Kahmann, J. D., Wecking, D. A., Putter, V., Lowenhaupt, K., Kim, Y., Schmieder, P., . . . Schade, M. (2004). The solution structure of the N-terminal domain of E3L shows a tyrosine conformation that may explain its reduced affinity to Z-DNA in vitro. National Academy of Sciences.

Kahmann, Jan D., Diana A. Wecking, Vera Putter, Ky Lowenhaupt, Yang-Gyun Kim, Peter Schmieder, Hartmut Oschkinat, Alexander Rich, and Markus Schade. The Solution Structure of the N-terminal Domain of E3L Shows a Tyrosine Conformation That May Explain Its Reduced Affinity to Z-DNA in Vitro. National Academy of Sciences, 2004.

Kahmann, Jan D., et al. The Solution Structure of the N-terminal Domain of E3L Shows a Tyrosine Conformation That May Explain Its Reduced Affinity to Z-DNA in Vitro. National Academy of Sciences, 2004.