Evidence map›Paper›PMID 34299548›Full record

ArticleMolecules (Basel, Switzerland)2021

In Situ Monitored Vortex Fluidic-Mediated Protein Refolding/Unfolding Using an Aggregation-Induced Emission Bioprobe.

Qi Hu, Haozhen Hu, Xinyi Zhang, Kyle Fan, Yuning Hong, Colin L Raston, Youhong Tang

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Molecules (Basel, Switzerland), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.3field-weighted citation impact, top 47% 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

1 citing paper in PubMed, 4 citations in OpenAlex.

  1. 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

7 authors at 2 institutions in 1 country.

Qi HuMedical Device Research Institute, College of Science and Engineering, Flinders University, Adelaide, SA 5042, Australia.
Haozhen HuMedical Device Research Institute, College of Science and Engineering, Flinders University, Adelaide, SA 5042, Australia.
Xinyi ZhangMedical Device Research Institute, College of Science and Engineering, Flinders University, Adelaide, SA 5042, Australia.
Kyle FanFlinders Institute for Nanoscale Science and Technology, College of Science and Engineering, Flinders University, Adelaide, SA 5042, Australia.
Yuning HongDepartment of Chemistry and Physics, La Trobe Institute for Molecular Science, La Trobe University, Melbourne, VIC 3086, Australia.ORCID 0000-0002-8085-1651
Colin L RastonFlinders Institute for Nanoscale Science and Technology, College of Science and Engineering, Flinders University, Adelaide, SA 5042, Australia.
Youhong TangMedical Device Research Institute, College of Science and Engineering, Flinders University, Adelaide, SA 5042, Australia.ORCID 0000-0003-2718-544X
Flinders University · AULa Trobe University · AU

Funding

Australia-China Science and Research Fund Joint Research Centre on Personal Health TechnologiesAustralian Research Council DP200101106
6 · The paper itself

Abstract

Protein folding is important for protein homeostasis/proteostasis in the human body. We have established the ability to manipulate protein unfolding/refolding for β-lactoglobulin using the induced mechanical energy in the thin film microfluidic vortex fluidic device (VFD) with monitoring as such using an aggregation-induced emission luminogen (AIEgen), TPE-MI. When denaturant (guanidine hydrochloride) is present with β-lactoglobulin, the VFD accelerates the denaturation reaction in a controlled way. Conversely, rapid renaturation of the unfolded protein occurs in the VFD in the absence of the denaturant. The novel TPE-MI reacts with exposed cysteine thiol when the protein unfolds, as established with an increase in fluorescence intensity. TPE-MI provides an easy and accurate way to monitor the protein folding, with comparable results established using conventional circular dichroism. The controlled VFD-mediated protein folding coupled with in situ bioprobe AIEgen monitoring is a viable methodology for studying the denaturing of proteins.

Indexed as

Biosensing TechniquesCircular DichroismCysteineGuanidineHumansKineticsLactoglobulinsProtein ConformationProtein DenaturationProtein FoldingProtein RefoldingProteinsProtein UnfoldingProteostasisSpectrometry, FluorescenceCysteineGuanidineLactoglobulinsProteinsaggregation induced emissionprotein folding/unfoldingvortex fluidic device

Identifiers

PMID34299548
PMCPMC8306882
OpenAlexW3181019022

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.