Evidence map›Paper›PMID 35576075›Full record

ArticleEuropean biophysics journal : EBJ2022

Ultrasound-induced protein restructuring and ordered aggregation to form amyloid crystals.

Rachana Pathak, Sukhvir Kaur Bhangu, Gregory J O Martin, Frances Separovic, Muthupandian Ashokkumar

Open access · hybridAbstract read
In one paragraph

Article in European biophysics journal : EBJ, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
4.3field-weighted citation impact, top 5% 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

9 citing papers in PubMed, 32 citations in OpenAlex.

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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

5 authors at 2 institutions in 1 country.

Rachana PathakSchool of Chemistry, The University of Melbourne, Melbourne, VIC, 3010, Australia.ORCID http://orcid.org/0000-0002-0563-9845
Sukhvir Kaur BhanguSchool of Science, RMIT University, Melbourne, VIC, 3000, Australia.ORCID http://orcid.org/0000-0002-9810-4304
Gregory J O MartinDepartment of Chemical Engineering, The University of Melbourne, Melbourne, VIC, 3010, Australia.ORCID http://orcid.org/0000-0002-7099-7913
Frances SeparovicSchool of Chemistry, The University of Melbourne, Melbourne, VIC, 3010, Australia. fs@unimelb.edu.au.ORCID http://orcid.org/0000-0002-6484-2763
Muthupandian AshokkumarSchool of Chemistry, The University of Melbourne, Melbourne, VIC, 3010, Australia. masho@unimelb.edu.au.ORCID http://orcid.org/0000-0002-8442-1499
The University of Melbourne · AURMIT University · AU

Funding

Australian Research Council IH120100005
6 · The paper itself

Abstract

Amyloid crystals, a form of ordered protein aggregates documented relatively recently, have not been studied as extensively as amyloid fibres. This study investigates the formation of amyloid crystals with low frequency ultrasound (20 kHz) using β-lactoglobulin, as a model protein for amyloid synthesis. Acoustic cavitation generates localised zones of intense shear, with extreme heat and pressure that could potentially drive the formation of amyloid structures at ambient bulk fluid temperatures (20 ± 1 °C). Thioflavin T fluorescence and electron microscopy showed that low-frequency ultrasound at 20 W/cm

Indexed as

AmyloidLactoglobulinsProtein AggregatesSpectroscopy, Fourier Transform InfraredAmyloidLactoglobulinsProtein AggregatesAmyloidAmyloid crystalsProtein aggregationUltrasoundβ-Lactoglobulin

Identifiers

PMID35576075
PMCPMC9233657
OpenAlexW4280496874

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.