Evidence map›Paper›PMID 25748120›Full record

ReviewMolecular and cellular neurosciences2015

Current and future implications of basic and translational research on amyloid-β peptide production and removal pathways.

C Bohm, F Chen, J Sevalle, S Qamar, R Dodd, Y Li, G Schmitt-Ulms, P E Fraser, P H St George-Hyslop

Open access · hybridAbstract readReview
In one paragraph

Review in Molecular and cellular neurosciences, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
8.3field-weighted citation impact, top 2% 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

29 citing papers in PubMed, 64 citations in OpenAlex.

  1. Trial
  2. Behaviour Hallmarks in Alzheimer's Disease 5xFAD Mouse Model.International journal of molecular sciences · 2024
    Review
  3. Amyloid-Beta Mediates Homeostatic Synaptic Plasticity.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2021
    Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Review
  9. Review
  10. Review
  11. Article
  12. The "glymphatic" mechanism for solute clearance in Alzheimer's disease: game changer or unproven speculation?FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2018
    Review
  13. Article
  14. Translational Research in Alzheimer's and Prion Diseases.Journal of Alzheimer's disease : JAD · 2018
    Review
  15. Article
  16. Review
  17. The Transcellular Propagation and Intracellular Trafficking of α-Synuclein.Cold Spring Harbor perspectives in medicine · 2017
    Review
  18. Article
  19. Article
  20. 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

9 authors at 2 institutions in 2 countries.

C BohmTanz Centre for Research in Neurodegenerative Diseases, Departments of Medicine, Laboratory Medicine and Pathobiology and Medical Biophysics, University of Toronto, Krembil Discovery Tower, 6th Floor-6KD417, 60 Leonard Avenue, Toronto, Ontario M5T 2S8, Canada.
F ChenTanz Centre for Research in Neurodegenerative Diseases, Departments of Medicine, Laboratory Medicine and Pathobiology and Medical Biophysics, University of Toronto, Krembil Discovery Tower, 6th Floor-6KD417, 60 Leonard Avenue, Toronto, Ontario M5T 2S8, Canada.
J SevalleTanz Centre for Research in Neurodegenerative Diseases, Departments of Medicine, Laboratory Medicine and Pathobiology and Medical Biophysics, University of Toronto, Krembil Discovery Tower, 6th Floor-6KD417, 60 Leonard Avenue, Toronto, Ontario M5T 2S8, Canada.
S QamarCambridge Institute for Medical Research, Wellcome Trust MRC Building, Addenbrookes Hospital, Hills Road, Cambridge CB2 0XY, UK.
R DoddCambridge Institute for Medical Research, Wellcome Trust MRC Building, Addenbrookes Hospital, Hills Road, Cambridge CB2 0XY, UK.
Y LiCambridge Institute for Medical Research, Wellcome Trust MRC Building, Addenbrookes Hospital, Hills Road, Cambridge CB2 0XY, UK.
G Schmitt-UlmsTanz Centre for Research in Neurodegenerative Diseases, Departments of Medicine, Laboratory Medicine and Pathobiology and Medical Biophysics, University of Toronto, Krembil Discovery Tower, 6th Floor-6KD417, 60 Leonard Avenue, Toronto, Ontario M5T 2S8, Canada.
P E FraserTanz Centre for Research in Neurodegenerative Diseases, Departments of Medicine, Laboratory Medicine and Pathobiology and Medical Biophysics, University of Toronto, Krembil Discovery Tower, 6th Floor-6KD417, 60 Leonard Avenue, Toronto, Ontario M5T 2S8, Canada.
P H St George-HyslopTanz Centre for Research in Neurodegenerative Diseases, Departments of Medicine, Laboratory Medicine and Pathobiology and Medical Biophysics, University of Toronto, Krembil Discovery Tower, 6th Floor-6KD417, 60 Leonard Avenue, Toronto, Ontario M5T 2S8, Canada; Cambridge Institute for Medical Research, Wellcome Trust MRC Building, Addenbrookes Hospital, Hills Road, Cambridge CB2 0XY, UK. Electronic address: phs22@cam.ac.uk.
University of Toronto · CAAddenbrooke's Hospital · GB

Funding

CIHRMedical Research Council MC_G1000734Wellcome Trust 081864Wellcome Trust 089703
6 · The paper itself

Abstract

Inherited variants in multiple different genes are associated with increased risk for Alzheimer's disease (AD). In many of these genes, the inherited variants alter some aspect of the production or clearance of the neurotoxic amyloid β-peptide (Aβ). Thus missense, splice site or duplication mutants in the presenilin 1 (PS1), presenilin 2 (PS2) or the amyloid precursor protein (APP) genes, which alter the levels or shift the balance of Aβ produced, are associated with rare, highly penetrant autosomal dominant forms of Familial Alzheimer's Disease (FAD). Similarly, the more prevalent late-onset forms of AD are associated with both coding and non-coding variants in genes such as SORL1, PICALM and ABCA7 that affect the production and clearance of Aβ. This review summarises some of the recent molecular and structural work on the role of these genes and the proteins coded by them in the biology of Aβ. We also briefly outline how the emerging knowledge about the pathways involved in Aβ generation and clearance can be potentially targeted therapeutically. This article is part of Special Issue entitled "Neuronal Protein".

Indexed as

Translational Research, BiomedicalAlzheimer DiseaseAmyloid beta-PeptidesAnimalsHumansSignal TransductionAmyloid beta-PeptidesAbetaAlzheimerAmyloidAPOEAPPDementiaEPHA1GeneticsNeurodegenerationNext generation sequencingNicastrinPICALMPresenilinPSEN1SecretaseSORL1TauVaccine

Identifiers

PMID25748120
PMCPMC4503820
OpenAlexW2018437537

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.