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Article

Specific Mutations in Aph1 Cause γ-Secretase Activation.

International journal of molecular sciences - 3 Jan 2022

Watanabe Hikari, Yoshida Chika, Hidaka Masafumi, Ogawa Tomohisa, Tomita Taisuke, Futai Eugene

Abstract excerpt

Amyloid beta peptides (Aβs) are generated from amyloid precursor protein (APP) through multiple cleavage steps mediated by γ-secretase, including endoproteolysis and carboxypeptidase-like trimming. The generation of neurotoxic Aβ42/43 species is enhanced by familial Alzheimer's disease (FAD) mutations within the catalytic subunit of γ-secretase, presenilin 1 (PS1). FAD mutations of PS1 cause partial...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 35008932
DOI: 10.3390/ijms23010507
PMCID: PMC8745412

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Specific Mutations in Aph1 Cause γ-Secretase Activation.PMID 35008932Read ↗

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Nicastrin is dispensable for gamma-secretase protease activity in the presence of specific presenilin mutations.Semantic proximity Read ↗

APH-1a Is the Principal Mammalian APH-1 Isoform Present in γ-Secretase Complexes during Embryonic DevelopmentSemantic proximity Read ↗

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