Pennybacker, M., Schuette, C. G., Liessem, B., Hepbildikler, S. T., Kopetka, J. A., Ellis, M. R., Myerowitz, R., Sandhoff, K., Proia, R. L. (1997) J. Biol. Chem. 272, 8002-6
Evidence for the involvement of Glu-355 in the catalytic action of human beta-hexosaminidase B.

Schuette, C. G., Lemm, T., Glombitza, G. J., Sandhoff, K. (1998) Protein Sci. 7,1039-45
Complete localization of disulfide bonds in GM2 activator protein.

Schuette, C. G., Doering, T., Kolter, T., Sandhoff, K. (1999) Biol. Chem. 380, 759-766
The glycosphingolipidoses - from disease to basic principles of metabolism.

Schuette, C. G., Doering, T., Kolter, T., Sandhoff, K. (1999) Biospektrum 5, 365-370
Die Glykosphingolipidosen - Von Krankheiten zu Prinzipien des Stoffwechsels.

Schuette, C. G., Weisgerber, J., Sandhoff, K. (2001) Glycobiology 11, 549-56
Complete analysis of the glycosylation and disulfide bond pattern of human beta-hexosaminidase B by MALDI-MS

Schuette, C. G., Pierstorff, B., Huettler, S., Sandhoff, K. (2001) Glycobiology 11, 81R-90R
Sphingolipid activator proteins: proteins with complex functions in lipid degradation and skin biogenesis.

Werth, N., Schuette, C. G., Wilkening, G., Lemm, T., Sandhoff, K. (2001) J. Biol. Chem. 276, 12685-90
Degradation of membrane-bound ganglioside GM2 by beta-hexosaminidase A. Stimulation by GM2 activator protein and lysosomal lipids.

Fasshauer, D., Schuette, C. G., Jahn, R. (2001) B.I.F. Futura 16, 13-23
Mechanisms of Membrane Fusion.

Lansmann, S., Schuette, C. G., Bartelsen, O., Hoernschemeyer, J., Linke, T., Weisgerber, J., Sandhoff, K. (2003) Eur. J. Biochem. 270,1076-88
Human acid sphingomyelinase.

Maier, T., Strater, N., Schuette, C. G., Klingenstein, R., Sandhoff, K., Saenger, W. (2003) J. Mol. Biol. 328, 669-81
The X-ray Crystal Structure of Human beta-Hexosaminidase B Provides Insights into Sandhoff Disease.

Schuette, C. G., Hatsuzawa, K., Margittai, M., Stein, A., Riedel, D., Kuster, P., Konig, M., Seidel, C., Jahn, R. (2004) Proc. Natl. Acad. Sci. USA 101, 2858-63
Determinants of liposome fusion mediated by synaptic SNARE proteins.

Bacia, K., Schuette C.G., Kahya, N., Jahn, R., Schwille P. (2004) J. Biol. Chem. 279, 37951-55
SNAREs prefer liquid-disordered over "raft"-(liquid-ordered) domains when reconstituted into Giant Unilamellar Vesicles.

Holt, M., Riedel, D., Stein, A., Schuette, C., Jahn, R. (2008) Curr. Biol. 18, 715-722.
Synaptic vesicles are constitutively active fusion machines that function independently of Ca2+.