(Q28568146)

31 January 2017

title

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

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31 January 2017

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Christian Haass

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Dieter Edbauer

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object named as

Dieter Edbauer

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31 January 2017

Michael Willem

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31 January 2017

Sven Lammich

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31 January 2017

Harald Steiner

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31 January 2017

language of work or name

English

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publication date

19 April 2002

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Journal of Biological Chemistry

31 January 2017

published in

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31 January 2017

volume

277

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31 January 2017

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31 January 2017

page(s)

13389–13393

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https://api.crossref.org/works/10.1074%2FJBC.M111571200

31 January 2017

1 reference

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Total inactivation of gamma-secretase activity in presenilin-deficient embryonic stem cells.

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Presenilin-dependent gamma-secretase processing of beta-amyloid precursor protein at a site corresponding to the S3 cleavage of Notch

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A transcriptionally [correction of transcriptively] active complex of APP with Fe65 and histone acetyltransferase Tip60

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The phosphotyrosine interaction domains of X11 and FE65 bind to distinct sites on the YENPTY motif of amyloid precursor protein

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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

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The intracellular cytoplasmic domain of the Alzheimer's disease amyloid precursor protein interacts with phosphotyrosine-binding domain proteins in the yeast two-hybrid system

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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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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

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The Notch intracellular domain is ubiquitinated and negatively regulated by the mammalian Sel-10 homolog

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Functional interaction between SEL-10, an F-box protein, and the nuclear form of activated Notch1 receptor

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Mutation of the beta-amyloid precursor protein in familial Alzheimer's disease increases beta-protein production

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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

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Inhibition of insulin degradation by hepatoma cells after microinjection of monoclonal antibodies to a specific cytosolic protease

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Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa

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Isolation of intracellular membranes by means of sodium carbonate treatment: application to endoplasmic reticulum

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Thimet oligopeptidase and oligopeptidase M or neurolysin.

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Development and characterization of novel potent and stable inhibitors of endopeptidase EC 3.4.24.15.

21 January 2018

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An unusual active site identified in a family of zinc metalloendopeptidases

21 January 2018

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Insulin-degrading enzyme regulates extracellular levels of amyloid beta-protein by degradation

21 January 2018

1 reference

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Degradation of Alzheimer's beta-amyloid protein by human and rat brain peptidases: involvement of insulin-degrading enzyme

21 January 2018

1 reference

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Alzheimer's beta-amyloid peptide specifically interacts with and is degraded by insulin degrading enzyme

21 January 2018

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Identification of the major Abeta1-42-degrading catabolic pathway in brain parenchyma: suppression leads to biochemical and pathological deposition

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Metabolic regulation of brain Abeta by neprilysin

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Neprilysin degrades both amyloid beta peptides 1-40 and 1-42 most rapidly and efficiently among thiorphan- and phosphoramidon-sensitive endopeptidases

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A Novel γ-Secretase Assay Based on Detection of the Putative C-terminal Fragment-γ of Amyloid β Protein Precursor

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21 January 2018

Identifiers

DOI

10.1074/JBC.M111571200

1 reference

Consolidated OpenCitations Corpus – April 2017

1 reference

Consolidated OpenCitations Corpus – April 2017

1 reference

Consolidated OpenCitations Corpus – April 2017