Ectodomain shedding and ADAMs in development

The Canonical Notch Signaling Pathway: Unfolding the Activation Mechanism

Kopan, R., & Ilagan, M. X. G. (2009) · Cell · doi:10.1016/j.cell.2009.03.045 · Cited by 3,643

A metalloproteinase disintegrin that releases tumour-necrosis factor-α from cells

Black, R. A., Rauch, C. T., Kozlosky, C. J., Peschon, J. J., Slack, J. L., Wolfson, M. F., Castner, B. J., Stocking, K. L., Reddy, P., Srinivasan, S., et al. (1997) · Nature · doi:10.1038/385729a0 · Cited by 3,149

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

EGF receptor transactivation by G-protein-coupled receptors requires metalloproteinase cleavage of proHB-EGF

Prenzel, N., Zwick, E., Daub, H., Leserer, M., Abraham, R., Wallasch, C., & Ullrich, A. (1999) · Nature · doi:10.1038/47260 · Cited by 1,504

Cloning of a disintegrin metalloproteinase that processes precursor tumour-necrosis factor-α

Moss, M. L., Jin, S.-L. C., Milla, M. E., Burkhart, W., Carter, H. L., Chen, W.-J., Clay, W. C., Didsbury, J. R., Hassler, D., Hoffman, C. R., et al. (1997) · Nature · doi:10.1038/385733a0 · Cited by 1,378

Tie2-Cre Transgenic Mice: A New Model for Endothelial Cell-Lineage Analysis in Vivo

Kisanuki, Y. Y., Hammer, R. E., Miyazaki, J.-I., Williams, S. C., Richardson, J. A., & Yanagisawa, M. (2001) · Developmental Biology · doi:10.1006/dbio.2000.0106 · Cited by 1,241

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

Association of the ADAM33 gene with asthma and bronchial hyperresponsiveness

Van Eerdewegh, P., Little, R. D., Dupuis, J., Del Mastro, R. G., Falls, K., Simon, J., Torrey, D., Pandit, S., McKenny, J., Braunschweiger, K., et al. (2002) · Nature · doi:10.1038/nature00878 · Cited by 1,099

A Novel Proteolytic Cleavage Involved in Notch Signaling

Brou, C., Logeat, F., Gupta, N., Bessia, C., LeBail, O., Doedens, J. R., Cumano, A., Roux, P., Black, R. A., & Israël, A. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)80417-7 · Cited by 1,094

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

The ADAMs family of metalloproteases: multidomain proteins with multiple functions

Seals, D. F., & Courtneidge, S. A. (2003) · Genes & Development · doi:10.1101/gad.1039703 · Cited by 1,059

Distinct roles for ADAM10 and ADAM17 in ectodomain shedding of six EGFR ligands

Sahin, U., Weskamp, G., Kelly, K., Zhou, H.-M., Higashiyama, S., Peschon, J., Hartmann, D., Saftig, P., & Blobel, C. P. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200307137 · Cited by 979

Constitutive and regulated α-secretase cleavage of Alzheimer’s amyloid precursor protein by a disintegrin metalloprotease

Lammich, S., Kojro, E., Postina, R., Gilbert, S., Pfeiffer, R., Jasionowski, M., Haass, C., & Fahrenholz, F. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.7.3922 · Cited by 975

Notch signaling: simplicity in design, versatility in function

Andersson, E. R., Sandberg, R., & Lendahl, U. (2011) · Development · doi:10.1242/dev.063610 · Cited by 950

Evidence That Tumor Necrosis Factor α Converting Enzyme Is Involved in Regulated α-Secretase Cleavage of the Alzheimer Amyloid Protein Precursor

Buxbaum, J. D., Liu, K.-N., Luo, Y., Slack, J. L., Stocking, K. L., Peschon, J. J., Johnson, R. S., Castner, B. J., Cerretti, D. P., & Black, R. A. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.43.27765 · Cited by 934

Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc‐binding environments (HEXXHXXGXXH and Met‐turn) and topologies and should be grouped into a common family, the ‘metzincins’

Bode, W., Gomis-Rüth, F.-X., & Stöckler, W. (1993) · FEBS Letters · doi:10.1016/0014-5793(93)80312-i · Cited by 757

Cardiac hypertrophy is inhibited by antagonism of ADAM12 processing of HB-EGF: Metalloproteinase inhibitors as a new therapy

Asakura, M., Kitakaze, M., Takashima, S., Liao, Y., Ishikura, F., Yoshinaka, T., Ohmoto, H., Node, K., Yoshino, K., Ishiguro, H., et al. (2002) · Nature Medicine · doi:10.1038/nm0102-35 · Cited by 724

The disintegrin-like metalloproteinase ADAM10 is involved in constitutive cleavage of CX3CL1 (fractalkine) and regulates CX3CL1-mediated cell-cell adhesion

Hundhausen, C., Misztela, D., Berkhout, T. A., Broadway, N., Saftig, P., Reiss, K., Hartmann, D., Fahrenholz, F., Postina, R., Matthews, V., et al. (2003) · Blood · doi:10.1182/blood-2002-12-3775 · Cited by 713

Tumor Necrosis Factor-α Convertase (ADAM17) Mediates Regulated Ectodomain Shedding of the Severe-acute Respiratory Syndrome-Coronavirus (SARS-CoV) Receptor, Angiotensin-converting Enzyme-2 (ACE2)

Lambert, D. W., Yarski, M., Warner, F. J., Thornhill, P., Parkin, E. T., Smith, A. I., Hooper, N. M., & Turner, A. J. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m505111200 · Cited by 694

The disintegrin/metalloprotease ADAM 10 is essential for Notch signalling but not for alpha-secretase activity in fibroblasts

Hartmann, D. (2002) · Human Molecular Genetics · doi:10.1093/hmg/11.21.2615 · Cited by 680

ADAM10 mediates E-cadherin shedding and regulates epithelial cell-cell adhesion, migration, and β-catenin translocation

Maretzky, T., Reiss, K., Ludwig, A., Buchholz, J., Scholz, F., Proksch, E., de Strooper, B., Hartmann, D., & Saftig, P. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0500918102 · Cited by 673

A potential fusion peptide and an integrin ligand domain in a protein active in sperm–egg fusion

Blobel, C. P., Wolfsberg, T. G., Turck, C. W., Myles, D. G., Primakoff, P., & White, J. M. (1992) · Nature · doi:10.1038/356248a0 · Cited by 672

A disintegrin-metalloproteinase prevents amyloid plaque formation and hippocampal defects in an Alzheimer disease mouse model

Postina, R., Schroeder, A., Dewachter, I., Bohl, J., Schmitt, U., Kojro, E., Prinzen, C., Endres, K., Hiemke, C., Blessing, M., et al. (2004) · Journal of Clinical Investigation · doi:10.1172/jci20864 · Cited by 638

ADAM10 is the physiologically relevant, constitutive α‐secretase of the amyloid precursor protein in primary neurons

Kuhn, P., Wang, H., Dislich, B., Colombo, A., Zeitschel, U., Ellwart, J. W., Kremmer, E., Roßner, S., & Lichtenthaler, S. F. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.167 · Cited by 621 · cited 1×

A metalloprotease-disintegrin, MDC9/meltrin-gamma /ADAM9 and PKCdelta are involved in TPA-induced ectodomain shedding of membrane-anchored heparin-binding EGF-like growth factor

Izumi, Y. (1998) · The EMBO Journal · doi:10.1093/emboj/17.24.7260 · Cited by 521

Kuzbanian Controls Proteolytic Processing of Notch and Mediates Lateral Inhibition during Drosophila and Vertebrate Neurogenesis

Pan, D., & Rubin, G. M. (1997) · Cell · doi:10.1016/s0092-8674(00)80335-9 · Cited by 519

Regulated Cleavage of a Contact-Mediated Axon Repellent

Hattori, M., Osterfield, M., & Flanagan, J. G. (2000) · Science · doi:10.1126/science.289.5483.1360 · Cited by 518

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

Reddy, P., Slack, J. L., Davis, R., Cerretti, D. P., Kozlosky, C. J., Blanton, R. A., Shows, D., Peschon, J. J., & Black, R. A. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.19.14608 · Cited by 501

Fertilization Defects in Sperm from Mice Lacking Fertilin β

Cho, C., O'Dell Bunch, D., Faure, J.-E., Goulding, E. H., Eddy, E. M., Primakoff, P., & Myles, D. G. (1998) · Science · doi:10.1126/science.281.5384.1857 · Cited by 499

A metalloprotease-disintegrin participating in myoblast fusion

Yagami-Hiromasa, T., Sato, T., Kurisaki, T., Kamijo, K., Nabeshima, Y.-I., & Fujisawa-Sehara, A. (1995) · Nature · doi:10.1038/377652a0 · Cited by 481

ADAM10 cleavage of N‐cadherin and regulation of cell–cell adhesion and β‐catenin nuclear signalling

Reiss, K., Maretzky, T., Ludwig, A., Tousseyn, T., de Strooper, B., Hartmann, D., & Saftig, P. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600548 · Cited by 481

Shedding light on ADAM metalloproteinases

Huovila, A.-P. J., Turner, A. J., Pelto-Huikko, M., Kärkkäinen, I., & Ortiz, R. M. (2005) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2005.05.006 · Cited by 453

Adam Meets Eph: An ADAM Substrate Recognition Module Acts as a Molecular Switch for Ephrin Cleavage In trans

Janes, P. W., Saha, N., Barton, W. A., Kolev, M. V., Wimmer-Kleikamp, S. H., Nievergall, E., Blobel, C. P., Himanen, J.-P., Lackmann, M., & Nikolov, D. B. (2005) · Cell · doi:10.1016/j.cell.2005.08.014 · Cited by 443

Regulation of vascular morphogenesis by Notch signaling

Roca, C., & Adams, R. H. (2007) · Genes & Development · doi:10.1101/gad.1589207 · Cited by 439

Notch–RBP-J signaling regulates the transcription factor IRF8 to promote inflammatory macrophage polarization

Xu, H., Zhu, J., Smith, S., Foldi, J., Zhao, B., Chung, A. Y., Outtz, H., Kitajewski, J., Shi, C., Weber, S., et al. (2012) · Nature Immunology · doi:10.1038/ni.2304 · Cited by 438

The “A Disintegrin And Metalloprotease” (ADAM) family of sheddases: Physiological and cellular functions

Reiss, K., & Saftig, P. (2009) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2008.11.002 · Cited by 423

Defective valvulogenesis in HB-EGF and TACE-null mice is associated with aberrant BMP signaling

Jackson, L. F. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg264 · Cited by 417

ADAMs: modulators of cell–cell and cell–matrix interactions

White, J. M. (2003) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2003.08.001 · Cited by 415

Tumor Necrosis Factor Signaling Requires iRhom2 to Promote Trafficking and Activation of TACE

Adrain, C., Zettl, M., Christova, Y., Taylor, N., & Freeman, M. (2012) · Science · doi:10.1126/science.1214400 · Cited by 407

Functional analysis of secreted and transmembrane proteins critical to mouse development.

Mitchell, K. J., Pinson, K. I., Kelly, O. G., Brennan, J., Zupicich, J., Scherz, P., Leighton, P. A., Goodrich, L. V., Lu, X., Avery, B. J., et al. (2001) · Nature Genetics · doi:10.1038/90074 · Cited by 400

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

Crystal structure of the catalytic domain of human tumor necrosis factor-α-converting enzyme

Maskos, K., Fernandez-Catalan, C., Huber, R., Bourenkov, G. P., Bartunik, H., Ellestad, G. A., Reddy, P., Wolfson, M. F., Rauch, C. T., Castner, B. J., et al. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.7.3408 · Cited by 387

Tumor-Associated MICA Is Shed by ADAM Proteases

Waldhauer, I., Goehlsdorf, D., Gieseke, F., Weinschenk, T., Wittenbrink, M., Ludwig, A., Stevanovic, S., Rammensee, H.-G., & Steinle, A. (2008) · Cancer Research · doi:10.1158/0008-5472.can-07-6768 · Cited by 375

The Disintegrin/Metalloproteinase ADAM10 Is Essential for the Establishment of the Brain Cortex

Jorissen, E., Prox, J., Bernreuther, C., Weber, S., Schwanbeck, R., Serneels, L., Snellinx, A., Craessaerts, K., Thathiah, A., Tesseur, I., et al. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.5221-09.2010 · Cited by 363

Intracellular maturation and localization of the tumour necrosis factor α convertase (TACE)

Schlöndorff, J. S., Becherer, J. D., & Blobel, C. (2000) · Biochemical Journal · doi:10.1042/0264-6021:3470131 · Cited by 359

Notch in the Vertebrate Nervous System: An Old Dog with New Tricks

Pierfelice, T., Alberi, L., & Gaiano, N. (2011) · Neuron · doi:10.1016/j.neuron.2011.02.031 · Cited by 353

In search of partners: linking extracellular proteases to substrates

Overall, C. M., & Blobel, C. P. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2120 · Cited by 349

Structural aspects of the metzincin clan of metalloendopeptidases

Gomis-Rüth, F. X. (2003) · Molecular Biotechnology · doi:10.1385/mb:24:2:157 · Cited by 340

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

KUZ, a Conserved Metalloprotease-Disintegrin Protein with Two Roles in Drosophila Neurogenesis

Rooke, J., Pan, D., Xu, T., & Rubin, G. M. (1996) · Science · doi:10.1126/science.273.5279.1227 · Cited by 328

iRhom2 Regulation of TACE Controls TNF-Mediated Protection Against Listeria and Responses to LPS

McIlwain, D. R., Lang, P. A., Maretzky, T., Hamada, K., Ohishi, K., Maney, S. K., Berger, T., Murthy, A., Duncan, G., Xu, H. C., et al. (2012) · Science · doi:10.1126/science.1214448 · Cited by 327

Metalloprotease-Disintegrin MDC9: Intracellular Maturation and Catalytic Activity

Roghani, M., Becherer, J. D., Moss, M. L., Atherton, R. E., Erdjument-Bromage, H., Arribas, J., Blackburn, R. K., Weskamp, G., Tempst, P., & Blobel, C. P. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.6.3531 · Cited by 319

ADAM 12-S Cleaves IGFBP-3 and IGFBP-5 and Is Inhibited by TIMP-3

Loechel, F., Fox, J. W., Murphy, G., Albrechtsen, R., & Wewer, U. M. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.3835 · Cited by 314

Selective Use of ADAM10 and ADAM17 in Activation of Notch1 Signaling

Bozkulak, E. C., & Weinmaster, G. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.00406-09 · Cited by 309

Inflammatory Skin and Bowel Disease Linked to ADAM17 Deletion

Blaydon, D. C., Biancheri, P., Di, W.-L., Plagnol, V., Cabral, R. M., Brooke, M. A., van Heel, D. A., Ruschendorf, F., Toynbee, M., Walne, A., et al. (2011) · New England Journal of Medicine · doi:10.1056/nejmoa1100721 · Cited by 308

Extracellular Signal-regulated Kinase Phosphorylates Tumor Necrosis Factor α-converting Enzyme at Threonine 735: A Potential Role in Regulated Shedding

Dı́az-Rodrı́guez, E., Montero, J. C., Esparı́s-Ogando, A., Yuste, L., & Pandiella, A. (2002) · Molecular Biology of the Cell · doi:10.1091/mbc.01-11-0561 · Cited by 308

Putative function of ADAM9, ADAM10, and ADAM17 as APP -secretase

Asai, M., Hattori, C., Szabó, B., Sasagawa, N., Maruyama, K., Tanuma, S.-I., & Ishiura, S. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(02)02999-6 · Cited by 303

ADAM10 Regulates Endothelial Permeability and T-Cell Transmigration by Proteolysis of Vascular Endothelial Cadherin

Schulz, B., Pruessmeyer, J., Maretzky, T., Ludwig, A., Blobel, C. P., Saftig, P., & Reiss, K. (2008) · Circulation Research · doi:10.1161/circresaha.107.169805 · Cited by 301

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

The “A Disintegrin And Metalloproteases” ADAM10 and ADAM17: Novel drug targets with therapeutic potential?

Saftig, P., & Reiss, K. (2011) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2010.11.005 · Cited by 297

Epidermal Notch signalling: differentiation, cancer and adhesion

Watt, F. M., Estrach, S., & Ambler, C. A. (2008) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2008.01.010 · Cited by 295

Cell–matrix interaction via CD44 is independently regulated by different metalloproteinases activated in response to extracellular Ca2+ influx and PKC activation

Nagano, O., Murakami, D., Hartmann, D., de Strooper, B., Saftig, P., Iwatsubo, T., Nakajima, M., Shinohara, M., & Saya, H. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200310024 · Cited by 294

The Disintegrins ADAM10 and TACE Contribute to the Constitutive and Phorbol Ester-regulated Normal Cleavage of the Cellular Prion Protein

Vincent, B., Paitel, E., Saftig, P., Frobert, Y., Hartmann, D., De Strooper, B., Grassi, J., Lopez-Perez, E., & Checler, F. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105677200 · Cited by 289

Stimulated Shedding of Vascular Cell Adhesion Molecule 1 (VCAM-1) Is Mediated by Tumor Necrosis Factor-α-converting Enzyme (ADAM 17)

Garton, K. J., Gough, P. J., Philalay, J., Wille, P. T., Blobel, C. P., Whitehead, R. H., Dempsey, P. J., & Raines, E. W. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m305877200 · Cited by 282

Metalloproteases regulate T‐cell proliferation and effector function via LAG‐3

Li, N., Wang, Y., Forbes, K., Vignali, K. M., Heale, B. S., Saftig, P., Hartmann, D., Black, R. A., Rossi, J. J., Blobel, C. P., et al. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601520 · Cited by 282

Membrane-anchored metalloprotease MDC9 has an α-secretase activity responsible for processing the amyloid precursor protein

KOIKE, H., Tomioka, S., Sorimachi, H., Saido, T. C., Maruyama, K., Okuyama, A., Fujisawa‐Sehara, A., Ohno, S., Suzuki, K., & Ishiura, S. (1999) · Biochemical Journal · doi:10.1042/0264-6021:3430371 · Cited by 278

T-cell-specific deletion of a polypeptide N-acetylgalactosaminyl-transferase gene by site-directed recombination.

Hennet, T., Hagen, F. K., Tabak, L. A., & Marth, J. D. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.26.12070 · Cited by 271

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

Multiple G-protein-coupled receptor signals converge on the epidermal growth factor receptor to promote migration and invasion

Schäfer, B., Gschwind, A., & Ullrich, A. (2004) · Oncogene · doi:10.1038/sj.onc.1207278 · Cited by 266

Role of ADAMs in Cancer Formation and Progression

Duffy, M. J., McKiernan, E., O'Donovan, N., & McGowan, P. M. (2009) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-08-1585 · Cited by 259

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

The Notch ligand Delta1 is sequentially cleaved by an ADAM protease and γ-secretase

Six, E., Ndiaye, D., Laâbi, Y., Brou, C., Gupta-Rossi, N., Israël, A., & Logeat, F. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1230693100 · Cited by 250

The Cysteine-Rich Domain of Human Adam 12 Supports Cell Adhesion through Syndecans and Triggers Signaling Events That Lead to β1 Integrin–Dependent Cell Spreading

Iba, K., Albrechtsen, R., Gilpin, B., Fröhlich, C., Loechel, F., Zolkiewska, A., Ishiguro, K., Kojima, T., Liu, W., Langford, J. K., et al. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.149.5.1143 · Cited by 248

ADAM 12 Cleaves Extracellular Matrix Proteins and Correlates with Cancer Status and Stage

Roy, R., Wewer, U. M., Zurakowski, D., Pories, S. E., & Moses, M. A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m409565200 · Cited by 244

Klotho is a substrate for α‐, β‐ and γ‐secretase

Bloch, L., Sineshchekova, O., Reichenbach, D., Reiss, K., Saftig, P., Kuro-o, M., & Kaether, C. (2009) · FEBS Letters · doi:10.1016/j.febslet.2009.09.009 · Cited by 243

Negative regulation of osteoclastogenesis by ectodomain shedding of receptor activator of NF-κB ligand.

Hikita, A., Yana, I., Wakeyama, H., Nakamura, M., Kadono, Y., Oshima, Y., Nakamura, K., Seiki, M., & Tanaka, S. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m606656200 · Cited by 236

Novel Research Horizons for Presenilins and γ-Secretases in Cell Biology and Disease

De Strooper, B., & Annaert, W. (2010) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-100109-104117 · Cited by 234

L1 Is Sequentially Processed by Two Differently Activated Metalloproteases and Presenilin/γ-Secretase and Regulates Neural Cell Adhesion, Cell Migration, and Neurite Outgrowth

Maretzky, T., Schulte, M., Ludwig, A., Rose-John, S., Blobel, C., Hartmann, D., Altevogt, P., Saftig, P., & Reiss, K. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.20.9040-9053.2005 · Cited by 232

Transmembrane collagen XVII, an epithelial adhesion protein, is shed from the cell surface by ADAMs

Franzke, C.-W., Tasanen, K., Schäcke, H., Zhou, Z., Tryggvason, K., Mauch, C., Zigrino, P., Sunnarborg, S., Lee, D. C., Fahrenholz, F., et al. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf532 · Cited by 230

Male Mice Deficient for Germ-Cell Cyritestin Are Infertile1

Shamsadin, R., Adham, I. M., Nayernia, K., Heinlein, U. A. O., Oberwinkler, H., & Engel, W. (1999) · Biology of Reproduction · doi:10.1095/biolreprod61.6.1445 · Cited by 226

ADAM10‐mediated cleavage of L1 adhesion molecule at the cell surface and in released membrane vesicles

Gutwein, P., Mechtersheimer, S., Riedle, S., Stoeck, A., Gast, D., Joumaa, S., Zentgraf, H., Fogel, M., & Altevogt, P. (2003) · The FASEB Journal · doi:10.1096/fj.02-0430fje · Cited by 225

Mice Lacking the Metalloprotease-Disintegrin MDC9 (ADAM9) Have No Evident Major Abnormalities during Development or Adult Life

Weskamp, G., Cai, H., Brodie, T. A., Higashyama, S., Manova, K., Ludwig, T., & Blobel, C. P. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.5.1537-1544.2002 · Cited by 215

RHBDF2 Mutations Are Associated with Tylosis, a Familial Esophageal Cancer Syndrome

Blaydon, D. C., Etheridge, S. L., Risk, J. M., Hennies, H.-C., Gay, L. J., Carroll, R., Plagnol, V., McRonald, F. E., Stevens, H. P., Spurr, N. K., et al. (2012) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2011.12.008 · Cited by 207

ADAM10 is a principal 'sheddase' of the low-affinity immunoglobulin E receptor CD23

Weskamp, G., Ford, J. W., Sturgill, J., Martin, S., Docherty, A. J. P., Swendeman, S., Broadway, N., Hartmann, D., Saftig, P., Umland, S., et al. (2006) · Nature Immunology · doi:10.1038/ni1399 · Cited by 206

Crystal structures of VAP1 reveal ADAMs' MDC domain architecture and its unique C‐shaped scaffold

Takeda, S., Igarashi, T., Mori, H., & Araki, S. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601131 · Cited by 202 · cited 1×

Possible Function of the ADAM1a/ADAM2 Fertilin Complex in the Appearance of ADAM3 on the Sperm Surface

Nishimura, H., Kim, E., Nakanishi, T., & Baba, T. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m314249200 · Cited by 198

The Ectodomain Shedding of E-cadherin by ADAM15 Supports ErbB Receptor Activation

Najy, A. J., Day, K. C., & Day, M. L. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m801329200 · Cited by 193

A Genomic Analysis of Rat Proteases and Protease Inhibitors

Puente, X. S., & López-Otín, C. (2004) · Genome Research · doi:10.1101/gr.1946304 · Cited by 192

A Secreted Form of ADAM9 Promotes Carcinoma Invasion through Tumor-Stromal Interactions

Mazzocca, A., Coppari, R., De Franco, R., Cho, J.-Y., Libermann, T. A., Pinzani, M., & Toker, A. (2005) · Cancer Research · doi:10.1158/0008-5472.can-04-4449 · Cited by 191

Potential Role for ADAM15 in Pathological Neovascularization in Mice

Horiuchi, K., Weskamp, G., Lum, L., Hammes, H.-P., Cai, H., Brodie, T. A., Ludwig, T., Chiusaroli, R., Baron, R., Preissner, K. T., et al. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.16.5614-5624.2003 · Cited by 189

ADAM10, the Rate-limiting Protease of Regulated Intramembrane Proteolysis of Notch and Other Proteins, Is Processed by ADAMS-9, ADAMS-15, and the γ-Secretase

Tousseyn, T., Thathiah, A., Jorissen, E., Raemaekers, T., Konietzko, U., Reiss, K., Maes, E., Snellinx, A., Serneels, L., Nyabi, O., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m805894200 · Cited by 188

Epidermal ADAM17 maintains the skin barrier by regulating EGFR ligand–dependent terminal keratinocyte differentiation

Franzke, C.-W., Cobzaru, C., Triantafyllopoulou, A., Löffek, S., Horiuchi, K., Threadgill, D. W., Kurz, T., van Rooijen, N., Bruckner-Tuderman, L., & Blobel, C. P. (2012) · Journal of Experimental Medicine · doi:10.1084/jem.20112258 · Cited by 186

Catalytic Activity of ADAM8, ADAM15, and MDC-L (ADAM28) on Synthetic Peptide Substrates and in Ectodomain Cleavage of CD23

Fourie, A. M., Coles, F., Moreno, V., & Karlsson, L. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m213157200 · Cited by 185

ADAM10 regulates FasL cell surface expression and modulates FasL-induced cytotoxicity and activation-induced cell death

Schulte, M., Reiss, K., Lettau, M., Maretzky, T., Ludwig, A., Hartmann, D., de Strooper, B., Janssen, O., & Saftig, P. (2007) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4402101 · Cited by 184

Roles of Meltrin β/ADAM19 in the Processing of Neuregulin

Shirakabe, K., Wakatsuki, S., Kurisaki, T., & Fujisawa-Sehara, A. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m007913200 · Cited by 181

The cell surface metalloprotease/disintegrin Kuzbanian is required for axonal extension in Drosophila

Fambrough, D., Pan, D., Rubin, G. M., & Goodman, C. S. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.23.13233 · Cited by 180

The precursor region of a protein active in sperm-egg fusion contains a metalloprotease and a disintegrin domain: structural, functional, and evolutionary implications.

Wolfsberg, T. G., Bazan, J. F., Blobel, C. P., Myles, D. G., Primakoff, P., & White, J. M. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.22.10783 · Cited by 179

Tumor Necrosis Factor-α-converting Enzyme (TACE/ADAM-17) Mediates the Ectodomain Cleavage of Intercellular Adhesion Molecule-1 (ICAM-1)

Tsakadze, N. L., Sithu, S. D., Sen, U., English, W. R., Murphy, G., & D'Souza, S. E. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m510797200 · Cited by 177

Ataxia and peripheral nerve hypomyelination in ADAM22-deficient mice

Sagane, K., Hayakawa, K., Kai, J., Hirohashi, T., Takahashi, E., Miyamoto, N., Ino, M., Oki, T., Yamazaki, K., & Nagasu, T. (2005) · BMC Neuroscience · doi:10.1186/1471-2202-6-33 · Cited by 174

The Metalloprotease Disintegrin ADAM8

Schlomann, U., Wildeboer, D., Webster, A., Antropova, O., Zeuschner, D., Knight, C. G., Docherty, A. J. P., Lambert, M., Skelton, L., Jockusch, H., et al. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m203355200 · Cited by 171

Intracellular Maturation of the Mouse Metalloprotease Disintegrin MDC15

Lum, L., Reid, M. S., & Blobel, C. P. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.40.26236 · Cited by 167

Nectin-4, a New Serological Breast Cancer Marker, Is a Substrate for Tumor Necrosis Factor-α-converting Enzyme (TACE)/ADAM-17

Fabre-Lafay, S., Garrido-Urbani, S., Reymond, N., Gonçalves, A., Dubreuil, P., & Lopez, M. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m410943200 · Cited by 163

Evaluation of the contributions of ADAMs 9, 12, 15, 17, and 19 to heart development and ectodomain shedding of neuregulins β1 and β2

Horiuchi, K., Zhou, H.-M., Kelly, K., Manova, K., & Blobel, C. P. (2005) · Developmental Biology · doi:10.1016/j.ydbio.2005.05.004 · Cited by 163

Cleavage of E-cadherin by ADAM10 mediates epithelial cell sorting downstream of EphB signalling

Solanas, G., Cortina, C., Sevillano, M., & Batlle, E. (2011) · Nature Cell Biology · doi:10.1038/ncb2298 · Cited by 162

SUP-17, a Caenorhabditis elegans ADAM protein related to Drosophila KUZBANIAN, and its role in LIN-12/NOTCH signalling

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Evaluation of the Contribution of Different ADAMs to Tumor Necrosis Factor α (TNFα) Shedding and of the Function of the TNFα Ectodomain in Ensuring Selective Stimulated Shedding by the TNFα Convertase (TACE/ADAM17)

Zheng, Y., Saftig, P., Hartmann, D., & Blobel, C. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m403193200 · Cited by 158

Regulated Intramembrane Proteolysis of Bri2 (Itm2b) by ADAM10 and SPPL2a/SPPL2b

Martin, L., Fluhrer, R., Reiß, K., Kremmer, E., Säftig, P., & Haass, C. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m706661200 · Cited by 157

Specific Sequence Elements Are Required for the Expression of Functional Tumor Necrosis Factor-α-converting Enzyme (TACE)

Milla, M. E., Leesnitzer, M. A., Moss, M. L., Clay, W. C., Carter, H. L., Miller, A. B., Su, J., Lambert, M. H., Willard, D. H., Sheeley, D. M., et al. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.43.30563 · Cited by 156

TACE (ADAM17) inhibits Schwann cell myelination

Marca, R. L., Cerri, F., Horiuchi, K., Bachi, A., Feltri, M. L., Wrabetz, L. G., Blobel, C., Quattrini, A., Salzer, J. L., & Taveggia, C. (2011) · Nature Neuroscience · doi:10.1038/nn.2849 · Cited by 155

Phenotypic Analysis of Meltrin α (ADAM12)-Deficient Mice: Involvement of Meltrin α in Adipogenesis and Myogenesis

Kurisaki, T., Masuda, A., Sudo, K., Sakagami, J., Higashiyama, S., Matsuda, Y., Nagabukuro, A., Tsuji, A. B., Nabeshima, Y.-I., Asano, M., et al. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.23.1.55-61.2003 · Cited by 155

ADAM10 is essential for Notch2-dependent marginal zone B cell development and CD23 cleavage in vivo

Gibb, D. R., Shikh, M. E. E., Kang, D.-J., Rowe, W. J., Sayed, R., Cichy, J., Yagita∥, H., Tew, J. G., Dempsey, P. J., Crawford, H. C., et al. (2010) · The Journal of Experimental Medicine · doi:10.1084/jem.20091990 · Cited by 154

The disintegrin/metalloproteinase Adam10 is essential for epidermal integrity and Notch-mediated signaling

Weber, S., Niessen, M. T., Prox, J., Lüllmann‐Rauch, R., Schmitz, A., Schwanbeck, R., Blobel, C., Jorissen, E., Strooper, B. D., Niessen, C. M., et al. (2011) · Development · doi:10.1242/dev.055210 · Cited by 153

A Role for ADAM12 in Breast Tumor Progression and Stromal Cell Apoptosis

Kveiborg, M., Fröhlich, C., Albrechtsen, R., Tischler, V., Dietrich, N., Holck, P., Kronqvist, P., Rank, F. E., Mercurio, A. M., & Wewer, U. M. (2005) · Cancer Research · doi:10.1158/0008-5472.can-05-0262 · Cited by 153

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

Essential Role for ADAM19 in Cardiovascular Morphogenesis

Zhou, H., Weskamp, G., Chesneau, V., Şahin, U., Vortkamp, A., Horiuchi, K., Chiusaroli, R., Hahn, R. T., Wilkes, D. C., Fisher, P. E., et al. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.24.1.96-104.2004 · Cited by 139

ErbB and HB-EGF Signaling in Heart Development and Function

Iwamoto, R., & Mekada, E. (2006) · Cell Structure and Function · doi:10.1247/csf.31.1 · Cited by 138

Cloning and characterization of ADAM28: evidence for autocatalytic pro-domain removal and for cell surface localization of mature ADAM28

Howard, L., Maciewicz, R. A., & Blobel, C. (2000) · Biochemical Journal · doi:10.1042/bj3480021 · Cited by 136

The evolution of the vertebrate metzincins; insights from Ciona intestinalis and Danio rerio

Huxley‐Jones, J., Clarke, T., Beck, C., Toubaris, G., Robertson, D. L., & Boot-Handford, R. (2007) · BMC Evolutionary Biology · doi:10.1186/1471-2148-7-63 · Cited by 135

Membrane-anchored CD40 Is Processed by the Tumor Necrosis Factor-α-converting Enzyme

Contin‐Bordes, C., Pitard, V., Itai, T., Nagata, S., Moreau, J., & Déchanet‐Merville, J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m209993200 · Cited by 135

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

Notch Activation by the Metalloproteinase ADAM17 Regulates Myeloproliferation and Atopic Barrier Immunity by Suppressing Epithelial Cytokine Synthesis

Murthy, A., Shao, Y. W., Narala, S., Molyneux, S. D., Zúñiga‐Pflücker, J. C., & Khokha, R. (2012) · Immunity · doi:10.1016/j.immuni.2012.01.005 · Cited by 131

An evolutionary recent neuroepithelial cell adhesion function of huntingtin implicates ADAM10-Ncadherin

Sardo, V. L., Zuccato, C., Gaudenzi, G., Vitali, B., Ramos, C., Tartari, M., Myre, M. A., Walker, J. A., Pistocchi, A., Conti, L., et al. (2012) · Nature Neuroscience · doi:10.1038/nn.3080 · Cited by 130

ADAM28 is activated by MMP-7 (matrilysin-1) and cleaves insulin-like growth factor binding protein-3

Mochizuki, S., Shimoda, M., Shiomi, T., Fujii, Y., & Okada, Y. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.01.022 · Cited by 129

Proteolytic Processing of Delta-like 1 by ADAM Proteases

Dyczynska, E., Sun, D., Yi, H., Sehara‐Fujisawa, A., Blobel, C., & Żółkiewska, A. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m605451200 · Cited by 129

Catalytic Properties of ADAM19

Chesneau, V., Becherer, J. D., Zheng, Y., Erdjument‐Bromage, H., Tempst, P., & Blobel, C. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m302781200 · Cited by 129

Tetraspanin15 regulates cellular trafficking and activity of the ectodomain sheddase ADAM10

Prox, J., Willenbrock, M., Weber, S., Lehmann, T., Schmidt‐Arras, D., Schwanbeck, R., Säftig, P., & Schwake, M. (2012) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-012-0960-2 · Cited by 125

The Role of ADAM 15 in Glomerular Mesangial Cell Migration

Martin, J. T., Eynstone, L. V., Davies, M., Williams, J. D., & Steadman, R. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m200988200 · Cited by 125

Proteomic Identification of Desmoglein 2 and Activated Leukocyte Cell Adhesion Molecule as Substrates of ADAM17 and ADAM10 by Difference Gel Electrophoresis

Bech‐Serra, J. J., Santiago‐Josefat, B., Esselens, C., Säftig, P., Baselga, J. M., Arribas, J., & Canals, F. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.02380-05 · Cited by 125

Ectodomain shedding of the EGF‐receptor ligand epigen is mediated by ADAM17

Şahin, U., & Blobel, C. (2006) · FEBS Letters · doi:10.1016/j.febslet.2006.11.074 · Cited by 123

Expression and Regulation of the Metalloproteinase ADAM-8 during Human Neutrophil Pathophysiological Activation and Its Catalytic Activity on L-Selectin Shedding

Gómez‐Gaviro, M. V., Domínguez‐Luis, M. J., Canchado, J., Calafat, J., Janssen, H., Lara‐Pezzi, E., Fourie, A. M., Tugores, A., Valenzuela-Fernández, A., Mollinedo, F., et al. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.178.12.8053 · Cited by 121

Lack of a-disintegrin-and-metalloproteinase ADAM10 leads to intracellular accumulation and loss of shedding of the cellular prion protein in vivo

Altmeppen, H. C., Prox, J., Puig, B., Kluth, M. A., Bernreuther, C., Thurm, D., Jorissen, E., Petrowitz, B., Bartsch, U., Strooper, B. D., et al. (2011) · Molecular Neurodegeneration · doi:10.1186/1750-1326-6-36 · Cited by 120

Metalloprotease‐disintegrin ADAM8: Expression analysis and targeted deletion in mice

Kelly, K., Hutchinson, G., Nebenius‐Oosthuizen, D., Smith, A. J. H., Bartsch, J. W., Horiuchi, K., Rittger, A., Manova, K., Docherty, A. J. P., & Blobel, C. (2004) · Developmental Dynamics · doi:10.1002/dvdy.20221 · Cited by 120

Regulated ADAM10-dependent Ectodomain Shedding of γ-Protocadherin C3 Modulates Cell-Cell Adhesion

Reiß, K., Maretzky, T., Haas, I. G., Schulte, M., Ludwig, A., Frank, M., & Säftig, P. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602663200 · Cited by 119

The Metallo-Disintegrin ADAM10 (MADM) from Bovine Kidney Has Type IV Collagenase Activityin Vitro

Millichip, M. I., Dallas, D. J., Wu, E., Dale, S., & McKie, N. (1998) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1998.8485 · Cited by 118

None of the integrins known to be present on the mouse egg or to be ADAM receptors are essential for sperm–egg binding and fusion

He, Z.-Y., Brakebusch, C., Fässler, R., Kreidberg, J. A., Primakoff, P., & Myles, D. G. (2003) · Developmental Biology · doi:10.1016/s0012-1606(02)00043-x · Cited by 118

Critical Function for ADAM9 in Mouse Prostate Cancer

Peduto, L., Reuter, V. E., Shaffer, D. R., Scher, H. I., & Blobel, C. (2005) · Cancer Research · doi:10.1158/0008-5472.can-05-1063 · Cited by 116

The cysteine-rich domain regulates ADAM protease function in vivo

Smith, K., Gaultier, A., Cousin, H., Alfandari, D., White, J. M., & DeSimone, D. W. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200206023 · Cited by 115

TACE is required for fetal murine cardiac development and modeling

Shi, W., Chen, H., Sun, J., Buckley, S., Zhao, J., Anderson, K. D., Williams, R. G., & Warburton, D. (2003) · Developmental Biology · doi:10.1016/s0012-1606(03)00315-4 · Cited by 115

ADAM33 polymorphisms and phenotype associations in childhood asthma

Raby, B. A., Silverman, E. K., Kwiatkowski, D. J., Lange, C., Lazarus, R. M., & Weiss, S. T. (2004) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2004.03.035 · Cited by 114

Genetic Requirement for ADAM10 in Severe Staphylococcus aureus Skin Infection

Inoshima, N., Wang, Y., & Wardenburg, J. B. (2012) · Journal of Investigative Dermatology · doi:10.1038/jid.2011.462 · Cited by 110

ADAM10 is essential for proteolytic activation of Notch during thymocyte development

Tian, L., Wu, X., Chi, C., Han, M., Xu, T., & Zhuang, Y. (2008) · International Immunology · doi:10.1093/intimm/dxn076 · Cited by 108

ADAM 13: A Novel ADAM Expressed in Somitic Mesoderm and Neural Crest Cells duringXenopus laevisDevelopment

Alfandari, D., Wolfsberg, T. G., White, J. M., & DeSimone, D. W. (1997) · Developmental Biology · doi:10.1006/dbio.1996.8458 · Cited by 106

CD30 Shedding from Karpas 299 Lymphoma Cells Is Mediated by TNF-α-Converting Enzyme

Hansen, H. P., Dietrich, S., Kisseleva, T., Mokros, T., Mentlein, R., Lange, H. H., Murphy, G., & Lemke, H. (2000) · The Journal of Immunology · doi:10.4049/jimmunol.165.12.6703 · Cited by 105

GPCR-induced migration of breast carcinoma cells depends on both EGFR signal transactivation and EGFR-independent pathways

Hart, S., Fischer, O. M., Prenzel, N., Zwick-Wallasch, E., Schneider, M., Hennighausen, L. G., & Ullrich, A. (2005) · Biological Chemistry · doi:10.1515/bc.2005.099 · Cited by 105

ADAM 12 Protease Induces Adipogenesis in Transgenic Mice

Kawaguchi, N., Xu, X., Tajima, R., Kronqvist, P., Sundberg, C., Loechel, F., Albrechtsen, R., & Wewer, U. M. (2002) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)61136-4 · Cited by 105

Essential roles of Meltrin β (ADAM19) in heart development

Kurohara, K., Komatsu, K., Kurisaki, T., Masuda, A., Irie, N., Asano, M., Sudo, K., Nabeshima, Y.-I., Iwakura, Y., & Sehara‐Fujisawa, A. (2003) · Developmental Biology · doi:10.1016/j.ydbio.2003.10.021 · Cited by 103

ADAM9 Is Involved in Pathological Retinal Neovascularization

Guaiquil, V. H., Swendeman, S. L., Yoshida, T., Chavala, S. H., Campochiaro, P. A., & Blobel, C. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.01460-08 · Cited by 101

Extracellular Cleavage of Cadherin-11 by ADAM Metalloproteases Is Essential for Xenopus Cranial Neural Crest Cell Migration

McCusker, C., Cousin, H., Neuner, R., & Alfandari, D. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-05-0535 · Cited by 96

Biochemical properties and functions of membrane-anchored metalloprotease-disintegrin proteins (ADAMs)

Becherer, J. D., & Blobel, C. (2003) · Current topics in developmental biology/Current Topics in Developmental Biology · doi:10.1016/s0070-2153(03)54006-6 · Cited by 94

PACSIN3 Binds ADAM12/Meltrin α and Up-regulates Ectodomain Shedding of Heparin-binding Epidermal Growth Factor-like Growth Factor

Mori, S., Tanaka, M., Nanba, D., Nishiwaki, E., Ishiguro, H., Higashiyama, S., & Matsuura∥, N. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m306393200 · Cited by 94

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

ADAM10 as a Target for Anti-Cancer Therapy

Moss, M. L., Stoeck, A., Yan, W., & Dempsey, P. J. (2008) · Current Pharmaceutical Biotechnology · doi:10.2174/138920108783497613 · Cited by 92

Crystal Structure of the Catalytic Domain of Human ADAM33

Orth, P., Reichert, P., Wang, W., Prosise, W. W., Yarosh-Tomaine, T., Hammond, G., Ingram, R. N., Xiao, L., Mirza, U. A., Zou, J., et al. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2003.10.037 · Cited by 90

Loss of the Metalloprotease ADAM9 Leads to Cone-Rod Dystrophy in Humans and Retinal Degeneration in Mice

Parry, D. A., Toomes, C., Bida, L., Danciger, M., Towns, K. V., McKibbin, M., Jacobson, S. G., Logan, C. V., Ali, M., Bond, J., et al. (2009) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2009.04.005 · Cited by 89

Tumor Necrosis Factor-α (TNF-α) Regulates Shedding of TNF-α Receptor 1 by the Metalloprotease-Disintegrin ADAM8: Evidence for a Protease-Regulated Feedback Loop in Neuroprotection

Bartsch, J. W., Wildeboer, D., Koller, G., Naus, S., Rittger, A., Moss, M. L., Minai, Y., & Jockusch, H. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.1520-10.2010 · Cited by 89

Deletion of Adam10 in endothelial cells leads to defects in organ-specific vascular structures

Glomski, K., Monette, S., Manova, K., Strooper, B. D., Säftig, P., & Blobel, C. (2011) · Blood · doi:10.1182/blood-2011-04-348557 · Cited by 88

Identification of candidate substrates for ectodomain shedding by the metalloprotease-disintegrin ADAM8

Naus, S., Reipschläger, S., Wildeboer, D., Lichtenthaler, S. F., Mitterreiter, S., Guan, Z., Moss, M. L., & Bartsch, J. W. (2006) · Biological Chemistry · doi:10.1515/bc.2006.045 · Cited by 87

Upregulation of the α‐secretase ADAM10 – risk or reason for hope?

Endres, K., & Fahrenholz, F. (2010) · FEBS Journal · doi:10.1111/j.1742-4658.2010.07566.x · Cited by 84

The membrane‐proximal domain of A Disintegrin and Metalloprotease 17 (ADAM17) is responsible for recognition of the interleukin‐6 receptor and interleukin‐1 receptor II

Lorenzen, I., Lokau, J., Düsterhöft, S., Trad, A., Garbers, C., Scheller, J., Rose‐John, S., & Grötzinger, J. (2012) · FEBS Letters · doi:10.1016/j.febslet.2012.03.012 · Cited by 79

Cytoplasmic Relaxation of Active Eph Controls Ephrin Shedding by ADAM10

Janes, P. W., Wimmer-Kleikamp, S. H., Frangakis, A. S., Treble, K., Griesshaber, B., Sabet, O., Grabenbauer, M., Ting, A. Y., Säftig, P., Bastiaens, P. I. H., et al. (2009) · PLoS Biology · doi:10.1371/journal.pbio.1000215 · Cited by 78

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

The Metalloprotease-Disintegrin ADAM8 Is Essential for the Development of Experimental Asthma

Naus, S., Blanchet, M., Gossens, K., Zaph, C., Bartsch, J. W., McNagny, K. M., & Ziltener, H. J. (2010) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.200909-1396oc · Cited by 75

Regulation of ADAM12 Cell-surface Expression by Protein Kinase C ϵ

Sundberg, C., Thodeti, C. K., Kveiborg, M., Larsson, C., Parker, P. J., Albrechtsen, R., & Wewer, U. M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m403753200 · Cited by 73

Catalytic activity of ADAM28

Howard, L., Zheng, Y., Horrocks, M., Maciewicz, R. A., & Blobel, C. (2001) · FEBS Letters · doi:10.1016/s0014-5793(01)02506-6 · Cited by 73

The role of ADAMs in disease pathophysiology

Duffy, M. J., McKiernan, E., O’Donovan, N., & McGowan, P. M. (2009) · Clinica Chimica Acta · doi:10.1016/j.cca.2009.01.007 · Cited by 72

Distinct Functions of Natural ADAM-15 Cytoplasmic Domain Variants in Human Mammary Carcinoma

Zhong, J. L., Poghosyan, Z. P., Pennington, C. J., Scott, X., Handsley, M. M., Warn, A., Gavrilović, J., Honert, K., Krüger, A., Span, P. N., et al. (2008) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-07-2028 · Cited by 72

An Arginine Stretch Limits ADAM10 Exit from the Endoplasmic Reticulum

Marcello, E. E., Gardoni, F., Luca, M. D., & Pérez‐Otaño, I. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.055947 · Cited by 71

Intracellular Processing of Metalloprotease Disintegrin ADAM12

Cao, Y., Kang, Q., Zhao, Z., & Żółkiewska, A. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m110814200 · Cited by 70

UNC-71, a disintegrin and metalloprotease (ADAM) protein, regulates motor axon guidance and sex myoblast migration in C. elegans

Huang, X., Huang, P., Robinson, M. K., Stern, M., & Jin, Y. (2003) · Development · doi:10.1242/dev.00518 · Cited by 69

ADAM10 Inhibition of Human CD30 Shedding Increases Specificity of Targeted ImmunotherapyIn vitro

Eichenauer, D. A., Simhadri, V. L., von Strandmann, E. P., Ludwig, A., Matthews, V. B., Reiners, K. S., von Tresckow, B., Säftig, P., Rose‐John, S., Engert, A., et al. (2007) · Cancer Research · doi:10.1158/0008-5472.can-06-2470 · Cited by 68

ADAM13 Induces Cranial Neural Crest by Cleaving Class B Ephrins and Regulating Wnt Signaling

Wei, S., Xu, G., Bridges, L. C., Williams, P., White, J. M., & DeSimone, D. W. (2010) · Developmental Cell · doi:10.1016/j.devcel.2010.07.012 · Cited by 67

ADAM12 Alleviates the Skeletal Muscle Pathology in mdx Dystrophic Mice

Kronqvist, P., Kawaguchi, N., Albrechtsen, R., Xu, X., Schrøder, H. D., Moghadaszadeh, B., Nielsen, F. C., Fröhlich, C., Engvall, E., & Wewer, U. M. (2002) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)64431-8 · Cited by 66

Homeostatic effects of the metalloproteinase disintegrin ADAM15 in degenerative cartilage remodeling

Böhm, B. B., Aigner, T. G., Roy, B., Brodie, T. A., Blobel, C., & Burkhardt, H. (2005) · Arthritis & Rheumatism · doi:10.1002/art.20974 · Cited by 66

ADAM33 Is Not Essential for Growth and Development and Does Not Modulate Allergic Asthma in Mice

Chen, C., Huang, X., & Sheppard, D. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.00646-06 · Cited by 66

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

Intracellular Activation of Human Adamalysin 19/Disintegrin and Metalloproteinase 19 by Furin Occurs via One of the Two Consecutive Recognition Sites

Kang, T., Zhao, Y.-G., Pei, D., Sucic, J. F., & Sang, Q. A. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m203532200 · Cited by 64

A Basolateral Sorting Signal Directs ADAM10 to Adherens Junctions and Is Required for Its Function in Cell Migration

Wild‐Bode, C., Fellerer, K., Kugler, J., et al. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m601542200 · Cited by 64

Intramembrane Proteolysis by Signal Peptide Peptidases: A Comparative Discussion of GXGD-type Aspartyl Proteases

Fluhrer, R., Steiner, H., & Haass, C. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.r800040200 · Cited by 63

Mechanism of Xenopus cranial neural crest cell migration

Alfandari, D., Cousin, H., & Marsden, M. (2010) · Cell Adhesion & Migration · doi:10.4161/cam.4.4.12202 · Cited by 62

Disintegrin-like/Cysteine-Rich Region of ADAM 12 Is an Active Cell Adhesion Domain

Żółkiewska, A. (1999) · Experimental Cell Research · doi:10.1006/excr.1999.4632 · Cited by 62

ADAM8 is a negative regulator of retinal neovascularization and of the growth of heterotopically injected tumor cells in mice

Guaiquil, V. H., Swendeman, S. L., Zhou, W., Guaiquil, P., Weskamp, G., Bartsch, J. W., & Blobel, C. (2010) · Journal of Molecular Medicine · doi:10.1007/s00109-010-0591-8 · Cited by 62

Translocation of the Cytoplasmic Domain of ADAM13 to the Nucleus Is Essential for Calpain8-a Expression and Cranial Neural Crest Cell Migration

Cousin, H., Abbruzzese, G., Kerdavid, E., Gaultier, A., & Alfandari, D. (2011) · Developmental Cell · doi:10.1016/j.devcel.2010.12.009 · Cited by 61

Substrate Requirements for SPPL2b-dependent Regulated Intramembrane Proteolysis

Martin, L., Fluhrer, R., & Haass, C. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m807485200 · Cited by 60

Sea urchin metalloproteases: A genomic survey of the BMP-1/tolloid-like, MMP and ADAM families

Angerer, L. M., Hussain, S., Zheng, W., et al. (2006) · Developmental Biology · doi:10.1016/j.ydbio.2006.07.046 · Cited by 60

ADAM12: a potential target for the treatment of chronic wounds

Harsha, A. K., Stojadinović, O., Brem, H., Sehara‐Fujisawa, A., Wewer, U. M., Loomis, C. A., Blobel, C., & Tomic‐Canic, M. (2008) · Journal of Molecular Medicine · doi:10.1007/s00109-008-0353-z · Cited by 60

Evidence for functional redundancy between C. elegans ADAM proteins SUP-17/Kuzbanian and ADM-4/TACE

Jarriault, S., & Greenwald, I. (2005) · Developmental Biology · doi:10.1016/j.ydbio.2005.08.014 · Cited by 59

Accelerated Wound Repair in ADAM-9 Knockout Animals

Mauch, C., Zamek, J., Abety, A. N., Grimberg, G., Fox, J. W., & Zigrino, P. (2010) · Journal of Investigative Dermatology · doi:10.1038/jid.2010.60 · Cited by 56

Deficits in spatial learning and motor coordination in ADAM11-deficient mice

Takahashi, E., Sagane, K., Oki, T., Yamazaki, K., Nagasu, T., & Kuromitsu, J. (2006) · BMC Neuroscience · doi:10.1186/1471-2202-7-19 · Cited by 53

ADAM10 Overexpression Shifts Lympho- and Myelopoiesis by Dysregulating Site 2/Site 3 Cleavage Products of Notch

Gibb, D. R., Saleem, S. J., Kang, D.-J., Subler, M. A., & Conrad, D. H. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1003318 · Cited by 53

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

Positionally cloned asthma susceptibility gene polymorphisms and disease risk in the British 1958 Birth Cohort

Blakey, J., Sayers, I., Ring, S. M., Strachan, D. P., & Hall, I. P. (2009) · Thorax · doi:10.1136/thx.2008.102053 · Cited by 51

Identification and preliminary characterization of mouse Adam33

Gunn, T. M., Azarani, A., Kim, P. H., Hyman, R. W., Davis, R. W., & Barsh, G. S. (2002) · BMC Genetics · doi:10.1186/1471-2156-3-2 · Cited by 50

Xenopus ADAM19 is involved in neural, neural crest and muscle development

Neuner, R., Cousin, H., McCusker, C., Coyne, M. J., & Alfandari, D. (2008) · Mechanisms of Development · doi:10.1016/j.mod.2008.10.010 · Cited by 50

A potential new target for asthma therapy: A Disintegrin and Metalloprotease 10 (ADAM10) involvement in murine experimental asthma

Mathews, J. A., Ford, J. W., Norton, S. K., Kang, D., Dellinger, A. L., Gibb, D. R., Ford, A. Q., Massay, H., Kepley, C. L., Scherle, P., et al. (2011) · Allergy · doi:10.1111/j.1398-9995.2011.02614.x · Cited by 49

Meltrin β/ADAM19 Interacting with EphA4 in Developing Neural Cells Participates in Formation of the Neuromuscular Junction

Yumoto, N., Wakatsuki, S., Kurisaki, T., Hara, Y., Osumi, N., Frisén, J., & Sehara‐Fujisawa, A. (2008) · PLoS ONE · doi:10.1371/journal.pone.0003322 · Cited by 48

Role of Meltrin α (ADAM12) in Obesity Induced by High- Fat Diet

Masaki, M., Kurisaki, T., Shirakawa, K., et al. (2005) · Endocrinology · doi:10.1210/en.2004-1082 · Cited by 48

The waved with open eyelids (woe) Locus Is a Hypomorphic Mouse Mutation in Adam17

Hassemer, E. L., Gall, S. M. L., Liegel, R. P., McNally, M. T., Chang, B., Zeiss, C. J., Dubielzig, R. D., Horiuchi, K., Kimura, T., Okada, Y., et al. (2010) · Genetics · doi:10.1534/genetics.109.113167 · Cited by 47

Multimerisation of A disintegrin and metalloprotease protein-17 (ADAM17) is mediated by its EGF-like domain

Lorenzen, I., Trad, A., & Grötzinger, J. (2011) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2011.10.056 · Cited by 46

ADAM8 enhances osteoclast precursor fusion and osteoclast formation in vitro and in vivo

Ishizuka, H., Palacios, V. G., Lu, G., Subler, M. A., Zhang, H., Boykin, C., Choi, S. J., Zhao, L., Patrene, K. D., Galson, D. L., et al. (2010) · Journal of Bone and Mineral Research · doi:10.1002/jbmr.199 · Cited by 46

Connective tissue growth factor is a substrate of ADAM28

Mochizuki, S., Tanaka, R., Shimoda, M., Onuma, J., Fujii, Y., Jinno, H., & Okada, Y. (2010) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2010.10.077 · Cited by 45

The shedding protease ADAM17: Physiology and pathophysiology

Zunke, F., & Rose-John, S. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2017.07.001 · Cited by 336

Proteolytic ectodomain shedding of membrane proteins in mammals-hardware, concepts, and recent developments

Lichtenthaler, S. F., Lemberg, M. K., & Fluhrer, R. (2018) · The EMBO Journal · doi:10.15252/embj.201899456 · Cited by 323

Systematic substrate identification indicates a central role for the metalloprotease ADAM10 in axon targeting and synapse function

Kuhn, P.-H., Colombo, A. V., Schusser, B., Dreymueller, D., Wetzel, S., Schepers, U., Herber, J., Ludwig, A., Kremmer, E., Montag, D., et al. (2016) · eLife · doi:10.7554/elife.12748 · Cited by 163

Bace1 and Neuregulin‐1 cooperate to control formation and maintenance of muscle spindles

Cheret, C., Willem, M., Fricker, F. R., Wende, H., Wulf‐Goldenberg, A., Tahirovic, S., Nave, K., Saftig, P., Haass, C., Garratt, A. N., et al. (2013) · The EMBO Journal · doi:10.1038/emboj.2013.146 · Cited by 124

A systematic study of modulation of ADAM-mediated ectodomain shedding by site-specific O-glycosylation

Goth, C. K., Halim, A., Khetarpal, S. A., Rader, D. J., Clausen, H., & Schjoldager, K. T.-B. G. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1511175112 · Cited by 123