About: Insulin-degrading enzyme rapidly removes the beta-amyloid precursor protein intracellular domain (AICD)

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description	artículu científicu espublizáu en 2002 (ast) vědecký článek publikovaný v roce 2002 (cs) 2002 թվականի ապրիլին հրատարակված գիտական հոդված (hy) наукова стаття, опублікована у квітні 2002 (uk) 2002 թուականի Ապրիլին հրատարակուած գիտական յօդուած (hyw) wetenschappelijk artikel (gepubliceerd op 2002/04/19) (nl) vedecký článok (publikovaný 2002/04/19) (sk) مقالة علمية (نشرت في 19-4-2002) (ar) article publié dans la revue scientifique Journal of Biological Chemistry (fr) im April 2002 veröffentlichter wissenschaftlicher Artikel (de) scientific journal article (en) 2002 ഏപ്രില്‍ 19 നു പ്രസിദ്ധീകരിച്ച ശാസ്ത്ര ലേഖനം (ml)
publication date	wds:Q28568146-EB5DDE21-3F83-4E77-B39E-53D8C7F6922A
publication date	2002-04-19 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q28568146-B0A09938-122B-41D5-A5ED-DFFB6FB6B112
language of work or name	English
cites work	wds:Q28568146-0089A1EE-954B-4689-B9D7-4716225B52FD wds:Q28568146-07AB678B-2BFC-4062-97B2-2AA2555CED77 wds:Q28568146-08EA8E88-054E-4633-B81F-ADCB01BA8CB9 wds:Q28568146-12A23055-8268-40EC-BC93-BB96A5A8EA0B wds:Q28568146-1387380F-B3FF-497A-9D5A-C26B20C81E6F wds:Q28568146-17070DB3-8874-4AAF-B197-45FDF14815C6 wds:Q28568146-1903A3BD-1FDC-44AA-B9C4-47D5648533C0 wds:Q28568146-1C7BFB06-6D0E-4BA3-8B06-9D723710BB1D wds:Q28568146-35CF9A9C-D75F-45E1-AF43-57B705F9E581 wds:Q28568146-47642476-20D4-4104-8637-B97E87B7443A wds:Q28568146-4A7A9F77-2FCF-44C1-A00F-39B3CBE22820 wds:Q28568146-5031DCF8-5381-4056-9B2E-9BC1C4F351B8 wds:Q28568146-5531F60D-905C-4304-B90C-39366578B3E0 wds:Q28568146-59212FB0-3601-421D-8C00-C27666B461CE wds:Q28568146-660DCAA8-6033-41AD-A0CA-6B2D1AA7454B wds:Q28568146-6735E317-B1B9-4D8D-AFA4-7DE478D054E8 wds:Q28568146-774FFFC1-0183-432D-A55E-BEFEA71871EA wds:Q28568146-7ECB01CD-1404-4C51-AEAB-5AF7AECED69D wds:Q28568146-7FA4409F-0652-44F1-803A-1C750ADD732F wds:Q28568146-86B65C30-8FF3-4404-A1B7-4E50361F5DD8 wds:Q28568146-9219DCB4-763D-4E08-830B-97DFAED9F1BE wds:Q28568146-A1FE0D59-EE7F-4BA6-917B-2EBBC2469CFB wds:Q28568146-A505AB96-5954-4E97-8B72-E3F7A9DEB077 wds:Q28568146-BD66F307-141A-4F49-BD6F-E1BC0DB26480 wds:Q28568146-C2C24E31-DDBA-490C-B3C0-A2E29CE48895 wds:Q28568146-C5677B6A-D171-496C-AE54-40862EB6FA81 wds:Q28568146-CCA87D90-8762-4544-96DA-9C85E9F17480 wds:Q28568146-D080D0AA-11AB-4A12-A514-0AE9C0C3B11C wds:Q28568146-D6A0592E-609E-45EE-B49D-29F1251CF4BE wds:Q28568146-D87C9934-A166-4063-BE61-B0AF55748AB2 wds:Q28568146-E1AA4CF7-E06A-4189-A8B6-F329C51455D9 wds:Q28568146-E5973E90-F438-48D6-9FA8-C558D3069316 wds:Q28568146-E5CF446C-F622-419A-B743-87213FB36C6E wds:Q28568146-F37894F0-E7DD-4A6C-BD0A-A517ABA6A4DB wds:Q28568146-F62021A2-DDA9-489D-A95E-FA5458491844
cites work	The phosphotyrosine interaction domains of X11 and FE65 bind to distinct sites on the YENPTY motif of amyloid precursor protein Insulin-degrading enzyme regulates extracellular levels of amyloid beta-protein by degradation The intracellular cytoplasmic domain of the Alzheimer's disease amyloid precursor protein interacts with phosphotyrosine-binding domain proteins in the yeast two-hybrid system Isolation of intracellular membranes by means of sodium carbonate treatment: application to endoplasmic reticulum A portrait of Alzheimer secretases--new features and familiar faces Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa Identification of the major Abeta1-42-degrading catabolic pathway in brain parenchyma: suppression leads to biochemical and pathological deposition Degradation of Alzheimer's beta-amyloid protein by human and rat brain peptidases: involvement of insulin-degrading enzyme. Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and gamma-secretase activity Mutation of the beta-amyloid precursor protein in familial Alzheimer's disease increases beta-protein production Glycine 384 is required for presenilin-1 function and is conserved in bacterial polytopic aspartyl proteases Total inactivation of gamma-secretase activity in presenilin-deficient embryonic stem cells. Metabolism of the "Swedish" amyloid precursor protein variant in neuro2a (N2a) cells. Evidence that cleavage at the "beta-secretase" site occurs in the golgi apparatus Presenilin-dependent gamma-secretase processing of beta-amyloid precursor protein at a site corresponding to the S3 cleavage of Notch The cell biology of Alzheimer's disease: uncovering the secrets of secretases Metabolic regulation of brain Abeta by neprilysin. A presenilin-1-dependent gamma-secretase-like protease mediates release of Notch intracellular domain wd:Q22251293 Notch signaling: from the outside in Mice lacking both presenilin genes exhibit early embryonic patterning defects Alzheimer's beta-amyloid peptide specifically interacts with and is degraded by insulin degrading enzyme Characterization of a presenilin-mediated amyloid precursor protein carboxyl-terminal fragment gamma. Evidence for distinct mechanisms involved in gamma -secretase processing of the APP and Notch1 transmembrane domains Functional interaction between SEL-10, an F-box protein, and the nuclear form of activated Notch1 receptor The Notch intracellular domain is ubiquitinated and negatively regulated by the mammalian Sel-10 homolog The amyloid precursor protein (APP)-cytoplasmic fragment generated by gamma-secretase is rapidly degraded but distributes partially in a nuclear fraction of neurones in culture Thimet oligopeptidase and oligopeptidase M or neurolysin. A transcriptionally [correction of transcriptively] active complex of APP with Fe65 and histone acetyltransferase Tip60 The intracellular domain of the beta-amyloid precursor protein is stabilized by Fe65 and translocates to the nucleus in a notch-like manner Clearing the brain's amyloid cobwebs The regions of the Fe65 protein homologous to the phosphotyrosine interaction/phosphotyrosine binding domain of Shc bind the intracellular domain of the Alzheimer's amyloid precursor protein Development and characterization of novel potent and stable inhibitors of endopeptidase EC 3.4.24.15. Inhibition of insulin degradation by hepatoma cells after microinjection of monoclonal antibodies to a specific cytosolic protease An unusual active site identified in a family of zinc metalloendopeptidases A Novel γ-Secretase Assay Based on Detection of the Putative C-terminal Fragment-γ of Amyloid β Protein Precursor Neprilysin degrades both amyloid beta peptides 1-40 and 1-42 most rapidly and efficiently among thiorphan- and phosphoramidon-sensitive endopeptidases
author name string	wds:Q28568146-462BC90C-E3B8-4C35-A68C-BFCDA82C2499 wds:Q28568146-C9B38913-87B0-46DB-92FF-420E08D61F1F wds:Q28568146-FEBDB901-876B-4E0B-BD74-D6E12BC8E857
OpenCitations bibliographic resource ID	wds:Q28568146-C66791E8-BA50-4AEC-9638-68C6982565A4
OpenCitations bibliographic resource ID	https://w3id.org/oc/corpus/br/4742121
author name string	Harald Steiner Michael Willem Sven Lammich
OpenCitations bibliographic resource ID	4742121
rdfs:label	Insulin-degrading enzyme rapidly removes the beta-amyloid precursor protein intracellular domain (AICD) (en) Insulin-degrading enzyme rapidly removes the beta-amyloid precursor protein intracellular domain (AICD) (nl) Insulin-degrading enzyme rapidly removes the beta-amyloid precursor protein intracellular domain (AICD) (ast)
skos:prefLabel	Insulin-degrading enzyme rapidly removes the beta-amyloid precursor protein intracellular domain (AICD) (en)

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