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PubMed:10764837 JSONTXT 53 Projects

Annnotations TAB TSV DIC JSON TextAE Lectin_function IAV-Glycan

Id Subject Object Predicate Lexical cue
TextSentencer_T1 0-101 Sentence denotes Two distinct domains of the beta-subunit of glucosidase II interact with the catalytic alpha-subunit.
T1 0-101 Sentence denotes Two distinct domains of the beta-subunit of glucosidase II interact with the catalytic alpha-subunit.
T1 0-101 Sentence denotes Two distinct domains of the beta-subunit of glucosidase II interact with the catalytic alpha-subunit.
TextSentencer_T2 102-372 Sentence denotes Recent purification and cDNA cloning of the endoplasmic reticulum processing enzyme glucosidase II have revealed that it is composed of two soluble proteins: a catalytic alpha-subunit and a beta-subunit of unknown function, both of which are highly conserved in mammals.
T2 102-372 Sentence denotes Recent purification and cDNA cloning of the endoplasmic reticulum processing enzyme glucosidase II have revealed that it is composed of two soluble proteins: a catalytic alpha-subunit and a beta-subunit of unknown function, both of which are highly conserved in mammals.
T2 102-372 Sentence denotes Recent purification and cDNA cloning of the endoplasmic reticulum processing enzyme glucosidase II have revealed that it is composed of two soluble proteins: a catalytic alpha-subunit and a beta-subunit of unknown function, both of which are highly conserved in mammals.
TextSentencer_T3 373-673 Sentence denotes Since the beta-subunit, which contains a C-terminal His-Asp-Glu-Leu (HDEL) motif, may function to link the catalytic subunit to the KDEL receptor as a retrieval mechanism, we sought to map the regions of the mouse beta-subunit protein responsible for mediating the association with the alpha-subunit.
T3 373-673 Sentence denotes Since the beta-subunit, which contains a C-terminal His-Asp-Glu-Leu (HDEL) motif, may function to link the catalytic subunit to the KDEL receptor as a retrieval mechanism, we sought to map the regions of the mouse beta-subunit protein responsible for mediating the association with the alpha-subunit.
T3 373-673 Sentence denotes Since the beta-subunit, which contains a C-terminal His-Asp-Glu-Leu (HDEL) motif, may function to link the catalytic subunit to the KDEL receptor as a retrieval mechanism, we sought to map the regions of the mouse beta-subunit protein responsible for mediating the association with the alpha-subunit.
TextSentencer_T4 674-918 Sentence denotes By screening a panel of recombinant beta-subunit glutathione S-transferase fusion proteins for the ability to precipitate glucosidase II activity, we have identified two non-overlapping interaction domains (ID1 and ID2) within the beta-subunit.
T4 674-918 Sentence denotes By screening a panel of recombinant beta-subunit glutathione S-transferase fusion proteins for the ability to precipitate glucosidase II activity, we have identified two non-overlapping interaction domains (ID1 and ID2) within the beta-subunit.
T4 674-918 Sentence denotes By screening a panel of recombinant beta-subunit glutathione S-transferase fusion proteins for the ability to precipitate glucosidase II activity, we have identified two non-overlapping interaction domains (ID1 and ID2) within the beta-subunit.
TextSentencer_T5 919-1046 Sentence denotes ID1 encompasses 118 amino acids at the N-terminus of the mature polypeptide, spanning the cysteine-rich element in this region.
T5 919-1046 Sentence denotes ID1 encompasses 118 amino acids at the N-terminus of the mature polypeptide, spanning the cysteine-rich element in this region.
T5 919-1046 Sentence denotes ID1 encompasses 118 amino acids at the N-terminus of the mature polypeptide, spanning the cysteine-rich element in this region.
TextSentencer_T6 1047-1180 Sentence denotes ID2, located near the C-terminus, is contained within amino acids 273-400, a region occupied in part by a stretch of acidic residues.
T6 1047-1180 Sentence denotes ID2, located near the C-terminus, is contained within amino acids 273-400, a region occupied in part by a stretch of acidic residues.
T6 1047-1180 Sentence denotes ID2, located near the C-terminus, is contained within amino acids 273-400, a region occupied in part by a stretch of acidic residues.
TextSentencer_T7 1181-1310 Sentence denotes Variable usage of 7 alternatively spliced amino acids within ID2 was found not to influence the association of the two sub-units.
T7 1181-1310 Sentence denotes Variable usage of 7 alternatively spliced amino acids within ID2 was found not to influence the association of the two sub-units.
T7 1181-1310 Sentence denotes Variable usage of 7 alternatively spliced amino acids within ID2 was found not to influence the association of the two sub-units.
TextSentencer_T8 1311-1470 Sentence denotes We theorize that the catalytic subunit of glucosidase II binds synergistically to ID1 and ID2, explaining the high associative stability of the enzyme complex.
T8 1311-1470 Sentence denotes We theorize that the catalytic subunit of glucosidase II binds synergistically to ID1 and ID2, explaining the high associative stability of the enzyme complex.
T8 1311-1470 Sentence denotes We theorize that the catalytic subunit of glucosidase II binds synergistically to ID1 and ID2, explaining the high associative stability of the enzyme complex.