Evidence map›Paper›PMID 25724722›Full record

ArticleMolecular and biochemical parasitology2014

Identification of novel cyclic nucleotide binding proteins in Trypanosoma cruzi.

Adriana V Jäger, Javier G De Gaudenzi, Jesica G Mild, Bárbara Mc Cormack, Sergio Pantano, Daniel L Altschuler, Martin M Edreira

Open access · greenAbstract read
In one paragraph

Article in Molecular and biochemical parasitology, 2014. 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
0.2field-weighted citation impact, top 40% 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, 23 citations in OpenAlex.

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  9. Review
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  11. Adenylate Cyclases ofPathogens (Basel, Switzerland) · 2018
    Review
  12. Review
  13. Gene editing of putative cAMP and CaThe Journal of eukaryotic microbiology
    Article
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

7 authors at 5 institutions in 4 countries.

Adriana V JägerInstituto de Investigaciones Biotecnológicas-Instituto Tecnológico de Chascomús, UNSAM-CONICET, Buenos Aires, Argentina.
Javier G De GaudenziInstituto de Investigaciones Biotecnológicas-Instituto Tecnológico de Chascomús, UNSAM-CONICET, Buenos Aires, Argentina.
Jesica G MildDepartamento de Química Biológica, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Ciudad de Buenos Aires, Argentina; IQUIBICEN-CONICET, Ciudad de Buenos Aires, Argentina.
Bárbara Mc CormackDepartamento de Química Biológica, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Ciudad de Buenos Aires, Argentina.
Sergio PantanoInstitut Pasteur de Montevideo, Uruguay.
Daniel L AltschulerDepartment of Pharmacology and Chemical Biology, School of Medicine, University of Pittsburgh, Pittsburgh, PA, USA. Electronic address: altschul@pitt.edu.
Martin M EdreiraDepartamento de Química Biológica, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Ciudad de Buenos Aires, Argentina; IQUIBICEN-CONICET, Ciudad de Buenos Aires, Argentina; Department of Pharmacology and Chemical Biology, School of Medicine, University of Pittsburgh, Pittsburgh, PA, USA. Electronic address: mme2@pitt.edu.
Consejo Nacional de Investigaciones Científicas y Técnicas · ARFundación Ciencias Exactas y Naturales · ARInstitut Pasteur · FRUniversidad de Buenos Aires · ARUniversity of Pittsburgh · US

Funding

Exploiting the cAMP pathway in Chagas Disease TherapyR03TW009001 · FIC · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI ALTSCHULER, DANIEL L · 2011 to 2013
$172k
FIC NIH HHS R03 TW009001FIC NIH HHS R03TW009001
6 · The paper itself

Abstract

Cyclic AMP has been implicated as second messenger in a wide range of cellular processes. In the protozoan parasite Trypanosoma cruzi, cAMP is involved in the development of the parasite's life cycle. While cAMP effectors have been widely studied in other eukaryotic cells, little is known about cAMP's mechanism of action in T. cruzi. To date, only a cAMP-dependent protein kinase A (PKA) has been cloned and characterised in this parasite; however experimental evidence indicates the existence of cAMP-dependent, PKA-independent events. In order to identify new cAMP binding proteins as potential cAMP effectors, we carried out in silico studies using the predicted T. cruzi proteome. Using a combination of search methods 27 proteins with putative cNMP binding domains (CBDs) were identified. Phylogenetic analysis of the CBDs presented a homogeneous distribution, with sequences segregated into two main branches: one containing kinases-like proteins and the other gathering hypothetical proteins with different function or no other known. Comparative modelling of the strongest candidates provides support for the hypothesis that these proteins may give rise to structurally viable cyclic nucleotide binding domains. Pull-down and nucleotide displacement assays strongly suggest that TcCLB.508523.80 could bind cAMP and eventually be a new putative PKA-independent cAMP effector in T. cruzi.

Indexed as

Carrier ProteinsCluster AnalysisComputational BiologyNucleotides, CyclicPhylogenyProtein BindingProtozoan ProteinsSequence Homology, Amino AcidTrypanosoma cruziCarrier ProteinsNucleotides, CyclicProtozoan ProteinscAMP binding proteinscAMP novel effectorscAMP signallingTrypanosoma cruzi

Identifiers

PMID25724722
PMCPMC8486353
OpenAlexW2079634357

What OpenQuestion holds

Textmetadata
LicenceTDM
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.