Evidence map›Paper›PMID 28416674›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2017

Inducing protein aggregation by extensional flow.

John Dobson, Amit Kumar, Leon F Willis, Roman Tuma, Daniel R Higazi, Richard Turner, David C Lowe, Alison E Ashcroft, Sheena E Radford, Nikil Kapur and 1 more

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing 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

44 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Review
  5. In the flow, how fluid dynamics shapes amyloid formation.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  6. Initiation of transthyretin aggregation at neutral pH by fluid agitation.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Article
  8. Article
  9. Article
  10. Aggregation of Transthyretin by Fluid Agitation.bioRxiv : the preprint server for biology · 2024
    Article
  11. Article
  12. Article
  13. Article
  14. Single molecule delivery into living cells.Nature communications · 2024
    Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  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

11 authors.

John DobsonSchool of Mechanical Engineering, University of Leeds, Leeds, LS2 9JT, United Kingdom.
Amit KumarSchool of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, LS2 9JT, United Kingdom.
Leon F WillisSchool of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, LS2 9JT, United Kingdom.
Roman TumaSchool of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, LS2 9JT, United Kingdom.
Daniel R HigaziMedImmune Ltd., Cambridge, CB21 6GH, United Kingdom.
Richard TurnerMedImmune Ltd., Cambridge, CB21 6GH, United Kingdom.
David C LoweMedImmune Ltd., Cambridge, CB21 6GH, United Kingdom.
Alison E AshcroftSchool of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, LS2 9JT, United Kingdom.
Sheena E RadfordSchool of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, LS2 9JT, United Kingdom.
Nikil KapurSchool of Mechanical Engineering, University of Leeds, Leeds, LS2 9JT, United Kingdom; N.Kapur@leeds.ac.uk d.j.brockwell@leeds.ac.uk.
David J BrockwellSchool of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, LS2 9JT, United Kingdom; N.Kapur@leeds.ac.uk d.j.brockwell@leeds.ac.uk.ORCID 0000-0002-0802-5937

Funding

European Research Council 322408Medical Research Council G0900958Wellcome TrustWellcome Trust 108466/Z/15/Z
6 · The paper itself

Abstract

Relative to other extrinsic factors, the effects of hydrodynamic flow fields on protein stability and conformation remain poorly understood. Flow-induced protein remodeling and/or aggregation is observed both in Nature and during the large-scale industrial manufacture of proteins. Despite its ubiquity, the relationships between the type and magnitude of hydrodynamic flow, a protein's structure and stability, and the resultant aggregation propensity are unclear. Here, we assess the effects of a defined and quantified flow field dominated by extensional flow on the aggregation of BSA, β

Indexed as

HydrodynamicsProtein AggregatesAnimalsAntibodies, Monoclonalbeta 2-MicroglobulinCattleGranulocyte Colony-Stimulating FactorHumansKineticsProtein StabilitySerum Albumin, BovineAntibodies, Monoclonalbeta 2-MicroglobulinGranulocyte Colony-Stimulating FactorProtein AggregatesSerum Albumin, Bovineaggregationantibodybioprocessingextensional flowunfolding

Identifiers

PMID28416674
PMCPMC5422818

What OpenQuestion holds

Textmetadata
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.