Jens Rahfeld

Crystal structure of Mip, a prolylisomerase from Legionella pneumophila.

Alan Riboldi‐Tunnicliffe, Bettina König, S. M. Jessen et al. · Nature Structural Biology · 2001 · 108 citations

Crystal Structure, Protein X-ray Crystallography, Molecular Biology +3

NMR solution structure of h Par14 reveals similarity to the peptidyl prolyl cis/trans isomerase domain of the mitotic regulator h Pin1 but indicates a different functionality of the protein 1 1Edited by A. Fersht

Elena Sekerina, Jens Rahfeld, Jonathan Müller et al. · Journal of Molecular Biology · 2000 · 65 citations

Nmr Solution Structure, Protein Function, Biochemistry +8

Catalysis of protein folding by parvulin 1 1Edited by P. E. Wright

Christian Schölz, Jens Rahfeld, Gunter Fischer et al. · Journal of Molecular Biology · 1997 · 56 citations

Protein Chemistry, Biochemistry, Protein Assembly +8

Characterization of Mip proteins of<i>Legionella pneumophila</i>

Birgit Ludwig, Jens Rahfeld, Bettina Schmidt et al. · FEMS Microbiology Letters · 1994 · 45 citations · Full text

Mature Mip, Medicine, Mip Genes +14

A maize FK506-sensitive immunophilin, mzFKBP-66, is a peptidylproline cis - trans -isomerase that interacts with calmodulin and a 36-kDa cytoplasmic protein

Gregorio Hueros, Jens Rahfeld, Francesco Salamini et al. · Planta · 1998 · 38 citations

Plant Molecular Biology, Maize Fk506-sensitive Immunophilin, Protein Expression +11