PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
28888661-5	2017	The primary SAR study showed that restricting the conformation of the catechol moiety in rolipram with the scaffold of oxazolidinone-fused tetrahydroisoquinoline could lead to an increase in selectivity for PDE4B over PDE4D, which was consistent with the observed docking simulation.	catechol	70-78	phosphodiesterase 4B	Homo sapiens	207-212	
26320621-3	2015	The docking results showed that the catechol diether moiety of compound 8 played a key role to form integral hydrogen bonds with PDE4B protein while the rest part of the molecule extended into the catalytic domain to block the access of cAMP and formed the foundation for inhibition of PDE4.	catechol	36-44	phosphodiesterase 4B	Homo sapiens	129-134