ArticleThe Journal of biological chemistry2012
Contribution of the γ-secretase subunits to the formation of catalytic pore of presenilin 1 protein.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 29 citations in OpenAlex.
- Article
- Article
- The PSEN1 E280G mutation leads to increased amyloid-β43 production in induced pluripotent stem cell neurons and deposition in brain tissue.Brain communications · 2023Article
- PSEN2 Thr421Met Mutation in a Patient with Early Onset Alzheimer's Disease.International journal of molecular sciences · 2022Article
- Structure and Function of the γ-Secretase Complex.Biochemistry · 2019Article
- NGP 555, a γ-Secretase Modulator, Lowers the Amyloid Biomarker, AβAlzheimer's & dementia (New York, N. Y.) · 2017Article
- Conformational Changes in Transmembrane Domain 4 of Presenilin 1 Are Associated with Altered Amyloid-β 42 Production.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2016Article
- Therapies for Prevention and Treatment of Alzheimer's Disease.BioMed research international · 2016Review
- Article
- An atomic structure of human γ-secretase.Nature · 2015Article
- Natural Product and Natural Product-Derived Gamma Secretase Modulators fromMedicines (Basel, Switzerland) · 2015Review
- Cooperative roles of hydrophilic loop 1 and the C-terminus of presenilin 1 in the substrate-gating mechanism of γ-secretase.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2015Article
- Allosteric regulation of γ-secretase activity by a phenylimidazole-type γ-secretase modulator.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Involvement of the Notch pathway in terminal astrocytic differentiation: role of PKA.ASN neuro · 2013Article
- Biological function of Presenilin and its role in AD pathogenesis.Translational neurodegeneration · 2013Article
- Structural biology of presenilins and signal peptide peptidases.The Journal of biological chemistry · 2013Review
- A patient with posterior cortical atrophy possesses a novel mutation in the presenilin 1 gene.PloS one · 2013Article
- Generation of amyloid-β is reduced by the interaction of calreticulin with amyloid precursor protein, presenilin and nicastrin.PloS one · 2013Article
- Modulation of gamma-secretase for the treatment of Alzheimer's disease.International journal of Alzheimer's disease · 2012Article
- γ-Secretase-Dependent Proteolysis of Transmembrane Domain of Amyloid Precursor Protein: Successive Tri- and Tetrapeptide Release in Amyloid β-Protein Production.International journal of Alzheimer's disease · 2012Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
γ-Secretase is an intramembrane-cleaving protease related to the etiology of Alzheimer disease. γ-Secretase is a membrane protein complex composed of presenilin (PS) and three indispensable subunits: nicastrin, Aph-1, and Pen-2. PS functions as a protease subunit forming a hydrophilic catalytic pore structure within the lipid bilayer. However, it remains unclear how other subunits are involved in the pore formation. Here, we show that the hydrophilic pore adopted with an open conformation has already been formed by PS within the immature γ-secretase complex. The binding of the subunits induces the close proximity between transmembrane domains facing the catalytic pore. We propose a model in which the γ-secretase subunits restrict the arrangement of the transmembrane domains of PS during the formation of the functional structure of the catalytic pore.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.