Evidence map›Paper›PMID 35866164›Full record

ArticleRSC chemical biology2022

Metastable intermediate during hIAPP aggregation catalyzed by membranes as detected with 2D IR spectroscopy.

Sidney S Dicke, Michał Maj, Caitlyn R Fields, Martin T Zanni

Open access · goldAbstract read
In one paragraph

Article in RSC chemical biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

8 citing papers in PubMed, 14 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Interspecies Variation Affects Islet Amyloid Polypeptide Membrane Binding.Journal of the American Society for Mass Spectrometry · 2023
    Article
  5. Article
  6. Article
  7. Article
  8. 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

4 authors at 1 institution in 2 countries.

Sidney S DickeDepartment of Chemistry, University of Wisconsin-Madison 1101 University Avenue Madison WI 53706 USA zanni@chem.wisc.edu.ORCID https://orcid.org/0000-0002-5925-9207
Michał MajDepartment of Chemistry, University of Wisconsin-Madison 1101 University Avenue Madison WI 53706 USA zanni@chem.wisc.edu.ORCID https://orcid.org/0000-0003-1567-9514
Caitlyn R FieldsDepartment of Chemistry, University of Wisconsin-Madison 1101 University Avenue Madison WI 53706 USA zanni@chem.wisc.edu.
Martin T ZanniDepartment of Chemistry, University of Wisconsin-Madison 1101 University Avenue Madison WI 53706 USA zanni@chem.wisc.edu.ORCID https://orcid.org/0000-0001-7191-9768
University of Wisconsin–Madison · US

Funding

Structural mechanism of diabetic amyloid formationR01DK079895 · NIDDK · UNIVERSITY OF WISCONSIN-MADISON · PI Martin T Zanni · 2008 to 2026
$7.7M
NIDDK NIH HHS R01 DK079895
6 · The paper itself

Abstract

The aggregation of human islet amyloid polypeptide (hIAPP) into amyloid fibrils involves formation of oligomeric intermediates that are thought to be the cytotoxic species responsible for β-cell dysfunction in type 2 diabetes. hIAPP oligomers permeating or disrupting the cellular membrane may be one mechanism of toxicity and so measuring the structural kinetics of aggregation in the presence of membranes is of much interest. In this study, we use 2D IR spectroscopy and

Identifiers

PMID35866164
PMCPMC9257649
OpenAlexW4285283300

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.