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Stetefeld, J. and Jenny, M. and Burkhard, P.. (2006) Intersubunit signaling in glutamate-1-semialdehyde-aminomutase. Proceedings of the National Academy of Sciences of the United States of America, Vol. 103, H. 37. pp. 13688-13693.

Raman, S. and Machaidze, G. and Lustig, A. and Aebi, U. and Burkhard, P.. (2006) Structure-based design of peptides that self-assemble into regular polyhedral nanoparticles. Nanomedicine, Vol. 2, H. 2. pp. 95-102.

Appenzeller-Herzog, C. and Nyfeler, B. and Burkhard, P. and Santamaria, I. and Lopez-Otin, C. and Hauri, H. -P.. (2005) Carbohydrate- and conformation-dependent cargo capture for ER-exit. Molecular Biology of the Cell, 16 (3). pp. 1258-1267.

Strelkov, S. V. and Schumacher, J. and Burkhard, P. and Aebi, U. and Herrmann, H.. (2004) Crystal structure of the human lamin A coil 2B dimer: implications for the head-to-tail association of nuclear lamins. Journal of molecular biology, Vol. 343, H. 4. pp. 1067-1080.

Meier, M. and Oliveriusova, J. and Kraus, J. P. and Burkhard, P.. (2003) Structural insights into mutations of cystathionine beta-synthase. Biochimica et biophysica acta, Vol. 1647, H. 1/2. pp. 206-213.

Burkhard, P. and Ivaninskii, S. and Lustig, A.. (2002) Improving coiled-coil stability by optimizing ionic interactions. Journal of molecular biology, Vol. 318, H. 3. pp. 901-910.

Strelkov, S. V. and Herrmann, H. and Geisler, N. and Wedig, T. and Zimbelmann, R. and Aebi, U. and Burkhard, P.. (2002) Conserved segments 1A and 2B of the intermediate filament dimer: their atomic structures and role in filament assembly. The EMBO journal, Vol. 21, H. 6. pp. 1255-1266.

Burkhard, P. and Dominici, P. and Borri-Voltattorni, C. and Jansonius, J. N. and Malashkevich, V. N.. (2001) Structural insight into Parkinson's disease treatment from drug-inhibited DOPA decarboxylase. Nature Structural biology, Vol. 8, H. 11. pp. 963-967.

Meier, M. and Janosik, M. and Kery, V. and Kraus, J. P. and Burkhard, P.. (2001) Structure of human cystathionine beta-synthase : a unique pyridoxal 5'-phosphate-dependent heme protein. The EMBO journal, Vol. 20, H. 15. pp. 3910-3916.

Strelkov, S. V. and Herrmann, H. and Geisler, N. and Lustig, A. and Ivaninskii, S. and Zimbelmann, R. and Burkhard, P. and Aebi, U.. (2001) Divide-and-conquer crystallographic approach towards an atomic structure of intermediate filaments. Journal of molecular biology, Vol. 306, H. 4. pp. 773-781.

Burkhard, P. and Stetefeld, J. and Strelkov, S. V.. (2001) Coiled coils : a highly versatile protein folding motif. Trends in cell biology, Vol. 11, H. 2. pp. 82-88.

Burkhard, P. and Meier, M. and Lustig, A.. (2000) Design of a minimal protein oligomerization domain by a structural approach. Protein Science, Vol. 9, H. 12. pp. 2294-2301.

Burkhard, P. and Kammerer, R. A. and Steinmetz, M. O. and Bourenkov, G. P. and Aebi, U.. (2000) The coiled-coil trigger site of the rod domain of cortexillin I unveils a distinct network of interhelical and intrahelical salt bridges. Structure: with folding and design, Vol. 8, H. 3. pp. 223-230.

Burkhard, P. and Taylor, P. and Walkinshaw, M. D.. (2000) X-ray structures of small ligand-FKBP complexes provide an estimate for hydrophobic interaction energies. Journal of molecular biology, Vol. 295, H. 4. pp. 953-962.

Burkhard, P. and Tai, C. H. and Ristroph, C. M. and Cook, P. F. and Jansonius, J. N.. (1999) Ligand binding induces a large conformational change in O-acetylserine sulfhydrylase from Salmonella typhimurium. Journal of molecular biology, Vol. 291, H. 4. pp. 941-953.

Malashkevich, V. N. and Burkhard, P. and Dominici, P. and Moore, P. S. and Borri Voltattorni, C. and Jansonius, J. N.. (1999) Preliminary X-ray analysis of a new crystal form of recombinant pig kidney DOPA decarboxylase. Acta Crystallographica. Section D, Biological Crystallography, Vol. 55, Pt. 2. pp. 568-570.

Burkhard, P. and Rao, G. S. and Hohenester, E. and Schnackerz, K. D. and Cook, P. F. and Jansonius, J. N.. (1998) Three-dimensional structure of O-acetylserine sulfhydrylase from Salmonella typhimurium. Journal of molecular biology, Vol. 283, H. 1. pp. 121-133.