PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
9380739-1	1997	HIV-1 specifically incorporates the peptidyl prolyl isomerase cyclophilin A (CyPA), the cytosolic receptor for the immunosuppressant cyclosporin A (CsA).	Cyclosporine	148-151	peptidylprolyl isomerase A	Homo sapiens	62-75	
9380739-1	1997	HIV-1 specifically incorporates the peptidyl prolyl isomerase cyclophilin A (CyPA), the cytosolic receptor for the immunosuppressant cyclosporin A (CsA).	Cyclosporine	148-151	peptidylprolyl isomerase A	Homo sapiens	77-81	
9380739-2	1997	HIV-1 replication is inhibited by CsA as well as by nonimmunosuppressive CsA analogues that bind to CyPA and interfere with its virion association.	Cyclosporine	73-76	peptidylprolyl isomerase A	Homo sapiens	100-104	
9380739-5	1997	We report here that the transfer of HIV-1 CA residues 86-93, which form part of an exposed loop, to the corresponding position in SIVmac resulted in the efficient incorporation of CyPA and conferred an HIV-1-like sensitivity to a nonimmunosuppressive cyclosporin.	Cyclosporine	251-262	peptidylprolyl isomerase A	Homo sapiens	180-184	
9380739-9	1997	By demonstrating that CyPA-binding-site residues can induce cyclosporin sensitivity in a heterologous context, this study provides direct in vivo evidence that the exposed loop between helices IV and V of HIV-1 CA not merely constitutes a docking site for CyPA but is a functional target of this cellular protein.	Cyclosporine	60-71	peptidylprolyl isomerase A	Homo sapiens	22-26	
9380739-9	1997	By demonstrating that CyPA-binding-site residues can induce cyclosporin sensitivity in a heterologous context, this study provides direct in vivo evidence that the exposed loop between helices IV and V of HIV-1 CA not merely constitutes a docking site for CyPA but is a functional target of this cellular protein.	Cyclosporine	60-71	peptidylprolyl isomerase A	Homo sapiens	256-260