PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 9207473-7 1997 However, oxidative derivatization of carbohydrate components with digoxigenin showed that human calreticulin produced in either HL-60 cells or Sf9 insect cells is glycosylated, indicating that glycosylated and nonglycosylated human calreticulin have indistinguishable electrophoretic mobilities. Carbohydrates 37-49 calreticulin Homo sapiens 96-108 9207473-8 1997 Direct measurement by phenol-H2SO4 confirmed the presence of carbohydrate on recombinant human calreticulin. Carbohydrates 61-73 calreticulin Homo sapiens 95-107 10580135-4 1999 Calnexin and calreticulin function via specific carbohydrates in quality control of newly synthesized glycoproteins in the ER, and ERGIC-53 seems to function in the transport of glycoproteins from ER to the Golgi complex. Carbohydrates 48-61 calreticulin Homo sapiens 13-25 34050860-4 2021 At the edge of the carbohydrate-binding site is a conserved, strained disulphide bridge, formed between C106 and C137 of human Calr, which lies in a polypeptide-binding site. Carbohydrates 19-31 calreticulin Homo sapiens 127-131 8626722-8 1996 The copurification of calreticulin and endomannosidase from a Golgi fraction in comparable amounts and the strikingly similar saccharide specificities of the chaperone and the processing enzyme have suggested a tentative model for the dissociation through glucose removal of calreticulin-glycoprotein complexes in a post-endoplasmic reticulum locale; in this scheme, deglucosylation would be brought about by the action of endomannosidase rather than glucosidase II. Carbohydrates 126-136 calreticulin Homo sapiens 22-34 16291754-3 2006 We have focused on two cysteine residues (Cys(88) and Cys(120)), which form a disulfide bridge in the N-terminal domain of calreticulin, on a tryptophan residue located in the carbohydrate binding site (Trp(302)), and on certain residues located at the tip of the "hairpin-like" P-domain of the protein (Glu(238), Glu(239), Asp(241), Glu(243), and Trp(244)). Carbohydrates 176-188 calreticulin Homo sapiens 123-135 25428988-2 2015 The reglucosylation of glycoproteins supports their rebinding to the carbohydrate-binding ER molecular chaperones calnexin and calreticulin. Carbohydrates 69-81 calreticulin Homo sapiens 127-139 32062378-2 2020 Mutagenesis studies have identified several residues on a concave beta-sheet surface of CRT critical for CRT binding to carbohydrate and other proteins/peptides. Carbohydrates 120-132 calreticulin Homo sapiens 88-91 32062378-2 2020 Mutagenesis studies have identified several residues on a concave beta-sheet surface of CRT critical for CRT binding to carbohydrate and other proteins/peptides. Carbohydrates 120-132 calreticulin Homo sapiens 105-108 32062378-3 2020 How the mutations of these key residues in CRT affect the conformation and dynamics of CRT, further influencing CRT binding to carbohydrates and other proteins to signal the important biological activities remain unknown. Carbohydrates 127-140 calreticulin Homo sapiens 43-46 32062378-3 2020 How the mutations of these key residues in CRT affect the conformation and dynamics of CRT, further influencing CRT binding to carbohydrates and other proteins to signal the important biological activities remain unknown. Carbohydrates 127-140 calreticulin Homo sapiens 87-90 32062378-3 2020 How the mutations of these key residues in CRT affect the conformation and dynamics of CRT, further influencing CRT binding to carbohydrates and other proteins to signal the important biological activities remain unknown. Carbohydrates 127-140 calreticulin Homo sapiens 87-90 26676362-1 2016 Helenius and colleagues proposed over 20-years ago a paradigm-shifting model for how chaperone binding in the endoplasmic reticulum was mediated and controlled for a new type of molecular chaperone- the carbohydrate-binding chaperones, calnexin and calreticulin. Carbohydrates 203-215 calreticulin Homo sapiens 249-261 20880849-0 2010 Structural basis of carbohydrate recognition by calreticulin. Carbohydrates 20-32 calreticulin Homo sapiens 48-60 17950701-0 2007 Analyses of carbohydrate binding property of lectin-chaperone calreticulin. Carbohydrates 12-24 calreticulin Homo sapiens 62-74 14705935-0 2004 Mutational analysis provides molecular insight into the carbohydrate-binding region of calreticulin: pivotal roles of tyrosine-109 and aspartate-135 in carbohydrate recognition. Carbohydrates 56-68 calreticulin Homo sapiens 87-99 14705935-0 2004 Mutational analysis provides molecular insight into the carbohydrate-binding region of calreticulin: pivotal roles of tyrosine-109 and aspartate-135 in carbohydrate recognition. Carbohydrates 152-164 calreticulin Homo sapiens 87-99 14705935-6 2004 The CRT mutants Y109F and D135L did not show any binding to the sugar substrates interacting with the wild-type protein, demonstrating the great importance of these residues in the carbohydrate-binding site of CRT. Carbohydrates 181-193 calreticulin Homo sapiens 4-7 14705935-6 2004 The CRT mutants Y109F and D135L did not show any binding to the sugar substrates interacting with the wild-type protein, demonstrating the great importance of these residues in the carbohydrate-binding site of CRT. Carbohydrates 181-193 calreticulin Homo sapiens 210-213 12464625-8 2003 Also, several novel findings about the recognition of saccharide ligands by calreticulin vis a vis legume lectins, which have the same fold as this chaperone, are discussed. Carbohydrates 54-64 calreticulin Homo sapiens 76-88