ArticleInternational journal of biological macromolecules2010
Role of tyrosine 33 residue for the stabilization of the tetrameric structure of human cytidine deaminase.
Article in International journal of biological macromolecules, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 4 papers.
What it found
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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.
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Who cites it
4 citing papers in PubMed, 7 citations in OpenAlex.
- Cytidine and dCMP Deaminases-Current Methods of Activity Analysis.International journal of molecular sciences · 2025Review
- Article
- Human cytidine deaminase: a biochemical characterization of its naturally occurring variants.International journal of biological macromolecules · 2014Article
- Delineation of the molecular mechanisms of nucleoside recognition by cytidine deaminase through virtual screening.ChemMedChem · 2011Article
Corrections and comments
- Erratum issued
Authors and funding
10 authors at 2 institutions in 2 countries.
Funding
Abstract
In the present work the effect of a mutation on tyrosine 33 residue (Y33G) of human cytidine deaminase (CDA) was investigated with regard to protein solubility and specific activity. Osmolytes and CDA ligands were used to increase the yield and the specific activity of the protein. The mutant enzyme was purified and subjected to a kinetic characterization and to stability studies. These investigations reinforced the hypothesis that in human CDA the side chain of Y33 is involved in intersubunit interactions with four glutamate residues (E108) forming a double latch that connects each of the two pairs of monomers of the tetrameric CDA.
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Registered trials
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