Evidence map›Paper›PMID 28287086›Full record

ArticleNature communications2017

Pre-plaque conformational changes in Alzheimer's disease-linked Aβ and APP.

O Klementieva, K Willén, I Martinsson, B Israelsson, A Engdahl, J Cladera, P Uvdal, G K Gouras

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
6.7field-weighted citation impact, top 3% 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

40 citing papers in PubMed, 95 citations in OpenAlex.

  1. Article
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  6. Article
  7. Review
  8. Evolving Experimental Techniques for Structure-Based Drug Design.The journal of physical chemistry. B · 2022
    Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. The Role of Amyloid-Beta and Tau in the Early Pathogenesis of Alzheimer's Disease.Medical science monitor : international medical journal of experimental and clinical research · 2021
    Review
  17. Article
  18. Review
  19. Article
  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

8 authors at 3 institutions in 2 countries.

O KlementievaExperimental Dementia Research Unit, Department of Experimental Medical Science, Lund University, 22184 Lund, Sweden.
K WillénExperimental Dementia Research Unit, Department of Experimental Medical Science, Lund University, 22184 Lund, Sweden.
I MartinssonExperimental Dementia Research Unit, Department of Experimental Medical Science, Lund University, 22184 Lund, Sweden.
B IsraelssonExperimental Dementia Research Unit, Department of Experimental Medical Science, Lund University, 22184 Lund, Sweden.
A EngdahlMAX IV Laboratory, Lund University, 22100 Lund, Sweden.
J CladeraDepartment of Biochemistry and Molecular Biology, Universitat Autònoma de Barcelona, 08193 Bellaterra, Spain.
P UvdalMAX IV Laboratory, Lund University, 22100 Lund, Sweden.
G K GourasExperimental Dementia Research Unit, Department of Experimental Medical Science, Lund University, 22184 Lund, Sweden.
Lund University · SEMAX IV Laboratory · SEUniversitat Autònoma de Barcelona · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Reducing levels of the aggregation-prone Aβ peptide that accumulates in the brain with Alzheimer's disease (AD) has been a major target of experimental therapies. An alternative approach may be to stabilize the physiological conformation of Aβ. To date, the physiological state of Aβ in brain remains unclear, since the available methods used to process brain tissue for determination of Aβ aggregate conformation can in themselves alter the structure and/or composition of the aggregates. Here, using synchrotron-based Fourier transform infrared micro-spectroscopy, non-denaturing gel electrophoresis and conformational specific antibodies we show that the physiological conformations of Aβ and amyloid precursor protein (APP) in brain of transgenic mouse models of AD are altered before formation of amyloid plaques. Furthermore, focal Aβ aggregates in brain that precede amyloid plaque formation localize to synaptic terminals. These changes in the states of Aβ and APP that occur prior to plaque formation may provide novel targets for AD therapy.

Indexed as

Alzheimer DiseaseAmyloid beta-PeptidesAmyloid beta-Protein PrecursorAnimalsBrainDisease Models, AnimalFemaleGene ExpressionHumansMiceMice, TransgenicNative Polyacrylamide Gel ElectrophoresisNeuronsNeuropeptidesPeptide FragmentsPlaque, AmyloidAmyloid beta-Peptidesamyloid beta-protein (1-40)amyloid beta-protein (1-42)Amyloid beta-Protein PrecursordrebrinsNeuropeptidesPeptide FragmentsProtein AggregatesSynaptophysinSyp protein, mouse

Identifiers

PMID28287086
PMCPMC5355803
OpenAlexW2596231972

What OpenQuestion holds

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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.