Presenilin 1 protein directly interacts with Bcl-2 (Q28145902)

L Gasparini

4

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Luisa Benussi

L Benussi

3

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Roberta Ghidoni

R Ghidoni

5

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John Growdon

10

J H Growdon

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author name string

A Alberici

1

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D Moratto

2

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L B Gatta

6

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G B Frisoni

8

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M Trabucchi

9

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R M Nitsch

11

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G Binetti

Journal of Biological Chemistry

12

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language of work or name

English

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publication date

22 October 1999

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published in

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volume

274

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issue

43

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page(s)

30764-9

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cites work

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Evidence for a six-transmembrane domain structure of presenilin 1.

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Endoproteolysis of presenilin 1 and accumulation of processed derivatives in vivo

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

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

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

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Calsenilin: a calcium-binding protein that interacts with the presenilins and regulates the levels of a presenilin fragment

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

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Direct association of presenilin-1 with beta-catenin

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Alzheimer-associated presenilin-2 confers increased sensitivity to apoptosis in PC12 cells

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

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

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Alternative cleavage of Alzheimer-associated presenilins during apoptosis by a caspase-3 family protease

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Destabilization of beta-catenin by mutations in presenilin-1 potentiates neuronal apoptosis

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Apoptosis. A sticky business.

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Suppression of signalling through transcription factor NF-AT by interactions between calcineurin and Bcl-2.

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Identification and characterization of a spinal muscular atrophy-determining gene

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Presenilin 1 binds to amyloid precursor protein directly.

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

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Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programmed cell death

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Chaperoning brain diseases.

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Interactions of the chaperone Hsp104 with yeast Sup35 and mammalian PrP.

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Chaperone-supervised conversion of prion protein to its protease-resistant form

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Identifiers

DOI

10.1074/JBC.274.43.30764

1 reference

Consolidated OpenCitations Corpus – April 2017

release_lqrpulgrmnc3dmsluglju7or5u

1810104

Fatcat ID

1 reference

Fatcat

https://api.fatcat.wiki/v0/release/lqrpulgrmnc3dmsluglju7or5u

mapped directly with Wikidata item

24 November 2022

based on heuristic

1810104

1 reference

Consolidated OpenCitations Corpus – April 2017

Consolidated OpenCitations Corpus – April 2017

1 reference