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

1 Jan 1997

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PMID: 9173929
DOI: 10.1006/nbdi.1997.0129

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Presenilin Proteins Undergo Heterogeneous Endoproteolysis between Thr291and Ala299and Occur as Stable N- and C-Terminal Fragments in Normal and Alzheimer Brain TissuePMID 9173929Read ↗

Endoproteolysis of Presenilin 1 and Accumulation of Processed Derivatives In VivoSemantic proximity Read ↗

Presenilin-1 adopts pathogenic conformation in normal aging and in sporadic Alzheimer’s diseaseSemantic proximity Read ↗

Presenilin structure, function and role in Alzheimer disease.Semantic proximity Read ↗

Presenilins: molecular switches between proteolysis and signal transductionSemantic proximity Read ↗

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

The presenilins.Semantic proximity Read ↗

Intramembrane proteolysis by presenilins.Semantic proximity Read ↗

Endoproteolytic Processing and Stabilization of Wild-type and Mutant PresenilinSemantic proximity Read ↗

Presenilins, processing of beta-amyloid precursor protein, and notch signaling.Semantic proximity Read ↗

The presenilin proteins are components of multiple membrane-bound complexes that have different biological activities.Semantic proximity Read ↗

Intramembrane proteolysis by presenilin and presenilin-like proteases.Semantic proximity Read ↗

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

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