The Metalloprotease Disintegrin ADAM8

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 · see citing works

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., Clay, W. C., Didsbury, J. R., Hassler, D. F., Hoffman, C. R., et al. (1997) · Nature · doi:10.1038/385733a0 · Cited by 1,611 · see citing works

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 1,606 · see citing works

The cysteine switch: a principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family.

Van Wart, H. E., & Birkedal-Hansen, H. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.14.5578 · Cited by 1,475 · see citing works

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 1,132 · see citing works

A Novel Proteolytic Cleavage Involved in Notch Signaling

Brou, C., Logeat, F., Gupta-Rossi, N., Chable-Bessia, C., Bail, O. L., 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 1,089 · see citing works

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 933 · see citing works

TNF‐α converting enzyme (TACE) is inhibited by TIMP‐3

Amour, A., Slocombe, P. M., Webster, A., Butler, M., Knight, C. G., Smith, B. J., Stephens, P. E., Shelley, C., Hutton, M., Knäuper, V., et al. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)01031-x · Cited by 609 · see citing works

The ADAM gene family: surface proteins with adhesion and protease activity

Primakoff, P., & Myles, D. G. (2000) · Trends in Genetics · doi:10.1016/s0168-9525(99)01926-5 · Cited by 582 · see citing works

A metalloprotease–disintegrin, MDC9/meltrin‐γ/ADAM9 and PKCδ are involved in TPA‐induced ectodomain shedding of membrane‐anchored heparin‐binding EGF‐like growth factor

Izumi, Y., Hirata, M., Hasuwa, H., Iwamoto, R., Umata, T., Miyado, K., Tamai, Y., Kurisaki, T., Sehara‐Fujisawa, A., Ohno, S., et al. (1998) · The EMBO Journal · doi:10.1093/emboj/17.24.7260 · Cited by 521 · see citing works

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 480 · see citing works

The in vitro activity of ADAM‐10 is inhibited by TIMP‐1 and TIMP‐3

Amour, A., Knight, C. G., Webster, A., Slocombe, P. M., Stephens, P. E., Knäuper, V., Docherty, A., & Murphy, G. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)01528-3 · Cited by 404 · see citing works

Defining brain wiring patterns and mechanisms through gene trapping in mice

Leighton, P. A., Mitchell, K. J., Goodrich, L. V., Lu, X., Pinson, K. I., Scherz, P., Skarnes, W. C., & Tessier‐Lavigne, M. (2001) · Nature · doi:10.1038/35065539 · Cited by 391 · see citing works

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, K., Weskamp, G., Tempst, P., & Blobel, C. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.6.3531 · Cited by 315 · see citing works

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 · see citing works

Structural features of a superfamily of zinc-endopeptidases: the metzincins

Stöcker, W., & Bode, W. (1995) · Current Opinion in Structural Biology · doi:10.1016/0959-440x(95)80101-4 · Cited by 244 · see citing works

Regulation of the α‐secretase ADAM10 by its prodomain and proprotein convertases

Anders, A., Gilbert, S., Garten, W., Postina, R., & Fahrenholz, F. (2001) · The FASEB Journal · doi:10.1096/fj.01-0007fje · Cited by 241 · see citing works

A Role for Polyproline Motifs in the Spinal Muscular Atrophy Protein SMN

Giesemann, T., Rathke‐Hartlieb, S., Rothkegel, M., Bartsch, J. W., Buchmeier, S., Jockusch, B. M., & Jockusch, H. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.53.37908 · Cited by 234 · see citing works

Remarkable roles of proteolysis on and beyond the cell surface

Blobel, C. (2000) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(00)00139-3 · Cited by 231 · see citing works

Specific Interaction of the Recombinant Disintegrin-like Domain of MDC-15 (Metargidin, ADAM-15) with Integrin αvβ3

Zhang, X.-P., Kamata, T., Yokoyama, K., Puzon-McLaughlin, W., & Takada, Y. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.13.7345 · Cited by 211 · see citing works

Interaction of metargidin (ADAM-15) with αvβ3 and α5β1 integrins on different haemopoietic cells

Nath, D., Slocombe, P. M., Stephens, P. E., Warn, A., Hutchinson, G. R., Yamada, K. M., Docherty, A., & Murphy, G. (1999) · Journal of Cell Science · doi:10.1242/jcs.112.4.579 · Cited by 193 · see citing works

Meltrin γ (ADAM-9) mediates cellular adhesion through α6β1 integrin, leading to a marked induction of fibroblast cell motility

Nath, D., Slocombe, P. M., Webster, A., Stephens, P. E., Docherty, A., & Murphy, G. (2000) · Journal of Cell Science · doi:10.1242/jcs.113.12.2319 · Cited by 189 · see citing works

Human ADAM 12 (Meltrin α) Is an Active Metalloprotease

Loechel, F., Gilpin, B., Engvall, E., Albrechtsen, R., & Wewer, U. M. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.27.16993 · Cited by 187 · see citing works

Metargidin, a Membrane-anchored Metalloprotease-Disintegrin Protein with an RGD Integrin Binding Sequence

Krätzschmar, J., Lum, L., & Blobel, C. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.9.4593 · Cited by 170 · see citing works

Intracellular Maturation of the Mouse Metalloprotease Disintegrin MDC15

Lum, L., Reid, M. S., & Blobel, C. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.40.26236 · Cited by 166 · see citing works

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 · see citing works

The enzymatic activity of ADAM8 and ADAM9 is not regulated by TIMPs

Amour, A., Knight, C. G., English, W., Webster, A., Slocombe, P. M., Knäuper, V., Docherty, A., Becherer, J. D., Blobel, C., & Murphy, G. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)03047-8 · Cited by 150 · see citing works

Tumor Necrosis Factor α Induces a Metalloprotease-Disintegrin, ADAM8 (CD 156): Implications for Neuron–Glia Interactions during Neurodegeneration

Schlomann, U., Rathke‐Hartlieb, S., Yamamoto, S., Jockusch, H., & Bartsch, J. W. (2000) · Journal of Neuroscience · doi:10.1523/jneurosci.20-21-07964.2000 · Cited by 139 · see citing works

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 131 · see citing works

Molecular cloning of cDNA encoding MS2 antigen, a novel cell surface antigen strongly expressed in murine monocytic lineage

Yoshida, S., Setoguchi, M., Higuchi, Y., Akizuki, S., & Yamamoto, S. (1990) · International Immunology · doi:10.1093/intimm/2.6.585 · Cited by 124 · see citing works

Evidence for Distinct Serine Protease Activities with a Potential Role in Processing the Sperm Protein Fertilin

Lum, L., & Blobel, C. (1997) · Developmental Biology · doi:10.1006/dbio.1997.8609 · Cited by 112 · see citing works

ADAM8: A Novel Osteoclast Stimulating Factor

Choi, S. J., Han, J.-H., & Roodman, G. D. (2001) · Journal of Bone and Mineral Research · doi:10.1359/jbmr.2001.16.5.814 · Cited by 107 · see citing works

Complex, Two-way Traffic of Molecules Across the Membrane of the Endoplasmic Reticulum

Suzuki, T., Yan, Q., & Lennarz, W. J. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.17.10083 · Cited by 78 · see citing works

A Novel Metalloproteinase Associated with Brain Myelin Membranes

Chantry, A., Gregson, N. A., & Glynn, P. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)88226-x · Cited by 73 · see citing works

Cloning and chromosomal mapping of mouse ADAM11, ADAM22 and ADAM23

Sagane, K., Yamazaki, K., Mizui, Y., & Tanaka, I. (1999) · Gene · doi:10.1016/s0378-1119(99)00253-x · Cited by 66 · see citing works

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 60 · see citing works

Epitope Tag-Antibody Combination Useful for the Detection of Protein Expression in Prokaryotic and Eukaryotic Cells

Rüdiger, M., Jockusch, B. M., & Rothkegel, M. (1997) · BioTechniques · doi:10.2144/97231bm20 · Cited by 31 · see citing works

Expression and Purification of Correctly Processed, Active Human TACE Catalytic Domain inSaccharomyces cerevisiae

Clarke, H. R. G., Wolfson, M. F., Rauch, C. T., Castner, B. J., Huang, C.-P., GERHART, M. J., Johnson, R. S., Cerretti, D. P., Paxton, R. J., Price, V. L., et al. (1998) · Protein Expression and Purification · doi:10.1006/prep.1998.0861 · Cited by 25 · see citing works

The disintegrin domain of ADAM 8 enhances protection against rat experimental autoimmune encephalomyelitis, neuritis and uveitis by a polyvalent autoantigen vaccine

Schluesener, H. J. (1998) · Journal of Neuroimmunology · doi:10.1016/s0165-5728(98)00080-0 · Cited by 19 · see citing works

The ADAM metalloproteinases

Edwards, D. R., Handsley, M. M., & Pennington, C. (2008) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2008.08.001 · Cited by 1,165 · see citing works

ADAMs: key components in EGFR signalling and development

Blobel, C. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1548 · Cited by 1,091 · see citing works

The ADAMs family of metalloproteases: multidomain proteins with multiple functionsPreprint

Seals, D. F., & Courtneidge, S. A. (2003) · Genes & Development · doi:10.1101/gad.1039703 · Cited by 1,058 · see citing works

Genome analysis of the platypus reveals unique signatures of evolution

paper, A. L. O. A. A. T. A. A. A. T. E. O. T. (2008) · Nature · doi:10.1038/nature06936 · Cited by 719 · see citing works

ADAMs in cancer cell proliferation and progression

Mochizuki, S., & Okada, Y. (2007) · Cancer Science · doi:10.1111/j.1349-7006.2007.00434.x · Cited by 546 · see citing works

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

Reiß, K., & Säftig, P. (2008) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2008.11.002 · Cited by 424 · see citing works

Ectodomain shedding and ADAMs in development

Weber, S., & Säftig, P. (2012) · Development · doi:10.1242/dev.076398 · Cited by 259 · see citing works

Human matrix metalloproteinases: an ubiquitarian class of enzymes involved in several pathological processes.

Sbardella, D., Fasciglione, G., Gioia, M., Ciaccio, C., Tundo, G., Marini, S., & Coletta, M. (2012) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2011.10.015 · Cited by 247 · see citing works

The role of ADAM-mediated shedding in vascular biology

Yildiz, D., Pruessmeyer, J., Groth, E., & Ludwig, A. (2011) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2011.09.003 · Cited by 208 · see citing works

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 · see citing works

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 · see citing works

Control of ErbB signaling through metalloprotease mediated ectodomain shedding of EGF-like factors

Sanderson, M. P., Dempsey, P. J., & Dunbar, A. J. (2006) · Growth Factors · doi:10.1080/08977190600634373 · Cited by 150 · see citing works

ADAM8 as a Novel Serological and Histochemical Marker for Lung Cancer

Ishikawa, N., Daigo, Y., Yasui, W., Inai, K., Nishimura, H., Tsuchiya, E., Kohno, N., & Nakamura, Y. (2004) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-04-1436 · Cited by 149 · see citing works

Metalloproteinase Disintegrins ADAM8 and ADAM19 Are Highly Regulated in Human Primary Brain Tumors and their Expression Levels and Activities Are Associated with Invasiveness

Wildeboer, D., Naus, S., Sang, Q. A., Bartsch, J. W., & Pagenstecher, A. (2006) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/01.jnen.0000229240.51490.d3 · Cited by 148 · see citing works

ADAM-family metalloproteinases in lung inflammation: potential therapeutic targets

Yildiz, D., Uhlig, S., & Ludwig, A. (2014) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00294.2014 · Cited by 140 · see citing works

Breaking up the tie: Disintegrin-like metalloproteinases as regulators of cell migration in inflammation and invasion

Reiß, K., Ludwig, A., & Säftig, P. (2006) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2006.02.009 · Cited by 138 · see citing works

Functions of ‘A disintegrin and metalloproteases (ADAMs)’ in the mammalian nervous system

Hsia, H., Tüshaus, J., Brummer, T., Zheng, Y., Scilabra, S. D., & Lichtenthaler, S. F. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03173-7 · Cited by 133 · see citing works

Ectodomain Shedding of the Neural Recognition Molecule CHL1 by the Metalloprotease-disintegrin ADAM8 Promotes Neurite Outgrowth and Suppresses Neuronal Cell Death

Naus, S., Richter, M., Wildeboer, D., Moss, M. L., Schachner, M., & Bartsch, J. W. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m400560200 · Cited by 128 · see citing works

ADAM8 as a drug target in pancreatic cancer

Schlomann, U., Koller, G., Conrad, C., Ferdous, T., Golfi, P., Garcia, A. M., Höfling, S., Parsons, M., Costa, P., Soper, R., et al. (2015) · Nature Communications · doi:10.1038/ncomms7175 · Cited by 121 · see citing works

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 · see citing works

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 · see citing works

A Disintegrin and Metalloproteinase (ADAM) and ADAM with thrombospondin motifs (ADAMTS) family in vascular biology and disease

Zhong, S., & Khalil, R. A. (2019) · Biochemical Pharmacology · doi:10.1016/j.bcp.2019.03.033 · Cited by 119 · see citing works

Extracellular proteolysis in cancer: Proteases, substrates, and mechanisms in tumor progression and metastasis

Radisky, E. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.107347 · Cited by 112 · see citing works

Catalytic Activity of Human ADAM33

Zou, J., Zhu, F., Liu, J., Wang, W., Zhang, R., Garlisi, C. G., Liu, Y., Wang, S., Shah, H., Wan, Y., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m309696200 · Cited by 118 · see citing works

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 116 · see citing works

ADAM8 expression in invasive breast cancer promotes tumor dissemination and metastasis

Romagnoli, M., Mineva, N. D., Polmear, M. M., Conrad, C., Srinivasan, S. S., Loussouarn, D., Barillé‐Nion, S., Georgakoudi, I., Dagg, Á., McDermott, E. W. M., et al. (2013) · EMBO Molecular Medicine · doi:10.1002/emmm.201303373 · Cited by 110 · see citing works

The Role of Adams in Notch Signaling

Groot, A. J., & Vooijs, M. (2012) · Advances in experimental medicine and biology · doi:10.1007/978-1-4614-0899-4_2 · Cited by 103 · see citing works

ADAM8 expression is associated with increased invasiveness and reduced patient survival in pancreatic cancer

Valkovskaya, N., Kayed, H., Felix, K., Hartmann, D., Giese, N. A., Osinsky, S., Friess, H., & Kleeff, J. H. (2007) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2007.00082.x · Cited by 93 · see citing works

Metalloproteinase Expression in PMA-stimulated THP-1 Cells

Worley, J. R., Baugh, M. D., Hughes, D. A., Edwards, D. R., Hogan, A., Sampson, M., & Gavrilović, J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m310865200 · Cited by 92 · see citing works

Evolutionary divergence and functions of the ADAM and ADAMTS gene families

Brocker, C. N., Vasiliou, V., & Nebert, D. W. (2009) · Human Genomics · doi:10.1186/1479-7364-4-1-43 · Cited by 90 · see citing works

The Functional Maturation of A Disintegrin and Metalloproteinase (ADAM) 9, 10, and 17 Requires Processing at a Newly Identified Proprotein Convertase (PC) Cleavage Site

Wong, E., Maretzky, T., Peleg, Y., Blobel, C., & Sagi, I. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.624072 · Cited by 92 · see citing works

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 · see citing works

Protease propeptide structures, mechanisms of activation, and functions

Boon, L., Ugarte-Berzal, E., Vandooren, J., & Opdenakker, G. (2020) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2020.1742090 · Cited by 91 · see citing works

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 · see citing works

ADAM8 in invasive cancers: links to tumor progression, metastasis, and chemoresistance

Conrad, C., Benzel, J., Dorzweiler, K., Cook, L., Schlomann, U., Zarbock, A., Slater, E. P., Nimsky, C., & Bartsch, J. W. (2019) · Clinical Science · doi:10.1042/cs20180906 · Cited by 86 · see citing works

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 · see citing works

Blocking of the P2X7 receptor inhibits the activation of the MMP-13 and NF-κB pathways in the cartilage tissue of rats with osteoarthritis

Hu, H., Yang, B., Li, Y., Zhang, S., & Li, Z. (2016) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2016.2770 · Cited by 69 · see citing works

Two separate metalloproteinase activities are responsible for the shedding and processing of the NG2 proteoglycan in vitro

Asher, R. A., Morgenstern, D. A., Properzi, F., Nishiyama, A., Levine, J. M., & Fawcett, J. W. (2005) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2005.02.001 · Cited by 69 · see citing works

ADAM8 is selectively up‐regulated in endothelial cells and is associated with angiogenesis after spinal cord injury in adult mice

Mahoney, E. T., Benton, R. L., Maddie, M. A., Whittemore, S. R., & Hagg, T. (2008) · The Journal of Comparative Neurology · doi:10.1002/cne.21902 · Cited by 65 · see citing works

Degradome of soluble ADAM10 and ADAM17 metalloproteases

Scharfenberg, F., Helbig, A. O., Sammel, M., Benzel, J., Schlomann, U., Peters, F., Wichert, R., Bettendorff, M., Schmidt‐Arras, D., Rose‐John, S., et al. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03184-4 · Cited by 65 · see citing works

Role of ADAM and ADAMTS metalloproteinases in airway diseases

Paulissen, G., Rocks, N., Gueders, M. M., Crahay, C., Quesada‐Calvo, F., Bekaert, S., Hacha, J., Hour, M. E., Foidart, J., Noël, A., et al. (2009) · Respiratory Research · doi:10.1186/1465-9921-10-127 · Cited by 64 · see citing works

Different ADAMs have distinct influences on Kit ligand processing: phorbol-ester-stimulated ectodomain shedding of Kitl1 by ADAM17 is reduced by ADAM19

Kawaguchi, N., Horiuchi, K., Becherer, J. D., Toyama, Y., Besmer, P., & Blobel, C. (2007) · Journal of Cell Science · doi:10.1242/jcs.03403 · Cited by 64 · see citing works

ADAMs family and relatives in cardiovascular physiology and pathology

Zhang, P., Shen, M., Fernández-Patrón, C., & Kassiri, Z. (2015) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2015.10.031 · Cited by 63 · see citing works

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 60 · see citing works

Bifunctional Role of theTreponema pallidumExtracellular Matrix Binding Adhesin Tp0751

Houston, S., Hof, R., Francescutti, T., Hawkes, A. R., Boulanger, M. J., & Cameron, C. E. (2010) · Infection and Immunity · doi:10.1128/iai.01083-10 · Cited by 60 · see citing works

What is the Future of Diabetic Wound Care?

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(Make) Stick and cut loose—Disintegrin metalloproteases in development and disease

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ADAM proteins in the brain

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Processing of Snake Venom Metalloproteinases: Generation of Toxin Diversity and Enzyme Inactivation

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miR-720 is a downstream target of an ADAM8-induced ERK signaling cascade that promotes the migratory and invasive phenotype of triple-negative breast cancer cells

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The Balance Between Metalloproteinases and TIMPs

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Characterization of the catalytic activity of the membrane-anchored metalloproteinase ADAM15 in cell-based assays

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ADAM8 signaling drives neutrophil migration and ARDS severity

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ADAM8: a new therapeutic target for asthma

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ADAM‐8 isolated from human osteoarthritic chondrocytes cleaves fibronectin at Ala 271

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Novel alternatively spliced ADAM8 isoforms contribute to the aggressive bone metastatic phenotype of lung cancer

Hernandez, I. M., Moreno, J. L., Zandueta, C., Montuenga, L. M., & Lecanda, F. (2010) · Oncogene · doi:10.1038/onc.2010.130 · Cited by 50 · see citing works

Matrix metalloproteinase profiling and their roles in disease

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Role of ADAM8 in experimental asthma

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Microarray analysis of peroxisome proliferator-activated receptor-γ induced changes in gene expression in macrophages

Hodgkinson, C. P., & Ye, S. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(03)01416-5 · Cited by 51 · see citing works

ADAM8 expression in prostate cancer is associated with parameters of unfavorable prognosis

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ADAM 9 contributes to vascular invasion in pancreatic ductal adenocarcinoma

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Regulated Expression of ADAM8 (a Disintegrin and Metalloprotease Domain 8) in the Mouse Ovary: Evidence for a Regulatory Role of Luteinizing Hormone, Progesterone Receptor, and Epidermal Growth Factor-Like Growth Factors1

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The detection of ADAM8 protein on cells of the human immune system and the demonstration of its expression on peripheral blood B cells, dendritic cells and monocyte subsets

Richens, J. L., Fairclough, L. C., Ghaemmaghami, A. M., Mahdavi, J., Shakib, F., & SEWELL, H. (2006) · Immunobiology · doi:10.1016/j.imbio.2006.06.012 · Cited by 42 · see citing works

ADAM23 is a cell‐surface glycoprotein expressed by central nervous system neurons

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Involvement of a disintegrin and a metalloproteinase 8 (ADAM8) in osteoclastogenesis and pathological bone destruction

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A novel peptide ADAM8 inhibitor attenuates bronchial hyperresponsiveness and Th2 cytokine mediated inflammation of murine asthmatic models

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The metalloprotease ADAM8 is associated with and regulates the function of the adhesion receptor PSGL‐1 through ERM proteins

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ADAM‐8, a metalloproteinase, drives acute allergen‐induced airway inflammation

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Sputum ADAM 8 expression is increased in severe asthma and COPD

Oreo, K. M., Gibson, P. G., Simpson, J. L., Wood, L. G., McDonald, V. M., & Baines, K. J. (2013) · Clinical & Experimental Allergy · doi:10.1111/cea.12223 · Cited by 39 · see citing works

Heparan Sulfate Regulates ADAM12 through a Molecular Switch Mechanism

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Identification of genes that are induced after cadmium exposure by suppression subtractive hybridization

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Abundance of ADAM-8, -9, -10, -12, -15 and -17 and ADAMTS-1 in mouse uterus during the oestrous cycle

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The emerging role of matrix metalloproteases of the ADAM family in male germ cell apoptosis

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Elevated Soluble ADAM8 in Bronchoalveolar Lavage Fluid in Patients with Eosinophilic Pneumonia

Matsuno, O., Miyazaki, E., Nureki, S., Ueno, T., Ando, M., Ito, K., Kumamoto, T., & Higuchi, Y. (2006) · International Archives of Allergy and Immunology · doi:10.1159/000097359 · Cited by 36 · see citing works

The versatile roles of ADAM8 in cancer cell migration, mechanics, and extracellular matrix remodeling

Mierke, C. T. (2023) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2023.1130823 · Cited by 34 · see citing works

Fluorescent Substrates Useful as High Throughput Screening Tools for ADAM9

Moss, M. L., Rasmussen, F., Nudelman, R., Dempsey, P. J., & Williams, J. G. (2010) · Combinatorial Chemistry & High Throughput Screening · doi:10.2174/138620710791054259 · Cited by 35 · see citing works

Unraveling the Processing and Activation of Snake Venom Metalloproteinases

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Implication of ADAM-8, -9, -10, -12, -15, -17, and ADAMTS-1 in Implantational Remodeling of a Mouse Uterus

Kim, J., Kang, S. G., Kim, J., Park, J. H., Kim, S. K., Cho, D. J., & Kim, H. (2006) · Yonsei Medical Journal · doi:10.3349/ymj.2006.47.4.558 · Cited by 33 · see citing works

Loss of Vps54 Function Leads to Vesicle Traffic Impairment, Protein Mis-Sorting and Embryonic Lethality

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The facial motor nucleus transcriptional program in response to peripheral nerve injury identifies Hn1 as a regeneration‐associated gene

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Fine Tuning Cell Migration by a Disintegrin and Metalloproteinases

Yildiz, D., Theodorou, K., Donners, M. M. P. C., & Ludwig, A. (2017) · Mediators of Inflammation · doi:10.1155/2017/9621724 · Cited by 31 · see citing works

The Murine Goblet Cell Protein mCLCA3 Is a Zinc-Dependent Metalloprotease with Autoproteolytic Activity

Bothe, M. K., Mundhenk, L., Kaup, M., Weise, C., & Gruber, A. D. (2011) · Molecules and Cells · doi:10.1007/s10059-011-0158-8 · Cited by 31 · see citing works

ADAMDEC1 Is a Metzincin Metalloprotease with Dampened Proteolytic Activity

Lund, J., Olsen, O. H., Sørensen, E. S., Stennicke, H. R., Petersen, H. H., & Overgaard, M. T. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.474536 · Cited by 31 · see citing works

ADAM Metalloproteinases as Potential Drug Targets

Camodeca, C., Cuffaro, D., Nuti, E., & Rossello, A. (2018) · Current Medicinal Chemistry · doi:10.2174/0929867325666180326164104 · Cited by 29 · see citing works

Expression levels of the metalloproteinase ADAM8 critically regulate proliferation, migration and malignant signalling events in hepatoma cells

Awan, T., Babendreyer, A., Alvi, A. M., Düsterhöft, S., Lambertz, D., Bartsch, J. W., Liedtke, C., & Ludwig, A. (2020) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.16015 · Cited by 29 · see citing works

Macrophage differentiation of myeloid progenitor cells in response to M-CSF is regulated by the dual-specificity phosphatase DUSP5

Grasset, M.-F., Gobert, S., Mouchiroud, G., & Bourette, R. P. (2009) · Journal of Leukocyte Biology · doi:10.1189/jlb.0309151 · Cited by 29 · see citing works

IL ‐5‐stimulated eosinophils adherent to periostin undergo stereotypic morphological changes and ADAM 8‐dependent migration

Johansson, M. W., Khanna, M., Bortnov, V., Annis, D. S., Nguyen, C. L., & Mosher, D. F. (2017) · Clinical & Experimental Allergy · doi:10.1111/cea.12934 · Cited by 29 · see citing works

SheddomeDB: the ectodomain shedding database for membrane-bound shed markers

Tien, W.-S., Chen, J., & Wu, K. (2017) · BMC Bioinformatics · doi:10.1186/s12859-017-1465-7 · Cited by 28 · see citing works

Regulation of Fibrotic Processes in the Liver by ADAM Proteases

Schmidt‐Arras, D., & Rose‐John, S. (2019) · Cells · doi:10.3390/cells8101226 · Cited by 27 · see citing works

Leukocyte Membrane Enzymes Play the Cell Adhesion Game

López-Cortés, G. I., Díaz-Alvarez, L., & Ortega, E. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.742292 · Cited by 26 · see citing works

Prodomain‐dependent tissue targeting of an ADAMTS protease controls cell migration in Caenorhabditis elegans

Ihara, S., & Nishiwaki, K. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601718 · Cited by 26 · see citing works

ADAM Proteases in Cancer: Biological Roles, Therapeutic Challenges, and Emerging Opportunities

Arora, S., Scott, A. M., & Janes, P. W. (2025) · Cancers · doi:10.3390/cancers17101703 · Cited by 25 · see citing works

N-Glycosylation Regulates ADAM8 Processing and Activation

Srinivasan, S. S., Romagnoli, M., Bohm, A., & Sonenshein, G. E. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.594242 · Cited by 24 · see citing works

ADAM8 and its single nucleotide polymorphism 2662 T/G are associated with advanced atherosclerosis and fatal myocardial infarction: Tampere vascular study

Levula, M., Airla, N., Oksala, N., Hernesniemi, J. A., Pelto‐Huikko, M., Salenius, J., Zeitlin, R., Järvinen, O., Huovila, A. J., Nikkari, S. T., et al. (2009) · Annals of Medicine · doi:10.1080/07853890903025945 · Cited by 24 · see citing works

Introduction to the ADAM Family

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Autoactivation of human ADAM8: a novel pre-processing step is required for catalytic activity

Hall, T., Leone, J. W., Wiese, J. F., Griggs, D. W., Pegg, L. E., Pauley, A. M., Tomasselli, A. G., & Zack, M. D. (2008) · Bioscience Reports · doi:10.1042/bsr20080145 · Cited by 23 · see citing works

ADAM proteases, ErbB pathways and cancer

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Deregulated PSGL-1 Expression in B Cells and Dendritic Cells May Be Implicated in Human Systemic Sclerosis Development

Silván, J., Rafael, G.-T., Vicente‐Rabaneda, E. F., Pérez-Frías, A., Espartero‐Santos, M., Muñoz‐Callejas, A., García-Lorenzo, E., Gamallo, C., Castañeda, S., & Urzainqui, A. (2018) · Journal of Investigative Dermatology · doi:10.1016/j.jid.2018.04.003 · Cited by 22 · see citing works

Notch1-ADAM8 positive feed-back loop regulates the degradation of chondrogenic extracellular matrix and osteoarthritis progression

Duan, B., Liu, Y., Hu, H., Shi, F.-G., Liu, Y.-L., Xue, H., Yun, X.-Y., Yan, M., Han, X.-R., Chen, A.-F., et al. (2019) · Cell Communication and Signaling · doi:10.1186/s12964-019-0443-2 · Cited by 22 · see citing works

Reduced incidence and severity of experimental autoimmune arthritis in mice expressing catalytically inactive A disintegrin and metalloproteinase 8 (ADAM8)

Zack, M. D., Melton, M. A., Stock, J. L., Storer, C. E., Barve, R. A., Minnerly, J. C., Weiss, D. J., Stejskal, J. A., Tortorella, M. D., Turk, J. R., et al. (2009) · Clinical & Experimental Immunology · doi:10.1111/j.1365-2249.2009.04009.x · Cited by 22 · see citing works

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 131 · see citing works

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 · see citing works

Reinigung und funktionelle Charakterisierung von rekombinanter humaner Protease ADAM8

Yu, X. (2015) · open_UMR Marburg DSpace 10.0 (Philipps-Universität Marburg) · doi:10.17192/z2015.0272

ADAM8

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Autoactivation of human ADAM8: a novel pre-processing step is required for catalytic activity

Hall, T., Leone, J. W., Wiese, J. F., Griggs, D. W., Pegg, L. E., Pauley, A. M., Tomasselli, A. G., & Zack, M. D. (2008) · Bioscience Reports · doi:10.1042/bsr20080145 · Cited by 23 · see citing works