Matrix metalloproteinases as modulators of inflammation and innate 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

How Matrix Metalloproteinases Regulate Cell Behavior

Sternlicht, M. D., & Werb, Z. (2001) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.17.1.463 · Cited by 3,959

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

Targeted disruption of the mouse transforming growth factor-β1 gene results in multifocal inflammatory disease

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Matrix metalloproteinase-9 triggers the angiogenic switch during carcinogenesis

Bergers, G., Brekken, R., McMahon, G., Vu, T. H., Itoh, T., Tamaki, K., Tanzawa, K., Thorpe, P., Itohara, S., Werb, Z., et al. (2000) · Nature Cell Biology · doi:10.1038/35036374 · Cited by 2,797

Matrix Metalloproteinase Inhibitors and Cancer—Trials and Tribulations

Coussens, L. M., Fingleton, B., & Matrisian, L. M. (2002) · Science · doi:10.1126/science.1067100 · Cited by 2,761

Points of control in inflammation

Nathan, C. (2002) · Nature · doi:10.1038/nature01320 · Cited by 2,738

A Mechanism for Regulating Pulmonary Inflammation and Fibrosis: The Integrin αvβ6 Binds and Activates Latent TGF β1

Munger, J. S., Huang, X., Kawakatsu, H., Griffiths, M. J. D., Dalton, S. L., Wu, J., Pittet, J.-F., Kaminski, N., Garat, C., Matthay, M. A., et al. (1999) · Cell · doi:10.1016/s0092-8674(00)80545-0 · Cited by 2,076

Cell surface-localized matrix metalloproteinase-9 proteolytically activates TGF-beta and promotes tumor invasion and angiogenesis.

Yu, Q., & Stamenkovic, I. (2000) · PubMed · Cited by 1,952

Cell surface-localized matrix metalloproteinase-9 proteolytically activates TGF-β and promotes tumor invasion and angiogenesis

Yu, Q., & Stamenkovic, I. (2000) · Genes & Development · doi:10.1101/gad.14.2.163 · Cited by 1,754

MMP-9/Gelatinase B Is a Key Regulator of Growth Plate Angiogenesis and Apoptosis of Hypertrophic Chondrocytes

Vu, T. H., Shipley, J. M., Bergers, G., Berger, J. E., Helms, J. A., Hanahan, D., Shapiro, S. D., Senior, R. M., & Werb, Z. (1998) · Cell · doi:10.1016/s0092-8674(00)81169-1 · Cited by 1,737

Mechanism Of Cell Surface Activation Of 72-kDa Type IV Collagenase

Strongin, A. Y., Collier, I. E., Bannikov, G. A., Marmer, B. L., Grant, G. A., & Goldberg, G. I. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.10.5331 · Cited by 1,589

Localization of Matrix Metalloproteinase MMP-2 to the Surface of Invasive Cells by Interaction with Integrin αvβ3

Brooks, P. C., Strömblad, S., Sanders, L. C., Schalscha, T. V., Aimes, R. T., Stetler‐Stevenson, W. G., Quigley, J. P., & Cheresh, D. A. (1996) · Cell · doi:10.1016/s0092-8674(00)81235-0 · Cited by 1,566

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

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

Requirement for Macrophage Elastase for Cigarette Smoke-Induced Emphysema in Mice

Hautamaki, R. D., Kobayashi, D. K., Senior, R. M., & Shapiro, S. D. (1997) · Science · doi:10.1126/science.277.5334.2002 · Cited by 1,470

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

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

Strategies for MMP inhibition in cancer: innovations for the post-trial era

Overall, C. M., & López-Otín, C. (2002) · Nature Reviews Cancer · doi:10.1038/nrc884 · Cited by 1,349

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

MMP-9 Supplied by Bone Marrow–Derived Cells Contributes to Skin Carcinogenesis

Coussens, L. M., Tinkle, C. L., Hanahan, D., & Werb, Z. (2000) · Cell · doi:10.1016/s0092-8674(00)00139-2 · Cited by 1,306

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

Matrix metalloproteinases: they're not just for matrix anymore!

McCawley, L. J., & Matrisian, L. M. (2001) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(00)00248-9 · Cited by 1,274

Processing of tumour necrosis factor-α precursor by metalloproteinases

Gearing, A. J. H., Beckett, P., Christodoulou, M., Churchill, M., Clements, J. M., Davidson, A. H., Drummond, A. H., GALLOWAY, W. A., Gilbert, R. J. C., Gordon, J. L., et al. (1994) · Nature · doi:10.1038/370555a0 · Cited by 1,194

Regulation of Intestinal α-Defensin Activation by the Metalloproteinase Matrilysin in Innate Host Defense

Wilson, C. L., Ouellette, A. J., Satchell, D. P., Ayabe, T., López-Boado, Y. S., Stratman, J. L., Hultgren, S. J., Matrisian, L. M., & Parks, W. C. (1999) · Science · doi:10.1126/science.286.5437.113 · Cited by 1,076

Effects of matrix metalloproteinase-9 gene knock-out on the proteolysis of blood-brain barrier and white matter components after cerebral ischemia

Asahi, M., Wang, X., Mori, T., Sumii, T., Jung, J.-C., Moskowitz, M. A., Fini, M. E., & Lo, E. H. (2001) · The Journal of Neuroscience · doi:10.1523/jneurosci.21-19-07724.2001 · Cited by 1,004

Matrix metalloproteinases 2 and 9 work in concert to produce aortic aneurysms

Longo, G. M., Xiong, W., Greiner, T. C., Zhao, Y., Fiotti, N., & Baxter, B. T. (2002) · Journal of Clinical Investigation · doi:10.1172/jci15334 · Cited by 979

Induction and Evasion of Host Defenses by Type 1-Piliated Uropathogenic Escherichia coli

Mulvey, M. A., López-Boado, Y. S., Wilson, C. L., Roth, R. A., Parks, W. C., Heuser, J., & Hultgren, S. J. (1998) · Science · doi:10.1126/science.282.5393.1494 · Cited by 971

Enhanced cleavage of type II collagen by collagenases in osteoarthritic articular cartilage.

Billinghurst, R. C., Dahlberg, L., Ionescu, M., Reiner, A., Bourne, R., Rorabeck, C. H., Mitchell, P. G., Hambor, J., Diekmann, O., Tschesche, H., et al. (1997) · Journal of Clinical Investigation · doi:10.1172/jci119316 · Cited by 970

S-nitrosylation of matrix metalloproteinases: signaling pathway to neuronal cell death

Gu, Z., Kaul, M., Yan, B., Kridel, S. J., Cui, J., Strongin, A., Smith, J. W., Liddington, R. C., & Lipton, S. A. (2002) · Science · doi:10.1126/science.1073634 · Cited by 950

2. Cytokines and chemokines

Borish, L., & Steinke, J. W. (2003) · Journal of Allergy and Clinical Immunology · doi:10.1067/mai.2003.108 · Cited by 914

Matrix metalloproteinases 2 and 9 work in concert to produce aortic aneurysms

Longo, G. M., Xiong, W., Greiner, T. C., Zhao, Y., Fiotti, N., & Baxter, B. T. (2002) · Journal of Clinical Investigation · doi:10.1172/jci0215334 · Cited by 877

Reduced angiogenesis and tumor progression in gelatinase A-deficient mice.

Itoh, T., Tanioka, M., Yoshida, H., Yoshioka, T., Nishimoto, H., & Itohara, S. (1998) · PubMed · Cited by 875

Targeted gene disruption of matrix metalloproteinase-9 (gelatinase B) suppresses development of experimental abdominal aortic aneurysms

Pyo, R. T., Lee, J. K., Shipley, J. M., Curci, J. A., Mao, D., Ziporin, S. J., Ennis, T. L., Shapiro, S. D., Senior, R. M., & Thompson, R. W. (2000) · Journal of Clinical Investigation · doi:10.1172/jci8931 · Cited by 829

Matrix metalloproteinases: structures, evolution, and diversification

Massova, I., Kotra, L. P., Fridman, R. A., & Mobashery, S. (1998) · The FASEB Journal · doi:10.1096/fasebj.12.12.1075 · Cited by 779

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

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

Bode, W., Gomis‐Rüth, F. X., & Stöckler, W. (1993) · FEBS Letters · doi:10.1016/0014-5793(93)80312-i · Cited by 762

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

The Membrane-Anchored MMP Inhibitor RECK Is a Key Regulator of Extracellular Matrix Integrity and Angiogenesis

Oh, J., Takahashi, R., Kondo, S., Mizoguchi, A., Adachi, E., Sasahara, R. M., Nishimura, S., Imamura, Y., Kitayama, H., Alexander, D. B., et al. (2001) · Cell · doi:10.1016/s0092-8674(01)00597-9 · Cited by 728

Matrix metalloproteinase degradation of extracellular matrix: biological consequences

Shapiro, S. D. (1998) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(98)80035-5 · Cited by 714

Mice lacking neutrophil elastase reveal impaired host defense against gram negative bacterial sepsis

Belaaouaj, A., McCarthy, R., Baumann, M. L., Gao, Z., Ley, T. J., Abraham, S. N., & Shapiro, S. D. (1998) · Nature Medicine · doi:10.1038/nm0598-615 · Cited by 691

Generation of biologically active IL-1 beta by matrix metalloproteinases: a novel caspase-1-independent pathway of IL-1 beta processing.

Schönbeck, U., Mach, F., & Libby, P. (1998) · PubMed · Cited by 681

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

Membrane Type I Matrix Metalloproteinase Usurps Tumor Growth Control Imposed by the Three-Dimensional Extracellular Matrix

Hotary, K. B., Allen, E. D., Brooks, P. C., Datta, N. S., Long, M. W., & Weiss, S. J. (2003) · Cell · doi:10.1016/s0092-8674(03)00513-0 · Cited by 674

Impaired endochondral ossification and angiogenesis in mice deficient in membrane-type matrix metalloproteinase I

Zhou, Z., Apte, S. S., Soininen, R., Cao, R., Baaklini, G. Y., Rauser, R. W., Wang, J., Cao, Y., & Tryggvason, K. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.060037197 · Cited by 666

A novel function for tissue inhibitor of metalloproteinases-3 (TIMP3): inhibition of angiogenesis by blockage of VEGF binding to VEGF receptor-2

Qi, J. H., Ebrahem, Q., Moore, N., Murphy, G., Claesson-Welsh, L., Bond, M., Baker, A., & Anand-Apte, B. (2003) · Nature Medicine · doi:10.1038/nm846 · Cited by 658

Matrix Metalloproteinase Stromelysin-1 Triggers a Cascade of Molecular Alterations That Leads to Stable Epithelial-to-Mesenchymal Conversion and a Premalignant Phenotype in Mammary Epithelial Cells

Lochter, A., Galosy, S., Muschler, J. L., Freedman, N. D., Werb, Z., & Bissell, M. J. (1997) · The Journal of Cell Biology · doi:10.1083/jcb.139.7.1861 · Cited by 657

Matrix Metalloproteinase Activity Inactivates the CXC Chemokine Stromal Cell-derived Factor-1

McQuibban, G. A., Butler, G. S., Gong, J.-H., Bendall, L. J., Power, C., Clark‐Lewis, I., & Overall, C. M. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m107736200 · Cited by 655

Epithelial cells as sensors for microbial infection.

Kagnoff, M. F., & Eckmann, L. (1997) · Journal of Clinical Investigation · doi:10.1172/jci119522 · Cited by 619

The Activity of Collagenase-1 Is Required for Keratinocyte Migration on a Type I Collagen Matrix

Pilcher, B. K., Dumin, J. A., Sudbeck, B. D., Krane, S. M., Welgus, H. G., & Parks, W. C. (1997) · The Journal of Cell Biology · doi:10.1083/jcb.137.6.1445 · Cited by 613

Matrix metalloproteinase processing of monocyte chemoattractant proteins generates CC chemokine receptor antagonists with anti-inflammatory properties in vivo

McQuibban, G. A., Gong, J.-H., Wong, J., Wallace, J. L., Clark‐Lewis, I., & Overall, C. M. (2002) · Blood · doi:10.1182/blood.v100.4.1160.h81602001160_1160_1167 · Cited by 611

Role for Matrix Metalloproteinase 9 after Focal Cerebral Ischemia: Effects of Gene Knockout and Enzyme Inhibition with BB-94

Asahi, M., Asahi, K., Jung, J., del Zoppo, G. J., Fini, M. E., & Lo, E. H. (2000) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1097/00004647-200012000-00007 · Cited by 610

Regulation of Cell Invasion and Morphogenesis in a Three-Dimensional Type I Collagen Matrix by Membrane-Type Matrix Metalloproteinases 1, 2, and 3

Hotary, K. B., Allen, E. D., Punturieri, A., Yana, I., & Weiss, S. J. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.149.6.1309 · Cited by 596

Generation of Biologically Active IL-1β by Matrix Metalloproteinases: A Novel Caspase-1-Independent Pathway of IL-1β Processing

Schönbeck, U., Mach, F., & Libby, P. (1998) · The Journal of Immunology · doi:10.4049/jimmunol.161.7.3340 · Cited by 595

Loss of collagenase-2 confers increased skin tumor susceptibility to male mice

Balbı́n, M., Fueyo, A., Tester, A. M., Pendás, A. M., Pitiot, A. S., Astudillo, A., Overall, C. M., Shapiro, S. D., & López-Otı́n, C. (2003) · Nature Genetics · doi:10.1038/ng1249 · Cited by 550

Cytokines and Chemokines

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TIMP-2 Mediated Inhibition of Angiogenesis

Seo, D. W., Li, H., Guédez, L., Wingfield, P. T., Diaz, T., Salloum, R., Wei, B., & Stetler‐Stevenson, W. G. (2003) · Cell · doi:10.1016/s0092-8674(03)00551-8 · Cited by 511

Metalloelastase is required for macrophage-mediated proteolysis and matrix invasion in mice.

Shipley, J. M., Wesselschmidt, R. L., Kobayashi, D. K., Ley, T. J., & Shapiro, S. D. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.9.3942 · Cited by 502

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

CD44 anchors the assembly of matrilysin/MMP-7 with heparin-binding epidermal growth factor precursor and ErbB4 and regulates female reproductive organ remodelingPreprint

Yu, W., Woessner, J. F., McNeish, J. D., & Stamenkovic, I. (2002) · Genes & Development · doi:10.1101/gad.925702 · Cited by 473

Oxidative Autoactivation of Latent Collagenase by Human Neutrophils

Weiss, S. J., Peppin, G. J., Ortiz, X., Ragsdale, C. G., & Test, S. T. (1985) · Science · doi:10.1126/science.2982211 · Cited by 472

The metalloproteinase matrilysin proteolytically generates active soluble Fas ligand and potentiates epithelial cell apoptosis

Powell, W. C., Fingleton, B., Wilson, C. L., Boothby, M. R., & Matrisian, L. M. (1999) · Current Biology · doi:10.1016/s0960-9822(00)80113-x · Cited by 421

Cleavage of Syndecan-1 by Membrane Type Matrix Metalloproteinase-1 Stimulates Cell Migration

Endo, K., Takino, T., Miyamori, H., Kinsen, H., Yoshizaki, T., Furukawa, M., & Sato, H. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m306736200 · Cited by 411

Targeted expression of stromelysin-1 in mammary gland provides evidence for a role of proteinases in branching morphogenesis and the requirement for an intact basement membrane for tissue-specific gene expression [published erratum appears in J Cell Biol 1996 Feb;132(4):following 752]

Sympson, C. J. (1994) · The Journal of Cell Biology · doi:10.1083/jcb.125.3.681 · Cited by 400

Gelatinase B: a tuner and amplifier of immune functions

Opdenakker, G., den Steen, P. E. V., & Damme, J. V. (2001) · Trends in Immunology · doi:10.1016/s1471-4906(01)02023-3 · Cited by 398

Degradation of Interleukin 1β by Matrix Metalloproteinases

Itô, A., Mukaiyama, A., Itoh, Y., Nagase, H., Thøgersen, I. B., Enghild, J. J., Sasaguri, Y., & Mori, Y. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.25.14657 · Cited by 390

TIMP-2 Is Required for Efficient Activation of proMMP-2 in Vivo

Wang, Z., Jüttermann, R., & Soloway, P. D. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m001270200 · Cited by 388

The Serpin α1-Proteinase Inhibitor Is a Critical Substrate for Gelatinase B/MMP-9 In Vivo

Liu, Z., Zhou, X., Shapiro, S. D., Shipley, J. M., Twining, S. S., Diaz, L. A., Senior, R. M., & Werb, Z. (2000) · Cell · doi:10.1016/s0092-8674(00)00087-8 · Cited by 386

Matrix metalloproteinases in repair

Parks, W. C. (1999) · Wound Repair and Regeneration · doi:10.1046/j.1524-475x.1999.00423.x · Cited by 384

Matrilysin: An epithelial matrix metalloproteinase with potentially novel functions

Wilson, C. L., & Matrisian, L. M. (1996) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/1357-2725(95)00121-2 · Cited by 373

Macrophage Metalloelastase Mediates Acute Cigarette Smoke–induced Inflammation via Tumor Necrosis Factor-α Release

Churg, A., Wang, R. D., Tai, H., Wang, X., Xie, C., Dai, J. M., Shapiro, S. D., & Wright, J. L. (2003) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.200212-1396oc · Cited by 366

Matrix metalloproteinase-7–dependent release of tumor necrosis factor-α in a model of herniated disc resorption

Haro, H., Crawford, H. C., Fingleton, B., Shinomiya, K., Spengler, D. M., & Matrisian, L. M. (2000) · Journal of Clinical Investigation · doi:10.1172/jci7091 · Cited by 364

Matrilysin is expressed by lipid-laden macrophages at sites of potential rupture in atherosclerotic lesions and localizes to areas of versican deposition, a proteoglycan substrate for the enzyme.

Halpert, I., Sires, U. I., Roby, J. D., Potter‐Perigo, S., Wight, T. N., Shapiro, S. D., Welgus, H. G., Wickline, S. A., & Parks, W. C. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.18.9748 · Cited by 361

Matrix metalloproteinase 2 releases active soluble ectodomain of fibroblast growth factor receptor 1.

Levi, E., Fridman, R., Miao, H. Q., Ma, Y. S., Yayon, A., & Vlodavsky, I. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.14.7069 · Cited by 351

The Secreted Protein Discovery Initiative (SPDI), a Large-Scale Effort to Identify Novel Human Secreted and Transmembrane Proteins: A Bioinformatics AssessmentPreprint

Clark, H. F., Gurney, A. L., Abaya, E., Baker, K. P., Baldwin, D. T., Brush, J., Chen, J., Chow, B., Chui, C. H., Crowley, C. W., et al. (2003) · Genome Research · doi:10.1101/gr.1293003 · Cited by 335

Matrix Metalloproteinase-3 Releases Active Heparin-binding EGF-like Growth Factor by Cleavage at a Specific Juxtamembrane Site

Suzuki, M., Raab, G., Moses, M. A., Fernández, C. A., & Klagsbrun, M. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.50.31730 · Cited by 331

Matrilysin (Matrix Metalloproteinase-7) Mediates E-Cadherin Ectodomain Shedding in Injured Lung Epithelium

McGuire, J. K., Li, Q., & Parks, W. C. (2003) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)64318-0 · Cited by 323

Binding of Active (57 kDa) Membrane Type 1-Matrix Metalloproteinase (MT1-MMP) to Tissue Inhibitor of Metalloproteinase (TIMP)-2 Regulates MT1-MMP Processing and Pro-MMP-2 Activation

Hernandez‐Barrantes, S., Tóth, M., Bernardo, M. M., Yurkova, M. S., Gervasi, D. C., Raz, Y., Sang, Q. A., & Fridman, R. A. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.16.12080 · Cited by 313

Loss of Matrix Metalloproteinase-9 or Matrix Metalloproteinase-12 Protects Apolipoprotein E–Deficient Mice Against Atherosclerotic Media Destruction but Differentially Affects Plaque Growth

Luttun, A., Lutgens, E., Manderveld, A., Maris, K., Collen, D., Carmeliet, P., & Moons, L. (2004) · Circulation · doi:10.1161/01.cir.0000121728.14930.de · Cited by 308

Overlapping and enzyme-specific contributions of matrix metalloproteinases-9 and -12 in IL-13–induced inflammation and remodeling

Lanone, S., Zheng, T., Zhu, Z., Liu, W., Lee, C. G., Ma, B., Chen, Q., Homer, R., Wang, J., Rabach, L. A., et al. (2002) · Journal of Clinical Investigation · doi:10.1172/jci14136 · Cited by 307

The Role of Matrix Metalloproteinase-2 and Matrix Metalloproteinase-9 in Antibody-Induced Arthritis

Itoh, T., Matsuda, H., Tanioka, M., Kuwabara, K., Itohara, S., & Suzuki, R. (2002) · The Journal of Immunology · doi:10.4049/jimmunol.169.5.2643 · Cited by 304

HIV-induced metalloproteinase processing of the chemokine stromal cell derived factor-1 causes neurodegeneration

Zhang, K., McQuibban, G. A., Silva, C., Butler, G. S., Johnston, J. B., Holden, J. K., Clark‐Lewis, I., Overall, C. M., & Power, C. (2003) · Nature Neuroscience · doi:10.1038/nn1127 · Cited by 304

Extracellular Matrix Metalloproteinase 2 Levels Are Regulated by the Low Density Lipoprotein-related Scavenger Receptor and Thrombospondin 2

Yang, Z., Strickland, D. K., & BORNSTEIN, P. K. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m008925200 · Cited by 301

Gelatinase B/MMP‐9 and neutrophil collagenase/MMP‐8 process the chemokines human GCP‐2/CXCL6, ENA‐78/CXCL5 and mouse GCP‐2/LIX and modulate their physiological activities

den Steen, P. E. V., Wuyts, A., Husson, S. J., Proost, P., Damme, J. V., & Opdenakker, G. (2003) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2003.03760.x · Cited by 293

Matrix Metalloproteinases 9 and 2 Are Necessary for the Migration of Langerhans Cells and Dermal Dendritic Cells from Human and Murine Skin

Ratzinger, G., Stoitzner, P., Ebner, S., Lutz, M. B., Layton, G. T., Rainer, C., Senior, R. M., Shipley, J. M., Fritsch, P. O., Schuler, G., et al. (2002) · The Journal of Immunology · doi:10.4049/jimmunol.168.9.4361 · Cited by 292

Paneth cell defensins: Endogenous peptide components of intestinal host defense

Ouellette, A. J., & Selsted, M. E. (1996) · The FASEB Journal · doi:10.1096/fasebj.10.11.8836041 · Cited by 283

Enamelysin (Matrix Metalloproteinase 20)-deficient Mice Display an Amelogenesis Imperfecta Phenotype

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Matrilysin expression and function in airway epithelium.

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Subantimicrobial Dose Doxycycline Efficacy as a Matrix Metalloproteinase Inhibitor in Chronic Periodontitis Patients Is Enhanced When Combined With a Non‐Steroidal Anti‐Inflammatory Drug

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Matrix Metalloproteinase 9 Protects Mice from Anti–Glomerular Basement Membrane Nephritis through Its Fibrinolytic Activity

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