PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
19853000-7	2010	Interestingly, the chemical structure of specific pyrethroid metabolites indicates that they may be more likely to interact with the estrogen receptor than the parent compounds.	Pyrethrins	50-60	estrogen receptor 1	Homo sapiens	133-150	
12396874-6	2002	In addition, pyrethroid pesticides inhibited the binding of [3H]estradiol to ER, while the organophosphorus failed to do so.	Pyrethrins	13-23	estrogen receptor 1	Homo sapiens	77-79	
16395479-3	2006	It has been noted that some metabolites of pyrethroids, in particular, permethrin and cypermethrin, have chemical structures that are more likely to interact with the cellular estrogen receptor than the parent pyrethroid.	Pyrethrins	43-54	estrogen receptor 1	Homo sapiens	176-193	
16395479-3	2006	It has been noted that some metabolites of pyrethroids, in particular, permethrin and cypermethrin, have chemical structures that are more likely to interact with the cellular estrogen receptor than the parent pyrethroid.	Pyrethrins	43-53	estrogen receptor 1	Homo sapiens	176-193	
16395479-7	2006	The results from this study show that pyrethroid metabolites are capable of interacting with the human estrogen receptor, and so might present a risk to human health and environmental well being.	Pyrethrins	38-48	estrogen receptor 1	Homo sapiens	103-120	
12396874-8	2002	Our findings provide evidence to support the idea that pyrethroid pesticides tested produce an ER-specific, agonist response.	Pyrethrins	55-65	estrogen receptor 1	Homo sapiens	95-97	
35588686-4	2022	To investigate the reproductive toxicity of pyrethroids, homology modeling, molecular docking, molecular dynamic simulations (MDs) were conducted to explore the interaction between pyrethroids and ERalpha from atomic scale.	Pyrethrins	44-55	estrogen receptor 1	Homo sapiens	197-204