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PubMed:11809755 JSONTXT 24 Projects

Annnotations TAB TSV DIC JSON TextAE Lectin_function IAV-Glycan

Id Subject Object Predicate Lexical cue
T1 0-104 Sentence denotes Insulin-degrading enzyme rapidly removes the beta-amyloid precursor protein intracellular domain (AICD).
T2 105-247 Sentence denotes The intramembranous gamma-secretase cleavage of the beta-amyloid precursor protein (APP) is dependent on biologically active presenilins (PS).
T3 248-631 Sentence denotes Notch also undergoes a similar PS-dependent gamma-secretase-like cleavage, resulting in the liberation of the Notch intracellular domain (NICD), which is critically required for developmental signal transduction. gamma-Secretase processing of APP results in the production of a similar fragment called AICD (APP intracellular domain), which may function in nuclear signaling as well.
T4 632-668 Sentence denotes AICD, like NICD, is rapidly removed.
T5 669-803 Sentence denotes By using a battery of protease inhibitors we demonstrate that AICD, in contrast to NICD, is degraded by a cytoplasmic metalloprotease.
T6 804-927 Sentence denotes In vitro degradation of AICD can be reconstituted with cytoplasmic fractions obtained from neuronal and non-neuronal cells.
T7 928-1218 Sentence denotes Taking into account the inhibition profile and the cytoplasmic localization, we identified three candidate enzymes (neurolysin, thimet oligopeptidase, and insulin-degrading enzyme (IDE), also known as insulysin), which all are involved in the degradation of bioactive peptides in the brain.
T8 1219-1357 Sentence denotes When insulin, a well characterized substrate of IDE, was added to the in vitro degradation assay, removal of AICD was efficiently blocked.
T9 1358-1520 Sentence denotes Moreover, overexpression of IDE resulted in enhanced degradation of AICD, whereas overexpression of the inactive IDE E111Q mutant did not affect AICD degradation.
T10 1521-1603 Sentence denotes Finally, immunodepletion of IDE significantly reduced the AICD degrading activity.
T11 1604-1793 Sentence denotes Therefore our data demonstrate that IDE, which is one of the proteases implicated in the removal of extracellular Abeta, also removes the cytoplasmic product of gamma-secretase cleaved APP.