PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
15901787-7	2005	Using the differential sensitivity of KCNQ3 and KCNQ1 to retigabine, we constructed chimeras to identify minimal segments required for sensitivity to the drug.	ezogabine	57-67	potassium voltage-gated channel subfamily Q member 1	Homo sapiens	48-53	
15901787-10	2005	Transfer of the tryptophan into the KCNQ1 scaffold resulted in retigabine-sensitive heteromers, suggesting that the tryptophan is necessary in all KCNQ subunits forming a functional tetramer to confer drug sensitivity.	ezogabine	63-73	potassium voltage-gated channel subfamily Q member 1	Homo sapiens	36-41	
22135213-5	2012	The M-type current was activated by 1) 10 muM retigabine, an opener of all KCNQ channels except KCNQ1, 2) 10 muM zinc pyrithione, which augments all KCNQ channels except KCNQ3, and 3) 50 muM N-ethylmaleimide, which activates KCNQ2, KCNQ4, and KCNQ5, but not KCNQ1 or KCNQ3, channels.	ezogabine	46-56	potassium voltage-gated channel subfamily Q member 1	Homo sapiens	96-112	
22135213-5	2012	The M-type current was activated by 1) 10 muM retigabine, an opener of all KCNQ channels except KCNQ1, 2) 10 muM zinc pyrithione, which augments all KCNQ channels except KCNQ3, and 3) 50 muM N-ethylmaleimide, which activates KCNQ2, KCNQ4, and KCNQ5, but not KCNQ1 or KCNQ3, channels.	ezogabine	46-56	potassium voltage-gated channel subfamily Q member 1	Homo sapiens	96-101	
22220513-5	2012	Furthermore, mutagenesis and modeling studies have pinpointed the RTG/EZG binding site to a hydrophobic pocket near the channel gate, indicating how RTG/EZG can stabilize the open form of KCNQ2-5 channels; the absence of this site in KCNQ1 also provides a clear explanation for the inbuilt selectivity RTG/EZG has for potassium channels other than the KCNQ cardiac channel.	ezogabine	66-69	potassium voltage-gated channel subfamily Q member 1	Homo sapiens	234-239	
22220513-5	2012	Furthermore, mutagenesis and modeling studies have pinpointed the RTG/EZG binding site to a hydrophobic pocket near the channel gate, indicating how RTG/EZG can stabilize the open form of KCNQ2-5 channels; the absence of this site in KCNQ1 also provides a clear explanation for the inbuilt selectivity RTG/EZG has for potassium channels other than the KCNQ cardiac channel.	ezogabine	70-73	potassium voltage-gated channel subfamily Q member 1	Homo sapiens	234-239	
22220513-5	2012	Furthermore, mutagenesis and modeling studies have pinpointed the RTG/EZG binding site to a hydrophobic pocket near the channel gate, indicating how RTG/EZG can stabilize the open form of KCNQ2-5 channels; the absence of this site in KCNQ1 also provides a clear explanation for the inbuilt selectivity RTG/EZG has for potassium channels other than the KCNQ cardiac channel.	ezogabine	149-152	potassium voltage-gated channel subfamily Q member 1	Homo sapiens	234-239	
22220513-5	2012	Furthermore, mutagenesis and modeling studies have pinpointed the RTG/EZG binding site to a hydrophobic pocket near the channel gate, indicating how RTG/EZG can stabilize the open form of KCNQ2-5 channels; the absence of this site in KCNQ1 also provides a clear explanation for the inbuilt selectivity RTG/EZG has for potassium channels other than the KCNQ cardiac channel.	ezogabine	153-156	potassium voltage-gated channel subfamily Q member 1	Homo sapiens	234-239	
22220513-5	2012	Furthermore, mutagenesis and modeling studies have pinpointed the RTG/EZG binding site to a hydrophobic pocket near the channel gate, indicating how RTG/EZG can stabilize the open form of KCNQ2-5 channels; the absence of this site in KCNQ1 also provides a clear explanation for the inbuilt selectivity RTG/EZG has for potassium channels other than the KCNQ cardiac channel.	ezogabine	149-152	potassium voltage-gated channel subfamily Q member 1	Homo sapiens	234-239	
22220513-5	2012	Furthermore, mutagenesis and modeling studies have pinpointed the RTG/EZG binding site to a hydrophobic pocket near the channel gate, indicating how RTG/EZG can stabilize the open form of KCNQ2-5 channels; the absence of this site in KCNQ1 also provides a clear explanation for the inbuilt selectivity RTG/EZG has for potassium channels other than the KCNQ cardiac channel.	ezogabine	153-156	potassium voltage-gated channel subfamily Q member 1	Homo sapiens	234-239