R. A. Fabianek

Structure of CcmG/DsbE at 1.14 A resolution: high-fidelity reducing activity in an indiscriminately oxidizing environment.

M. A. Edeling, L. Guddat, R. A. Fabianek, 2002, Structure.

Periplasmic protein thiol:disulfide oxidoreductases of Escherichia coli.

R. A. Fabianek, H. Hennecke, L. Thöny‐meyer, 2000, FEMS microbiology reviews.

Characterization of the Escherichia coli CcmH protein reveals new insights into the redox pathway required for cytochrome c maturation

R. A. Fabianek, T. Hofer, L. Thöny‐meyer, 1999, Archives of Microbiology.

Crystallization and preliminary diffraction studies of native and selenomethionine CcmG (CycY, DsbE).

M. A. Edeling, L. Guddat, R. A. Fabianek, 2001, Acta crystallographica. Section D, Biological crystallography.

Characterization of the Bradyrhizobium japonicum CycY Protein, a Membrane-anchored Periplasmic Thioredoxin That May Play a Role as a Reductant in the Biogenesis of c-Type Cytochromes*

R. Glockshuber, R. A. Fabianek, H. Hennecke, 1997, The Journal of Biological Chemistry.

The Active-Site Cysteines of the Periplasmic Thioredoxin-Like Protein CcmG of Escherichia coli Are Important but Not Essential for Cytochrome c Maturation In Vivo

R. A. Fabianek, H. Hennecke, L. Thöny‐meyer, 1998, Journal of bacteriology.

Heme transfer to the heme chaperone CcmE during cytochrome c maturation requires the CcmC protein, which may function independently of the ABC-transporter CcmAB.

R. A. Fabianek, H. Hennecke, H. Schulz, 1999, Proceedings of the National Academy of Sciences of the United States of America.