Evidence map›Paper›PMID 34122996›Full record

ArticleChemical science2020

Templating S100A9 amyloids on Aβ fibrillar surfaces revealed by charge detection mass spectrometry, microscopy, kinetic and microfluidic analyses.

Jonathan Pansieri, Igor A Iashchishyn, Hussein Fakhouri, Lucija Ostojić, Mantas Malisauskas, Greta Musteikyte, Vytautas Smirnovas, Matthias M Schneider, Tom Scheidt, Catherine K Xu and 5 more

Open access · diamondAbstract read
In one paragraph

Article in Chemical science, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

23 citing papers in PubMed, 33 citations in OpenAlex.

  1. Review
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  11. Heterotypic Seeding Generates Mixed Amyloid Polymorphs.bioRxiv : the preprint server for biology · 2024
    Article
  12. Self-replication of AProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  13. ApoE Isoforms Inhibit Amyloid Aggregation of Proinflammatory Protein S100A9.International journal of molecular sciences · 2024
    Article
  14. Mechanisms and pathology of protein misfolding and aggregation.Nature reviews. Molecular cell biology · 2023
    Review
  15. Article
  16. Amyloid inhibition by molecular chaperonesRSC medicinal chemistry · 2023
    Review
  17. Article
  18. Article
  19. Article
  20. S100A9 Alters the Pathway of Alpha-Synuclein Amyloid Aggregation.International journal of molecular sciences · 2021
    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

15 authors at 4 institutions in 5 countries.

Jonathan PansieriDepartment of Medical Biochemistry and Biophysics, Umeå University SE-90187 Umeå Sweden ludmilla.morozova-roche@umu.se.ORCID https://orcid.org/0000-0001-8918-9943
Igor A IashchishynDepartment of Medical Biochemistry and Biophysics, Umeå University SE-90187 Umeå Sweden ludmilla.morozova-roche@umu.se.ORCID https://orcid.org/0000-0002-1691-9025
Hussein FakhouriInstitut Lumière Matière, UMR 5306, Université Claude Bernard Lyon 1, CNRS, Univ Lyon F-69100 Villeurbanne France.
Lucija OstojićDepartment of Medical Biochemistry and Biophysics, Umeå University SE-90187 Umeå Sweden ludmilla.morozova-roche@umu.se.
Mantas MalisauskasDepartment of Medical Biochemistry and Biophysics, Umeå University SE-90187 Umeå Sweden ludmilla.morozova-roche@umu.se.
Greta MusteikyteInstitute of Biotechnology, Life Sciences Center, Vilnius University Vilnius Lithuania.ORCID https://orcid.org/0000-0002-4585-5091
Vytautas SmirnovasInstitute of Biotechnology, Life Sciences Center, Vilnius University Vilnius Lithuania.ORCID https://orcid.org/0000-0002-1829-5455
Matthias M SchneiderCentre for Misfolding Diseases, Department of Chemistry, University of Cambridge Lensfield Road Cambridge CB2 1EW UK.ORCID https://orcid.org/0000-0002-1894-1859
Tom ScheidtCentre for Misfolding Diseases, Department of Chemistry, University of Cambridge Lensfield Road Cambridge CB2 1EW UK.ORCID https://orcid.org/0000-0002-0185-7730
Catherine K XuCentre for Misfolding Diseases, Department of Chemistry, University of Cambridge Lensfield Road Cambridge CB2 1EW UK.
Georg MeislCentre for Misfolding Diseases, Department of Chemistry, University of Cambridge Lensfield Road Cambridge CB2 1EW UK.ORCID https://orcid.org/0000-0002-6562-7715
Tuomas P J KnowlesCentre for Misfolding Diseases, Department of Chemistry, University of Cambridge Lensfield Road Cambridge CB2 1EW UK.
Ehud GazitDepartment of Medical Biochemistry and Biophysics, Umeå University SE-90187 Umeå Sweden ludmilla.morozova-roche@umu.se.
Rodolphe AntoineInstitut Lumière Matière, UMR 5306, Université Claude Bernard Lyon 1, CNRS, Univ Lyon F-69100 Villeurbanne France.ORCID https://orcid.org/0000-0001-5682-8550
Ludmilla A Morozova-RocheDepartment of Medical Biochemistry and Biophysics, Umeå University SE-90187 Umeå Sweden ludmilla.morozova-roche@umu.se.ORCID https://orcid.org/0000-0001-5886-2023
Umeå University · SEUniversity of Cambridge · GBUniversité Claude Bernard Lyon 1 · FRVilnius University · LT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The mechanism of amyloid co-aggregation and its nucleation process are not fully understood in spite of extensive studies. Deciphering the interactions between proinflammatory S100A9 protein and Aβ

Identifiers

PMID34122996
PMCPMC8159403
OpenAlexW3035798057

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.