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

Modulation of γ-secretase activity by multiple enzyme-substrate interactions: implications in pathogenesis of Alzheimer's disease.

PloS one - 1 Jan 2012

Svedružić Zeljko M, Popović Katarina, Smoljan Ivana, Sendula-Jengić Vesna

Abstract excerpt

BACKGROUND: We describe molecular processes that can facilitate pathogenesis of Alzheimer's disease (AD) by analyzing the catalytic cycle of a membrane-imbedded protease γ-secretase, from the initial interaction with its C99 substrate to the final release of toxic Aβ peptides. RESULTS: The C-terminal AICD fragment is cleaved first in a pre-steady-state burst. The lowest Aβ42/Aβ40 ratio is observed in...

Read the complete abstract on PubMed

Topics

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

Share to Alanine
Share to Amyloid beta-Peptides
Share to Amyloid beta-Protein Precursor

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Amyloid Precursor Protein Secretases

Share to Azepines

Share to Biocatalysis

Share to Peptide Fragments

Share to Presenilin-1

Source

Open in PubMed Open full text

Identifiers

PMID: 22479317
DOI: 10.1371/journal.pone.0032293
PMCID: PMC3316526

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

Modulation of γ-secretase activity by multiple enzyme-substrate interactions: implications in pathogenesis of Alzheimer's disease.PMID 22479317Read ↗

Binding of different substrate molecules at the docking site and the active site of γ-secretase can trigger toxic events in sporadic and familial Alzheimer’s diseaseSemantic proximity Read ↗

Presenilin, γ-Secretase, and the Search for Pathogenic Triggers of Alzheimer's Disease.Semantic proximity Read ↗

Pathogenic Aβ generation in familial Alzheimer's disease: novel mechanistic insights and therapeutic implications.Semantic proximity Read ↗

γ-Secretase exosites as targets for substrate-selective lowering of Aβ generation.Semantic proximity Read ↗

{gamma}-Secretase Substrate Concentration Modulates the Abeta42/Abeta40 Ratio: IMPLICATIONS FOR ALZHEIMER DISEASE.Semantic proximity Read ↗

Alzheimer presenilin-1 mutations dramatically reduce trimming of long amyloid β-peptides (Aβ) by γ-secretase to increase 42-to-40-residue Aβ.Semantic proximity Read ↗

γ-Secretase structure and activity are modified by alterations in its membrane localization and ambient environment.Semantic proximity Read ↗

Independent relationship between amyloid precursor protein (APP) dimerization and γ-secretase processivity.Semantic proximity Read ↗

The mechanism of γ‐Secretase dysfunction in familial Alzheimer diseaseSemantic proximity Read ↗

Familial Alzheimer Mutations in Presenilin-1 Decrease APP Substrate Proteolysis by γ-Secretase via Stable Enzyme-Substrate Complex FormationSemantic proximity Read ↗

Structural Analysis of Simultaneous Activation and Inhibition of γ-Secretase Activity in Development of Drugs for Alzheimer’s diseaseSemantic proximity Read ↗

Closing in on the amyloid cascade: recent insights into the cell biology of Alzheimer's disease.Semantic proximity Read ↗

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