PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
23353701-7	2013	In agreement with these data, the exogenous treatment of SAH or inhibition of SAHH by specific siRNA or another type of inhibitor, 3-deazaadenosine (DAZA), similarly resulted in antitumorigenic responses, suppressive activity on Src, the alteration of actin cytoskeleton, and a change of the colocalization pattern between actin and Src.	3-deazaadenosine	131-147	adenosylhomocysteinase	Homo sapiens	78-82	
23994169-7	2013	Furthermore, we found that suppression of SAHH by siRNA and 3-deazaadenosine, knock down of isoprenylcysteine carboxyl methyltransferase (ICMT), and treatment with SAH showed inhibitory patterns similar to those of AdOx.	3-deazaadenosine	60-76	adenosylhomocysteinase	Homo sapiens	42-46	
23353701-7	2013	In agreement with these data, the exogenous treatment of SAH or inhibition of SAHH by specific siRNA or another type of inhibitor, 3-deazaadenosine (DAZA), similarly resulted in antitumorigenic responses, suppressive activity on Src, the alteration of actin cytoskeleton, and a change of the colocalization pattern between actin and Src.	3-deazaadenosine	149-153	adenosylhomocysteinase	Homo sapiens	78-82	
1586132-1	1992	Red blood cell S-adenosylhomocysteine hydrolase (AHCY) from individuals of 1, 2-1 and 3-1 phenotypes was partially purified and Km and Vmax determined in the absence and in the presence of the following inhibitors: 3-deaza-adenosine (DZA), 3-deaza-aristeromycin (DZAry), 2-chloro adenosine (2-Cl-ado) and purine riboside (or nebularine).	3-deazaadenosine	234-237	adenosylhomocysteinase	Homo sapiens	49-53	
12910461-3	2003	Even though the expressed recombinant enzyme, PfSAHH, could use 3-deaza-adenosine (DZA) as an alternative substrate in contrast to the human SAHH, it has a unique inability to substitute 3-deaza-(+/-)aristeromycin (DZAri) for adenosine.	3-deazaadenosine	64-81	adenosylhomocysteinase	Homo sapiens	48-52	
12910461-3	2003	Even though the expressed recombinant enzyme, PfSAHH, could use 3-deaza-adenosine (DZA) as an alternative substrate in contrast to the human SAHH, it has a unique inability to substitute 3-deaza-(+/-)aristeromycin (DZAri) for adenosine.	3-deazaadenosine	83-86	adenosylhomocysteinase	Homo sapiens	48-52	
9920939-3	1999	Sodium reabsorption was decreased within 2 h by 3-deazaadenosine, a competitive inhibitor of SAHHase, with a half inhibitory concentration between 40 and 50 microM.	3-deazaadenosine	48-64	adenosylhomocysteinase	Homo sapiens	93-100	
8206944-7	1994	Transformed E. coli cells produce a protein with a relative molecular weight of 56,000 which possesses SAHH activity as evidenced by the conversion of 3-deazaadenosine to S-3-deazaadenosylhomocysteine.	3-deazaadenosine	151-167	adenosylhomocysteinase	Homo sapiens	103-107	
1537874-2	1992	3-Deazaadenosine analogs can function as inhibitors and also as alternative substrates of S-adenosylhomocysteine (AdoHcy) hydrolase.	3-deazaadenosine	0-16	adenosylhomocysteinase	Homo sapiens	90-131	
1375133-7	1992	With 3-deaza-adenosine, which is not incorporated into DNA but produces DNA hypomethylation through inhibition of S-adenosylhomocysteine hydrolase, a primarily antagonistic interaction was observed in the two cell lines studied.	3-deazaadenosine	5-22	adenosylhomocysteinase	Homo sapiens	114-146	
1586132-1	1992	Red blood cell S-adenosylhomocysteine hydrolase (AHCY) from individuals of 1, 2-1 and 3-1 phenotypes was partially purified and Km and Vmax determined in the absence and in the presence of the following inhibitors: 3-deaza-adenosine (DZA), 3-deaza-aristeromycin (DZAry), 2-chloro adenosine (2-Cl-ado) and purine riboside (or nebularine).	3-deazaadenosine	215-232	adenosylhomocysteinase	Homo sapiens	15-47	
1586132-1	1992	Red blood cell S-adenosylhomocysteine hydrolase (AHCY) from individuals of 1, 2-1 and 3-1 phenotypes was partially purified and Km and Vmax determined in the absence and in the presence of the following inhibitors: 3-deaza-adenosine (DZA), 3-deaza-aristeromycin (DZAry), 2-chloro adenosine (2-Cl-ado) and purine riboside (or nebularine).	3-deazaadenosine	215-232	adenosylhomocysteinase	Homo sapiens	49-53	
33035507-0	2020	3-Deazaadenosine, an S-adenosylhomocysteine hydrolase inhibitor, attenuates lipopolysaccharide-induced inflammatory responses via inhibition of AP-1 and NF-kappaB signaling.	3-deazaadenosine	0-16	adenosylhomocysteinase	Homo sapiens	21-53