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Article

Requirement for small side chain residues within the GxGD-motif of presenilin for gamma-secretase substrate cleavage.

Journal of neurochemistry - 1 Feb 2010

Pérez-Revuelta Blanca Isabel, Fukumori Akio, Lammich Sven, Yamasaki Aya, Haass Christian, Steiner Harald

Abstract excerpt

gamma-Secretase is a pivotal intramembrane-cleaving protease complex and important drug target for Alzheimer's disease. The protease not only releases small peptides, such as the amyloid-beta peptide, which drives Alzheimer's disease pathogenesis, but also intracellular domains, which can have cr...

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Share to Amyloid beta-Protein Precursor
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 20021564
DOI: 10.1111/j.1471-4159.2009.06510.x

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-20021564-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

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Requirement for small side chain residues within the GxGD-motif of presenilin for gamma-secretase substrate cleavage.PMID 20021564Read ↗

Important functional role of residue x of the presenilin GxGD protease active site motif for APP substrate cleavage specificity and substrate selectivity of γ-secretase.Semantic proximity Read ↗

Mutation analysis of the presenilin 1 N-terminal domain reveals a broad spectrum of gamma-secretase activity toward amyloid precursor protein and other substrates.Semantic proximity Read ↗

Presenilin transmembrane domain 8 conserved AXXXAXXXG motifs are required for the activity of the γ-secretase complex.Semantic proximity Read ↗

Three-amino acid spacing of presenilin endoproteolysis suggests a general stepwise cleavage of gamma-secretase-mediated intramembrane proteolysis.Semantic proximity Read ↗

Hydrophilic loop 1 of Presenilin-1 and the APP GxxxG transmembrane motif regulate γ-secretase function in generating Alzheimer-causing Aβ peptides.Semantic proximity Read ↗

Intramembrane proteolysis of GXGD-type aspartyl proteases is slowed by a familial Alzheimer disease-like mutation.Semantic proximity Read ↗

C-terminal PAL motif of presenilin and presenilin homologues required for normal active site conformation.Semantic proximity Read ↗

Intramembrane proteolysis by gamma-secretase.Semantic proximity Read ↗

Structure and function of gamma-secretase.Semantic proximity Read ↗

Residues at P2-P1 positions of epsilon- and zeta-cleavage sites are important in formation of beta-amyloid peptide.Semantic proximity Read ↗

Functional domains in presenilin 1: the Tyr-288 residue controls gamma-secretase activity and endoproteolysis.Semantic proximity Read ↗

Pen-2 is essential for γ-secretase complex stability and trafficking but partially dispensable for endoproteolysis.Semantic proximity Read ↗

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