N. Oppenheimer

Structural basis for enzymatic evolution from a dedicated ADP-ribosyl cyclase to a multifunctional NAD Hydrolase (2009)

Liu, Q., Graeff, R., Kriksunov, I. A., Jiang, H., Zhang, B., Oppenheimer, N., ...

Novel hydrolysis-resistant analogues of cyclic ADP-ribose: modification of the "northern" ribose and calcium release activity (2002)

Guse, A. H., Cakir-Kiefer, C., Fukuoka, M., Shuto, S., Weber, K., Bailey, V. C., ...

Kinetic competence of the cADP-ribose-CD38 complex as an intermediate in the CD38/NAD+ glycohydrolase-catalysed reactions: implication for CD38 signalling.

Cakir-Kiefer, C, Muller-Steffner, H, Oppenheimer, N, Schuber, F

CD38/NAD(+) glycohydrolase is a type II transmembrane glycoprotein widely used to study T- and B-cell activation and differentiation. CD38 is endowed with two different activities: it is a signal...

Kinetic competence of the cADP-ribose-CD38 complex as an intermediate in the CD38/NAD+ glycohydrolase-catalysed reactions: implication for CD38 signalling.

Cakir-Kiefer, C, Muller-Steffner, H, Oppenheimer, N, Schuber, F

CD38/NAD(+) glycohydrolase is a type II transmembrane glycoprotein widely used to study T- and B-cell activation and differentiation. CD38 is endowed with two different activities: it is a signal...