Evidence map›Paper›PMID 22122372›Full record

ReviewJournal of neurochemistry2012

Proteolytic processing of Alzheimer's β-amyloid precursor protein.

Han Zhang, Qilin Ma, Yun-Wu Zhang, Huaxi Xu

Open access · bronzeAbstract readReview
In one paragraph

Review in Journal of neurochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 185 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
185citing papers in PubMed, 1 pooled it
10.9field-weighted citation impact, top 1% 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

185 citing papers in PubMed, 1 synthesis or guideline pooled it, 320 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Article
  4. Article
  5. Article
  6. Astrocytoma-Specific Prognostic Associations of Amyloid-Related Biological Processes.Pathophysiology : the official journal of the International Society for Pathophysiology · 2026
    Article
  7. Review
  8. Article
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  10. Article
  11. Article
  12. Review
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  16. Article
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125 more citing papers are in PubMed but not listed here.

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 3 institutions in 2 countries.

Han ZhangFujian Provincial Key Laboratory of Neurodegenerative Disease and Aging Research, College of Medicine, Xiamen University, Xiamen, Fujian, China.
Qilin MaDepartment of Neurology, The First Affiliated Hospital of Xiamen University, Xiamen, Fujian, China.
Yun-Wu ZhangFujian Provincial Key Laboratory of Neurodegenerative Disease and Aging Research, College of Medicine, Xiamen University, Xiamen, Fujian, China.
Huaxi XuFujian Provincial Key Laboratory of Neurodegenerative Disease and Aging Research, College of Medicine, Xiamen University, Xiamen, Fujian, China.
Sanford Burnham Prebys Medical Discovery Institute · USFirst Affiliated Hospital of Xiamen University · CNXiamen University · CN

Funding

Regulation of Protein Trafficking in NeurodegenerationR01NS046673 · NINDS · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI XU, HUAXI · 2003 to 2018
$5.8M
Identifying genes in Beta-Amyloid ProductionR01AG021173 · NIA · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI XU, HUAXI · 2004 to 2015
$3.3M
Transcriptional Regulation of BACE and the Components of the gamma-Secretase CompR01AG030197 · NIA · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI XU, HUAXI · 2007 to 2011
$1.9M
Generation of a Transgenic Mouse Model for Functional Study of a Novel Gene FG01R03AG034366 · NIA · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI XU, HUAXI · 2009 to 2010
$167k
NIA NIH HHS R01 AG021173NIA NIH HHS R01AG021173NIA NIH HHS R01 AG030197NIA NIH HHS R01AG030197NIA NIH HHS R03 AG034366NIA NIH HHS R03AG034366NINDS NIH HHS R01 NS046673NINDS NIH HHS R01NS046673
6 · The paper itself

Abstract

β-Amyloid precursor protein (APP) is a critical factor in the pathogenesis of Alzheimer's disease (AD). APP undergoes post-translational proteolysis/processing to generate the hydrophobic β-amyloid (Aβ) peptides. Deposition of Aβ in the brain, forming oligomeric Aβ and plaques, is identified as one of the key pathological hallmarks of AD. The processing of APP to generate Aβ is executed by β- and γ-secretase and is highly regulated. Aβ toxicity can lead to synaptic dysfunction, neuronal cell death, impaired learning/memory and abnormal behaviors in AD models in vitro and in vivo. Aside from Aβ, proteolytic cleavages of APP can also give rise to the APP intracellular domain, reportedly involved in multiple types of cellular events such as gene transcription and apoptotic cell death. In addition to amyloidogenic processing, APP can also be cleaved by α-secretase to form a soluble or secreted APP ectodomain (sAPP-α) that has been shown to be mostly neuro-protective. In this review, we describe the mechanisms involved in APP metabolism and the likely functions of its various proteolytic products to give a better understanding of the patho/physiological functions of APP.

Indexed as

ProteolysisAlzheimer DiseaseAmyloid beta-Protein PrecursorAnimalsHumansPlaque, AmyloidProtein Processing, Post-TranslationalAmyloid beta-Protein Precursor

Identifiers

PMID22122372
PMCPMC3254787
OpenAlexW1504590764

What OpenQuestion 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 OpenQuestion graph.