Evidence map›Paper›PMID 38362440›Full record

ArticleChemical science2024

Thermodynamic characterization of amyloid polymorphism by microfluidic transient incomplete separation.

Azad Farzadfard, Antonin Kunka, Thomas Oliver Mason, Jacob Aunstrup Larsen, Rasmus Krogh Norrild, Elisa Torrescasana Dominguez, Soumik Ray, Alexander K Buell

Abstract read
In one paragraph

Article in Chemical science, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing 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

16 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. α-Synuclein Forms Distinct Micelle-Like Assemblies at Low Ionic Strengths.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  5. Article
  6. A functional amyloid scaffold shapes insect egg coats.bioRxiv : the preprint server for biology · 2026
    Article
  7. Reverse-engineering amyloid strains with generative protein design.bioRxiv : the preprint server for biology · 2026
    Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. Review
  16. 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

8 authors.

Azad FarzadfardProtein Biophysics Group, Department of Biotechnology and Biomedicine, Technical University of Denmark Søltofts Plads, Building 227, Kgs. Lyngby 2800 Denmark alebu@dtu.dk.ORCID https://orcid.org/0000-0003-1433-2439
Antonin KunkaProtein Biophysics Group, Department of Biotechnology and Biomedicine, Technical University of Denmark Søltofts Plads, Building 227, Kgs. Lyngby 2800 Denmark alebu@dtu.dk.ORCID https://orcid.org/0000-0002-1170-165X
Thomas Oliver MasonProtein Biophysics Group, Department of Biotechnology and Biomedicine, Technical University of Denmark Søltofts Plads, Building 227, Kgs. Lyngby 2800 Denmark alebu@dtu.dk.
Jacob Aunstrup LarsenProtein Biophysics Group, Department of Biotechnology and Biomedicine, Technical University of Denmark Søltofts Plads, Building 227, Kgs. Lyngby 2800 Denmark alebu@dtu.dk.ORCID https://orcid.org/0000-0002-6782-0594
Rasmus Krogh NorrildProtein Biophysics Group, Department of Biotechnology and Biomedicine, Technical University of Denmark Søltofts Plads, Building 227, Kgs. Lyngby 2800 Denmark alebu@dtu.dk.ORCID https://orcid.org/0000-0002-9120-2745
Elisa Torrescasana DominguezProtein Biophysics Group, Department of Biotechnology and Biomedicine, Technical University of Denmark Søltofts Plads, Building 227, Kgs. Lyngby 2800 Denmark alebu@dtu.dk.
Soumik RayProtein Biophysics Group, Department of Biotechnology and Biomedicine, Technical University of Denmark Søltofts Plads, Building 227, Kgs. Lyngby 2800 Denmark alebu@dtu.dk.ORCID https://orcid.org/0000-0002-1933-5471
Alexander K BuellProtein Biophysics Group, Department of Biotechnology and Biomedicine, Technical University of Denmark Søltofts Plads, Building 227, Kgs. Lyngby 2800 Denmark alebu@dtu.dk.ORCID https://orcid.org/0000-0003-1161-3622

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Amyloid fibrils of proteins such as α-synuclein are a hallmark of neurodegenerative diseases and much research has focused on their kinetics and mechanisms of formation. The question as to the thermodynamic stability of such structures has received much less attention. Here, we newly utilize the principle of transient incomplete separation of species in laminar flow in combination with chemical depolymerization for the quantification of amyloid fibril stability. The relative concentrations of fibrils and monomer at equilibrium are determined through an

Identifiers

PMID38362440
PMCPMC10866369

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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.