| Staff Details | ||||
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| Personal Information | ||
| Name | Kelly, Vincent Patrick | |
| Main Department | Biochemistry | |
| College Title | Lecturer/Academic Co-Ordinator | |
| kellyvp@tcd.ie | ||
| College Tel | +353 1 896 3507 | |
| Web | http://people.tcd.ie/kellyvp | |
| Biography | |
| In November 2005, I joined the staff of the School of Biochemistry & Immunology having secured an SFI principle investigator award to study the role of a transfer RNA modification in tyrosine biosynthesis. The scope and direction of the work has diversified since to include studies on cancer and immunology using cell based and transgenic models. I performed my postdoctoral studies in the laboratory of Prof. Masayuki Yamamoto, Tsukuba, Japan where I gained expertise in mouse transgenics. My interest in transfer RNA arose from my time in Banyu Pharmaceuticals (a subsidiary of Merck) in Japan where I worked with Dr. Susumu Nishimura, generating a knockout mouse for the seleocysteine tRNA gene. My PhD was performed in the laboratory of Prof. John Hayes, at the University of Dundee, Scotland. My project focused on characterizing the AFAR1 enzyme (an Aldo-Keto Reductase family member) and research on a novel related enzyme called AFAR2, which I discovered can produce the hypnotic gamma-hydroxybutyrate, a chemical that is vital for sleep and hibernation. | |
| Membership of Professional Institutions, Associations, Societies |
| Details | Date From | Date To |
| Biochemical Society | Sept 2000 | Present date |
| Languages |
| Language | Skill Reading | Skill Writing | Skill Speaking |
| English | Fluent | Fluent | Fluent |
| Japanese | Basic | Basic | Medium |
| Description of Research Interests |
| Our laboratory researches on RNA. In particular we are interested in modified nucleotides and their impact on basic metabolism. The research techniques that the laboratory use are varied and include cell culture, the generation of transgenic animals, HPLC and protein purification. |
| Research Interests | |||
| Animal Biotechnology | Animal Reproduction | Embryology | Immunology, Immunotherapy |
| Nutrition |
| Research Projects | |
| Project title | Q-base; an essential nutrient for tyrosine biosynthesis.Implications for the disease phenylketonuria and transfer RNA biology. |
| Summary | Ireland has the highest incidence in the world of the metabolic disease phenylketonuria (PKU). Individuals with PKU have abnormally high levels of phenylalanine in their blood because their bodies cannot break down phenylalanine to tyrosine. Babies in particular are at risk of developing severe mental retardation, hence why this disease is routinely screened for in new-born infants. We are studying a molecule found in everyday food called queuine. Animals with no queuine are unable to convert phenylalanine to tyrosine in the same way as individuals with PKU. Understanding why this is true will open up a whole new understanding of the PKU disease and could provide novel drug targets. It is even possible that administering the queuine molecule itself to PKU sufferers could be of therapeutic potential. |
| Funding Agency | Science Foundation Ireland |
| Programme | |
| Type of Project | Basic Research |
| Date from | November 2005 |
| Date to | November 2009 |
| Person Months | 168 |
| Publications |
| Peer Reviewed |
| Kawatani Y, Suzuki T, Shimizu R, Kelly VP, Yamamoto M., Nrf2 and selenoproteins are essential for maintaining oxidative homeostasis in erythrocytes and protecting against hemolytic anemia., Blood, 20, (1), 2011, p986 - 996 | |
| MacLeod AK, Kelly VP, Higgins LG, Kelleher MO, Price SA, Bigley AL, Betton GR, Hayes JD., Expression and localization of rat aldo-keto reductases and induction of the 1B13 and 1D2 isoforms by phenolic antioxidants., Drug Metabolism & Disposition, 38, (2), 2010, p341 - 346 Notes: [PMID: 19920056 ] |
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| Arai T, Kelly VP, Minowa O, Noda T, Nishimura S. , The study using wild-type and Ogg1 knockout mice exposed to potassium bromate shows no tumor induction despite an extensive accumulation of 8-hydroxyguanine in kidney DNA , Toxicology , 221, 2006, p179 - 186 Notes: [PubMed ID: 16494984] DOI |
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| Kobayashi T, Takimura T, Sekine R, Kelly VP, Kamata K, Sakamoto K, Nishimura S, Yokoyama S., Structural snapshots of the KMSKS loop rearrangement for amino acid activation by bacterial tyrosyl-tRNA synthetase, J. Mol. Biol., 346, (1), 2005, p105 - 117 Notes: [PubMed ID: 15663931] DOI |
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| More Publications>>> | |
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