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Background Research Publications Current Lab |
| Professor Ron Hay |
| E: r.t.hay@dundee.ac.uk |
| T: 44 1382 386309 |
| F: 44 1382 223778 |
Professor Ron Hay FRS FRSE - Honorary Programme Leader
Publications
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Larance, M., Bailly, A.P., Pourkarimi, E., Hay, R.T., Buchanan, G., Coulthurst, S., Xirodimas, D.P., Gartner, A., and Lamond, A.I. (2011). Stable-isotope labeling with amino acids in nematodes. Nat Methods 8, 849-851. |
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Matic, I., Jaffray, E.G., Oxenham, S.K., Groves, M.J., Barratt, C.L., Tauro, S., Stanley-Wall, N.R., and Hay, R.T. (2011). Absolute SILAC-Compatible Expression Strain Allows Sumo-2 Copy Number Determination in Clinical Samples. J Proteome Res 10, 4869-4875. |
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Plechanovova, A., Jaffray, E.G., McMahon, S.A., Johnson, K.A., Navratilova, I., Naismith, J.H., and Hay, R.T. (2011). Mechanism of ubiquitylation by dimeric RING ligase RNF4. Nat Struct Mol Biol 18, 1052-1059. |
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Tatham, M.H., Matic, I., Mann, M., and Hay, R.T. (2011). Comparative proteomic analysis identifies a role for SUMO in protein quality control. Sci Signal 4, rs4. |
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Bruderer, R., Tatham, M.H., Plechanovova, A., Matic, I., Garg, A.K., and Hay, R.T. (2011). Purification and identification of endogenous polySUMO conjugates. EMBO Rep 12, 142-148. |
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Hattersley, N., Shen, L., Jaffray, E.G., and Hay, R.T. (2011). The SUMO protease SENP6 is a direct regulator of PML nuclear bodies. Mol Biol Cell 22, 78-90. |
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Napolitano, L.M., Jaffray, E.G., Hay, R.T., and Meroni, G. (2011). Functional interactions between ubiquitin E2 enzymes and TRIM proteins. Biochem J 434, 309-319. |
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Li, X., Vadrevu, S., Dunlop, A., Day, J., Advant, N., Troeger, J., Klussmann, E., Jaffrey, E., Hay, R.T., Adams, D.R., Houslay, M.D. and Baillie, G.S. (2010). Selective SUMO modification of cAMP-specific phosphodiesterase-4D5 (PDE4D5) regulates the functional consequences of phosphorylation by PKA and ERK. Biochem J 428, 55-65. |
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Hjerpe, R., Aillet, F., Lopitz-Otsoa, F., Lang, V., Torres-Ramos, M., Farras, R., Hay, R.T., and Rodriguez, M.S. (2010). Oligomerization conditions Mdm2-mediated efficient p53 polyubiquitylation but not its proteasomal degradation. Int J Biochem Cell Biol 42, 725-735. |
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Golebiowski, F., Tatham, M.H., Nakamura, A., and Hay, R.T. (2010). High-stringency tandem affinity purification of proteins conjugated to ubiquitin-like moieties. Nat Protoc 5, 873-882. |
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Hannoun, Z., Greenhough, S., Jaffray, E., Hay, R.T., and Hay, D.C. (2010). Post-translational modification by SUMO. Toxicology 278, 288-293. |
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Castillo-Lluva, S., Tatham, M.H., Jones, R.C., Jaffray, E.G., Edmondson, R.D., Hay, R.T., and Malliri, A. (2010). SUMOylation of the GTPase Rac1 is required for optimal cell migration. Nat Cell Biol 12, 1078-1085. |
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Geoffroy, M.C., Jaffray, E.G., Walker, K.J., and Hay, R.T. (2010). Arsenic-induced SUMO-dependent recruitment of RNF4 into PML nuclear bodies. Mol Biol Cell 21, 4227-4239. |
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Geoffroy, M.C., and Hay, R.T. (2009). An additional role for SUMO in ubiquitin-mediated proteolysis. Nat Rev Mol Cell Biol 10, 564-568. |
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Golebiowski, F., Matic, I., Tatham, M.H., Cole, C., Yin, Y., Nakamura, A., Cox, J., Barton, G.J., Mann, M., and Hay, R.T. (2009). System-wide changes to SUMO modifications in response to heat shock. Sci Signal 2, ra24. |
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Shen, L.N., Geoffroy, M.C., Jaffray, E.G., and Hay, R.T. (2009). Characterization of SENP7, a SUMO-2/3-specific isopeptidase. Biochem J 421, 223-230. |
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Tatham, M.H., and Hay, R.T. (2009). FRET-based in vitro assays for the analysis of SUMO protease activities. Methods Mol Biol 497, 253-268. |
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Miles, W.O., Jaffray, E., Campbell, S.G., Takeda, S., Bayston, L.J., Basu, S.P., Li, M., Raftery, L.A., Ashe, M.P., Hay, R.T., and Ashe, H.L. (2008). Medea SUMOylation restricts the signaling range of the Dpp morphogen in the Drosophila embryo. Genes Dev 22, 2578-2590. |
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Tatham, M.H., Geoffroy, M.C., Shen, L., Plechanovova, A., Hattersley, N., Jaffray, E.G., Palvimo, J.J., and Hay, R.T. (2008). RNF4 is a poly-SUMO-specific E3 ubiquitin ligase required for arsenic-induced PML degradation. Nat Cell Biol 10, 538-546. |
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Agostinho, M., Santos, V., Ferreira, F., Costa, R., Cardoso, J., Pinheiro, I., Rino, J., Jaffray, E., Hay, R.T., and Ferreira, J. (2008). Conjugation of human topoisomerase 2 alpha with small ubiquitin-like modifiers 2/3 in response to topoisomerase inhibitors: cell cycle stage and chromosome domain specificity. Cancer Res 68, 2409-2418. |
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Martin, S.F., Tatham, M.H., Hay, R.T., and Samuel, I.D. (2008). Quantitative analysis of multi-protein interactions using FRET: application to the SUMO pathway. Protein Sci 17, 777-784. |
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Xirodimas, D.P., Sundqvist, A., Nakamura, A., Shen, L., Botting, C., and Hay, R.T. (2008). Ribosomal proteins are targets for the NEDD8 pathway. EMBO Rep 9, 280-286. |
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Matic, I., van Hagen, M., Schimmel, J., Macek, B., Ogg, S.C., Tatham, M.H., Hay, R.T., Lamond, A.I., Mann, M., and Vertegaal, A.C. (2008). In vivo identification of human small ubiquitin-like modifier polymerization sites by high accuracy mass spectrometry and an in vitro to in vivo strategy. Mol Cell Proteomics 7, 132-144. |
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Hay, R.T. (2007). SUMO-specific proteases: a twist in the tail. Trends Cell Biol 17, 370-376. |
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Tillmanns, S., Otto, C., Jaffray, E., Du Roure, C., Bakri, Y., Vanhille, L., Sarrazin, S., Hay, R.T., and Sieweke, M.H. (2007). SUMO modification regulates MafB-driven macrophage differentiation by enabling Myb-dependent transcriptional repression. Mol Cell Biol 27, 5554-5564. |
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Jacobs, A.M., Nicol, S.M., Hislop, R.G., Jaffray, E.G., Hay, R.T., and Fuller-Pace, F.V. (2007). SUMO modification of the DEAD box protein p68 modulates its transcriptional activity and promotes its interaction with HDAC1. Oncogene 26, 5866-5876. |
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Meinecke, I., Cinski, A., Baier, A., Peters, M.A., Dankbar, B., Wille, A., Drynda, A., Mendoza, H., Gay, R.E., Hay, R.T., Ink, B., Gay, S. and Pap, T. (2007). Modification of nuclear PML protein by SUMO-1 regulates Fas-induced apoptosis in rheumatoid arthritis synovial fibroblasts. Proc Natl Acad Sci U S A 104, 5073-5078. |
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Dorval, V., Mazzella, M.J., Mathews, P.M., Hay, R.T., and Fraser, P.E. (2007). Modulation of Abeta generation by small ubiquitin-like modifiers does not require conjugation to target proteins. Biochem J 404, 309-316. |
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Martin, S.F., Hattersley, N., Samuel, I.D., Hay, R.T., and Tatham, M.H. (2007). A fluorescence-resonance-energy-transfer-based protease activity assay and its use to monitor paralog-specific small ubiquitin-like modifier processing. Anal Biochem 363, 83-90. |
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Janssen, K., Hofmann, T.G., Jans, D.A., Hay, R.T., Schulze-Osthoff, K., and Fischer, U. (2007). Apoptin is modified by SUMO conjugation and targeted to promyelocytic leukemia protein nuclear bodies. Oncogene 26, 1557-1566. |
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