Evidence map›Paper›PMID 16756667›Full record

ArticleBMC biology2006

Three rounds (1R/2R/3R) of genome duplications and the evolution of the glycolytic pathway in vertebrates.

Dirk Steinke, Simone Hoegg, Henner Brinkmann, Axel Meyer

Open access · goldAbstract read
In one paragraph

Article in BMC biology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
4.6field-weighted citation impact, top 4% 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

52 citing papers in PubMed, 119 citations in OpenAlex.

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  11. Expression and regulation ofFrontiers in genetics · 2022
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  16. Network-based microsynteny analysis identifies major differences and genomic outliers in mammalian and angiosperm genomes.Proceedings of the National Academy of Sciences of the United States of America · 2019
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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

4 authors at 2 institutions in 2 countries.

Dirk SteinkeLehrstuhl für Evolutionsbiologie und Zoologie, Department of Biology, University of Konstanz, 78457 Konstanz, Germany. dsteinke@uoguelph.ca
Simone Hoegg
Henner Brinkmann
Axel Meyer
University of Konstanz · DEUniversité de Montréal · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundEvolution of the deuterostome lineage was accompanied by an increase in systematic complexity especially with regard to highly specialized tissues and organs. Based on the observation of an increased number of paralogous genes in vertebrates compared with invertebrates, two entire genome duplications (2R) were proposed during the early evolution of vertebrates. Most glycolytic enzymes occur as several copies in vertebrate genomes, which are specifically expressed in certain tissues. Therefore, the glycolytic pathway is particularly suitable for testing theories of the involvement of gene/genome duplications in enzyme evolution.

resultsWe assembled datasets from genomic databases of at least nine vertebrate species and at least three outgroups (one deuterostome and two protostomes), and used maximum likelihood and Bayesian methods to construct phylogenies of the 10 enzymes of the glycolytic pathway. Through this approach, we intended to gain insights into the vertebrate specific evolution of enzymes of the glycolytic pathway. Many of the obtained gene trees generally reflect the history of two rounds of duplication during vertebrate evolution, and were in agreement with the hypothesis of an additional duplication event within the lineage of teleost fish. The retention of paralogs differed greatly between genes, and no direct link to the multimeric structure of the active enzyme was found.

conclusionThe glycolytic pathway has subsequently evolved by gene duplication and divergence of each constituent enzyme with taxon-specific individual gene losses or lineage-specific duplications. The tissue-specific expression might have led to an increased retention for some genes since paralogs can subdivide the ancestral expression domain or find new functions, which are not necessarily related to the original function.

Indexed as

Evolution, MolecularGene DuplicationGenomePhylogenyAnimalsDatabases, ProteinFructose-Bisphosphate AldolaseGlucose-6-Phosphate IsomeraseGlyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating)GlycolysisHexokinaseHumansPhosphofructokinase-1Phosphoglycerate KinasePhosphoglycerate MutasePhosphopyruvate HydrataseFructose-Bisphosphate AldolaseGlucose-6-Phosphate IsomeraseGlyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating)HexokinasePhosphofructokinase-1Phosphoglycerate KinasePhosphoglycerate MutasePhosphopyruvate HydratasePyruvate KinaseTriose-Phosphate Isomerase

Identifiers

PMID16756667
PMCPMC1508162
OpenAlexW2171671247

What OpenQuestion holds

Textmetadata
LicenceCC BY
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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.