Nielsen, J. E., Beier, L.
, Otzen, D., Borchert, T. V., Frantzen, H. B.
, Andersen, K. V. & Svendsen, A. (1999).
Electrostatics in the active site of an α-amylase.
European Journal of Biochemistry,
264(3), 816-824.
https://doi.org/10.1046/j.1432-1327.1999.00664.x
Christophersen, C.
, Otzen, D. E., Norman, B. E., Christensen, S. & Schäfer, T. (1998).
Enzymatic characterisation of novamyl®, a thermostable α-amylase.
Starch/Staerke,
50(1), 39-45.
https://doi.org/10.1002/(SICI)1521-379X(199801)50:1<39::AID-STAR39>3.0.CO;2-S
Neira, J. L., Itzhaki, L. S.
, Otzen, D. E., Davis, B. & Fersht, A. R. (1997).
Hydrogen exchange in chymotrypsin inhibitor 2 probed by mutagenesis.
Journal of Molecular Biology,
270(1), 99-110.
https://doi.org/10.1006/jmbi.1997.1088
Daggett, V., Li, A., Itzhaki, L. S.
, Otzen, D. E. & Fersht, A. R. (1996).
Structure of the transition state for folding of a protein derived from experiment and simulation.
Journal of Molecular Biology,
257(2), 430-440.
https://doi.org/10.1006/jmbi.1996.0173
De Prat Gay, G., Ruiz-Sanz, J., Neira, J. L., Corrales, F. J.
, Otzen, D. E., Ladurner, A. G. & Fersht, A. R. (1995).
Conformational pathway of the polypeptide chain of chymotrypsin inhibitor-2 growing from its N terminus in vitro. Parallels with the protein folding pathway.
Journal of Molecular Biology,
254(5), 968-979.
https://doi.org/10.1006/jmbi.1995.0669
Matouschek, A.
, Otzen, D. E., Itzhaki, L. S., Jackson, S. E. & Fersht, A. R. (1995).
Movement of the Position of the Transition State in Protein Folding.
Biochemistry,
34(41), 13656-13662.
https://doi.org/10.1021/bi00041a047
Fersht, A. R., Itzhaki, L. S., Elmasry, N. F., Matthews, J. M.
& Otzen, D. E. (1994).
Single versus parallel pathways of protein folding and fractional formation of structure in the transition state.
Proceedings of the National Academy of Sciences,
91(22), 10426-10429.
https://doi.org/10.1073/pnas.91.22.10426
Otzen, D. E., Itzhaki, L. S., Elmasry, N. F., Jackson, S. E. & Fersht, A. R. (1994).
Structure of the transition state for the folding/unfolding of the barley chymotrypsin inhibitor 2 and its implications for mechanisms of protein folding.
Proceedings of the National Academy of Sciences,
91(22), 10422-10425.
https://doi.org/10.1073/pnas.91.22.10422
Barciszewski, J.
, Rattan, S., Siboska, G., Otzen, D. & Clark, B. F. C. (1993).
Reduction in the amount of 8-hydroxy-2´-deoxyguanosine in the DNA of SV40-transformed human fibroblasts as compared with normal cells in culture. F E B S Letters,
318, 186-188.