PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
9525969-4	1998	Protein chaperones calnexin (CNX) and calreticulin (CRT) preferentially interact with glycoproteins containing monoglucosylated N-linked oligosaccharides and are proposed to traffic proteins through degradative and/or secretory pathways.	n-linked oligosaccharides	128-153	calnexin	Homo sapiens	19-27	
16938437-5	2006	Here, we have observed that NCT N-linked oligosaccharides mediated specific interactions with the secretory pathway lectins calnexin and ERGIC-53.	n-linked oligosaccharides	32-57	calnexin	Homo sapiens	124-132	
9525969-4	1998	Protein chaperones calnexin (CNX) and calreticulin (CRT) preferentially interact with glycoproteins containing monoglucosylated N-linked oligosaccharides and are proposed to traffic proteins through degradative and/or secretory pathways.	n-linked oligosaccharides	128-153	calnexin	Homo sapiens	29-32	
7592804-1	1995	Increasing evidence shows that calnexin, a membrane-bound chaperone in the endoplasmic reticulum, is a lectin that binds to newly synthesized glycoproteins that have partially trimmed N-linked oligosaccharides.	n-linked oligosaccharides	184-209	calnexin	Homo sapiens	31-39	
8918549-7	1996	Complete inhibition of the binding of these glycoprotein precursors to calnexin by tunicamycin or castanospermine indicates the importance of partially trimmed N-linked oligosaccharides for their association.	n-linked oligosaccharides	160-185	calnexin	Homo sapiens	71-79