Evidence map›Paper›PMID 23589300›Full record

ArticleThe Journal of biological chemistry2013

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

Amy Hye Won Jeon, Christopher Böhm, Fusheng Chen, Hairu Huo, Xueying Ruan, Carl He Ren, Keith Ho, Seema Qamar, Paul M Mathews, Paul E Fraser and 3 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.5field-weighted citation impact, top 31% 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

8 citing papers in PubMed, 11 citations in OpenAlex.

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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

13 authors at 3 institutions in 3 countries.

Amy Hye Won JeonDepartment of Laboratory Medicine and Pathobiology, Tanz Centre for Research in Neurodegenerative Diseases, University of Toronto, Ontario M5S3H2, Canada.
Christopher Böhm
Fusheng Chen
Hairu Huo
Xueying Ruan
Carl He Ren
Keith Ho
Seema Qamar
Paul M Mathews
Paul E Fraser
Howard T J Mount
Peter St George-Hyslop
Gerold Schmitt-Ulms
University of Toronto · CAUniversity of Cambridge · GBNew York University · US

Funding

CIHRHoward Hughes Medical InstituteWellcome Trust 081864Wellcome Trust 089703Wellcome Trust 100140
6 · The paper itself

Abstract

γ-Secretase plays a pivotal role in the production of neurotoxic amyloid β-peptides (Aβ) in Alzheimer disease (AD) and consists of a heterotetrameric core complex that includes the aspartyl intramembrane protease presenilin (PS). The human genome codes for two presenilin paralogs. To understand the causes for distinct phenotypes of PS paralog-deficient mice and elucidate whether PS mutations associated with early-onset AD affect the molecular environment of mature γ-secretase complexes, quantitative interactome comparisons were undertaken. Brains of mice engineered to express wild-type or mutant PS1, or HEK293 cells stably expressing PS paralogs with N-terminal tandem-affinity purification tags served as biological source materials. The analyses revealed novel interactions of the γ-secretase core complex with a molecular machinery that targets and fuses synaptic vesicles to cellular membranes and with the H(+)-transporting lysosomal ATPase macrocomplex but uncovered no differences in the interactomes of wild-type and mutant PS1. The catenin/cadherin network was almost exclusively found associated with PS1. Another intramembrane protease, signal peptide peptidase, predominantly co-purified with PS2-containing γ-secretase complexes and was observed to influence Aβ production.

Indexed as

Alzheimer DiseaseAmyloid beta-PeptidesAmyloid Precursor Protein SecretasesAnimalsCadherinsCateninsHEK293 CellsHumansMembrane ProteinsMiceMice, TransgenicMutationPresenilin-2Protein BindingSerine EndopeptidasesVacuolar Proton-Translocating ATPasesAmyloid beta-PeptidesAmyloid Precursor Protein SecretasesCadherinsCateninsMembrane ProteinsPresenilin-2PSEN2 protein, humanSerine Endopeptidasestype I signal peptidaseVacuolar Proton-Translocating ATPasesAlzheimers DiseaseInteractomeMass Spectrometry (MS)PresenilinProteomicsSecretasesTransgenic

Identifiers

PMID23589300
PMCPMC3663554
OpenAlexW2074814566

What OpenQuestion holds

Textmetadata
LicenceCC BY
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 OpenQuestion graph.