PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
21994697-3	2010	The major proline substrates are located in domain II of NS5A, centered around a "DY" dipeptide motif that regulates CyPA dependence and CsA resistance.	Dipeptides	86-95	peptidylprolyl isomerase A	Homo sapiens	117-121	
9223641-6	1997	The energetic contributions to CypA binding were quantified for each residue in this loop, and the results demonstrate that the Gly89-Pro90 dipeptide is the primary cyclophilin A recognition motif, with Pro85, Val86, His87, Ala88, and Pro93 also making energetically favorable contacts.	Dipeptides	140-149	peptidylprolyl isomerase A	Homo sapiens	31-35	
9223641-6	1997	The energetic contributions to CypA binding were quantified for each residue in this loop, and the results demonstrate that the Gly89-Pro90 dipeptide is the primary cyclophilin A recognition motif, with Pro85, Val86, His87, Ala88, and Pro93 also making energetically favorable contacts.	Dipeptides	140-149	peptidylprolyl isomerase A	Homo sapiens	165-178	
20886100-5	2010	Five independent selections revealed related mutations in a single dipeptide motif (D316 and Y317) located in a proline-rich region of NS5A domain II, which has been implicated in CyPA binding.	Dipeptides	67-76	peptidylprolyl isomerase A	Homo sapiens	180-184	
8075981-6	1994	Comparison of these structures with previously determined structures of unligated CyPA and CyPA complexed with a candidate substrate for the isomerase activity, the dipeptide AlaPro, reveals that subtle conformational changes occur in both CsA and CyPA on complex formation.	Dipeptides	165-174	peptidylprolyl isomerase A	Homo sapiens	82-86	
8075981-6	1994	Comparison of these structures with previously determined structures of unligated CyPA and CyPA complexed with a candidate substrate for the isomerase activity, the dipeptide AlaPro, reveals that subtle conformational changes occur in both CsA and CyPA on complex formation.	Dipeptides	165-174	peptidylprolyl isomerase A	Homo sapiens	91-95	
8075981-6	1994	Comparison of these structures with previously determined structures of unligated CyPA and CyPA complexed with a candidate substrate for the isomerase activity, the dipeptide AlaPro, reveals that subtle conformational changes occur in both CsA and CyPA on complex formation.	Dipeptides	165-174	peptidylprolyl isomerase A	Homo sapiens	91-95