Evidence map›Paper›PMID 37033831›Full record

ArticleACS omega2023

Human Amylin in the Presence of SARS-COV-2 Protein Fragments.

Andrew D Chesney, Buddhadev Maiti, Ulrich H E Hansmann

Open access · goldAbstract read
In one paragraph

Article in ACS omega, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

7 citing papers in PubMed, 13 citations in OpenAlex.

  1. Modulation of AβJournal of chemical information and modeling · 2025
    Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. SARS-COV-2 Spike Protein Fragment eases Amyloidogenesis of α-Synuclein.bioRxiv : the preprint server for biology · 2023
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Andrew D ChesneyDepartment of Chemistry & Biochemistry, University of Oklahoma, Norman, Oklahoma 73019, United States.
Buddhadev MaitiDepartment of Chemistry & Biochemistry, University of Oklahoma, Norman, Oklahoma 73019, United States.
Ulrich H E HansmannDepartment of Chemistry & Biochemistry, University of Oklahoma, Norman, Oklahoma 73019, United States.ORCID https://orcid.org/0000-0002-0700-4835
University of Oklahoma · US

Funding

Structural Transitions in Proteins and Protein AssembliesR01GM120634 · NIGMS · UNIVERSITY OF OKLAHOMA · PI HANSMANN, ULRICH H.E. · 2017 to 2020
$1.2M
NIGMS NIH HHS R01 GM120634
6 · The paper itself

Abstract

COVID-19 can lead to the onset of type-II diabetes, which is associated with the aggregation of islet amyloid polypeptides, also called amylin. Using molecular dynamics simulations, we investigate how the equilibrium between amylin monomers in its functional form and fibrils associated with diabetes is altered in the presence of SARS-COV-2 protein fragments. For this purpose, we study the interaction between the fragment SFYVYSRVK of the envelope protein or the fragment FKNIDGYFKI of the spike protein with the monomer and two amylin fibril models. Our results are compared with earlier work studying such interactions for the two different proteins.

Identifiers

PMID37033831
PMCPMC10077547
OpenAlexW4360605430

What OpenQuestion 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 OpenQuestion graph.