Becker-Pauly, Christoph

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Journal Article

Jefferson, Tamara; Auf dem Keller, Ulrich; Bellac, Caroline; Metz, Verena V.; Broder, Claudia; Hedrich, Jana; Ohler, Anke; Maier, Wladislaw; Magdolen, Viktor; Sterchi, Erwin-Ernst; Bond, Judith S; Jayakumar, Arumugam; Traupe, Heiko; Chalaris, Athena; Rose-John, Stefan; Pietrzik, Claus U.; Postina, Rolf; Overall, Christopher M.; Becker-Pauly, Christoph (2013). The substrate degradome of meprin metalloproteases reveals an unexpected proteolytic link between meprin β and ADAM10. Cellular and molecular life sciences, 70(2), pp. 309-333. Springer 10.1007/s00018-012-1106-2

Arolas, Joan L; Broder, Claudia; Jefferson, Tamara; Guevara, Tibisay; Sterchi, Erwin E; Bode, Wolfram; Stöcker, Walter; Becker-Pauly, Christoph; Gomis-Rüth, F Xavier (2012). Structural basis for the sheddase function of human meprin β metalloproteinase at the plasma membrane. Proceedings of the National Academy of Sciences of the United States of America - PNAS, 109(40), pp. 16131-6. Washington, D.C.: National Academy of Sciences NAS 10.1073/pnas.1211076109

Minder, Petra; Bayha, Elke; Becker-Pauly, Christoph; Sterchi, Erwin E (2012). Meprinα transactivates the epidermal growth factor receptor (EGFR) via ligand shedding, thereby enhancing colorectal cancer cell proliferation and migration. Journal of biological chemistry, 287(42), pp. 35201-11. Bethesda, Md.: American Society for Biochemistry and Molecular Biology 10.1074/jbc.M112.368910

Lottaz, Daniel; Maurer, Christoph A; Noël, Agnès; Blacher, Silvia; Huguenin, Maya; Nievergelt, Alexandra; Niggli, Verena; Kern, Alexander; Müller, Stefan; Seibold, Frank; Friess, Helmut; Becker-Pauly, Christoph; Stöcker, Walter; Sterchi, Erwin E (2011). Enhanced activity of meprin-?, a pro-migratory and pro-angiogenic protease, in colorectal cancer. PLoS ONE, 6(11), e26450. Lawrence, Kans.: Public Library of Science 10.1371/journal.pone.0026450

Ambort, Daniel; Brellier, Florence; Becker-Pauly, Christoph; Stöcker, Walter; Andrejevic-Blant, Snezana; Chiquet, Matthias; Sterchi, Erwin E (2010). Specific processing of tenascin-C by the metalloprotease meprinbeta neutralizes its inhibition of cell spreading. Matrix biology, 29(1), pp. 31-42. Amsterdam: Elsevier 10.1016/j.matbio.2009.08.007

Hedrich, Jana; Lottaz, Daniel; Meyer, Katharina; Yiallouros, Irene; Jahnen-Dechent, Willi; Stöcker, Walter; Becker-Pauly, Christoph (2010). Fetuin-A and cystatin C are endogenous inhibitors of human meprin metalloproteases. Biochemistry, 49(39), pp. 8599-607. Washington, D.C.: American Chemical Society 10.1021/bi1004238

Kronenberg, Daniel; Bruns, Bernd C; Moali, Catherine; Vadon-Le Goff, Sandrine; Sterchi, Erwin E; Traupe, Heiko; Böhm, Markus; Hulmes, David J S; Stöcker, Walter; Becker-Pauly, Christoph (2010). Processing of procollagen III by meprins: new players in extracellular matrix assembly? Journal of Investigative Dermatology, 130(12), pp. 2727-35. New York, N.Y.: Nature Publishing 10.1038/jid.2010.202

Oneda, Beatrice; Lods, Nadège; Lottaz, Daniel; Becker-Pauly, Christoph; Stöcker, Walter; Pippin, Jeffrey; Huguenin, Maya; Ambort, Daniel; Marti, Hans-Peter; Sterchi, Erwin E (2008). Metalloprotease meprin beta in rat kidney: glomerular localization and differential expression in glomerulonephritis. PLoS ONE, 3(5), e2278. Lawrence, Kans.: Public Library of Science 10.1371/journal.pone.0002278

Schütte, Andre; Lottaz, Daniel; Sterchi, Erwin E; Stöcker, Walter; Becker-Pauly, Christoph (2007). Two alpha subunits and one beta subunit of meprin zinc-endopeptidases are differentially expressed in the zebrafish Danio rerio. Biological chemistry, 388(5), pp. 523-31. Berlin: Walter de Gruyter 10.1515/BC.2007.060

Becker-Pauly, Christoph; Höwel, Markus; Walker, Tatjana; Vlad, Annica; Aufenvenne, Karin; Oji, Vinzenz; Lottaz, Daniel; Sterchi, Erwin E; Debela, Mekdes; Magdolen, Viktor; Traupe, Heiko; Stöcker, Walter (2007). The alpha and beta subunits of the metalloprotease meprin are expressed in separate layers of human epidermis, revealing different functions in keratinocyte proliferation and differentiation. Journal of Investigative Dermatology, 127(5), pp. 1115-25. New York, N.Y.: Nature Publishing 10.1038/sj.jid.5700675

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