Evidence map›Paper›PMID 30894486›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2019

Amyloid found in human cataracts with two-dimensional infrared spectroscopy.

Ariel M Alperstein, Joshua S Ostrander, Tianqi O Zhang, Martin T Zanni

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
4.8field-weighted citation impact, top 4% 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

21 citing papers in PubMed, 80 citations in OpenAlex.

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  8. DThe journal of physical chemistry. B · 2023
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  11. A polarization scheme that resolves cross-peaks with transient absorption and eliminates diagonal peaks in 2D spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2022
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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

4 authors at 1 institution in 1 country.

Ariel M AlpersteinDepartment of Chemistry, University of Wisconsin-Madison, Madison, WI 53706.ORCID 0000-0003-1310-1081
Joshua S OstranderDepartment of Chemistry, University of Wisconsin-Madison, Madison, WI 53706.
Tianqi O ZhangDepartment of Chemistry, University of Wisconsin-Madison, Madison, WI 53706.
Martin T ZanniDepartment of Chemistry, University of Wisconsin-Madison, Madison, WI 53706 zanni@chem.wisc.edu.
University of Wisconsin–Madison · US

Funding

Crystallin aggregation and stabilizationR01GM102387 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI ZANNI, MARTIN T · 2014 to 2017
$1.1M
NIGMS NIH HHS R01 GM102387
6 · The paper itself

Abstract

UV light and other factors damage crystallin proteins in the eye lens, resulting in cataracts that scatter light and affect vision. Little information exists about protein structures within these disease-causing aggregates. We examined postmortem lens tissue from individuals with and without cataracts using 2D infrared (2DIR) spectroscopy. Amyloid β-sheet secondary structure was detected in cataract lenses along with denatured structures. No amyloid structures were found in lenses from juveniles, but mature lenses with no cataract diagnosis also contained amyloid, indicating that amyloid structures begin forming before diagnosis. Light scatters more strongly in regions with amyloid structure, and UV light induces amyloid β-sheet structures, linking the presence of amyloid structures to disease pathology. Establishing that age-related cataracts involve amyloid structures gives molecular insight into a common human affliction and provides a possible structural target for pharmaceuticals as an alternative to surgery.

Indexed as

AmyloidLens Capsule, CrystallineUltraviolet RaysAgedCataractFemaleHumansMaleProtein Aggregation, PathologicalProtein Structure, SecondarySpectrophotometry, InfraredAmyloid2DIR spectroscopyamyloidcataractsprotein misfolding

Identifiers

PMID30894486
PMCPMC6452718
OpenAlexW2924528101

What OpenQuestion holds

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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.