PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 10026140-2 1999 CyPA binds to the previously identified Gly-Pro90 site of the capsid protein p24, but its role remained unclear. Glycine 40-43 peptidylprolyl isomerase A Homo sapiens 0-4 10026140-2 1999 CyPA binds to the previously identified Gly-Pro90 site of the capsid protein p24, but its role remained unclear. Glycine 40-43 transmembrane p24 trafficking protein 2 Homo sapiens 77-80 10026140-4 1999 Both are located in the C-terminal domain of p24 around Gly-Pro157 and Gly-Pro224. Glycine 56-59 transmembrane p24 trafficking protein 2 Homo sapiens 45-48 10026140-4 1999 Both are located in the C-terminal domain of p24 around Gly-Pro157 and Gly-Pro224. Glycine 71-74 transmembrane p24 trafficking protein 2 Homo sapiens 45-48 10026140-5 1999 Peptides corresponding to these regions showed higher affinities (Kd approximately 0.3 microM) for both CyPA and cyclophilin B than the best peptide derived from the Gly-Pro90 site ( approximately 8 microM) and thus revealed new sequence motifs flanking Gly-Pro that are important for tight interaction of peptide ligands with cyclophilins. Glycine 166-169 peptidylprolyl isomerase A Homo sapiens 104-108 10026140-5 1999 Peptides corresponding to these regions showed higher affinities (Kd approximately 0.3 microM) for both CyPA and cyclophilin B than the best peptide derived from the Gly-Pro90 site ( approximately 8 microM) and thus revealed new sequence motifs flanking Gly-Pro that are important for tight interaction of peptide ligands with cyclophilins. Glycine 166-169 peptidylprolyl isomerase A Homo sapiens 327-339 10026140-5 1999 Peptides corresponding to these regions showed higher affinities (Kd approximately 0.3 microM) for both CyPA and cyclophilin B than the best peptide derived from the Gly-Pro90 site ( approximately 8 microM) and thus revealed new sequence motifs flanking Gly-Pro that are important for tight interaction of peptide ligands with cyclophilins. glycylproline 166-173 peptidylprolyl isomerase A Homo sapiens 104-108 10026140-5 1999 Peptides corresponding to these regions showed higher affinities (Kd approximately 0.3 microM) for both CyPA and cyclophilin B than the best peptide derived from the Gly-Pro90 site ( approximately 8 microM) and thus revealed new sequence motifs flanking Gly-Pro that are important for tight interaction of peptide ligands with cyclophilins. glycylproline 166-173 peptidylprolyl isomerase A Homo sapiens 327-339 10026140-6 1999 Between CyPA and an immature (unprocessed) form of p24, a Kd of approximately 8 microM was measured, which corresponded with the Kd of the best of the Gly-Pro90 peptides, indicating an association via this site. Glycine 151-154 peptidylprolyl isomerase A Homo sapiens 8-12 10026140-6 1999 Between CyPA and an immature (unprocessed) form of p24, a Kd of approximately 8 microM was measured, which corresponded with the Kd of the best of the Gly-Pro90 peptides, indicating an association via this site. Glycine 151-154 transmembrane p24 trafficking protein 2 Homo sapiens 51-54 10026140-7 1999 Processing of immature p24 by the viral protease, yielding mature p24, elicited a conformational change in its C-terminal domain that was signaled by the covalently attached fluorescence label acrylodan. acrylodan 193-202 transmembrane p24 trafficking protein 2 Homo sapiens 23-26 10026140-7 1999 Processing of immature p24 by the viral protease, yielding mature p24, elicited a conformational change in its C-terminal domain that was signaled by the covalently attached fluorescence label acrylodan. acrylodan 193-202 transmembrane p24 trafficking protein 2 Homo sapiens 66-69