Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Characterization of the reconstituted gamma-secretase complex from Sf9 cells co-expressing presenilin 1, nicastrin [correction of nacastrin], aph-1a, and pen-2.

Biochemistry - 22 Mar 2005

Zhang Lili, Lee Julie, Song Lixin, Sun Xiaoyan, Shen Jie, Terracina Giuseppe, Parker Eric M

Abstract excerpt

Gamma-secretase catalyzes the proteolytic processing of a number of integral membrane proteins, including amyloid precursor protein (APP) and Notch. The native gamma-secretase is a heterogeneous population of large membrane protein complexes containing presenilin 1 (PS1) or presenilin 2 (PS2), aph-1a or aph-1b, nicastrin, and pen-2. Here we report the reconstitution of a gamma-secretase complex in Sf9 cells by...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amyloid Precursor Protein Secretases
Share to Aspartic Acid Endopeptidases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Baculoviridae

Share to Endopeptidases

Share to Multiprotein Complexes

Share to Peptide Hydrolases

Share to Presenilin-1

Share to Spodoptera

Source

Identifiers

PMID: 15766275
DOI: 10.1021/bi0481500

Genes

APP

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Characterization of the reconstituted gamma-secretase complex from Sf9 cells co-expressing presenilin 1, nicastrin [correction of nacastrin], aph-1a, and pen-2.PMID 15766275Read ↗

Co-expression of nicastrin and presenilin rescues a loss of function mutant of APH-1.Semantic proximity Read ↗

Alzheimer's disease-linked mutations in presenilin-1 result in a drastic loss of activity in purified γ-secretase complexes.Semantic proximity Read ↗

Different cofactor activities in gamma-secretase assembly: evidence for a nicastrin-Aph-1 subcomplex.Semantic proximity Read ↗

Activation and intrinsic gamma-secretase activity of presenilin 1.Semantic proximity Read ↗

Presenilins mutated at Asp-257 or Asp-385 restore Pen-2 expression and Nicastrin glycosylation but remain catalytically inactive in the absence of wild type Presenilin.Semantic proximity Read ↗

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

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

In vivo reconstitution of gamma-secretase in Drosophila results in substrate specificity.Semantic proximity Read ↗

Intramembrane proteolysis by gamma-secretase.Semantic proximity Read ↗

Interactome analyses of mature γ-secretase complexes reveal distinct molecular environments of presenilin (PS) paralogs and preferential binding of signal peptide peptidase to PS2.Semantic proximity Read ↗

Increased expression of PS1 is sufficient to elevate the level and activity of γ-secretase in vivo.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 ↗

⌁Select a neighboring publication to make it the new centre.