Evidence map›Paper›PMID 30814252›Full record

ArticleThe Journal of biological chemistry2019

Pyroglutamation of amyloid-βx-42 (Aβx-42) followed by Aβ1-40 deposition underlies plaque polymorphism in progressing Alzheimer's disease pathology.

Wojciech Michno, Sofie Nyström, Patrick Wehrli, Tammaryn Lashley, Gunnar Brinkmalm, Laurent Guerard, Stina Syvänen, Dag Sehlin, Ibrahim Kaya, Dimitri Brinet and 5 more

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing 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

50 citing papers in PubMed.

  1. Article
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  5. The Uppsala APP Mutation Promotes Wild-Type Amyloid-β Aggregation and Deposition In Vivo.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
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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

15 authors.

Wojciech MichnoFrom the Department of Psychiatry and Neurochemistry, Sahlgrenska Academy at the University of Gothenburg, 43180 Mölndal, Sweden.
Sofie Nyströmthe Department of Physics, Chemistry and Biology, Linköping University, 58183 Linköping, Sweden.
Patrick WehrliFrom the Department of Psychiatry and Neurochemistry, Sahlgrenska Academy at the University of Gothenburg, 43180 Mölndal, Sweden.
Tammaryn Lashleythe Department of Neurodegenerative Disease, UCL Queen Square Institute of Neurology, University College London, London WC1N 3BG, United Kingdom.
Gunnar BrinkmalmFrom the Department of Psychiatry and Neurochemistry, Sahlgrenska Academy at the University of Gothenburg, 43180 Mölndal, Sweden.
Laurent Guerardthe Center for Cellular Imaging, Core Facilities, Sahlgrenska Academy at the University of Gothenburg, 41390 Gothenburg, Sweden.
Stina Syvänenthe Department of Public Health and Caring Sciences, Uppsala University, 75236 Uppsala, Sweden.
Dag Sehlinthe Department of Public Health and Caring Sciences, Uppsala University, 75236 Uppsala, Sweden.
Ibrahim KayaFrom the Department of Psychiatry and Neurochemistry, Sahlgrenska Academy at the University of Gothenburg, 43180 Mölndal, Sweden.
Dimitri BrinetFrom the Department of Psychiatry and Neurochemistry, Sahlgrenska Academy at the University of Gothenburg, 43180 Mölndal, Sweden.
K Peter R Nilssonthe Department of Physics, Chemistry and Biology, Linköping University, 58183 Linköping, Sweden.
Per Hammarströmthe Department of Physics, Chemistry and Biology, Linköping University, 58183 Linköping, Sweden.
Kaj BlennowFrom the Department of Psychiatry and Neurochemistry, Sahlgrenska Academy at the University of Gothenburg, 43180 Mölndal, Sweden.
Henrik ZetterbergFrom the Department of Psychiatry and Neurochemistry, Sahlgrenska Academy at the University of Gothenburg, 43180 Mölndal, Sweden.
Jörg HanriederFrom the Department of Psychiatry and Neurochemistry, Sahlgrenska Academy at the University of Gothenburg, 43180 Mölndal, Sweden, jh@gu.se.ORCID 0000-0001-6059-198X

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Amyloid-β (Aβ) pathology in Alzheimer's disease (AD) is characterized by the formation of polymorphic deposits comprising diffuse and cored plaques. Because diffuse plaques are predominantly observed in cognitively unaffected, amyloid-positive (CU-AP) individuals, pathogenic conversion into cored plaques appears to be critical to AD pathogenesis. Herein, we identified the distinct Aβ species associated with amyloid polymorphism in brain tissue from individuals with sporadic AD (s-AD) and CU-AP. To this end, we interrogated Aβ polymorphism with amyloid conformation-sensitive dyes and a novel

Indexed as

Alzheimer DiseaseAmyloid beta-PeptidesAnimalsDisease ProgressionHumansMaleMiceMice, TransgenicModels, AnimalPeptide FragmentsPlaque, AmyloidProtein ConformationPyrrolidonecarboxylic AcidSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationAmyloid beta-Peptidesamyloid beta-protein (1-40)amyloid beta-protein (1-42)Peptide FragmentsPyrrolidonecarboxylic AcidAlzheimer diseaseamyloid-beta (Aβ)hyperspectral imagingimagingmass spectrometry (MS)neurodegenerationplaque polymorphismprotein aggregationpyroglutamationpyroglutamic acidtransgenic mice

Identifiers

PMID30814252
PMCPMC6497931

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.