Evidence map›Paper›PMID 29182566›Full record

ArticleInternational journal of molecular sciences2017

Insights into Insulin Fibril Assembly at Physiological and Acidic pH and Related Amyloid Intrinsic Fluorescence.

Clara Iannuzzi, Margherita Borriello, Marianna Portaccio, Gaetano Irace, Ivana Sirangelo

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

28 citing papers in PubMed, 78 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Review
  9. Article
  10. Peptide Inhibitors of Insulin Fibrillation: Current and Future Challenges.International journal of molecular sciences · 2023
    Review
  11. Article
  12. Article
  13. Article
  14. Intrinsic fluorescence-based label-free detection of bovine amyloid A amyloidosis.Journal of veterinary diagnostic investigation : official publication of the American Association of Veterinary Laboratory Diagnosticians, Inc · 2022
    Article
  15. Plants (Basel, Switzerland) · 2021
    Article
  16. Article
  17. Aggregation Condition-Structure Relationship of Mouse Prion Protein Fibrils.International journal of molecular sciences · 2021
    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

5 authors at 1 institution in 1 country.

Clara IannuzziDepartment of Biochemistry, Biophysics and General Pathology, Università degli Studi della Campania "Luigi Vanvitelli", 80138 Naples, Italy. clara.iannuzzi@unicampania.it.ORCID 0000-0003-0092-5997
Margherita BorrielloDepartment of Biochemistry, Biophysics and General Pathology, Università degli Studi della Campania "Luigi Vanvitelli", 80138 Naples, Italy. margherita.borriello@unicampania.it.
Marianna PortaccioDepartment of Experimental Medicine, Università degli Studi della Campania "Luigi Vanvitelli", 80138 Naples, Italy. marianna.portaccio@unicampania.it.
Gaetano IraceDepartment of Biochemistry, Biophysics and General Pathology, Università degli Studi della Campania "Luigi Vanvitelli", 80138 Naples, Italy. gaetano.irace@unicampania.it.
Ivana SirangeloDepartment of Biochemistry, Biophysics and General Pathology, Università degli Studi della Campania "Luigi Vanvitelli", 80138 Naples, Italy. ivana.sirangelo@unicampania.it.ORCID 0000-0003-0092-5997
University of Campania "Luigi Vanvitelli" · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Human insulin is a widely used model protein for the study of amyloid formation as both associated to insulin injection amyloidosis in type II diabetes and highly prone to form amyloid fibrils in vitro. In this study, we aim to gain new structural insights into insulin fibril formation under two different aggregating conditions at neutral and acidic pH, using a combination of fluorescence, circular dichroism, Fourier-transform infrared spectroscopy, and transmission electron miscroscopy. We reveal that fibrils formed at neutral pH are morphologically different from those obtained at lower pH. Moreover, differences in FTIR spectra were also detected. In addition, only insulin fibrils formed at neutral pH showed the characteristic blue-green fluorescence generally associated to amyloid fibrils. So far, the molecular origin of this fluorescence phenomenon has not been clarified and different hypotheses have been proposed. In this respect, our data provide experimental evidence that allow identifying the molecular origin of such intrinsic property.

Indexed as

AmyloidCircular DichroismDiabetes Mellitus, Type 2HumansHydrogen-Ion ConcentrationInsulinKineticsProtein FoldingSpectroscopy, Fourier Transform InfraredAmyloidInsulinamyloid aggregationamyloid intrinsic fluorescenceprotein misfolding

Identifiers

PMID29182566
PMCPMC5751154
OpenAlexW2769603921

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.