Evidence map›Paper›PMID 33024804›Full record

ArticleData in brief2020

Electrochemical data on redox properties of human Cofilin-2 and its Mutant S3D.

Marcello Pignataro, Giulia Di Rocco, Lidia Lancellotti, Fabrizio Bernini, Khaushik Subramanian, Elena Castellini, Carlo Augusto Bortolotti, Daniele Malferrari, Daniele Moro, Giovanni Valdrè and 2 more

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In one paragraph

Article in Data in brief, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0citing papers in PubMed
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1 · What the graph read from it

What it found

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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

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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

0 citing papers in PubMed, 0 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

12 authors at 5 institutions in 2 countries.

Marcello PignataroDepartment of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, USA.
Giulia Di RoccoDepartment of Life Sciences, University of Modena and Reggio Emilia, Modena, Italy.
Lidia LancellottiDepartment of Chemical and Geological Sciences, University of Modena and Reggio Emilia, Modena, Italy.
Fabrizio BerniniDepartment of Chemical and Geological Sciences, University of Modena and Reggio Emilia, Modena, Italy.
Khaushik SubramanianNovartis Institutes of Biomedical Research, Boston, USA.
Elena CastelliniDepartment of Chemical and Geological Sciences, University of Modena and Reggio Emilia, Modena, Italy.
Carlo Augusto BortolottiDepartment of Life Sciences, University of Modena and Reggio Emilia, Modena, Italy.
Daniele MalferrariDepartment of Chemical and Geological Sciences, University of Modena and Reggio Emilia, Modena, Italy.
Daniele MoroDepartment of Biological, Geological and Environmental Sciences, University of Bologna, Bologna, Italy.
Giovanni ValdrèDepartment of Biological, Geological and Environmental Sciences, University of Bologna, Bologna, Italy.
Marco BorsariDepartment of Chemical and Geological Sciences, University of Modena and Reggio Emilia, Modena, Italy.
Federica Del MonteGazes Cardiac Research Institute, Medical University of South Carolina, Charleston, USA.
University of Modena and Reggio Emilia · ITUniversity of Bologna · ITColorado State University · USMedical University of South Carolina · USNovartis (United States) · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The reported data are related to a research paper entitled "Phosphorylated cofilin-2 is more prone to oxidative modifications on Cys39 and favors amyloid fibril formation" [1]. Info about the formation and redox properties of the disulfide bridge of a protein is quite difficult to obtain and only in a few cases was it possible to observe a cyclic voltammetry (CV) signal [2,3]. Human cofilin-2 contains two cysteines (Cys39 and Cys80) which can be oxidized in suitable conditions and form a disulfide bridge [1]. For this purpose, CV measurements were carried out on human cofilin-2 WT and its mutant S3D immobilized on a gold electrode coated by an anionic self-assembled monolayer (SAM), after a pre-oxidation time which was fundamental for observing a CV signal relating to the oxidation/reduction process of the disulfide bridge of the proteins. The data include CV curves obtained with and without electrochemical pre-oxidation and after oxidation with H

Indexed as

Cyclic voltammetryCysteineDisulfide bridgeElectrochemistryHuman cofilinRedox properties

Identifiers

PMID33024804
PMCPMC7528206
OpenAlexW3087975611

What OpenQuestion holds

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LicenceCC BY-NC-ND
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Registered trials

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