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Genomic Distribution of Pro-Virulent cpdB -like Genes in Eubacteria and Comparison of the Enzyme Specificity of CpdB-like Proteins from Salmonella enterica , Escherichia coli and Streptococcus suis.
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- International Journal of Molecular Sciences, 2023, v. 24, n. 4, p. 4150, doi. 10.3390/ijms24044150
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- Article
Molecular Dissection of Escherichia coli CpdB: Roles of the N Domain in Catalysis and Phosphate Inhibition, and of the C Domain in Substrate Specificity and Adenosine Inhibition.
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- International Journal of Molecular Sciences, 2021, v. 22, n. 4, p. 1977, doi. 10.3390/ijms22041977
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- Article
Enzyme Characterization of Pro-virulent SntA, a Cell Wall-Anchored Protein of Streptococcus suis , With Phosphodiesterase Activity on cyclic-di-AMP at a Level Suited to Limit the Innate Immune System.
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- Frontiers in Microbiology, 2022, v. 13, p. 1, doi. 10.3389/fmicb.2022.843068
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- Article
CGDEase, a Pseudomonas fluorescens protein of the PLC/APase superfamily with CDP-ethanolamine and (dihexanoyl)glycerophosphoethanolamine hydrolase activity induced by osmoprotectants under phosphate-deficient conditions.
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- Molecular Microbiology, 2010, v. 78, n. 6, p. 1556, doi. 10.1111/j.1365-2958.2010.07425.x
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- Article
Molecular Bases of Catalysis and ADP-Ribose Preference of Human Mn<sup>2+</sup>-Dependent ADP-Ribose/CDP-Alcohol Diphosphatase and Conversion by Mutagenesis to a Preferential Cyclic ADP-Ribose Phosphohydrolase.
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- PLoS ONE, 2015, v. 10, n. 2, p. 1, doi. 10.1371/journal.pone.0118680
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- Article
Alternative Splicing of the Last TKFC Intron Yields Transcripts Differentially Expressed in Human Tissues That Code In Vitro for a Protein Devoid of Triokinase and FMN Cyclase Activity.
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- Biomolecules (2218-273X), 2024, v. 14, n. 10, p. 1288, doi. 10.3390/biom14101288
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- Article
¿HAY UNA PEDAGOGíA NACIONAL DE LA LECTO-ESCRITURA?
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- Lectura y Vida, 2005, v. 26, n. 1, p. 14
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The Characterization of Escherichia coli CpdB as a Recombinant Protein Reveals that, besides Having the Expected 3´-Nucleotidase and 2´,3´-Cyclic Mononucleotide Phosphodiesterase Activities, It Is Also Active as Cyclic Dinucleotide Phosphodiesterase
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- PLoS ONE, 2016, v. 11, n. 6, p. 1, doi. 10.1371/journal.pone.0157308
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- Article