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PubMed_ArguminSci

Id	Subject	Object	Predicate	Lexical cue
T1	230-483	DRI_Background	denotes	Increasing evidence suggests that the low density lipoprotein receptor-related protein (LRP) affects the processing of amyloid precursor protein (APP) and amyloid beta (Abeta) protein production as well as mediates the clearance of Abeta from the brain.
T2	484-668	DRI_Background	denotes	Recent studies indicate that the cytoplasmic domain of LRP is critical for this modulation of APP processing requiring perhaps a complex between APP, the adaptor protein FE65, and LRP.
T3	669-895	DRI_Approach	denotes	In this study, we expressed a small LRP domain consisting of the C-terminal 97 amino acids of the cytoplasmic domain, or LRP-soluble tail (LRP-ST), in CHO cells to test the hypothesis that the APP.LRP complex can be disrupted.
T4	896-1051	DRI_Outcome	denotes	We anticipated that LRP-ST would inhibit the normal interaction between LRP and APP and therefore perturb APP processing to resemble a LRP-deficient state.
T5	1052-1272	DRI_Outcome	denotes	Surprisingly, CHO cells expressing LRP-ST demonstrated an increase in both sAPP secretion and Abeta production compared with control CHO cells in a manner reminiscent of the cellular effects of the APP "Swedish mutation.
T6	1274-1381	DRI_Background	denotes	The increase in sAPP secretion consisted mainly of sAPPbeta, consistent with the increase in Abeta release.
T7	1382-1554	DRI_Outcome	denotes	Further, this effect is LRP-independent, as the same alterations remained when LRP-ST was expressed in LRP-deficient cells but not when the construct was membrane-anchored.
T8	1555-1720	DRI_Approach	denotes	Finally, deletion experiments suggested that the last 50 amino acid residues of LRP-ST contain the important domain for altering APP processing and Abeta production.
T9	1721-1872	DRI_FutureWork	denotes	These observations indicate that there are cellular pathways that may suppress Abeta generation but that can be altered to facilitate Abeta production.

sentences

Id	Subject	Object	Predicate	Lexical cue
T1	0-229	Sentence	denotes	Sequences from the low density lipoprotein receptor-related protein (LRP) cytoplasmic domain enhance amyloid beta protein production via the beta-secretase pathway without altering amyloid precursor protein/LRP nuclear signaling.
T2	230-483	Sentence	denotes	Increasing evidence suggests that the low density lipoprotein receptor-related protein (LRP) affects the processing of amyloid precursor protein (APP) and amyloid beta (Abeta) protein production as well as mediates the clearance of Abeta from the brain.
T3	484-668	Sentence	denotes	Recent studies indicate that the cytoplasmic domain of LRP is critical for this modulation of APP processing requiring perhaps a complex between APP, the adaptor protein FE65, and LRP.
T4	669-895	Sentence	denotes	In this study, we expressed a small LRP domain consisting of the C-terminal 97 amino acids of the cytoplasmic domain, or LRP-soluble tail (LRP-ST), in CHO cells to test the hypothesis that the APP.LRP complex can be disrupted.
T5	896-1051	Sentence	denotes	We anticipated that LRP-ST would inhibit the normal interaction between LRP and APP and therefore perturb APP processing to resemble a LRP-deficient state.
T6	1052-1381	Sentence	denotes	Surprisingly, CHO cells expressing LRP-ST demonstrated an increase in both sAPP secretion and Abeta production compared with control CHO cells in a manner reminiscent of the cellular effects of the APP "Swedish mutation." The increase in sAPP secretion consisted mainly of sAPPbeta, consistent with the increase in Abeta release.
T7	1382-1554	Sentence	denotes	Further, this effect is LRP-independent, as the same alterations remained when LRP-ST was expressed in LRP-deficient cells but not when the construct was membrane-anchored.
T8	1555-1720	Sentence	denotes	Finally, deletion experiments suggested that the last 50 amino acid residues of LRP-ST contain the important domain for altering APP processing and Abeta production.
T9	1721-1872	Sentence	denotes	These observations indicate that there are cellular pathways that may suppress Abeta generation but that can be altered to facilitate Abeta production.

Glycosmos6-MAT

Id	Subject	Object	Predicate	Lexical cue
T1	477-482	http://purl.obolibrary.org/obo/MAT_0000098	denotes	brain

UseCases_ArguminSci_Discourse

Id	Subject	Object	Predicate	Lexical cue
T1	0-229	DRI_Approach	denotes	Sequences from the low density lipoprotein receptor-related protein (LRP) cytoplasmic domain enhance amyloid beta protein production via the beta-secretase pathway without altering amyloid precursor protein/LRP nuclear signaling.
T2	230-483	DRI_Background	denotes	Increasing evidence suggests that the low density lipoprotein receptor-related protein (LRP) affects the processing of amyloid precursor protein (APP) and amyloid beta (Abeta) protein production as well as mediates the clearance of Abeta from the brain.
T3	484-668	DRI_Background	denotes	Recent studies indicate that the cytoplasmic domain of LRP is critical for this modulation of APP processing requiring perhaps a complex between APP, the adaptor protein FE65, and LRP.
T4	669-895	DRI_Approach	denotes	In this study, we expressed a small LRP domain consisting of the C-terminal 97 amino acids of the cytoplasmic domain, or LRP-soluble tail (LRP-ST), in CHO cells to test the hypothesis that the APP.LRP complex can be disrupted.
T5	896-1051	DRI_Outcome	denotes	We anticipated that LRP-ST would inhibit the normal interaction between LRP and APP and therefore perturb APP processing to resemble a LRP-deficient state.
T6	1052-1273	DRI_Outcome	denotes	Surprisingly, CHO cells expressing LRP-ST demonstrated an increase in both sAPP secretion and Abeta production compared with control CHO cells in a manner reminiscent of the cellular effects of the APP "Swedish mutation."
T7	1274-1381	DRI_Background	denotes	The increase in sAPP secretion consisted mainly of sAPPbeta, consistent with the increase in Abeta release.
T8	1382-1554	DRI_Outcome	denotes	Further, this effect is LRP-independent, as the same alterations remained when LRP-ST was expressed in LRP-deficient cells but not when the construct was membrane-anchored.
T9	1555-1720	DRI_Approach	denotes	Finally, deletion experiments suggested that the last 50 amino acid residues of LRP-ST contain the important domain for altering APP processing and Abeta production.
T10	1721-1872	DRI_FutureWork	denotes	These observations indicate that there are cellular pathways that may suppress Abeta generation but that can be altered to facilitate Abeta production.

mondo_disease

Id	Subject	Object	Predicate	Lexical cue	mondo_id
T1	101-108	Disease	denotes	amyloid	http://purl.obolibrary.org/obo/MONDO_0019065
T2	181-188	Disease	denotes	amyloid	http://purl.obolibrary.org/obo/MONDO_0019065
T3	349-356	Disease	denotes	amyloid	http://purl.obolibrary.org/obo/MONDO_0019065
T4	385-392	Disease	denotes	amyloid	http://purl.obolibrary.org/obo/MONDO_0019065

Anatomy-MAT

Id	Subject	Object	Predicate	Lexical cue	mat_id
T1	477-482	Body_part	denotes	brain	http://purl.obolibrary.org/obo/MAT_0000098

Anatomy-UBERON

Id	Subject	Object	Predicate	Lexical cue	uberon_id
T1	74-85	Body_part	denotes	cytoplasmic	http://purl.obolibrary.org/obo/GO_0005737
T2	477-482	Body_part	denotes	brain	http://purl.obolibrary.org/obo/UBERON_0000955\|http://purl.obolibrary.org/obo/UBERON_6110636
T4	517-528	Body_part	denotes	cytoplasmic	http://purl.obolibrary.org/obo/GO_0005737
T5	767-778	Body_part	denotes	cytoplasmic	http://purl.obolibrary.org/obo/GO_0005737
T6	802-806	Body_part	denotes	tail	http://purl.obolibrary.org/obo/UBERON_0002415\|http://purl.obolibrary.org/obo/UBERON_4000164
T8	1536-1544	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