Owen, D., Campbell, L.J., Littlefield, K., Evetts, K.A., Li, Z., Sacks, D.B., Lowe, P.N. and Mott, H.R. (2008) The IQGAP1-Rac1 and IQGAP1-Cdc42 Interactions: Interfaces differ between the complexes J. Biol. Chem. 283: 1692–1704 Fenwick, R.B., Prasannan, S., Campbell, L.J., Nietlispach,D., Evetts, K.A., Camonis, J., Mott, H.R. and Owen, D. (2009) Solution structure and dynamics of the small GTPase RalB in its active conformation: significance for effector protein binding. Biochemistry 48: 2192-2206 Fenwick, R.B., Campbell, L.J., Rajasekar, K., Prasannan, S., Nietlispach, D., Camonis, J., Owen, D. and Mott, H.R. (2010) The RalB-RLIP76/RalBP1 complex reveals a novel mode of Ral-effector interaction. Structure 18: 985-995 Hutchinson, C.L., Lowe, P.N., McLaughlin, S.H., Mott, H.R. and Owen, D. (2011) Mutational analysis reveals a single binding interface between RhoA and its effector, PRK1. Biochemistry 50(14): 2860-2869 Rajasekar, K.V., Campbell, L.J., Nietlispach, D., Owen, D. and Mott, H.R. (2013). The structure of the RLIP76 (RalBP1) RhoGAP domain-Ral binding domain dyad: fixed position of the domains leads to dual engagement of small G proteins at the membrane. Structure 21:2131–2142, Hutchinson, C.L., Lowe, P.N., McLaughlin, S.H., Mott, H.R.and Owen, D. (2013) Differential binding of RhoA, B and C to the PRK isoforms PRK1, 2 and 3: PRKs have highest affinity for RhoB. Biochemistry 52(45):7999-8011