Publications of Stephan Kuppig

Mukherjee, O.; Weingarten, L.; Padberg, I.; Pracht, C.; Sinha, R.; Hochdörfer, T.; Kuppig, S.; Backofen, R.; Reth, M.; Huber, M.: The SH2-domain of SHIP1 interacts with the SHIP1 C-terminus: Impact on SHIP1/Ig-α interaction. Biochimica et Biophysica Acta 1823, pp. 206 - 214 (2012)

Mukherjee, O.; Weingarten, L.; Padberg, I.; Pracht, C.; Sinha, R.; Hochdörfer, T.; Kuppig, S.; Backofen, R.; Reth, M.; Huber, M.: The SH2-comain of SHIP1 interacts with the SHIP1 C-terminus: Impact on SHIP1/Ig-α interaction. Biochimica et Biophysica Acta 1823, pp. 206 - 214 (2011)

Köhler, F.; Storch, B.; Kulathu, Y.; Herzog, S.; Kuppig, S.; Reth, M.; Jumaa, H.: A leucine zipper in the N terminus confers membrane association to SLP-65. Nature Immunology 6, pp. 204 - 210 (2005)

Gimborn, K.; Lessmann, E.; Kuppig, S.; Krystal, G.; Huber, M.: SHIP Down-Regulates FcεR-1-Induced Degranulation at Supraoptimal IgE or Antigen Levels. The Journal of Immunology 174, pp. 507 - 516 (2005)

Thierse, H.-J.; Moulon, C.; Allespach, Y.; Zimmermann, B.; Doetze, A.; Kuppig, S.; Wild, D.; Herberg, F.; Weltzien, H.-U.: Metal-Protein Complex-Mediated Transport and Delivery of Ni²⁺ to TCR/MHC Contact Sites in Nickel-Specific Human T Cell Activation. The Journal of Immunology 172, pp. 1926 - 1934 (2004)

Schamel, W. W. A.; Kuppig, S.; Becker, B.; Gimborn, K.; Hauri, H.-P.; Reth, M.: A high-molecular-weight complex of membrane proteins BAP29/BAP31 is involved in the retention of membrane-bound IgD in the endoplasmic reticulum. Proceedings of the National Academy of Sciences of the United States of America 100 (17), pp. 9861 - 9866 (2003)

Wang, B.; Nguyen, M.; Breckenridge, D. G.; Stojanovic, M.; Clemons, P. A.; Kuppig, S.; Shore, G. C.: Uncleaved BAP31 in Association with A4 Protein at the Endoplasmic Reticulum is an Inhibitor of Fas-initiated Release of Cytochrome c from Mitochondria. Journal of Biological Chemistry 278 (16), pp. 14461 - 14468 (2003)

Breckenridge, D. G.; Nguyen, M.; Kuppig, S.; Reth, M.; Shore, G. C.: The procaspase-8 isoform, procaspase-8L, recruited to the BAP31 complex at the endoplasmic reticulum. Proceedings of the National Academy of Sciences of the United States of America 99 (7), pp. 4331 - 4336 (2002)

Pelanda, R.; Hobeika, E.; Kurokawa, T.; Zhang, Y.; Kuppig, S.; Reth, M.: Cre Recombinase-Controlled Expression of the mb-1 Allele. Genesis 32 (2 Sp. Iss. SI), pp. 154 - 157 (2002)