About: The intracellular domain of the beta-amyloid precursor protein is stabilized by Fe65 and translocates to the nucleus in a notch-like manner

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About: The intracellular domain of the beta-amyloid precursor protein is stabilized by Fe65 and translocates to the nucleus in a notch-like manner Goto Sponge NotDistinct Permalink

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scientific journal article

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rdf:type	Item
description	artículu científicu espublizáu en 2001 (ast) vědecký článek publikovaný v roce 2001 (cs) 2001 թվականի հոտեմբերին հրատարակված գիտական հոդված (hy) 2001 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած (hyw) наукова стаття, опублікована в жовтні 2001 (uk) wetenschappelijk artikel (gepubliceerd op 2001/10/26) (nl) vedecký článok (publikovaný 2001/10/26) (sk) مقالة علمية (نشرت في 26-10-2001) (ar) article publié dans la revue scientifique Journal of Biological Chemistry (fr) im Oktober 2001 veröffentlichter wissenschaftlicher Artikel (de) scientific journal article (en)
publication date	wds:Q28510317-FF0DC79A-C6F9-4BEA-8196-B4410D3BA056
publication date	2001-10-26 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q28510317-73DFA8F1-246F-48B1-8661-DCC35E219BFC
language of work or name	English
author name string	wds:Q28510317-3D361209-018B-4C8F-840D-3F2AA218E8A2 wds:Q28510317-70928935-9F3F-4F2F-B4C6-8FC03468B637 wds:Q28510317-87768BD7-5EC0-4D40-83E2-6822CA913F50 wds:Q28510317-8DDFD3D3-FFCD-4C65-A7B9-917D4859F48E
OpenCitations bibliographic resource ID	wds:Q28510317-B1C67FC9-95F0-4D1D-AAA7-0EC7DD8E3D6C
OpenCitations bibliographic resource ID	https://w3id.org/oc/corpus/br/1661869
author name string	D. J. Selkoe J. B. Zheng S. Y. Guénette W. T. Kimberly
OpenCitations bibliographic resource ID	1661869
rdfs:label	The intracellular domain of the beta-amyloid precursor protein is stabilized by Fe65 and translocates to the nucleus in a notch-like manner (en) The intracellular domain of the beta-amyloid precursor protein is stabilized by Fe65 and translocates to the nucleus in a notch-like manner (nl) The intracellular domain of the beta-amyloid precursor protein is stabilized by Fe65 and translocates to the nucleus in a notch-like manner (ast)
skos:prefLabel	The intracellular domain of the beta-amyloid precursor protein is stabilized by Fe65 and translocates to the nucleus in a notch-like manner (en) The intracellular domain of the beta-amyloid precursor protein is stabilized by Fe65 and translocates to the nucleus in a notch-like manner (nl) The intracellular domain of the beta-amyloid precursor protein is stabilized by Fe65 and translocates to the nucleus in a notch-like manner (ast)
name	The intracellular domain of the beta-amyloid precursor protein is stabilized by Fe65 and translocates to the nucleus in a notch-like manner (en) The intracellular domain of the beta-amyloid precursor protein is stabilized by Fe65 and translocates to the nucleus in a notch-like manner (nl) The intracellular domain of the beta-amyloid precursor protein is stabilized by Fe65 and translocates to the nucleus in a notch-like manner (ast)
title	wds:Q28510317-5EDBF11A-4A27-41D3-9491-BA4036D163E3
title	The intracellular domain of the beta-amyloid precursor protein is stabilized by Fe65 and translocates to the nucleus in a notch-like manner (en)
page(s)	wds:Q28510317-AA695611-1749-4B95-8E8A-CAD6A018C0CB
page(s)	40288–40292
instance of	wds:Q28510317-48D601D6-FFEC-4D2B-828E-19F5E0A33BC6
instance of	scholarly article
main subject	wds:Q28510317-1EFCAF03-8BCB-4B80-9613-E22E309C005E wds:Q28510317-94671A7D-1622-4C2F-A1D3-669BE1A87D10
main subject	Amyloid beta (A4) precursor protein-binding, family B, member 1 Amyloid beta (A4) precursor protein-binding, family B, member 2
PubMed ID	wds:Q28510317-14F5633E-49B8-4D86-9A49-45F15D5F03B5
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/11544248
PubMed ID	11544248
published in	wds:Q28510317-630926A3-EB6E-4D09-A0DE-529BF684AB1F
published in	Journal of Biological Chemistry
issue	wds:Q28510317-D2BE46C3-157E-47BC-8156-E821B84B2AB5
volume	wds:Q28510317-D1AA5931-B6A7-4F49-8E46-8CD8E20B6452
issue	43
volume	276
DOI	wds:Q28510317-5AC776DD-7465-425A-9F10-EB0A37A46F51
DOI	http://dx.doi.org/10.1074/JBC.C100447200
DOI	10.1074/JBC.C100447200
ResearchGate publication ID	wds:Q28510317-DDE37AA6-F9A6-46D6-8FD5-83625F633882
ResearchGate publication ID	11802705
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q28510317
is cites work of	Pathways towards and away from Alzheimer's disease Reversal of learning deficits in hAPP transgenic mice carrying a mutation at Asp664: a role for early experience Long-term prevention of Alzheimer's disease-like behavioral deficits in PDAPP mice carrying a mutation in Asp664. The Fas ligand intracellular domain is released by ADAM10 and SPPL2a cleavage in T-cells The intracellular domain of amyloid precursor protein interacts with flotillin-1, a lipid raft protein A pilot proteomic study of amyloid precursor interactors in Alzheimer's disease Neprilysin gene expression requires binding of the amyloid precursor protein intracellular domain to its promoter: implications for Alzheimer disease Physiological functions of APP family proteins The Ubiquitin-Proteasome System and Molecular Chaperone Deregulation in Alzheimer's Disease Amyloid precursor proteins are protective in Drosophila models of progressive neurodegeneration Generation of the β-Amyloid Peptide and the Amyloid Precursor Protein C-terminal Fragment γ Are Potentiated by FE65L1 Amyloid-β peptide: Dr. Jekyll or Mr. Hyde? Calcium dyshomeostasis and intracellular signalling in Alzheimer's disease The multifaceted nature of amyloid precursor protein and its proteolytic fragments: friends and foes The many substrates of presenilin/γ-secretase Epigenetic mechanisms in memory formation. Nerve growth factor, neural stem cells and Alzheimer's disease Activation of GSK-3 and phosphorylation of CRMP2 in transgenic mice expressing APP intracellular domain Alteration of intracellular structure and function of glyceraldehyde-3-phosphate dehydrogenase: a common phenotype of neurodegenerative disorders? The ABCA2 transporter: intracellular roles in trafficking and metabolism of LDL-derived cholesterol and sterol-related compounds. Embryonic stem cell-derived neurons as a cellular system to study gene function: lack of amyloid precursor proteins APP and APLP2 leads to defective synaptic transmission Biology and pathophysiology of the amyloid precursor protein Regulation of APP-dependent transcription complexes by Mint/X11s: differential functions of Mint isoforms Intramembrane-cleaving proteases: controlled liberation of proteins and bioactive peptides The in vivo brain interactome of the amyloid precursor protein Presenilin/gamma-secretase-dependent processing of beta-amyloid precursor protein regulates EGF receptor expression All in the Family: How the APPs Regulate Neurogenesis γ-Secretase-regulated mechanisms similar to notch signaling may play a role in signaling events, including APP signaling, which leads to Alzheimer's disease Effects of Alzheimer's amyloid-beta and tau protein on mitochondrial function -- role of glucose metabolism and insulin signalling Identity and function of γ‐secretase The Notch ligands, Jagged and Delta, are sequentially processed by alpha-secretase and presenilin/gamma-secretase and release signaling fragments Hydrogen peroxide promotes Abeta production through JNK-dependent activation of gamma-secretase Apoptotic cell death and amyloid precursor protein signaling in neuroblastoma SH-SY5Y cells. Reduced hippocampal insulin-degrading enzyme in late-onset Alzheimer's disease is associated with the apolipoprotein E-epsilon4 allele Roles of amyloid precursor protein and its fragments in regulating neural activity, plasticity and memory Transcriptional regulation of human FE65, a ligand of Alzheimer's disease amyloid precursor protein, by Sp1 Dexras1 interacts with FE65 to regulate FE65-amyloid precursor protein-dependent transcription Insulin-degrading enzyme rapidly removes the beta-amyloid precursor protein intracellular domain (AICD) Direct visualization of the gamma secretase-generated carboxyl-terminal domain of the amyloid precursor protein: association with Fe65 and translocation to the nucleus

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