Evidence map›Paper›PMID 25775131›Full record

ArticlePloS one2015

Glyceraldehyde 3-phosphate dehydrogenase-telomere association correlates with redox status in Trypanosoma cruzi.

Ricardo Pariona-Llanos, Raphael Souza Pavani, Marcelo Reis, Vincent Noël, Ariel Mariano Silber, Hugo Aguirre Armelin, Maria Isabel Nogueira Cano, Maria Carolina Elias

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

13 citing papers in PubMed, 35 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

8 authors at 3 institutions in 1 country.

Ricardo Pariona-LlanosLaboratório Especial de Ciclo Celular, Instituto Butantan, São Paulo, Brazil; Center of Toxins, Immune Response and Cell Signaling-CeTICS, Instituto Butantan, São Paulo, Brazil.
Raphael Souza PavaniLaboratório Especial de Ciclo Celular, Instituto Butantan, São Paulo, Brazil; Center of Toxins, Immune Response and Cell Signaling-CeTICS, Instituto Butantan, São Paulo, Brazil.
Marcelo ReisLaboratório Especial de Ciclo Celular, Instituto Butantan, São Paulo, Brazil; Center of Toxins, Immune Response and Cell Signaling-CeTICS, Instituto Butantan, São Paulo, Brazil.
Vincent NoëlLaboratório Especial de Ciclo Celular, Instituto Butantan, São Paulo, Brazil; Center of Toxins, Immune Response and Cell Signaling-CeTICS, Instituto Butantan, São Paulo, Brazil.
Ariel Mariano SilberUnit for Drug Discovery-Departamento de Parasitologia, Instituto de Ciências Biomédicas, Universidade de São Paulo, São Paulo, Brazil.
Hugo Aguirre ArmelinLaboratório Especial de Ciclo Celular, Instituto Butantan, São Paulo, Brazil; Center of Toxins, Immune Response and Cell Signaling-CeTICS, Instituto Butantan, São Paulo, Brazil; Departamento de Bioquímica, Instituto de Química, Universidade de São Paulo, São Paulo, Brazil.
Maria Isabel Nogueira CanoDepartamento de Genética, Instituto de Biociências, Universidade Estadual Paulista Júlio de Mesquita Filho-UNESP, Botucatu, Brazil.
Maria Carolina EliasLaboratório Especial de Ciclo Celular, Instituto Butantan, São Paulo, Brazil; Center of Toxins, Immune Response and Cell Signaling-CeTICS, Instituto Butantan, São Paulo, Brazil.
Instituto Butantan · BRUniversidade de São Paulo · BRUniversidade Estadual Paulista (Unesp) · BR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glyceraldehyde 3-phosphate dehydrogenase (GAPDH) is a classical metabolic enzyme involved in energy production and plays a role in additional nuclear functions, including transcriptional control, recognition of misincorporated nucleotides in DNA and maintenance of telomere structure. Here, we show that the recombinant protein T. cruzi GAPDH (rTcGAPDH) binds single-stranded telomeric DNA. We demonstrate that the binding of GAPDH to telomeric DNA correlates with the balance between oxidized and reduced forms of nicotinamide adenine dinucleotides (NAD+/NADH). We observed that GAPDH-telomere association and NAD+/NADH balance changed throughout the T. cruzi life cycle. For example, in replicative epimastigote forms of T. cruzi, which show similar intracellular concentrations of NAD+ and NADH, GAPDH binds to telomeric DNA in vivo and this binding activity is inhibited by exogenous NAD+. In contrast, in the T. cruzi non-proliferative trypomastigote forms, which show higher NAD+ concentration, GAPDH was absent from telomeres. In addition, NAD+ abolishes physical interaction between recombinant GAPDH and synthetic telomere oligonucleotide in a cell free system, mimicking exogenous NAD+ that reduces GAPDH-telomere interaction in vivo. We propose that the balance in the NAD+/NADH ratio during T. cruzi life cycle homeostatically regulates GAPDH telomere association, suggesting that in trypanosomes redox status locally modulates GAPDH association with telomeric DNA.

Indexed as

Oxidation-ReductionActive Transport, Cell NucleusGlyceraldehyde-3-Phosphate DehydrogenasesModels, TheoreticalNADProtein BindingProtein TransportTelomereTrypanosoma cruziGlyceraldehyde-3-Phosphate DehydrogenasesNAD

Identifiers

PMID25775131
PMCPMC4361584
OpenAlexW1994946529

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.