PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
33107166-2	2020	After the removal of specific sugar residues, glycoproteins acquire signals in the glycoprotein quality control (GPQC) system and enter the folding cycle composed of lectin-chaperones calnexin (CNX) and calreticulin (CRT), glucosidase II (G-II), and UDP-Glc:glycoprotein glucosyltransferase (UGGT).	Sugars	30-35	calreticulin	Homo sapiens	203-215	
22086461-12	2012	The details therefore, strongly implicate gentamicin as a competitive inhibitor of sugar binding with calreticulin.	Sugars	83-88	calreticulin	Homo sapiens	102-114	
17278394-5	2006	It binds to neutral sugar arrays on microorganisms and acts as an opsonin either directly (by binding to cell-surface calreticulin) or indirectly by activating complement.	Sugars	20-25	calreticulin	Homo sapiens	118-130	
14705935-3	2004	To provide further insight into these lectin-glycan interactions, we are investigating the interaction of CRT with various sugars.	Sugars	123-129	calreticulin	Homo sapiens	106-109	
14705935-4	2004	We have earlier modeled the complex between CRT and the Glc(1)Man(3) tetrasaccharide, a derivative of the native Glc(1)Man(9)GlcNAc(2) sugar moiety.	Sugars	135-140	calreticulin	Homo sapiens	44-47	
14705935-5	2004	Here, we have systematically mutated the residues implicated by the model in the interaction of CRT to its sugar substrates and categorized the role played by each of the subsites of calreticulin toward the glycan binding.	Sugars	107-112	calreticulin	Homo sapiens	96-99	
14705935-10	2004	These studies provide detailed molecular insight into the sugar binding specificity of CRT.	Sugars	58-63	calreticulin	Homo sapiens	87-90