Evidence map›Paper›PMID 24042052›Full record

ArticleFEBS letters2013

Blockade of islet amyloid polypeptide fibrillation and cytotoxicity by the secretory chaperones 7B2 and proSAAS.

Juan R Peinado, Furqan Sami, Nina Rajpurohit, Iris Lindberg

Open access · greenAbstract read
In one paragraph

Article in FEBS letters, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.3field-weighted citation impact, top 21% 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

21 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Secreted Chaperones in Neurodegeneration.Frontiers in aging neuroscience · 2020
    Review
  10. Article
  11. Review
  12. Article
  13. Modulation of Amyloid States by Molecular Chaperones.Cold Spring Harbor perspectives in biology · 2019
    Review
  14. Article
  15. Article
  16. Diabetes Drug Discovery: hIAPPMolecules (Basel, Switzerland) · 2018
    Article
  17. Article
  18. The neural chaperone proSAAS blocks α-synuclein fibrillation and neurotoxicity.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  19. Article
  20. PCSK1 Variants and Human Obesity.Progress in molecular biology and translational science · 2016
    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

4 authors at 1 institution in 1 country.

Juan R PeinadoDepartment of Anatomy and Neurobiology, University of Maryland-Baltimore, Baltimore, MD 21201, United States.
Furqan Sami
Nina Rajpurohit
Iris Lindberg
University of Maryland, Baltimore · US

Funding

CONTROL OF PEPTIDE HORMONE BIOSYNTHESIS BY PC2 AND 7B2R01DK049703 · NIDDK · UNIVERSITY OF MARYLAND BALTIMORE · PI LINDBERG, IRIS · 1996 to 2012
$3.7M
NIDDK NIH HHS DK49703NIDDK NIH HHS R01 DK049703
6 · The paper itself

Abstract

The deposition of fibrillated human islet β-cell peptide islet amyloid polypeptide (hIAPP) into amyloid plaques is characteristic of the pathogenesis of islet cell death during type 2 diabetes. We investigated the effects of the neuroendocrine secretory proteins 7B2 and proSAAS on hIAPP fibrillation in vitro and on cytotoxicity. In vitro, 21-kDa 7B2 and proSAAS blocked hIAPP fibrillation. Structure-function studies showed that a central region within 21-kDa 7B2 is important in this effect and revealed the importance of the N-terminal region of proSAAS. Both chaperones blocked the cytotoxic effects of exogenous hIAPP on Rin5f cells; 7B2 generated by overexpression was also effective. ProSAAS and 7B2 may perform a chaperone role as secretory anti-aggregants in normal islet cell function and in type 2 diabetes.

Indexed as

AnimalsCells, CulturedHumansIslet Amyloid PolypeptideMiceMolecular ChaperonesNerve Tissue ProteinsNeuroendocrine Secretory Protein 7B2NeuropeptidesRatsIslet Amyloid PolypeptideMolecular ChaperonesNerve Tissue ProteinsNeuroendocrine Secretory Protein 7B2NeuropeptidesPcsk1n protein, mouseSCG5 protein, human7B2ADAlzheimer’s diseasebovine serum albuminBSACAcarbonic anhydraseFBSfetal bovine serumhIAPPIAPPislet amyloid polypeptideParkinson’s diseasePBSPC1/3PDphosphate–buffered salineprohormone convertase 1/3proSAAST2DMTBSthioflavin TThTtris–buffered salinetype 2 diabetesType 2 diabetes

Identifiers

PMID24042052
PMCPMC3845801
OpenAlexW2156135176

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.