FeSO(4) (25 microM)/ascorbic acid (50 microM; Fe/Asc).	Ascorbic Acid	182-195	potassium voltage-gated channel subfamily H member 2	Homo sapiens	83-88
10570058-8	1999	Collectively, the present results suggest that NO(*), both endogenously produced and pharmacologically delivered, may exert in a cGMP-independent way an inhibitory effect on hERG1 outward K(+) currents via an interaction with radical oxygen species either generated under resting conditions or triggered by Fe/Asc.	Oxygen	234-240	potassium voltage-gated channel subfamily H member 2	Homo sapiens	174-179
10690305-12	1999	CONCLUSIONS: The data revealed that arginine at position 534 in the S4 region of HERG is indeed involved in voltage-dependence of channel activation as a voltage sensor.	Arginine	36-44	potassium voltage-gated channel subfamily H member 2	Homo sapiens	81-85
10388757-1	1999	The proton and Zn2+ effects on the human ether-a-go-go related gene (HERG) channels were studied after expression in Xenopus oocytes and stable transfection in the mammalian L929 cell line.	Zinc	15-19	potassium voltage-gated channel subfamily H member 2	Homo sapiens	69-73
10531299-5	1999	We further show that the antiarrhythmic drug E-4031, which selectively blocks HERG channels, also corrects defective protein trafficking of the N470D mutant and can restore the generation of HERG current.	E 4031	45-51	potassium voltage-gated channel subfamily H member 2	Homo sapiens	78-82
10531299-5	1999	We further show that the antiarrhythmic drug E-4031, which selectively blocks HERG channels, also corrects defective protein trafficking of the N470D mutant and can restore the generation of HERG current.	E 4031	45-51	potassium voltage-gated channel subfamily H member 2	Homo sapiens	191-195
10531299-7	1999	The effect of E-4031 on HERG protein trafficking was concentration-dependent and required low drug concentrations (saturation present at 5 microM), developed rapidly with drug exposure, and occurred post-translationally.	E 4031	14-20	potassium voltage-gated channel subfamily H member 2	Homo sapiens	24-28
10510456-0	1999	Inhibition of the human ether-a-go-go-related gene (HERG) potassium channel by cisapride: affinity for open and inactivated states.	Cisapride	79-88	potassium voltage-gated channel subfamily H member 2	Homo sapiens	52-56
10510456-3	1999	2 In a chronic transfection model using CHO-K1 cells, cisapride inhibited HERG tail currents after a step to +25 mV with similar potency at room and physiological temperatures (IC50 16.	Cisapride	54-63	potassium voltage-gated channel subfamily H member 2	Homo sapiens	74-78
10510456-10	1999	6 In conclusion, HERG channel inhibition by cisapride exhibits features consistent with open and inactivated state binding and is sensitive to external potassium concentration.	Cisapride	44-53	potassium voltage-gated channel subfamily H member 2	Homo sapiens	17-21
10510456-10	1999	6 In conclusion, HERG channel inhibition by cisapride exhibits features consistent with open and inactivated state binding and is sensitive to external potassium concentration.	Potassium	152-161	potassium voltage-gated channel subfamily H member 2	Homo sapiens	17-21
10413451-1	1999	The modulation of herg gene and HERG currents (I(HERG)) was studied in SH-SY5Y neuroblastoma (NB) cells treated with all-trans-retinoic acid (RA) in the absence or presence of the neurotrophin brain-derived neurotrophic factor (BDNF).	Tretinoin	142-144	potassium voltage-gated channel subfamily H member 2	Homo sapiens	18-22
10413451-3	1999	Differentiation of NB cells was accompanied by an increase in herg gene transcription, which attained its maximum after 6 days of treatment with RA and was not further increased by BDNF.	Tretinoin	145-147	potassium voltage-gated channel subfamily H member 2	Homo sapiens	62-66
10413451-4	1999	This effect evidently reflected on HERG currents: In fact, RA produced an increase in HERG current density which was strongly potentiated by BDNF.	Tretinoin	59-61	potassium voltage-gated channel subfamily H member 2	Homo sapiens	35-39
10413451-4	1999	This effect evidently reflected on HERG currents: In fact, RA produced an increase in HERG current density which was strongly potentiated by BDNF.	Tretinoin	59-61	potassium voltage-gated channel subfamily H member 2	Homo sapiens	86-90
10413451-5	1999	Moreover, RA treatment affected the biophysical properties of I(HERG), inducing an increase in the deactivation time constant and a left shift of the activation curve.	Tretinoin	10-12	potassium voltage-gated channel subfamily H member 2	Homo sapiens	64-68
10516162-6	1999	The following were ruled out as the underlying mechanisms: 1) voltage shift in channel activation, 2) pore blockade by protons, 3) protonation of histidines on the extracellular domain of HERG, 4) acceleration of recovery from C-type inactivation, and 5) interaction between an external H(+) binding site and the cytoplasmic NH(2)-terminal domain (a key determinant of HERG deactivation rate).	Histidine	146-156	potassium voltage-gated channel subfamily H member 2	Homo sapiens	188-192
10516162-7	1999	Extracellular application of diethylpyrocarbonate caused an irreversible acceleration of HERG deactivation and prevented further acceleration by external acidification.	Diethyl Pyrocarbonate	29-49	potassium voltage-gated channel subfamily H member 2	Homo sapiens	89-93
10488078-4	1999	Application of the cAMP-specific phosphodiesterase (PDE IV) inhibitor Ro-20-1724 (100 microM), which results in an increased cAMP level and PKA stimulation, induced a reduction of HERG wild type outward currents by 19.1% due to a shift in the activation curve of 12.4 mV.	Cyclic AMP	19-23	potassium voltage-gated channel subfamily H member 2	Homo sapiens	180-184
10488078-4	1999	Application of the cAMP-specific phosphodiesterase (PDE IV) inhibitor Ro-20-1724 (100 microM), which results in an increased cAMP level and PKA stimulation, induced a reduction of HERG wild type outward currents by 19.1% due to a shift in the activation curve of 12.4 mV.	4-(3-Butoxy-4-methoxybenzyl)-2-imidazolidinone	70-80	potassium voltage-gated channel subfamily H member 2	Homo sapiens	180-184
10488078-4	1999	Application of the cAMP-specific phosphodiesterase (PDE IV) inhibitor Ro-20-1724 (100 microM), which results in an increased cAMP level and PKA stimulation, induced a reduction of HERG wild type outward currents by 19.1% due to a shift in the activation curve of 12.4 mV.	Cyclic AMP	125-129	potassium voltage-gated channel subfamily H member 2	Homo sapiens	180-184
10488078-6	1999	Furthermore, the adenylate cyclase activator forskolin that leads to PKA activation (400 microM, 60 min), shifted HERG wild type channel activation by 14.1 mV and reduced currents by 39.9%, whereas HERG 4M channels showed only a small shift of 4.3 mV and a weaker current reduction of 22.3%.	Colforsin	45-54	potassium voltage-gated channel subfamily H member 2	Homo sapiens	114-118
10488078-6	1999	Furthermore, the adenylate cyclase activator forskolin that leads to PKA activation (400 microM, 60 min), shifted HERG wild type channel activation by 14.1 mV and reduced currents by 39.9%, whereas HERG 4M channels showed only a small shift of 4.3 mV and a weaker current reduction of 22.3%.	Colforsin	45-54	potassium voltage-gated channel subfamily H member 2	Homo sapiens	198-202
10484431-0	1999	Inactivation gating determines nicotine blockade of human HERG channels.	Nicotine	31-39	potassium voltage-gated channel subfamily H member 2	Homo sapiens	58-62
10484431-2	1999	To shed some light on the mechanisms of interaction between nicotine and channels, we performed detailed analysis on the human ether-a-go-go-related gene (HERG) channels, which are believed to be equivalent to the native I(Kr) when expressed in Xenopus oocytes.	Nicotine	60-68	potassium voltage-gated channel subfamily H member 2	Homo sapiens	155-159
10484431-3	1999	Nicotine suppressed the HERG channels in a concentration-dependent manner with greater potency with voltage protocols, which favor channel inactivation.	Nicotine	0-8	potassium voltage-gated channel subfamily H member 2	Homo sapiens	24-28
10484431-7	1999	Moreover, nicotine lost its ability to block the HERG channels when a single mutation was introduced to a residue located after transmembrane domain 6 (S631A) to remove the rapid channel inactivation.	Nicotine	10-18	potassium voltage-gated channel subfamily H member 2	Homo sapiens	49-53
10484431-8	1999	Our data suggest that the inactivation gating determines nicotine blockade of the HERG channels.	Nicotine	57-65	potassium voltage-gated channel subfamily H member 2	Homo sapiens	82-86
10560244-6	1999	A C-->T transition in codon 614, leading to substitution of a valine for an alanine residue in the pore region of the HERG protein, was identified.	Valine	65-71	potassium voltage-gated channel subfamily H member 2	Homo sapiens	121-125
10560244-6	1999	A C-->T transition in codon 614, leading to substitution of a valine for an alanine residue in the pore region of the HERG protein, was identified.	Alanine	79-86	potassium voltage-gated channel subfamily H member 2	Homo sapiens	121-125
10388757-11	1999	We conclude that protons and Zn2+ directly interact with HERG channels and that the interaction results, preferentially, in the regulation of channel deactivation mechanism.	Zinc	29-33	potassium voltage-gated channel subfamily H member 2	Homo sapiens	57-61
10444235-4	1999	In fact, both terfenadine and astemizole have been shown to block HERG K+ channels in a concentration range similar to that found in the plasma of subjects with cardiotoxic manifestations.	Terfenadine	14-25	potassium voltage-gated channel subfamily H member 2	Homo sapiens	66-70
10444235-4	1999	In fact, both terfenadine and astemizole have been shown to block HERG K+ channels in a concentration range similar to that found in the plasma of subjects with cardiotoxic manifestations.	Astemizole	30-40	potassium voltage-gated channel subfamily H member 2	Homo sapiens	66-70
10444235-6	1999	In fact, other molecules such as cetirizine, loratadine, acrivastine, and fexofenadine seem to lack both cardiotoxic potential and HERG-blocking ability at therapeutically relevant concentrations.	fexofenadine	74-86	potassium voltage-gated channel subfamily H member 2	Homo sapiens	131-135
10096894-1	1999	We have investigated actions of various divalent cations (Ba2+, Sr2+, Mn2+, Co2+, Ni2+, Zn2+) on human ether-a-go-go related gene (HERG) channels expressed in Xenopus laevis oocytes using the voltage clamp technique.	N-methyl-valyl-amiclenomycin	58-62	potassium voltage-gated channel subfamily H member 2	Homo sapiens	131-135
10422790-1	1999	Terfenadine and astemizole rarely cause cardiac arrhythmias by suppressing the cardiac rapid delayed rectifier K+ channel encoded by the human ether-a-go-go-related gene (HERG).	Terfenadine	0-11	potassium voltage-gated channel subfamily H member 2	Homo sapiens	171-175
10422790-1	1999	Terfenadine and astemizole rarely cause cardiac arrhythmias by suppressing the cardiac rapid delayed rectifier K+ channel encoded by the human ether-a-go-go-related gene (HERG).	Astemizole	16-26	potassium voltage-gated channel subfamily H member 2	Homo sapiens	171-175
10422790-3	1999	We have therefore compared the effects of epinastine, terfenadine and astemizole on HERG channels expressed in Xenopus oocytes.	Astemizole	70-80	potassium voltage-gated channel subfamily H member 2	Homo sapiens	84-88
10422790-4	1999	Terfenadine and astemizole suppressed the HERG current with IC50 of 431 nM and 69 nM, respectively.	Terfenadine	0-11	potassium voltage-gated channel subfamily H member 2	Homo sapiens	42-46
10422790-4	1999	Terfenadine and astemizole suppressed the HERG current with IC50 of 431 nM and 69 nM, respectively.	Astemizole	16-26	potassium voltage-gated channel subfamily H member 2	Homo sapiens	42-46
10422790-5	1999	In contrast, 100 microM epinastine inhibited the HERG current by only 11+/-2.1%.	epinastine	24-34	potassium voltage-gated channel subfamily H member 2	Homo sapiens	49-53
10325236-0	1999	Mechanism of block and identification of the verapamil binding domain to HERG potassium channels.	Verapamil	45-54	potassium voltage-gated channel subfamily H member 2	Homo sapiens	73-77
10325236-2	1999	We studied the effects of verapamil, diltiazem, and nifedipine on HERG K+ channels that encode IKr in native heart cells.	Nifedipine	52-62	potassium voltage-gated channel subfamily H member 2	Homo sapiens	66-70
10325236-3	1999	In our experiments, verapamil caused high-affinity block of HERG current (IC50=143.0 nmol/L), a value close to those reported for verapamil block of L-type Ca2+ channels, whereas diltiazem weakly blocked HERG current (IC50=17.3 micromol/L), and nifedipine did not block HERG current.	Verapamil	20-29	potassium voltage-gated channel subfamily H member 2	Homo sapiens	60-64
10325236-3	1999	In our experiments, verapamil caused high-affinity block of HERG current (IC50=143.0 nmol/L), a value close to those reported for verapamil block of L-type Ca2+ channels, whereas diltiazem weakly blocked HERG current (IC50=17.3 micromol/L), and nifedipine did not block HERG current.	Verapamil	20-29	potassium voltage-gated channel subfamily H member 2	Homo sapiens	204-208
10325236-3	1999	In our experiments, verapamil caused high-affinity block of HERG current (IC50=143.0 nmol/L), a value close to those reported for verapamil block of L-type Ca2+ channels, whereas diltiazem weakly blocked HERG current (IC50=17.3 micromol/L), and nifedipine did not block HERG current.	Verapamil	20-29	potassium voltage-gated channel subfamily H member 2	Homo sapiens	204-208
10325236-4	1999	Verapamil block of HERG channels was use and frequency dependent, and verapamil unbound from HERG channels at voltages near the normal cardiac cell resting potential or with drug washout.	Verapamil	0-9	potassium voltage-gated channel subfamily H member 2	Homo sapiens	19-23
10325236-5	1999	Block of HERG current by verapamil was reduced by lowering pHO, which decreases the proportion of drug in the membrane-permeable neutral form.	Verapamil	25-34	potassium voltage-gated channel subfamily H member 2	Homo sapiens	9-13
10325236-6	1999	N-methyl-verapamil, a membrane-impermeable, permanently charged verapamil analogue, blocked HERG channels only when applied intracellularly.	n-methyl-verapamil	0-18	potassium voltage-gated channel subfamily H member 2	Homo sapiens	92-96
10325236-6	1999	N-methyl-verapamil, a membrane-impermeable, permanently charged verapamil analogue, blocked HERG channels only when applied intracellularly.	Verapamil	9-18	potassium voltage-gated channel subfamily H member 2	Homo sapiens	92-96
10325236-7	1999	Verapamil antagonized dofetilide block of HERG channels, which suggests that they may share a common binding site.	Verapamil	0-9	potassium voltage-gated channel subfamily H member 2	Homo sapiens	42-46
10325236-7	1999	Verapamil antagonized dofetilide block of HERG channels, which suggests that they may share a common binding site.	dofetilide	22-32	potassium voltage-gated channel subfamily H member 2	Homo sapiens	42-46
10325236-10	1999	Thus, verapamil shares high-affinity HERG channel blocking properties with other class III antiarrhythmic drugs, and this may contribute to its antiarrhythmic mechanism.	Verapamil	6-15	potassium voltage-gated channel subfamily H member 2	Homo sapiens	37-41
10369479-0	1999	Inhibition of HERG channels stably expressed in a mammalian cell line by the antianginal agent perhexiline maleate.	perhexiline maleate	95-114	potassium voltage-gated channel subfamily H member 2	Homo sapiens	14-18
10369479-4	1999	Perhexiline caused voltage- and frequency-dependent block of HERG (IC50 7.8 microM).	Perhexiline	0-11	potassium voltage-gated channel subfamily H member 2	Homo sapiens	61-65
10369479-6	1999	In conclusion, perhexiline potently inhibits transfected HERG channels and this is the probable mechanism for QT prolongation and torsades de pointes.	Perhexiline	15-26	potassium voltage-gated channel subfamily H member 2	Homo sapiens	57-61
10187793-8	1999	The amino-terminal region of HERG was recently crystallized and shown to possess a Per-Arnt-Sim (PAS) domain.	Aminosalicylic Acid	97-100	potassium voltage-gated channel subfamily H member 2	Homo sapiens	29-33
10187793-9	1999	The location of these mutations suggests they may disrupt the PAS domain and interfere with its interaction with the S4-S5 linker of the HERG channel.	Aminosalicylic Acid	62-65	potassium voltage-gated channel subfamily H member 2	Homo sapiens	137-141
10376921-0	1999	Block of HERG potassium channels by the antihistamine astemizole and its metabolites desmethylastemizole and norastemizole.	Astemizole	54-64	potassium voltage-gated channel subfamily H member 2	Homo sapiens	9-13
10376921-0	1999	Block of HERG potassium channels by the antihistamine astemizole and its metabolites desmethylastemizole and norastemizole.	desmethylastemizole	85-104	potassium voltage-gated channel subfamily H member 2	Homo sapiens	9-13
10376921-0	1999	Block of HERG potassium channels by the antihistamine astemizole and its metabolites desmethylastemizole and norastemizole.	tecastemizole	109-122	potassium voltage-gated channel subfamily H member 2	Homo sapiens	9-13
10376921-2	1999	Astemizole blocks the rapidly activating delayed rectifier K+ current I(Kr) and the human ether-a go-go-related gene (HERG) K+ channels that underlie it.	Astemizole	0-10	potassium voltage-gated channel subfamily H member 2	Homo sapiens	118-122
10376921-6	1999	Our objective in the present work was to study the effects of desmethylastemizole, norastemizole, and astemizole on HERG K+ channels.	desmethylastemizole	62-81	potassium voltage-gated channel subfamily H member 2	Homo sapiens	116-120
10376921-6	1999	Our objective in the present work was to study the effects of desmethylastemizole, norastemizole, and astemizole on HERG K+ channels.	tecastemizole	83-96	potassium voltage-gated channel subfamily H member 2	Homo sapiens	116-120
10376921-6	1999	Our objective in the present work was to study the effects of desmethylastemizole, norastemizole, and astemizole on HERG K+ channels.	Astemizole	71-81	potassium voltage-gated channel subfamily H member 2	Homo sapiens	116-120
10376921-8	1999	Desmethylastemizole and astemizole blocked HERG current with similar concentration dependence (half-maximal block of 1.0 and 0.9 nM, respectively) and block was use dependent.	desmethylastemizole	0-19	potassium voltage-gated channel subfamily H member 2	Homo sapiens	43-47
10376921-8	1999	Desmethylastemizole and astemizole blocked HERG current with similar concentration dependence (half-maximal block of 1.0 and 0.9 nM, respectively) and block was use dependent.	Astemizole	9-19	potassium voltage-gated channel subfamily H member 2	Homo sapiens	43-47
10376921-9	1999	Norastemizole also blocked HERG current; however, block was incomplete and required higher drug concentrations (half-maximal block of 27.7 nM).	tecastemizole	0-13	potassium voltage-gated channel subfamily H member 2	Homo sapiens	27-31
10376921-10	1999	CONCLUSIONS: Desmethylastemizole and astemizole cause equipotent block of HERG channels, and these are among the most potent HERG channel antagonists yet studied.	desmethylastemizole	13-32	potassium voltage-gated channel subfamily H member 2	Homo sapiens	74-78
10376921-10	1999	CONCLUSIONS: Desmethylastemizole and astemizole cause equipotent block of HERG channels, and these are among the most potent HERG channel antagonists yet studied.	desmethylastemizole	13-32	potassium voltage-gated channel subfamily H member 2	Homo sapiens	125-129
10376921-10	1999	CONCLUSIONS: Desmethylastemizole and astemizole cause equipotent block of HERG channels, and these are among the most potent HERG channel antagonists yet studied.	Astemizole	22-32	potassium voltage-gated channel subfamily H member 2	Homo sapiens	74-78
10376921-10	1999	CONCLUSIONS: Desmethylastemizole and astemizole cause equipotent block of HERG channels, and these are among the most potent HERG channel antagonists yet studied.	Astemizole	22-32	potassium voltage-gated channel subfamily H member 2	Homo sapiens	125-129
10376921-12	1999	Norastemizole block of HERG channels is weaker; thus, the risk of producing ventricular arrhythmias may be lower.	tecastemizole	0-13	potassium voltage-gated channel subfamily H member 2	Homo sapiens	23-27
10096894-1	1999	We have investigated actions of various divalent cations (Ba2+, Sr2+, Mn2+, Co2+, Ni2+, Zn2+) on human ether-a-go-go related gene (HERG) channels expressed in Xenopus laevis oocytes using the voltage clamp technique.	strontium cation	64-68	potassium voltage-gated channel subfamily H member 2	Homo sapiens	131-135
10096894-1	1999	We have investigated actions of various divalent cations (Ba2+, Sr2+, Mn2+, Co2+, Ni2+, Zn2+) on human ether-a-go-go related gene (HERG) channels expressed in Xenopus laevis oocytes using the voltage clamp technique.	Manganese(2+)	70-74	potassium voltage-gated channel subfamily H member 2	Homo sapiens	131-135
10096894-1	1999	We have investigated actions of various divalent cations (Ba2+, Sr2+, Mn2+, Co2+, Ni2+, Zn2+) on human ether-a-go-go related gene (HERG) channels expressed in Xenopus laevis oocytes using the voltage clamp technique.	Cobalt(2+)	76-80	potassium voltage-gated channel subfamily H member 2	Homo sapiens	131-135
10096894-1	1999	We have investigated actions of various divalent cations (Ba2+, Sr2+, Mn2+, Co2+, Ni2+, Zn2+) on human ether-a-go-go related gene (HERG) channels expressed in Xenopus laevis oocytes using the voltage clamp technique.	Nickel(2+)	82-86	potassium voltage-gated channel subfamily H member 2	Homo sapiens	131-135
10096894-1	1999	We have investigated actions of various divalent cations (Ba2+, Sr2+, Mn2+, Co2+, Ni2+, Zn2+) on human ether-a-go-go related gene (HERG) channels expressed in Xenopus laevis oocytes using the voltage clamp technique.	Zinc	88-92	potassium voltage-gated channel subfamily H member 2	Homo sapiens	131-135
10086971-4	1999	METHODS AND RESULTS: New specific primers allowed the amplification of the 3" part of HERG, the identification of 2 missense mutations, S818L and V822 M, in the putative cyclic nucleotide binding domain, and a 1-bp insertion, 3108+1G.	Nucleotides, Cyclic	170-187	potassium voltage-gated channel subfamily H member 2	Homo sapiens	86-90
10028924-0	1999	Modulation of HERG potassium channels by extracellular magnesium and quinidine.	Magnesium	55-64	potassium voltage-gated channel subfamily H member 2	Homo sapiens	14-18
10208308-0	1999	Inhibitory effects of the class III antiarrhythmic drug amiodarone on cloned HERG potassium channels.	Amiodarone	56-66	potassium voltage-gated channel subfamily H member 2	Homo sapiens	77-81
10208308-3	1999	In this study, we investigated the acute effects of the class III antiarrhythmic drug amiodarone on HERG channels expressed heterologously in Xenopus oocytes by use of the two-microelectrode voltage clamp technique.	Amiodarone	86-96	potassium voltage-gated channel subfamily H member 2	Homo sapiens	100-104
10208308-4	1999	Amiodarone blocked HERG channels with an IC50 of 9.8 microM with a maximum outward tail current reduction of 62.8%.	Amiodarone	0-10	potassium voltage-gated channel subfamily H member 2	Homo sapiens	19-23
10208308-7	1999	These results indicate that HERG channels can be blocked by amiodarone in closed, open and inactivated states.	Amiodarone	60-70	potassium voltage-gated channel subfamily H member 2	Homo sapiens	28-32
10208308-9	1999	In summary, our data suggest that the strong class III antiarrhythmic action of amiodarone is at least partially based upon its acute inhibitory effects on HERG potassium channels.	Amiodarone	80-90	potassium voltage-gated channel subfamily H member 2	Homo sapiens	156-160
9925876-0	1999	N-linked glycosylation sites determine HERG channel surface membrane expression.	Nitrogen	0-1	potassium voltage-gated channel subfamily H member 2	Homo sapiens	39-43
9925876-4	1999	While a recent report indicates that LQT in some patients is associated with a mutation of HERG at a consensus extracellular N-linked glycosylation site (N629), earlier studies failed to identify a role for N-linked glycosylation in the functional expression of voltage-gated K+ channels.	Nitrogen	125-126	potassium voltage-gated channel subfamily H member 2	Homo sapiens	91-95
9925876-4	1999	While a recent report indicates that LQT in some patients is associated with a mutation of HERG at a consensus extracellular N-linked glycosylation site (N629), earlier studies failed to identify a role for N-linked glycosylation in the functional expression of voltage-gated K+ channels.	Nitrogen	154-155	potassium voltage-gated channel subfamily H member 2	Homo sapiens	91-95
9925876-5	1999	In this study we used pharmacological agents and site-directed mutagenesis to assess the contribution of N-linked glycosylation to the surface localization of HERG channels.	Nitrogen	105-106	potassium voltage-gated channel subfamily H member 2	Homo sapiens	159-163
9925876-7	1999	Tunicamycin, an inhibitor of N-linked glycosylation, blocked normal surface membrane expression of a HERG-green fluorescent protein (GFP) fusion protein (HERGGFP) transiently expressed in human embryonic kidney (HEK 293) cells imaged with confocal microscopy.	Tunicamycin	0-11	potassium voltage-gated channel subfamily H member 2	Homo sapiens	101-105
9925876-11	1999	Furthermore, patch clamp analysis revealed that there was a virtual absence of HERG current in the N-glycosylation mutants.	Nitrogen	99-100	potassium voltage-gated channel subfamily H member 2	Homo sapiens	79-83
9925876-13	1999	Taken together, these results strongly suggest that N-linked glycosylation is required for surface membrane expression of HERG.	Nitrogen	52-53	potassium voltage-gated channel subfamily H member 2	Homo sapiens	122-126
9925876-14	1999	These findings may provide insight into a mechanism responsible for LQT2 due to N-linked glycosylation-related mutations of HERG.	Nitrogen	80-81	potassium voltage-gated channel subfamily H member 2	Homo sapiens	68-72
9925876-14	1999	These findings may provide insight into a mechanism responsible for LQT2 due to N-linked glycosylation-related mutations of HERG.	Nitrogen	80-81	potassium voltage-gated channel subfamily H member 2	Homo sapiens	124-128
10028924-10	1999	Quinidine (3 microM) inhibited HERG currents expressed in oocytes by 32.1 +/- 3.2% (n = 5), whereas 1 microM quinidine inhibited HERG currents in tsA201 cells by 75.8 +/- 2.4% (n = 12).	Quinidine	0-9	potassium voltage-gated channel subfamily H member 2	Homo sapiens	31-35
10028924-10	1999	Quinidine (3 microM) inhibited HERG currents expressed in oocytes by 32.1 +/- 3.2% (n = 5), whereas 1 microM quinidine inhibited HERG currents in tsA201 cells by 75.8 +/- 2.4% (n = 12).	Quinidine	109-118	potassium voltage-gated channel subfamily H member 2	Homo sapiens	129-133
10028924-0	1999	Modulation of HERG potassium channels by extracellular magnesium and quinidine.	Quinidine	69-78	potassium voltage-gated channel subfamily H member 2	Homo sapiens	14-18
10028924-12	1999	These results indicate that extracellular Mg2+ exerts a direct action on HERG potassium channels, resulting in suppression of outward repolarizing potassium current.	magnesium ion	42-46	potassium voltage-gated channel subfamily H member 2	Homo sapiens	73-77
10028924-14	1999	Potent suppression of HERG channel current by quinidine, compared with that of I(Ks) and I(Na), is a likely contributor to torsades de pointes arrhythmias.	Quinidine	46-55	potassium voltage-gated channel subfamily H member 2	Homo sapiens	22-26
10028924-5	1999	This study was designed to investigate the effects of extracellular magnesium (Mg2+) on HERG potassium currents.	Magnesium	68-77	potassium voltage-gated channel subfamily H member 2	Homo sapiens	88-92
10028924-5	1999	This study was designed to investigate the effects of extracellular magnesium (Mg2+) on HERG potassium currents.	magnesium ion	79-83	potassium voltage-gated channel subfamily H member 2	Homo sapiens	88-92
10028924-5	1999	This study was designed to investigate the effects of extracellular magnesium (Mg2+) on HERG potassium currents.	Potassium	93-102	potassium voltage-gated channel subfamily H member 2	Homo sapiens	88-92
10028924-7	1999	Extracellular Mg2+ (0.3-10 mM) caused a concentration-dependent shift in the membrane-potential dependence of HERG channel opening, causing a reduction in K+ current.	magnesium ion	14-18	potassium voltage-gated channel subfamily H member 2	Homo sapiens	110-114
10688323-8	1999	Propranolol (1 micromol/L), a beta blocker, completely prevented the effect of isoproterenol to persistently or transiently increase TDR and to induce TdP in the LQT1 and LQT2 models, but facilitated TdP in the LQT3 model.	Propranolol	0-11	potassium voltage-gated channel subfamily H member 2	Homo sapiens	171-175
9882738-5	1999	Mutation of acidic residues (D540, E544) in the S4-S5 linker of HERG channels to neutral (Ala) or basic (Lys) residues accelerated the rate of channel deactivation.	Alanine	90-93	potassium voltage-gated channel subfamily H member 2	Homo sapiens	64-68
9882738-5	1999	Mutation of acidic residues (D540, E544) in the S4-S5 linker of HERG channels to neutral (Ala) or basic (Lys) residues accelerated the rate of channel deactivation.	Lysine	105-108	potassium voltage-gated channel subfamily H member 2	Homo sapiens	64-68
10090227-0	1999	Long-term (subacute) potassium treatment in congenital HERG-related long QT syndrome (LQTS2).	Potassium	21-30	potassium voltage-gated channel subfamily H member 2	Homo sapiens	55-59
10688323-8	1999	Propranolol (1 micromol/L), a beta blocker, completely prevented the effect of isoproterenol to persistently or transiently increase TDR and to induce TdP in the LQT1 and LQT2 models, but facilitated TdP in the LQT3 model.	Isoproterenol	79-92	potassium voltage-gated channel subfamily H member 2	Homo sapiens	171-175
9862440-0	1998	Sulfonylureas blockade of neural and cardiac HERG channels.	Sulfonylurea Compounds	0-13	potassium voltage-gated channel subfamily H member 2	Homo sapiens	45-49
9862440-2	1998	In this paper we show that I(HERG), recorded in neuroblastoma cells and guinea-pig ventricular myocytes, was reversibly inhibited by the K(ATP) channel blocker glibenclamide (IC50 = 74 microM).	Glyburide	160-173	potassium voltage-gated channel subfamily H member 2	Homo sapiens	29-33
9862440-4	1998	Another sulfonylurea, glimepiride, had less effective results in blocking I(HERG).	Sulfonylurea Compounds	8-20	potassium voltage-gated channel subfamily H member 2	Homo sapiens	76-80
9862440-4	1998	Another sulfonylurea, glimepiride, had less effective results in blocking I(HERG).	glimepiride	22-33	potassium voltage-gated channel subfamily H member 2	Homo sapiens	76-80
9679158-0	1998	Transfer of rapid inactivation and sensitivity to the class III antiarrhythmic drug E-4031 from HERG to M-eag channels.	E 4031	84-90	potassium voltage-gated channel subfamily H member 2	Homo sapiens	96-100
9737994-0	1998	HERG potassium channel activation is shifted by phorbol esters via protein kinase A-dependent pathways.	Phorbol Esters	48-62	potassium voltage-gated channel subfamily H member 2	Homo sapiens	0-4
9737994-11	1998	Forskolin (400 microM), an activator of the adenylate cyclase that results in PKA activation, shifted the HERG activation curve by 14 mV.	Colforsin	0-9	potassium voltage-gated channel subfamily H member 2	Homo sapiens	106-110
9845367-0	1998	Crystal structure and functional analysis of the HERG potassium channel N terminus: a eukaryotic PAS domain.	Protactinium	97-100	potassium voltage-gated channel subfamily H member 2	Homo sapiens	49-53
9765513-1	1998	We examined the effects of the calcium channel blockers nitrendipine, diltiazem, verapamil, bepridil, and mibefradil on the cloned HERG and KvLQT1/IsK K+ channels.	Nitrendipine	56-68	potassium voltage-gated channel subfamily H member 2	Homo sapiens	131-135
9765513-1	1998	We examined the effects of the calcium channel blockers nitrendipine, diltiazem, verapamil, bepridil, and mibefradil on the cloned HERG and KvLQT1/IsK K+ channels.	Diltiazem	70-79	potassium voltage-gated channel subfamily H member 2	Homo sapiens	131-135
9765513-1	1998	We examined the effects of the calcium channel blockers nitrendipine, diltiazem, verapamil, bepridil, and mibefradil on the cloned HERG and KvLQT1/IsK K+ channels.	Verapamil	81-90	potassium voltage-gated channel subfamily H member 2	Homo sapiens	131-135
9765513-1	1998	We examined the effects of the calcium channel blockers nitrendipine, diltiazem, verapamil, bepridil, and mibefradil on the cloned HERG and KvLQT1/IsK K+ channels.	Bepridil	92-100	potassium voltage-gated channel subfamily H member 2	Homo sapiens	131-135
9765513-1	1998	We examined the effects of the calcium channel blockers nitrendipine, diltiazem, verapamil, bepridil, and mibefradil on the cloned HERG and KvLQT1/IsK K+ channels.	Mibefradil	106-116	potassium voltage-gated channel subfamily H member 2	Homo sapiens	131-135
9765513-3	1998	When expressed in transfected COS cells, HERG is blocked in a concentration-dependent manner by bepridil (EC50 = 0.55 microM), verapamil (EC50 = 0.83 microM), and mibefradil (EC50 = 1.43 microM), whereas nitrendipine and diltiazem have negligible effects.	Bepridil	96-104	potassium voltage-gated channel subfamily H member 2	Homo sapiens	41-45
9765513-3	1998	When expressed in transfected COS cells, HERG is blocked in a concentration-dependent manner by bepridil (EC50 = 0.55 microM), verapamil (EC50 = 0.83 microM), and mibefradil (EC50 = 1.43 microM), whereas nitrendipine and diltiazem have negligible effects.	Verapamil	127-136	potassium voltage-gated channel subfamily H member 2	Homo sapiens	41-45
9765513-3	1998	When expressed in transfected COS cells, HERG is blocked in a concentration-dependent manner by bepridil (EC50 = 0.55 microM), verapamil (EC50 = 0.83 microM), and mibefradil (EC50 = 1.43 microM), whereas nitrendipine and diltiazem have negligible effects.	Mibefradil	163-173	potassium voltage-gated channel subfamily H member 2	Homo sapiens	41-45
9765513-3	1998	When expressed in transfected COS cells, HERG is blocked in a concentration-dependent manner by bepridil (EC50 = 0.55 microM), verapamil (EC50 = 0.83 microM), and mibefradil (EC50 = 1.43 microM), whereas nitrendipine and diltiazem have negligible effects.	Nitrendipine	204-216	potassium voltage-gated channel subfamily H member 2	Homo sapiens	41-45
9765513-3	1998	When expressed in transfected COS cells, HERG is blocked in a concentration-dependent manner by bepridil (EC50 = 0.55 microM), verapamil (EC50 = 0.83 microM), and mibefradil (EC50 = 1.43 microM), whereas nitrendipine and diltiazem have negligible effects.	Diltiazem	221-230	potassium voltage-gated channel subfamily H member 2	Homo sapiens	41-45
9679158-1	1998	The gating behaviour and pharmacological sensitivity of HERG are remarkably different from the corresponding properties of M-eag, a structurally similar member of the Eag family of potassium channels.	m-eag	123-128	potassium voltage-gated channel subfamily H member 2	Homo sapiens	56-60
9679158-5	1998	Transfer of a small segment of the HERG polypeptide to M-eag, consisting largely of the P region and part of the S6 transmembrane domain, is sufficient to confer rapid inactivation and E-4031 sensitivity to M-eag.	Methyl 2-acetamido-2-deoxy-beta-D-glucopyranoside	57-60	potassium voltage-gated channel subfamily H member 2	Homo sapiens	35-39
9714291-5	1998	In fact, interference with HERG K+ channels seems to be the main mechanism explaining both the therapeutic actions of the class III antiarrhythmics and the potential cardiotoxicity of second-generation H1 receptor antagonists such as terfenadine and astemizole, as well as of psychotropic drugs such as some antidepressants and neuroleptics.	Terfenadine	234-245	potassium voltage-gated channel subfamily H member 2	Homo sapiens	27-31
9694927-12	1998	These potential dual actions on HERG currents suggest that precautions should be taken in long-term ketoconazole treatment, particularly for patients who have decreased liver function or are on a drug regimen requiring simultaneous medications that use cytochrome-P450 for breakdown, such as terfenadine or erythromycin, or Class III antiarrhythmic drugs.	Terfenadine	292-303	potassium voltage-gated channel subfamily H member 2	Homo sapiens	32-36
9694927-12	1998	These potential dual actions on HERG currents suggest that precautions should be taken in long-term ketoconazole treatment, particularly for patients who have decreased liver function or are on a drug regimen requiring simultaneous medications that use cytochrome-P450 for breakdown, such as terfenadine or erythromycin, or Class III antiarrhythmic drugs.	Erythromycin	307-319	potassium voltage-gated channel subfamily H member 2	Homo sapiens	32-36
9694935-0	1998	The antipsychotic agent sertindole is a high affinity antagonist of the human cardiac potassium channel HERG.	sertindole	24-34	potassium voltage-gated channel subfamily H member 2	Homo sapiens	104-108
9694935-5	1998	Using patch clamp electrophysiology, we found sertindole blocked HERG currents with an IC50 value of 14.0 nM when tail currents at -40 mV were measured after a 2-sec depolarization to +20 mV.	sertindole	46-56	potassium voltage-gated channel subfamily H member 2	Homo sapiens	65-69
9694935-11	1998	It is concluded that sertindole is a high affinity antagonist of the human cardiac potassium channel HERG and that this blockade underlies the prolongation of QT interval observed with this drug.	sertindole	21-31	potassium voltage-gated channel subfamily H member 2	Homo sapiens	101-105
9694935-12	1998	Furthermore, the sertindole molecule may provide a useful starting point for the development of very high affinity ligands for HERG.	sertindole	17-27	potassium voltage-gated channel subfamily H member 2	Homo sapiens	127-131
9694927-0	1998	Blockade of HERG and Kv1.5 by ketoconazole.	Ketoconazole	30-42	potassium voltage-gated channel subfamily H member 2	Homo sapiens	12-16
9694927-3	1998	We previously showed that terfenadine blocked HERG (Human Ether-a-Gogo Related Gene), an important component of the repolarizing cardiac delayed rectifier IK with concentration needed to obtain 50% of the block (IC50) in the therapeutic range (300 nM).	Terfenadine	26-37	potassium voltage-gated channel subfamily H member 2	Homo sapiens	46-50
9694927-5	1998	Whether Kv1.5 and HERG proteins are direct targets for ketoconazole has yet to be addressed.	Ketoconazole	55-67	potassium voltage-gated channel subfamily H member 2	Homo sapiens	18-22
9694927-6	1998	We heterologously expressed HERG and Kv1.5 in Xenopus oocytes and compared their sensitivities to ketoconazole.	Ketoconazole	98-110	potassium voltage-gated channel subfamily H member 2	Homo sapiens	28-32
9694927-11	1998	We conclude that ketoconazole may potentiate the effects of terfenadine first by an indirect pharmacokinetic action to elevate plasma levels and second by a direct pharmacodynamic action on HERG currents.	Ketoconazole	17-29	potassium voltage-gated channel subfamily H member 2	Homo sapiens	190-194
9694927-11	1998	We conclude that ketoconazole may potentiate the effects of terfenadine first by an indirect pharmacokinetic action to elevate plasma levels and second by a direct pharmacodynamic action on HERG currents.	Terfenadine	60-71	potassium voltage-gated channel subfamily H member 2	Homo sapiens	190-194
9694927-12	1998	These potential dual actions on HERG currents suggest that precautions should be taken in long-term ketoconazole treatment, particularly for patients who have decreased liver function or are on a drug regimen requiring simultaneous medications that use cytochrome-P450 for breakdown, such as terfenadine or erythromycin, or Class III antiarrhythmic drugs.	Ketoconazole	100-112	potassium voltage-gated channel subfamily H member 2	Homo sapiens	32-36
9658196-0	1998	Molecular basis for the lack of HERG K+ channel block-related cardiotoxicity by the H1 receptor blocker cetirizine compared with other second-generation antihistamines.	Cetirizine	104-114	potassium voltage-gated channel subfamily H member 2	Homo sapiens	32-36
9658196-1	1998	In the current study, the potential blocking ability of K+ channels encoded by the human ether-a-go-go related gene (HERG) by the piperazine H1 receptor antagonist cetirizine has been examined and compared with that of other second-generation antihistamines (astemizole, terfenadine, and loratadine).	Cetirizine	164-174	potassium voltage-gated channel subfamily H member 2	Homo sapiens	117-121
9658196-1	1998	In the current study, the potential blocking ability of K+ channels encoded by the human ether-a-go-go related gene (HERG) by the piperazine H1 receptor antagonist cetirizine has been examined and compared with that of other second-generation antihistamines (astemizole, terfenadine, and loratadine).	Astemizole	259-269	potassium voltage-gated channel subfamily H member 2	Homo sapiens	117-121
9658196-1	1998	In the current study, the potential blocking ability of K+ channels encoded by the human ether-a-go-go related gene (HERG) by the piperazine H1 receptor antagonist cetirizine has been examined and compared with that of other second-generation antihistamines (astemizole, terfenadine, and loratadine).	Terfenadine	271-282	potassium voltage-gated channel subfamily H member 2	Homo sapiens	117-121
9658196-1	1998	In the current study, the potential blocking ability of K+ channels encoded by the human ether-a-go-go related gene (HERG) by the piperazine H1 receptor antagonist cetirizine has been examined and compared with that of other second-generation antihistamines (astemizole, terfenadine, and loratadine).	Loratadine	288-298	potassium voltage-gated channel subfamily H member 2	Homo sapiens	117-121
9658196-3	1998	On the other hand, terfenadine and astemizole effectively blocked HERG K+ channels with nanomolar affinities (the estimated IC50 values were 330 and 480 nM, respectively), whereas loratadine was approximately 300-fold less potent (IC50 approximately 100 microM).	Terfenadine	19-30	potassium voltage-gated channel subfamily H member 2	Homo sapiens	66-70
9658196-3	1998	On the other hand, terfenadine and astemizole effectively blocked HERG K+ channels with nanomolar affinities (the estimated IC50 values were 330 and 480 nM, respectively), whereas loratadine was approximately 300-fold less potent (IC50 approximately 100 microM).	Astemizole	35-45	potassium voltage-gated channel subfamily H member 2	Homo sapiens	66-70
9658196-8	1998	Furthermore, the application of cetirizine (3 microM) on the intracellular side of the membrane of HERG-transfected human embryonic kidney 293 cells did not affect IHERG, whereas the same intracellular concentration of astemizole caused a complete block.	Cetirizine	32-42	potassium voltage-gated channel subfamily H member 2	Homo sapiens	99-103
9658196-10	1998	Cetirizine in particular, which possesses more polar and smaller substituent groups attached to the tertiary amine compared with other antihistamines, lacks HERG-blocking properties, possibly explaining the absence of torsade de pointes ventricular arrhythmias associated with its therapeutical use.	Cetirizine	0-10	potassium voltage-gated channel subfamily H member 2	Homo sapiens	157-161
9714291-5	1998	In fact, interference with HERG K+ channels seems to be the main mechanism explaining both the therapeutic actions of the class III antiarrhythmics and the potential cardiotoxicity of second-generation H1 receptor antagonists such as terfenadine and astemizole, as well as of psychotropic drugs such as some antidepressants and neuroleptics.	Astemizole	250-260	potassium voltage-gated channel subfamily H member 2	Homo sapiens	27-31
9654228-1	1998	INTRODUCTION: Inherited long QT syndrome (LQTS) recently has been associated with mutations in genes coding for potassium (KVLQT1, KCNE1, and HERG) or sodium (SCN5A) ion channels involved in regulating either sodium inward or potassium outward currents of heart cells, resulting in prolongation of the repolarization period.	Potassium	112-121	potassium voltage-gated channel subfamily H member 2	Homo sapiens	142-146
9654228-1	1998	INTRODUCTION: Inherited long QT syndrome (LQTS) recently has been associated with mutations in genes coding for potassium (KVLQT1, KCNE1, and HERG) or sodium (SCN5A) ion channels involved in regulating either sodium inward or potassium outward currents of heart cells, resulting in prolongation of the repolarization period.	Sodium	209-215	potassium voltage-gated channel subfamily H member 2	Homo sapiens	142-146
9654228-1	1998	INTRODUCTION: Inherited long QT syndrome (LQTS) recently has been associated with mutations in genes coding for potassium (KVLQT1, KCNE1, and HERG) or sodium (SCN5A) ion channels involved in regulating either sodium inward or potassium outward currents of heart cells, resulting in prolongation of the repolarization period.	Potassium	226-235	potassium voltage-gated channel subfamily H member 2	Homo sapiens	142-146
9570196-3	1998	Genes responsible for LQT1, LQT2, and LQT3 have been identified as cardiac potassium channel genes (KVLQT1, HERG) and the cardiac sodium channel gene (SCN5A).	Sodium	130-136	potassium voltage-gated channel subfamily H member 2	Homo sapiens	28-32
9535729-0	1998	Long-term exposure to retinoic acid induces the expression of IRK1 channels in HERG channel-endowed neuroblastoma cells.	Tretinoin	22-35	potassium voltage-gated channel subfamily H member 2	Homo sapiens	79-83
9490815-13	1998	Down-regulation of h-eag by long-term exposure to retinoic acid was paralleled by a right shift in the activation potential of HERG-like channels.	Tretinoin	50-63	potassium voltage-gated channel subfamily H member 2	Homo sapiens	127-131
9535729-3	1998	After 10-20 days exposure to Retinoic Acid (RA), SH-SY5Y cells showed, in addition to HERG currents, a novel current characterized by inward rectification, dependence on the extracellular K+ concentration, and blockade by Cs+ and Ba2+, the main features of the IRK1 current.	Tretinoin	29-42	potassium voltage-gated channel subfamily H member 2	Homo sapiens	86-90
9535729-3	1998	After 10-20 days exposure to Retinoic Acid (RA), SH-SY5Y cells showed, in addition to HERG currents, a novel current characterized by inward rectification, dependence on the extracellular K+ concentration, and blockade by Cs+ and Ba2+, the main features of the IRK1 current.	Tretinoin	44-46	potassium voltage-gated channel subfamily H member 2	Homo sapiens	86-90
9535729-6	1998	On the whole, data here presented demonstrate that RA-induced neuronal differentiation of neuroblastoma cells is accompanied by the switch from a HERG-driven to a IRK1-driven control of Vrest, similarly to what happens in normal differentiating neurons; however, in tumor cells, this switch does not imply the abolition of HERG channel expression.	Tretinoin	51-53	potassium voltage-gated channel subfamily H member 2	Homo sapiens	146-150
9535729-6	1998	On the whole, data here presented demonstrate that RA-induced neuronal differentiation of neuroblastoma cells is accompanied by the switch from a HERG-driven to a IRK1-driven control of Vrest, similarly to what happens in normal differentiating neurons; however, in tumor cells, this switch does not imply the abolition of HERG channel expression.	Tretinoin	51-53	potassium voltage-gated channel subfamily H member 2	Homo sapiens	323-327
9508824-0	1998	Voltage-dependent blockade of HERG channels expressed in Xenopus oocytes by external Ca2+ and Mg2+.	magnesium ion	94-98	potassium voltage-gated channel subfamily H member 2	Homo sapiens	30-34
9508824-3	1998	Using a two-microelectrode voltage clamp technique, the effect of external Ca2+ and Mg2+ on the HERG current (IHERG) was investigated.	magnesium ion	84-88	potassium voltage-gated channel subfamily H member 2	Homo sapiens	96-100
9508824-18	1998	These results suggest that external Ca2+ and Mg2+ block the HERG channel in a voltage- and time-dependent manner, resulting in a voltage dependence which has been regarded as a property of the activation gate.	magnesium ion	45-49	potassium voltage-gated channel subfamily H member 2	Homo sapiens	60-64
9484850-0	1998	Blockade of HERG channels by the class III antiarrhythmic azimilide: mode of action.	azimilide	58-67	potassium voltage-gated channel subfamily H member 2	Homo sapiens	12-16
9556090-8	1998	Raising the serum potassium concentration can increase outward HERG potassium current and is effective in shortening the QTc of patients with HERG mutations.	Potassium	18-27	potassium voltage-gated channel subfamily H member 2	Homo sapiens	63-67
9556090-8	1998	Raising the serum potassium concentration can increase outward HERG potassium current and is effective in shortening the QTc of patients with HERG mutations.	Potassium	18-27	potassium voltage-gated channel subfamily H member 2	Homo sapiens	142-146
9556090-8	1998	Raising the serum potassium concentration can increase outward HERG potassium current and is effective in shortening the QTc of patients with HERG mutations.	Potassium	68-77	potassium voltage-gated channel subfamily H member 2	Homo sapiens	63-67
9484850-10	1998	Azimilide blockade of HERG channels expressed in Xenopus oocytes and I(Kr) in mouse AT-1 cells was decreased under conditions of high [K+]e, whereas block of slowly activating I(Ks) channels was not affected by changes in [K+]e. 5.	azimilide	0-9	potassium voltage-gated channel subfamily H member 2	Homo sapiens	22-26
9484850-11	1998	In summary, azimilide is a blocker of cardiac delayed rectifier channels, I(Ks) and HERG.	azimilide	12-21	potassium voltage-gated channel subfamily H member 2	Homo sapiens	84-88
9486667-0	1998	Molecular determinants of dofetilide block of HERG K+ channels.	dofetilide	26-36	potassium voltage-gated channel subfamily H member 2	Homo sapiens	46-50
9486667-2	1998	HERG/IKr channels are a prime target for the pharmacological management of arrhythmias and are selectively blocked by class III antiarrhythmic methanesulfonanilide drugs, such as dofetilide, E4031, and MK-499, at submicromolar concentrations.	N-Phenylmethanesulfonamide	143-163	potassium voltage-gated channel subfamily H member 2	Homo sapiens	0-4
9486667-2	1998	HERG/IKr channels are a prime target for the pharmacological management of arrhythmias and are selectively blocked by class III antiarrhythmic methanesulfonanilide drugs, such as dofetilide, E4031, and MK-499, at submicromolar concentrations.	dofetilide	179-189	potassium voltage-gated channel subfamily H member 2	Homo sapiens	0-4
9486667-2	1998	HERG/IKr channels are a prime target for the pharmacological management of arrhythmias and are selectively blocked by class III antiarrhythmic methanesulfonanilide drugs, such as dofetilide, E4031, and MK-499, at submicromolar concentrations.	E 4031	191-196	potassium voltage-gated channel subfamily H member 2	Homo sapiens	0-4
9486667-2	1998	HERG/IKr channels are a prime target for the pharmacological management of arrhythmias and are selectively blocked by class III antiarrhythmic methanesulfonanilide drugs, such as dofetilide, E4031, and MK-499, at submicromolar concentrations.	L 706000	202-208	potassium voltage-gated channel subfamily H member 2	Homo sapiens	0-4
9486667-5	1998	Using constructs heterologously expressed in Xenopus oocytes, we found that transplantation of the S5-S6 linker from BEAG into HERG removed high-affinity block by dofetilide.	dofetilide	163-173	potassium voltage-gated channel subfamily H member 2	Homo sapiens	127-131
9486667-7	1998	Thus, our results indicate that important determinants of dofetilide binding are localized to the pore region of HERG.	dofetilide	58-68	potassium voltage-gated channel subfamily H member 2	Homo sapiens	113-117
9486667-11	1998	Thus, the serine in position HERG 620 may participate directly in dofetilide binding; however, an intact C-type inactivation process seems to be crucial for high-affinity drug binding.	Serine	10-16	potassium voltage-gated channel subfamily H member 2	Homo sapiens	29-33
9486667-11	1998	Thus, the serine in position HERG 620 may participate directly in dofetilide binding; however, an intact C-type inactivation process seems to be crucial for high-affinity drug binding.	dofetilide	66-76	potassium voltage-gated channel subfamily H member 2	Homo sapiens	29-33
9484850-3	1998	Because HERG channels underly the conductance I(Kr), in human heart, the effects of azimilide on HERG channels expressed in Xenopus oocytes were the focus of the present study.	azimilide	84-93	potassium voltage-gated channel subfamily H member 2	Homo sapiens	97-101
9484850-5	1998	In contrast to other well characterized HERG channel blockers, azimilide blockade was reverse use-dependent, i.e., the relative block and apparent affinity of azimilide decreased with an increase in channel activation frequency.	azimilide	63-72	potassium voltage-gated channel subfamily H member 2	Homo sapiens	40-44
9484850-6	1998	Azimilide blocked HERG channels at 0.1 and 1 Hz with IC50s of 1.4 microM and 5.2 microM respectively.	azimilide	0-9	potassium voltage-gated channel subfamily H member 2	Homo sapiens	18-22
9484850-8	1998	In an envelope of tail test, HERG channel blockade increased with increasing channel activation, indicating binding of azimilide to open channels.	azimilide	119-128	potassium voltage-gated channel subfamily H member 2	Homo sapiens	29-33
9359911-9	1997	Furthermore, the inwardly rectifying current was blocked by astemizole, a potent and selective inhibitor of human ether-a-go-go -related gene (HERG) K+ channels.	Astemizole	60-70	potassium voltage-gated channel subfamily H member 2	Homo sapiens	143-147
9449325-12	1998	HERG current was blocked by low concentrations of E-4031 (IC50 7.7 nM), a value close to that reported for I(Kr) in native cardiac myocytes.	E 4031	50-56	potassium voltage-gated channel subfamily H member 2	Homo sapiens	0-4
9517465-4	1997	This current (quail I[IR] or ql[IR]), which is active at membrane potentials positive to -35 mV, was blocked by Cs+ and by class III antiarrhythmic drugs, thus resembling the K+ current encoded by the human ether-a-go-go-related gene (HERG).	Cesium	112-115	potassium voltage-gated channel subfamily H member 2	Homo sapiens	235-239
9395068-0	1997	A mechanism for the proarrhythmic effects of cisapride (Propulsid): high affinity blockade of the human cardiac potassium channel HERG.	Cisapride	45-54	potassium voltage-gated channel subfamily H member 2	Homo sapiens	130-134
9395068-0	1997	A mechanism for the proarrhythmic effects of cisapride (Propulsid): high affinity blockade of the human cardiac potassium channel HERG.	Cisapride	56-65	potassium voltage-gated channel subfamily H member 2	Homo sapiens	130-134
9395068-5	1997	Using patch clamp electrophysiology, we found that cisapride was a potent inhibitor of HERG displaying an IC50 value of 44.5 nmol/l when tail currents at -40 mV were measured following a 2 s test depolarization to +20 mV.	Cisapride	51-60	potassium voltage-gated channel subfamily H member 2	Homo sapiens	87-91
9395068-6	1997	When HERG currents were measured at the end of prolonged (20 s) depolarizing steps to +20 mV, the apparent affinity of cisapride was increased and measured 6.70 nmol/l.	Cisapride	119-128	potassium voltage-gated channel subfamily H member 2	Homo sapiens	5-9
9395068-7	1997	The main effect of cisapride was to enhance the rate of HERG current decay thereby reducing current at the end of the voltage clamp pulse.	Cisapride	19-28	potassium voltage-gated channel subfamily H member 2	Homo sapiens	56-60
9395068-8	1997	Furthermore, the potency of cisapride for the HERG channel was similar to that observed for the class III antiarrhythmic agent dofetilide (IC50 = 15.3 nmol/l) and the nonsedating antihistamine terfenadine (IC50 = 56.0 nmol/l).	Cisapride	28-37	potassium voltage-gated channel subfamily H member 2	Homo sapiens	46-50
9395068-10	1997	It is concluded that cisapride displays specific, high affinity block of the human cardiac K+ channel HERG.	Cisapride	21-30	potassium voltage-gated channel subfamily H member 2	Homo sapiens	102-106
9351462-7	1997	The Merg1 isoforms, like HERG, produce inwardly rectifying E-4031-sensitive currents when heterologously expressed in Xenopus oocytes.	E 4031	59-65	potassium voltage-gated channel subfamily H member 2	Homo sapiens	25-29
9374794-0	1997	Blockage of the HERG human cardiac K+ channel by the gastrointestinal prokinetic agent cisapride.	Cisapride	87-96	potassium voltage-gated channel subfamily H member 2	Homo sapiens	16-20
9374794-3	1997	The human ether-a-go-go-related gene (HERG), which encodes the rapidly activating delayed rectifier K+ current and is important in cardiac repolarization, may serve as a target for the action of cisapride.	Cisapride	195-204	potassium voltage-gated channel subfamily H member 2	Homo sapiens	38-42
9374794-4	1997	We tested the hypothesis that cisapride blocks HERG.	Cisapride	30-39	potassium voltage-gated channel subfamily H member 2	Homo sapiens	47-51
9374794-6	1997	Under voltage-clamp conditions, cisapride block of HERG is dose dependent with a half-maximal inhibitory concentration of 6.5 nM at 22 degrees C (n = 25 cells).	Cisapride	32-41	potassium voltage-gated channel subfamily H member 2	Homo sapiens	51-55
9374794-9	1997	Block of HERG with cisapride after channel activation was voltage dependent.	Cisapride	19-28	potassium voltage-gated channel subfamily H member 2	Homo sapiens	9-13
9374794-10	1997	At -20 mV, 10 nM cisapride reduced HERG tail-current amplitude by 5%, whereas, at + 20 mV, the tail-current amplitude was reduced by 45% (n = 4 cells).	Cisapride	17-26	potassium voltage-gated channel subfamily H member 2	Homo sapiens	35-39
9374794-12	1997	We conclude that cisapride is a potent blocker of HERG channels expressed in HEK293 cells.	Cisapride	17-26	potassium voltage-gated channel subfamily H member 2	Homo sapiens	50-54
9326673-0	1997	Regulation of the human ether-a-gogo related gene (HERG) K+ channels by reactive oxygen species.	Reactive Oxygen Species	72-95	potassium voltage-gated channel subfamily H member 2	Homo sapiens	51-55
9395171-1	1997	INTRODUCTION: Recent clinical studies have reported a greater effectiveness of sodium channel block with mexiletine to abbreviate the QT interval in patients with the chromosome 3 variant (SCN5A, LQT3) of the long QT syndrome (LQTS) than those with the chromosome 7 form of the disease (HERG, LQT2), suggesting the possibility of gene-specific therapy for the two distinct forms of the congenital LQTS.	Mexiletine	105-115	potassium voltage-gated channel subfamily H member 2	Homo sapiens	287-291
9395171-1	1997	INTRODUCTION: Recent clinical studies have reported a greater effectiveness of sodium channel block with mexiletine to abbreviate the QT interval in patients with the chromosome 3 variant (SCN5A, LQT3) of the long QT syndrome (LQTS) than those with the chromosome 7 form of the disease (HERG, LQT2), suggesting the possibility of gene-specific therapy for the two distinct forms of the congenital LQTS.	Mexiletine	105-115	potassium voltage-gated channel subfamily H member 2	Homo sapiens	293-297
9395171-14	1997	The data provide further support for the hypothesis that block of the late sodium current may be of value in the treatment of LQT2 as well as LQT3 and perhaps other congenital and acquired (drug-induced) forms of LQTS.	Sodium	75-81	potassium voltage-gated channel subfamily H member 2	Homo sapiens	126-130
9326673-2	1997	For this reason, the possible modulation by reactive oxygen species (ROS) of HERG and other cloned K+ channels expressed in Xenopus oocytes has been explored in the present study.	Reactive Oxygen Species	44-67	potassium voltage-gated channel subfamily H member 2	Homo sapiens	77-81
9326673-2	1997	For this reason, the possible modulation by reactive oxygen species (ROS) of HERG and other cloned K+ channels expressed in Xenopus oocytes has been explored in the present study.	Reactive Oxygen Species	69-72	potassium voltage-gated channel subfamily H member 2	Homo sapiens	77-81
9326673-5	1997	This ROS-induced increase in HERG outward K+ currents was due to a depolarizing shift of the voltage-dependence of channel inactivation, with no change in channel activation.	Reactive Oxygen Species	5-8	potassium voltage-gated channel subfamily H member 2	Homo sapiens	29-33
9326673-7	1997	Fe/Asc-induced stimulation of HERG outward currents was completely prevented by perfusion of the oocytes with a ROS scavenger mixture (containing 1,000 units/ml catalase, 200 ng/ml superoxide dismutase, and 2 mM mannitol).	Reactive Oxygen Species	112-115	potassium voltage-gated channel subfamily H member 2	Homo sapiens	30-34
9326673-7	1997	Fe/Asc-induced stimulation of HERG outward currents was completely prevented by perfusion of the oocytes with a ROS scavenger mixture (containing 1,000 units/ml catalase, 200 ng/ml superoxide dismutase, and 2 mM mannitol).	Mannitol	212-220	potassium voltage-gated channel subfamily H member 2	Homo sapiens	30-34
9326673-9	1997	In conclusion, the present results seem to suggest that changes in ROS production can specifically influence K+ currents carried by the HERG channels.	Reactive Oxygen Species	67-70	potassium voltage-gated channel subfamily H member 2	Homo sapiens	136-140
9272507-11	1997	Conversely, LQT2 patients are at higher risk to develop syncope under stressful conditions, because of the combined arrhythmogenic effect of catecholamines with the insufficient adaptation of their QT interval.	Catecholamines	141-155	potassium voltage-gated channel subfamily H member 2	Homo sapiens	12-16
9315735-0	1997	Specific block of cloned Herg channels by clofilium and its tertiary analog LY97241.	clofilium	42-51	potassium voltage-gated channel subfamily H member 2	Homo sapiens	25-29
9315735-0	1997	Specific block of cloned Herg channels by clofilium and its tertiary analog LY97241.	LY 97241	76-83	potassium voltage-gated channel subfamily H member 2	Homo sapiens	25-29
9315735-2	1997	In the present study we investigated the potency of clofilium and its tertiary analog LY97241 to inhibit K+ channels, encoded by the human ether-a-go-go related gene (HERG).	clofilium	52-61	potassium voltage-gated channel subfamily H member 2	Homo sapiens	167-171
9315735-2	1997	In the present study we investigated the potency of clofilium and its tertiary analog LY97241 to inhibit K+ channels, encoded by the human ether-a-go-go related gene (HERG).	LY 97241	86-93	potassium voltage-gated channel subfamily H member 2	Homo sapiens	167-171
9315735-3	1997	Clofilium blocked HERG channels in a voltage-dependent fashion with an IC50 of 250 nM and 150 nM at 0 and +40 mV, respectively.	clofilium	0-9	potassium voltage-gated channel subfamily H member 2	Homo sapiens	18-22
9315735-6	1997	Block of HERG channels by LY97241 was voltage dependent and the rate of HERG inactivation was increased by LY97241.	LY 97241	26-33	potassium voltage-gated channel subfamily H member 2	Homo sapiens	9-13
9315735-6	1997	Block of HERG channels by LY97241 was voltage dependent and the rate of HERG inactivation was increased by LY97241.	LY 97241	26-33	potassium voltage-gated channel subfamily H member 2	Homo sapiens	72-76
9315735-6	1997	Block of HERG channels by LY97241 was voltage dependent and the rate of HERG inactivation was increased by LY97241.	LY 97241	107-114	potassium voltage-gated channel subfamily H member 2	Homo sapiens	9-13
9315735-6	1997	Block of HERG channels by LY97241 was voltage dependent and the rate of HERG inactivation was increased by LY97241.	LY 97241	107-114	potassium voltage-gated channel subfamily H member 2	Homo sapiens	72-76
9315735-8	1997	The HERG S631A and S620T mutant channels which have a strongly reduced degree of inactivation were 7-fold and 33-fold less sensitive to LY97241 blockade, indicating that LY97241 binding is affected by HERG channel inactivation.	LY 97241	136-143	potassium voltage-gated channel subfamily H member 2	Homo sapiens	4-8
9315735-8	1997	The HERG S631A and S620T mutant channels which have a strongly reduced degree of inactivation were 7-fold and 33-fold less sensitive to LY97241 blockade, indicating that LY97241 binding is affected by HERG channel inactivation.	LY 97241	170-177	potassium voltage-gated channel subfamily H member 2	Homo sapiens	4-8
9315735-8	1997	The HERG S631A and S620T mutant channels which have a strongly reduced degree of inactivation were 7-fold and 33-fold less sensitive to LY97241 blockade, indicating that LY97241 binding is affected by HERG channel inactivation.	LY 97241	170-177	potassium voltage-gated channel subfamily H member 2	Homo sapiens	201-205
9315735-9	1997	In summary, the antiarrhythmic action of clofilium and its analog LY97241 appears to be caused by their potent, but distinct ability for blocking HERG channels.	clofilium	41-50	potassium voltage-gated channel subfamily H member 2	Homo sapiens	146-150
9315735-9	1997	In summary, the antiarrhythmic action of clofilium and its analog LY97241 appears to be caused by their potent, but distinct ability for blocking HERG channels.	LY 97241	66-73	potassium voltage-gated channel subfamily H member 2	Homo sapiens	146-150
9272507-12	1997	Along the same line of development of gene-specific therapy, recent data demonstrated that an increase in the extracellular concentration of potassium shortens the QT interval in LQT2 patients suggesting that intervention aimed at increasing potassium plasma levels may represent a specific treatment for LQT2.	Potassium	141-150	potassium voltage-gated channel subfamily H member 2	Homo sapiens	179-183
9272507-12	1997	Along the same line of development of gene-specific therapy, recent data demonstrated that an increase in the extracellular concentration of potassium shortens the QT interval in LQT2 patients suggesting that intervention aimed at increasing potassium plasma levels may represent a specific treatment for LQT2.	Potassium	141-150	potassium voltage-gated channel subfamily H member 2	Homo sapiens	305-309
9272507-12	1997	Along the same line of development of gene-specific therapy, recent data demonstrated that an increase in the extracellular concentration of potassium shortens the QT interval in LQT2 patients suggesting that intervention aimed at increasing potassium plasma levels may represent a specific treatment for LQT2.	Potassium	242-251	potassium voltage-gated channel subfamily H member 2	Homo sapiens	179-183
9272507-12	1997	Along the same line of development of gene-specific therapy, recent data demonstrated that an increase in the extracellular concentration of potassium shortens the QT interval in LQT2 patients suggesting that intervention aimed at increasing potassium plasma levels may represent a specific treatment for LQT2.	Potassium	242-251	potassium voltage-gated channel subfamily H member 2	Homo sapiens	305-309
9230439-0	1997	A minK-HERG complex regulates the cardiac potassium current I(Kr).	Potassium	42-51	potassium voltage-gated channel subfamily H member 2	Homo sapiens	7-11
9138706-0	1997	The inhibitory effect of the antipsychotic drug haloperidol on HERG potassium channels expressed in Xenopus oocytes.	Haloperidol	48-59	potassium voltage-gated channel subfamily H member 2	Homo sapiens	63-67
9297927-4	1997	Both LQT1 and LQT2 relate with inward rectifying potassium currents and is repolarization related, therefore, it is speculate that patients of LQT1 and LQT2 may have an abnormal T-U-wave on their surface ECG.	Potassium	49-58	potassium voltage-gated channel subfamily H member 2	Homo sapiens	14-18
9297927-4	1997	Both LQT1 and LQT2 relate with inward rectifying potassium currents and is repolarization related, therefore, it is speculate that patients of LQT1 and LQT2 may have an abnormal T-U-wave on their surface ECG.	Potassium	49-58	potassium voltage-gated channel subfamily H member 2	Homo sapiens	152-156
9138706-3	1997	In this study, we expressed several cloned cardiac K+ channels, including the human ether-a-go-go related gene (HERG) channels, in Xenopus oocytes and tested them for their haloperidol sensitivity.	Haloperidol	173-184	potassium voltage-gated channel subfamily H member 2	Homo sapiens	112-116
9138706-7	1997	In contrast, haloperidol blocked HERG channels potently with an IC50 value of approximately 1 microM.	Haloperidol	13-24	potassium voltage-gated channel subfamily H member 2	Homo sapiens	33-37
9138706-10	1997	Haloperidol block was use- and voltage-dependent, suggesting that it binds preferentially to either open or inactivated HERG channels.	Haloperidol	0-11	potassium voltage-gated channel subfamily H member 2	Homo sapiens	120-124
9138706-11	1997	As haloperidol increased the degree and rate of HERG inactivation, binding to inactivated HERG channels is suggested.	Haloperidol	3-14	potassium voltage-gated channel subfamily H member 2	Homo sapiens	48-52
9138706-11	1997	As haloperidol increased the degree and rate of HERG inactivation, binding to inactivated HERG channels is suggested.	Haloperidol	3-14	potassium voltage-gated channel subfamily H member 2	Homo sapiens	90-94
9138706-14	1997	Haloperidol block of HERG S631A at 0 mV was four fold weaker than for HERG wild-type channels.	Haloperidol	0-11	potassium voltage-gated channel subfamily H member 2	Homo sapiens	21-25
9138706-15	1997	Haloperidol affinity for HERG S631A was increased four fold at +40 mV compared to 0 mV.	Haloperidol	0-11	potassium voltage-gated channel subfamily H member 2	Homo sapiens	25-29
9138706-17	1997	In summary, the data suggest that HERG channel blockade is involved in the arrhythmogenic side effects of haloperidol.	Haloperidol	106-117	potassium voltage-gated channel subfamily H member 2	Homo sapiens	34-38
9138706-18	1997	The mechanism of haloperidol block involves binding to inactivated HERG channels.	Haloperidol	17-28	potassium voltage-gated channel subfamily H member 2	Homo sapiens	67-71
8995352-5	1997	Truncated HERG proteins containing NAB(HERG), including one that resulted from the delta1261 human mutation, inhibit the functional expression of the HERG channel in transfected cells.	nab	35-38	potassium voltage-gated channel subfamily H member 2	Homo sapiens	10-14
9087606-7	1997	Single HERG channels were blocked by MK-499, a class III antiarrhythmic agent that blocks I(Kr) in cardiac myocytes.	L 706000	37-43	potassium voltage-gated channel subfamily H member 2	Homo sapiens	7-11
8995352-5	1997	Truncated HERG proteins containing NAB(HERG), including one that resulted from the delta1261 human mutation, inhibit the functional expression of the HERG channel in transfected cells.	nab	35-38	potassium voltage-gated channel subfamily H member 2	Homo sapiens	39-43
8995352-5	1997	Truncated HERG proteins containing NAB(HERG), including one that resulted from the delta1261 human mutation, inhibit the functional expression of the HERG channel in transfected cells.	nab	35-38	potassium voltage-gated channel subfamily H member 2	Homo sapiens	39-43
8873679-8	1996	The SCN5A mutations result in defective sodium channel inactivation, whereas HERG mutations result in decreased outward potassium current.	Potassium	120-129	potassium voltage-gated channel subfamily H member 2	Homo sapiens	77-81
8921803-10	1996	In excised macro patches, HERG currents were blocked by the class III antiarrhythmic drug dofetilide, with an IC50 of 35 nmol/L.	dofetilide	90-100	potassium voltage-gated channel subfamily H member 2	Homo sapiens	26-30
8921803-11	1996	Dofetilide block was slow and greatly attenuated at positive potentials at which HERG rectifies.	dofetilide	0-10	potassium voltage-gated channel subfamily H member 2	Homo sapiens	81-85
9117354-3	1996	IIR was blocked by Cs+ ions and by the antiarrhythmic drug E-4031, a specific inhibitor of the HERG-codified channels.	E 4031	59-65	potassium voltage-gated channel subfamily H member 2	Homo sapiens	95-99
8641472-0	1996	Blockade of HERG channels expressed in Xenopus oocytes by the histamine receptor antagonists terfenadine and astemizole.	Terfenadine	93-104	potassium voltage-gated channel subfamily H member 2	Homo sapiens	12-16
8952843-5	1996	We developed a cellular model in which ventricular myocytes were exposed to anthopleurin and dofetilide in order to mimic LQT3 and LQT2, respectively.	anthopleurin	76-88	potassium voltage-gated channel subfamily H member 2	Homo sapiens	131-135
8952843-5	1996	We developed a cellular model in which ventricular myocytes were exposed to anthopleurin and dofetilide in order to mimic LQT3 and LQT2, respectively.	dofetilide	93-103	potassium voltage-gated channel subfamily H member 2	Homo sapiens	131-135
8952843-11	1996	Conversely, LQT2 patients are at higher risk to develop syncope under stressful conditions, because of the combined arrhythmogenic effect of cathecolamines with the insufficient adaptation of their QT interval when heart rate increases.	cathecolamines	141-155	potassium voltage-gated channel subfamily H member 2	Homo sapiens	12-16
8790040-2	1996	BACKGROUND: Many members of families with inherited long-QT (LQT) syndrome have mutations in HERG, a gene encoding a cardiac potassium channel that is modulated by extracellular potassium.	Potassium	125-134	potassium voltage-gated channel subfamily H member 2	Homo sapiens	93-97
8799887-12	1996	Activity of HERG channels depended on extracellular cations, which are effective for channel activation, in the order Cs+ > K+ > > Li+ > Na+.	Cesium	118-120	potassium voltage-gated channel subfamily H member 2	Homo sapiens	12-16
8649354-0	1996	High affinity open channel block by dofetilide of HERG expressed in a human cell line.	dofetilide	36-46	potassium voltage-gated channel subfamily H member 2	Homo sapiens	50-54
8635257-4	1996	A single nucleotide substitution of thymidine to guanine (T1961G) changed the coding sense of HERG from isoleucine to arginine (Ile593Arg) in the channel pore region.	Thymidine	36-45	potassium voltage-gated channel subfamily H member 2	Homo sapiens	94-98
8635257-4	1996	A single nucleotide substitution of thymidine to guanine (T1961G) changed the coding sense of HERG from isoleucine to arginine (Ile593Arg) in the channel pore region.	Guanine	49-56	potassium voltage-gated channel subfamily H member 2	Homo sapiens	94-98
8914737-0	1996	Novel missense mutation in the cyclic nucleotide-binding domain of HERG causes long QT syndrome.	Nucleotides, Cyclic	31-48	potassium voltage-gated channel subfamily H member 2	Homo sapiens	67-71
8914737-11	1996	Furthermore, the location and character of this mutation suggests that the cyclic nucleotide-binding domain of the potassium channel encoded by HERG plays an important role in normal cardiac repolarization and may decrease susceptibility to ventricular tachyarrhythmias.	Nucleotides, Cyclic	75-92	potassium voltage-gated channel subfamily H member 2	Homo sapiens	144-148
8772706-0	1996	HERG, a primary human ventricular target of the nonsedating antihistamine terfenadine.	antihistamine terfenadine	60-85	potassium voltage-gated channel subfamily H member 2	Homo sapiens	0-4
8772706-5	1996	We found that HERG was 10 times more sensitive than Kv1.5 to terfenadine block.	Terfenadine	61-72	potassium voltage-gated channel subfamily H member 2	Homo sapiens	14-18
8772706-8	1996	The Kd value for HERG block is relevant to the toxicity of the antihistamine, since the clinical terfenadine concentrations in human plasma may reach the 100 nmol/L range.	Terfenadine	97-108	potassium voltage-gated channel subfamily H member 2	Homo sapiens	17-21
8772706-10	1996	We propose that the blocking of HERG by terfenadine explains the acquired long QT syndrome.	Terfenadine	40-51	potassium voltage-gated channel subfamily H member 2	Homo sapiens	32-36
8877771-4	1996	By SSCP analysis and direct sequencing, we determined a new missense mutation in the HERG coding sequence, a G to A transition at position 1681 resulting in the substitution of threonine for a highly conserved alanine at codon 561.	Threonine	177-186	potassium voltage-gated channel subfamily H member 2	Homo sapiens	85-89
8877771-4	1996	By SSCP analysis and direct sequencing, we determined a new missense mutation in the HERG coding sequence, a G to A transition at position 1681 resulting in the substitution of threonine for a highly conserved alanine at codon 561.	Alanine	210-217	potassium voltage-gated channel subfamily H member 2	Homo sapiens	85-89
8766823-3	1996	We measured the instantaneous current to voltage relationship for h-erg channels using the saponin permeabilized variation of the cut-open oocyte clamp technique.	Saponins	91-98	potassium voltage-gated channel subfamily H member 2	Homo sapiens	66-71
8635257-4	1996	A single nucleotide substitution of thymidine to guanine (T1961G) changed the coding sense of HERG from isoleucine to arginine (Ile593Arg) in the channel pore region.	Isoleucine	104-114	potassium voltage-gated channel subfamily H member 2	Homo sapiens	94-98
8635257-4	1996	A single nucleotide substitution of thymidine to guanine (T1961G) changed the coding sense of HERG from isoleucine to arginine (Ile593Arg) in the channel pore region.	Arginine	118-126	potassium voltage-gated channel subfamily H member 2	Homo sapiens	94-98
8635257-4	1996	A single nucleotide substitution of thymidine to guanine (T1961G) changed the coding sense of HERG from isoleucine to arginine (Ile593Arg) in the channel pore region.	ile593arg	128-137	potassium voltage-gated channel subfamily H member 2	Homo sapiens	94-98
8635257-6	1996	CONCLUSIONS: We conclude that the Ile593Arg missense mutation in HERG is the cause of LQT in this family because it segregates with disease, its presence was confirmed in three ways, and it is not found in normal individuals.	ile593arg	34-43	potassium voltage-gated channel subfamily H member 2	Homo sapiens	65-69
8635257-7	1996	The Ile593Arg mutation may result in a change in potassium selectivity and permeability leading to a loss of HERG function, thereby resulting in LQT.	Potassium	49-58	potassium voltage-gated channel subfamily H member 2	Homo sapiens	109-113
8641472-0	1996	Blockade of HERG channels expressed in Xenopus oocytes by the histamine receptor antagonists terfenadine and astemizole.	Astemizole	109-119	potassium voltage-gated channel subfamily H member 2	Homo sapiens	12-16
8641472-2	1996	Here, terfenadine and astemizole both inhibited the human ether-a-go-go related gene (HERG) encoded channels expressed in Xenopus oocytes at nanomolar concentrations in a use- and voltage-dependent fashion.	Terfenadine	6-17	potassium voltage-gated channel subfamily H member 2	Homo sapiens	86-90
8641472-2	1996	Here, terfenadine and astemizole both inhibited the human ether-a-go-go related gene (HERG) encoded channels expressed in Xenopus oocytes at nanomolar concentrations in a use- and voltage-dependent fashion.	Astemizole	22-32	potassium voltage-gated channel subfamily H member 2	Homo sapiens	86-90
8641472-4	1996	These results suggest that blockade of HERG channels by terfenadine and astemizole might contribute to the cardiac side effects of these compounds.	Terfenadine	56-67	potassium voltage-gated channel subfamily H member 2	Homo sapiens	39-43
8641472-4	1996	These results suggest that blockade of HERG channels by terfenadine and astemizole might contribute to the cardiac side effects of these compounds.	Astemizole	72-82	potassium voltage-gated channel subfamily H member 2	Homo sapiens	39-43
8593709-8	1996	However, MK-499 did block HERG current if oocytes were repetitively pulsed, or clamped at a voltage positive to the threshold potential for channel activation.	L 706000	9-15	potassium voltage-gated channel subfamily H member 2	Homo sapiens	26-30
8593709-11	1996	Under steady state conditions, block of HERG by MK-499 was half maximal at 123 +/- 12 nmol/L at a test potential of -20 mV.	L 706000	48-54	potassium voltage-gated channel subfamily H member 2	Homo sapiens	40-44
34592322-3	2021	Previously we reported BZT and DMP as high-affinity human ether-a-go-go related gene (HERG) channel inhibitors with unknown proarrhythmic risk.	Benzethonium	23-26	potassium voltage-gated channel subfamily H member 2	Homo sapiens	86-90
7604285-2	1995	The properties of HERG channels are consistent with the gating properties of Eag-related and other outwardly rectifying, S4-containing potassium channels, but with the addition of an inactivation mechanism that attenuates potassium efflux during depolarization.	Potassium	135-144	potassium voltage-gated channel subfamily H member 2	Homo sapiens	18-22
24356123-8	2013	HERG channel phosphorylation was assayed by [(32)P]orthophosphate methods.	[(32)p]orthophosphate	44-65	potassium voltage-gated channel subfamily H member 2	Homo sapiens	0-4
24356123-11	2013	Antioxidants vitamin E and MnTBAP both abolished the depressive effects of PKA or PKC activators on HERG function.	Vitamin E	13-22	potassium voltage-gated channel subfamily H member 2	Homo sapiens	100-104
24356123-13	2013	CONCLUSIONS: HERG function is insensitive to PKA or PKC phosphorylation modulation per se, but can be impaired by the activators of PKA or PKC with long exposure likely via generation of ROS.	Reactive Oxygen Species	187-190	potassium voltage-gated channel subfamily H member 2	Homo sapiens	13-17
24356123-14	2013	In view of the critical role of HERG K(+) channel in regulating cardiac repolarization and the sustained activation of both PKA and PKC in many pathological conditions of the heart such as heart failure, it is conceivable that HERG impairment by ROS accumulation induced by PKA and PKC contributes to the impaired cardiac repolarization.	Reactive Oxygen Species	246-249	potassium voltage-gated channel subfamily H member 2	Homo sapiens	32-36
24356123-14	2013	In view of the critical role of HERG K(+) channel in regulating cardiac repolarization and the sustained activation of both PKA and PKC in many pathological conditions of the heart such as heart failure, it is conceivable that HERG impairment by ROS accumulation induced by PKA and PKC contributes to the impaired cardiac repolarization.	Reactive Oxygen Species	246-249	potassium voltage-gated channel subfamily H member 2	Homo sapiens	227-231
34767653-1	2022	BACKGROUND: The T. indotineae population shows a high amount of terbinafine resistant isolates based on different point mutations of squalene epoxidase erg1 (ergosterol) gene.	Terbinafine	64-75	potassium voltage-gated channel subfamily H member 2	Homo sapiens	152-156
34727194-3	2021	This study was undertaken to investigate the ability of phenanthrene to interact with hERG (human Ether-a-go-go-Related Gene) encoded Kv11.1 K+ channels, which play a central role in human ventricular repolarization.	phenanthrene	56-68	potassium voltage-gated channel subfamily H member 2	Homo sapiens	134-140
8521555-4	1995	We tested the hypothesis that the QT interval would shorten more in LQT3 than in LQT2 patients in response to mexiletine and also in response to increases in heart rate.	Mexiletine	110-120	potassium voltage-gated channel subfamily H member 2	Homo sapiens	81-85
8521555-12	1995	Conversely, LQT2 patients may be at higher risk to develop syncope under stressful conditions because of the combined arrhythmogenic effect of catecholamines with the insufficient adaptation of their QT interval when heart rate increases.	Catecholamines	143-157	potassium voltage-gated channel subfamily H member 2	Homo sapiens	12-16
34907251-14	2021	Of note, dexmedetomidine might be antiarrhythmic in acquired LQT2 by reducing SDR.	Dexmedetomidine	9-24	potassium voltage-gated channel subfamily H member 2	Homo sapiens	61-65
34592322-3	2021	Previously we reported BZT and DMP as high-affinity human ether-a-go-go related gene (HERG) channel inhibitors with unknown proarrhythmic risk.	domiphen	31-34	potassium voltage-gated channel subfamily H member 2	Homo sapiens	86-90
34427958-8	2021	Sodium channel blockers significantly shortened QTc both in LQT3 and LQT2 patients, while the QTc shortening effect in LQT3 was superior to that in LQT2 (57.39 ms vs. 36.61 ms).	Sodium	0-6	potassium voltage-gated channel subfamily H member 2	Homo sapiens	69-73
34427958-10	2021	CONCLUSIONS: sodium channel blockers can be useful both in LQT3 and LQT2 patients.	Sodium	13-19	potassium voltage-gated channel subfamily H member 2	Homo sapiens	68-72
35455047-0	2022	KCNH2 p.Gly262AlafsTer98: A New Threatening Variant Associated with Long QT Syndrome in a Spanish Cohort.	gly262alafster98	8-24	potassium voltage-gated channel subfamily H member 2	Homo sapiens	0-5
34383081-4	2022	The observed spontaneous inhibition of outward currents persisted in the presence of 4-aminopyridine, tetraethylammonium chloride or E-4031, the selective class III antiarrhythmic agent that blocks HERG channels.	4-Aminopyridine	85-100	potassium voltage-gated channel subfamily H member 2	Homo sapiens	198-202
34383081-4	2022	The observed spontaneous inhibition of outward currents persisted in the presence of 4-aminopyridine, tetraethylammonium chloride or E-4031, the selective class III antiarrhythmic agent that blocks HERG channels.	Tetraethylammonium	102-129	potassium voltage-gated channel subfamily H member 2	Homo sapiens	198-202
34383081-4	2022	The observed spontaneous inhibition of outward currents persisted in the presence of 4-aminopyridine, tetraethylammonium chloride or E-4031, the selective class III antiarrhythmic agent that blocks HERG channels.	E 4031	133-139	potassium voltage-gated channel subfamily H member 2	Homo sapiens	198-202
34901807-1	2021	A novel frameshift mutation in the KCNH2 gene for long QT syndrome type 2 (LQTS2) was identified after torsades des pointes ventricular tachycardia in a 49-year-old patient managed with octreotide and nadolol for an acute variceal bleed.	Octreotide	186-196	potassium voltage-gated channel subfamily H member 2	Homo sapiens	35-40
34901807-1	2021	A novel frameshift mutation in the KCNH2 gene for long QT syndrome type 2 (LQTS2) was identified after torsades des pointes ventricular tachycardia in a 49-year-old patient managed with octreotide and nadolol for an acute variceal bleed.	Nadolol	201-208	potassium voltage-gated channel subfamily H member 2	Homo sapiens	35-40
35587358-3	2022	Our data uncover a key enzyme of sterol synthesis, the hairpin membrane protein squalene monooxygenase (Erg1), as a non-canonical GET pathway client, thus rationalizing the lipotoxicity phenotypes of GET pathway mutants.	Sterols	33-39	potassium voltage-gated channel subfamily H member 2	Homo sapiens	104-108
35587358-5	2022	Intriguingly, we find that the GET pathway is especially important for the acute upregulation of Erg1 induced by low sterol conditions.	Sterols	117-123	potassium voltage-gated channel subfamily H member 2	Homo sapiens	97-101
34514026-7	2021	Consequently, human ether-a-go-go-related gene (HERG) channel blockers with high arrhythmogenic risk caused prolongation of contraction-relaxation duration and arrhythmia-like waveforms.	ether-a	20-27	potassium voltage-gated channel subfamily H member 2	Homo sapiens	48-52
35525425-7	2022	In LQT2 women, linear mixed effects models showed significant inverse correlations of QTc with progesterone (p<0.001), and the progesterone to estradiol ratio (p<0.001).	Progesterone	95-107	potassium voltage-gated channel subfamily H member 2	Homo sapiens	3-7
35525425-7	2022	In LQT2 women, linear mixed effects models showed significant inverse correlations of QTc with progesterone (p<0.001), and the progesterone to estradiol ratio (p<0.001).	Progesterone	127-139	potassium voltage-gated channel subfamily H member 2	Homo sapiens	3-7
35525425-7	2022	In LQT2 women, linear mixed effects models showed significant inverse correlations of QTc with progesterone (p<0.001), and the progesterone to estradiol ratio (p<0.001).	Estradiol	143-152	potassium voltage-gated channel subfamily H member 2	Homo sapiens	3-7
35525425-8	2022	Inverse relationships of the RR interval with estradiol levels (p=0.003) and of the T-wave duration with testosterone levels (p=0.014) were also observed in women with LQT2.	Testosterone	105-117	potassium voltage-gated channel subfamily H member 2	Homo sapiens	168-172
35455047-4	2022	In this study, we identified all index patients referred for NGS genetic sequencing due to LQTS, in a Spanish cohort, who were carriers of a new pathogenic variant (KCNH2 p.Gly262AlafsTer98).	gly262alafster98	173-189	potassium voltage-gated channel subfamily H member 2	Homo sapiens	165-170
35125346-4	2022	Methods: The thallium (Tl+) flux assay technique, widely used for drug screening, was optimized using human embryonic kidney (HEK-293) cells expressing a trafficking-deficient KV11.1 variant in 384-well plates.	Thallium	13-21	potassium voltage-gated channel subfamily H member 2	Homo sapiens	176-182
35125346-7	2022	Results: The combination of: 1) truncating the trafficking-deficient variant KV11.1-G601S (KV11.1-G601S-G965*X), and addition of 2) KV11.1 channel activator (VU0405601) and 3) cesium (Cs+) to the Tl+ flux assay buffer resulted in an outstanding Z" of 0.83.	Thallium	196-199	potassium voltage-gated channel subfamily H member 2	Homo sapiens	91-97
35125346-7	2022	Results: The combination of: 1) truncating the trafficking-deficient variant KV11.1-G601S (KV11.1-G601S-G965*X), and addition of 2) KV11.1 channel activator (VU0405601) and 3) cesium (Cs+) to the Tl+ flux assay buffer resulted in an outstanding Z" of 0.83.	VU0405601	158-167	potassium voltage-gated channel subfamily H member 2	Homo sapiens	91-97
35125346-7	2022	Results: The combination of: 1) truncating the trafficking-deficient variant KV11.1-G601S (KV11.1-G601S-G965*X), and addition of 2) KV11.1 channel activator (VU0405601) and 3) cesium (Cs+) to the Tl+ flux assay buffer resulted in an outstanding Z" of 0.83.	Thallium	196-199	potassium voltage-gated channel subfamily H member 2	Homo sapiens	132-138
35125346-8	2022	To validate the optimized trafficking assay, we carried out a pilot screen that identified three drugs (ibutilide, azaperone, and azelastine) as drugs that increase KV11.1 trafficking.	ibutilide	104-113	potassium voltage-gated channel subfamily H member 2	Homo sapiens	165-171
35125346-8	2022	To validate the optimized trafficking assay, we carried out a pilot screen that identified three drugs (ibutilide, azaperone, and azelastine) as drugs that increase KV11.1 trafficking.	Azaperone	115-124	potassium voltage-gated channel subfamily H member 2	Homo sapiens	165-171
35125346-7	2022	Results: The combination of: 1) truncating the trafficking-deficient variant KV11.1-G601S (KV11.1-G601S-G965*X), and addition of 2) KV11.1 channel activator (VU0405601) and 3) cesium (Cs+) to the Tl+ flux assay buffer resulted in an outstanding Z" of 0.83.	VU0405601	158-167	potassium voltage-gated channel subfamily H member 2	Homo sapiens	132-138
35125346-8	2022	To validate the optimized trafficking assay, we carried out a pilot screen that identified three drugs (ibutilide, azaperone, and azelastine) as drugs that increase KV11.1 trafficking.	azelastine	130-140	potassium voltage-gated channel subfamily H member 2	Homo sapiens	165-171
35125346-7	2022	Results: The combination of: 1) truncating the trafficking-deficient variant KV11.1-G601S (KV11.1-G601S-G965*X), and addition of 2) KV11.1 channel activator (VU0405601) and 3) cesium (Cs+) to the Tl+ flux assay buffer resulted in an outstanding Z" of 0.83.	Cesium	176-182	potassium voltage-gated channel subfamily H member 2	Homo sapiens	91-97
35125346-7	2022	Results: The combination of: 1) truncating the trafficking-deficient variant KV11.1-G601S (KV11.1-G601S-G965*X), and addition of 2) KV11.1 channel activator (VU0405601) and 3) cesium (Cs+) to the Tl+ flux assay buffer resulted in an outstanding Z" of 0.83.	Cesium	176-182	potassium voltage-gated channel subfamily H member 2	Homo sapiens	132-138
35125346-7	2022	Results: The combination of: 1) truncating the trafficking-deficient variant KV11.1-G601S (KV11.1-G601S-G965*X), and addition of 2) KV11.1 channel activator (VU0405601) and 3) cesium (Cs+) to the Tl+ flux assay buffer resulted in an outstanding Z" of 0.83.	Cesium	184-187	potassium voltage-gated channel subfamily H member 2	Homo sapiens	91-97
35125346-7	2022	Results: The combination of: 1) truncating the trafficking-deficient variant KV11.1-G601S (KV11.1-G601S-G965*X), and addition of 2) KV11.1 channel activator (VU0405601) and 3) cesium (Cs+) to the Tl+ flux assay buffer resulted in an outstanding Z" of 0.83.	Cesium	184-187	potassium voltage-gated channel subfamily H member 2	Homo sapiens	132-138
35087712-6	2022	The pro-arrhythmic action results from drug-induced inhibition of Kv11.1 (hERG) channels interfering with the repolarizing potassium IKr currents, leading to long QT and increased risk of triggered arrhythmias.	Potassium	123-132	potassium voltage-gated channel subfamily H member 2	Homo sapiens	66-72
34025432-8	2021	Conclusion: The window current-reducing and deactivation-slowing effects may be important for the antiarrhythmic effect of ajmaline, ivabradine, quinidine and mexiletine in SQT1-cells.	Ajmaline	123-131	potassium voltage-gated channel subfamily H member 2	Homo sapiens	173-177
33945158-4	2022	Inhibition of Eag1 reduces tumor growth, but the search for potent inhibitors for tumor therapy suffers from the structural similarities with the cardiac HERG channel, a major off-target.	eag1	14-18	potassium voltage-gated channel subfamily H member 2	Homo sapiens	154-158
34025432-8	2021	Conclusion: The window current-reducing and deactivation-slowing effects may be important for the antiarrhythmic effect of ajmaline, ivabradine, quinidine and mexiletine in SQT1-cells.	Ivabradine	133-143	potassium voltage-gated channel subfamily H member 2	Homo sapiens	173-177
34025432-8	2021	Conclusion: The window current-reducing and deactivation-slowing effects may be important for the antiarrhythmic effect of ajmaline, ivabradine, quinidine and mexiletine in SQT1-cells.	Quinidine	145-154	potassium voltage-gated channel subfamily H member 2	Homo sapiens	173-177
34025432-8	2021	Conclusion: The window current-reducing and deactivation-slowing effects may be important for the antiarrhythmic effect of ajmaline, ivabradine, quinidine and mexiletine in SQT1-cells.	Mexiletine	159-169	potassium voltage-gated channel subfamily H member 2	Homo sapiens	173-177
33658490-2	2021	In this work, we combine molecular dynamics simulations, mutagenesis, and electrophysiology to provide mechanistic insights into how lipophilic molecules (ceramide-sphingolipid probe) alter gating kinetics and K+ currents of hERG1.	Ceramides	155-163	potassium voltage-gated channel subfamily H member 2	Homo sapiens	225-230
33829343-1	2021	The human ether-a-go-go related gene (hERG, KCNH2) encodes the pore-forming subunit of the potassium channel responsible for a fast component of the cardiac delayed rectifier potassium current (IKr).	Potassium	91-100	potassium voltage-gated channel subfamily H member 2	Homo sapiens	44-49
33854869-3	2021	In addition to these apparent assets of Bedaquiline, potential disadvantages of Bedaquiline include inhibition of the hERG (human Ether-a-go-related gene; KCNH2), potassium channel (concurrent risk of cardiac toxicity), and risk of phospholipidosis due to its more lipophilic nature.	bedaquiline	80-91	potassium voltage-gated channel subfamily H member 2	Homo sapiens	155-160
33722764-7	2021	Moreover, a drug-induced LQT was modelled by treating the pigs with the hERG1 blocker dofetilide (DOF).	dofetilide	86-96	potassium voltage-gated channel subfamily H member 2	Homo sapiens	72-77
33722764-7	2021	Moreover, a drug-induced LQT was modelled by treating the pigs with the hERG1 blocker dofetilide (DOF).	dofetilide	98-101	potassium voltage-gated channel subfamily H member 2	Homo sapiens	72-77
33658490-2	2021	In this work, we combine molecular dynamics simulations, mutagenesis, and electrophysiology to provide mechanistic insights into how lipophilic molecules (ceramide-sphingolipid probe) alter gating kinetics and K+ currents of hERG1.	Sphingolipids	164-176	potassium voltage-gated channel subfamily H member 2	Homo sapiens	225-230
33658490-3	2021	We show that the sphingolipid probe induced a significant left shift of activation voltage, faster deactivation rates, and current blockade comparable to traditional hERG1 blockers.	Sphingolipids	17-29	potassium voltage-gated channel subfamily H member 2	Homo sapiens	166-171
33611903-18	2021	Mexiletine significantly improved symptoms in 2 patients with LQT2 post ineffective beta-blocker medication.	Mexiletine	0-10	potassium voltage-gated channel subfamily H member 2	Homo sapiens	62-66
33611903-17	2021	Nadolol succeeded in eliminating cardiac events in one patient with LQT2 post ineffective metoprolol medication.	Nadolol	0-7	potassium voltage-gated channel subfamily H member 2	Homo sapiens	68-72
33040444-0	2021	Letrozole targets the Human ether-a-go-go-related gene (HERG) potassium current in glioblastoma.	Letrozole	0-9	potassium voltage-gated channel subfamily H member 2	Homo sapiens	56-60
33040444-0	2021	Letrozole targets the Human ether-a-go-go-related gene (HERG) potassium current in glioblastoma.	Potassium	62-71	potassium voltage-gated channel subfamily H member 2	Homo sapiens	56-60
33261899-2	2021	We synthesized and evaluated three novel series of substituted benzophenones for their allosteric modulation of the human Kv11.1 (hERG) channel.	Benzophenones	63-76	potassium voltage-gated channel subfamily H member 2	Homo sapiens	122-128
33381033-5	2020	In conclusion, nadolol was recommended as a relatively effective strategy for LQT2 in order to improve the prognosis of patients during a long follow-up period.	Nadolol	15-22	potassium voltage-gated channel subfamily H member 2	Homo sapiens	78-82
33196188-10	2020	The original SILCS model was based on the all-atom modeling of the hERG1 channel in an explicit lipid bilayer and was further augmented with a Bayesian-optimization/machine-learning (BML) stage employing an independent literature-derived training set of 163 molecules.	Lipid Bilayers	96-109	potassium voltage-gated channel subfamily H member 2	Homo sapiens	67-72
33452554-0	2021	Influence of Kv11.1 (hERG1) K+ channel expression on DNA damage induced by the genotoxic agent methyl methanesulfonate.	Methyl Methanesulfonate	95-118	potassium voltage-gated channel subfamily H member 2	Homo sapiens	13-19
33452554-0	2021	Influence of Kv11.1 (hERG1) K+ channel expression on DNA damage induced by the genotoxic agent methyl methanesulfonate.	Methyl Methanesulfonate	95-118	potassium voltage-gated channel subfamily H member 2	Homo sapiens	21-26
33452554-6	2021	Moreover, direct DNA damage measurements, using the comet assay, demonstrated for the first time that Kv11.1 conduction activity was able to modify MMS-induced DNA damage, decreasing it particularly at high MMS concentration, in a way related to PARP1 gene expression.	Methyl Methanesulfonate	148-151	potassium voltage-gated channel subfamily H member 2	Homo sapiens	102-108
33467093-5	2021	In this study, we tested the hypothesis that the RNA polyadenylate binding protein nuclear 1 (PABPN1) interacts with a unique 22 nt adenosine stretch adjacent to the intron 9 poly(A) signal and regulates KCNH2 pre-mRNA alternative polyadenylation and the relative expression of Kv11.1a C-terminal isoforms.	Adenosine	132-141	potassium voltage-gated channel subfamily H member 2	Homo sapiens	204-209
32587517-8	2020	Blocking KV11.1 with E4031 shows that channel activity contributed to modulate the beta1 integrin-dependent pHi increase.	E 4031	21-26	potassium voltage-gated channel subfamily H member 2	Homo sapiens	9-15
32253972-2	2020	A frequent cause for LQTS are mutations in the KCNH2 gene (also known as the human ether-a-go-go-related gene or hERG), which reduce or modulate the potassium current IKr and hence alter cardiac repolarization.	ether-a-go	83-93	potassium voltage-gated channel subfamily H member 2	Homo sapiens	47-52
32253972-2	2020	A frequent cause for LQTS are mutations in the KCNH2 gene (also known as the human ether-a-go-go-related gene or hERG), which reduce or modulate the potassium current IKr and hence alter cardiac repolarization.	Potassium	149-158	potassium voltage-gated channel subfamily H member 2	Homo sapiens	47-52
33154722-3	2020	The aim of this study was to investigate the mechanisms of disopyramide underlying its antiarrhythmic effects in SQTS1 with the N588K mutation in HERG channel.	Disopyramide	59-71	potassium voltage-gated channel subfamily H member 2	Homo sapiens	146-150
33154722-10	2020	The results demonstrated that disopyramide may be effective for preventing tachyarrhythmias in SQTS1-patients carrying the N588K mutation in HERG channel by APD-prolongation via enhancing ICa-L, late INa, INCX, and reducing ISK.	Disopyramide	30-42	potassium voltage-gated channel subfamily H member 2	Homo sapiens	141-145
33002116-6	2021	METHODS AND RESULTS: Meta-analysis of 3653 public human RNA-seq datasets identified a strong correlation between expression of CACNA1C (L-type calcium current, ICaL) and KCNH2 (rapid delayed rectifier K+ current, IKr), which was also observed in human adult heart tissue samples.	Calcium	143-150	potassium voltage-gated channel subfamily H member 2	Homo sapiens	170-175
32940533-3	2020	Recently, FDA-approved cystic fibrosis protein trafficking chaperone, lumacaftor (LUM), has been proposed as novel therapy for LQT2.	lumacaftor	70-80	potassium voltage-gated channel subfamily H member 2	Homo sapiens	127-131
32940533-3	2020	Recently, FDA-approved cystic fibrosis protein trafficking chaperone, lumacaftor (LUM), has been proposed as novel therapy for LQT2.	lumacaftor	82-85	potassium voltage-gated channel subfamily H member 2	Homo sapiens	127-131
32940533-4	2020	Here, we test the efficacy of LUM treatment in patient-specific induced pluripotent stem cell-cardiomyocytes (iPSC-CMs) derived from two patients with known LQT2 trafficking defective mutations and a patient with novel KCNH2 variant, p.R685P.	lumacaftor	30-33	potassium voltage-gated channel subfamily H member 2	Homo sapiens	157-161
32940533-4	2020	Here, we test the efficacy of LUM treatment in patient-specific induced pluripotent stem cell-cardiomyocytes (iPSC-CMs) derived from two patients with known LQT2 trafficking defective mutations and a patient with novel KCNH2 variant, p.R685P.	lumacaftor	30-33	potassium voltage-gated channel subfamily H member 2	Homo sapiens	219-224
32940533-10	2020	While LUM treatment rescued the phenotype of KCNH2-N633S and KCNH2-R685P, LUM paradoxically prolonged the APD90 in KCNH2-G604S iPSC-CMs.	lumacaftor	6-9	potassium voltage-gated channel subfamily H member 2	Homo sapiens	45-50
32940533-10	2020	While LUM treatment rescued the phenotype of KCNH2-N633S and KCNH2-R685P, LUM paradoxically prolonged the APD90 in KCNH2-G604S iPSC-CMs.	lumacaftor	6-9	potassium voltage-gated channel subfamily H member 2	Homo sapiens	61-66
32940533-10	2020	While LUM treatment rescued the phenotype of KCNH2-N633S and KCNH2-R685P, LUM paradoxically prolonged the APD90 in KCNH2-G604S iPSC-CMs.	lumacaftor	6-9	potassium voltage-gated channel subfamily H member 2	Homo sapiens	61-66
32710951-5	2020	Sevoflurane, but not propofol, prolonged ventricular action potential duration and QT interval in wild-type, LQT1 and LQT2 models.	Sevoflurane	0-11	potassium voltage-gated channel subfamily H member 2	Homo sapiens	118-122
32922187-11	2020	Molecular docking analysis successfully combined KCNH2, NCOA1, KDR and ADRB2 to Myricanone with docking scores from 4.61 to 6.28.	myricanone	80-90	potassium voltage-gated channel subfamily H member 2	Homo sapiens	49-54
32694995-7	2020	Using multi-microseconds Molecular Dynamics (MD) simulations of wild-type and M651T mutant hERG1, we suggested the block of the channel through the lipid mediated pathway, the opening of which is facilitated by the flexible phenylalanine ring (F656).	Phenylalanine	224-237	potassium voltage-gated channel subfamily H member 2	Homo sapiens	91-96
32534368-7	2020	To achieve therapeutic targeting, DTX-Au-PEG complex and DTX IN PEG-AuNPs were chemical combined with the human anti-EGFR polyclonal antibody, which recognizes the hERG1 channel aberrantly expressed on the membrane of human lung cancer cells.	Docetaxel	34-37	potassium voltage-gated channel subfamily H member 2	Homo sapiens	164-169
32710951-6	2020	The QT-prolonging effect of sevoflurane was more profound in LQT2 than in wild-type and LQT1 models.	Sevoflurane	28-39	potassium voltage-gated channel subfamily H member 2	Homo sapiens	61-65
32710951-8	2020	In LQT2 model, IKs was considerably enhanced during excessive prolongation of ventricular action potential duration by reduction of IKr and relative contribution of IKs to ventricular repolarization was markedly elevated, which appears to underlie more pronounced QT-prolonging effect of sevoflurane in LQT2 model, compared with wild-type and LQT1 models.	Sevoflurane	288-299	potassium voltage-gated channel subfamily H member 2	Homo sapiens	3-7
32710951-9	2020	This simulation study clearly elucidates the electrophysiological basis underlying the difference in QT-prolonging effect of sevoflurane among wild-type, LQT1 and LQT2 models, and may provide important information for developing anesthetic strategies for patients with long QT syndrome in clinical settings.	Sevoflurane	125-136	potassium voltage-gated channel subfamily H member 2	Homo sapiens	163-167
32533968-2	2020	In this study, Procyanidin B1, a natural compound extracted from the grape seed, was identified as a potent, specific inhibitor, which can inhibit the Kv10.1 channel in a concentration-dependent manner (IC50 = 10.38 +- 0.87 muM), but has negligible effects on other potassium channels, including Kir2.1, HERG or KCNQ1.	procyanidin B1	15-29	potassium voltage-gated channel subfamily H member 2	Homo sapiens	304-308
33304417-6	2020	This is the first report that demonstrates the efficacy and safety of trans-maternal administration of nadolol for treatment of symptomatic LQT2 fetuses with TdP.	Nadolol	103-110	potassium voltage-gated channel subfamily H member 2	Homo sapiens	140-144
32694995-9	2020	We investigated two well-established hERG1 blockers (ivabradine and dofetilide) for M651 sensitivity through electrophysiology and mutagenesis techniques.	Ivabradine	53-63	potassium voltage-gated channel subfamily H member 2	Homo sapiens	37-42
32694995-9	2020	We investigated two well-established hERG1 blockers (ivabradine and dofetilide) for M651 sensitivity through electrophysiology and mutagenesis techniques.	dofetilide	68-78	potassium voltage-gated channel subfamily H member 2	Homo sapiens	37-42
32694995-11	2020	Moreover, we show that the dofetilide-induced block of hERG1 occurs through the intracellular space, whereas little to no block of ivabradine is observed during the intracellular application of the drug.	dofetilide	27-37	potassium voltage-gated channel subfamily H member 2	Homo sapiens	55-60
32231201-0	2020	Correction: Clarithromycin inhibits autophagy in colorectal cancer by regulating the hERG1 potassium channel interaction with PI3K.	Clarithromycin	12-26	potassium voltage-gated channel subfamily H member 2	Homo sapiens	85-90
32173522-3	2020	Here, HEK293 cells were transfected with the HERG gene alone or co-transfected with HERG and AKAP5 using Lipofectamine 2000.	Lipofectamine	105-123	potassium voltage-gated channel subfamily H member 2	Homo sapiens	84-88
32390841-6	2020	Attenuating the K+ channel function by applying the hERG1 channel inhibitor E4031 modulated Ca2+ signaling, impaired inhibition of the mitosis promoting subunit cdc2, overrode cell cycle arrest, and decreased clonogenic survival of the irradiated cells but did not affect repair of DNA double strand breaks suggesting a critical role of the hERG1 K+ channels for the Ca2+ signaling and the cell cycle control during DNA damage response.	E 4031	76-81	potassium voltage-gated channel subfamily H member 2	Homo sapiens	52-57
32390841-6	2020	Attenuating the K+ channel function by applying the hERG1 channel inhibitor E4031 modulated Ca2+ signaling, impaired inhibition of the mitosis promoting subunit cdc2, overrode cell cycle arrest, and decreased clonogenic survival of the irradiated cells but did not affect repair of DNA double strand breaks suggesting a critical role of the hERG1 K+ channels for the Ca2+ signaling and the cell cycle control during DNA damage response.	E 4031	76-81	potassium voltage-gated channel subfamily H member 2	Homo sapiens	341-346
32191791-0	2020	Structure of KCNH2 cyclic nucleotide-binding homology domain reveals a functionally vital salt-bridge.	Nucleotides, Cyclic	19-36	potassium voltage-gated channel subfamily H member 2	Homo sapiens	13-18
32191791-2	2020	Like other KCNH family members, hKCNH2 channels contain a unique intracellular complex, consisting of an N-terminal eag domain and a C-terminal cyclic nucleotide-binding homology domain (CNBHD), which is crucial for channel function.	Methyl 2-acetamido-2-deoxy-beta-D-glucopyranoside	116-119	potassium voltage-gated channel subfamily H member 2	Homo sapiens	32-38
32191791-2	2020	Like other KCNH family members, hKCNH2 channels contain a unique intracellular complex, consisting of an N-terminal eag domain and a C-terminal cyclic nucleotide-binding homology domain (CNBHD), which is crucial for channel function.	Nucleotides, Cyclic	144-161	potassium voltage-gated channel subfamily H member 2	Homo sapiens	32-38
31901677-0	2020	Elucidation of interaction mechanism of hERG1 potassium channel with scorpion toxins BeKm-1 and BmTx3b.	Potassium	46-55	potassium voltage-gated channel subfamily H member 2	Homo sapiens	40-45
31877041-5	2020	ICA-105574 (ICA), a 3-Nitro-n-(4-phenoxyphenyl) benzamide derivative activates hERG1 by strongly attenuating pore-type inactivation.	3-nitro-N-(4-phenoxyphenyl)benzamide	0-10	potassium voltage-gated channel subfamily H member 2	Homo sapiens	79-84
32391435-2	2020	Our findings indicate that the antibiotic clarithromycin can target hERG1 and modulate autophagy to promote the death of chemoresistant colorectal cancer cells.	Clarithromycin	42-56	potassium voltage-gated channel subfamily H member 2	Homo sapiens	68-73
32123164-0	2020	Clarithromycin inhibits autophagy in colorectal cancer by regulating the hERG1 potassium channel interaction with PI3K.	Clarithromycin	0-14	potassium voltage-gated channel subfamily H member 2	Homo sapiens	73-78
32123164-4	2020	Because Cla is known to bind human Ether-a-go-go Related Gene 1 (hERG1) K+ channels, we studied if its effects depended on hERG1 and its conformational states.	Clarithromycin	8-11	potassium voltage-gated channel subfamily H member 2	Homo sapiens	65-70
32123164-4	2020	Because Cla is known to bind human Ether-a-go-go Related Gene 1 (hERG1) K+ channels, we studied if its effects depended on hERG1 and its conformational states.	Clarithromycin	8-11	potassium voltage-gated channel subfamily H member 2	Homo sapiens	123-128
32123164-5	2020	By availing of hERG1 mutants with different gating properties, we found that fluorescently labelled Cla preferentially bound to the closed channels.	Clarithromycin	100-103	potassium voltage-gated channel subfamily H member 2	Homo sapiens	15-20
32123164-6	2020	Furthermore, by sequestering the channel in the closed conformation, Cla inhibited the formation of a macromolecular complex between hERG1 and the p85 subunit of PI3K.	Clarithromycin	69-72	potassium voltage-gated channel subfamily H member 2	Homo sapiens	133-138
32123164-9	2020	We conclude that Cla affects the autophagic flux by impairing the signaling pathway linking hERG1 and PI3K.	Clarithromycin	17-20	potassium voltage-gated channel subfamily H member 2	Homo sapiens	92-97
31472168-10	2020	The hERG1 (KV11.1) blocker, E4031, followed by the IKs blocker, JNJ303, increased extracellular field potential duration in CPC-iPSC-CMs to a greater extent than in BMC- and HDF-iPSC-CMs.	bmc	165-168	potassium voltage-gated channel subfamily H member 2	Homo sapiens	4-9
31557540-1	2020	BACKGROUND: KCNH2 encodes the human ether-a-go-go-related gene (hERG) potassium channel, which passes the rapid delayed rectifier potassium current, IKr.	Potassium	70-79	potassium voltage-gated channel subfamily H member 2	Homo sapiens	12-17
31557540-1	2020	BACKGROUND: KCNH2 encodes the human ether-a-go-go-related gene (hERG) potassium channel, which passes the rapid delayed rectifier potassium current, IKr.	Potassium	130-139	potassium voltage-gated channel subfamily H member 2	Homo sapiens	12-17
31877041-5	2020	ICA-105574 (ICA), a 3-Nitro-n-(4-phenoxyphenyl) benzamide derivative activates hERG1 by strongly attenuating pore-type inactivation.	3-nitro-N-(4-phenoxyphenyl)benzamide	20-57	potassium voltage-gated channel subfamily H member 2	Homo sapiens	79-84
32071644-0	2020	Mexiletine shortens the QT interval in a pedigree of KCNH2 related long QT syndrome.	Mexiletine	0-10	potassium voltage-gated channel subfamily H member 2	Homo sapiens	53-58
31948476-0	2020	The ERG1a potassium channel increases basal intracellular calcium concentration and calpain activity in skeletal muscle cells.	Potassium	10-19	potassium voltage-gated channel subfamily H member 2	Homo sapiens	4-8
31948476-0	2020	The ERG1a potassium channel increases basal intracellular calcium concentration and calpain activity in skeletal muscle cells.	Calcium	58-65	potassium voltage-gated channel subfamily H member 2	Homo sapiens	4-8
31570775-5	2020	Translating to humans, we find analogous dysfunctional interactions between hippocampus and prefrontal cortex in coupling of the fMRI blood oxygen level-dependent (BOLD) signal during working memory in healthy subjects carrying alleles associated with increased KCNH2-3.1 expression in brain.	Oxygen	140-146	potassium voltage-gated channel subfamily H member 2	Homo sapiens	262-267
31751991-6	2020	This study focuses on investigating the potential variants on SCN5A, KCNQ1, and KCNH2 contributing to AMI with VA in a Chinese population.	Vanillic Acid	111-113	potassium voltage-gated channel subfamily H member 2	Homo sapiens	80-85
30826123-8	2019	In this study we show that the activation kinetics in iPSC-CMs resemble hERG1b kinetics using Cs+ as a charge carrier.	Cesium	94-97	potassium voltage-gated channel subfamily H member 2	Homo sapiens	72-77
31874991-3	2019	The human ether-a-go-go-related gene 1 (hERG1) encodes the pore-forming subunit underlying cardiac rapidly delayed rectifier potassium current (IKr).	Potassium	125-134	potassium voltage-gated channel subfamily H member 2	Homo sapiens	40-45
31874991-7	2019	Quantitative RT-PCR, Western blot analysis, immunofluorescence and co-immunoprecipitation methods were used to determine the effects of mitragynine on hERG1a/1b expression and hERG1-cytosolic chaperones interaction.	mitragynine	136-147	potassium voltage-gated channel subfamily H member 2	Homo sapiens	151-156
31664867-1	2019	There is significant interest in the potential utility of small molecule activator compounds to mitigate cardiac arrhythmia caused by loss-of-function of hERG1a voltage-gated potassium channels.	Potassium	175-184	potassium voltage-gated channel subfamily H member 2	Homo sapiens	154-159
31664867-5	2019	Our functional data from isolated zkcnh6a channels show that these channels respond to hERG1a channel blockers (dofetilide and terfenadine), and type 1 (RPR260243) and type 2 (NS1643, PD-118057) hERG1a activator compounds, in a similar manner to hKCNH2a channels, with minor differences largely accounted for by subtly different biophysical properties in the two channels.	dofetilide	112-122	potassium voltage-gated channel subfamily H member 2	Homo sapiens	87-92
31664867-5	2019	Our functional data from isolated zkcnh6a channels show that these channels respond to hERG1a channel blockers (dofetilide and terfenadine), and type 1 (RPR260243) and type 2 (NS1643, PD-118057) hERG1a activator compounds, in a similar manner to hKCNH2a channels, with minor differences largely accounted for by subtly different biophysical properties in the two channels.	Terfenadine	127-138	potassium voltage-gated channel subfamily H member 2	Homo sapiens	87-92
31573043-5	2019	However, how the sequence context influences the efficiency of aminoglycosides in rescuing the human ether-a-go-go-related (HERG) protein in mammalian cells remains to be fully elucidated.	Aminoglycosides	63-78	potassium voltage-gated channel subfamily H member 2	Homo sapiens	124-128
31573043-6	2019	Therefore, the present study was devised to examine the susceptibility of different termination codons on the HERG gene and the +4 nucleotide immediately following them to be suppressed by aminoglycosides in 293 cells.	Aminoglycosides	189-204	potassium voltage-gated channel subfamily H member 2	Homo sapiens	110-114
31573043-8	2019	The read-through effect was subsequently examined by adding aminoglycoside G418 into the culture medium, followed by incubation of the cells for 24 h. An immunofluorescence method was then used to observe the protein expression of HERG prior to and following drug treatment.	Aminoglycosides	60-74	potassium voltage-gated channel subfamily H member 2	Homo sapiens	231-235
31573043-13	2019	The level of red fluorescence was observed prior to and following the administration of G418 using antibodies targeting the N- or C-terminus of the HERG protein.	Nitrogen	124-125	potassium voltage-gated channel subfamily H member 2	Homo sapiens	148-152
31573043-13	2019	The level of red fluorescence was observed prior to and following the administration of G418 using antibodies targeting the N- or C-terminus of the HERG protein.	Carbon	130-131	potassium voltage-gated channel subfamily H member 2	Homo sapiens	148-152
31447465-0	2019	Mexiletine Suppressed Recurrent Ventricular Tachycardia Triggered by Hemodialysis in an Old Patient with LQT2.	Mexiletine	0-10	potassium voltage-gated channel subfamily H member 2	Homo sapiens	105-109
31807018-0	2019	The hERG1 Potassium Channel Behaves As Prognostic Factor In Gastric Dysplasia Endoscopic Samples.	Potassium	10-19	potassium voltage-gated channel subfamily H member 2	Homo sapiens	4-9
30947366-6	2019	Ivabradine, ajmaline, and mexiletine inhibited KCNH2 channel currents significantly, which may underlie their APD-prolonging effects.	Ivabradine	0-10	potassium voltage-gated channel subfamily H member 2	Homo sapiens	47-52
31484079-1	2019	The human ether-a-go-go-related gene KCNH2 encodes the voltage-gated potassium channel underlying IKr, a current critical for the repolarization phase of the cardiac action potential.	ether-a	10-17	potassium voltage-gated channel subfamily H member 2	Homo sapiens	37-42
30947366-6	2019	Ivabradine, ajmaline, and mexiletine inhibited KCNH2 channel currents significantly, which may underlie their APD-prolonging effects.	Ajmaline	12-20	potassium voltage-gated channel subfamily H member 2	Homo sapiens	47-52
30947366-6	2019	Ivabradine, ajmaline, and mexiletine inhibited KCNH2 channel currents significantly, which may underlie their APD-prolonging effects.	Mexiletine	26-36	potassium voltage-gated channel subfamily H member 2	Homo sapiens	47-52
31946488-2	2019	The SQT1, SQT2 and SQT3 variants of the SQTS result from inherited gain-of-function mutations (e.g. N588K, V307L and D172N, respectively) to potassium channels.	Potassium	141-150	potassium voltage-gated channel subfamily H member 2	Homo sapiens	4-8
31182542-0	2019	The Pore-Lipid Interface: Role of Amino-Acid Determinants of Lipophilic Access by Ivabradine to the hERG1 Pore Domain.	Ivabradine	82-92	potassium voltage-gated channel subfamily H member 2	Homo sapiens	100-105
31347270-0	2019	Long QT syndrome in chromosome 7q35q36.3 deletion involving KCNH2 gene: Warning for chlorpheniramine prescription.	Chlorpheniramine	84-100	potassium voltage-gated channel subfamily H member 2	Homo sapiens	60-65
31347270-3	2019	RESULTS: Among the deleted genes, two genes have cardiac implications: PRKAG2 (OMIM #602743), associated with hypertrophic cardiomyopathy, cardiac conduction disease, and sudden death, and KCNH2 (OMIM #152427), coding for a cardiac potassium channel involved in long QT syndrome, unmasked by the chlorpheniramine treatment.	Chlorpheniramine	296-312	potassium voltage-gated channel subfamily H member 2	Homo sapiens	189-194
31032878-5	2019	EXPERIMENTAL APPROACH: We analysed sensitivity of recombinant Kv 12.1 channels to quinine, a substituted quinoline that blocks Kv 10.1 and Kv 11.1 at low micromolar concentrations.	Quinine	82-89	potassium voltage-gated channel subfamily H member 2	Homo sapiens	139-146
31032878-5	2019	EXPERIMENTAL APPROACH: We analysed sensitivity of recombinant Kv 12.1 channels to quinine, a substituted quinoline that blocks Kv 10.1 and Kv 11.1 at low micromolar concentrations.	quinoline	105-114	potassium voltage-gated channel subfamily H member 2	Homo sapiens	139-146
31032878-8	2019	Low sensitivity of Kv 12.1 and characteristics of quinine-dependent inhibition were determined by histidine 462, as site-directed mutagenesis of this residue into the homologous tyrosine of Kv 11.1 conferred Kv 11.1-like quinine block to Kv 12.1(H462Y).	Quinine	50-57	potassium voltage-gated channel subfamily H member 2	Homo sapiens	190-197
31032878-8	2019	Low sensitivity of Kv 12.1 and characteristics of quinine-dependent inhibition were determined by histidine 462, as site-directed mutagenesis of this residue into the homologous tyrosine of Kv 11.1 conferred Kv 11.1-like quinine block to Kv 12.1(H462Y).	Quinine	50-57	potassium voltage-gated channel subfamily H member 2	Homo sapiens	208-215
31032878-8	2019	Low sensitivity of Kv 12.1 and characteristics of quinine-dependent inhibition were determined by histidine 462, as site-directed mutagenesis of this residue into the homologous tyrosine of Kv 11.1 conferred Kv 11.1-like quinine block to Kv 12.1(H462Y).	Histidine	98-107	potassium voltage-gated channel subfamily H member 2	Homo sapiens	190-197
31032878-8	2019	Low sensitivity of Kv 12.1 and characteristics of quinine-dependent inhibition were determined by histidine 462, as site-directed mutagenesis of this residue into the homologous tyrosine of Kv 11.1 conferred Kv 11.1-like quinine block to Kv 12.1(H462Y).	Histidine	98-107	potassium voltage-gated channel subfamily H member 2	Homo sapiens	208-215
31032878-8	2019	Low sensitivity of Kv 12.1 and characteristics of quinine-dependent inhibition were determined by histidine 462, as site-directed mutagenesis of this residue into the homologous tyrosine of Kv 11.1 conferred Kv 11.1-like quinine block to Kv 12.1(H462Y).	Tyrosine	178-186	potassium voltage-gated channel subfamily H member 2	Homo sapiens	190-197
31032878-8	2019	Low sensitivity of Kv 12.1 and characteristics of quinine-dependent inhibition were determined by histidine 462, as site-directed mutagenesis of this residue into the homologous tyrosine of Kv 11.1 conferred Kv 11.1-like quinine block to Kv 12.1(H462Y).	Tyrosine	178-186	potassium voltage-gated channel subfamily H member 2	Homo sapiens	208-215
31032878-8	2019	Low sensitivity of Kv 12.1 and characteristics of quinine-dependent inhibition were determined by histidine 462, as site-directed mutagenesis of this residue into the homologous tyrosine of Kv 11.1 conferred Kv 11.1-like quinine block to Kv 12.1(H462Y).	Quinine	221-228	potassium voltage-gated channel subfamily H member 2	Homo sapiens	190-197
31032878-8	2019	Low sensitivity of Kv 12.1 and characteristics of quinine-dependent inhibition were determined by histidine 462, as site-directed mutagenesis of this residue into the homologous tyrosine of Kv 11.1 conferred Kv 11.1-like quinine block to Kv 12.1(H462Y).	Quinine	221-228	potassium voltage-gated channel subfamily H member 2	Homo sapiens	208-215
31032878-10	2019	In contrast, more favourable interactions can explain the higher quinine sensitivity of Kv 12.1(H462Y) and Kv 11.1 channels.	Quinine	65-72	potassium voltage-gated channel subfamily H member 2	Homo sapiens	107-114
31946488-4	2019	In this study, computational modelling was used to investigate pharmacotherapeutic effects of selected class I drug quinidine on SQT1, SQT2 and SQT3 variants.	Quinidine	116-125	potassium voltage-gated channel subfamily H member 2	Homo sapiens	129-133
31946488-10	2019	At the 10 muM concentration tested in this study, quinidine effectively prolonged the action potential duration (APD) under all the SQT1, SQT2 and SQT3 conditions.	Quinidine	50-59	potassium voltage-gated channel subfamily H member 2	Homo sapiens	132-136
31275424-6	2019	The results of molecular docking showed that linalool, caryophyllene, dibutyl phthalate, (-)-4-terpineol, and (-)-alpha-terpineol have good binding activity with ADRB2, DRD2, ESR1, KCNH2, NR1H4, NR1I2, NR1I3, and TRPV1 targets.	linalool	45-53	potassium voltage-gated channel subfamily H member 2	Homo sapiens	181-186
30938413-7	2019	Oxytocin prolonged QTc and steepened QT/RR-slope in vivo and prolonged ex vivo APD75 in LQT2 hearts.	Oxytocin	0-8	potassium voltage-gated channel subfamily H member 2	Homo sapiens	88-92
31275424-6	2019	The results of molecular docking showed that linalool, caryophyllene, dibutyl phthalate, (-)-4-terpineol, and (-)-alpha-terpineol have good binding activity with ADRB2, DRD2, ESR1, KCNH2, NR1H4, NR1I2, NR1I3, and TRPV1 targets.	alpha-terpineol	110-129	potassium voltage-gated channel subfamily H member 2	Homo sapiens	181-186
31275424-6	2019	The results of molecular docking showed that linalool, caryophyllene, dibutyl phthalate, (-)-4-terpineol, and (-)-alpha-terpineol have good binding activity with ADRB2, DRD2, ESR1, KCNH2, NR1H4, NR1I2, NR1I3, and TRPV1 targets.	caryophyllene	55-68	potassium voltage-gated channel subfamily H member 2	Homo sapiens	181-186
31275424-6	2019	The results of molecular docking showed that linalool, caryophyllene, dibutyl phthalate, (-)-4-terpineol, and (-)-alpha-terpineol have good binding activity with ADRB2, DRD2, ESR1, KCNH2, NR1H4, NR1I2, NR1I3, and TRPV1 targets.	Dibutyl Phthalate	70-87	potassium voltage-gated channel subfamily H member 2	Homo sapiens	181-186
31275424-6	2019	The results of molecular docking showed that linalool, caryophyllene, dibutyl phthalate, (-)-4-terpineol, and (-)-alpha-terpineol have good binding activity with ADRB2, DRD2, ESR1, KCNH2, NR1H4, NR1I2, NR1I3, and TRPV1 targets.	(-)-Terpinen-4-ol	89-104	potassium voltage-gated channel subfamily H member 2	Homo sapiens	181-186
30689740-3	2019	The generally accepted common mechanism whereby drugs prolong QT is block of a key repolarizing potassium current in heart, IKr, generated by expression of KCNH2, also known as HERG.	Potassium	96-105	potassium voltage-gated channel subfamily H member 2	Homo sapiens	156-161
31186788-0	2019	hERG1 is involved in the pathophysiological process and inhibited by berberine in SKOV3 cells.	Berberine	69-78	potassium voltage-gated channel subfamily H member 2	Homo sapiens	0-5
31186788-11	2019	In addition, berberine (BBR) may be used as a potential drug in the treatment of ovarian cancer, possibly due to its inhibitory effects on the hERG1 channels.	Berberine	13-22	potassium voltage-gated channel subfamily H member 2	Homo sapiens	143-148
31186788-11	2019	In addition, berberine (BBR) may be used as a potential drug in the treatment of ovarian cancer, possibly due to its inhibitory effects on the hERG1 channels.	Berberine	24-27	potassium voltage-gated channel subfamily H member 2	Homo sapiens	143-148
31186788-12	2019	In conclusion, the present study demonstrated that hERG1 may be a potential therapeutic target in the treatment of ovarian cancer and provided novel insights into the mechanism underlying the antitumor effects of BBR in ovarian cancer.	Berberine	213-216	potassium voltage-gated channel subfamily H member 2	Homo sapiens	51-56
31006312-12	2019	CONCLUSIONS: Although commonly prescribed in patients with LQT3, mexiletine also shortens the QTc significantly in two-thirds of a small subset of patients with potassium channel-mediated LQT2.	Mexiletine	65-75	potassium voltage-gated channel subfamily H member 2	Homo sapiens	188-192
31006312-13	2019	In patients with LQT2, pharmacological targeting of the physiological late sodium current may provide added therapeutic efficacy to beta-blocker therapy.	Sodium	75-81	potassium voltage-gated channel subfamily H member 2	Homo sapiens	17-21
30689740-3	2019	The generally accepted common mechanism whereby drugs prolong QT is block of a key repolarizing potassium current in heart, IKr, generated by expression of KCNH2, also known as HERG.	Potassium	96-105	potassium voltage-gated channel subfamily H member 2	Homo sapiens	177-181
31169990-4	2019	Recent evidence, however, has shown significant affinity of ivabradine towards Kv11.1 (ether-a-go-go related gene, ERG) potassium channels.	Ivabradine	60-70	potassium voltage-gated channel subfamily H member 2	Homo sapiens	79-85
30687112-8	2018	At the concentrations tested in this study, quinidine most effectively prolonged the APD and ERP in the setting of SQT1, followed by disopyramide and propafenone.	Quinidine	44-53	potassium voltage-gated channel subfamily H member 2	Homo sapiens	115-119
30582453-10	2019	Moreover, QTc of SQT patient and action potential durations of SQT iPSC-CMs were both normalized by quinidine, indicating that quinidine is beneficial to KCNH2 T618I of SQT.	Quinidine	100-109	potassium voltage-gated channel subfamily H member 2	Homo sapiens	154-159
30582453-10	2019	Moreover, QTc of SQT patient and action potential durations of SQT iPSC-CMs were both normalized by quinidine, indicating that quinidine is beneficial to KCNH2 T618I of SQT.	Quinidine	127-136	potassium voltage-gated channel subfamily H member 2	Homo sapiens	154-159
31169990-5	2019	Despite the inhibition of Kv11.1 channels by ivabradine, cardiac action potential (AP) duration and heart rate corrected QT interval (QTc) of the human electrocardiogram (ECG) were not prolonged.	Ivabradine	45-55	potassium voltage-gated channel subfamily H member 2	Homo sapiens	26-32
31169990-11	2019	Within this study we also confirm recent findings of human Kv11.1 inhibition by low microM concentrations of ivabradine and observed no prolongation of ventricular-like APs in cardiomyocytes derived from iPSCs.	Ivabradine	109-119	potassium voltage-gated channel subfamily H member 2	Homo sapiens	59-65
31169990-12	2019	CONCLUSION: Our results provide an explanation why ivabradine, despite its affinity for Kv11.1 channels, does not prolong the cardiac AP and QTc interval.	Ivabradine	51-61	potassium voltage-gated channel subfamily H member 2	Homo sapiens	88-94
29875689-6	2018	The microtubule depolymerizing drug nocodazole differentially affected G601S- and F805C-Kv11.1 protein immunostaining.	Nocodazole	36-46	potassium voltage-gated channel subfamily H member 2	Homo sapiens	88-94
30567462-5	2019	RESULTS: Dofetilide and cisapride (IKr or Kv11.1 blockers) were associated with significant increases in QTca and JTpca, while sotalol was associated with significant increases in QTca, JTpca, and Tpeca.	Cisapride	24-33	potassium voltage-gated channel subfamily H member 2	Homo sapiens	42-48
30567462-6	2019	Verapamil (a Kv11.1 and Cav1.2 blocker) resulted in a reduction in QTca and JTpca, however, and increased Tpeca.	Verapamil	0-9	potassium voltage-gated channel subfamily H member 2	Homo sapiens	13-19
30405887-5	2018	The resulting scFv-hERG1-Cys showed much higher stability and protein yield, increased affinity and more advantageous binding kinetics, compared to the "native" anti-hERG1scFv.	Cysteine	25-28	potassium voltage-gated channel subfamily H member 2	Homo sapiens	19-24
30405887-6	2018	The scFv-hERG1-Cys was hence chosen and characterized: it showed a good binding to the native hERG1 antigen expressed on cells, was stable in serum and displayed a fast pharmacokinetic profile once injected intravenously in nude mice.	Cysteine	15-18	potassium voltage-gated channel subfamily H member 2	Homo sapiens	9-14
30405887-6	2018	The scFv-hERG1-Cys was hence chosen and characterized: it showed a good binding to the native hERG1 antigen expressed on cells, was stable in serum and displayed a fast pharmacokinetic profile once injected intravenously in nude mice.	Cysteine	15-18	potassium voltage-gated channel subfamily H member 2	Homo sapiens	94-99
30405887-8	2018	Finally, the in vivo distribution of an Alexa Fluor 750 conjugated scFv-hERG1-Cys was evaluated both in healthy and tumor-bearing nude mice, showing a good tumor-to-organ ratio, ideal for visualizing hERG1-expressing tumor masses in vivo.	Alexa Fluor 750	40-55	potassium voltage-gated channel subfamily H member 2	Homo sapiens	72-77
30405887-8	2018	Finally, the in vivo distribution of an Alexa Fluor 750 conjugated scFv-hERG1-Cys was evaluated both in healthy and tumor-bearing nude mice, showing a good tumor-to-organ ratio, ideal for visualizing hERG1-expressing tumor masses in vivo.	Alexa Fluor 750	40-55	potassium voltage-gated channel subfamily H member 2	Homo sapiens	200-205
30405887-8	2018	Finally, the in vivo distribution of an Alexa Fluor 750 conjugated scFv-hERG1-Cys was evaluated both in healthy and tumor-bearing nude mice, showing a good tumor-to-organ ratio, ideal for visualizing hERG1-expressing tumor masses in vivo.	Cysteine	78-81	potassium voltage-gated channel subfamily H member 2	Homo sapiens	72-77
30405887-8	2018	Finally, the in vivo distribution of an Alexa Fluor 750 conjugated scFv-hERG1-Cys was evaluated both in healthy and tumor-bearing nude mice, showing a good tumor-to-organ ratio, ideal for visualizing hERG1-expressing tumor masses in vivo.	Cysteine	78-81	potassium voltage-gated channel subfamily H member 2	Homo sapiens	200-205
30405887-9	2018	In conclusion, the scFv-hERG1-Cys possesses features which make it a suitable tool for application in cancer molecular imaging.	Cysteine	30-33	potassium voltage-gated channel subfamily H member 2	Homo sapiens	24-29
30110354-3	2018	In contrast, ostruthin inhibited other K+ channels, e.g. human ether-a-go-go-related gene (HERG1), inward-rectifier (Kir2.1), voltage-gated (Kv1.4), and two-pore domain (TASK-1) at higher concentrations, without affecting voltage-gated potassium channel (KCNQ1 and 3).	ostruthin	13-22	potassium voltage-gated channel subfamily H member 2	Homo sapiens	91-96
29617054-10	2018	Telmisartan-mediated prolongation of AP was attenuated in KCNH2 siRNA-transfected HL-1 cells.	Telmisartan	0-11	potassium voltage-gated channel subfamily H member 2	Homo sapiens	58-63
30341381-3	2018	Here we used the voltage-dependent dipicrylamine (DPA)-induced quench of fluorescent proteins (FPS) linked to different positions at the cytoplasmic domains of KCNH2 (hERG) to gain some insights about the coarse structure of these channel parts.	dipicrylamine	35-48	potassium voltage-gated channel subfamily H member 2	Homo sapiens	160-165
30341381-3	2018	Here we used the voltage-dependent dipicrylamine (DPA)-induced quench of fluorescent proteins (FPS) linked to different positions at the cytoplasmic domains of KCNH2 (hERG) to gain some insights about the coarse structure of these channel parts.	dipicrylamine	50-53	potassium voltage-gated channel subfamily H member 2	Homo sapiens	160-165
29875689-7	2018	Nocodazole caused G601S-Kv11.1 protein to distribute into peripheral reticular structures, and it increased the diffuse immunostaining of F805C-Kv11.1 protein around the transitional ER subcompartments.	Nocodazole	0-10	potassium voltage-gated channel subfamily H member 2	Homo sapiens	24-30
29875689-7	2018	Nocodazole caused G601S-Kv11.1 protein to distribute into peripheral reticular structures, and it increased the diffuse immunostaining of F805C-Kv11.1 protein around the transitional ER subcompartments.	Nocodazole	0-10	potassium voltage-gated channel subfamily H member 2	Homo sapiens	144-150
29875689-9	2018	Incubating cells in MG132 minimally impacted G601S-Kv11.1 immunostaining, but it dramatically increased the diffuse immunostaining of F805C-Kv11.1 protein in the transitional ER.	benzyloxycarbonylleucyl-leucyl-leucine aldehyde	20-25	potassium voltage-gated channel subfamily H member 2	Homo sapiens	51-57
29875689-9	2018	Incubating cells in MG132 minimally impacted G601S-Kv11.1 immunostaining, but it dramatically increased the diffuse immunostaining of F805C-Kv11.1 protein in the transitional ER.	benzyloxycarbonylleucyl-leucyl-leucine aldehyde	20-25	potassium voltage-gated channel subfamily H member 2	Homo sapiens	140-146
29650123-8	2018	Intergenotype comparison showed that the risk for patients with LQT2 and LQT3 increased by 130% and 157% at any QTc duration versus patients with LQT1.	qtc	112-115	potassium voltage-gated channel subfamily H member 2	Homo sapiens	64-68
29725305-5	2018	To test our method, we focused on 16 LQT2 mutations in the hERG Per-Arnt-Sim (PAS) domain that were previously studied via a widely used biochemical approach that compares levels of 135-kDa immature and 155-kDa fully glycosylated hERG protein to infer surface expression.	Aminosalicylic Acid	78-81	potassium voltage-gated channel subfamily H member 2	Homo sapiens	37-41
29146210-7	2018	We also examined pharmacological rescue of homozygous mutant Kv11.1 current in cells treated with E-4031 or dofetilide.	E 4031	98-104	potassium voltage-gated channel subfamily H member 2	Homo sapiens	61-67
29146210-7	2018	We also examined pharmacological rescue of homozygous mutant Kv11.1 current in cells treated with E-4031 or dofetilide.	dofetilide	108-118	potassium voltage-gated channel subfamily H member 2	Homo sapiens	61-67
29479853-2	2018	Here, silica, titanium, zinc, and magnesium oxide nanoparticles are screened against human hERG (Kv 11.1) voltage-gated potassium channels under a whole-cell voltage clamp.	Silicon Dioxide	6-12	potassium voltage-gated channel subfamily H member 2	Homo sapiens	97-104
29479853-2	2018	Here, silica, titanium, zinc, and magnesium oxide nanoparticles are screened against human hERG (Kv 11.1) voltage-gated potassium channels under a whole-cell voltage clamp.	Magnesium Oxide	34-49	potassium voltage-gated channel subfamily H member 2	Homo sapiens	97-104
29449809-4	2018	As a proof of principle, we evaluated extensively lipid membrane partitioning of d-sotalol, well-known blocker of a cardiac potassium channel Kv11.1 encoded by the hERG gene, with reported substantial proclivity for arrhythmogenesis.	Dexsotalol	81-90	potassium voltage-gated channel subfamily H member 2	Homo sapiens	142-148
29548277-0	2018	Common variants in the hERG (KCNH2) voltage-gated potassium channel are associated with altered fasting and glucose-stimulated plasma incretin and glucagon responses.	Glucose	108-115	potassium voltage-gated channel subfamily H member 2	Homo sapiens	29-34
29161243-0	2018	The combined activation of KCa3.1 and inhibition of Kv11.1/hERG1 currents contribute to overcome Cisplatin resistance in colorectal cancer cells.	Cisplatin	97-106	potassium voltage-gated channel subfamily H member 2	Homo sapiens	59-64
29203485-4	2018	These quinolines showed high probabilities of Caco2 permeability and human intestinal absorption and low probabilities of mutagenicity and of hERG1 inhibition.	Quinolines	6-16	potassium voltage-gated channel subfamily H member 2	Homo sapiens	142-147
28743763-0	2017	A key role for peroxynitrite-mediated inhibition of cardiac ERG (Kv11.1) K+ channels in carbon monoxide-induced proarrhythmic early afterdepolarizations.	Peroxynitrous Acid	15-28	potassium voltage-gated channel subfamily H member 2	Homo sapiens	65-71
30036649-9	2018	One additional patient had variance of unknown significance (VUS) in KCNH2 and another one in ANK2.	3-[(3~{a}~{S},4~{S},6~{a}~{R})-4-carboxy-2,3,4,5,6,6~{a}-hexahydro-1~{H}-pyrrolo[2,3-c]pyrrol-3~{a}-yl]propyl-$l^{3}-oxidanyl-bis(oxidanyl)boranuide	61-64	potassium voltage-gated channel subfamily H member 2	Homo sapiens	69-74
29255512-12	2017	Conclusions: Atenolol is an effective treatment for genetically proven LQT1 and LQT2 children and adolescents, with good tolerability.	Atenolol	13-21	potassium voltage-gated channel subfamily H member 2	Homo sapiens	80-84
28987271-7	2017	For Kv11.1 channels (hERG1) the extracellularly accessible histidines H578 and H587 are CORM-2 targets.	Histidine	59-69	potassium voltage-gated channel subfamily H member 2	Homo sapiens	4-10
28987271-7	2017	For Kv11.1 channels (hERG1) the extracellularly accessible histidines H578 and H587 are CORM-2 targets.	Histidine	59-69	potassium voltage-gated channel subfamily H member 2	Homo sapiens	21-26
28987271-8	2017	The strong CO-independent action of CORM-2 on Kv11.1 and Kv1.5 channels can be completely abolished when CORM-2 is applied in the presence of an excess of free histidine or human serum albumin; cysteine and methionine are further potential targets.	Histidine	160-169	potassium voltage-gated channel subfamily H member 2	Homo sapiens	46-52
28987271-8	2017	The strong CO-independent action of CORM-2 on Kv11.1 and Kv1.5 channels can be completely abolished when CORM-2 is applied in the presence of an excess of free histidine or human serum albumin; cysteine and methionine are further potential targets.	Cysteine	194-202	potassium voltage-gated channel subfamily H member 2	Homo sapiens	46-52
28987271-8	2017	The strong CO-independent action of CORM-2 on Kv11.1 and Kv1.5 channels can be completely abolished when CORM-2 is applied in the presence of an excess of free histidine or human serum albumin; cysteine and methionine are further potential targets.	Methionine	207-217	potassium voltage-gated channel subfamily H member 2	Homo sapiens	46-52
29089383-5	2017	We report 1) that hERG1a dominant-negative subunits suppress hERG1b currents (and vice versa), 2) that disulfide bonds form between single cysteine residues experimentally introduced into an extracellular loop of hERG1a and hERG1b subunits and produce hERG1a-hERG1b dimers, and 3) that hERG1a and hERG1b subunits tagged with fluorescent proteins that are FRET pairs exhibit robust energy transfer at the plasma membrane.	Disulfides	103-112	potassium voltage-gated channel subfamily H member 2	Homo sapiens	18-23
29089383-5	2017	We report 1) that hERG1a dominant-negative subunits suppress hERG1b currents (and vice versa), 2) that disulfide bonds form between single cysteine residues experimentally introduced into an extracellular loop of hERG1a and hERG1b subunits and produce hERG1a-hERG1b dimers, and 3) that hERG1a and hERG1b subunits tagged with fluorescent proteins that are FRET pairs exhibit robust energy transfer at the plasma membrane.	Cysteine	139-147	potassium voltage-gated channel subfamily H member 2	Homo sapiens	18-23
28150511-8	2017	Since tadalafil blocks hERG1 K channels in concentration dependent manner, the cardiotoxicity prediction of the hit molecules was also tested.	Tadalafil	6-15	potassium voltage-gated channel subfamily H member 2	Homo sapiens	23-28
28743763-9	2017	CO also raised ONOO- levels, an effect that was reversed by the ONOO- scavenger, FeTPPS [5,10,15,20-tetrakis-(4-sulfonatophenyl)-porphyrinato-iron(III)], which also prevented the CO inhibition of Kv11.1 currents and abolished the effects of CO on Kv11.1 tail currents and APs in guinea pig myocytes.	onoo	64-68	potassium voltage-gated channel subfamily H member 2	Homo sapiens	196-202
28743763-9	2017	CO also raised ONOO- levels, an effect that was reversed by the ONOO- scavenger, FeTPPS [5,10,15,20-tetrakis-(4-sulfonatophenyl)-porphyrinato-iron(III)], which also prevented the CO inhibition of Kv11.1 currents and abolished the effects of CO on Kv11.1 tail currents and APs in guinea pig myocytes.	onoo	64-68	potassium voltage-gated channel subfamily H member 2	Homo sapiens	247-253
28743763-0	2017	A key role for peroxynitrite-mediated inhibition of cardiac ERG (Kv11.1) K+ channels in carbon monoxide-induced proarrhythmic early afterdepolarizations.	Carbon Monoxide	88-103	potassium voltage-gated channel subfamily H member 2	Homo sapiens	65-71
28743763-9	2017	CO also raised ONOO- levels, an effect that was reversed by the ONOO- scavenger, FeTPPS [5,10,15,20-tetrakis-(4-sulfonatophenyl)-porphyrinato-iron(III)], which also prevented the CO inhibition of Kv11.1 currents and abolished the effects of CO on Kv11.1 tail currents and APs in guinea pig myocytes.	fetpps	81-87	potassium voltage-gated channel subfamily H member 2	Homo sapiens	196-202
28743763-9	2017	CO also raised ONOO- levels, an effect that was reversed by the ONOO- scavenger, FeTPPS [5,10,15,20-tetrakis-(4-sulfonatophenyl)-porphyrinato-iron(III)], which also prevented the CO inhibition of Kv11.1 currents and abolished the effects of CO on Kv11.1 tail currents and APs in guinea pig myocytes.	fetpps	81-87	potassium voltage-gated channel subfamily H member 2	Homo sapiens	247-253
29059199-8	2017	Among the beta-blockers, nadolol showed a significant risk reduction in both LQT1 and LQT2 (HR 0.47 and 0.27, respectively), whereas atenolol and propranolol decreased the risk only in LQT1 (HR 0.36 and 0.46, respectively).	Nadolol	25-32	potassium voltage-gated channel subfamily H member 2	Homo sapiens	86-90
28743763-9	2017	CO also raised ONOO- levels, an effect that was reversed by the ONOO- scavenger, FeTPPS [5,10,15,20-tetrakis-(4-sulfonatophenyl)-porphyrinato-iron(III)], which also prevented the CO inhibition of Kv11.1 currents and abolished the effects of CO on Kv11.1 tail currents and APs in guinea pig myocytes.	15,20-tetrakis-(4-sulfonatophenyl)-porphyrinato-iron	94-146	potassium voltage-gated channel subfamily H member 2	Homo sapiens	196-202
28768059-0	2017	(-)-Epicatechin rescues the As2 O3 -induced HERG K+ channel deficiency possibly through upregulating transcription factor SP1 expression.	Catechin	0-15	potassium voltage-gated channel subfamily H member 2	Homo sapiens	44-48
28768059-0	2017	(-)-Epicatechin rescues the As2 O3 -induced HERG K+ channel deficiency possibly through upregulating transcription factor SP1 expression.	Aligeron	28-31	potassium voltage-gated channel subfamily H member 2	Homo sapiens	44-48
28768059-5	2017	However, As2 O3 can induce the deficiency of HERG channel and cause LQT2.	Arsenic Trioxide	9-15	potassium voltage-gated channel subfamily H member 2	Homo sapiens	68-72
28768059-8	2017	EPI was able to recover the protein expression and current of HERG channel disrupted by As2 O3 .	Arsenic Trioxide	88-94	potassium voltage-gated channel subfamily H member 2	Homo sapiens	62-66
29059199-12	2017	Among them, nadolol was effective in LQT1 and LQT2, whereas other drugs showed different effectiveness depending on LQT genotype.	Nadolol	12-19	potassium voltage-gated channel subfamily H member 2	Homo sapiens	46-50
28705808-0	2017	Molecular Basis of Altered hERG1 Channel Gating Induced by Ginsenoside Rg3.	Ginsenosides	59-70	potassium voltage-gated channel subfamily H member 2	Homo sapiens	27-32
27581752-4	2017	Patch clamp experiments showed that the IC50 values of the human ether-a-go-go-related gene (hERG1) potassium (K) ion channel blocking affinity of PDE5 inhibitors sildenafil, vardenafil, and tadalafil as 33, 12, and 100 muM, respectively.	Sildenafil Citrate	163-173	potassium voltage-gated channel subfamily H member 2	Homo sapiens	93-98
27581752-4	2017	Patch clamp experiments showed that the IC50 values of the human ether-a-go-go-related gene (hERG1) potassium (K) ion channel blocking affinity of PDE5 inhibitors sildenafil, vardenafil, and tadalafil as 33, 12, and 100 muM, respectively.	Vardenafil Dihydrochloride	175-185	potassium voltage-gated channel subfamily H member 2	Homo sapiens	93-98
27581752-4	2017	Patch clamp experiments showed that the IC50 values of the human ether-a-go-go-related gene (hERG1) potassium (K) ion channel blocking affinity of PDE5 inhibitors sildenafil, vardenafil, and tadalafil as 33, 12, and 100 muM, respectively.	Tadalafil	191-200	potassium voltage-gated channel subfamily H member 2	Homo sapiens	93-98
28705808-7	2017	Mutation to Ala of specific residues in the S1 (Tyr420), S2 (Leu452, Phe463), and S4 (Ile521, Lys525) segments partially inhibited the effects of Rg3 on hERG1.	Alanine	12-15	potassium voltage-gated channel subfamily H member 2	Homo sapiens	153-158
28800628-1	2017	Many drugs used for non-cardiovascular and cardiovascular purposes, such as sotalol, have the side effect of prolonging cardiac repolarization, which can trigger life-threatening cardiac arrhythmias by inhibiting the potassium-channel IKr (KCNH2).	Sotalol	76-83	potassium voltage-gated channel subfamily H member 2	Homo sapiens	240-245
29264083-5	2017	Paroxetine blocks the human ether-a-go-go-related gene (HERG) channels.	Paroxetine	0-10	potassium voltage-gated channel subfamily H member 2	Homo sapiens	56-60
28963955-0	2017	Structural investigation of vesnarinone at the pore domains of open and open-inactivated states of hERG1 K+ channel.	vesnarinone	28-39	potassium voltage-gated channel subfamily H member 2	Homo sapiens	99-104
28963955-1	2017	In this study, the dynamics of vesnarinone bounded hERG1 K+ channels are investigated using in silico approaches such as molecular docking, molecular dynamics (MD) simulations, MM/PBSA (Molecular Mechanics/Poisson Boltzmann Surface Area) calculations and Principal Component Analysis (PCA).	vesnarinone	31-42	potassium voltage-gated channel subfamily H member 2	Homo sapiens	51-56
28593575-5	2017	Here, we investigated the role of ether-a-go-go-related 1 (hERG1) ion channels in the EMT of colorectal cancer cells.	Ether	34-39	potassium voltage-gated channel subfamily H member 2	Homo sapiens	59-64
27466471-6	2016	In contrast, mutations in the cyclic nucleotide binding domain (cNBD) of KCNH2 conferred a negative risk of seizures, but not arrhythmias.	Nucleotides, Cyclic	30-47	potassium voltage-gated channel subfamily H member 2	Homo sapiens	73-78
28500657-0	2017	Modulation of Kv 11.1 (hERG) channels by 5-(((1H-indazol-5-yl)oxy)methyl)-N-(4-(trifluoromethoxy)phenyl)pyrimidin-2-amine (ITP-2), a novel small molecule activator.	5-(((1h-indazol-5-yl)oxy)methyl)-n-(4-(trifluoromethoxy)phenyl)pyrimidin-2-amine	41-121	potassium voltage-gated channel subfamily H member 2	Homo sapiens	14-21
28500657-0	2017	Modulation of Kv 11.1 (hERG) channels by 5-(((1H-indazol-5-yl)oxy)methyl)-N-(4-(trifluoromethoxy)phenyl)pyrimidin-2-amine (ITP-2), a novel small molecule activator.	itp-2	123-128	potassium voltage-gated channel subfamily H member 2	Homo sapiens	14-21
28632743-4	2017	Therefore, this study aimed to assess the potential effects of E-4031, disopyramide and quinidine on SQT1 using a mathematical model of human ventricular electrophysiology.	E 4031	63-69	potassium voltage-gated channel subfamily H member 2	Homo sapiens	101-105
28632743-4	2017	Therefore, this study aimed to assess the potential effects of E-4031, disopyramide and quinidine on SQT1 using a mathematical model of human ventricular electrophysiology.	Quinidine	88-97	potassium voltage-gated channel subfamily H member 2	Homo sapiens	101-105
28632743-15	2017	Quinidine exhibited significantly better therapeutic effects on SQT1 than E-4031 and disopyramide.	Quinidine	0-9	potassium voltage-gated channel subfamily H member 2	Homo sapiens	64-68
28632743-16	2017	CONCLUSIONS: The simulated pharmacological actions of quinidine exhibited antiarrhythmic effects on SQT1.	Quinidine	54-63	potassium voltage-gated channel subfamily H member 2	Homo sapiens	100-104
28632743-17	2017	This study substantiates a causal link between quinidine and QT interval prolongation in SQT1 and suggests that quinidine may be a potential pharmacological agent for treating SQT1 patients.	Quinidine	47-56	potassium voltage-gated channel subfamily H member 2	Homo sapiens	89-93
28632743-17	2017	This study substantiates a causal link between quinidine and QT interval prolongation in SQT1 and suggests that quinidine may be a potential pharmacological agent for treating SQT1 patients.	Quinidine	47-56	potassium voltage-gated channel subfamily H member 2	Homo sapiens	176-180
28632743-17	2017	This study substantiates a causal link between quinidine and QT interval prolongation in SQT1 and suggests that quinidine may be a potential pharmacological agent for treating SQT1 patients.	Quinidine	112-121	potassium voltage-gated channel subfamily H member 2	Homo sapiens	89-93
28632743-17	2017	This study substantiates a causal link between quinidine and QT interval prolongation in SQT1 and suggests that quinidine may be a potential pharmacological agent for treating SQT1 patients.	Quinidine	112-121	potassium voltage-gated channel subfamily H member 2	Homo sapiens	176-180
28525371-0	2017	Arsenic trioxide and angiotensin II have inhibitory effects on HERG protein expression: Evidence for the role of PML SUMOylation.	Arsenic Trioxide	0-16	potassium voltage-gated channel subfamily H member 2	Homo sapiens	63-67
28525371-3	2017	Both arsenic trioxide (ATO) and angiotensin II (Ang II) were able to significantly reduce HERG protein expression, while also increasing PML SUMOylation and accelerating the formation of PML-NBs.	Arsenic Trioxide	5-21	potassium voltage-gated channel subfamily H member 2	Homo sapiens	90-94
28525371-3	2017	Both arsenic trioxide (ATO) and angiotensin II (Ang II) were able to significantly reduce HERG protein expression, while also increasing PML SUMOylation and accelerating the formation of PML-NBs.	Arsenic Trioxide	23-26	potassium voltage-gated channel subfamily H member 2	Homo sapiens	90-94
28525371-4	2017	Pre-exposure of cardiomyocytes to a SUMOylation chemical inhibitor, ginkgolic acid, or the silencing of UBC9 suppressed PML SUMOylation, subsequently preventing the downregulation of HERG induced by ATO or Ang II.	ginkgolic acid	68-82	potassium voltage-gated channel subfamily H member 2	Homo sapiens	183-187
27394160-14	2016	CONCLUSIONS: Bisoprolol treatment results in QTc shortening in gene-positive LQT1 and LQT2 patients and is well tolerated during long-term administration.	Bisoprolol	13-23	potassium voltage-gated channel subfamily H member 2	Homo sapiens	86-90
27761169-9	2016	The proteasome inhibitor MG132 increased the expression of immature A78T-HERG and increased both the immature and mature forms of WT-HERG.	benzyloxycarbonylleucyl-leucyl-leucine aldehyde	25-30	potassium voltage-gated channel subfamily H member 2	Homo sapiens	73-77
27761169-9	2016	The proteasome inhibitor MG132 increased the expression of immature A78T-HERG and increased both the immature and mature forms of WT-HERG.	benzyloxycarbonylleucyl-leucyl-leucine aldehyde	25-30	potassium voltage-gated channel subfamily H member 2	Homo sapiens	133-137
27761169-13	2016	Maturation of the A78T-HERG protein was facilitated by HS, expression of HSF-1, or exposure to geranyl geranyl acetone.	geranylgeranylacetone	95-118	potassium voltage-gated channel subfamily H member 2	Homo sapiens	23-27
27517748-10	2016	Finally, a novel fluorophore- conjugated recombinant single chain variable fragment antibody (scFv-hERG1-Alexa488) was tested on freshly collected live BE biopsies: it could recognize hERG1 positive samples, perfectly matching IHC data.Overall, hERG1 can be considered a novel BE biomarker to be exploited for a novel endoscopic surveillance protocol, either in biopsies or through endoscopy, to identify those BE patients with higher risk to progress to EA.	alexa488	105-113	potassium voltage-gated channel subfamily H member 2	Homo sapiens	184-189
27502018-1	2016	Ginsenoside 20(S)-Rg3 (Rg3) is a steroid glycoside that induces human ether-a-go-go-related gene type 1 (hERG1, Kv11.1) channels to activate at more negative potentials and to deactivate more slowly than normal.	Ginsenosides	0-11	potassium voltage-gated channel subfamily H member 2	Homo sapiens	105-110
27502018-1	2016	Ginsenoside 20(S)-Rg3 (Rg3) is a steroid glycoside that induces human ether-a-go-go-related gene type 1 (hERG1, Kv11.1) channels to activate at more negative potentials and to deactivate more slowly than normal.	Ginsenosides	0-11	potassium voltage-gated channel subfamily H member 2	Homo sapiens	112-118
27502018-1	2016	Ginsenoside 20(S)-Rg3 (Rg3) is a steroid glycoside that induces human ether-a-go-go-related gene type 1 (hERG1, Kv11.1) channels to activate at more negative potentials and to deactivate more slowly than normal.	steroid glycoside	33-50	potassium voltage-gated channel subfamily H member 2	Homo sapiens	105-110
27502018-1	2016	Ginsenoside 20(S)-Rg3 (Rg3) is a steroid glycoside that induces human ether-a-go-go-related gene type 1 (hERG1, Kv11.1) channels to activate at more negative potentials and to deactivate more slowly than normal.	steroid glycoside	33-50	potassium voltage-gated channel subfamily H member 2	Homo sapiens	112-118
27517748-10	2016	Finally, a novel fluorophore- conjugated recombinant single chain variable fragment antibody (scFv-hERG1-Alexa488) was tested on freshly collected live BE biopsies: it could recognize hERG1 positive samples, perfectly matching IHC data.Overall, hERG1 can be considered a novel BE biomarker to be exploited for a novel endoscopic surveillance protocol, either in biopsies or through endoscopy, to identify those BE patients with higher risk to progress to EA.	alexa488	105-113	potassium voltage-gated channel subfamily H member 2	Homo sapiens	99-104
27517748-10	2016	Finally, a novel fluorophore- conjugated recombinant single chain variable fragment antibody (scFv-hERG1-Alexa488) was tested on freshly collected live BE biopsies: it could recognize hERG1 positive samples, perfectly matching IHC data.Overall, hERG1 can be considered a novel BE biomarker to be exploited for a novel endoscopic surveillance protocol, either in biopsies or through endoscopy, to identify those BE patients with higher risk to progress to EA.	alexa488	105-113	potassium voltage-gated channel subfamily H member 2	Homo sapiens	184-189
26887900-8	2016	Following LCSD, there was a 57 +- 35 ms decrease in QTc in LQT1 (P = .16) and 23 +- 21 ms decrease in QTc in LQT2 (P = .3).	lcsd	10-14	potassium voltage-gated channel subfamily H member 2	Homo sapiens	109-113
25945833-4	2016	We have demonstrated that the Kv11.1 channel activator NS1643 activates a calcineurin-dependent transcription of p21waf/cip and that this event is fundamental for the inhibitory effect of NS1643 on cell proliferation.	1,3-bis(2-hydroxy-5-trifluoromethylphenyl)urea	55-61	potassium voltage-gated channel subfamily H member 2	Homo sapiens	30-36
25945833-4	2016	We have demonstrated that the Kv11.1 channel activator NS1643 activates a calcineurin-dependent transcription of p21waf/cip and that this event is fundamental for the inhibitory effect of NS1643 on cell proliferation.	1,3-bis(2-hydroxy-5-trifluoromethylphenyl)urea	188-194	potassium voltage-gated channel subfamily H member 2	Homo sapiens	30-36
26887900-8	2016	Following LCSD, there was a 57 +- 35 ms decrease in QTc in LQT1 (P = .16) and 23 +- 21 ms decrease in QTc in LQT2 (P = .3).	qtc	102-105	potassium voltage-gated channel subfamily H member 2	Homo sapiens	109-113
27190211-7	2016	Here we present the first complete study of the temperature-dependent kinetics of block and unblock of a proarrhythmic drug, cisapride, to KV11.1.	Cisapride	125-134	potassium voltage-gated channel subfamily H member 2	Homo sapiens	139-145
27555138-2	2016	We describe a case of torsade de pointes (TdP) caused by sevoflurane in a patient with c-LQTS genotype 2 (LQT2).	Sevoflurane	57-68	potassium voltage-gated channel subfamily H member 2	Homo sapiens	87-104
27555138-2	2016	We describe a case of torsade de pointes (TdP) caused by sevoflurane in a patient with c-LQTS genotype 2 (LQT2).	Sevoflurane	57-68	potassium voltage-gated channel subfamily H member 2	Homo sapiens	106-110
27555138-6	2016	Analysis of the electrocardiogram revealed that the corrected QT interval before anesthesia was 530 ms and 2.0% sevoflurane markedly prolonged the corrected QT interval to 693 ms. Postoperative studies revealed a mutation in the KCNH2 gene.	Sevoflurane	112-123	potassium voltage-gated channel subfamily H member 2	Homo sapiens	229-234
26022375-7	2016	Later, genetic analysis demonstrated that this patient had a mutation in KCNH2 gene, and she was diagnosed as a type-2 long-QT syndrome which was accentuated by use of garenoxacin.	garenoxacin	168-179	potassium voltage-gated channel subfamily H member 2	Homo sapiens	73-78