David J. Mann
University of Dundee
8 Papers
168 Citations
David J. Mann is an academic researcher from University of Dundee. The author has contributed to research in topics: Complementary DNA & Phosphatase. The author has an hindex of 5, co-authored 8 publications. Previous affiliations of David J. Mann include University of Sheffield.
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Papers
Protein serine/threonine phosphatases; an expanding family
TL;DR: Five protein serine/threonine phosphatases (PP) have been identified by cloning cDNA from mammalian and Drosophila libraries and the complete amino acid sequences of PPX, PPY and PPZ and an almost complete sequence of PPV are presented.
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Mammalian protein serine/threonine phosphatase 2C: cDNA cloning and comparative analysis of amino acid sequences.
TL;DR: Complementary DNA encoding rat protein phosphatase 2C alpha was obtained from a liver library and used to isolate the homologous cDNAs from rabbit liver and human teratocarcinoma libraries, and amino acid sequences of the three enzymes deduced from the cDNA were extremely similar.
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Drosophila protein phosphatase V functionally complements a SIT4 mutant in Saccharomyces cerevisiae and its amino-terminal region can confer this complementation to a heterologous phosphatase catalytic domain.
TL;DR: In Drosophila, a substantial transient increase in both PPV mRNA and protein occurs in late syncytial and early cellular blastoderm embryos, indicating that PPV may play a role in one or more of these processes.
56
Cloning of the fourth functional gene for protein phosphatase 1 in Drosophila melanogaster from its chromosomal location.
TL;DR: The fourth gene, PP1 13C, is most closely related to the isoform PP1 87B, which is involved in the control of chromosome separation at cell division and the regulation of chromosome condensation at interphase, and was shown to be expressed at a very low level.
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Pre-translational control of hepatic malic enzyme expression during the development of the rat.
David J. Mann,Ernest Bailey +1 more
TL;DR: Northern-blot analysis demonstrated that the two major malic enzyme mRNA species displayed non-co-ordinate control during development, with the 2.0 kb form accumulating to a greater extent than the 3.1 kb form.