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Presenilin-1 differentially facilitates endoproteolysis of the [beta]-amyloid precursor protein and...

Presenilin-1 differentially facilitates endoproteolysis of the [beta]-amyloid precursor protein and...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_journals_222278798

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

About this item

Full title

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

Publisher

London: Nature Publishing Group

Journal title

Nature cell biology, 2000-04, Vol.2 (4), p.205

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group

More information

Scope and Contents

Contents

Mutations in the presenilin-1 (PS1) gene are associated with Alzheimer's disease and cause increased secretion of the neurotoxic amyloid-beta peptide (Abeta). Critical intramembraneous aspartates at residues 257 and 385 are required for the function of PS1 protein. Here we investigate the biological function of a naturally occurring PS1 splice vari...

Alternative Titles

Full title

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

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_proquest_journals_222278798

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_journals_222278798

Other Identifiers

ISSN

1465-7392

E-ISSN

1476-4679

DOI

10.1038/35008626

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