Nicastrin binds to membrane-tethered Notch (Q43694706)

25 November 2017

Nicastrin binds to membrane-tethered Notch (English)

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Rogaeva E

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Kawarai T

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Chen F

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Yu G

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Arawaka S

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Nishimura M

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Yu H

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Tandon A

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Supala A

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Song YQ

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Milman P

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Sato C

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Yu C

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Janus C

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Lee J

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Song L

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Zhang L

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Fraser PE

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St George-Hyslop PH

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1 August 2001

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3

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751-754

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https://scigraph.springernature.com/pub.10.1038/35087069

25 November 2017

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cites work

Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease

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7 January 2021

Familial Alzheimer's disease in kindreds with missense mutations in a gene on chromosome 1 related to the Alzheimer's disease type 3 gene

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7 January 2021

Nicastrin modulates presenilin-mediated notch/glp-1 signal transduction and betaAPP processing

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7 January 2021

Mutant presenilins of Alzheimer's disease increase production of 42-residue amyloid beta-protein in both transfected cells and transgenic mice

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7 January 2021

Deficiency of presenilin-1 inhibits the normal cleavage of amyloid precursor protein

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7 January 2021

Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and gamma-secretase activity

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7 January 2021

Photoactivated gamma-secretase inhibitors directed to the active site covalently label presenilin 1

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7 January 2021

Facilitation of lin-12-mediated signalling by sel-12, a Caenorhabditis elegans S182 Alzheimer's disease gene

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7 January 2021

Neurogenic phenotypes and altered Notch processing in Drosophila Presenilin mutants.

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7 January 2021

Presenilin is required for activity and nuclear access of Notch in Drosophila

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7 January 2021

A presenilin-1-dependent gamma-secretase-like protease mediates release of Notch intracellular domain

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7 January 2021

Notch-1 signalling requires ligand-induced proteolytic release of intracellular domain

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7 January 2021

The presenilin 1 protein is a component of a high molecular weight intracellular complex that contains beta-catenin

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7 January 2021

The proteolytic fragments of the Alzheimer's disease-associated presenilin-1 form heterodimers and occur as a 100-150-kDa molecular mass complex

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7 January 2021

Evidence for a physical interaction between presenilin and Notch

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7 January 2021

Formation of stable complexes between two Alzheimer's disease gene products: presenilin-2 and beta-amyloid precursor protein

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7 January 2021

Interaction between amyloid precursor protein and presenilins in mammalian cells: implications for the pathogenesis of Alzheimer disease

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7 January 2021

Stable association of presenilin derivatives and absence of presenilin interactions with APP.

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7 January 2021

Calpain inhibitor I increases beta-amyloid peptide production by inhibiting the degradation of the substrate of gamma-secretase. Evidence that substrate availability limits beta-amyloid peptide production

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7 January 2021

Characterization of new polyclonal antibodies specific for 40 and 42 amino acid-long amyloid beta peptides: their use to examine the cell biology of presenilins and the immunohistochemistry of sporadic Alzheimer's disease and cerebral amyloid angiop

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7 January 2021

Cell surface presenilin-1 participates in the gamma-secretase-like proteolysis of Notch

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7 January 2021

The presenilins in Alzheimer's disease--proteolysis holds the key.

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7 January 2021

Separation of presenilin function in amyloid beta-peptide generation and endoproteolysis of Notch

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7 January 2021

Presenilin-1 differentially facilitates endoproteolysis of the beta-amyloid precursor protein and Notch

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7 January 2021

Mutation of the conserved N-terminal cysteine (Cys92) of human presenilin 1 causes increased A beta42 secretion in mammalian cells but impaired Notch/lin-12 signalling in C. elegans

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7 January 2021

New protease inhibitors prevent gamma-secretase-mediated production of Abeta40/42 without affecting Notch cleavage

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7 January 2021

Carboxyl-terminal fragments of Alzheimer beta-amyloid precursor protein accumulate in restricted and unpredicted intracellular compartments in presenilin 1-deficient cells.

1 reference

7 January 2021

Identifiers

DOI

10.1038/35087069

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25 November 2017

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