(Q40967509)

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The biological and pathological function of the presenilin-1 Deltaexon 9 mutation is independent of its defect to undergo proteolytic processing

scientific article published on March 1999

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Europe PubMed Central

PubMed publication ID

25 September 2017

The biological and pathological function of the presenilin-1 Deltaexon 9 mutation is independent of its defect to undergo proteolytic processing (English)

1 reference

Europe PubMed Central

PubMed publication ID

25 September 2017

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Christian Haass

8

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Haass C

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25 September 2017

author name string

Steiner H

1

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Europe PubMed Central

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25 September 2017

Romig H

2

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Europe PubMed Central

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25 September 2017

Grim MG

3

1 reference

Europe PubMed Central

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25 September 2017

Philipp U

4

1 reference

Europe PubMed Central

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25 September 2017

Pesold B

5

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25 September 2017

Citron M

6

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25 September 2017

Baumeister R

7

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25 September 2017

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publication date

1 March 1999

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25 September 2017

Journal of Biological Chemistry

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25 September 2017

274

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25 September 2017

12

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Europe PubMed Central

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25 September 2017

7615-7618

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Europe PubMed Central

PubMed publication ID

25 September 2017

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

1 reference

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21 January 2018

Candidate gene for the chromosome 1 familial Alzheimer's disease locus

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21 January 2018

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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Mutant genes in familial Alzheimer's disease and transgenic models

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Amyloid beta-protein and the genetics of Alzheimer's disease

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Seeding "one-dimensional crystallization" of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie?

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21 January 2018

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

1 reference

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21 January 2018

Endoproteolysis of presenilin 1 and accumulation of processed derivatives in vivo

1 reference

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21 January 2018

Evidence that levels of presenilins (PS1 and PS2) are coordinately regulated by competition for limiting cellular factors

1 reference

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21 January 2018

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

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21 January 2018

Hyperaccumulation of FAD-linked presenilin 1 variants in vivo

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21 January 2018

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

1 reference

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21 January 2018

Different effects of Alzheimer-associated mutations of presenilin 1 on its processing

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21 January 2018

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

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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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21 January 2018

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

1 reference

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21 January 2018

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

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21 January 2018

Amyloid beta-peptide is produced by cultured cells during normal metabolism

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21 January 2018

Human presenilin-1, but not familial Alzheimer's disease (FAD) mutants, facilitate Caenorhabditis elegans Notch signalling independently of proteolytic processing

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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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21 January 2018

Assessment of normal and mutant human presenilin function in Caenorhabditis elegans

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21 January 2018

Familial Alzheimer's disease-linked presenilin 1 variants elevate Abeta1-42/1-40 ratio in vitro and in vivo

1 reference

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21 January 2018

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

1 reference

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21 January 2018

Presenilin Proteins Undergo Heterogeneous Endoproteolysis between Thr291and Ala299and Occur as Stable N- and C-Terminal Fragments in Normal and Alzheimer Brain Tissue

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Electrophoretic Separation of βA4 Peptides (1–40) and (1–42)

1 reference

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21 January 2018

Identifiers

10.1074/JBC.274.12.7615

1 reference

Europe PubMed Central

PubMed publication ID

25 September 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

25 September 2017

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