Evidence map›Paper›PMID 23607096›Full record

ReviewBioMed research international2013

Amylin uncovered: a review on the polypeptide responsible for type II diabetes.

Karen Pillay, Patrick Govender

Open access · hybridAbstract readReview
In one paragraph

Review in BioMed research international, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
4.6field-weighted citation impact, top 5% 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

34 citing papers in PubMed, 91 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. The pro-apoptotic domain of BIM protein forms toxic amyloid fibrils.Cellular and molecular life sciences : CMLS · 2021
    Article
  7. Review
  8. d-Retro Inverso Amylin and the Stability of Amylin Fibrils.Journal of chemical theory and computation · 2020
    Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Review
  17. Review
  18. 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

2 authors at 1 institution in 1 country.

Karen PillayDepartment of Biochemistry, School of Life Sciences, University of KwaZulu Natal, Westville Campus, Block F3, University Road, Private Bag X54001, Durban 4000, South Africa.
Patrick Govender
University of KwaZulu-Natal · ZA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Amylin is primarily responsible for classifying type II diabetes as an amyloid (protein misfolding) disease as it has great potential to aggregate into toxic nanoparticles, thereby resulting in loss of pancreatic β-cells. Although type II diabetes is on the increase each year, possibly due to bad eating habits of modern society, research on the culprit for this disease is still in its early days. In addition, unlike the culprit for Alzheimer's disease, amyloid β-peptide, amylin has failed to receive attention worthy of being featured in an abundance of review articles. Thus, the aim of this paper is to shine the spotlight on amylin in an attempt to put it onto the top of researchers' to-do list since the secondary complications of type II diabetes have far-reaching and severe consequences on public health both in developing and fully developed countries alike. This paper will cover characteristics of the amylin aggregates, mechanisms of toxicity, and a particular focus on inhibitors of toxicity and techniques used to assess these inhibitors.

Indexed as

Amino Acid SequenceAmyloid beta-PeptidesDiabetes Mellitus, Type 2HumansInsulin-Secreting CellsIslet Amyloid PolypeptideIslets of LangerhansNanofibersPeptidesProteostasis DeficienciesAmyloid beta-PeptidesIslet Amyloid PolypeptidePeptides

Identifiers

PMID23607096
PMCPMC3626316
OpenAlexW1974122968

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.