Evidence map›Paper›PMID 11414282›Full record

ReviewMolecular neurobiology

Closing in on the amyloid cascade: recent insights into the cell biology of Alzheimer's disease.

J T Huse, R W Doms

Abstract readReview
PubMed Publisher
In one paragraph

Review in Molecular neurobiology. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
–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

15 citing papers in PubMed.

  1. Review
  2. Novel Roles for the Insulin-Regulated Glucose Transporter-4 in Hippocampally Dependent Memory.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2016
    Article
  3. Article
  4. Review
  5. Physiological and pathological phosphorylation of tau by Cdk5.Frontiers in molecular neuroscience · 2014
    Review
  6. Article
  7. Article
  8. Article
  9. β-Secretases, Alzheimer's Disease, and Down Syndrome.Current gerontology and geriatrics research · 2012
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
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.

J T HuseDepartment of Microbiology, University of Pennsylvania School of Medicine, Philadelphia 19104, USA.
R W Doms

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Accumulation of the amyloid-beta (A beta) peptide in the central nervous system (CNS) is considered by many to be the crucial pathological insult that ultimately leads to the development of Alzheimer's disease (AD). Regulating the production and/or aggregation of A beta could therefore be of considerable benefit to patients afflicted with AD. It has long been known that A beta is derived from the proteolytic processing of the amyloid precursor protein (APP) by two enzymatic activities, beta-secretase and gamma-secretase. Recent breakthroughs have led to the identification of the aspartyl protease BACE (beta-site APP-cleaving enzyme) as beta-secretase and the probable identification of the presenilin proteins as gamma-secretases. This review discusses what is know about BACE and the presenilins, focusing on their capacity as secretases, as well as the options for therapeutic advancement the careful characterization of these proteins will provide. These findings are presented in the context of the "amyloid cascade hypothesis" and its physiological relevance in AD pathogenesis.

Indexed as

Alzheimer DiseaseAmyloid beta-PeptidesAmyloid beta-Protein PrecursorAmyloid Precursor Protein SecretasesAspartic Acid EndopeptidasesDNA Mutational AnalysisEndopeptidasesForecastingGenetic Predisposition to DiseaseGlycosylationHumansImmunotherapy, ActiveMembrane ProteinsModels, MolecularModels, NeurologicalNerve Tissue ProteinsAmyloid beta-PeptidesAmyloid beta-Protein PrecursorAmyloid Precursor Protein SecretasesAspartic Acid EndopeptidasesBACE1 protein, humanBACE2 protein, humanEndopeptidasesMembrane ProteinsNerve Tissue ProteinsPresenilin-1Presenilin-2PSEN1 protein, humanPSEN2 protein, human

Identifiers

PMID11414282

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.