Evidence map›Paper›PMID 21456963›Full record

ReviewAnnual review of neuroscience2011

Amyloid precursor protein processing and Alzheimer's disease.

Richard J O'Brien, Philip C Wong

Abstract readReview
PubMed Full text at PMC Publisher
In one paragraph

Review in Annual review of neuroscience, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1,031 papers, 3 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
1,031citing papers in PubMed, 3 pooled it
–field-weighted citation impact
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

1,031 citing papers in PubMed, 3 syntheses or guidelines pooled it.

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971 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

2 authors.

Richard J O'BrienDepartment of Neurology, Johns Hopkins Bayview Medical Center, USA. robrien@jhmi.edu
Philip C Wong

Funding

'T V ASSESSMENT - MEMORY DISORDERED PATIENTS'P50AG005146 · NIA · JOHNS HOPKINS UNIVERSITY · PI HUGANIR, RICHARD L · 1985 to 2019
$37.6M
NIA NIH HHS P50 AG005146
6 · The paper itself

Abstract

Alzheimer's disease (AD), the leading cause of dementia worldwide, is characterized by the accumulation of the β-amyloid peptide (Aβ) within the brain along with hyperphosphorylated and cleaved forms of the microtubule-associated protein tau. Genetic, biochemical, and behavioral research suggest that physiologic generation of the neurotoxic Aβ peptide from sequential amyloid precursor protein (APP) proteolysis is the crucial step in the development of AD. APP is a single-pass transmembrane protein expressed at high levels in the brain and metabolized in a rapid and highly complex fashion by a series of sequential proteases, including the intramembranous γ-secretase complex, which also process other key regulatory molecules. Why Aβ accumulates in the brains of elderly individuals is unclear but could relate to changes in APP metabolism or Aβ elimination. Lessons learned from biochemical and genetic studies of APP processing will be crucial to the development of therapeutic targets to treat AD.

Indexed as

Alzheimer DiseaseAmyloid beta-Protein PrecursorAmyloidogenic ProteinsAnimalsBrainHumansModels, BiologicalAmyloid beta-Protein PrecursorAmyloidogenic Proteins

Identifiers

PMID21456963
PMCPMC3174086

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.