Evidence map›Paper›PMID 19541956›Full record

ArticleScience (New York, N.Y.)2009

Functional amyloids as natural storage of peptide hormones in pituitary secretory granules.

Samir K Maji, Marilyn H Perrin, Michael R Sawaya, Sebastian Jessberger, Krishna Vadodaria, Robert A Rissman, Praful S Singru, K Peter R Nilsson, Rozalyn Simon, David Schubert and 5 more

Open access · greenAbstract read
In one paragraph

Article in Science (New York, N.Y.), 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 474 papers.

0numbers the graph read from it
0cells of the map it votes in
474citing papers in PubMed
29.7field-weighted citation impact, top 1% 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

474 citing papers in PubMed, 1,048 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. amyloid-predict and LLPS-predict: Predicting phase separation propensities in the intrinsically disordered proteome.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  7. A functional amyloid scaffold shapes insect egg coats.bioRxiv : the preprint server for biology · 2026
    Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. The Importance of Being Imperfect: Structure and Function of Bacterial Amyloid.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Review
  17. Article
  18. Review
  19. Article
  20. Article

414 more citing papers are in PubMed but not listed here.

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

15 authors at 5 institutions in 3 countries.

Samir K MajiLaboratory of Physical Chemistry, Eidgenössische Technische Hochschule (ETH) Zürich, Wolfgang-Paulistrasse 10, CH-8093 Zürich, Switzerland.
Marilyn H Perrin
Michael R Sawaya
Sebastian Jessberger
Krishna Vadodaria
Robert A Rissman
Praful S Singru
K Peter R Nilsson
Rozalyn Simon
David Schubert
David Eisenberg
Jean Rivier
Paul Sawchenko
Wylie Vale
Roland Riek
Salk Institute for Biological Studies · USETH Zurich · CHLinköping University · SETufts Medical Center · USUniversity of California, San Diego · US

Funding

TARGETED DISRUPTION OF NEUROENDOCRINE GENESP01DK026741 · NIDDK · SALK INSTITUTE FOR BIOLOGICAL STUDIES · PI ZORRILLA, ERIC P, ZORRILLA, ERIC P · 1986 to 2014
$31.6M
NIDDK NIH HHS P01 DK026741
6 · The paper itself

Abstract

Amyloids are highly organized cross-beta-sheet-rich protein or peptide aggregates that are associated with pathological conditions including Alzheimer's disease and type II diabetes. However, amyloids may also have a normal biological function, as demonstrated by fungal prions, which are involved in prion replication, and the amyloid protein Pmel17, which is involved in mammalian skin pigmentation. We found that peptide and protein hormones in secretory granules of the endocrine system are stored in an amyloid-like cross-beta-sheet-rich conformation. Thus, functional amyloids in the pituitary and other organs can contribute to normal cell and tissue physiology.

Indexed as

Adrenocorticotropic HormoneAmyloidAnimalsbeta-EndorphinCell SurvivalCorticotropin-Releasing HormoneHeparin, Low-Molecular-WeightHumansHydrogen-Ion ConcentrationMiceNeuronsPeptide HormonesPituitary GlandPituitary Gland, AnteriorPituitary Gland, PosteriorPituitary HormonesAdrenocorticotropic HormoneAmyloidbeta-EndorphinCorticotropin-Releasing HormoneHeparin, Low-Molecular-WeightPeptide HormonesPituitary HormonesUrocortins

Identifiers

PMID19541956
PMCPMC2865899
OpenAlexW2046093999

What OpenQuestion holds

Textmetadata
LicenceTDM
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.