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Aachmann, F. L., Otzen, D. E., Larsen, K. L. & Wimmer, R. (2003). Structural background of cyclodextrin-protein interactions. Protein Engineering, 16(12), 905-912.

Melo, E. P., Chen, L. Y., Cabral, J. M. S., Fojan, P., Petersen, S. B. & Otzen, D. E. (2003). Trehalose favors a cutinase compact intermediate off-folding pathway. Biochemistry, 42(24), 7611-7617. https://doi.org/10.1021/bi034267x

Otzen, D. E. & Oliveberg, M. (2002). Burst-phase expansion of native protein prior to global unfolding in SDS. Journal of Molecular Biology, 315(5), 1231-1240. https://doi.org/10.1006/jmbi.2001.5300

Otzen, D. E. & Oliveberg, M. (2002). Conformational plasticity in folding of the split β-α-β protein S6: Evidence for burst-phase disruption of the native state. Journal of Molecular Biology, 317(4), 613-627. https://doi.org/10.1006/jmbi.2002.5423

Otzen, D. E. (2002). Protein unfolding in detergents: Effect of micelle structure, ionic strength, pH, and temperature. Biophysical Journal, 83(4), 2219-2230. https://doi.org/10.1016/S0006-3495(02)73982-9

Otzen, D. E., Knudsen, B. R., Aachmann, F., Larsen, K. L. & Wimmer, R. (2002). Structural basis for cyclodextrins' suppression of human growth hormone aggregation. Protein Science, 11(7), 1779-1787. https://doi.org/10.1110/ps.0202702

Mogensen, J. E., Wimmer, R., Larsen, J. N., Spangfort, M. D. & Otzen, D. E. (2002). The major birch allergen, Bet v 1, shows affinity for a broad spectrum of physiological ligands. Journal of Biological Chemistry, 277(26), 23684-23692. https://doi.org/10.1074/jbc.M202065200

Otzen, D. E. & Oliveberg, M. (2001). A simple way to measure protein refolding rates in water. Journal of Molecular Biology, 313(3), 479-483. https://doi.org/10.1006/jmbi.2001.5039

Lindberg, M. O., Tångrot, J., Otzen, D. E., Dolgikh, D. A., Finkelstein, A. V. & Oliveberg, M. (2001). Folding of circular permutants with decreased contact order: General trend balanced by protein stability. Journal of Molecular Biology, 314(4), 891-900. https://doi.org/10.1006/jmbi.2001.5186

Otzen, D. & Schülein, M. (2001). Stability and Folding of Endoglucanase I (CEL7B) from Humicoia Insolens. Biocatalysis and Biotransformation, 19(42130), 469-487. https://doi.org/10.3109/10242420108992031

Otzen, D. E., Kristensen, O. & Oliveberg, M. (2000). Designed protein tetramer zipped together with a hydrophobic Alzheimer homology: A structural clue to amyloid assembly. Proceedings of the National Academy of Sciences (PNAS), 97(18), 9907-9912. https://doi.org/10.1073/pnas.160086297

Umakoshi, H., Persson, J., Kroon, M., Johansson, H. O., Otzen, D. E., Kuboi, R. & Tjerneld, F. (2000). Model process for separation based on unfolding and refolding of chymotrypsin inhibitor 2 in thermoseparating polymer two-phase systems. Journal of Chromatography B: Biomedical Sciences and Applications, 743(1-2), 13-19. https://doi.org/10.1016/S0378-4347(00)00190-0

Cavallin, A., Arozenius, H., Kristensson, K., Antonsson, P., Otzen, D. E., Björk, P. & Forsberg, G. (2000). The spectral and thermodynamic properties of staphylococcal enterotoxin A, E, and variants suggest that structural modifications are important to control their function. Journal of Biological Chemistry, 275(3), 1665-1672. https://doi.org/10.1074/jbc.275.3.1665

Otzen, D. E., Christiansen, L. & Schülein, M. (1999). A comparative study of the unfolding of the endoglucanase Ce145 from Humicola insolens in denaturant and surfactant. Protein Science, 8(9), 1878-1887. https://doi.org/10.1110/ps.8.9.1878

Otzen, D. E. & Fersht, A. R. (1999). Analysis of protein-protein interactions by mutagenesis: Direct versus indirect effects. Protein Engineering, 12(1), 41-45.

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

Otzen, D. E. & Oliveberg, M. (1999). Salt-induced detour through compact regions of the protein folding landscape. Proceedings of the National Academy of Sciences (PNAS), 96(21), 11746-11751. https://doi.org/10.1073/pnas.96.21.11746

Otzen, D. E., Kristensen, O., Proctor, M. & Oliveberg, M. (1999). Structural changes in the transition state of protein folding: Alternative interpretations of curved chevron plots. Biochemistry, 38(20), 6499-6511. https://doi.org/10.1021/bi982819j

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

Otzen, D. E. & Fersht, A. R. (1998). Folding of circular and permuted chymotrypsin inhibitor 2: Retention of the folding nucleus. Biochemistry, 37(22), 8139-8146. https://doi.org/10.1021/bi980250g

Fatum, T. M., Olsen, A. A., Fuglsang, C. C. & Otzen, D. (1998). Properties of PEG-modified microbial proteases. Activity and stability studies. Progress in Biotechnology, 15(C), 147-150. https://doi.org/10.1016/S0921-0423(98)80024-5

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

Tan, Y. J., Oliveberg, M., Otzen, D. E. & Fersht, A. R. (1997). Rate of isomerisation of peptidyl-proline bonds as a probe for interactions in the physiological denatured state of chymotrypsin inhibitor 2. Journal of Molecular Biology, 269(4), 611-622. https://doi.org/10.1006/jmbi.1997.1043

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

Itzhaki, L. S., Otzen, D. E. & Fersht, A. R. (1995). Nature and Consequences of GroEL-Protein Interactions. Biochemistry, 34(44), 14581-14587. https://doi.org/10.1021/bi00044a037

Ruiz-Sanz, J., de Prat Gay, G., Otzen, D. E. & Fersht, A. R. (1995). Protein Fragments as Models for Events in Protein Folding Pathways: Protein Engineering Analysis of the Association of Two Complementary Fragments of the Barley Chymotrypsin Inhibitor 2 (CI-2). Biochemistry, 34(5), 1695-1701. https://doi.org/10.1021/bi00005a026

Otzen, D. E. & Fersht, A. R. (1995). Side-Chain Determinants of β-Sheet Stability. Biochemistry, 34(17), 5718-5724. https://doi.org/10.1021/bi00017a003

Otzen, D. E., Rheinnecker, M. & Fersht, A. R. (1995). Structural Factors Contributing to the Hydrophobic Effect: The Partly Exposed Hydrophobic Minicore in Chymotrypsin Inhibitor. Biochemistry, 34(40), 13051-13058. https://doi.org/10.1021/bi00040a016

Itzhaki, L. S., Otzen, D. E. & Fersht, A. R. (1995). The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: Evidence for a nucleation-condensation mechanism for protein folding. Journal of Molecular Biology, 254(2), 260-288. https://doi.org/10.1006/jmbi.1995.0616

Otzen, D. E., Barciszewski, J. & Clark, B. F. C. (1994). Dual hydrolytic role for Pb(II) ions. Biochimie, 76(1), 15-21. https://doi.org/10.1016/0300-9084(94)90058-2

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 (PNAS), 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 (PNAS), 91(22), 10422-10425. https://doi.org/10.1073/pnas.91.22.10422

Otzen, D. E., Barciszewski, J. & Clark, B. F. C. (1993). Altered lead(II)-cleavage pattern of free Phe-tRNA(Phe) and Phe-tRNA(Phe) in ternary complex with EF-Tu:GTP. Biochemistry and Molecular Biology International, 31(1), 95-103.

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. FEBS Letters, 318, 186-188.

Barciszewski, J., Otzen, D., Rattan, S. I. S. & Clark, B. F. C. (1992). Specific incorporation of kinetin into eukaryotic and prokaryotic transfer ribonucleic acid molecules. Biochemistry international, 28(5), 805-811.

Barciszewski, J., Rattan, S., Otzen, D. & Clark, B. F. C. (1992). Specific incorportation of kinetin into eukaryotic and prokaryotic transfer ribonucleic acid molecules. Biochemistry international, 28, 805-811.

Displaying results 401 to 438 out of 438

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Revised 17.04.2023

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Lise Refstrup Linnebjerg Pedersen