PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
209007-2	1978	It was observed that substitution at N1 or N2 with a bulky alkyl group or cyclic phosphorylation of the ribose moiety made formycin resistant to adenosine deaminase.	Ribose	104-110	adenosine deaminase	Homo sapiens	145-164	
12057661-4	2002	In these substrates the fused cyclopropane moiety constrains the cyclopentane ring to mimic the conformation of a furanose sugar in the North hemisphere of the pseudorotational cycle, which matches the conformation of the ribose ring of adenosine in complex with ADA.	Ribose	222-228	adenosine deaminase	Homo sapiens	263-266	
19361992-0	2009	Enhanced activity or resistance of adenosine derivatives towards adenosine deaminase-catalyzed deamination: Influence of ribose modifications.	Ribose	121-127	adenosine deaminase	Homo sapiens	65-84	
8485104-3	1993	Adenosine deaminase is found to bind more strongly to compound I than to compound II, therefore compound I is a stronger inhibitor than II, because the position of (5") OH on the ribose moiety decreases the inhibitory strength on the ring opened analogue.	Ribose	179-185	adenosine deaminase	Homo sapiens	0-19	
1504093-2	1992	The specificity of the yeast enzyme is more restricted than that of mammalian adenosine deaminase, particularly towards the ribose moiety and around position 6 and 1 of the substrate.	Ribose	124-130	adenosine deaminase	Homo sapiens	78-97