iRhoms 1 and 2 are essential upstream regulators of ADAM17-dependent EGFR signaling von Li, Xue, Maretzky, Thorsten, Weskamp, Gisela, Monette, Sébastien, Qing, Xiaoping, Issuree, Priya Darshinee A., Crawford, Howard C., McIlwain, David R., Mak, Tak W., Salmon, Jane E., Blobel, Carl P.

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The Disintegrin/Metalloproteinase ADAM10 Is Essential for the Establishment of the Brain Cortex von Jorissen, Ellen, Prox, Johannes, Bernreuther, Christian, Weber, Silvio, Schwanbeck, Ralf, Serneels, Lutgarde, Snellinx, An, Craessaerts, Katleen, Thathiah, Amantha, Tesseur, Ina, Bartsch, Udo, Weskamp, Gisela, Blobel, Carl P, Glatzel, Markus, De Strooper, Bart, Saftig, Paul

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Structural modeling defines transmembrane residues in ADAM17 that are crucial for Rhbdf2-ADAM17-dependent proteolysis von Li, Xue, Maretzky, Thorsten, Perez-Aguilar, Jose Manuel, Monette, Sébastien, Weskamp, Gisela, Le Gall, Sylvain, Beutler, Bruce, Weinstein, Harel, Blobel, Carl P

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Distinct Roles for ADAM10 and ADAM17 in Ectodomain Shedding of Six EGFR Ligands von Sahin, Umut, Weskamp, Gisela, Kelly, Kristine, Zhou, Hong-Ming, Higashiyama, Shigeki, Peschon, Jacques, Hartmann, Dieter, Saftig, Paul, Blobel, Carl P.

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VEGF-A Stimulates ADAM17-Dependent Shedding of VEGFR2 and Crosstalk Between VEGFR2 and ERK Signaling von Swendeman, Steven, Mendelson, Karen, Weskamp, Gisela, Horiuchi, Keisuke, Deutsch, Urban, Scherle, Peggy, Hooper, Andrea, Rafii, Shahin, Blobel, Carl P

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Characterization of the catalytic properties of the membrane-anchored metalloproteinase ADAM9 in cell-based assays von Maretzky, Thorsten, Swendeman, Steven, Mogollon, Elin, Weskamp, Gisela, Sahin, Umut, Reiss, Karina, Blobel, Carl P

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Role of iRhoms 1 and 2 in Endochondral Ossification von Fang, Renpeng, Haxaire, Coline, Otero, Miguel, Lessard, Samantha, Weskamp, Gisela, McIlwain, David R, Mak, Tak W, Lichtenthaler, Stefan F, Blobel, Carl P

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ADAM10 is a principal 'sheddase' of the low-affinity immunoglobulin E receptor CD23 von Weskamp, Gisela, Ford, Jill W, Sturgill, Jamie, Martin, Steve, Docherty, Andrew J P, Swendeman, Steven, Broadway, Neil, Hartmann, Dieter, Saftig, Paul, Umland, Shelby, Sehara-Fujisawa, Atsuko, Black, Roy A, Ludwig, Andreas, Becherer, J David, Conrad, Daniel H, Blobel, Carl P

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ADAM8 is a negative regulator of retinal neovascularization and of the growth of heterotopically injected tumor cells in mice von Guaiquil, Victor H., Swendeman, Steven, Zhou, Wenhui, Guaiquil, Patricio, Weskamp, Gisela, Bartsch, Jörg W., Blobel, Carl P.

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Mice Lacking the Metalloprotease-Disintegrin MDC9 (ADAM9) Have No Evident Major Abnormalities during Development or Adult Life von Weskamp, Gisela, Cai, Hui, Brodie, Thomas A., Higashyama, Shigeki, Manova, Katia, Ludwig, Thomas, Blobel, Carl P.

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Potential Role for ADAM15 in Pathological Neovascularization in Mice von Horiuchi, Keisuke, Weskamp, Gisela, Lum, Lawrence, Hammes, Hans-Peter, Cai, Hui, Brodie, Thomas A., Ludwig, Thomas, Chiusaroli, Riccardo, Baron, Roland, Preissner, Klaus T., Manova, Katia, Blobel, Carl P.

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Essential Role for ADAM19 in Cardiovascular Morphogenesis von Zhou, Hong-Ming, Weskamp, Gisela, Chesneau, Valérie, Sahin, Umut, Vortkamp, Andrea, Horiuchi, Keisuke, Chiusaroli, Riccardo, Hahn, Rebecca, Wilkes, David, Fisher, Peter, Baron, Roland, Manova, Katia, Basson, Craig T., Hempstead, Barbara, Blobel, Carl P.

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Metalloprotease-Disintegrin MDC9: Intracellular Maturation and Catalytic Activity von Roghani, Monireh, Becherer, J. David, Moss, Marcia L., Atherton, Ruth E., Erdjument-Bromage, Hediye, Arribas, Joaquin, Blackburn, R. Kevin, Weskamp, Gisela, Tempst, Paul, Blobel, Carl P.

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Analysis of the function of ADAM17 in iRhom2 curly-bare and tylosis with esophageal cancer mutant mice von Rabinowitsch, Ariana I, Maretzky, Thorsten, Weskamp, Gisela, Haxaire, Coline, Tueshaus, Johanna, Lichtenthaler, Stefan F, Monette, Sébastien, Blobel, Carl P

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ADAM10-Dependent Signaling Through Notch1 and Notch4 Controls Development of Organ-Specific Vascular Beds von Alabi, Rolake O, Glomski, Krzysztof, Haxaire, Coline, Weskamp, Gisela, Monette, Sébastien, Blobel, Carl P

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ADAM17 stabilizes its interacting partner inactive Rhomboid 2 (iRhom2) but not inactive Rhomboid 1 (iRhom1) von Weskamp, Gisela, Tüshaus, Johanna, Li, Daniel, Feederle, Regina, Maretzky, Thorsten, Swendemann, Steven, Falck-Pedersen, Erik, McIlwain, David R., Mak, Tak W., Salmon, Jane E., Lichtenthaler, Stefan F., Blobel, Carl P.

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Pathological Neovascularization Is Reduced by Inactivation of ADAM17 in Endothelial Cells but Not in Pericytes von Weskamp, Gisela, Mendelson, Karen, Swendeman, Steve, Le Gall, Sylvain, Ma, Yan, Lyman, Stephen, Hinoki, Akinari, Eguchi, Satoru, Guaiquil, Victor, Horiuchi, Keisuke, Blobel, Carl P

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Targeted truncation of the ADAM17 cytoplasmic domain in mice results in protein destabilization and a hypomorphic phenotype von Lora, Jose, Weskamp, Gisela, Li, Thomas M., Maretzky, Thorsten, Shola, Dorjee T.N., Monette, Sébastien, Lichtenthaler, Stefan F., Lu, Theresa T., Yang, Chingwen, Blobel, Carl P.

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Characterization of the Catalytic Properties of the Membrane-anchored Metalloprotease ADAM9 in Cell-based assays von Maretzky, Thorsten, Swendeman, Steven, Mogollon, Elin, Weskamp, Gisela, Sahin, Umut, Reiss, Karina, Blobel, Carl P.

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Intravitreal injection of TIMP3 or the EGFR inhibitor erlotinib offers protection from oxygen-induced retinopathy in mice von Hewing, Nina Jasmin, Weskamp, Gisela, Vermaat, Joost, Farage, Eric, Glomski, Krzysztof, Swendeman, Steven, Chan, Robison Vernon Paul, Chiang, Michael F, Khokha, Rama, Anand-Apte, Bela, Blobel, Carl Peter

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