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Gene|November 30, 1990
A general method for rapid site-directed mutagenesis using the polymerase chain reactionO Landt, H P Grunert, U HahnBiological Chemistry|June 1, 1997
Ribonuclease T1 is active when both catalytic histidines are replaced by aspartateO Landt, J Thölke, H P Grunert, et al.Biochemical and Biophysical Research Communications|February 28, 1994
Extended kinetic analysis of ribonuclease T1 variants leads to an improved scheme for the reaction mechanismJ Backmann, C C Doray, H P Grunert, et al.Journal of Molecular Biology|May 20, 1992
RNase T1 mutant Glu46Gln binds the inhibitors 2'GMP and 2'AMP at the 3' subsiteJ Granzin, R Puras-Lutzke, O Landt, et al.Protein Engineering|September 1, 1993
Trp59 to Tyr substitution enhances the catalytic activity of RNase T1 and of the Tyr to Trp variants in positions 24, 42 and 45H P Grunert, O Landt, M Zirpel-Giesebrecht, et al.European Journal of Biochemistry|October 1, 1991
Crystal structure of the Tyr45Trp mutant of ribonuclease T1 in a complex with 2'-adenylic acidG Koellner, H P Grunert, O Landt, et al.Journal of Biotechnology|June 1, 1992
Improving purification of recombinant ribonuclease T1O Landt, M Zirpel-Giesebrecht, A Milde, et al.Biochemistry|July 10, 1990
Replacement of a cis proline simplifies the mechanism of ribonuclease T1 foldingT Kiefhaber, H P Grunert, U Hahn, et al.Proteins|February 1, 1992
Folding of RNase T1 is decelerated by a specific tertiary contact in a folding intermediateT Kiefhaber, H P Grunert, U Hahn, et al.Journal of Molecular Biology|June 5, 1993
Stability and folding kinetics of ribonuclease T1 are strongly altered by the replacement of cis-proline 39 with alanineL M Mayr, O Landt, U Hahn, et al.Pageof 24