Metalloproteinases and their natural inhibitors in inflammation and immunity

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

Visse, R., & Nagase, H. (2003) · Circulation Research · doi:10.1161/01.res.0000070112.80711.3d · Cited by 4,575 · see citing works

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 3,416 · see citing works

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

Defensins: antimicrobial peptides of innate immunity

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

Inflammasomes in health and disease

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

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

Groh, V., Wu, J. D., Yee, C., & Spies, T. A. (2002) · Nature · doi:10.1038/nature01112 · Cited by 1,596 · see citing works

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 · see citing works

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 · see citing works

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 1,314 · see citing works

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 · see citing works

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

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

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 · see citing works

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

(2012) · The Lancet · doi:10.1016/s0140-6736(12)60110-x · Cited by 1,146 · see citing works

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

Rajagopalan, S., Meng, X. P., Ramasamy, S., Harrison, D. G., & Galis, Z. S. (1996) · Journal of Clinical Investigation · doi:10.1172/jci119076 · Cited by 1,137 · 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

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 979 · see citing works

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

(2012) · The Lancet · doi:10.1016/s0140-6736(11)61931-4 · Cited by 823 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 683 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 407 · 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

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 384 · see citing works

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

Kaiser, B. K., Yim, D., Chow, I., Gonzalez, S. R., Dai, Z., Mann, H. H., Strong, R. K., Groh, V., & Spies, T. A. (2007) · Nature · doi:10.1038/nature05768 · Cited by 378 · see citing works

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 376 · see citing works

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 362 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 284 · see citing works

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 281 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 224 · see citing works

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 · see citing works

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 210 · see citing works

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 · see citing works

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 · see citing works

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 200 · see citing works

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 · see citing works

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 194 · see citing works

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 191 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 173 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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

Yang, S.-C., Liu, F., Wang, Q. J., Rosenberg, S., & Morgan, R. (2011) · PLoS ONE · doi:10.1371/journal.pone.0022560 · Cited by 154 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 151 · see citing works

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 150 · see citing works

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 149 · see citing works

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 · see citing works

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 142 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 126 · see citing works

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 121 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 112 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 107 · see citing works

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 · see citing works

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 · see citing works

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 102 · see citing works

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 · see citing works

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 97 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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. L., Lastra, A., García‐Suárez, O., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0908507106 · Cited by 91 · see citing works

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 · see citing works

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 · see citing works

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 90 · see citing works

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 86 · see citing works

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 · see citing works

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 85 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 76 · see citing works

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 74 · see citing works

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 73 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 69 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

Functional interactions between matrix metalloproteinases and glycosaminoglycans

Tocchi, A., & Parks, W. C. (2013) · FEBS Journal · doi:10.1111/febs.12198 · Cited by 63 · see citing works

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 60 · see citing works

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 59 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 40 · see citing works

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 38 · see citing works

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 · see citing works

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 33 · see citing works

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 · see citing works

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 32 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 2,815 · see citing works

Is there new hope for therapeutic matrix metalloproteinase inhibition?

Vandenbroucke, R. E., & Libert, C. (2014) · Nature Reviews Drug Discovery · doi:10.1038/nrd4390 · Cited by 840 · see citing works

The role of TIMPs in regulation of extracellular matrix proteolysis

Arpino, V., Brock, M. S., & Gill, S. E. (2015) · Matrix Biology · doi:10.1016/j.matbio.2015.03.005 · Cited by 738 · see citing works

Resveratrol regulates neuro-inflammation and induces adaptive immunity in Alzheimer’s disease

Moussa, C., Hebron, M. L., Huang, X., Ahn, J., Rissman, R. A., Aisen, P. S. S., & Turner, R. S. (2017) · Journal of Neuroinflammation · doi:10.1186/s12974-016-0779-0 · Cited by 712 · see citing works

Functions of ROS in Macrophages and Antimicrobial Immunity

Herb, M., & Schramm, M. (2021) · Antioxidants · doi:10.3390/antiox10020313 · Cited by 633 · see citing works

Matrix Metalloproteinases: From Molecular Mechanisms to Physiology, Pathophysiology, and Pharmacology

de Almeida, L. G. N., Thode, H., Eslambolchi, Y., Chopra, S., Young, D. W., Gill, S. E., Devel, L., & Dufour, A. (2022) · Pharmacological Reviews · doi:10.1124/pharmrev.121.000349 · Cited by 555 · see citing works

Inflammation and fibrosis

Mack, M. (2017) · Matrix Biology · doi:10.1016/j.matbio.2017.11.010 · Cited by 516 · see citing works

TIMPs: versatile extracellular regulators in cancer

Jackson, H. W., Defamie, V., Waterhouse, P. D., & Khokha, R. (2016) · Nature reviews. Cancer · doi:10.1038/nrc.2016.115 · Cited by 454 · see citing works

Immune mechanisms in medium and large-vessel vasculitis

Weyand, C. M., & Goronzy, J. J. (2013) · Nature Reviews Rheumatology · doi:10.1038/nrrheum.2013.161 · Cited by 412 · see citing works

Matrix remodeling by MMPs during wound repair

Rohani, M. G., & Parks, W. C. (2015) · Matrix Biology · doi:10.1016/j.matbio.2015.03.002 · Cited by 407 · see citing works

Modulating extracellular matrix stiffness: A strategic approach to boost cancer immunotherapy

Mai, Z., Lin, Y., Lin, P., Zhao, X., & Cui, L. (2024) · Cell Death & Disease · doi:10.1038/s41419-024-06697-4 · Cited by 398 · see citing works

MMP ‐9 in translation: from molecule to brain physiology, pathology, and therapy

Vafadari, B., Salamian, A., & Kaczmarek, L. (2015) · Journal of Neurochemistry · doi:10.1111/jnc.13415 · Cited by 381 · see citing works

Annexin A1–containing extracellular vesicles and polymeric nanoparticles promote epithelial wound repair

Leoni, G., Neumann, P., Kamaly, N., Quirós, M., Nishio, H., Jones, H. R., Sumagin, R., Hilgarth, R., Alam, A. M., Fredman, G., et al. (2015) · Journal of Clinical Investigation · doi:10.1172/jci76693 · Cited by 355 · see citing works

Resolution of organ fibrosis

Jun, J.-I., & Lau, L. F. (2018) · Journal of Clinical Investigation · doi:10.1172/jci93563 · Cited by 348 · see citing works

Angiogenesis and Inflammation Crosstalk in Diabetic Retinopathy

Capitão, M., & Soares, R. A. (2016) · Journal of Cellular Biochemistry · doi:10.1002/jcb.25575 · Cited by 310 · see citing works

Interleukin-6: from basic biology to selective blockade of pro-inflammatory activities

Scheller, J., Garbers, C., & Rose-John, S. (2014) · Seminars in Immunology · doi:10.1016/j.smim.2013.11.002 · Cited by 308 · see citing works

Re-Emergence of Dendritic Cell Vaccines for Cancer Treatment

Saxena, M., & Bhardwaj, N. (2018) · Trends in cancer · doi:10.1016/j.trecan.2017.12.007 · Cited by 305 · see citing works

Origin and function of stress-induced IL-6 in murine models

Qing, H., Desrouleaux, R., Israni-Winger, K., Mineur, Y. S., Fogelman, N., Zhang, C., Rashed, S., Palm, N. W., Sinha, R., Picciotto, M. R., et al. (2020) · Cell · doi:10.1016/j.cell.2020.05.054 · Cited by 303 · see citing works

The Rebirth of Matrix Metalloproteinase Inhibitors: Moving Beyond the Dogma

Fields, G. B. (2019) · Cells · doi:10.3390/cells8090984 · Cited by 304 · see citing works

Chimeric antigen receptor macrophage therapy for breast tumours mediated by targeting the tumour extracellular matrix

Zhang, W., Liu, L., Su, H., Liu, Q., Shen, J., Dai, H., Zheng, W., Lu, Y., Zhang, W., Bei, Y., et al. (2019) · British Journal of Cancer · doi:10.1038/s41416-019-0578-3 · Cited by 296 · see citing works

Fibroblast activation in cancer: when seed fertilizes soil

Kužet, S.-E., & Gaggioli, C. (2016) · Cell and Tissue Research · doi:10.1007/s00441-016-2467-x · Cited by 286 · see citing works

Ciliary Hedgehog Signaling Restricts Injury-Induced Adipogenesis

Kopinke, D., Roberson, E. C., & Reiter, J. F. (2017) · Cell · doi:10.1016/j.cell.2017.06.035 · Cited by 260 · see citing works

Leukaemogenic effects of Ptpn11 activating mutations in the stem cell microenvironment

Dong, L., Yu, W., Zheng, H., Loh, M. L., Bunting, S. T., Pauly, M. G., Huang, G., Zhou, M., Broxmeyer, H. E., Scadden, D. T., et al. (2016) · Nature · doi:10.1038/nature20131 · Cited by 260 · see citing works

Monocyte and macrophage immunometabolism in atherosclerosis

Groh, L. A., Keating, S. T., Joosten, L. A. B., Netea, M. G., & Riksen, N. P. (2017) · Seminars in Immunopathology · doi:10.1007/s00281-017-0656-7 · Cited by 255 · see citing works

Tuberculosis, Pulmonary Cavitation, and Matrix Metalloproteinases

Ong, C. W. M., Elkington, P. T., & Friedland, J. S. (2014) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.201311-2106pp · Cited by 231 · see citing works

Proteolytic Cleavage—Mechanisms, Function, and “Omic” Approaches for a Near-Ubiquitous Posttranslational Modification

Klein, T., Eckhard, U., Dufour, A., Solis, N., & Overall, C. M. (2017) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00120 · Cited by 229 · see citing works

Metalloproteinases in atherosclerosis

Johnson, J. L. (2017) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2017.09.007 · Cited by 227 · see citing works

Matrix metalloproteinases in arthritis: towards precision medicine

Grillet, B. A. M., Pereira, R. V. S., Damme, J. V., El‐Asrar, A. M. A., Proost, P., & Opdenakker, G. (2023) · Nature Reviews Rheumatology · doi:10.1038/s41584-023-00966-w · Cited by 217 · see citing works

Janus Kinase Inhibitors in the Treatment of Vitiligo: A Review

Qi, F., Liu, F., & Gao, L. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.790125 · Cited by 203 · see citing works

Loss of the Timp gene family is sufficient for the acquisition of the CAF-like cell state

Shimoda, M., Principe, S., Jackson, H. W., Luga, V., Fang, H., Molyneux, S. D., Shao, Y. W., Aiken, A., Waterhouse, P. D., Karamboulas, C., et al. (2014) · Nature Cell Biology · doi:10.1038/ncb3021 · Cited by 199 · see citing works

The impact of cancer-associated fibroblasts on major hallmarks of pancreatic cancer

Sun, Q., Zhang, B., Hu, Q., Qin, Y., Xu, W., Liu, W., Yu, X., & Xu, J. (2018) · Theranostics · doi:10.7150/thno.26546 · Cited by 193 · see citing works

From Structure to Phenotype: Impact of Collagen Alterations on Human Health

Arseni, L., Lombardi, A., & Orioli, D. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19051407 · Cited by 186 · see citing works

Targeting inflammation in diabetes: Newer therapeutic options

Agrawal, N. K. (2014) · World Journal of Diabetes · doi:10.4239/wjd.v5.i5.697 · Cited by 188 · see citing works

New intracellular activities of matrix metalloproteinases shine in the moonlight

Jobin, P. G., Butler, G. S., & Overall, C. M. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2017.05.013 · Cited by 184 · see citing works

Susceptibility of low-density lipoprotein particles to aggregate depends on particle lipidome, is modifiable, and associates with future cardiovascular deaths

Ruuth, M., Nguyen, S. D., Vihervaara, T., Hilvo, M., Laajala, T. D., Kondadi, P. K., Gisterå, A., Lähteenmäki, H., Kittilä, T., Huusko, J., et al. (2018) · European Heart Journal · doi:10.1093/eurheartj/ehy319 · Cited by 180 · see citing works

The Extracellular Matrix: Its Composition, Function, Remodeling, and Role in Tumorigenesis

Dzobo, K., & Dandara, C. (2023) · Biomimetics · doi:10.3390/biomimetics8020146 · Cited by 173 · see citing works

Metalloproteinases in extracellular vesicles

Shimoda, M., & Khokha, R. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2017.05.027 · Cited by 169 · see citing works

Stimuli-Responsive Polymeric Nanoplatforms for Cancer Therapy

Chang, D., Ma, Y., Xu, X., Xie, J., & Ju, S. (2021) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2021.707319 · Cited by 169 · see citing works

Metalloproteinase production from macrophages – a perfect storm leading to atherosclerotic plaque rupture and myocardial infarction

Newby, A. C. (2016) · Experimental Physiology · doi:10.1113/ep085567 · Cited by 156 · see citing works

Shedding of Endogenous Interleukin-6 Receptor (IL-6R) Is Governed by A Disintegrin and Metalloproteinase (ADAM) Proteases while a Full-length IL-6R Isoform Localizes to Circulating Microvesicles

Schumacher, N., Meyer, D., Mauermann, A., von der Heyde, J., Wolf, J., Schwarz, J., Knittler, K., Murphy, G., Michalek, M., Garbers, C., et al. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.649509 · Cited by 152 · see citing works

Stanford-A acute aortic dissection, inflammation, and metalloproteinases: A review

Cifani, N., Proietta, M., Tritapepe, L., Gioia, C. R. T. D., Ferri, L., Taurino, M., & Porto, F. D. (2015) · Annals of Medicine · doi:10.3109/07853890.2015.1073346 · Cited by 145 · see citing works

The Dynamic Interplay Between Cardiac Inflammation and Fibrosis

Thomas, T. P., & Grisanti, L. A. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.529075 · Cited by 146 · see citing works

A novel function of artesunate on inhibiting migration and invasion of fibroblast-like synoviocytes from rheumatoid arthritis patients

Ma, J., Jing, J., Jun-wei, W., Yan, T., Li, Q., Mo, Y., Zheng, D.-H., Gao, J., Nguyen, K.-A. T., & Dai, L. (2019) · Arthritis Research & Therapy · doi:10.1186/s13075-019-1935-6 · Cited by 144 · see citing works

The immunomodulatory role of matrix metalloproteinases in colitis-associated cancer

He, L., Kang, Q., Chan, K. I., Zhang, Y., Zhong, Z., & Tan, W. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2022.1093990 · Cited by 144 · see citing works

Squalene targets pro- and anti-inflammatory mediators and pathways to modulate over-activation of neutrophils, monocytes and macrophages

Cárdeno, A., Aparicio‐Soto, M., la Paz, S. M., Bermúdez, B., Muriana, F. J. G., & Alarcón‐de‐la‐Lastra, C. (2015) · Journal of Functional Foods · doi:10.1016/j.jff.2015.03.009 · Cited by 141 · see citing works

Biology of Tissue Inhibitor of Metalloproteinase 3 (TIMP3), and Its Therapeutic Implications in Cardiovascular Pathology

Dong, F., & Kassiri, Z. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.00661 · Cited by 140 · 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

Proteolytic Cleavage Governs Interleukin-11 Trans-signaling

Lokau, J., Nitz, R., Agthe, M., Monhasery, N., Aparicio-Siegmund, S., Schumacher, N., Wolf, J., Möller‐Hackbarth, K., Waetzig, G. H., Grötzinger, J., et al. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.01.053 · Cited by 136 · see citing works

Immunomodulatory biomaterials and their application in therapies for chronic inflammation-related diseases

Nakkala, J. R., Li, Z., Ahmad, W., Wang, K., & Gao, C. (2021) · Acta Biomaterialia · doi:10.1016/j.actbio.2021.01.025 · Cited by 136 · see citing works

Cerebral Malaria in Mouse and Man

Ghazanfari, N., Mueller, S. N., & Heath, W. R. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.02016 · Cited by 134 · see citing works

Perturbations of the cerebrovascular matrisome: A convergent mechanism in small vessel disease of the brain?

Joutel, A., Haddad, I., Ratelade, J., & Nelson, M. T. (2015) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/jcbfm.2015.62 · Cited by 126 · see citing works

Role of Matrix Metalloproteinases in the Pathogenesis of Traumatic Brain Injury

Muneer, P. M. A., Pfister, B. J., Haorah, J., & Chandra, N. (2015) · Molecular Neurobiology · doi:10.1007/s12035-015-9520-8 · Cited by 126 · see citing works

Regulation of A disintegrin and metalloproteinase (ADAM) family sheddases ADAM10 and ADAM17: The emerging role of tetraspanins and rhomboids

Matthews, A. L., Noy, P. J., Reyat, J. S., & Tomlinson, M. G. (2016) · Platelets · doi:10.1080/09537104.2016.1184751 · Cited by 122 · see citing works

Metalloproteinases promote plaque rupture and myocardial infarction: A persuasive concept waiting for clinical translation

Newby, A. C. (2015) · Matrix Biology · doi:10.1016/j.matbio.2015.01.015 · Cited by 119 · see citing works

Role of matrix metalloproteinase in wound healing.

Kandhwal, M., Behl, T., Singh, S., Sharma, N., Arora, S., Bhatia, S., Al‐Harrasi, A., Sachdeva, M., & BUNGAU, S. G. (2022) · PubMed Central · Cited by 116 · see citing works

Matrix Metalloproteinases on Skin Photoaging

Feng, C., Chen, X., Yin, X., Jiang, Y., & Zhao, C. (2024) · Journal of Cosmetic Dermatology · doi:10.1111/jocd.16558 · Cited by 112 · see citing works

Activation of cell-surface proteases promotes necroptosis, inflammation and cell migration

Cai, Z., Zhang, A., Choksi, S., Li, W., Li, T., Zhang, X.-M., & Liu, Z.-G. (2016) · Cell Research · doi:10.1038/cr.2016.87 · Cited by 103 · see citing works

Intratumoral fate of functional nanoparticles in response to microenvironment factor: Implications on cancer diagnosis and therapy

Peng, J., Yang, Q., Shi, K., Xiao, Y., Wei, X., & Qian, Z. (2019) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2019.06.007 · Cited by 105 · see citing works

Harnessing the antitumor potential of macrophages for cancer immunotherapy

Long, K. B., & Beatty, G. L. (2013) · OncoImmunology · doi:10.4161/onci.26860 · Cited by 103 · see citing works

Matrix Metalloproteinases in Non-Neoplastic Disorders

Tokito, A., & Jougasaki, M. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17071178 · Cited by 96 · see citing works

Polysialylation and lipopolysaccharide‐induced shedding of E‐selectin ligand‐1 and neuropilin‐2 by microglia and THP‐1 macrophages

Werneburg, S., Buettner, F. F. R., Erben, L., Mathews, M., Neumann, H., Mühlenhoff, M., & Hildebrandt, H. (2016) · Glia · doi:10.1002/glia.23004 · Cited by 91 · see citing works

Roles of Matrix Metalloproteinases and Their Natural Inhibitors in Metabolism: Insights into Health and Disease

Molière, S., Jaulin, A., Tomasetto, C., & Dali‐Youcef, N. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241310649 · Cited by 93 · see citing works

Matrix metalloproteinases: Expression, regulation and role in the immunopathology of tuberculosis

Sabir, N., Hussain, T. A., Mangi, M. H., Zhao, D., & Zhou, X. (2019) · Cell Proliferation · doi:10.1111/cpr.12649 · Cited by 100 · see citing works

A novel regulation of PD-1 ligands on mesenchymal stromal cells through MMP-mediated proteolytic cleavage

Dezutter‐Dambuyant, C., Durand, I., Alberti, L., Bendriss‐Vermare, N., Valladeau‐Guilemond, J., Duc, A., Magron, A., Morel, A., Sisirak, V., Rodriguez, C., et al. (2015) · OncoImmunology · doi:10.1080/2162402x.2015.1091146 · Cited by 91 · see citing works

Antifibrotic, Antioxidant, and Immunomodulatory Effects of Mesenchymal Stem Cells in HOCl‐Induced Systemic Sclerosis

Maria, A. T. J., Toupet, K., Bony, C., Pirot, N., Vozenin, M., Petit, B., Roger, P., Batteux, F., Quellec, A. L., Jørgensen, C., et al. (2015) · Arthritis & Rheumatology · doi:10.1002/art.39477 · Cited by 90 · see citing works

Matrix metalloproteinase-9 activity and a downregulated Hedgehog pathway impair blood-brain barrier function in an in vitro model of CNS tuberculosis

Brilha, S., Ong, C. W. M., Weksler, B. B., Romero, N., Couraud, P., & Friedland, J. S. (2017) · Scientific Reports · doi:10.1038/s41598-017-16250-3 · Cited by 86 · see citing works

Innate immune system and tissue regeneration in planarians: An area ripe for exploration

Peiris, T. H., Hoyer, K. K., & Oviedo, N. J. (2014) · Seminars in Immunology · doi:10.1016/j.smim.2014.06.005 · Cited by 86 · see citing works

Matrix metalloproteinases and inhibitors in dentistry

Boelen, G., Boute, L., d’Hoop, J., EzEldeen, M., Lambrichts, I., & Opdenakker, G. (2019) · Clinical Oral Investigations · doi:10.1007/s00784-019-02915-y · Cited by 89 · see citing works

Augmented Th17 differentiation in Trim21 deficiency promotes a stable phenotype of atherosclerotic plaques with high collagen content

Brauner, S., Jiang, X., Thorlacius, G. E., Lundberg, A. M., Östberg, T., Yan, Z.-Q., Kuchroo, V. K., Hansson, G. K., & Wahren‐Herlenius, M. (2017) · Cardiovascular Research · doi:10.1093/cvr/cvx181 · Cited by 86 · see citing works

Matrix Metalloproteases as Influencers of the Cells’ Social Media

Young, D., Das, N. S., Anowai, A., & Dufour, A. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20163847 · Cited by 77 · see citing works

Transcriptome of American Oysters, Crassostrea virginica, in Response to Bacterial Challenge: Insights into Potential Mechanisms of Disease Resistance

McDowell, I. C., Nikapitiya, C., Aguiar, D., Lane, C. E., Istrail, S., & Marta Gómez-chiarri, G. (2014) · PLoS ONE · doi:10.1371/journal.pone.0105097 · Cited by 86 · see citing works

Metalloproteinases and their roles in human cancer

Roy, R., Morad, G., Jedinak, A., & Moses, M. A. (2019) · The Anatomical Record · doi:10.1002/ar.24188 · Cited by 84 · see citing works

Matrix metalloproteinase contribution in management of cancer proliferation, metastasis and drug targeting

Abdel‐Hamid, N. M., & Abass, S. A. (2021) · Molecular Biology Reports · doi:10.1007/s11033-021-06635-z · Cited by 83 · see citing works

Matrix Metalloproteinase-19 Promotes Metastatic Behavior In Vitro and is Associated with Increased Mortality in Non–Small Cell Lung Cancer

Yu, G., Herazo‐Maya, J. D., Nukui, T., Romkes, M., Parwani, A. V., Juan-Guardela, B. M., Robertson, J. V., Gauldie, J., Siegfried, J. M., Kaminski, N., et al. (2014) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.201310-1903oc · Cited by 82 · see citing works

Mechanisms of receptor shedding in platelets

Montague, S. J., Andrews, R. K., & Gardiner, E. E. (2018) · Blood · doi:10.1182/blood-2018-03-742668 · Cited by 82 · see citing works

Type-1 cytokines regulate MMP-9 production and E-cadherin disruption to promote melanocyte loss in vitiligo

Boukhedouni, N., Martins, C. P., Darrigade, A. ‐., Drullion, C., Rambert, J., Barrault, C., Garnier, J., Jacquemin, C., Thiolat, D., Lucchese, F., et al. (2020) · JCI Insight · doi:10.1172/jci.insight.133772 · Cited by 82 · see citing works

Matrix metalloproteinases in impaired wound healing

Keller, U. A. D., & Sabino, F. (2015) · Metalloproteinases In Medicine · doi:10.2147/mnm.s68420 · Cited by 79 · see citing works

Next-Generation Sequencing Reveals Low-Dose Effects of Cationic Dendrimers in Primary Human Bronchial Epithelial Cells

Feliu, N., Kohonen, P. J., Ji, J., Zhang, Y., Karlsson, H. L., Palmberg, L., Nyström, A. M., & Fadeel, B. (2014) · ACS Nano · doi:10.1021/nn5061783 · Cited by 79 · see citing works

Immunomodulatory roles of metalloproteinases in rheumatoid arthritis

Bian, Y., Xiang, Z., Wang, Y., Ren, Q., Chen, G., Xiang, B., Wang, J., Zhang, C., Pei, S., Guo, S., et al. (2023) · Frontiers in Pharmacology · doi:10.3389/fphar.2023.1285455 · Cited by 84 · see citing works

Matrix Metalloproteinases and Protein Tyrosine Kinases

Aschner, Y., Zemans, R. L., Yamashita, C. M., & Downey, G. P. (2014) · CHEST Journal · doi:10.1378/chest.14-0397 · Cited by 76 · see citing works

Matrix metalloproteinase inhibitors enhance the efficacy of frontline drugs against Mycobacterium tuberculosis

Xu, Y., Wang, L., Zimmerman, M. D., Chen, K., Huang, L., Fu, D., Kaya, F., Rakhilin, N., Nazarova, E. V., Bu, P., et al. (2018) · PLoS Pathogens · doi:10.1371/journal.ppat.1006974 · Cited by 75 · see citing works

ADAM Proteases and Gastrointestinal Function

Jones, J. C., Rustagi, S., & Dempsey, P. J. (2015) · Annual Review of Physiology · doi:10.1146/annurev-physiol-021014-071720 · Cited by 74 · see citing works

Salvianolic acid A attenuates ischemia reperfusion induced rat brain damage by protecting the blood brain barrier through MMP-9 inhibition and anti-inflammation

Zhang, W., Jun-Ke, S. O. N. G., Zhang, X., Zhou, Q., He, G., Xu, X., Rong, Y., Zhou, W., & Du, G. (2018) · Chinese Journal of Natural Medicines · doi:10.1016/s1875-5364(18)30046-3 · Cited by 74 · see citing works

TGFβ-induced switch from adipogenic to osteogenic differentiation of human mesenchymal stem cells: identification of drug targets for prevention of fat cell differentiation

van Zoelen, E. J. J., Duarte, I., Hendriks, J. M. A., & van der Woning, S. P. (2016) · Stem Cell Research & Therapy · doi:10.1186/s13287-016-0375-3 · Cited by 72 · see citing works

A novel indomethacin/methotrexate/MMP-9 siRNA in situ hydrogel with dual effects of anti-inflammatory activity and reversal of cartilage disruption for the synergistic treatment of rheumatoid arthritis

Yin, N., Tan, X., Liu, H., He, F., Ding, N., Gou, J., Yin, T., He, H., Zhang, Y. X., & Tang, X. (2020) · Nanoscale · doi:10.1039/d0nr00454e · Cited by 71 · see citing works

Functional peptide-based drug delivery systems

Lian, Z., & Ji, T. (2020) · Journal of Materials Chemistry B · doi:10.1039/d0tb00713g · Cited by 71 · see citing works

Scissor sisters: regulation of ADAM10 by the TspanC8 tetraspanins

Matthews, A. L., Szyroka, J., Collier, R., Noy, P. J., & Tomlinson, M. G. (2017) · Biochemical Society Transactions · doi:10.1042/bst20160290 · Cited by 71 · see citing works

New approaches to selectively target cancer-associated matrix metalloproteinase activity

Tauro, M., McGuire, J., & Lynch, C. C. (2014) · Cancer and Metastasis Reviews · doi:10.1007/s10555-014-9530-4 · Cited by 70 · see citing works

Molecular pathogenesis of genetic and sporadic aortic aneurysms and dissections

Shen, Y. H., & LeMaire, S. A. (2017) · Current Problems in Surgery · doi:10.1067/j.cpsurg.2017.01.001 · Cited by 70 · see citing works

The human brain NGF metabolic pathway is impaired in the pre-clinical and clinical continuum of Alzheimers disease

Pentz, R., Iulita, M. F., Ducatenzeiler, A., Bennett, D. A., & Cuello, A. C. (2021) · Molecular Psychiatry · doi:10.1038/s41380-020-0797-2 · Cited by 68 · see citing works

Mechanistic insights into a TIMP3-sensitive pathway constitutively engaged in the regulation of cerebral hemodynamics

Capone, C., Dabertrand, F., Baron‐Menguy, C., Chalaris, A., Ghezali, L., Domenga, V., Schmidt, S., Huneau, C., Rose‐John, S., Nelson, M. T., et al. (2016) · eLife · doi:10.7554/elife.17536 · Cited by 68 · see citing works

Genetic Polymorphisms and Sepsis in Premature Neonates

Esposito, S., Zampiero, A., Pugni, L., Tabano, S. M., Pelucchi, C., Ghirardi, B., Terranova, L., Miozzo, M. R., Mosca, F., & Principi, N. (2014) · PLoS ONE · doi:10.1371/journal.pone.0101248 · Cited by 67 · see citing works

Activity and components of the granulocyte colony‐stimulating factor pathway in hidradenitis suppurativa*

Wolk, K., Brembach, T.-C., Šimaitė, D., Bartnik, E., Cucinotta, S., Pokrywka, A., Irmer, M. L., Triebus, J., Witte‐Händel, E., Salinas, G., et al. (2021) · British Journal of Dermatology · doi:10.1111/bjd.19795 · Cited by 66 · see citing works

Research Progress on the Pathogenesis of Aortic Dissection

Yin, Z., Han, H., Yan, X., & Zheng, Q. (2022) · Current Problems in Cardiology · doi:10.1016/j.cpcardiol.2022.101249 · Cited by 66 · see citing works

Endothelial Glycocalyx Turnover in Vascular Health and Disease: Rethinking Endothelial Dysfunction

Toledo, A. G., Golden, G. J., Cummings, R. D., Malmström, J. A., & Esko, J. D. (2025) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-032620-104745 · Cited by 66 · see citing works

ADAM17 controls IL‐6 signaling by cleavage of the murine IL‐6Rα from the cell surface of leukocytes during inflammatory responses

Yan, I., Schwarz, J., Lücke, K., Schumacher, N., Schumacher, V., Schmidt, S., Rabe, B., Saftig, P., Donners, M., Rose-John, S., et al. (2016) · Journal of Leukocyte Biology · doi:10.1189/jlb.3a0515-207r · Cited by 67 · see citing works

Semaphorin 4D inhibits neutrophil activation and is involved in the pathogenesis of neutrophil-mediated autoimmune vasculitis

Nishide, M., Nojima, S., Ito, D., Takamatsu, H., Koyama, S., Kang, S., Kimura, T., Morimoto, K., Hosokawa, T., Hayama, Y., et al. (2017) · Annals of the Rheumatic Diseases · doi:10.1136/annrheumdis-2016-210706 · Cited by 66 · see citing works

Ectodomain Shedding by ADAM17: Its Role in Neutrophil Recruitment and the Impairment of This Process during Sepsis

Mishra, H. K., Ma, J., & Walcheck, B. K. (2017) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2017.00138 · Cited by 65 · see citing works

Matrix metalloproteinases as modulators of inflammation and innate immunity

Parks, W. C., Wilson, C. L., & López-Boado, Y. S. (2004) · Nature Reviews Immunology · doi:10.1038/nri1418 · Cited by 1,929 · see citing works

Metalloproteinases and their inhibitors in matrix remodeling

Matrisian, L. M. (1990) · Trends in Genetics · doi:10.1016/0168-9525(90)90126-q · Cited by 1,626 · see citing works

Metalloproteinases: a Functional Pathway for Myeloid Cells

Chou, J., Chan, M. F., & Werb, Z. (2016) · Microbiology Spectrum · doi:10.1128/microbiolspec.mchd-0002-2015 · Cited by 32 · see citing works

Metalloproteinases and Their Inhibitors: Potential for the Development of New Therapeutics

Raeeszadeh‐Sarmazdeh, M., Do, L. D., & Hritz, B. (2020) · Cells · doi:10.3390/cells9051313 · Cited by 333 · see citing works

Tissue inhibitors of metalloproteinases

Murphy, G. (2011) · Genome biology · doi:10.1186/gb-2011-12-11-233 · Cited by 472 · see citing works