Evidence map›Paper›PMID 21626267›Full record

ArticleProtein & cell2011

APP and APLP1 are degraded through autophagy in response to proteasome inhibition in neuronal cells.

Fangfang Zhou, Theo van Laar, Huizhe Huang, Long Zhang

Open access · bronzeAbstract read
In one paragraph

Article in Protein & cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
2.3field-weighted citation impact, top 13% 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

39 citing papers in PubMed, 64 citations in OpenAlex.

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  13. The p97 Inhibitor UPCDC-30245 Blocks Endo-Lysosomal Degradation.Pharmaceuticals (Basel, Switzerland) · 2022
    Article
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  16. Article
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  19. Selective autophagy as a therapeutic target for neurological diseases.Cellular and molecular life sciences : CMLS · 2021
    Review
  20. Review
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

4 authors at 2 institutions in 2 countries.

Fangfang ZhouMedical College of Chongqing Medical University, Chongqing, China.
Theo van Laar
Huizhe Huang
Long Zhang
Chongqing Medical University · CNLeiden University Medical Center · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Amyloid beta (Aβ) precursor protein (APP) is a key protein in the pathogenesis of Alzheimer's disease (AD). Both APP and its paralogue APLP1 (amyloid beta precursor-like protein 1) have multiple functions in cell adhesion and proliferation. Previously it was thought that autophagy is a novel beta-amyloid peptide (Aβ)-generating pathway activated in AD. However, the protein proteolysis of APLP1 is still largely unknown. The present study shows that APLP1 is rapidly degraded in neuronal cells in response to stresses, such as proteasome inhibition. Activation of the endoplasmic reticulum (ER) stress by proteasome inhibitors induces autophagy, causing reduction of mature APLP1/APP. Blocking autophagy or JNK stress kinase rescues the protein expression for both APP and APLP1. Therefore, our results suggest that APP/APLP1 is degraded through autophagy and the APLP1 proteolysis is mainly mediated by autophagy-lysosome pathway.

Indexed as

AutophagyProteasome InhibitorsAmyloid beta-Protein PrecursorAnimalsCell LineEndoplasmic ReticulumJNK Mitogen-Activated Protein KinasesLeupeptinsMiceNeuronsProteasome Endopeptidase ComplexProtein StabilityRatsAmyloid beta-Protein PrecursorAplp1 protein, mousebenzyloxycarbonylleucyl-leucyl-leucine aldehydeJNK Mitogen-Activated Protein KinasesLeupeptinsProteasome Endopeptidase ComplexProteasome Inhibitors

Identifiers

PMID21626267
PMCPMC4875337
OpenAlexW1964677366

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.