P. Mackeldanz

发表

Overexpression and affinity chromatography purification of the Type III restriction endonuclease EcoP15I for use in transcriptome analysis.

D. Krüger, E. Möncke-Buchner, M. Reuter, 2004, Journal of Biotechnology.

A single mutation of restriction endonuclease EcoRII led to a new crystal form that diffracts to 2.1 A resolution.

D. Krüger, Liqing Chen, Xiaoyin Zhou, 2003, Acta crystallographica. Section D, Biological crystallography.

Safety, reactogenicity, and immunogenicity of homologous and heterologous prime-boost immunisation with ChAdOx1 nCoV-19 and BNT162b2: a prospective cohort study

C. von Kalle, N. Suttorp, D. Treue, 2021, The Lancet Respiratory Medicine.

Regions of Endonuclease EcoRII Involved in DNA Target Recognition Identified by Membrane-bound Peptide Repertoires*

J. Schneider-Mergener, D. Krüger, M. Reuter, 1999, The Journal of Biological Chemistry.

Type III restriction endonuclease EcoP15I is a heterotrimeric complex containing one Res subunit with several DNA-binding regions and ATPase activity

D. Krüger, J. Alves, M. Schutkowski, 2011, Nucleic acids research.

Type III restriction endonucleases translocate DNA in a reaction driven by recognition site‐specific ATP hydrolysis.

T. Bickle, D. Krüger, C. Schroeder, 1995, The EMBO journal.

Molecular analysis of restriction endonuclease EcoRII from Escherichia coli reveals precise regulation of its enzymatic activity by autoinhibition

D. Krüger, M. Szczepek, J. Alves, 2009, Molecular microbiology.

Functional consequences of mutating conserved SF2 helicase motifs in the Type III restriction endonuclease EcoP15I translocase domain.

D. Krüger, J. Alves, E. Möncke-Buchner, 2013, Biochimie.

Imaging DNA loops induced by restriction endonuclease EcoRII. A single amino acid substitution uncouples target recognition from cooperative DNA interaction and cleavage.

D. Krüger, J. Behlke, R. Lurz, 2000, The Journal of biological chemistry.

Hyperexpressed EcoRII renatured from inclusion bodies and native enzyme both exhibit essential cooperativity with two DNA sites.

D. Krüger, M. Reuter, C. Schroeder, 1995, Protein expression and purification.

Reactogenicity of homologous and heterologous prime-boost immunization with BNT162b2 and ChAdOx1-nCoV19: a prospective cohort study

N. Suttorp, D. Treue, V. Corman, 2021, medRxiv.

Structural domains in the type III restriction endonuclease EcoP15I: characterization by limited proteolysis, mass spectrometry and insertional mutagenesis.

D. Krüger, M. Reuter, M. Linscheid, 2007, Journal of molecular biology.