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Xu, T.-R., Lu, R.-F., Romano, D., Pitt, A., Houslay, M. D., Milligan, G. and Kolch, W. (2012) Eukaryotic translation initiation factor 3, subunit a, regulates the extracellular signal-regulated kinase pathway. Molecular and Cellular Biology, 32(1), pp. 88-95. (doi: 10.1128/​MCB.05770-11)

Xu, T. et al. (2010) Inferring signaling pathway topologies from multiple perturbation measurements of specific biochemical species. Science Signaling, 3(113), ra20. (doi: 10.1126/scisignal.2000517)

Kiely, P. A., Baillie, G. S. , Barrett, R., Buckley, D. A., Adams, D. R., Houslay, M. D. and O'Connor, R. (2009) Phosphorylation of RACK1 on tyrosine 52 by c-Abl is required for IGF-I-mediated regulation of focal adhesion kinase (FAK). Journal of Biological Chemistry, 284, pp. 20263-20274. (doi: 10.1074/jbc.M109.017640) (PMID:19423701) (PMCID:PMC2740452)

Meng, D., Lynch, M. J., Huston, E., Beyermann, M., Eichhorst, J., Adams, D. R., Klusmann, E., Houslay, M. D. and Baillie, G. S. (2009) MEK1 binds directly to βArrestin1, influencing both its phosphorylation by ERK and the timing of its isoprenaline-stimulated internalization. Journal of Biological Chemistry, 284(17), pp. 11425-11435. (doi: 10.1074/jbc.M806395200) (PMID:19153083) (PMCID:PMC2670148)

Ward, R. J., Jenkins, L. and Milligan, G. (2009) Selectivity and functional consequences of interactions of family A G protein-coupled receptors with neurochondrin and periplakin. Journal of Neurochemistry, 109(1), pp. 182-192. (doi: 10.1111/j.1471-4159.2009.05918.x)

Huston, E., Lynch, M. J., Mohamed, A., Collins, D. M., Hill, E. V., McLeod, R., Krause, E., Baillie, G. S. and Houslay, M. D. (2008) EPAC and PKA allow cAMP dual control over DNA-PK nuclear translocation. Proceedings of the National Academy of Sciences of the United States of America, 105(35), pp. 12791-12796. (doi: 10.1073/pnas.0805167105)

Xu, T.-R., Baillie, G. S. , Bhari, N., Houslay, T. M., Pitt, A. M., Adams, D. R., Kolch, W., Houslay, M. D. and Milligan, G. (2008) Mutations of β-arrestin 2 that limit self-association also interfere with interactions with the β2-adrenoceptor and the ERK1/2 MAPKs: implications for β2-adrenoceptor signalling via the ERK1/2 MAPKs. Biochemical Journal, 413(1), pp. 51-60. (doi: 10.1042/BJ20080685)

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