Evidence map›Paper›PMID 31810296›Full record

ArticleJournal of clinical medicine2019

FAD/NADH Dependent Oxidoreductases: From Different Amino Acid Sequences to Similar Protein Shapes for Playing an Ancient Function.

Lucia Trisolini, Nicola Gambacorta, Ruggiero Gorgoglione, Michele Montaruli, Luna Laera, Francesco Colella, Mariateresa Volpicella, Anna De Grassi, Ciro Leonardo Pierri

Open access · goldAbstract read
In one paragraph

Article in Journal of clinical medicine, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
2.5field-weighted citation impact, top 10% 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

34 citing papers in PubMed, 79 citations in OpenAlex.

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  11. Three-Dimensional Modeling ofAntibodies (Basel, Switzerland) · 2025
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  12. Article
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  14. Review
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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

9 authors at 1 institution in 1 country.

Lucia TrisoliniLaboratory of Biochemistry; Molecular and Structural Biology; Department of Biosciences, Biotechnologies, Biopharmaceutics; University of Bari; Via E. Orabona 4; 70125 Bari, Italy.
Nicola GambacortaLaboratory of Biochemistry; Molecular and Structural Biology; Department of Biosciences, Biotechnologies, Biopharmaceutics; University of Bari; Via E. Orabona 4; 70125 Bari, Italy.
Ruggiero GorgoglioneLaboratory of Biochemistry; Molecular and Structural Biology; Department of Biosciences, Biotechnologies, Biopharmaceutics; University of Bari; Via E. Orabona 4; 70125 Bari, Italy.
Michele MontaruliLaboratory of Biochemistry; Molecular and Structural Biology; Department of Biosciences, Biotechnologies, Biopharmaceutics; University of Bari; Via E. Orabona 4; 70125 Bari, Italy.
Luna LaeraLaboratory of Biochemistry; Molecular and Structural Biology; Department of Biosciences, Biotechnologies, Biopharmaceutics; University of Bari; Via E. Orabona 4; 70125 Bari, Italy.
Francesco ColellaLaboratory of Biochemistry; Molecular and Structural Biology; Department of Biosciences, Biotechnologies, Biopharmaceutics; University of Bari; Via E. Orabona 4; 70125 Bari, Italy.
Mariateresa VolpicellaLaboratory of Biochemistry; Molecular and Structural Biology; Department of Biosciences, Biotechnologies, Biopharmaceutics; University of Bari; Via E. Orabona 4; 70125 Bari, Italy.
Anna De GrassiLaboratory of Biochemistry; Molecular and Structural Biology; Department of Biosciences, Biotechnologies, Biopharmaceutics; University of Bari; Via E. Orabona 4; 70125 Bari, Italy.
Ciro Leonardo PierriLaboratory of Biochemistry; Molecular and Structural Biology; Department of Biosciences, Biotechnologies, Biopharmaceutics; University of Bari; Via E. Orabona 4; 70125 Bari, Italy.
University of Bari Aldo Moro · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Flavoprotein oxidoreductases are members of a large protein family of specialized dehydrogenases, which include type II NADH dehydrogenase, pyridine nucleotide-disulphide oxidoreductases, ferredoxin-NAD+ reductases, NADH oxidases, and NADH peroxidases, playing a crucial role in the metabolism of several prokaryotes and eukaryotes. Although several studies have been performed on single members or protein subgroups of flavoprotein oxidoreductases, a comprehensive analysis on structure-function relationships among the different members and subgroups of this great dehydrogenase family is still missing. Here, we present a structural comparative analysis showing that the investigated flavoprotein oxidoreductases have a highly similar overall structure, although the investigated dehydrogenases are quite different in functional annotations and global amino acid composition. The different functional annotation is ascribed to their participation in species-specific metabolic pathways based on the same biochemical reaction, i.e., the oxidation of specific cofactors, like NADH and FADH

Indexed as

antibioticsapoptosis-inducing factor (AIF)dihydrolipoamide dehydrogenase (DLD)flavoprotein oxidoreductasesmitochondrial respirationmolecular modelingprotein shapethioredoxin reductase (TrxR1)type II NADH dehydrogenase (NDH-2)ubiquinone

Identifiers

PMID31810296
PMCPMC6947548
OpenAlexW2990938360

What OpenQuestion holds

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LicenceCC BY
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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.