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PubMed:12665519 JSONTXT

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PubMed_ArguminSci

Id Subject Object Predicate Lexical cue
T1 121-240 DRI_Background denotes The amyloid beta peptides (Abeta) are the major components of the senile plaques characteristic of Alzheimer's disease.
T2 241-353 DRI_Outcome denotes Abeta peptides are generated from the cleavage of amyloid precursor protein (APP) by beta- and gamma-secretases.
T3 354-545 DRI_Approach denotes Beta-secretase (BACE), a type-I transmembrane aspartyl protease, cleaves APP first to generate a 99-amino acid membrane-associated fragment (CT99) containing the N terminus of Abeta peptides.
T4 546-685 DRI_Approach denotes Gamma-secretase, a multi-protein complex, then cleaves within the transmembrane region of CT99 to generate the C termini of Abeta peptides.
T5 686-795 DRI_Approach denotes The production of Abeta peptides is, therefore, dependent on the activities of both BACE and gamma-secretase.
T6 796-897 DRI_Approach denotes The cleavage of APP by BACE is believed to be a prerequisite for gamma-secretase-mediated processing.
T7 898-1110 DRI_Outcome denotes In the present study, we provide evidence both in vitro and in cells that BACE-mediated cleavage between amino acid residues 34 and 35 (Abeta-34 site) in the Abeta region is dependent on gamma-secretase activity.
T8 1111-1245 DRI_Background denotes In vitro, the Abeta-34 site is processed specifically by BACE1 and BACE2, but not by cathepsin D, a closely related aspartyl protease.
T9 1246-1414 DRI_Outcome denotes Moreover, the cleavage of the Abeta-34 site by BACE1 or BACE2 occurred only when Abeta 1- 40 peptide, a gamma-secretase cleavage product, was used as substrate, not the
T10 1431-1432 DRI_Outcome denotes .
T11 1433-1540 DRI_Background denotes In cells, overexpression of BACE1 or BACE2 dramatically increased the production of the Abeta 1-34 species.
T12 1541-1745 DRI_Background denotes More importantly, the cellular production of Abeta 1-34 species induced by overexpression of BACE1 or BACE2 was blocked by a number of known gamma-secretase inhibitors in a concentration-dependent manner.
T13 1746-1842 DRI_Background denotes These gamma-secretase inhibitors had no effect on enzymatic activity of BACE1 or BACE2 in vitro.
T14 1843-1967 DRI_Approach denotes Our data thus suggest that gamma-secretase cleavage of CT99 is a prerequisite for BACE-mediated processing at Abeta-34 site.
T15 1968-2039 DRI_Approach denotes Therefore, BACE and gamma-secretase activity can be mutually dependent.

sentences

Id Subject Object Predicate Lexical cue
T1 0-120 Sentence denotes Beta-secretase cleavage at amino acid residue 34 in the amyloid beta peptide is dependent upon gamma-secretase activity.
T2 121-240 Sentence denotes The amyloid beta peptides (Abeta) are the major components of the senile plaques characteristic of Alzheimer's disease.
T3 241-353 Sentence denotes Abeta peptides are generated from the cleavage of amyloid precursor protein (APP) by beta- and gamma-secretases.
T4 354-545 Sentence denotes Beta-secretase (BACE), a type-I transmembrane aspartyl protease, cleaves APP first to generate a 99-amino acid membrane-associated fragment (CT99) containing the N terminus of Abeta peptides.
T5 546-685 Sentence denotes Gamma-secretase, a multi-protein complex, then cleaves within the transmembrane region of CT99 to generate the C termini of Abeta peptides.
T6 686-795 Sentence denotes The production of Abeta peptides is, therefore, dependent on the activities of both BACE and gamma-secretase.
T7 796-897 Sentence denotes The cleavage of APP by BACE is believed to be a prerequisite for gamma-secretase-mediated processing.
T8 898-1110 Sentence denotes In the present study, we provide evidence both in vitro and in cells that BACE-mediated cleavage between amino acid residues 34 and 35 (Abeta-34 site) in the Abeta region is dependent on gamma-secretase activity.
T9 1111-1245 Sentence denotes In vitro, the Abeta-34 site is processed specifically by BACE1 and BACE2, but not by cathepsin D, a closely related aspartyl protease.
T10 1246-1432 Sentence denotes Moreover, the cleavage of the Abeta-34 site by BACE1 or BACE2 occurred only when Abeta 1- 40 peptide, a gamma-secretase cleavage product, was used as substrate, not the non-cleaved CT99.
T11 1433-1540 Sentence denotes In cells, overexpression of BACE1 or BACE2 dramatically increased the production of the Abeta 1-34 species.
T12 1541-1745 Sentence denotes More importantly, the cellular production of Abeta 1-34 species induced by overexpression of BACE1 or BACE2 was blocked by a number of known gamma-secretase inhibitors in a concentration-dependent manner.
T13 1746-1842 Sentence denotes These gamma-secretase inhibitors had no effect on enzymatic activity of BACE1 or BACE2 in vitro.
T14 1843-1967 Sentence denotes Our data thus suggest that gamma-secretase cleavage of CT99 is a prerequisite for BACE-mediated processing at Abeta-34 site.
T15 1968-2039 Sentence denotes Therefore, BACE and gamma-secretase activity can be mutually dependent.

PubmedHPO

Id Subject Object Predicate Lexical cue
T1 125-132 HP_0011034 denotes amyloid
T2 187-201 HP_0100256 denotes senile plaques
T3 220-239 HP_0002511 denotes Alzheimer's disease
T4 291-298 HP_0011034 denotes amyloid

UseCases_ArguminSci_Discourse

Id Subject Object Predicate Lexical cue
T1 0-120 DRI_Background denotes Beta-secretase cleavage at amino acid residue 34 in the amyloid beta peptide is dependent upon gamma-secretase activity.
T2 121-240 DRI_Background denotes The amyloid beta peptides (Abeta) are the major components of the senile plaques characteristic of Alzheimer's disease.
T3 241-353 DRI_Outcome denotes Abeta peptides are generated from the cleavage of amyloid precursor protein (APP) by beta- and gamma-secretases.
T4 354-545 DRI_Approach denotes Beta-secretase (BACE), a type-I transmembrane aspartyl protease, cleaves APP first to generate a 99-amino acid membrane-associated fragment (CT99) containing the N terminus of Abeta peptides.
T5 546-685 DRI_Approach denotes Gamma-secretase, a multi-protein complex, then cleaves within the transmembrane region of CT99 to generate the C termini of Abeta peptides.
T6 686-795 DRI_Approach denotes The production of Abeta peptides is, therefore, dependent on the activities of both BACE and gamma-secretase.
T7 796-897 DRI_Approach denotes The cleavage of APP by BACE is believed to be a prerequisite for gamma-secretase-mediated processing.
T8 898-1110 DRI_Outcome denotes In the present study, we provide evidence both in vitro and in cells that BACE-mediated cleavage between amino acid residues 34 and 35 (Abeta-34 site) in the Abeta region is dependent on gamma-secretase activity.
T9 1111-1245 DRI_Background denotes In vitro, the Abeta-34 site is processed specifically by BACE1 and BACE2, but not by cathepsin D, a closely related aspartyl protease.
T10 1246-1414 DRI_Outcome denotes Moreover, the cleavage of the Abeta-34 site by BACE1 or BACE2 occurred only when Abeta 1- 40 peptide, a gamma-secretase cleavage product, was used as substrate, not the
T11 1415-1431 Token_Label.OUTSIDE denotes non-cleaved CT99
T12 1431-1432 DRI_Outcome denotes .
T13 1433-1540 DRI_Background denotes In cells, overexpression of BACE1 or BACE2 dramatically increased the production of the Abeta 1-34 species.
T14 1541-1745 DRI_Background denotes More importantly, the cellular production of Abeta 1-34 species induced by overexpression of BACE1 or BACE2 was blocked by a number of known gamma-secretase inhibitors in a concentration-dependent manner.
T15 1746-1842 DRI_Background denotes These gamma-secretase inhibitors had no effect on enzymatic activity of BACE1 or BACE2 in vitro.
T16 1843-1967 DRI_Approach denotes Our data thus suggest that gamma-secretase cleavage of CT99 is a prerequisite for BACE-mediated processing at Abeta-34 site.
T17 1968-2039 DRI_Approach denotes Therefore, BACE and gamma-secretase activity can be mutually dependent.

mondo_disease

Id Subject Object Predicate Lexical cue mondo_id
T1 56-63 Disease denotes amyloid http://purl.obolibrary.org/obo/MONDO_0019065
T2 125-132 Disease denotes amyloid http://purl.obolibrary.org/obo/MONDO_0019065
T3 220-239 Disease denotes Alzheimer's disease http://purl.obolibrary.org/obo/MONDO_0004975
T4 291-298 Disease denotes amyloid http://purl.obolibrary.org/obo/MONDO_0019065

HP-phenotype

Id Subject Object Predicate Lexical cue hp_id
T1 187-201 Phenotype denotes senile plaques HP:0100256
T2 220-239 Phenotype denotes Alzheimer's disease HP:0002511

Anatomy-UBERON

Id Subject Object Predicate Lexical cue uberon_id
T1 386-399 Body_part denotes transmembrane http://purl.obolibrary.org/obo/GO_0016020
T2 465-473 Body_part denotes membrane http://purl.obolibrary.org/obo/GO_0016020|http://purl.obolibrary.org/obo/UBERON_0000094|http://purl.obolibrary.org/obo/UBERON_0000158
T5 612-625 Body_part denotes transmembrane http://purl.obolibrary.org/obo/GO_0016020

CL-cell

Id Subject Object Predicate Lexical cue cl_id
T1 379-385 Cell denotes type-I http://purl.obolibrary.org/obo/CL:0004120|http://purl.obolibrary.org/obo/CL:0004138