Bernd Mayer

Tetrahydrobiopterin-dependent formation of endothelium-derived relaxing factor (nitric oxide) in aortic endothelial cells.

E. Werner, B. Mayer, H. Wachter, 1992, The Biochemical journal.

Multiple catalytic functions of brain nitric oxide synthase. Biochemical characterization, cofactor-requirement, and the role of N omega-hydroxy-L-arginine as an intermediate.

P. Klatt, B. Mayer, G. Uray, 1993, The Journal of biological chemistry.

Biosynthesis of endothelium-derived relaxing factor: a cytosolic enzyme in porcine aortic endothelial cells Ca2+-dependently converts L-arginine into an activator of soluble guanylyl cyclase.

B. Mayer, E. Böhme, K. Schmidt, 1989, Biochemical and biophysical research communications.

Ca2+/calmodulin-dependent cytochrome c reductase activity of brain nitric oxide synthase.

P. Klatt, B. Mayer, M. John, 1992, The Journal of biological chemistry.

Activation of soluble guanylyl cyclase by the nitrovasodilator 3-morpholinosydnonimine involves formation of S-nitrosoglutathione.

B. Mayer, A. Schrammel, D. Koesling, 1998, Molecular pharmacology.

Purification of soluble guanylyl cyclase from bovine lung by a new immunoaffinity chromatographic method.

G. Schultz, B. Mayer, E. Böhme, 1990, European journal of biochemistry.

Determination of nitric oxide synthase cofactors: heme, FAD, FMN, and tetrahydrobiopterin.

E. Werner, P. Klatt, B. Mayer, 1996, Methods in enzymology.