U. Selent

发表

A site-directed mutagenesis study to identify amino acid residues involved in the catalytic function of the restriction endonuclease EcoRV.

T. Oelgeschläger, A. Pingoud, J. Alves, 1992, Biochemistry.

DNA binding specificity of the EcoRV restriction endonuclease is increased by Mg2+ binding to a metal ion binding site distinct from the catalytic center of the enzyme.

A. Jeltsch, A. Pingoud, B. Connolly, 1995, Biochemistry.

Evidence for substrate-assisted catalysis in the DNA cleavage of several restriction endonucleases.

A. Jeltsch, A. Pingoud, M. Pleckaityte, 1995, Gene.

Does the restriction endonuclease EcoRV employ a two-metal-Ion mechanism for DNA cleavage?

A. Jeltsch, A. Pingoud, U. Selent, 1997, Biochemistry.

Protein engineering of the restriction endonuclease EcoRV: replacement of an amino acid residue in the DNA binding site leads to an altered selectivity towards unmodified and modified substrates.

A. Jeltsch, A. Pingoud, W. Wende, 1994, Biochimica et biophysica acta.

Accuracy of the EcoRV restriction endonuclease: binding and cleavage studies with oligodeoxynucleotide substrates containing degenerate recognition sequences.

J. Alves, H. Wolfes, U. Selent, 1990, Biochemistry.

Mg2+ confers DNA binding specificity to the EcoRV restriction endonuclease.

A. Pingoud, J. Alves, H. Wolfes, 1992, Biochemistry.

Engineering novel restriction endonucleases: principles and applications.

W Wende, A. Jeltsch, A. Pingoud, 1996, Trends in biotechnology.

Site-directed mutagenesis studies with EcoRV restriction endonuclease to identify regions involved in recognition and catalysis.

F. Winkler, R. Geiger, A. Pingoud, 1991, Biochemistry.