• Kad N. M., Wang H., Kennedy G. G., Warshaw D. M., Van Houten B. Collaborative Dynamic DNA Scanning by Nucleotide Excision Repair Proteins Investigated by Single-Molecule Imaging of Quantum-Dot-Labeled Proteins. Molecular Cell (2010)Vol No. 37, 702-13. (pdf)

• Walcott S., Kad N.M. Theoretical distribution of run speed distribution for a molecular motor. Proceedings of the 2008 ASME international mechanical engineering congress and exposition. 2009. Vol 2, 437-446. (pdf)

• Kad N. M.,Trybus K. M., Warshaw D. M., Load and Pi Control Flux through the Branched Kinetic Cycle of Myosin V. J. Biol. Chem. 2008. Vol 283 No. 25 17477-84. (pdf)

• Mason, J.M., Mueller, K.M., and Arndt, K.M., iPEP – Peptides Designed and Selected for Interfering with Protein Interaction and Function. Biochem. Soc. Trans., 36, 1442-1447 (2008). (pdf)

• Hagemann, U.B., Mason, J.M., Müller, K.M. and Arndt, K.M., Selectional and mutational scope of peptides sequestering the Jun-Fos coiled-coil domain, J. Mol. Biol. 381, 73-88 (2008). (pdf)

• Willemsen T, Hagemann U.B., Jouaux E.M., Stebel S.C., Mason J.M., Müller K.M., and Arndt K.M., Protein Engineering. Book Chapter in ‘Molecular Biomethods Handbook’, 2nd Edition, Eds John M Walker and Ralph Rapley (2008). (pdf)

• Kad N. M., Patlak J. B., Fagnant P. M., Trybus K. M., Warshaw D. M., Mutation of a conserved glycine in the SH1-SH2 helix affects the load-dependent kinetics of myosin. Biophysical journal. 2007. Biophysical Journal, Vol 92, pp. 1623-31. (pdf)

• Mason, J.M., Hagemann, U., Arndt, K.M., Improved stability of the Jun−Fos Activator Protein-1 coiled coil motif: A stopped-flow circular dichroism kinetic analysis J. Biol. Chem. 282, 23015-23024 (2007). (pdf)

• Mason, J.M., Müller, K.M., and Arndt. K.M., Positive Aspects of Negative Protein Design: Simultaneous Selection of Specificity and Stability. Biochemistry, 46, 4804-4814 (2007). (pdf)

• Mason, J.M., Müller, K.M., and Arndt K.M., Considerations in the Design and Optimization of Coiled coil Structures. Methods. Mol. Biol., 352, 35-70 (2007). (pdf)

• Hecky, J., Mason, J.M., Arndt, K.M., and Müller, K.M., A General Method of Terminal Truncation, Evolution, and Re-Elongation to Generate Enzymes of Enhanced Stability. Methods. Mol. Biol., 352, 275-304 (2007). (pdf)

• Mason, J.M., Müller, K.M., Schmitz, M.A., and Arndt, K.M., Semirational Design of Jun-Fos Coiled coils with Increased Affinity: Universal Implications in Leucine zipper Prediction and Design. P.N.A.S. 103, 8989-8994, (2006). (pdf)

• Kokkoni, N., Stott, K., Amijee, H., Mason, J.M., and Doig, A.J., N-Methylated Peptide Inhibitors of beta-Amyloid Aggreggation and Toxicity. Optimisation of Inhibitor Structure. Biochemistry, 45, 9906-9918, (2006). (pdf)

• Compton, E.L.R., Farmer, N.A., Lorch, M., Mason, J.M., Moreton, K.M., and Booth, P.J., Kinetics of an Individual Transmembrane Helix during Bacteriorhodopsin Folding, J. Mol. Biol. 357, 325-38, (2006). (pdf)

• Kad N. M., Kim S., Warshaw D. M., VanBuren P., Baker J.E. Single myosin crossbridge interactions with actin filaments regulated by troponin-tropomyosin. Proceedings of the National Academy of Sciences (USA). 2005. Vol. 102 No. 47, 16990-5. (pdf)

• Mason, J.M., Cliff M.J., Sessions, R.B., and Clarke, A.R., Low-energy pathways and non-native interactions: The influence of artificial disulfide bridges on the mechanism of folding J.Biol.Chem. 280, 40494-40499 (2005). (pdf)

• Mason, J.M., and Arndt K.M., Coiled coils: stability, specificity, and biological implications. Chembiochem., 5, 170-6, (2004). (pdf)

• Kad N. M., Rovner A. S., Fagnant P. M., Joel P. B., Kennedy G. G., Patlak J. B., Warshaw D. M., Trybus K. M. A mutant heterodimeric myosin with one inactive head generates maximal displacement. Journal of Cell Biology. 2003. Vol. 162. No. 3, 481-8. (pdf)

• Mason J.M., Kokkoni N., Stott K., and Doig A.J., Design strategies for anti-amyloid agents. Curr. Op. Struct. Biol., 13, 526-32, (2003). (pdf)

• Kad N. M., Myers S. L., Smith D. P., Smith D.A.M., Radford S. E., Thomson N. H. Hierarchical assembly of β2-microglobulin amyloid in vitro revealed by atomic force microscopy. Journal of Molecular Biology, 2003, Vol. 330, No. 4, 785-97. (pdf)

• Jones S., Manning J., Kad N. M., Radford S.E. Amyloid-forming Peptides from β2-Microglobulin - Insights into the Mechanism of Fibril Formation in vitro. Journal of Molecular Biology, 2003, Vol. 325, No. 2, p. 249-257. (pdf) 

• Mason, J.M., Gibbs, N., Sessions, R.B., and Clarke A.R., The Influence of Intramolecular Bridges on the Dynamics of a Protein Folding Reaction. Biochemistry, 40, 12093-12099, (2002). (pdf)

• Kad N.M., Thomson, N., Smith, D.P., Smith, D.A.M., Radford, S.E. β2-Microglobulin and its Deamidated Variant, N17D Form Amyloid Fibrils with a Range of Morphologies in vitro. Journal of Molecular Biology, 2001, Vol. 313, No. 3, p. 559-571. (pdf)

 Book Chapters

• Kad N.M. and Radford, S.E. Partial unfolding as a precursor to amyloidosis: A discussion of the occurrence, role and implications. Frontiers in Molecular Biology. 2000, Ed. P. Lund, Oxford University Press

• Lorch, M., Mason, J.M., and Clarke, A.R., Effects of Mutations on the Thermodynamics of a Protein Folding Reaction: Implications for the Mechanism of Formation of Intermediate and transition States. Biochemistry, 39, 3480-3485, (2000). (pdf)

• McParland V. J., Kad N. M., Kalverda A. P., Brown A., Kirwin-Jones P., Hunter M. G., Sunde M., Radford S. E. Partially unfolded states of β2-microglobulin and amyloid formation in vitro. Biochemistry, 2000, Vol.39, No.30, p.8735 –8746. (pdf)

• Lorch, M., Mason, J.M., Clarke, A.R., and Parker, M.J., Effects of Core Mutations on the Folding of a β-sheet Protein: Implications for Backbone Organisation in the I-state Biochemistry, 38, 1377-1385, (1999). (pdf)

• Cliff M. J., Kad N. M., Hay N., Lund P. A., Webb M. R., Burston S. G., Clarke A. R. A kinetic analysis of the nucleotide-induced allosteric transitions of GroEL. Journal of Molecular Biology, 1999, Vol.293, No.3, p.667-684. (pdf)

• Kad N. M., Ranson N. A., Cliff M. J., Clarke A. R. Asymmetry, commitment and inhibition in the GroE ATPase cycle impose alternating functions on the two GroEL rings. Journal of Molecular Biology, 1998, Vol.278, No.1, p.267-278. (pdf)