PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
12464625-1	2003	Calreticulin is a molecular chaperone found in the endoplasmic reticulum in eukaryotes, and its interaction with N-glycosylated polypeptides is mediated by the glycan Glc(1)Man(7-9)GlcNAc(2) present on the target glycoproteins.	Nitrogen	113-114	calreticulin	Homo sapiens	0-12	
10823661-5	2000	Furthermore, since the stability of N-glycosylated proteins is known to be regulated by lectin family chaperones, such as calnexin, a type I transmembrane protein located in the endoplasmic reticulum (ER), and calreticulin, a soluble protein in the ER lumen, the effect of the processing inhibitors on the interaction of IFN-gamma with calnexin and calreticulin was investigated.	Nitrogen	36-37	calreticulin	Homo sapiens	210-222	
10823661-5	2000	Furthermore, since the stability of N-glycosylated proteins is known to be regulated by lectin family chaperones, such as calnexin, a type I transmembrane protein located in the endoplasmic reticulum (ER), and calreticulin, a soluble protein in the ER lumen, the effect of the processing inhibitors on the interaction of IFN-gamma with calnexin and calreticulin was investigated.	Nitrogen	36-37	calreticulin	Homo sapiens	349-361	
10353723-6	1998	Levels of the mRNA encoding the fusion protein were also increased by tunicamycin, but not thapsigargin, suggesting that, in agreement with our previous observations, inhibition of N-linked glycosylation may increase the stability of calreticulin mRNA.	Nitrogen	16-17	calreticulin	Homo sapiens	234-246	
9551918-0	1998	Distinct patterns of folding and interactions with calnexin and calreticulin in human class I MHC proteins with altered N-glycosylation.	Nitrogen	120-121	calreticulin	Homo sapiens	64-76	
9207473-9	1997	These data show that human myeloid calreticulin undergoes cotranslational signal peptide cleavage and posttranslational N-linked glycosylation.	Nitrogen	120-121	calreticulin	Homo sapiens	35-47	
26362185-0	2015	Calreticulin discriminates the proximal region at the N-glycosylation site of Glc1Man9GlcNAc2 ligand.	Nitrogen	54-55	calreticulin	Homo sapiens	0-12	
34495528-6	2021	Subsequently, the N-glycosylated nascent proteins enter the folding step, in which N-glycans contribute largely to attaining the correct protein fold by recruiting the lectin-like chaperones, calnexin, and calreticulin.	Nitrogen	18-19	calreticulin	Homo sapiens	206-218	
28178702-9	2017	We also demonstrated that the altered pattern of N-linked glycosylation induces an over-expression of binding immunoglobulin protein and calreticulin, suggesting ER stress.	Nitrogen	49-50	calreticulin	Homo sapiens	137-149	
26344782-1	2015	Dinitrogen complexes of the type Tp(R,R)Cr-N2-CrTp(R,R) are not the most labile precursors for Cr(i) chemistry, as they are sterically protected from obligatory associative ligand substitution.	Nitrogen	0-10	calreticulin	Homo sapiens	46-50	
8809046-0	1996	Induction of calreticulin expression in HeLa cells by depletion of the endoplasmic reticulum Ca2+ store and inhibition of N-linked glycosylation.	Nitrogen	122-123	calreticulin	Homo sapiens	13-25	
34756244-1	2021	Calreticulin (CALR) is a chaperone present in the endoplasmic reticulum, which is involved in the quality control of N-glycosylated proteins and storage of calcium ions.	Nitrogen	117-118	calreticulin	Homo sapiens	0-12	
34756244-1	2021	Calreticulin (CALR) is a chaperone present in the endoplasmic reticulum, which is involved in the quality control of N-glycosylated proteins and storage of calcium ions.	Nitrogen	117-118	calreticulin	Homo sapiens	14-18	
28408900-6	2017	More recently, a novel activation mechanism was identified whereby mutated forms of calreticulin form complexes with TPO-R via its extracellular N-glycosylated domain.	Nitrogen	145-146	calreticulin	Homo sapiens	84-96	
26362185-5	2015	Our results indicate that, similar to UGGT, CRT discriminates the proximal region at the N-glycosylation site, suggesting a similar mechanism mediating the recognition of aglycone moieties in the ER glycoprotein quality control system.	Nitrogen	89-90	calreticulin	Homo sapiens	44-47	
26207422-6	2015	Removal of N-glycosylation at residue 38 revealed an amino acid-dependent strong interaction with CALR likely preventing unloading of the misfolded protein from the ER chaperone down the normal secretory pathway.	Nitrogen	11-12	calreticulin	Homo sapiens	98-102	
26207422-8	2015	This is mediated, however, through a novel mechanism of cloaking an N-glycosylation-independent strong interaction with the ER-resident CALR.	Nitrogen	68-69	calreticulin	Homo sapiens	136-140