S. Göthel

Peptidyl-prolyl cis-trans isomerases, a superfamily of ubiquitous folding catalysts

M. Marahiel, S. Göthel, M. A. Marahiel, 1999, Cellular and Molecular Life Sciences CMLS.

An internal FK506-binding domain is the catalytic core of the prolyl isomerase activity associated with the Bacillus subtilis trigger factor.

M. Marahiel, A. Wipat, C. Harwood, 1997, European journal of biochemistry.

Histidine 109 in peptidyl-prolyl cis-trans isomerase of Bacillus subtilis plays an important role in catalysis and in cyclosporin A binding.

M. Marahiel, S. Göthel, T. Achenbach, 1997, FEMS microbiology letters.

Cyclophilin and trigger factor from Bacillus subtilis catalyze in vitro protein folding and are necessary for viability under starvation conditions.

M. Marahiel, F. Schmid, S. Göthel, 1998, Biochemistry.

Peptidyl-prolyl cis-trans isomerase of Bacillus subtilis: identification of residues involved in cyclosporin A affinity and catalytic efficiency.

M. Marahiel, M. Herrler, S. Göthel, 1996, Biochemistry.

Two protein-protein interaction sites on the spliceosome-associated human cyclophilin CypH.

M. Marahiel, R. Lührmann, R. Ficner, 2003, Nucleic acids research.

The 20kD protein of human [U4/U6.U5] tri-snRNPs is a novel cyclophilin that forms a complex with the U4/U6-specific 60kD and 90kD proteins.

M. Marahiel, William Arbuthnot Sir Lane, R. Lührmann, 1998, RNA.