Evidence map›Paper›PMID 29700324›Full record

ArticleScientific reports2018

Self-homodimerization of an actinoporin by disulfide bridging reveals implications for their structure and pore formation.

Aisel Valle, Luis Benito Pérez-Socas, Liem Canet, Yadira de la Patria Hervis, German de Armas-Guitart, Diogo Martins-de-Sa, Jônatas Cunha Barbosa Lima, Adolfo Carlos Barros Souza, João Alexandre Ribeiro Gonçalves Barbosa, Sonia Maria de Freitas and 1 more

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

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
0.9field-weighted citation impact, top 18% 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

0 citing papers in PubMed, 13 citations in OpenAlex.

No citing paper in PubMed yet.

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

11 authors at 2 institutions in 2 countries.

Aisel ValleLaboratory of Molecular Biophysics, Institute of Biological Sciences, University of Brasília (IB-CEL/UnB), Campus Darcy Ribeiro, Asa Norte, Brasília, DF-70910-900, Brazil. aiselvalle@gmail.com.ORCID 0000-0001-6947-1087
Luis Benito Pérez-SocasBiochemistry Department and Center for Protein Studies, Faculty of Biology, Havana, University (Bq-CEP/UH), Universidad de la Habana, Calle 25 No. 455, Plaza de la Revolución, La Habana, CP-10 400, Cuba.ORCID 0000-0003-2392-4663
Liem CanetBiochemistry Department and Center for Protein Studies, Faculty of Biology, Havana, University (Bq-CEP/UH), Universidad de la Habana, Calle 25 No. 455, Plaza de la Revolución, La Habana, CP-10 400, Cuba.
Yadira de la Patria HervisBiochemistry Department and Center for Protein Studies, Faculty of Biology, Havana, University (Bq-CEP/UH), Universidad de la Habana, Calle 25 No. 455, Plaza de la Revolución, La Habana, CP-10 400, Cuba.
German de Armas-GuitartBiochemistry Department and Center for Protein Studies, Faculty of Biology, Havana, University (Bq-CEP/UH), Universidad de la Habana, Calle 25 No. 455, Plaza de la Revolución, La Habana, CP-10 400, Cuba.
Diogo Martins-de-SaLaboratory of Molecular Biophysics, Institute of Biological Sciences, University of Brasília (IB-CEL/UnB), Campus Darcy Ribeiro, Asa Norte, Brasília, DF-70910-900, Brazil.ORCID 0000-0001-6981-7738
Jônatas Cunha Barbosa LimaLaboratory of Molecular Biophysics, Institute of Biological Sciences, University of Brasília (IB-CEL/UnB), Campus Darcy Ribeiro, Asa Norte, Brasília, DF-70910-900, Brazil.
Adolfo Carlos Barros SouzaLaboratory of Molecular Biophysics, Institute of Biological Sciences, University of Brasília (IB-CEL/UnB), Campus Darcy Ribeiro, Asa Norte, Brasília, DF-70910-900, Brazil.
João Alexandre Ribeiro Gonçalves BarbosaLaboratory of Molecular Biophysics, Institute of Biological Sciences, University of Brasília (IB-CEL/UnB), Campus Darcy Ribeiro, Asa Norte, Brasília, DF-70910-900, Brazil.
Sonia Maria de FreitasLaboratory of Molecular Biophysics, Institute of Biological Sciences, University of Brasília (IB-CEL/UnB), Campus Darcy Ribeiro, Asa Norte, Brasília, DF-70910-900, Brazil.
Isabel Fabiola PazosBiochemistry Department and Center for Protein Studies, Faculty of Biology, Havana, University (Bq-CEP/UH), Universidad de la Habana, Calle 25 No. 455, Plaza de la Revolución, La Habana, CP-10 400, Cuba.
Universidade de Brasília · BRUniversity of Havana · CU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Trp111 to Cys mutant of sticholysin I, an actinoporin from Stichodactyla helianthus sea anemone, forms a homodimer via a disulfide bridge. The purified dimer is 193 times less hemolytic than the monomer. Ultracentrifugation, dynamic light scattering and size-exclusion chromatography demonstrate that monomers and dimers are the only independent oligomeric states encountered. Indeed, circular dichroism and fluorescence spectroscopies showed that Trp/Tyr residues participate in homodimerization and that the dimer is less thermostable than the monomer. A homodimer three-dimensional model was constructed and indicates that Trp147/Tyr137 are at the homodimer interface. Spectroscopy results validated the 3D-model and assigned 85° to the disulfide bridge dihedral angle responsible for dimerization. The homodimer model suggests that alterations in the membrane/carbohydrate-binding sites in one of the monomers, as result of dimerization, could explain the decrease in the homodimer ability to form pores.

Identifiers

PMID29700324
PMCPMC5920107
OpenAlexW2806023392

What OpenQuestion holds

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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.