Evidence map›Paper›PMID 28234257›Full record

ArticleJournal of Alzheimer's disease : JAD2017

Pen-2 and Presenilin are Sufficient to Catalyze Notch Processing.

Chen Hu, Junjie Xu, Linlin Zeng, Ting Li, Mei-Zhen Cui, Xuemin Xu

Abstract read
In one paragraph

Article in Journal of Alzheimer's disease : JAD, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
1.1field-weighted citation impact, top 23% of its field
1 · What the graph read from 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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

7 citing papers in PubMed, 11 citations in OpenAlex.

  1. IncreasedInternational journal of molecular sciences · 2024
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  6. Conditional Inactivation of Pen-2 in the Developing Neocortex Leads to Rapid Switch of Apical Progenitors to Basal Progenitors.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2019
    Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 4 institutions in 2 countries.

Chen HuDepartment of Biomedical and Diagnostic Sciences, College of Veterinary Medicine, University of Tennessee, Knoxville, TN, USA.
Junjie XuDepartment of Biomedical and Diagnostic Sciences, College of Veterinary Medicine, University of Tennessee, Knoxville, TN, USA.
Linlin ZengDepartment of Biomedical and Diagnostic Sciences, College of Veterinary Medicine, University of Tennessee, Knoxville, TN, USA.
Ting LiDepartment of Biomedical and Diagnostic Sciences, College of Veterinary Medicine, University of Tennessee, Knoxville, TN, USA.
Mei-Zhen CuiDepartment of Biomedical and Diagnostic Sciences, College of Veterinary Medicine, University of Tennessee, Knoxville, TN, USA.
Xuemin XuDepartment of Biomedical and Diagnostic Sciences, College of Veterinary Medicine, University of Tennessee, Knoxville, TN, USA.
University of Tennessee at Knoxville · USJilin Medical University · CNJilin University · CNTianjin Medical University · CN

Funding

Novel mechanism mediating LPA-induced smooth muscle cell and vascular responsesR01HL107466 · NHLBI · UNIVERSITY OF TEXAS OF THE PERMIAN BASIN · PI CUI, MEI-ZHEN · 2011 to 2020
$3.3M
Pathogenic ROle of the Novel Mitochondrial Apoptotic PSAP in ALSR21NS095256 · NINDS · UNIVERSITY OF TEXAS OF THE PERMIAN BASIN · PI CUI, MEI-ZHEN · 2016 to 2017
$404k
Role of Presenilin Associated Protein (PSAP) in Apoptosis and in Abeta FormationR21AG039596 · NIA · UNIVERSITY OF TENNESSEE KNOXVILLE · PI XU, XUEMIN · 2011 to 2012
$329k
NHLBI NIH HHS R01 HL107466NIA NIH HHS R21 AG039596NINDS NIH HHS R21 NS095256
6 · The paper itself

Abstract

Presenilin-1 (PS1) or presenilin-2 (PS2), nicastrin (NCT), anterior pharynx-defective 1 (Aph-1), and presenilin enhancer-2 (Pen-2) have been considered the minimal essential subunits required to form an active γ-secretase complex. Besides PS, which has been widely believed to function as the catalytic subunit of the complex, the functional roles of the other subunits in the γ-secretase complex remain debatable. In the current study, we set out to determine the role of Pen-2 in γ-secretase activity. To this end, using knockout cells in combination with siRNA and immunoprecipitation approaches, our results revealed that Pen-2 together with presenilin are sufficient to form a functionally active enzyme to process Notch. Specifically, our data demonstrated that Pen-2 plays a crucial role in substrate binding, a mechanism by which Pen-2 contributes directly to the catalytic mechanism of γ-secretase activity. Our data also suggested that there may be different requirements for components to process AβPP and Notch. This information would be important for therapeutic strategy aimed at inhibition or modulation of γ-secretase activity.

Indexed as

Amyloid beta-Protein PrecursorAmyloid Precursor Protein SecretasesAnimalsCatalysisCell LineFibroblastsHumansMice, KnockoutPresenilin-1Presenilin-2Protein BindingProtein MultimerizationProtein StabilityReceptors, NotchAmyloid beta-Protein PrecursorAmyloid Precursor Protein SecretasesAPP protein, humanPresenilin-1presenilin 1, mousePresenilin-2presenilin enhancer 2, mousePSEN1 protein, humanPsen2 protein, mouseReceptors, NotchAlzheimer’s diseaseAph-1AβPPnicastrinNotchPen-2presenilinγ-secretase

Identifiers

PMID28234257
PMCPMC5644992
OpenAlexW2590642265

What Socratic holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

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 Socratic graph.