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Generation of aggregation prone N-terminally truncated amyloid [beta] peptides by meprin [beta] depe...

Generation of aggregation prone N-terminally truncated amyloid [beta] peptides by meprin [beta] depe...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_gale_infotracmisc_A443754331

Generation of aggregation prone N-terminally truncated amyloid [beta] peptides by meprin [beta] depends on the sequence specificity at the cleavage site

About this item

Full title

Generation of aggregation prone N-terminally truncated amyloid [beta] peptides by meprin [beta] depends on the sequence specificity at the cleavage site

Publisher

BioMed Central Ltd

Journal title

Molecular Neurodegeneration, 2016, Vol.11 (19)

Language

English

Formats

Publication information

Publisher

BioMed Central Ltd

More information

Scope and Contents

Contents

The metalloprotease meprin [beta] cleaves the Alzheimer's Disease (AD) relevant amyloid precursor protein (APP) as a [beta]-secretase reminiscent of BACE-1, however, predominantly generating N-terminally truncated A[beta]2-x variants. Herein, we observed increased endogenous sAPP[alpha] levels in the brains of meprin [beta] knock-out (ko) mice comp...

Alternative Titles

Full title

Generation of aggregation prone N-terminally truncated amyloid [beta] peptides by meprin [beta] depends on the sequence specificity at the cleavage site

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_gale_infotracmisc_A443754331

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_gale_infotracmisc_A443754331

Other Identifiers

ISSN

1750-1326

E-ISSN

1750-1326

DOI

10.1186/s13024-016-0084-5

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