ADAM17: a molecular switch to control inflammation and tissue regeneration

An Essential Role for Ectodomain Shedding in Mammalian Development

Peschon, J. J., Slack, J. L., Reddy, P., Stocking, K. L., Sunnarborg, S. W., Lee, D. C., Russell, W. E., Castner, B. J., Johnson, R. S., Fitzner, J. N., et al. (1998) · Science · doi:10.1126/science.282.5392.1281 · Cited by 1,607

A brief history of TH17, the first major revision in the TH1/TH2 hypothesis of T cell–mediated tissue damage

Steinman, L. (2007) · Nature Medicine · doi:10.1038/nm1551 · Cited by 1,376

The ADAM metalloproteinases

EDWARDS, D., HANDSLEY, M., & PENNINGTON, C. (2008) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2008.08.001 · Cited by 1,161

Regulatory T cells exert checks and balances on self tolerance and autoimmunity

Wing, K., & Sakaguchi, S. (2010) · Nature Immunology · doi:10.1038/ni.1818 · Cited by 1,107

ADAMs: key components in EGFR signalling and development

Blobel, C. P. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1548 · Cited by 1,090

Nuclear signalling by tumour-associated antigen EpCAM

Maetzel, D., Denzel, S., Mack, B., Canis, M., Went, P., Benk, M., Kieu, C., Papior, P., Baeuerle, P. A., Munz, M., et al. (2009) · Nature Cell Biology · doi:10.1038/ncb1824 · Cited by 719

Protection against a lethal dose of endotoxin by an inhibitor of tumour necrosis factor processing

Mohler, K. M., Sleath, P. R., Fitzner, J. N., Cerretti, D. P., Alderson, M., Kerwar, S. S., Torranee, D. S., Otten-Evans, C., Greenstreet, T., Weerawarna, K., et al. (1994) · Nature · doi:10.1038/370218a0 · Cited by 588

Functional Analysis of the Domain Structure of Tumor Necrosis Factor-α Converting Enzyme

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Evidence for a Role of a Tumor Necrosis Factor-α (TNF-α)-converting Enzyme-like Protease in Shedding of TRANCE, a TNF Family Member Involved in Osteoclastogenesis and Dendritic Cell Survival

Lum, L., Wong, B. R., Josien, R., Becherer, J. D., Erdjument-Bromage, H., Schlöndorff, J., Tempst, P., Choi, Y., & Blobel, C. P. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.19.13613 · Cited by 410

Cellular Cholesterol Depletion Triggers Shedding of the Human Interleukin-6 Receptor by ADAM10 and ADAM17 (TACE)

Matthews, V., Schuster, B., Schütze, S., Bussmeyer, I., Ludwig, A., Hundhausen, C., Sadowski, T., Saftig, P., Hartmann, D., Kallen, K.-J., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210584200 · Cited by 390

Role of cytokines in rheumatoid arthritis: an education in pathophysiology and therapeutics

Feldmann, M., & Maini, S. R. N. (2008) · Immunological Reviews · doi:10.1111/j.1600-065x.2008.00626.x · Cited by 381

ADAM-17: the enzyme that does it all

Gooz, M. (2010) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409231003628015 · Cited by 377

The IL-6/sIL-6R complex as a novel target for therapeutic approaches

Rose-John, S., Waetzig, G. H., Scheller, J., Grötzinger, J., & Seegert, D. (2007) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.11.5.613 · Cited by 360

Apoptosis is a natural stimulus of IL6R shedding and contributes to the proinflammatory trans-signaling function of neutrophils

Chalaris, A., Rabe, B., Paliga, K., Lange, H., Laskay, T., Fielding, C. A., Jones, S. A., Rose-John, S., & Scheller, J. (2007) · Blood · doi:10.1182/blood-2007-01-067918 · Cited by 329

Cutting Edge: TNF-α-Converting Enzyme (TACE/ADAM17) Inactivation in Mouse Myeloid Cells Prevents Lethality from Endotoxin Shock

Horiuchi, K., Kimura, T., Miyamoto, T., Takaishi, H., Okada, Y., Toyama, Y., & Blobel, C. P. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.179.5.2686 · Cited by 301

Design of effective immunotherapy for human autoimmunity

Feldmann, M., & Steinman, L. (2005) · Nature · doi:10.1038/nature03727 · Cited by 277

The soluble human IL-6 receptor. Mutational characterization of the proteolytic cleavage site.

Müllberg, J., Oberthür, W., Lottspeich, F., Mehl, E., Dittrich, E., Graeve, L., Heinrich, P. C., & Rose-John, S. (1994) · The Journal of Immunology · doi:10.4049/jimmunol.152.10.4958 · Cited by 269

Critical role of the disintegrin metalloprotease ADAM17 for intestinal inflammation and regeneration in mice

Chalaris, A., Adam, N., Sina, C., Rosenstiel, P., Lehmann-Koch, J., Schirmacher, P., Hartmann, D., Cichy, J., Gavrilova, O., Schreiber, S., et al. (2010) · Journal of Experimental Medicine · doi:10.1084/jem.20092366 · Cited by 269

Direct Activation of TACE-Mediated Ectodomain Shedding by p38 MAP Kinase Regulates EGF Receptor-Dependent Cell Proliferation

Xu, P., & Derynck, R. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.01.034 · Cited by 257

Targeting TACE-dependent EGFR ligand shedding in breast cancer

Kenny, P. A., & Bissell, M. J. (2007) · Journal of Clinical Investigation · doi:10.1172/jci29518 · Cited by 252

ADAMs 10 and 17 Represent Differentially Regulated Components of a General Shedding Machinery for Membrane Proteins Such as Transforming Growth Factor α, L-Selectin, and Tumor Necrosis Factor α

Le Gall, S. M., Bobé, P., Reiss, K., Horiuchi, K., Niu, X.-D., Lundell, D., Gibb, D. R., Conrad, D., Saftig, P., & Blobel, C. P. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-11-1135 · Cited by 250

ERK-mediated phosphorylation of Thr735 in TNFα-converting enzyme and its potential role in TACE protein trafficking

Soond, S. M., Everson, B., Riches, D. W. H., & Murphy, G. (2005) · Journal of Cell Science · doi:10.1242/jcs.02357 · Cited by 234

L-selectin: mechanisms and physiological significance of ectodomain cleavage

Smalley, D. M., & Ley, K. (2005) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2005.tb00354.x · Cited by 233

Cutting Edge: Trans- Signaling via the Soluble IL-6R Abrogates the Induction of FoxP3 in Naive CD4+CD25− T Cells

Dominitzki, S., Fantini, M. C., Neufert, C., Nikolaev, A., Galle, P. R., Scheller, J., Monteleone, G., Rose-John, S., Neurath, M. F., & Becker, C. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.179.4.2041 · Cited by 227

Tumor Necrosis Factor-α–Converting Enzyme (ADAM17) Mediates GPIbα Shedding From Platelets In Vitro and In Vivo

Bergmeier, W., Piffath, C. L., Cheng, G., Dole, V. S., Zhang, Y., von Andrian, U. H., & Wagner, D. D. (2004) · Circulation Research · doi:10.1161/01.res.0000143899.73453.11 · Cited by 226

Therapeutic Targeting of IL-6 Trans Signaling Counteracts STAT3 Control of Experimental Inflammatory Arthritis

Nowell, M. A., Williams, A. S., Carty, S. A., Scheller, J., Hayes, A. J., Jones, G. W., Richards, P. J., Slinn, S., Ernst, M., Jenkins, B. J., et al. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.182.1.613 · Cited by 215

Tumor necrosis factor α-converting enzyme (TACE/ADAM17) mediates ectodomain shedding of the scavenger receptor CD163

Etzerodt, A., Maniecki, M. B., Møller, K., Møller, H. J., & Moestrup, S. K. (2010) · Journal of Leukocyte Biology · doi:10.1189/jlb.0410235 · Cited by 211

Species Specificity of ADAM10 and ADAM17 Proteins in Interleukin-6 (IL-6) Trans-signaling and Novel Role of ADAM10 in Inducible IL-6 Receptor Shedding

Garbers, C., Jänner, N., Chalaris, A., Moss, M. L., Floss, D. M., Meyer, D., Koch-Nolte, F., Rose-John, S., & Scheller, J. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.229393 · Cited by 201

Drug Insight: tumor necrosis factor-converting enzyme as a pharmaceutical target for rheumatoid arthritis

Moss, M. L., Sklair-Tavron, L., & Nudelman, R. (2008) · Nature Clinical Practice Rheumatology · doi:10.1038/ncprheum0797 · Cited by 198

IL-6 Trans-Signaling in Formation and Progression of Malignant Ascites in Ovarian Cancer

Lo, C.-W., Chen, M.-W., Hsiao, M., Wang, S., Chen, C.-A., Hsiao, S.-M., Chang, J.-S., Lai, T.-C., Rose-John, S., Kuo, M.-L., et al. (2011) · Cancer Research · doi:10.1158/0008-5472.can-10-1496 · Cited by 193

Loss of CD4+ T Cell IL-6R Expression during Inflammation Underlines a Role for IL-6 Trans Signaling in the Local Maintenance of Th17 Cells

Jones, G. W., McLoughlin, R. M., Hammond, V. J., Parker, C. R., Williams, J. D., Malhotra, R., Scheller, J., Williams, A. S., Rose-John, S., Topley, N., et al. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.0901528 · Cited by 189

Active-site determinants of substrate recognition by the metalloproteinases TACE and ADAM10

Caescu, C. I., Jeschke, G. R., & Turk, B. E. (2009) · Biochemical Journal · doi:10.1042/bj20090549 · Cited by 179

Regulated release and functional modulation of junctional adhesion molecule A by disintegrin metalloproteinases

Koenen, R. R., Pruessmeyer, J., Soehnlein, O., Fraemohs, L., Zernecke, A., Schwarz, N., Reiss, K., Sarabi, A., Lindbom, L., Hackeng, T. M., et al. (2009) · Blood · doi:10.1182/blood-2008-04-152330 · Cited by 175

Deciphering the human platelet sheddome

Fong, K. P., Barry, C., Tran, A. N., Traxler, E. A., Wannemacher, K. M., Tang, H.-Y., Speicher, K. D., Blair, I. A., Speicher, D. W., Grosser, T., et al. (2011) · Blood · doi:10.1182/blood-2010-05-283838 · Cited by 172

ADAM17 as a Therapeutic Target in Multiple Diseases

Arribas, J., & Esselens, C. (2009) · Current Pharmaceutical Design · doi:10.2174/138161209788682398 · Cited by 171

Cutting Edge: Soluble IL-6R Is Produced by IL-6R Ectodomain Shedding in Activated CD4 T Cells

Briso, E. M., Dienz, O., & Rincon, M. (2008) · The Journal of Immunology · doi:10.4049/jimmunol.180.11.7102 · Cited by 165

Thiol isomerases negatively regulate the cellular shedding activity of ADAM17

Willems, S. H., Tape, C. J., Stanley, P. L., Taylor, N. A., Mills, I. G., Neal, D. E., McCafferty, J., & Murphy, G. (2010) · Biochemical Journal · doi:10.1042/bj20100179 · Cited by 165

A Disintegrin and Metalloproteinase 17 (ADAM17) Mediates Inflammation-induced Shedding of Syndecan-1 and -4 by Lung Epithelial Cells

Pruessmeyer, J., Martin, C., Hess, F. M., Schwarz, N., Schmidt, S., Kogel, T., Hoettecke, N., Schmidt, B., Sechi, A., Uhlig, S., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.059394 · Cited by 164

VEGF-A Stimulates ADAM17-Dependent Shedding of VEGFR2 and Crosstalk Between VEGFR2 and ERK Signaling

Swendeman, S., Mendelson, K., Weskamp, G., Horiuchi, K., Deutsch, U., Scherle, P., Hooper, A., Rafii, S., & Blobel, C. P. (2008) · Circulation Research · doi:10.1161/circresaha.108.184416 · Cited by 164

Role of ADAM17 in the ectodomain shedding of TNF-α and its receptors by neutrophils and macrophages

Bell, J. H., Herrera, A. H., Li, Y., & Walcheck, B. (2007) · Journal of Leukocyte Biology · doi:10.1189/jlb.0307193 · Cited by 162

The shedding activity of ADAM17 is sequestered in lipid rafts

Tellier, E., Canault, M., Rebsomen, L., Bonardo, B., Juhan-Vague, I., Nalbone, G., & Peiretti, F. (2006) · Experimental Cell Research · doi:10.1016/j.yexcr.2006.08.027 · Cited by 155

Leukocyte Migration Is Regulated by L-Selectin Endoproteolytic Release

Venturi, G. M., Tu, L., Kadono, T., Khan, A. I., Fujimoto, Y., Oshel, P. E., Bock, C. B., Miller, A. S., Albrecht, R. M., Kubes, P., et al. (2003) · Immunity · doi:10.1016/s1074-7613(03)00295-4 · Cited by 155

The ADAM10 Prodomain Is a Specific Inhibitor of ADAM10 Proteolytic Activity and Inhibits Cellular Shedding Events

Moss, M. L., Bomar, M. G., Liu, Q., Sage, H. J., Dempsey, P. J., Lenhart, P., Gillispie, P. A., Stoeck, A., Wildeboer, D., Bartsch, J. W., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m703231200 · Cited by 149

Pathological Neovascularization Is Reduced by Inactivation of ADAM17 in Endothelial Cells but Not in Pericytes

Weskamp, G., Mendelson, K., Swendeman, S. L., Gall, S. M. L., Ma, Y., Lyman, S. L., Hinoki, A., Eguchi, S., Guaiquil, V. H., Horiuchi, K., et al. (2010) · Circulation Research · doi:10.1161/circresaha.109.207415 · Cited by 147

Cutting Edge: The Metalloproteinase ADAM17/TNF-α-Converting Enzyme Regulates Proteolytic Shedding of the MHC Class I-Related Chain B Protein

Boutet, P., Agüera‐González, S., Atkinson, S. J., Pennington, C. J., Edwards, D. R., Murphy, G., Reyburn, H. T., & Valés‐Gómez, M. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.182.1.49 · Cited by 146

MyD88 signaling in nonhematopoietic cells protects mice against induced colitis by regulating specific EGF receptor ligands

Brandl, K., Sun, L., Neppl, C., Siggs, O. M., Gall, S. M. L., Tomisato, W., Li, X., Du, X., Männel, D. N., Blobel, C., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1014669107 · Cited by 145

Regulation of Mature ADAM17 by Redox Agents for L-Selectin Shedding

Wang, Y., Herrera, A. H., Li, Y., Belani, K., & Walcheck, B. K. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0802770 · Cited by 136

HER2 Phosphorylation Is Maintained by a PKB Negative Feedback Loop in Response to Anti-HER2 Herceptin in Breast Cancer

Gijsen, M., King, P., Perera, T., Parker, P. J., Harris, A. L., Larijani, B., & Kong, A. H. (2010) · PLoS Biology · doi:10.1371/journal.pbio.1000563 · Cited by 133

Differentially regulated GPVI ectodomain shedding by multiple platelet–expressed proteinases

Bender, M., Hofmann, S., Stegner, D., Chalaris, A., Bösl, M. R., Braun, A., Scheller, J., Rose‐John, S., & Nieswandt, B. (2010) · Blood · doi:10.1182/blood-2010-06-289108 · Cited by 132

Transmembrane TNF protects mutant mice against intracellular bacterial infections, chronic inflammation and autoimmunity

Alexopoulou, L., Kranidioti, K., Xanthoulea, S., Denis, M. C., Kotanidou, A. N., Douni, E. K., Blackshear, P. J., Kontoyiannis, D. L., & Kollias, G. A. (2006) · European Journal of Immunology · doi:10.1002/eji.200635921 · Cited by 126

ADAM17 deficiency by mature neutrophils has differential effects on L-selectin shedding

Li, Y., Brazzell, J. L., Herrera, A. H., & Walcheck, B. K. (2006) · Blood · doi:10.1182/blood-2006-02-005827 · Cited by 121

Soluble Jagged 1 Represses the Function of Its Transmembrane Form to Induce the Formation of the Src-dependent Chord-like Phenotype

Small, D. J., Kovalenko, D., Kacer, D., et al. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100933200 · Cited by 121

Inhibition of the Tumor Necrosis Factor-α-converting Enzyme by Its Pro Domain

Gil, P. G., Solomon, A., Miller, A. B., Leesnitzer, M. A., Sagi, I., & Milla, M. E. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m401311200 · Cited by 121

Correction: HER2 Phosphorylation Is Maintained by a PKB Negative Feedback Loop in Response to Anti-HER2 Herceptin in Breast Cancer

Gijsen, M., King, P., Perera, T., Parker, P. J., Harris, A. L., Larijani, B., & Kong, A. H. (2016) · PLoS Biology · doi:10.1371/journal.pbio.1002414 · Cited by 119

LRP1 shedding in human brain: roles of ADAM10 and ADAM17

Liu, Q., Zhang, J., Tran, H., Verbeek, M. M., Reiss, K., Estus, S., & Bu, G. (2009) · Molecular Neurodegeneration · doi:10.1186/1750-1326-4-17 · Cited by 116

Oxidative stress activates ADAM17/TACE and induces its target receptor shedding in platelets in a p38-dependent fashion

Brill, A. G., Chauhan, A. K., Canault, M., Walsh, M. T., Bergmeier, W., & Wagner, D. D. (2009) · Cardiovascular Research · doi:10.1093/cvr/cvp176 · Cited by 111

Evidence for a Role of ADAM17 (TACE) in the Regulation of Platelet Glycoprotein V

Rabie, T., Strehl, A., Ludwig, A., & Nieswandt, B. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500041200 · Cited by 106

Anti-TNF therapies in rheumatoid arthritis, Crohn's disease, sepsis, and myelodysplastic syndromes

Raza, A. (2000) · Microscopy Research and Technique · doi:10.1002/1097-0029(20000801)50:3<229::aid-jemt6>3.0.co;2-h · Cited by 101

The sheddase activity of ADAM17/TACE is regulated by the tetraspanin CD9

Gutiérrez‐López, M. D., Gilsanz, Á., Yáñez‐Mó, M., Ovalle, S., Lafuente, E. M., Domínguez, C., Monk, P. N., González‐Álvaro, I., Sánchez‐Madrid, F., & Cabañas, C. (2011) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-011-0639-0 · Cited by 100

Chemotherapy-induced activation of ADAM-17: a novel mechanism of drug resistance in colorectal cancer

Kyula, J. N., Van Schaeybroeck, S., Doherty, J., Fenning, C. S., Longley, D. B., & Johnston, P. G. (2010) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-10-0014 · Cited by 99

ADAM17 Regulates Epidermal Growth Factor Receptor Expression through the Activation of Notch1 in Non–Small Cell Lung Cancer

Baumgart, A., Seidl, S., Vlachou, P., Michel, L., Mitova, N., Schatz, N., Specht, K., Koch, I., Schuster, T., Grundler, R., et al. (2010) · Cancer Research · doi:10.1158/0008-5472.can-09-3763 · Cited by 97

ATP-mediated Activation of the NADPH Oxidase DUOX1 Mediates Airway Epithelial Responses to Bacterial Stimuli

Boots, A. W., Hristova, M., Kasahara, D. I., Haenen, G. R. M. M., Bast, A., & van der Vliet, A. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m809761200 · Cited by 96

Selective Modulation of Integrin-mediated Cell Migration by Distinct ADAM Family Members

Huang, J., Bridges, L. C., & White, J. M. (2005) · Molecular Biology of the Cell · doi:10.1091/mbc.e05-03-0258 · Cited by 96

ADAM17 (TACE) regulates TGFβ signaling through the cleavage of vasorin

Malapeira, J., Esselens, C., Bech‐Serra, J. J., Canals, F., & Arribas, J. (2010) · Oncogene · doi:10.1038/onc.2010.565 · Cited by 95

Ectodomain shedding of EGFR ligands and TNFR1 dictates hepatocyte apoptosis during fulminant hepatitis in mice

Murthy, A., Defamie, V., Smookler, D. S., Grappa, M. A. D., Horiuchi, K., Federici, M., Sibilia, M. C., Blobel, C., & Khokha, R. (2010) · Journal of Clinical Investigation · doi:10.1172/jci42686 · Cited by 93

Insulin-degrading enzyme is exported via an unconventional protein secretion pathway

Zhao, J., Li, L., & Leissring, M. A. (2009) · Molecular Neurodegeneration · doi:10.1186/1750-1326-4-4 · Cited by 90

TLR ligand–induced podosome disassembly in dendritic cells is ADAM17 dependent

West, M. A., Prescott, A. R., Chan, K. M., Zhou, Z., Rose‐John, S., Scheller, J., & Watts, C. K. W. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200801022 · Cited by 87

TNFα shedding and epidermal inflammation are controlled by Jun proteinsPreprint

Guinea‐Viniegra, J., Zenz, R., Scheuch, H., Hnisz, D., Holcmann, M., Bakiri, L., Schönthaler, H. B., Sibilia, M. C., & Wagner, E. F. (2009) · Genes & Development · doi:10.1101/gad.543109 · Cited by 76

Metalloproteinase- and γ-Secretase-mediated Cleavage of Protein-tyrosine Phosphatase Receptor Type Z

Chow, J. P. H., Fujikawa, A., Shimizu, H., Suzuki, R., & Noda, M. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m802976200 · Cited by 75

Deficiency of TNFα Converting Enzyme (TACE/ADAM17) Causes a Lean, Hypermetabolic Phenotype in Mice

Gelling, R. W., Yan, W., Al‐Noori, S., Pardini, A. W., Morton, G. J., Ogimoto, K., Schwartz, M. W., & Dempsey, P. J. (2008) · Endocrinology · doi:10.1210/en.2008-0775 · Cited by 75

In vivo role of leukocyte ADAM17 in the inflammatory and host responses during E. coli-mediated peritonitis

Long, C., Wang, Y., Herrera, A. H., Horiuchi, K., & Walcheck, B. K. (2010) · Journal of Leukocyte Biology · doi:10.1189/jlb.1109763 · Cited by 66

A transforming Src mutant increases the bioavailability of EGFR ligands via stimulation of the cell-surface metalloproteinase ADAM17

Maretzky, T., Zhou, W., Huang, X.-Y., & Blobel, C. (2010) · Oncogene · doi:10.1038/onc.2010.443 · Cited by 64

Formation of Pmel17 Amyloid Is Regulated by Juxtamembrane Metalloproteinase Cleavage, and the Resulting C-terminal Fragment Is a Substrate for γ-Secretase

Kummer, M. P., Maruyama, H., Hülsmann, C., Baches, S., Weggen, S., & Koo, E. H. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m808904200 · Cited by 63

Conditional Inactivation of TACE by a Sox9 Promoter Leads to Osteoporosis and Increased Granulopoiesis via Dysregulation of IL-17 and G-CSF

Horiuchi, K., Kimura, T., Miyamoto, T. K., Miyamoto, K., Akiyama, H., Takaishi, H., Morioka, H., Nakamura, T., Okada, Y., Blobel, C., et al. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0802491 · Cited by 60

Multiple Mechanisms Are Responsible for Transactivation of the Epidermal Growth Factor Receptor in Mammary Epithelial Cells

Rodland, K., Bollinger, N., Ippolito, D. L., Opresko, L. K., Coffey, R. J., Zangar, R. C., & Wiley, H. S. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m800456200 · Cited by 60

Chaperone-like properties of the prodomain of TNFα-converting enzyme (TACE) and the functional role of its cysteine switch

Leonard, J. D., Lin, F. C., & Milla, M. E. (2005) · Biochemical Journal · doi:10.1042/bj20041727 · Cited by 60

CRP enhances soluble LOX-1 release from macrophages by activating TNF-α converting enzyme

Zhao, X. Q., Zhang, M. W., Wang, F., Zhao, Y. X., Li, J. J., Wang, X. P., Bu, P. L., Yang, J. M., Liu, X. L., Zhang, M. X., et al. (2011) · Journal of Lipid Research · doi:10.1194/jlr.m015156 · Cited by 58

Lymphotoxin-αβ heterotrimers are cleaved by metalloproteinases and contribute to synovitis in rheumatoid arthritis

Young, J., Yu, X., Wolslegel, K., Nguyen, A., Kung, C., Chiang, E. Y., Kolumam, G. A., Wei, N., Wong, W. L., DeForge, L. E., et al. (2010) · Cytokine · doi:10.1016/j.cyto.2010.03.003 · Cited by 55

Ectodomain shedding of the Notch ligand Jagged1 is mediated by ADAM17, but is not a lipid-raft-associated event

Parr-Sturgess, C. A., Rushton, D. J., & Parkin, E. T. (2010) · Biochemical Journal · doi:10.1042/bj20100321 · Cited by 52

ADAM17 Activity and Other Mechanisms of Soluble L-selectin Production during Death Receptor-Induced Leukocyte Apoptosis

Wang, Y., Zhang, A. C., Ni, Z., Herrera, A. H., & Walcheck, B. K. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.0902925 · Cited by 51

Oncogenic Kras Promotes Chemotherapy-Induced Growth Factor Shedding via ADAM17

Van Schaeybroeck, S., Kyula, J. N., Fenton, A., Fenning, C. S., Sasazuki, T., Shirasawa, S., Longley, D. B., & Johnston, P. G. (2011) · Cancer Research · doi:10.1158/0008-5472.can-10-0714 · Cited by 51

Ectodomain Shedding of FLT3 Ligand Is Mediated by TNF-α Converting Enzyme

Horiuchi, K., Morioka, H., Takaishi, H., Akiyama, H., Blobel, C., & Toyama, Y. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0801931 · Cited by 45

Double-Stranded RNA Induces Shedding of the 34-kDa Soluble TNFR1 from Human Airway Epithelial Cells via TLR3–TRIF–RIP1-Dependent Signaling: Roles for Dual Oxidase 2- and Caspase-Dependent Pathways

Yu, M., Lam, J., Rada, B., Leto, T. L., & Levine, S. J. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.1001499 · Cited by 44

Non-Cell Autonomous Expression of TNF-α-Converting Enzyme ADAM17 Is Required for Normal Lymphocyte Development

Li, N., Boyd, K. L., Dempsey, P. J., & Vignali, D. A. A. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.178.7.4214 · Cited by 39

Ectodomain shedding of CD30 is specifically regulated by peptide motifs in its cysteine‐rich domains 2 and 5

Hansen, H. P., Recke, A., Reineke, U., von Tresckow, B., Borchmann, P., von Strandmann, E. P., Lange, H., Lemke, H., & Engert, A. (2004) · The FASEB Journal · doi:10.1096/fj.03-0901fje · Cited by 38

Soluble M6P/IGF2R Released by TACE Controls Angiogenesis via Blocking Plasminogen Activation

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Phorbol Ester-induced Shedding of the Prostate Cancer Marker Transmembrane Protein with Epidermal Growth Factor and Two Follistatin Motifs 2 Is Mediated by the Disintegrin and Metalloproteinase-17

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Soluble form of Jagged1: Unique product of epithelial keratinocytes and a regulator of keratinocyte differentiation

Aho, S. (2004) · Journal of Cellular Biochemistry · doi:10.1002/jcb.20125 · Cited by 36

Attractive shedding

DeLeo, F. R. (2007) · Blood · doi:10.1182/blood-2007-06-096677 · Cited by 15

IL-6 Trans-Signaling via the Soluble IL-6 Receptor: Importance for the Pro-Inflammatory Activities of IL-6

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Reparative inflammation takes charge of tissue regeneration

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How COVID-19 induces cytokine storm with high mortality

Hojyo, S., Uchida, M., Tanaka, K., Hasebe, R., Tanaka, Y., Murakami, M., & Hirano, T. (2020) · Inflammation and Regeneration · doi:10.1186/s41232-020-00146-3 · Cited by 663

Interleukin-6: designing specific therapeutics for a complex cytokine

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NK cell CD16 surface expression and function is regulated by a disintegrin and metalloprotease-17 (ADAM17)

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