Evidence map›Paper›PMID 37101572›Full record

ReviewACS bio & med chem Au2022

Molecular Aspects of Insulin Aggregation and Various Therapeutic Interventions.

Anirban Das, Mosami Shah, Ishu Saraogi

Open access · goldAbstract readReview
In one paragraph

Review in ACS bio & med chem Au, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
9.0field-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

30 citing papers in PubMed, 82 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. 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
  8. Article
  9. Review
  10. Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  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

3 authors at 1 institution in 1 country.

Anirban DasDepartment of Chemistry and Department of Biological Sciences, Indian Institute of Science Education and Research Bhopal, Bhopal Bypass Road, Bhauri, Bhopal 462066, Madhya Pradesh, India.
Mosami ShahDepartment of Chemistry and Department of Biological Sciences, Indian Institute of Science Education and Research Bhopal, Bhopal Bypass Road, Bhauri, Bhopal 462066, Madhya Pradesh, India.
Ishu SaraogiDepartment of Chemistry and Department of Biological Sciences, Indian Institute of Science Education and Research Bhopal, Bhopal Bypass Road, Bhauri, Bhopal 462066, Madhya Pradesh, India.ORCID https://orcid.org/0000-0003-0567-6029
Indian Institute of Science Education and Research, Bhopal · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein aggregation leading to the formation of amyloid fibrils has various adverse effects on human health ranging from fatigue and numbness to organ failure and death in extreme cases. Insulin, a peptide hormone commonly used to treat diabetes, undergoes aggregation at the site of repeated injections in diabetic patients as well as during its industrial production and transport. The reduced bioavailability of insulin due to aggregation hinders the proper control of glucose levels in diabetic patients. Thus, it is necessary to develop rational approaches for inhibiting insulin aggregation, which in turn requires a detailed understanding of the mechanism of fibrillation. Given the relative simplicity of insulin and ease of access, insulin has also served as a model system for studying amyloids. Approaches to inhibit insulin aggregation have included the use of natural molecules, synthetic peptides or small molecules, and bacterial chaperone machinery. This review focuses on insulin aggregation with an emphasis on its mechanism, the structural features of insulin fibrils, and the reported inhibitors that act at different stages in the aggregation pathway. We discuss molecules that can serve as leads for improved inhibitors for use in commercial insulin formulations. We also discuss the aggregation propensity of fast- and slow-acting insulin biosimilars, commonly administered to diabetic patients. The development of better insulin aggregation inhibitors and insights into their mechanism of action will not only aid diabetic therapies, but also enhance our knowledge of protein amyloidosis.

Identifiers

PMID37101572
PMCPMC10114644
OpenAlexW4207030462

What Socratic holds

Textmetadata
LicenceCC BY-NC-ND
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 Socratic graph.