PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
7938008-3	1994	We show here that the SH3 domains of p47-phox bind to proline-rich sequences in p47-phox itself and the p22-phox subunit of cytochrome b558.	Proline	54-61	neutrophil cytosolic factor 1	Homo sapiens	37-45	
7938008-3	1994	We show here that the SH3 domains of p47-phox bind to proline-rich sequences in p47-phox itself and the p22-phox subunit of cytochrome b558.	Proline	54-61	pleckstrin	Homo sapiens	37-40	
7938008-3	1994	We show here that the SH3 domains of p47-phox bind to proline-rich sequences in p47-phox itself and the p22-phox subunit of cytochrome b558.	Proline	54-61	cytochrome b-245 alpha chain	Homo sapiens	104-112	
7938008-4	1994	Binding of the p47-phox SH3 domains to p22-phox was abolished by a mutation in one proline-rich sequence (Pro156-->Gln) noted in a distinct form of chronic granulomatous disease and was inhibited by a short proline-rich synthetic peptide corresponding to residues 149-162 of p22-phox.	Proline	83-90	pleckstrin	Homo sapiens	15-18	
7938008-4	1994	Binding of the p47-phox SH3 domains to p22-phox was abolished by a mutation in one proline-rich sequence (Pro156-->Gln) noted in a distinct form of chronic granulomatous disease and was inhibited by a short proline-rich synthetic peptide corresponding to residues 149-162 of p22-phox.	Proline	83-90	calcineurin like EF-hand protein 1	Homo sapiens	39-42	
7938008-4	1994	Binding of the p47-phox SH3 domains to p22-phox was abolished by a mutation in one proline-rich sequence (Pro156-->Gln) noted in a distinct form of chronic granulomatous disease and was inhibited by a short proline-rich synthetic peptide corresponding to residues 149-162 of p22-phox.	Proline	83-90	calcineurin like EF-hand protein 1	Homo sapiens	278-281	
7938008-4	1994	Binding of the p47-phox SH3 domains to p22-phox was abolished by a mutation in one proline-rich sequence (Pro156-->Gln) noted in a distinct form of chronic granulomatous disease and was inhibited by a short proline-rich synthetic peptide corresponding to residues 149-162 of p22-phox.	Glutamine	118-121	pleckstrin	Homo sapiens	15-18	
7938008-4	1994	Binding of the p47-phox SH3 domains to p22-phox was abolished by a mutation in one proline-rich sequence (Pro156-->Gln) noted in a distinct form of chronic granulomatous disease and was inhibited by a short proline-rich synthetic peptide corresponding to residues 149-162 of p22-phox.	Glutamine	118-121	calcineurin like EF-hand protein 1	Homo sapiens	39-42	
7938008-4	1994	Binding of the p47-phox SH3 domains to p22-phox was abolished by a mutation in one proline-rich sequence (Pro156-->Gln) noted in a distinct form of chronic granulomatous disease and was inhibited by a short proline-rich synthetic peptide corresponding to residues 149-162 of p22-phox.	Glutamine	118-121	calcineurin like EF-hand protein 1	Homo sapiens	278-281	
7938008-4	1994	Binding of the p47-phox SH3 domains to p22-phox was abolished by a mutation in one proline-rich sequence (Pro156-->Gln) noted in a distinct form of chronic granulomatous disease and was inhibited by a short proline-rich synthetic peptide corresponding to residues 149-162 of p22-phox.	Proline	210-217	pleckstrin	Homo sapiens	15-18	
7938008-4	1994	Binding of the p47-phox SH3 domains to p22-phox was abolished by a mutation in one proline-rich sequence (Pro156-->Gln) noted in a distinct form of chronic granulomatous disease and was inhibited by a short proline-rich synthetic peptide corresponding to residues 149-162 of p22-phox.	Proline	210-217	calcineurin like EF-hand protein 1	Homo sapiens	39-42	
7938008-4	1994	Binding of the p47-phox SH3 domains to p22-phox was abolished by a mutation in one proline-rich sequence (Pro156-->Gln) noted in a distinct form of chronic granulomatous disease and was inhibited by a short proline-rich synthetic peptide corresponding to residues 149-162 of p22-phox.	Proline	210-217	calcineurin like EF-hand protein 1	Homo sapiens	278-281	
7938008-6	1994	We also show that the cytosolic oxidase components associate with one another through the C-terminal SH3 domain of p67-phox and a proline-rich C-terminal sequence in p47-phox.	Proline	130-137	pleckstrin	Homo sapiens	166-169