Evidence map›Paper›PMID 29915031›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2018

Kinetic analysis of the multistep aggregation pathway of human transthyretin.

Xun Sun, H Jane Dyson, Peter E Wright

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
1.9field-weighted citation impact, top 13% 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

27 citing papers in PubMed, 46 citations in OpenAlex.

  1. Article
  2. Analytical chemistry · 2026
    Article
  3. Article
  4. Hydration (HJournal of the American Chemical Society · 2025
    Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Water Plays Key Roles in Stabilities of Wild Type and Mutant Transthyretin Complexes.Journal of the American Society for Mass Spectrometry · 2024
    Article
  11. Article
  12. Article
  13. Proteolytic stability and aggregation in a key metabolic enzyme of bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Transthyretin Misfolding, A Fatal Structural Pathogenesis Mechanism.International journal of molecular sciences · 2021
    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

3 authors at 1 institution in 1 country.

Xun SunDepartment of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037.
H Jane DysonDepartment of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037.ORCID 0000-0001-6855-3398
Peter E WrightDepartment of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037; wright@scripps.edu.ORCID 0000-0002-1368-0223
Scripps Research Institute · US

Funding

Structural Characterization of Globin Folding PathwaysR01DK034909 · NIDDK · SCRIPPS RESEARCH INSTITUTE, THE · PI WRIGHT, PETER EDWIN · 1986 to 2017
$4.8M
STRUCTURAL CHARACTERIZATION OF GLOBIN FOLDING PATHWAYSR37DK034909 · NIDDK · SCRIPPS RESEARCH INSTITUTE · PI WRIGHT, PETER EDWIN · 1994 to 2001
$559k
American Heart Association-American Stroke Association 17POST32810003NIDDK NIH HHS R01 DK034909NIDDK NIH HHS R37 DK034909
6 · The paper itself

Abstract

Aggregation of transthyretin (TTR) is the causative agent for TTR cardiomyopathy and polyneuropathy amyloidoses. Aggregation is initiated by dissociation of the TTR tetramer into a monomeric intermediate, which self-assembles into amyloid. The coupled multiple-step equilibria and low-concentration, aggregation-prone intermediates are challenging to probe using conventional assays. We report a

Indexed as

Mutation, MissenseProtein Aggregation, PathologicalProtein MultimerizationAmino Acid SubstitutionCardiomyopathiesHumansNuclear Magnetic Resonance, BiomolecularPrealbuminProtein Structure, QuaternaryPrealbuminaggregation kineticsamyloidogenic proteinhydrophobic interactionlow-population intermediatereal-time NMR

Identifiers

PMID29915031
PMCPMC6142231
OpenAlexW2809533771

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.