Evidence map›Paper›PMID 16449386›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2006

Presenilin-1 uses phospholipase D1 as a negative regulator of beta-amyloid formation.

Dongming Cai, William J Netzer, Minghao Zhong, Yixin Lin, Guangwei Du, Michael Frohman, David A Foster, Sangram S Sisodia, Huaxi Xu, Fred S Gorelick and 1 more

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed
5.3field-weighted citation impact, top 4% 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

60 citing papers in PubMed, 107 citations in OpenAlex.

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  8. Association of Variants inFrontiers in genetics · 2020
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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

11 authors at 8 institutions in 1 country.

Dongming CaiLaboratory of Molecular and Cellular Neuroscience, and Fisher Center for Research on Alzheimer Disease, The Rockefeller University, 1230 York Avenue, New York, NY 10021, USA.
William J Netzer
Minghao Zhong
Yixin Lin
Guangwei Du
Michael Frohman
David A Foster
Sangram S Sisodia
Huaxi Xu
Fred S Gorelick
Paul Greengard
Rockefeller University · USCity University of New York · USHunter College · USSanford Burnham Prebys Medical Discovery Institute · USStony Brook University · USUniversity Medical Center · USUniversity of Chicago · USYale University · US

Funding

THE MECHANISMS OF y-SECRETASE REGULATIONP01AG009464 · NIA · ROCKEFELLER UNIVERSITY · PI KIM, YONG I · 1991 to 2011
$15.0M
Regulation of Protein Trafficking in NeurodegenerationR01NS046673 · NINDS · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI XU, HUAXI · 2003 to 2018
$5.8M
Role of phospholipase D in tumorigenesisR01CA046677 · NCI · HUNTER COLLEGE · PI FOSTER, DAVID A · 1997 to 2014
$3.6M
Regulation of BetaAPP Trafficking and Neuronal FunctionsF32AG023431 · NIA · ROCKEFELLER UNIVERSITY · PI CAI, DONGMING · 2003 to 2006
$136k
BASIS FOR TRANSFORMATION BY FUJINAMI SARCOMA VIRUSR29CA046677 · NCI · HUNTER COLLEGE · PI FOSTER, DAVID A · 1989 to 1993
–
NCI NIH HHS CA46677NCI NIH HHS R01 CA046677NIA NIH HHS 5F32AG023431NIA NIH HHS AG09464NIA NIH HHS F32 AG023431NIA NIH HHS P01 AG009464NINDS NIH HHS NS046673NINDS NIH HHS R01 NS046673
6 · The paper itself

Abstract

Presenilin (PS1/PS2) is a major component of gamma-secretase, the activity that mediates proteolysis of beta-amyloid precursor protein to generate beta-amyloid (Abeta). Here we demonstrate that PS1, through its loop region, binds to phospholipase D1 (PLD1), thereby recruiting it to the Golgi/trans-Golgi network. Overexpression of wild-type PLD1 reduces Abeta generation. Conversely, down-regulation of endogenous PLD1 by small hairpin RNA elevates Abeta production. The Abeta-lowering effect of PLD1 is independent of its ability to promote vesicular budding of beta-amyloid precursor protein. The data indicate that overexpression of PLD1 decreases, and down-regulation of PLD1 increases, the catalytic activity, and the association of the subunits, of gamma-secretase.

Indexed as

Protein Processing, Post-TranslationalAmyloid beta-PeptidesAmyloid beta-Protein PrecursorAmyloid Precursor Protein SecretasesAnimalsAspartic Acid EndopeptidasesCell LineEndopeptidasesGene Expression RegulationHumansMembrane ProteinsMiceMice, KnockoutPhospholipase DPresenilin-1Protein BindingAmyloid beta-PeptidesAmyloid beta-Protein PrecursorAmyloid Precursor Protein SecretasesAspartic Acid EndopeptidasesBACE1 protein, humanBace1 protein, mouseEndopeptidasesMembrane ProteinsPhospholipase Dphospholipase D1Presenilin-1PSEN1 protein, human

Identifiers

PMID16449386
PMCPMC1413665
OpenAlexW2117067724

What OpenQuestion holds

Textmetadata
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.