Evidence map›Paper›PMID 27140609›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2016

Electron tomography reveals the fibril structure and lipid interactions in amyloid deposits.

Marius Kollmer, Katrin Meinhardt, Christian Haupt, Falk Liberta, Melanie Wulff, Julia Linder, Lisa Handl, Liesa Heinrich, Cornelia Loos, Matthias Schmidt and 8 more

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing 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

38 citing papers in PubMed.

  1. Article
  2. Article
  3. Mechanisms and pathology of protein misfolding and aggregation.Nature reviews. Molecular cell biology · 2023
    Review
  4. Article
  5. Review
  6. Review
  7. Article
  8. Amyloidogenesis: What Do We Know So Far?International journal of molecular sciences · 2022
    Review
  9. Review
  10. Review
  11. Review
  12. Article
  13. Article
  14. Myosin Binding Protein-C Forms Amyloid-Like Aggregates In Vitro.International journal of molecular sciences · 2021
    Article
  15. Review
  16. Article
  17. Review
  18. Article
  19. Review
  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

18 authors.

Marius KollmerInstitute of Protein Biochemistry, Ulm University, 89081 Ulm, Germany;
Katrin MeinhardtInstitute of Protein Biochemistry, Ulm University, 89081 Ulm, Germany;
Christian HauptInstitute of Protein Biochemistry, Ulm University, 89081 Ulm, Germany;
Falk LibertaInstitute of Protein Biochemistry, Ulm University, 89081 Ulm, Germany;
Melanie WulffInstitute of Protein Biochemistry, Ulm University, 89081 Ulm, Germany;
Julia LinderInstitute of Protein Biochemistry, Ulm University, 89081 Ulm, Germany;
Lisa HandlInstitute of Stochastics, Ulm University, 89081 Ulm, Germany;
Liesa HeinrichLeibniz Institute for Natural Product Research and Infection Biology, Hans Knoell Institute, 07745 Jena, Germany;
Cornelia LoosInstitute of Protein Biochemistry, Ulm University, 89081 Ulm, Germany;
Matthias SchmidtInstitute of Protein Biochemistry, Ulm University, 89081 Ulm, Germany;
Tatiana SyrovetsInstitute of Pharmacology of Natural Products & Clinical Pharmacology, Ulm University, 89081 Ulm, Germany;
Thomas SimmetInstitute of Pharmacology of Natural Products & Clinical Pharmacology, Ulm University, 89081 Ulm, Germany;
Per WestermarkDepartment of Immunology, Genetics, and Pathology, Rudbeck Laboratory, Uppsala University, Uppsala SE-751 85, Sweden;
Gunilla T WestermarkDepartment of Medical Cell Biology, Uppsala University, SE-75123 Uppsala, Sweden;
Uwe HornLeibniz Institute for Natural Product Research and Infection Biology, Hans Knoell Institute, 07745 Jena, Germany;
Volker SchmidtInstitute of Stochastics, Ulm University, 89081 Ulm, Germany;
Paul WaltherCentral Electron Microscopy Facility, Ulm University, 89081 Ulm, Germany paul.walther@uni-ulm.de marcus.faendrich@uni-ulm.de.
Marcus FändrichInstitute of Protein Biochemistry, Ulm University, 89081 Ulm, Germany; paul.walther@uni-ulm.de marcus.faendrich@uni-ulm.de.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Electron tomography is an increasingly powerful method to study the detailed architecture of macromolecular complexes or cellular structures. Applied to amyloid deposits formed in a cell culture model of systemic amyloid A amyloidosis, we could determine the structural morphology of the fibrils directly in the deposit. The deposited fibrils are arranged in different networks, and depending on the relative fibril orientation, we can distinguish between fibril meshworks, fibril bundles, and amyloid stars. These networks are frequently infiltrated by vesicular lipid inclusions that may originate from the death of the amyloid-forming cells. Our data support the role of nonfibril components for constructing fibril deposits and provide structural views of different types of lipid-fibril interactions.

Indexed as

AmyloidAnimalsCells, CulturedElectron Microscope TomographyFemaleLipid BilayersLipidsMiceSerum Amyloid A ProteinAmyloidLipid BilayersLipidsSAA1 protein, humanSerum Amyloid A Proteinaggregationconformational diseaseelectron tomographyprionprotein assembly

Identifiers

PMID27140609
PMCPMC4878484

What OpenQuestion holds

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Registered trials

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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.