ReviewBiochimica et biophysica acta. Biomembranes2020
Substrate recognition and processing by γ-secretase.
Review in Biochimica et biophysica acta. Biomembranes, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers, 1 of them a synthesis that pooled it.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
26 citing papers in PubMed, 1 synthesis or guideline pooled it, 44 citations in OpenAlex.
- Pooled it
- The γ-secretase complex: from discovery to a therapeutic target.RSC chemical biology · 2026Review
- Conformational Flexibility of Transmembrane Helices: How it Works and Where it Matters.Chemical reviews · 2026Review
- Understanding the role of NOTCH2 mutation in centronuclear myopathy.Molecular therapy : the journal of the American Society of Gene Therapy · 2025Article
- γ-Secretase-Mediated Endoproteolysis of Neuregulin-1 and E-Cadherin.Biochemistry · 2025Article
- The N-terminal PA domains of signal-peptide-peptidase-like 2 (SPPL2) proteases impact on TNFα cleavage.Communications biology · 2025Article
- Potential drugs for the treatment of Alzheimer's disease.Pharmacological reports : PR · 2023Review
- Different transmembrane domains determine the specificity and efficiency of the cleavage activity of the γ-secretase subunit presenilin.The Journal of biological chemistry · 2023Article
- Photobiomodulation in Alzheimer's Disease-A Complementary Method to State-of-the-Art Pharmaceutical Formulations and Nanomedicine?Pharmaceutics · 2023Review
- Cooperation of N- and C-terminal substrate transmembrane domain segments in intramembrane proteolysis by γ-secretase.Communications biology · 2023Article
- γ-Secretase in Alzheimer's disease.Experimental & molecular medicine · 2022Review
- Insights into T-cell dysfunction in Alzheimer's disease.Aging cell · 2021Review
- Structural Studies Providing Insights into Production and Conformational Behavior of Amyloid-β Peptide Associated with Alzheimer's Disease Development.Molecules (Basel, Switzerland) · 2021Review
- The role of Niemann-Pick type C2 in zebrafish embryonic development.Development (Cambridge, England) · 2021Article
- OMA1-An integral membrane protease?Biochimica et biophysica acta. Proteins and proteomics · 2021Review
- Novel Bicyclic Heteroaryl Compounds as γ-Secretase Modulators for Treating Alzheimer's Disease.ACS medicinal chemistry letters · 2020Article
- Regulatory feedback cycle of the insulin-degrading enzyme and the amyloid precursor protein intracellular domain: Implications for Alzheimer's disease.Aging cell · 2020Article
- Review
- Recent developments of small molecule γ-secretase modulators for Alzheimer's disease.RSC medicinal chemistry · 2020Review
- Transcription factors activated through RIP (regulated intramembrane proteolysis) and RAT (regulated alternative translocation).The Journal of biological chemistry · 2020Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
1 author at 1 institution in 1 country.
Funding
Abstract
The γ-secretase complex is composed of four membrane protein subunits, including presenilin as the catalytic component with aspartyl protease activity. The enzyme cleaves within the transmembrane domain of >70 different type I integral membrane proteins and has been dubbed "the proteasome of the membrane". The most studied substrates include the Notch family of receptors, involved in cell differentiation, and the amyloid precursor protein (APP), involved in the pathogenesis of Alzheimer's disease. A central mechanistic question is how γ-secretase recognizes helical transmembrane substrates and carries out processive proteolysis. Recent findings addressing substrate recognition and processing will be discussed, including the role of protease subunit nicastrin as a gatekeeper, the effects of Alzheimer-causing mutations in presenilin on processive proteolysis of APP, and evidence that three pockets in the active site (S1', S2', and S3') determine carboxypeptidase cleavage of substrate in intervals of three residues. This article is part of a Special Issue entitled: Molecular biophysics of membranes and membrane proteins.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.