Evidence map›Paper›PMID 27679488›Full record

ArticleThe Journal of biological chemistry2016

Inhibition of Insulin Amyloid Fibrillation by a Novel Amphipathic Heptapeptide: MECHANISTIC DETAILS STUDIED BY SPECTROSCOPY IN COMBINATION WITH MICROSCOPY.

Bhisma N Ratha, Anirban Ghosh, Jeffrey R Brender, Nilanjan Gayen, Humaira Ilyas, Chilukoti Neeraja, Kali P Das, Atin K Mandal, Anirban Bhunia

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
3.3field-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

18 citing papers in PubMed, 72 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Peptide Inhibitors of Insulin Fibrillation: Current and Future Challenges.International journal of molecular sciences · 2023
    Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Semen-derived amyloidogenic peptides-Key players of HIV infection.Protein science : a publication of the Protein Society · 2018
    Review
  18. 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

9 authors at 3 institutions in 2 countries.

Bhisma N RathaFrom the Department of Biophysics and.
Anirban GhoshFrom the Department of Biophysics and.
Jeffrey R BrenderRadiation Biology Branch, National Institutes of Health, Bethesda, Maryland 20814.
Nilanjan GayenDepartment of Molecular Medicine, Bose Institute, P-1/12 CIT Scheme VII (M), Kolkata 700054, India.
Humaira IlyasFrom the Department of Biophysics and.
Chilukoti NeerajaTIFR Centre for Interdisciplinary Sciences (TCIS), Narsingi, Hyderabad 500075, India, and.
Kali P DasDepartment of Chemistry, 93/1 APC Road, Bose Institute, Kolkata 700009, India.
Atin K MandalDepartment of Molecular Medicine, Bose Institute, P-1/12 CIT Scheme VII (M), Kolkata 700054, India.
Anirban BhuniaFrom the Department of Biophysics and anirbanbhunia@gmail.com bhunia@jcbose.ac.in.
Bose Institute · INNational Institutes of Health · USTIFR Centre for Interdisciplinary Sciences · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The aggregation of insulin into amyloid fibers has been a limiting factor in the development of fast acting insulin analogues, creating a demand for excipients that limit aggregation. Despite the potential demand, inhibitors specifically targeting insulin have been few in number. Here we report a non-toxic and serum stable-designed heptapeptide, KR7 (KPWWPRR-NH

Indexed as

Amino Acid SequenceAmyloidCircular DichroismFluorescence PolarizationHumansHydrophobic and Hydrophilic InteractionsHypoglycemic AgentsInsulinMicroscopy, Atomic ForceModels, MolecularNuclear Magnetic Resonance, BiomolecularOligopeptidesProtein AggregatesAmyloidHypoglycemic AgentsInsulinOligopeptidesProtein Aggregatesamyloidatomic force microscopy (AFM)fluorescence anisotropyinhibitorinsulin

Identifiers

PMID27679488
PMCPMC5095409
OpenAlexW2524419901

What Socratic holds

Textmetadata
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.