A structural explanation for the binding of endocytic dileucine motifs by the AP2 complex Bernard T. Kelly, Airlie J. McCoy, Kira Späte, Sharon E. Miller, Philip R. Evans, Stefan Höning and David J. Owen Nature, 456, 976-979 (2008)(PDF)
Molecular Basis for the Sorting of the SNARE VAMP7 into Endocytic Clathrin-Coated Vesicles by the ArfGAP Hrb. Paul R. Pryor, Lauren Jackson, Sally R. Gray, Melissa A. Edeling, Amanda Thompson, Christopher M. Sanderson, Philip R. Evans, David J. Owen, and J. Paul Luzio. Cell 134, 817–827 (2008)(PDF)
Structure and Analysis of FCHo2 F-BAR Domain: A Dimerizing and Membrane Recruitment Module that Effects Membrane Curvature (2007) William Mike Henne, Helen M. Kent, Marijn G.J. Ford, Balachandra G. Hegde, Oliver Daumke, P. Jonathan G. Butler, Rohit Mittal, Ralf Langen, Philip R. Evans and Harvey T. McMahon Structure 15, 1–14(PDF)
Mechanism of endophilin N-BAR domain-mediated membrane curvature. Jennifer L. Gallop, Christine C. Jao, Helen M. Kent, P. Jonathan G. Butler, Philip R. Evans, Ralf Langen & Harvey T. McMahon Embo J. 25, 2898-2910 (2006)(PDF)
Structural Analysis of the Interaction Between the SNARE Tlg1 and Vps51. Yael Fridmann-Sirkis, Helen M. Kent, Michael J. Lewis, Philip R. Evans and Hugh R. B. Pelham, Traffic, 7, 182–190 (2006)(PDF)
Non-canonical YXXGF endocytic motifs: recognition by AP2 and preferential utilization in P2X4 receptors. Stephen J. Royle, Omar S. Qureshi, Laura K. Bobanovic, Philip R. Evans, David J. Owen & Ruth D. Murrell-Lagnado, J. Cell Science, 118, 3073-3080 (2005)(PDF)
Adaptors for clathrin coats: structure and function. D.J.Owen, B.M.Collins and P.R.Evans, Annual Reviews of Cell and Developmental Biology 20, 153-191 (2004)
Two distinct interaction motifs in amphiphysin bind two independent sites on the clathrin terminal domain beta-propeller. Adriana E. Miele, Peter J. Watson, Philip R. Evans, Linton M. Traub & David J. Owen, Nature Structural and Molecular Biology, 11, 242-248 (2004)(PDF)
BAR domains as sensors of membrane curvature: the amphiphysin BAR structure. B.J.Peter, H.M.Kent, I.G.Mills, Y.Vallis, P.J.G.Butler, P.R.Evans and H.T.McMahon, Science, 303, 495-499 (2004)(PDF)
Endocytosis and vesicle trafficking. P.R.Evans & D.J.Owen, Current Opinions in Structural Biology, 12, 814-821 (2002)(PDF)
Curvature of clathrin-coated pits driven by epsin. Marijn G.J. Ford, Ian G. Mills, Brian J. Peter, Yvonne Vallis, Gerrit J.K. Praefcke, Philip R. Evans and Harvey T. McMahon, Nature, 419, 361-366 (2002)(PDF)
Gamma-adaptin appendage domain : Structure and binding site for Eps15 and gamma-synergin , H.M.Kent, H.T.McMahon, P.R. Evans, A. Benmerah and D.J.Owen, Structure, 10, 1139-1148 (2002) (PDF)
Molecular architecture and functional model of the endocytic AP2 complex. B.M.Collins, A.J.McCoy, H.M.Kent, P.R.Evans and D.J.Owen, Cell, 109, 523-535 (2002) (PDF)
Simultaneous binding of PtdIns(4,5)P2 and Clathrin by AP180 in the nucleation of Clathrin Lattices on Membranes, M.G.J.Ford, B.M.F.Pearse, M.K.Higgins, Y.Vallis, D.J.Owen, A.Gibson, C.Hopkins, P.R.Evans and H.T.McMahon, Science, 291, 1051-1055 (2001) (PDF)
A third hydrophobic binding site in µ2 adaptin for sequences upstream of YxxF internalization motifs, D.J.Owen, H.Setiadi, P.R.Evans, R.P.McEver and S.A.Green, Traffic, 2, 105-110 (2001) (PDF)
The structure and function of the beta2-adaptin appendage domain, D.J.Owen, Y.Vallis, B.M.F.Pearse, H.T.McMahon and P.R.Evans, EMBO J. 19, 4216-4227 (2000) (PDF)
A structural explanation for the binding of multiple ligands by the alpha-adaptin appendage domain. Owen, D.J., Vallis, Y., Noble, M.E.M., Hunter, J.B., Dafforn,T.R., Evans, P.R. & McMahon, H.T. Cell. 97, 805-815 (1999) (PDF).
A structural explanation for the recognition of tyrosine-based endocytotic signals, D.J.Owen & P.R.Evans, Science, 282, 1327-1332 (1998) (PDF)
Crystal structure of the amphiphysin-2 SH3 domain and its role in the prevention of dynamin ring formation, D.J.Owen, P.Wigge, Y.Vallis, J.D.A.Moore, P.R.Evans & H.T.McMahon, EMBO J.17, 5273-5285 (1998) (PDF)
Decoding of methylated histone H3 tail by the Pygo-BCL9 Wnt signaling complex. Fiedler M, Sánchez-Barrena MJ, Nekrasov M, Mieszczanek J, Rybin V, Müller J, Evans P, Bienz M (2008) Molecular Cell 30, 507-518 (PDF)
The structural basis for the recognition of acetylated histone H4 by the bromodomain of histone acetyltransferase Gcn5p, D.J.Owen, P.Ornaghi, J-C. Wang, N.Lowe, P.R.Evans, P.Ballario, D.Neuhaus, P.Filetici and A.A.Travers, EMBO J 19, 6141-6149 (2000) (PDF)
Protection of radical intermediates at the active site of adenosylcobalamin-dependent methylmalonyl-CoA mutase. Thomä, N.H., Evans, P.R. and Leadlay, P.F. Biochemistry (2000), 39, 9213-9221 (PDF)
The crystal structure of substrate complexes of methylmalonyl-CoA mutase, F.Mancia, G.A.Smith & P.R.Evans, Biochemistry, 38, 7999-8005 (1999) (PDF)
Stabilization of radical intermediates by an active-site tyrosine residue in methylmalonyl-CoA mutase, N.H.Thomä, T.W.Meier, P.R.Evans & P.F.Leadlay, Biochemistry, 37, 14386-14393 (1998) (PDF)
Conformational changes on substrate binding to methylmalonyl CoA mutase and new insights into the free radical mechanism, F.Mancia & P.R.Evans, Structure, 6, 711-720 (1998)
How coenzyme B12 radicals are generated: the crystal structure of methylmalonyl-coenzyme A mutase at 2Å resolution, F.Mancia, N.H.Keep, A.Nakagawa, P.F.Leadlay, S.McSweeney, B.Rasmussen, P.Bösecke, O.Diat & P.R.Evans, Structure 4, 339-350 (1996)
An Introduction to Molecular Replacement. P.R.Evans & A.J.McCoy. Acta Cryst D64, 1-10 (2008)
An introduction to stereochemical restraints. P.R.Evans Acta Cryst. D63, 58-61 (2007) (PDF)
Scaling and assessment of data quality P.R.Evans, Acta Cryst . D62, 72-82 (2006) (PDF)
Phasing the AP2 core complex with Xe, Hg and Se. P.R.Evans, Acta Cryst. D59, 2039-2043 (2003)(PDF)
Rotations and rotation matrices, Evans, P.R. Acta Cryst. D57, 1355-1359 (2001) (Proceedings of the 2001 CCP4 Study Weekend on Molecular Replacement) (PDF)
Scaling of MAD data P.R.Evans, Proceedings of the CCP4 Study Weekend, January 1997, ed. K.S.Wilson, G.Davies, A.W.Ashton, S.Bailey, (CCLRC Daresbury Laboratory, Warrington), pg 97-102