Evidence map›Paper›PMID 31552823›Full record

ArticleeLife2019

Structural mapping of oligomeric intermediates in an amyloid assembly pathway.

Theodoros K Karamanos, Matthew P Jackson, Antonio N Calabrese, Sophia C Goodchild, Emma E Cawood, Gary S Thompson, Arnout P Kalverda, Eric W Hewitt, Sheena E Radford

Open access · goldAbstract read
In one paragraph

Article in eLife, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
3.0field-weighted citation impact, top 8% 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

31 citing papers in PubMed, 59 citations in OpenAlex.

  1. Article
  2. Review
  3. Characterizing heterogeneity in amyloid formation processes.Current opinion in structural biology · 2024
    Review
  4. Review
  5. The Role of α-Synuclein in Etiology of Neurodegenerative Diseases.International journal of molecular sciences · 2024
    Review
  6. Review
  7. International journal of molecular sciences · 2024
    Article
  8. Article
  9. Article
  10. Review
  11. Disease-relevant βNature communications · 2023
    Article
  12. Review
  13. Article
  14. Tissue-specific isoform expression of GNE gene in human tissues.Journal of muscle research and cell motility · 2022
    Article
  15. The effect of mutation on an aggregation-prone protein: An in vivo, in vitro, and in silico analysis.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  16. Article
  17. Review
  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

9 authors at 1 institution in 1 country.

Theodoros K KaramanosThe Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, United Kingdom.ORCID 0000-0003-2297-540X
Matthew P JacksonThe Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, United Kingdom.
Antonio N CalabreseThe Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, United Kingdom.ORCID 0000-0003-2437-7761
Sophia C GoodchildThe Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, United Kingdom.
Emma E CawoodThe Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, United Kingdom.ORCID 0000-0002-2707-8022
Gary S ThompsonThe Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, United Kingdom.
Arnout P KalverdaThe Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, United Kingdom.
Eric W HewittThe Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, United Kingdom.ORCID 0000-0002-6238-6303
Sheena E RadfordThe Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, United Kingdom.ORCID 0000-0002-3079-8039
University of Leeds · GB

Funding

Biotechnology and Biological Sciences Research Council BB/E012558/1Biotechnology and Biological Sciences Research Council BB/K000659/1Biotechnology and Biological Sciences Research Council BB/P000037/1European Research Council 322408Medical Research Council MR/P018491/1Wellcome Trust 089311/Z/09/ZWellcome Trust 092896Wellcome Trust 092896MAWellcome Trust 094232Wellcome Trust 109154/Z/15/ZWellcome Trust 204963Wellcome Trust 204963/Z/16/Z
6 · The paper itself

Abstract

Transient oligomers are commonly formed in the early stages of amyloid assembly. Determining the structure(s) of these species and defining their role(s) in assembly is key to devising new routes to control disease. Here, using a combination of chemical kinetics, NMR spectroscopy and other biophysical methods, we identify and structurally characterize the oligomers required for amyloid assembly of the protein ΔN6, a truncation variant of human β

Indexed as

Protein MultimerizationAmyloidbeta 2-MicroglobulinBiophysical PhenomenaHumansKineticsMacromolecular SubstancesMagnetic Resonance SpectroscopyProtein BindingAmyloidbeta 2-MicroglobulinMacromolecular SubstancesaggregationamyloidE. colimicroglobulinmolecular biophysicsNMRoligomerstructural biology

Identifiers

PMID31552823
PMCPMC6783270
OpenAlexW2976197779

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.