Evidence map›Paper›PMID 35266717›Full record

ArticleThe journal of physical chemistry letters2022

Nanoscale Structural Analysis of a Lipid-Driven Aggregation of Insulin.

Stanislav Rizevsky, Mikhail Matveyenka, Dmitry Kurouski

Open access · greenAbstract read
In one paragraph

Article in The journal of physical chemistry letters, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
9.5field-weighted citation impact, top 2% 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

34 citing papers in PubMed, 38 citations in OpenAlex.

  1. Article
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  5. Food science & nutrition · 2025
    Article
  6. Experimental methods for studying amyloid cross-interactions.Protein science : a publication of the Protein Society · 2025
    Review
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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 2 institutions in 2 countries.

Stanislav RizevskyDepartment of Biochemistry and Biophysics, Texas A&M University, College Station, Texas 77843, United States.
Mikhail MatveyenkaDepartment of Biochemistry and Biophysics, Texas A&M University, College Station, Texas 77843, United States.
Dmitry KurouskiDepartment of Biochemistry and Biophysics, Texas A&M University, College Station, Texas 77843, United States.ORCID https://orcid.org/0000-0002-6040-4213
Texas A&M University · USBình Dương University · VN

Funding

Biophysical determination of the underlying cause of α-Syn oligomer toxicityR35GM142869 · NIGMS · TEXAS A&M AGRILIFE RESEARCH · PI KUROUSKI, DMITRY · 2021 to 2025
$1.6M
NIGMS NIH HHS R35 GM142869
6 · The paper itself

Abstract

Abrupt aggregation of misfolded proteins is a hallmark of a large number of severe pathologies, including diabetes types 1 and 2, Alzheimer, and Parkinson diseases. A growing body of evidence suggests that lipids can uniquely change rates of amyloid-associated proteins as well as modify the structure of formed oligomers and fibrils. In this study, we utilize atomic force microscopy infrared (AFM-IR) spectroscopy, also known as nano-IR spectroscopy, to examine the structure of individual insulin oligomers, protofilaments, and fibrils grown in the presence of phospholipids. Our findings show that AFM-IR spectra of insulin oligomers have strong signals of C-H and PO

Indexed as

InsulinProteinsAmyloidMicroscopy, Atomic ForcePhospholipidsSpectrophotometry, InfraredAmyloidInsulinPhospholipidsProteins

Identifiers

PMID35266717
PMCPMC9169669
OpenAlexW4220762287

What OpenQuestion holds

Textmetadata
LicenceTDM
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.