Glycogen synthase kinase-3beta regulates presenilin 1 C-terminal fragment levels (Q46731928)

24 December 2017

title

Glycogen synthase kinase-3beta regulates presenilin 1 C-terminal fragment levels (English)

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24 December 2017

author name string

Kirschenbaum F

1

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24 December 2017

Hsu SC

2

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24 December 2017

Cordell B

3

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24 December 2017

McCarthy JV

4

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24 December 2017

language of work or name

English

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publication date

11 June 2001

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24 December 2017

Journal of Biological Chemistry

published in

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24 December 2017

volume

276

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24 December 2017

issue

33

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24 December 2017

page(s)

30701-30707

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24 December 2017

Presenilin mutations in Alzheimer's disease

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Characterization of human presenilin 1 using N-terminal specific monoclonal antibodies: Evidence that Alzheimer mutations affect proteolytic processing.

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Endoproteolytic processing and stabilization of wild-type and mutant presenilin

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Expression of Alzheimer's disease-associated presenilin-1 is controlled by proteolytic degradation and complex formation

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Distinct processing of endogenous and overexpressed recombinant presenilin 1.

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

21 January 2018

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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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Dual roles of proteasome in the metabolism of presenilin 1.

21 January 2018

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Presenilin 1 interaction in the brain with a novel member of the Armadillo family

21 January 2018

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Presenilins interact with armadillo proteins including neural-specific plakophilin-related protein and beta-catenin

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

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Direct association of presenilin-1 with beta-catenin

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Abrogation of the presenilin 1/beta-catenin interaction and preservation of the heterodimeric presenilin 1 complex following caspase activation

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Presenilin 1 associates with glycogen synthase kinase-3beta and its substrate tau

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Primary structure, tissue distribution, and expression of mouse phosphoinositide-dependent protein kinase-1, a protein kinase that phosphorylates and activates protein kinase Czeta

21 January 2018

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Proteolytic fragments of the Alzheimer's disease associated presenilins-1 and -2 are phosphorylated in vivo by distinct cellular mechanisms

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Proteolytic processing of the Alzheimer disease-associated presenilin-1 generates an in vivo substrate for protein kinase C.

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Evidence for phosphorylation and oligomeric assembly of presenilin 1.

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Presenilin 1 is required for Notch1 and DII1 expression in the paraxial mesoderm

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Presenilin 2 deficiency causes a mild pulmonary phenotype and no changes in amyloid precursor protein processing but enhances the embryonic lethal phenotype of presenilin 1 deficiency

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

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Wnt signaling in oncogenesis and embryogenesis--a look outside the nucleus

21 January 2018

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Identification of ubiquilin, a novel presenilin interactor that increases presenilin protein accumulation

21 January 2018

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Requirement of the familial Alzheimer's disease gene PS2 for apoptosis. Opposing effect of ALG-3

21 January 2018

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Participation of presenilin 2 in apoptosis: enhanced basal activity conferred by an Alzheimer mutation

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Evidence That Intramolecular Associations between Presenilin Domains Are Obligatory for Endoproteolytic Processing

21 January 2018

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Presenilins, the endoplasmic reticulum, and neuronal apoptosis in Alzheimer's disease.

21 January 2018

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21 January 2018

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21 January 2018

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Overexpression of a C-terminal fragment of presenilin 1 delays anti-Fas induced apoptosis in Jurkat cells.

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21 January 2018

Identifiers

DOI

10.1074/JBC.M102849200

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24 December 2017

PubMed ID

11402035

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24 December 2017