PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
35379233-10	2022	Protein structure analysis also revealed that the variant probably leads to the deletion of DHH (Asp-His-His) domain, the active site of the protein, and loss of PRUNE1 function.	2-(3,5-dihydroxyphenyl)-6-hydroxybenzothiazole	97-104	desert hedgehog signaling molecule	Homo sapiens	92-95	
29203646-1	2018	The Asp-His-His and Asp-His-His-associated (DHH/DHHA1) domain-containing phosphodiesterases (PDEs) that catalyze degradation of cyclic di-adenosine monophosphate (c-di-AMP) could be subdivided into two subfamilies based on the final product [5"-phosphadenylyl-adenosine (5"-pApA) or AMP].	2-(3,5-dihydroxyphenyl)-6-hydroxybenzothiazole	4-11	desert hedgehog signaling molecule	Homo sapiens	44-47	
29203646-1	2018	The Asp-His-His and Asp-His-His-associated (DHH/DHHA1) domain-containing phosphodiesterases (PDEs) that catalyze degradation of cyclic di-adenosine monophosphate (c-di-AMP) could be subdivided into two subfamilies based on the final product [5"-phosphadenylyl-adenosine (5"-pApA) or AMP].	2-(3,5-dihydroxyphenyl)-6-hydroxybenzothiazole	20-27	desert hedgehog signaling molecule	Homo sapiens	44-47	
17655525-3	2007	H-Prune shows no sequence similarity with known mammalian PDEs, but instead appears to belong to the DHH (Asp-His-His) superfamily of phosphoesterases.	2-(3,5-dihydroxyphenyl)-6-hydroxybenzothiazole	106-113	desert hedgehog signaling molecule	Homo sapiens	101-104