Evidence map›Paper›PMID 26779997›Full record

ArticleBMB reports2016

Regulation of amyloid precursor protein processing by its KFERQ motif.

Ji-Seon Park, Dong-Hou Kim, Seung-Yong Yoon

Open access · goldAbstract readNews
In one paragraph

Article in BMB reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
2.5field-weighted citation impact, top 11% 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

51 citing papers in PubMed, 63 citations in OpenAlex.

  1. Review
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  6. Autophagy-lysosomal pathway in neurodegeneration.Molecular neurodegeneration advances · 2026
    Review
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  9. Article
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  17. The emerging mechanisms and functions of microautophagy.Nature reviews. Molecular cell biology · 2023
    Review
  18. Protein Interactome of Amyloid-β as a Therapeutic Target.Pharmaceuticals (Basel, Switzerland) · 2023
    Review
  19. 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

3 authors at 2 institutions in 2 countries.

Ji-Seon ParkAlzheimer's Disease Experts Lab (ADEL), Asan Medical Center; Department of Brain Science; Bio-Medical Institute of Technology (BMIT); Cell Dysfunction Research Center (CDRC), University of Ulsan College of Medicine, Seoul 05505, Korea.
Dong-Hou KimAlzheimer's Disease Experts Lab (ADEL), Asan Medical Center; Department of Brain Science; Bio-Medical Institute of Technology (BMIT); Cell Dysfunction Research Center (CDRC), University of Ulsan College of Medicine, Seoul 05505, Korea.
Seung-Yong YoonAlzheimer's Disease Experts Lab (ADEL), Asan Medical Center; Department of Brain Science; Bio-Medical Institute of Technology (BMIT); Cell Dysfunction Research Center (CDRC), University of Ulsan College of Medicine, Seoul 05505, Korea.
Ulsan College · KRUniversity of Ulsan · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Understanding of trafficking, processing, and degradation mechanisms of amyloid precursor protein (APP) is important because APP can be processed to produce β-amyloid (Aβ), a key pathogenic molecule in Alzheimer's disease (AD). Here, we found that APP contains KFERQ motif at its C-terminus, a consensus sequence for chaperone-mediated autophagy (CMA) or microautophagy which are another types of autophagy for degradation of pathogenic molecules in neurodegenerative diseases. Deletion of KFERQ in APP increased C-terminal fragments (CTFs) and secreted N-terminal fragments of APP and kept it away from lysosomes. KFERQ deletion did not abolish the interaction of APP or its cleaved products with heat shock cognate protein 70 (Hsc70), a protein necessary for CMA or microautophagy. These findings suggest that KFERQ motif is important for normal processing and degradation of APP to preclude the accumulation of APP-CTFs although it may not be important for CMA or microautophagy. [BMB Reports 2016; 49(6): 337-342].

Indexed as

Protein Processing, Post-TranslationalAmino Acid MotifsAmino Acid SequenceAmyloid beta-Protein PrecursorCell Line, TumorHSC70 Heat-Shock ProteinsHumansLysosomesPhosphorylationProtein BindingStructure-Activity Relationshiptau ProteinsAmyloid beta-Protein PrecursorHSC70 Heat-Shock Proteinstau Proteins

Identifiers

PMID26779997
PMCPMC5070722
OpenAlexW2411638070

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.