Evidence map›Paper›PMID 27090422›Full record

ArticleJournal of molecular evolution2016

Molecular Evolution of Alternative Oxidase Proteins: A Phylogenetic and Structure Modeling Approach.

Rosa Pennisi, Daniele Salvi, Valentina Brandi, Riccardo Angelini, Paolo Ascenzi, Fabio Polticelli

Abstract read
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In one paragraph

Article in Journal of molecular evolution, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.4field-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

18 citing papers in PubMed, 34 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

6 authors at 3 institutions in 2 countries.

Rosa PennisiDepartment of Sciences, Roma Tre University, Viale Guglielmo Marconi 446, 00146, Rome, Italy.
Daniele SalviCIBIO-InBIO, Centro de Investigação em Biodiversidade e Recursos Genéticos, Universidade do Porto, Campus Agrário de Vairão, 4485-661, Vairão, Portugal.
Valentina BrandiDepartment of Sciences, Roma Tre University, Viale Guglielmo Marconi 446, 00146, Rome, Italy.
Riccardo AngeliniDepartment of Sciences, Roma Tre University, Viale Guglielmo Marconi 446, 00146, Rome, Italy.
Paolo AscenziDepartment of Sciences, Roma Tre University, Viale Guglielmo Marconi 446, 00146, Rome, Italy.
Fabio PolticelliDepartment of Sciences, Roma Tre University, Viale Guglielmo Marconi 446, 00146, Rome, Italy. fabio.polticelli@uniroma3.it.
Roma Tre University · ITMarconi University · ITUniversidade do Porto · PT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Alternative oxidases (AOXs) are mitochondrial cyanide-resistant membrane-bound metallo-proteins catalyzing the oxidation of ubiquinol and the reduction of oxygen to water bypassing two sites of proton pumping, thus dissipating a major part of redox energy into heat. Here, the structure of Arabidopsis thaliana AOX 1A has been modeled using the crystal structure of Trypanosoma brucei AOX as a template. Analysis of this model and multiple sequence alignment of members of the AOX family from all kingdoms of Life indicate that AOXs display a high degree of conservation of the catalytic core, which is formed by a four-α-helix bundle, hosting the di-iron catalytic site, and is flanked by two additional α-helices anchoring the protein to the membrane. Plant AOXs display a peculiar covalent dimerization mode due to the conservation in the N-terminal region of a Cys residue forming the inter-monomer disulfide bond. The multiple sequence alignment has also been used to infer a phylogenetic tree of AOXs whose analysis shows a polyphyletic origin for the AOXs found in Fungi and a monophyletic origin of the AOXs of Eubacteria, Mycetozoa, Euglenozoa, Metazoa, and Land Plants. This suggests that AOXs evolved from a common ancestral protein in each of these kingdoms. Within the Plant AOX clade, the AOXs of monocotyledon plants form two distinct clades which have unresolved relationships relative to the monophyletic clade of the AOXs of dicotyledonous plants. This reflects the sequence divergence of the N-terminal region, probably due to a low selective pressure for sequence conservation linked to the covalent homo-dimerization mode.

Indexed as

Alternative OxidaseAmino Acid SequenceArabidopsisCatalytic DomainConserved SequenceEvolution, MolecularMitochondrial ProteinsModels, MolecularOxidation-ReductionOxidoreductasesPhylogenyPlant ProteinsPlantsProtein ConformationSequence AlignmentStructure-Activity RelationshipAlternative OxidaseMitochondrial ProteinsOxidoreductasesPlant ProteinsAlternative oxidaseMolecular evolutionMolecular modelingPhylogenetic analysis

Identifiers

PMID27090422
OpenAlexW2337800756

What OpenQuestion holds

Textmetadata
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.