Metalloproteinases and their natural inhibitors in inflammation and immunity

Matrix Metalloproteinases and Tissue Inhibitors of Metalloproteinases: Structure, Function, and Biochemistry

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Structure and function of matrix metalloproteinases and TIMPs

Nagase, H., Visse, R., & MURPHY, G. (2006) · Cardiovascular Research · doi:10.1016/j.cardiores.2005.12.002 · Cited by 3,507

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

Defensins: antimicrobial peptides of innate immunity

Ganz, T. (2003) · Nature Reviews Immunology · doi:10.1038/nri1180 · Cited by 3,066

Inflammasomes in health and disease

Strowig, T., Henao-Mejia, J., Elinav, E., & Flavell, R. (2012) · Nature · doi:10.1038/nature10759 · Cited by 2,230

Tumour-derived soluble MIC ligands impair expression of NKG2D and T-cell activation

Groh, V., Wu, J. D., Yee, C., & Spies, T. (2002) · Nature · doi:10.1038/nature01112 · Cited by 1,674

An Essential Role for Ectodomain Shedding in Mammalian Development

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

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The transmembrane form of tumor necrosis factor is the prime activating ligand of the 80 kDa tumor necrosis factor receptor

Grell, M., Douni, E. K., Wajant, H., Löhden, M., Clauss, M. A., Maxeiner, B., Georgopoulos, S., Lesslauer, W., Kollias, G. A., Pfizenmaier, K., et al. (1995) · Cell · doi:10.1016/0092-8674(95)90192-2 · Cited by 1,328

Innate lymphoid cells promote lung-tissue homeostasis after infection with influenza virus

Monticelli, L. A., Sonnenberg, G. F., Abt, M. C., Alenghat, T., Ziegler, C. G. K., Doering, T. A., Angelosanto, J., Laidlaw, B. J., Yang, C. Y., Sathaliyawala, T., et al. (2011) · Nature Immunology · doi:10.1038/ni.2131 · Cited by 1,327

COLLAGENOLYTIC ACTIVITY IN AMPHIBIAN TISSUES: A TISSUE CULTURE ASSAY

Gross, J., & Lapiere, C. M. (1962) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.48.6.1014 · Cited by 1,325

MT1-MMP-Deficient Mice Develop Dwarfism, Osteopenia, Arthritis, and Connective Tissue Disease due to Inadequate Collagen Turnover

Holmbeck, K., Bianco, P., Caterina, J., Yamada, S., Kromer, M., Kuznetsov, S. A., Mankani, M., Gehron Robey, P., Poole, A. R., Pidoux, I., et al. (1999) · Cell · doi:10.1016/s0092-8674(00)80064-1 · Cited by 1,298

Innate lymphoid cells promote lung-tissue homeostasis after infection with influenza virus

Monticelli (2011) · PubMed · doi:10.1031/ni.2131 · Cited by 1,286

Enteric defensins are essential regulators of intestinal microbial ecology

Salzman, N. H., Hung, K., Haribhai, D., Chu, H., Karlsson-Sjöberg, J., Amir, E., Teggatz, P., Barman, M., Hayward, M., Eastwood, D., et al. (2010) · Nature Immunology · doi:10.1038/ni.1825 · Cited by 1,156

The interleukin-6 receptor as a target for prevention of coronary heart disease: a mendelian randomisation analysis

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Reactive oxygen species produced by macrophage-derived foam cells regulate the activity of vascular matrix metalloproteinases in vitro. Implications for atherosclerotic plaque stability.

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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 1,115

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

Şahin, U., Weskamp, G., Kelly, K., Zhou, H., Higashiyama, S., Peschon, J. J., Hartmann, D., Säftig, P., & Blobel, C. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200307137 · Cited by 1,013

Interleukin-6 receptor pathways in coronary heart disease: a collaborative meta-analysis of 82 studies

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Inflammation Dampened by Gelatinase A Cleavage of Monocyte Chemoattractant Protein-3

McQuibban, G. A., Gong, J.-H., Tam, E. M., McCulloch, C. A., Clark‐Lewis, I., & Overall, C. M. (2000) · Science · doi:10.1126/science.289.5482.1202 · Cited by 772

Matrilysin Shedding of Syndecan-1 Regulates Chemokine Mobilization and Transepithelial Efflux of Neutrophils in Acute Lung Injury

Li, Q., Park, P. W., Wilson, C. L., & Parks, W. C. (2002) · Cell · doi:10.1016/s0092-8674(02)01079-6 · Cited by 752

Therapeutic strategies for the clinical blockade of IL-6/gp130 signaling

Jones, S. A., Scheller, J., & Rose‐John, S. (2011) · Journal of Clinical Investigation · doi:10.1172/jci57158 · Cited by 689

Sequence of human tissue inhibitor of metalloproteinases and its identity to erythroid-potentiating activity

Docherty, A., Lyons, A., Smith, B. J., Wright, E. M., Stephens, P. E., Harris, T. J. R., Murphy, G., & Reynolds, J. J. (1985) · Nature · doi:10.1038/318066a0 · Cited by 689

Neutrophil gelatinase B potentiates interleukin-8 tenfold by aminoterminal processing, whereas it degrades CTAP-III, PF-4, and GRO-α and leaves RANTES and MCP-2 intact

den Steen, P. E. V., Proost, P., Wuyts, A., Damme, J. V., & Opdenakker, G. (2000) · Blood · doi:10.1182/blood.v96.8.2673 · Cited by 680

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

The regulation of matrix metalloproteinases and their inhibitors

Clark, I. M., Swingler, T. E., Sampieri, C. L., & Edwards, D. R. (2008) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2007.12.006 · Cited by 555

Gelatinase B functions as regulator and effector in leukocyte biology

Opdenakker, G., Van den Steen, P. E., Dubois, B., Nelissen, I., Van Coillie, E., Masure, S., Proost, P., & Van Damme, J. (2001) · Journal of Leukocyte Biology · doi:10.1189/jlb.69.6.851 · Cited by 553

Hypochlorous Acid Oxygenates the Cysteine Switch Domain of Pro-matrilysin (MMP-7)

Fu, X., Kassim, S. Y., Parks, W. C., & Heinecke, J. W. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m106958200 · Cited by 482

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

Adrain, C., Zettl, M., Christova, Y., Taylor, N. A., & Freeman, M. (2012) · Science · doi:10.1126/science.1214400 · Cited by 415

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

Disulphide-isomerase-enabled shedding of tumour-associated NKG2D ligands

Kaiser, B., Yim, D., Chow, I.-T., González, S., Dai, Z., Mann, H. H., Strong, R., Groh, V., & Spies, T. (2007) · Nature · doi:10.1038/nature05768 · Cited by 403

TNF receptor 1 genetic risk mirrors outcome of anti-TNF therapy in multiple sclerosis

Gregory, A., Dendrou, C. A., Attfield, K. E., Haghikia, A., Xifara, D. K., Butter, F., Poschmann, G., Kaur, G., Lambert, L., Leach, O. A., et al. (2012) · Nature · doi:10.1038/nature11307 · Cited by 395

Colon-specific delivery of a probiotic-derived soluble protein ameliorates intestinal inflammation in mice through an EGFR-dependent mechanism

Yan, F., Cao, H., Cover, T. L., Washington, M. K., Shi, Y., Liu, L., Chaturvedi, R., Peek, R. M., Wilson, K. T., & Polk, D. B. (2011) · Journal of Clinical Investigation · doi:10.1172/jci44031 · Cited by 386

Analyses of all matrix metalloproteinase members in leukocytes emphasize monocytes as major inflammatory mediators in multiple sclerosis

Bar‐Or, A. (2003) · Brain · doi:10.1093/brain/awg285 · Cited by 367

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. S., Xu, H. C., et al. (2012) · Science · doi:10.1126/science.1214448 · Cited by 327

Selective Use of ADAM10 and ADAM17 in Activation of Notch1 Signaling

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

Inflammatory Skin and Bowel Disease Linked toADAM17Deletion

Blaydon, D. C., Biancheri, P., Di, W., Plagnol, V., Cabral, R. M., Brooke, M. A., van Heel, D. A., Rüschendorf, F., Toynbee, M., Walne, A. J., et al. (2011) · New England Journal of Medicine · doi:10.1056/nejmoa1100721 · Cited by 307

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

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

Abnormal TNF activity in Timp3−/− mice leads to chronic hepatic inflammation and failure of liver regeneration

Mohammed, F. F., Smookler, D. S., Taylor, S. E. M., Fingleton, B., Kassiri, Z., Sanchez, O. H., English, J. L., Matrisian, L. M., Au, B., Yeh, W., et al. (2004) · Nature Genetics · doi:10.1038/ng1413 · Cited by 290

Increased inflammation delays wound healing in mice deficient in collagenase‐2 (MMP‐8)

Gutiérrez‐Fernández, A., Inada, M., Balbı́n, M., Fueyo, A., Pitiot, A. S., Astudillo, A., Hirose, K., Hirata, M., Shapiro, S. D., Noël, A., et al. (2007) · The FASEB Journal · doi:10.1096/fj.06-7860com · Cited by 289

Metalloprotease ADAM10 Is Required for Notch1 Site 2 Cleavage

van Tetering, G., van Diest, P. J., Verlaan-Klink, I., van der Wall, E., Kopan, R., & Vooijs, M. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.006775 · Cited by 274

Molecular characterization and expression of the gene encoding human erythroid-potentiating activity

Gasson, J. C., Golde, D. W., Kaufman, S., Westbrook, C. A., Hewick, R. M., Kaufman, R. J., Wong, G. G., Temple, P. A., Leary, A. C., Brown, E. L., et al. (1985) · Nature · doi:10.1038/315768a0 · Cited by 273

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

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

Macrophage-specific metalloelastase (MMP-12) truncates and inactivates ELR+ CXC chemokines and generates CCL2, -7, -8, and -13 antagonists: potential role of the macrophage in terminating polymorphonuclear leukocyte influx

Dean, R. A., Cox, J. H., Bellac, C. L., Doucet, A., Starr, A. E., & Overall, C. M. (2008) · Blood · doi:10.1182/blood-2007-12-129080 · Cited by 257

Purification and identification of 91‐kDa neutrophil gelatinase

Masure, S., Proost, P., Damme, J. V., & Opdenakker, G. (1991) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1991.tb16027.x · Cited by 253

Fever-range thermal stress promotes lymphocyte trafficking across high endothelial venules via an interleukin 6 trans-signaling mechanism

Chen, Q., Fisher, D. T., CLANCY, K. A., Gauguet, J.-M., Wang, W., Unger, E., Rose‐John, S., von Andrian, U. H., Baumann, H., & Evans, S. S. (2006) · Nature Immunology · doi:10.1038/ni1406 · Cited by 233

Induction of a MT1-MMP and MT2-MMP-dependent basement membrane transmigration program in cancer cells by Snail1

Ota, I., Li, X.-Y., Hu, Y., & Weiss, S. J. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0910962106 · Cited by 232

L-selectin: mechanisms and physiological significance of ectodomain cleavage

Smalley, D. M., & Ley, K. F. (2005) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2005.tb00354.x · Cited by 232

LPS Responsiveness and Neutrophil Chemotaxis In Vivo Require PMN MMP-8 Activity

Tester, A. M., Cox, J. H., Connor, A. R., Starr, A. E., Dean, R. A., Puente, X. S., López-Otı́n, C., & Overall, C. M. (2007) · PLoS ONE · doi:10.1371/journal.pone.0000312 · Cited by 214

Human Neutrophils Secrete Gelatinase B In Vitro and In Vivo in Response to Endotoxin and Proinflammatory Mediators

Pugin, J., Widmer, M.-C., Kossodo, S. D., Liang, C.-M., Preas, H. L., & Suffredini, A. F. (1999) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/ajrcmb.20.3.3311 · Cited by 212

Direct Proteomic Quantification of the Secretome of Activated Immune Cells

Meissner, F., Scheltema, R. A., Mollenkopf, H., & Mann, M. (2013) · Science · doi:10.1126/science.1232578 · Cited by 207

Matrix metalloprotease 9 mediates neutrophil migration into the airways in response to influenza virus-induced toll-like receptor signaling

Bradley, L. M., Douglass, M. F., Chatterjee, D., Akira, S., & Baaten, B. J. G. (2012) · PLoS Pathogens · doi:10.1371/journal.ppat.1002641 · Cited by 207

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

Classical Macrophage Activation Up-Regulates Several Matrix Metalloproteinases through Mitogen Activated Protein Kinases and Nuclear Factor-κB

Huang, W., Sala‐Newby, G. B., Susana, A., Johnson, J. L., & Newby, A. C. (2012) · PLoS ONE · doi:10.1371/journal.pone.0042507 · Cited by 200

Inactivation of tissue inhibitor of metalloproteinases by neutrophil elastase and other serine proteinases

Okada, Y., Watanabe, S., Nakanishi, I., Kishi, J.-I., Hayakawa, T., Wątorek, W., Travis, J. W., & Nagase, H. (1988) · FEBS Letters · doi:10.1016/0014-5793(88)80817-2 · Cited by 199

Expression analysis of the entire MMP and TIMP gene families during mouse tissue development

Nuttall, R. K., Sampieri, C. L., Pennington, C. J., Gill, S. E., Schultz, G. A., & Edwards, D. R. (2004) · FEBS Letters · doi:10.1016/s0014-5793(04)00281-9 · Cited by 195

ADAM17 is regulated by a rapid and reversible mechanism that controls access to its catalytic site

Gall, S. M. L., Maretzky, T., Issuree, P. D. A., Niu, X., Reiß, K., Säftig, P., Khokha, R., Lundell, D. J., & Blobel, C. (2010) · Journal of Cell Science · doi:10.1242/jcs.069997 · Cited by 191

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

Active Metalloproteases of the A Disintegrin And Metalloprotease (ADAM) Family: Biological Function and Structure

Klein, T., & Bischoff, R. (2011) · Journal of Proteome Research · doi:10.1021/pr100556z · Cited by 179

Increased Expression of Membrane Type 3-Matrix Metalloproteinase in Human Atherosclerotic Plaque

Uzui, H., Zemljic‐Harpf, A. E., Ming, L., Doherty, T. M., Shukla, A., Chai, N., Tripathi, P. V., Jovinge, S. V., Wilkin, D. J., Asotra, K., et al. (2002) · Circulation · doi:10.1161/01.cir.0000041433.94868.12 · Cited by 175

Notch-Deficient Skin Induces a Lethal Systemic B-Lymphoproliferative Disorder by Secreting TSLP, a Sentinel for Epidermal Integrity

Demehri, S., Liu, Z., Lee, J., Lin, M., Crosby, S. D., Roberts, C. J., Grigsby, P. W., Miner, J. H., Farr, A. G., & Kopan, R. (2008) · PLoS Biology · doi:10.1371/journal.pbio.0060123 · Cited by 174

Tissue inhibitor of metalloproteinases-3 induces apoptosis in melanoma cells by stabilization of death receptors

Ahonen, M., Poukkula, M., Baker, A. H., Kashiwagi, M., Nagase, H., Eriksson, J., & Kähäri, V. (2003) · Oncogene · doi:10.1038/sj.onc.1206292 · Cited by 174

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

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

The Shedding of CD62L (L-Selectin) Regulates the Acquisition of Lytic Activity in Human Tumor Reactive T Lymphocytes

Yang, S., Liu, F., Wang, Q. J., Rosenberg, S. A., & Morgan, R. A. (2011) · PLoS ONE · doi:10.1371/journal.pone.0022560 · Cited by 165

Thiol isomerases negatively regulate the cellular shedding activity of ADAM17

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

Atopic Dermatitis-Like Disease and Associated Lethal Myeloproliferative Disorder Arise from Loss of Notch Signaling in the Murine Skin

Dumortier, A., Durham, A., Piazza, M., Vauclair, S., Koch, U., Ferrand, G., Ferrero, I., Demehri, S., Song, L. L., Farr, A. G., et al. (2010) · PLoS ONE · doi:10.1371/journal.pone.0009258 · Cited by 165

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. K. (2007) · Journal of Leukocyte Biology · doi:10.1189/jlb.0307193 · Cited by 163

Hemopexin domains as multifunctional liganding modules in matrix metalloproteinases and other proteins

Piccard, H., den Steen, P. E. V., & Opdenakker, G. (2006) · Journal of Leukocyte Biology · doi:10.1189/jlb.1006629 · Cited by 162

Fine-tuning of dendritic cell biology by the TNF superfamily

deLuca, L. S., & Gommerman, J. L. (2012) · Nature reviews. Immunology · doi:10.1038/nri3193 · Cited by 154

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

Expression of Stromelysin-3 in Atherosclerotic Lesions: Regulation via CD40–CD40 Ligand Signaling In Vitro and In Vivo

Schönbeck, U., Mach, F., Sukhova, G. K., Atkinson, E., Levesque, E. B., Herman, M. P., Graber, P., Basset, P., & Libby, P. (1999) · The Journal of Experimental Medicine · doi:10.1084/jem.189.5.843 · Cited by 154

Cutting Edge: Tissue Inhibitor of Metalloproteinase 3 Regulates TNF-Dependent Systemic Inflammation

Smookler, D. S., Mohammed, F. F., Kassiri, Z., Duncan, G. S., Mak, T. W., & Khokha, R. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.176.2.721 · Cited by 154

TACE Activation by MAPK-Mediated Regulation of Cell Surface Dimerization and TIMP3 Association

Xu, P., Liu, J., Sakaki‐Yumoto, M., & Derynck, R. (2012) · Science Signaling · doi:10.1126/scisignal.2002689 · Cited by 151

Cellular turnover and extracellular matrix remodeling in female reproductive tissues: functions of metalloproteinases and their inhibitors

Fata, J. E., Ho, A. T. V., Leco, K. J., Moorehead, R. A., & Khokha, R. (2000) · Cellular and Molecular Life Sciences · doi:10.1007/s000180050500 · Cited by 151

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 149

TIMP3 Is Reduced in Atherosclerotic Plaques From Subjects With Type 2 Diabetes and Increased by SirT1

Cardellini, M., Menghini, R., Martelli, E., Casagrande, V., Marino, A., Rizza, S., Porzio, O., Mauriello, A., Solini, A., Ippoliti, A., et al. (2009) · Diabetes · doi:10.2337/db09-0280 · Cited by 147

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

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 142

Key Metalloproteinases Are Expressed by Specific Cell Types in Experimental Autoimmune Encephalomyelitis1

Toft-hansen, H., Nuttall, R., Edwards, D., & Owens, T. (2004) · Journal of Immunology · doi:10.4049/jimmunol.173.8.5209 · Cited by 141

The metalloproteases meprin α and meprin β: unique enzymes in inflammation, neurodegeneration, cancer and fibrosis

Broder, C., & Becker‐Pauly, C. (2013) · Biochemical Journal · doi:10.1042/bj20121751 · Cited by 135

The substrate degradome of meprin metalloproteases reveals an unexpected proteolytic link between meprin β and ADAM10

Jefferson, T., Keller, U. A. D., Bellac, C. L., Metz, V. V., Broder, C., Hedrich, J., Ohler, A., Maier, W., Magdolen, V., Sterchi, E. E., et al. (2012) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-012-1106-2 · Cited by 133

Matrix metalloproteinase deficiencies affect contact hypersensitivity: Stromelysin-1 deficiency prevents the response and gelatinase B deficiency prolongs the response

Wang, M., Qin, X., Mudgett, J. S., Ferguson, T. A., Senior, R. M., & Welgus, H. G. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.12.6885 · Cited by 133

Macrophage metalloelastase (MMP-12) as a target for inflammatory respiratory diseases

Lagente, V., Quément, C. L., & Boichot, E. (2009) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728220902751632 · Cited by 133

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 129

Tissue Inhibitor of Metalloproteinase 3 Deficiency Causes Hepatic Steatosis and Adipose Tissue Inflammation in Mice

Menghini, R., Menini, S., Amoruso, R., Fiorentino, L., Casagrande, V., Marzano, V., Tornei, F., Bertucci, P., Iacobini, C., Sérino, M., et al. (2008) · Gastroenterology · doi:10.1053/j.gastro.2008.10.079 · Cited by 127

Expression of Tissue Inhibitor of Metalloproteinases-3 in Human Atheroma and Regulation in Lesion-Associated Cells

Fabunmi, R. P., Sukhova, G. K., Sugiyama, S., & Libby, P. (1998) · Circulation Research · doi:10.1161/01.res.83.3.270 · Cited by 120

Expression and activity profiling of selected cysteine cathepsins and matrix metalloproteinases in synovial fluids from patients with rheumatoid arthritis and osteoarthritis

Požgan, U., Caglič, D., Rozman, B., Nagase, H., Türk, V., & Turk, B. (2010) · Biological Chemistry · doi:10.1515/bc.2010.035 · Cited by 119

Calcium pentosan polysulfate is a multifaceted exosite inhibitor of aggrecanases

Troeberg, L., Fushimi, K., Khokha, R., Emonard, H., Ghosh, P. B., & Nagase, H. (2008) · The FASEB Journal · doi:10.1096/fj.08-112680 · Cited by 115

Tissue Inhibitor of Metalloproteinase-1 Deficiency Amplifies Acute Lung Injury in Bleomycin-Exposed Mice

Kim, K. H., Burkhart, K. M., Chen, P., Frevert, C. W., Randolph‐Habecker, J., Hackman, R. C., Soloway, P. D., & Madtes, D. K. (2005) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2005-0111oc · Cited by 115

Matrix Metalloproteinase-19 Is a Key Regulator of Lung Fibrosis in Mice and Humans

Yu, G., Kovkarova-Naumovski, E., Jara, P., Parwani, A. V., Kass, D. J., Ruiz, V., López-Otı́n, C., Rosas, I. O., Gibson, K. F., Cabrera, S., et al. (2012) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.201202-0302oc · Cited by 115

Epidermal Growth Factor Receptor Activation Protects Gastric Epithelial Cells From Helicobacter pylori-Induced Apoptosis

Yan, F., Cao, H., Chaturvedi, R., Krishna, U. S., Hobbs, S. S., Dempsey, P. J., Peek, R. M., Cover, T. L., Washington, M. K., Wilson, K. T., et al. (2009) · Gastroenterology · doi:10.1053/j.gastro.2008.12.059 · Cited by 111

Prointerleukin-18 Is Activated by Meprin β in Vitro and in Vivo in Intestinal Inflammation

Banerjee, S., & Bond, J. S. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m802814200 · Cited by 110

Central Role of IL-6 Receptor Signal-Transducing Chain gp130 in Activation of L-Selectin Adhesion by Fever-Range Thermal Stress

Chen, Q., Wang, W., Bruce, R., Li, H., Schleider, D. M., Mulbury, M. J., Bain, M. D., Wallace, P. K., Baumann, H., & Evans, S. S. (2004) · Immunity · doi:10.1016/s1074-7613(03)00358-3 · Cited by 110

Diet-Induced Obesity and Reduced Skin Cancer Susceptibility in Matrix Metalloproteinase 19-Deficient Mice

Pendás, A. M., Folgueras, A. R., Llano, E., Caterina, J. J., Frerard, F., Rodríguez, F. J., Astudillo, A., Noël, A., Birkedal‐Hansen, H., & López-Otı́n, C. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.12.5304-5313.2004 · 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

Helicobacter pylori CagL Activates ADAM17 to Induce Repression of the Gastric H, K-ATPase α Subunit

Saha, A., Backert, S., Hammond, C. E., Gooz, M. B., & Smolka, A. J. (2010) · Gastroenterology · doi:10.1053/j.gastro.2010.03.036 · Cited by 105

Activation of TNFR1 ectodomain shedding by mitochondrial Ca2+ determines the severity of inflammation in mouse lung microvessels

Rowlands, D. J., Islam, M. N., Das, S., Huertas, A., Quadri, S. K., Horiuchi, K., Inamdar, N. M., Emin, M. T., Lindert, J., Ten, V. S., et al. (2011) · Journal of Clinical Investigation · doi:10.1172/jci43839 · Cited by 105

The Helicobacter pylori Virulence Effector CagA Abrogates Human β-Defensin 3 Expression via Inactivation of EGFR Signaling

Bauer, B., Pang, E., Holland, C., Kessler, M., Bartfeld, S., & Meyer, T. F. (2012) · Cell Host & Microbe · doi:10.1016/j.chom.2012.04.013 · Cited by 103

In Vivo Processing of CXCL5 (LIX) by Matrix Metalloproteinase (MMP)-2 and MMP-9 Promotes Early Neutrophil Recruitment in IL-1β–Induced Peritonitis

Song, J., Wu, C., Zhang, X., & Sorokin, L. M. (2012) · The Journal of Immunology · doi:10.4049/jimmunol.1202286 · Cited by 99

MT1-MMP regulates the PI3Kδ·Mi-2/NuRD-dependent control of macrophage immune functionPreprint

Shimizu‐Hirota, R., Xiong, W., Baxter, B. T., Kunkel, S. L., Maillard, I. P., Chen, X., Sabeh, F., Liu, R., Li, X.-Y., & Weiss, S. J. (2012) · Genes & Development · doi:10.1101/gad.178749.111 · Cited by 99

ADAM17 cleaves CD16b (FcγRIIIb) in human neutrophils

Wang, Y., Wu, J., Newton, R. C., Bahaie, N. S., Long, C., & Walcheck, B. K. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2012.11.027 · Cited by 95

Reduced Degradation of the Chemokine MCP-3 by Matrix Metalloproteinase-2 Exacerbates Myocardial Inflammation in Experimental Viral Cardiomyopathy

Westermann, D., Savvatis, K., Lindner, D., Zietsch, C., Becher, P. M., Hammer, E., Heimesaat, M. M., Bereswill, S., Völker, U., Escher, F., et al. (2011) · Circulation · doi:10.1161/circulationaha.111.035964 · 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

Tissue inhibitor of metalloproteinases 4 (TIMP4) is involved in inflammatory processes of human cardiovascular pathology

Koskivirta, I., Rahkonen, O. P., Mäyränpää, M. I., Pakkanen, S. H., Michael, H., Sainio, A., Hakovirta, H. H., Laine, J., Jokinen, E. V., VUORIO, E. I., et al. (2006) · Histochemistry and Cell Biology · doi:10.1007/s00418-006-0163-8 · Cited by 91

Epilysin (MMP-28) Restrains Early Macrophage Recruitment in Pseudomonas aeruginosa Pneumonia

Manicone, A. M., Birkland, T. P., Lin, M. J., Betsuyaku, T., van Rooijen, N., Lohi, J., Keski‐Oja, J., Wang, Y., Skerrett, S. J., & Parks, W. C. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0713949 · Cited by 91

Mice with Tissue Inhibitor of Metalloproteinases 4 (Timp4) Deletion Succumb to Induced Myocardial Infarction but Not to Cardiac Pressure Overload

Koskivirta, I., Kassiri, Z., Rahkonen, O. P., Kiviranta, R., Oudit, G. Y., McKee, T. D., Kytö, V., Saraste, A., Jokinen, E., Liu, P. P., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.136820 · Cited by 90

Differential Regulation of Extracellular Tissue Inhibitor of Metalloproteinases-3 Levels by Cell Membrane-bound and Shed Low Density Lipoprotein Receptor-related Protein 1

Scilabra, S. D., Troeberg, L., Yamamoto, K., Emonard, H., Thøgersen, I. B., Enghild, J. J., Strickland, D. K., & Nagase, H. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.393322 · Cited by 89

Glucocorticosteroids Differentially Regulate MMP-9 and Neutrophil Elastase in COPD

Vlahos, R., Wark, P. A. B., Anderson, G. P., & Bozinovski, S. (2012) · PLoS ONE · doi:10.1371/journal.pone.0033277 · Cited by 86

Tissue Inhibitor of Metalloproteinases 3 Regulates Resolution of Inflammation following Acute Lung Injury

Gill, S. E., Huizar, I., Bench, E. M., Sussman, S. W., Wang, Y., Khokha, R., & Parks, W. C. (2009) · American Journal Of Pathology · doi:10.2353/ajpath.2010.090158 · Cited by 85

MEP1A allele for meprin A metalloprotease is a susceptibility gene for inflammatory bowel disease

Banerjee, S., Oneda, B., Yap, L. M., Jewell, D. P., Matters, G. L., Fitzpatrick, L. R., Seibold, F., Sterchi, E. E., Ahmad, T., Lottaz, D., et al. (2009) · Mucosal Immunology · doi:10.1038/mi.2009.3 · Cited by 83

Meprin A and meprin α generate biologically functional IL-1β from pro-IL-1β

Herzog, C., Haun, R. S., Kaushal, V., Mayeux, P. R., Shah, S. V., & Kaushal, G. P. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.12.161 · Cited by 81

Direct observation of proteolytic cleavage at the S2 site upon forced unfolding of the Notch negative regulatory region

Stephenson, N. L., & Avis, J. M. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1205788109 · Cited by 80

Matrix metalloproteinase 12 overexpression in myeloid lineage cells plays a key role in modulating myelopoiesis, immune suppression, and lung tumorigenesis

Qu, P., Yan, C., & Du, H. (2011) · Blood · doi:10.1182/blood-2010-07-298380 · Cited by 80

Metalloproteinase MT5-MMP is an essential modulator of neuro-immune interactions in thermal pain stimulation

Folgueras, A. R., Valdés-Sánchez, T., Llano, E., Menéndez, L., Baamonde, A., Denlinger, B. L., Belmonte, C., Juárez, L., Lastra, A., García-Suárez, O., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0908507106 · Cited by 80

Deletion of the Mouse Meprin β Metalloprotease Gene Diminishes the Ability of Leukocytes to Disseminate through Extracellular Matrix

Crisman, J. M., Zhang, B., Norman, L. P., & Bond, J. S. (2004) · The Journal of Immunology · doi:10.4049/jimmunol.172.7.4510 · Cited by 78

Innate Immune Responses Are Increased in Chronic Obstructive Pulmonary Disease

Baines, K. J., Simpson, J. L., & Gibson, P. G. (2011) · PLoS ONE · doi:10.1371/journal.pone.0018426 · Cited by 77

Overexpression of Tissue Inhibitor of Metalloproteinase 3 in Macrophages Reduces Atherosclerosis in Low-Density Lipoprotein Receptor Knockout Mice

Casagrande, V., Menghini, R., Menini, S., Marino, A., Marchetti, V., Cavalera, M., Fabrizi, M., Hribal, M. L., Pugliese, G., Gentileschi, P., et al. (2011) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.111.238402 · Cited by 77

ADAM17-mediated shedding of the IL6R induces cleavage of the membrane stub by γ-secretase

Chalaris, A., Gewiese, J., Paliga, K., Fleig, L., Schneede, A., Krieger, K., Rose‐John, S., & Scheller, J. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2009.12.001 · Cited by 75

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 72

Matrix Metalloproteinase-2 Conditions Human Dendritic Cells to Prime Inflammatory TH2 Cells via an IL-12- and OX40L-Dependent Pathway

Godefroy, E., Manches, O., Dréno, B., Hochman, T., Rolnitzky, L. M., Labarrière, N., Guilloux, Y., Goldberg, J. D., Jotereau, F., & Bhardwaj, N. (2011) · Cancer Cell · doi:10.1016/j.ccr.2011.01.037 · Cited by 70

Epigenetic regulation of matrix metalloproteinases and their collagen substrates in cancer

Chernov, A. V., & Strongin, A. Y. (2011) · bmc · doi:10.1515/bmc.2011.017 · Cited by 69

Matrix Metalloproteinase 9 (MMP-9)-dependent Processing of βig-h3 Protein Regulates Cell Migration, Invasion, and Adhesion

Kim, Y. H., Kwon, H., & Kim, D. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.357863 · Cited by 68

Functional interactions between matrix metalloproteinases and glycosaminoglycans

Tocchi, A., & Parks, W. C. (2013) · FEBS Journal · doi:10.1111/febs.12198 · Cited by 66

Matrix metalloproteinase-3 (stromelysin-1) in acute inflammatory tissue injury

Nerusu, K. C., Warner, R. L., Bhagavathula, N., McClintock, S. D., Johnson, K. J., & Varani, J. (2007) · Experimental and Molecular Pathology · doi:10.1016/j.yexmp.2007.04.003 · Cited by 65

Differentiation-induced skin cancer suppression by FOS, p53, and TACE/ADAM17

Guinea‐Viniegra, J., Zenz, R., Scheuch, H., Jiménez, M., Bakiri, L., Petzelbauer, P., & Wagner, E. F. (2012) · Journal of Clinical Investigation · doi:10.1172/jci63103 · Cited by 64

Role of TIMPs (tissue inhibitors of metalloproteinases) in pericellular proteolysis: the specificity is in the detail

Murphy, G., Knäuper, V., Lee, M., Amour, A., Worley, J. R., Hutton, M., Atkinson, S. J., Rapti, M., & Williamson, R. A. (2003) · Biochemical Society Symposia · doi:10.1042/bss0700065 · Cited by 63

MMP19 Is Essential for T Cell Development and T Cell-Mediated Cutaneous Immune Responses

Beck, I. M., Rückert, R., Brandt, K., Mueller, M. S., Sadowski, T., Brauer, R., Schirmacher, P., Mentlein, R., & Sedlacek, R. (2008) · PLoS ONE · doi:10.1371/journal.pone.0002343 · Cited by 63

Tissue Inhibitor of Metalloproteinase-3 (TIMP-3) Regulates Hematopoiesis and Bone Formation In Vivo

Shen, Y., Winkler, I. G., Barbier, V., Sims, N. A., Hendy, J., & Lévesque, J.-P. (2010) · PLoS ONE · doi:10.1371/journal.pone.0013086 · Cited by 61

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

A Novel Pathway of Aerobic Benzoate Catabolism in the BacteriaAzoarcus evansii and Bacillus stearothermophilus

Zaar, A., Eisenreich, W., Bacher, A., & Fuchs, G. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100291200 · Cited by 56

Meprin A metalloproteases enhance renal damage and bladder inflammation after LPS challenge

Yura, R., Bradley, S. G., Ramesh, G., Reeves, W. B., & Bond, J. S. (2008) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.90524.2008 · Cited by 56

Adam17-dependent shedding limits early neutrophil influx but does not alter early monocyte recruitment to inflammatory sites

Tang, J., Zarbock, A., Gomez, I. G., Wilson, C. L., Lefort, C. T., Stadtmann, A., Bell, B., Huang, L.-C., Ley, K. F., & Raines, E. W. (2011) · Blood · doi:10.1182/blood-2010-11-321406 · Cited by 55

The C4 and C2 but not C1 components of complement are responsible for the complement activation triggered by the Ra-reactive factor.

Ji, Y. H., Matsushita, M., Okada, H., Fujita, T., & Kawakami, M. (1988) · The Journal of Immunology · doi:10.4049/jimmunol.141.12.4271 · Cited by 53

ADAM8: a new therapeutic target for asthma

Knolle, M. D., & Owen, C. A. (2009) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728220902889788 · Cited by 53

Matrix Metalloproteinase Mmp-1a Is Dispensable for Normal Growth and Fertility in Mice and Promotes Lung Cancer Progression by Modulating Inflammatory Responses

Fanjul‐Fernández, M., Folgueras, A. R., Fueyo, A., Balbı́n, M., Suárez, M. F., Fernández-García, M. S., Shapiro, S. D., Freije, J. M. P., & López-Otı́n, C. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.439893 · Cited by 52

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. (2010) · Cytokine · doi:10.1016/j.cyto.2010.03.003 · Cited by 52

ADAMTS-12 Metalloprotease Is Necessary for Normal Inflammatory Response

Moncada-Pazos, Á., Obaya, Á. J., Prada, M. L., Heljäsvaara, R., Suárez, M. F., Colado, E., Noël, A., Cal, S., & López-Otı́n, C. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.408625 · Cited by 50

Neutrophil-derived matrix metalloproteinase-9 is a potent activator of trypsinogen in acinar cells in acute pancreatitis

Awla, D., Abdulla, A., Syk, I., Jeppsson, B. W., Regnér, S., & Thorlacius, H. (2011) · Journal of Leukocyte Biology · doi:10.1189/jlb.0811443 · Cited by 50

Balance of meprin A and B in mice affects the progression of experimental inflammatory bowel disease

Banerjee, S., Jin, G., Bradley, S. G., Matters, G. L., Gailey, R. D., Crisman, J. M., & Bond, J. S. (2010) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00504.2009 · Cited by 49

Role of Meprins to Protect Ileal Mucosa of Crohn's Disease Patients from Colonization by Adherent-Invasive E. coli

Vazeille, E., Bringer, M.-A., Gardarin, A., Chambon, C., Becker‐Pauly, C., Pender, S. L. F., Jakob, C., Müller, S., Lottaz, D., & Darfeuille–Michaud, A. (2011) · PLoS ONE · doi:10.1371/journal.pone.0021199 · Cited by 46

Matrix metalloprotease 1a deficiency suppresses tumor growth and angiogenesis

Foley, C., Fanjul‐Fernández, M., Bohm, A., Nguyen, N. T. B., Agarwal, A., Austin, K., Κούκος, Γ., Covic, L., López-Otı́n, C., & Kuliopulos, A. (2013) · Oncogene · doi:10.1038/onc.2013.157 · Cited by 44

Presenilin/γ-secretase and α-secretase-like peptidases cleave human MHC Class I proteins

Carey, B. W., Kim, D. Y., & Kovacs, D. M. (2006) · Biochemical Journal · doi:10.1042/bj20060847 · Cited by 43

Shedding and γ-secretase-mediated intramembrane proteolysis of the mucin-type molecule CD43

Andersson, C. X., Fernández-Rodrı́guez, J., Laos, S., Baeckström, D., Haass, C., & Hansson, G. C. (2005) · Biochemical Journal · doi:10.1042/bj20041387 · Cited by 42

Oxidatively modified high density lipoprotein promotes inflammatory response in human monocytes–macrophages by enhanced production of ROS, TNF-α, MMP-9, and MMP-2

Soumyarani, V. S., & Jayakumari, N. (2012) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-012-1306-y · Cited by 42

ADAM17 activation in circulating neutrophils following bacterial challenge impairs their recruitment

Long, C., Hosseinkhani, M. R., Wang, Y., Sriramarao, P., & Walcheck, B. K. (2012) · Journal of Leukocyte Biology · doi:10.1189/jlb.0312112 · Cited by 40

Deficiency of matrix metalloproteinase-13 increases inflammation after acute lung injury

Sen, A. I., Shiomi, T., Okada, Y., & D'Armiento, J. M. (2010) · Experimental Lung Research · doi:10.3109/01902148.2010.497201 · Cited by 40

Dual Protective Mechanisms of Matrix Metalloproteinases 2 and 9 in Immune Defense against Streptococcus pneumoniae

Hong, J.-S., Greenlee, K. J., Pitchumani, R., Lee, S., Song, L., Shan, M., Chang, S. H., Park, P. W., Dong, C., Werb, Z., et al. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1003449 · Cited by 39

Regulation of Th1/Th2 polarization by tissue inhibitor of metalloproteinase-3 via modulating dendritic cells

Shao, Q., Ning, H., Lv, J., Liu, Y., Zhao, X., Ren, G., Feng, A., Xie, Q., Sun, J., Song, B., et al. (2012) · Blood · doi:10.1182/blood-2011-08-376418 · Cited by 34

Macrophage Metalloelastase (MMP-12) Deficiency Mitigates Retinal Inflammation and Pathological Angiogenesis in Ischemic Retinopathy

Li, J., Wang, J. J., Peng, Q., Chen, C., Humphrey, M. B., Heinecke, J. W., & Zhang, S. X. (2012) · PLoS ONE · doi:10.1371/journal.pone.0052699 · Cited by 34

TIMP-3 recruits quiescent hematopoietic stem cells into active cell cycle and expands multipotent progenitor pool

Nakajima, H., Ito, M., Smookler, D. S., Shibata, F., Fukuchi, Y., Morikawa, Y., Ikeda, Y., Arai, F., Suda, T., Khokha, R., et al. (2010) · Blood · doi:10.1182/blood-2010-01-266528 · Cited by 33

Stromal TIMP3 Regulates Liver Lymphocyte Populations and Provides Protection against Th1 T Cell-Driven Autoimmune Hepatitis

Murthy, A., Shao, Y. W., Defamie, V., Wedeles, C. J., Smookler, D. S., & Khokha, R. (2012) · The Journal of Immunology · doi:10.4049/jimmunol.1102199 · Cited by 33

The Lack of ADAM17 Activity during Embryonic Development Causes Hemorrhage and Impairs Vessel Formation

Canault, M., Certel, K., Schatzberg, D., Wagner, D. D., & Hynes, R. O. (2010) · PLoS ONE · doi:10.1371/journal.pone.0013433 · Cited by 31

Meprins process matrix metalloproteinase‐9 (MMP‐9)/gelatinase B and enhance the activation kinetics by MMP‐3

Geurts, N., Becker‐Pauly, C., Martens, E., Proost, P., den Steen, P. E. V., Stöcker, W., & Opdenakker, G. (2012) · FEBS Letters · doi:10.1016/j.febslet.2012.10.033 · Cited by 30

Modulation of integrin α4β1 by ADAM28 promotes lymphocyte adhesion and transendothelial migration

McGinn, O. J., English, W., Roberts, S., Ager, A., Newham, P., & Murphy, G. (2011) · Cell Biology International · doi:10.1042/cbi20100885 · Cited by 28

Serum CD40/CD40L System in Graves' Disease and Hashimoto's Thyroiditis Related to Soluble Fas, FasL and Humoral Markers of Autoimmune Response

Myśliwiec, J., Okłota, M., Nikołajuk, A., Waligórski, D., & Górska, M. (2007) · Immunological Investigations · doi:10.1080/08820130601069715 · Cited by 28

TIMP3 Regulates Mammary Epithelial Apoptosis with Immune Cell Recruitment Through Differential TNF Dependence

Hojilla, C. V., Jackson, H. W., & Khokha, R. (2011) · PLoS ONE · doi:10.1371/journal.pone.0026718 · Cited by 26

Epidermal ADAM17 Is Dispensable for Notch Activation

Groot, A. J., Cobzaru, C., Weber, S., Säftig, P., Blobel, C., Kopan, R., Vooijs, M., & Franzke, C.-W. (2013) · Journal of Investigative Dermatology · doi:10.1038/jid.2013.162 · Cited by 26

A Staphylococcus aureus pore-forming toxin subverts the activity of ADAM10 to cause lethal infection in mice

Inoshima, I., Inoshima, N., Wilke, G. A., Powers, M. E., Frank, K. M., Wang, Y., & Wardenburg, J. B. (2011) · Nature Medicine · doi:10.1038/nm.2451 · Cited by 21

Cell Distribution Differences Of Matrix Metalloproteinase-9 and Tissue Inhibitor of Matrix Metalloproteinase-1 in Patients With Kawasaki Disease

Korematsu, S., Ohta, Y., Tamai, N., Takeguchi, M., Goto, C., Miyahara, H., Kawano, T., & Izumi, T. (2012) · The Pediatric Infectious Disease Journal · doi:10.1097/inf.0b013e31825ba6b3 · Cited by 21

TIMP-1 deficiency subverts cell-cycle dynamics in murine long-term HSCs

Rossi, L., Ergen, A. V., & Goodell, M. A. (2011) · Blood · doi:10.1182/blood-2009-10-248955 · Cited by 18

Matrix Metalloproteinase-9 Increases in the Sputum from Allergic Occupational Asthma Patients after Specific Inhalation Challenge

Castaño, R., Miedinger, D., Maghni, K., Ghezzo, H., Trudeau, C., Castellanos, L., Wattiez, M., Vandenplas, O., & Malo, J. (2012) · International Archives of Allergy and Immunology · doi:10.1159/000339737 · Cited by 15

Remodelling the extracellular matrix in development and disease

Bonnans, C., Chou, J., & Werb, Z. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3904 · Cited by 4,367

The history and advances in cancer immunotherapy: understanding the characteristics of tumor-infiltrating immune cells and their therapeutic implications

Zhang, Y., & Zhang, Z. (2020) · Cellular and Molecular Immunology · doi:10.1038/s41423-020-0488-6 · Cited by 2,906

Is there new hope for therapeutic matrix metalloproteinase inhibition?

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