Evidence map›Paper›PMID 36674720›Full record

ArticleInternational journal of molecular sciences2023

DMSO-Induced Unfolding of the Antifungal Disulfide Protein PAF and Its Inactive Variant: A Combined NMR and DSC Study.

András Czajlik, Ágnes Batta, Kinga Kerner, Ádám Fizil, Dorottya Hajdu, Mária Raics, Katalin E Kövér, Gyula Batta

Abstract read
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In one paragraph

Article in International journal of molecular sciences, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
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

2 citing papers in PubMed.

  1. Article
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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

8 authors.

András CzajlikDepartment of Organic Chemistry, Faculty of Science and Technology, University of Debrecen, Egyetem tér 1, H-4032 Debrecen, Hungary.
Ágnes BattaDepartment of Biophysics and Cell Biology, Faculty of Medicine, University of Debrecen, Egyetem tér 1, H-4032 Debrecen, Hungary.
Kinga KernerDepartment of Organic Chemistry, Faculty of Science and Technology, University of Debrecen, Egyetem tér 1, H-4032 Debrecen, Hungary.
Ádám FizilDepartment of Organic Chemistry, Faculty of Science and Technology, University of Debrecen, Egyetem tér 1, H-4032 Debrecen, Hungary.
Dorottya HajduDepartment of Organic Chemistry, Faculty of Science and Technology, University of Debrecen, Egyetem tér 1, H-4032 Debrecen, Hungary.
Mária RaicsDepartment of Inorganic and Analytical Chemistry, Faculty of Science and Technology, University of Debrecen, Egyetem tér 1, H-4032 Debrecen, Hungary.
Katalin E KövérMTA-DE Molecular Recognition and Interaction Research Group, Department of Inorganic and Analytical Chemistry, Faculty of Science and Technology, University of Debrecen, Egyetem tér 1, H-4032 Debrecen, Hungary.ORCID 0000-0001-5020-4456
Gyula BattaDepartment of Organic Chemistry, Faculty of Science and Technology, University of Debrecen, Egyetem tér 1, H-4032 Debrecen, Hungary.ORCID 0000-0002-0442-1828

Funding

European Regional 439 Development Fund GINOP-2.3.2-15-2016-00008, GINOP-2.3.3-15-2016-440 00004National Research, Development, Innovation Office (NKFI) NKFI/OTKA NN 128368 (K.E.K.)National Research, Development, Innovation Office (NKFI) TKP2020-NKA-11
6 · The paper itself

Abstract

PAF and related antifungal proteins are promising antimicrobial agents. They have highly stable folds around room temperature due to the presence of 3-4 disulfide bonds. However, unfolded states persist and contribute to the thermal equilibrium in aqueous solution, and low-populated states might influence their biological impact. To explore such equilibria during dimethyl sulfoxide (DMSO)-induced chemical unfolding, we studied PAF and its inactive variant PAF

Indexed as

Antifungal AgentsDimethyl SulfoxideCalorimetry, Differential ScanningDisulfidesMagnetic Resonance SpectroscopyProtein DenaturationProteinsProtein UnfoldingThermodynamicsWaterAntifungal AgentsDimethyl SulfoxideDisulfidesProteinsWaterantifungal proteindifferential scanning calorimetry (DSC)disulfide bondDMSO-induced unfoldingnuclear magnetic resonance (NMR)PAF

Identifiers

PMID36674720
PMCPMC9864379

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Registered trials

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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.