S. Kuppig

A high-molecular-weight complex of membrane proteins BAP29/BAP31 is involved in the retention of membrane-bound IgD in the endoplasmic reticulum

H. Hauri, M. Reth, W. Schamel, 2003, Proceedings of the National Academy of Sciences of the United States of America.

SHIP Down-Regulates FcεR1-Induced Degranulation at Supraoptimal IgE or Antigen Levels

M. Huber, G. Krystal, Kerstin Gimborn, 2005, The Journal of Immunology.

A leucine zipper in the N terminus confers membrane association to SLP-65

M. Reth, H. Jumaa, Y. Kulathu, 2005, Nature Immunology.

Cre recombinase‐controlled expression of the mb‐1 allele

M. Reth, E. Hobeika, R. Pelanda, 2002, Genesis.

The SH2-domain of SHIP1 interacts with the SHIP1 C-terminus: impact on SHIP1/Ig-α interaction.

Rileen Sinha, R. Backofen, M. Huber, 2012, Biochimica et biophysica acta.

Activation Sites in Nickel-Specific Human T Cell to TCR / MHC Contact 2 + and Delivery of Ni Metal-Protein Complex-Mediated Transport Weltzien

B. Zimmermann, F. Herberg, H. Weltzien, 2004 .

Uncleaved BAP31 in Association with A4 Protein at the Endoplasmic Reticulum Is an Inhibitor of Fas-initiated Release of Cytochromec from Mitochondria*

P. Clemons, G. Shore, Bing Wang, 2003, The Journal of Biological Chemistry.

The procaspase-8 isoform, procaspase-8L, recruited to the BAP31 complex at the endoplasmic reticulum

M. Nguyen, M. Reth, G. Shore, 2002, Proceedings of the National Academy of Sciences of the United States of America.

SHIP down-regulates FcepsilonR1-induced degranulation at supraoptimal IgE or antigen levels.

M. Huber, G. Krystal, Kerstin Gimborn, 2005, Journal of immunology.

Metal-Protein Complex-Mediated Transport and Delivery of Ni2+ to TCR/MHC Contact Sites in Nickel-Specific Human T Cell Activation1

Friedrich Herberg, Bastian Zimmermann, Stephan Kuppig, 2004, The Journal of Immunology.