D
David Coates
Researcher at University of Leeds
Publications - 37
Citations - 3649
David Coates is an academic researcher from University of Leeds. The author has contributed to research in topics: Angiotensin-converting enzyme & Drosophila melanogaster. The author has an hindex of 21, co-authored 37 publications receiving 3510 citations. Previous affiliations of David Coates include University of Oxford & French Alternative Energies and Atomic Energy Commission.
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Journal ArticleDOI
Comparative Genomics of the Eukaryotes
Gerald M. Rubin,Mark Yandell,Jennifer R. Wortman,George L. Gabor,Miklos,Catherine R. Nelson,Iswar K. Hariharan,Mark E. Fortini,Peter W. Li,Rolf Apweiler,Wolfgang Fleischmann,J. Michael Cherry,Steven Henikoff,Marian P. Skupski,Sima Misra,Michael Ashburner,Ewan Birney,Mark S. Boguski,Thomas Brody,Peter Brokstein,Susan E. Celniker,Stephen A. Chervitz,David Coates,Anibal Cravchik,Andrei Gabrielian,Richard F. Galle,William M. Gelbart,Reed A. George,Lawrence S.B. Goldstein,Fangcheng Gong,Ping Guan,Nomi L. Harris,Bruce A. Hay,Roger A. Hoskins,Jiayin Li,Zhenya Li,Richard O. Hynes,Steven J.M. Jones,Peter M. Kuehl,Bruno Lemaitre,J. Troy Littleton,Deborah K. Morrison,Christopher J. Mungall,Patrick H. O'Farrell,Oxana K. Pickeral,Chris Shue,Leslie B. Vosshall,Jiong Zhang,Qi Zhao,Xiangqun H. Zheng,Fei Zhong,Wenyan Zhong,Richard A. Gibbs,J. Craig Venter,Mark Raymond Adams,Suzanna E. Lewis +55 more
TL;DR: The fly has orthologs to 177 of the 289 human disease genes examined and provides the foundation for rapid analysis of some of the basic processes involved in human disease.
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The neprilysin (NEP) family of zinc metalloendopeptidases: genomics and function.
TL;DR: Knowledge of the complete genomes of Caenorhabditis elegans and Drosophila melanogaster allows the full complement of NEP‐like activities to be analysed in a single organism, and reveals the power of functional genomics.
Journal ArticleDOI
The angiotensin converting enzyme (ACE).
TL;DR: Mouse knockout experiments, and comparative work with invertebrate homologues, suggest that the two domains of angiotensin converting enzyme have clearly distinct roles.
Journal ArticleDOI
The code within the codons
F.J.R. Taylor,David Coates +1 more
TL;DR: It is shown that each of the three codon bases has a general correlation with a different, predictable amino acid property, depending on position within the codon, and the apparently systematic nature of these relationships has profound implications for the origin of the genetic code.
Journal ArticleDOI
Cloning and Expression of an Evolutionary Conserved Single-domain Angiotensin Converting Enzyme from Drosophila melanogaster
M. J. Cornell,Tracy Ann Williams,N. S. Lamango,David Coates,P. Corvol,F. Soubrier,Joerg Hoheisel,H. Lehrach,R. E. Isaac +8 more
TL;DR: An apparent single-domain (67 kDa) insect angiotensin converting enzyme (AnCE) in embryos of Drosophila melanogaster is identified and the cloning and expression of a Drosophile AnCE cDNA is reported which codes for a single- domain 615-amino acid protein with a predicted 17-AMino acid signal peptide and regions with high levels of homology to both the N- and C-domains of mammalian somatic ACE.