Evidence map›Paper›PMID 11687657›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2001

Support for the multigenic hypothesis of amyloidosis: the binding stoichiometry of retinol-binding protein, vitamin A, and thyroid hormone influences transthyretin amyloidogenicity in vitro.

J T White, J W Kelly

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

39 citing papers in PubMed, 84 citations in OpenAlex.

  1. Article
  2. Review
  3. Sex and Age but Not Body Mass Index (BMI) Predict Serum Retinol Binding Protein 4 (RBP4) and Transthyretin (TTR) Concentrations.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025
    Article
  4. Review
  5. Article
  6. Review
  7. Tafamidis concentration required for transthyretin stabilisation in cerebrospinal fluid.Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis · 2023
    Article
  8. A molecular basis for tetramer destabilization and aggregation of transthyretin Ala97Ser.Protein science : a publication of the Protein Society · 2023
    Article
  9. Review
  10. Review
  11. Review
  12. Review
  13. Article
  14. Per- and polyfluoroalkyl substances (PFASs) in Swedish household dust and exposure of pet cats.Environmental science and pollution research international · 2021
    Article
  15. The interaction of zinc with the multi-functional plasma thyroid hormone distributor protein, transthyretin: evolutionary and cross-species comparative aspects.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2021
    Review
  16. Blinded potency comparison of transthyretin kinetic stabilisers by subunit exchange in human plasma.Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis · 2021
    Article
  17. Article
  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

2 authors at 1 institution in 1 country.

J T WhiteDepartment of Chemistry and the Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road BCC-506, La Jolla, CA 92037, USA.
J W Kelly
Scripps Research Institute · US

Funding

Probing the Biochemical Mechanisms of Amyloid DiseaseR01DK046335 · NIDDK · SCRIPPS RESEARCH INSTITUTE, THE · PI KELLY, JEFFERY W · 1998 to 2025
$8.8M
NIDDK NIH HHS R01 DK046335NIDDK NIH HHS R01 DK46335
6 · The paper itself

Abstract

The amyloidoses are a large group of protein misfolding diseases. Genetic and biochemical evidence support the hypothesis that amyloid formation from wild-type or 1 of 80 sequence variants of transthyretin causes the human amyloid diseases senile systemic amyloidosis or familial amyloid polyneuropathy, respectively. The late onset and variable penetrance of these diseases has led to their designation as multigenic--implying that the expression levels and alleles of multiple gene products influence the course of pathology. Here we show that the binding stoichiometry of three interacting molecules, retinol-binding protein, vitamin A, and L-thyroxine, notably influenced transthyretin amyloidogenicity in vitro. At least 70 genes control retinol-binding protein, vitamin A, and L-thyroxine levels in plasma and have the potential to modulate the course of senile systemic amyloidosis or familial amyloid polyneuropathy.

Indexed as

AmyloidosisCalorimetryHydrogen-Ion ConcentrationPrealbuminProtein BindingRetinol-Binding ProteinsRetinol-Binding Proteins, PlasmaThyroid HormonesVitamin APrealbuminRetinol-Binding ProteinsRetinol-Binding Proteins, PlasmaThyroid HormonesVitamin A

Identifiers

PMID11687657
PMCPMC60817
OpenAlexW2160710758

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.