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 · see citing works

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 · 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

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

Shull, M. M., Ormsby, I., Kier, A. B., Pawlowski, S., Diebold, R. J., Yin, M., Allen, R., Sidman, C., Proetzel, G., Calvin, D., et al. (1992) · Nature · doi:10.1038/359693a0 · Cited by 2,985 · see citing works

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 · see citing works

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 · see citing works

Points of control in inflammation

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

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 · see citing works

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 · see citing works

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 · see citing works

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 · 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

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 · see citing works

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 1,552 · see citing works

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

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

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 · see citing works

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 · 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

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 · 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

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 951 · see citing works

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 · see citing works

2. Cytokines and chemokines

Borish, L., & Steinke, J. W. (2003) · Journal of Allergy and Clinical Immunology · doi:10.1067/mai.2003.108 · Cited by 881 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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

Zhou, Z., Apte, 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 791 · see citing works

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 · 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

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 · 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

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 · see citing works

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 · see citing works

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 · see citing works

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 · 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

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 677 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

Epithelial cells as sensors for microbial infection.

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

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 · see citing works

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 · see citing works

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 · see citing works

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 605 · see citing works

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 594 · see citing works

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 536 · see citing works

Cytokines and Chemokines

(2010) · CRC Press eBooks · doi:10.1201/ebk1439802687-c10 · Cited by 516 · see citing works

TIMP-2 Mediated Inhibition of Angiogenesis

Seo, D. W., Li, H., Guédez, L., Wingfield, P. T., Diaz, T., Salloum, R. G., Wei, B., & Stetler‐Stevenson, W. G. (2003) · Cell · doi:10.1016/s0092-8674(03)00551-8 · Cited by 508 · see citing works

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 · 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

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 · see citing works

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 472 · see citing works

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 424 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 388 · see citing works

Matrix metalloproteinases in repair

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

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 · see citing works

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 · see citing works

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 · see citing works

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 359 · see citing works

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 · see citing works

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 · see citing works

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 330 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 306 · see citing works

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 305 · see citing works

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 · see citing works

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 297 · see citing works

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 · see citing works

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 289 · see citing works

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 · see citing works

Membrane protease proteomics: Isotope-coded affinity tag MS identification of undescribed MT1–matrix metalloproteinase substrates

Tam, E. M., Morrison, C., Wu, Y., Stack, M. S., & Overall, C. M. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0305862101 · Cited by 277 · see citing works

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

Caterina, J. J., Skobe, Z., Shi, J., Ding, Y., Simmer, J. P., Birkedal‐Hansen, H., & Bartlett, J. D. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m209100200 · Cited by 270 · see citing works

Matrilysin expression and function in airway epithelium.

Dunsmore, S. E., Saarialho‐Kere, U., Roby, J. D., Wilson, C. L., Matrisian, L. M., Welgus, H. G., & Parks, W. C. (1998) · Journal of Clinical Investigation · doi:10.1172/jci1516 · Cited by 270 · see citing works

Decreased allergic lung inflammatory cell egression and increased susceptibility to asphyxiation in MMP2-deficiency

Corry, D. B., Rishi, K., Kanellis, J., Kiss, A., Song, L., Xu, J., Feng, L., Werb, Z., & Kheradmand, F. (2002) · Nature Immunology · doi:10.1038/ni773 · Cited by 263 · see citing works

Resistance of young gelatinase B–deficient mice to experimental autoimmune encephalomyelitis and necrotizing tail lesions

Dubois, B., Masure, S., Hurtenbach, U., Paemen, L. R., Heremans, H., van den Oord, J., Sciot, R., Meinhardt, T., Hämmerling, G. J., Opdenakker, G., et al. (1999) · Journal of Clinical Investigation · doi:10.1172/jci6886 · Cited by 262 · see citing works

Matrix Metalloproteinase-9 Facilitates Remyelination in Part by Processing the Inhibitory NG2 Proteoglycan

Larsen, P. H., Wells, J. E. A., Stallcup, W. B., Opdenakker, G., & Yong, V. W. (2003) · Journal of Neuroscience · doi:10.1523/jneurosci.23-35-11127.2003 · Cited by 260 · see citing works

Activation of the endogenous metalloproteinase, gelatinase, by triggered human neutrophils.

Peppin, G. J., & Weiss, S. J. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.12.4322 · Cited by 258 · see citing works

Sites of collagenase cleavage and denaturation of type II collagen in aging and osteoarthritic articular cartilage and their relationship to the distribution of matrix metalloproteinase 1 and matrix metalloproteinase 13

Wu, W. K. K., Billinghurst, R. C., Pidoux, I., Antoniou, J., Zukor, D. J., Tänzer, M., & Poole, A. R. (2002) · Arthritis & Rheumatism · doi:10.1002/art.10428 · Cited by 250 · see citing works

Matrix Metalloproteinase-dependent Activation of Latent Transforming Growth Factor-β Controls the Conversion of Osteoblasts into Osteocytes by Blocking Osteoblast Apoptosis

Karsdal, M. A., Larsen, L., Engsig, M. T., Lou, H., Ferreras, M., Lochter, A., Delaissé, J., & Foged, N. T. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m207205200 · Cited by 249 · see citing works

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/jci0214136 · Cited by 247 · see citing works

Gelatinase B–deficient Mice Are Resistant to Experimental Bullous Pemphigoid

Liu, Z., Shipley, J. M., Vu, T. H., Zhou, X., Diaz, L. A., Werb, Z., & Senior, R. M. (1998) · The Journal of Experimental Medicine · doi:10.1084/jem.188.3.475 · Cited by 243 · see citing works

Identification and Enzymatic Characterization of Two Diverging Murine Counterparts of Human Interstitial Collagenase (MMP-1) Expressed at Sites of Embryo Implantation

Balbı́n, M., Fueyo, A., Knäuper, V., López, J. M., Álvarez, J., Sánchez, L. M., Quesada, V., Bordallo, J., Murphy, G., & López-Otı́n, C. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m007674200 · Cited by 239 · see citing works

Airway Epithelial Cell Migration Dynamics: MMP-9 Role in Cell–Extracellular Matrix Remodeling

Legrand, C., Gilles, C., Zahm, J., Polette, M., Buisson, A., Kaplan, H., Birembaut, P. L., & Tournier, J. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.146.2.517 · Cited by 237 · see citing works

Transforming growth factor-beta 1 knockout mice. A mutation in one cytokine gene causes a dramatic inflammatory disease.

Kulkarni, A. B., & Karlsson, S. (1993) · PubMed · Cited by 234 · see citing works

Response to local inflammation of IL-1 beta-converting enzyme- deficient mice

Fantuzzi, G., Ku, G., Harding, M. W., Livingston, D. J., Sipe, J. D., Kuida, K., Flavell, R. A., & Dinarello, C. A. (1997) · The Journal of Immunology · doi:10.4049/jimmunol.158.4.1818 · Cited by 232 · see citing works

Heparan Sulfate Proteoglycans as Extracellular Docking Molecules for Matrilysin (Matrix Metalloproteinase 7)

Yu, W., & Woessner, J. F. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.6.4183 · Cited by 232 · see citing works

Cloning and Characterization of Human MMP-23, a New Matrix Metalloproteinase Predominantly Expressed in Reproductive Tissues and Lacking Conserved Domains in Other Family Members

Velasco, G., Pendás, A. M., Fueyo, A., Knäuper, V., Murphy, G., & López-Otı́n, C. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.8.4570 · Cited by 232 · see citing works

Membrane Type 4 Matrix Metalloproteinase (MMP17) Has Tumor Necrosis Factor-α Convertase Activity but Does Not Activate Pro-MMP2

English, W., Puente, X. S., Freije, J. M. P., Knäuper, V., Amour, A., Merryweather, A., López-Otı́n, C., & Murphy, G. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.19.14046 · Cited by 229 · see citing works

Persistence of Atherosclerotic Plaque but Reduced Aneurysm Formation in Mice With Stromelysin-1 (MMP-3) Gene Inactivation

Silence, J., Lupu, F., Collen, D., & LIJNEN, H. R. (2001) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/hq0901.097004 · Cited by 229 · see citing works

Prevention of interleukin-8-induced mobilization of hematopoietic progenitor cells in rhesus monkeys by inhibitory antibodies against the Metalloproteinase gelatinase B (MMP-9)

Pruijt, H., Fibbe, W. E., Laterveer, L., Pieters, R. A., Lindley, I. J. D., Paemen, L. R., Masure, S., Willemze, R., & Opdenakker, G. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.19.10863 · Cited by 228 · see citing works

Matrix Metalloproteinases (MMPs) Regulate Fibrin-invasive Activity via MT1-MMP–dependent and –independent Processes

Hotary, K. B., Yana, I., Sabeh, F., Li, X.-Y., Holmbeck, K., Birkedal‐Hansen, H., Allen, E. D., Hiraoka, N., & Weiss, S. J. (2002) · The Journal of Experimental Medicine · doi:10.1084/jem.20010815 · Cited by 217 · see citing works

Pro-collagenase-1 (Matrix Metalloproteinase-1) Binds the α2β1 Integrin upon Release from Keratinocytes Migrating on Type I Collagen

Dumin, J. A., Dickeson, S. K., Stricker, T. P., Bhattacharyya‐Pakrasi, M., Roby, J. D., Santoro, S. A., & Parks, W. C. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m104179200 · Cited by 211 · see citing works

Overlapping and independent contributions of MMP2 and MMP9 to lung allergic inflammatory cell egression through decreased CC chemokines

Corry, D. B., Kiss, A., Song, L., Song, L., Xu, J., Lee, S., Werb, Z., & Kheradmand, F. (2004) · The FASEB Journal · doi:10.1096/fj.03-1412fje · Cited by 209 · see citing works

Symptomatic efficacy of avocado/soybean unsaponifiables in the treatment of osteoarthritis of the knee and hip: A prospective, randomized, double-blind, placebo-controlled, multicenter clinical trial with a six-month treatment period and a two-month followup demonstrating a persistent effect

Maheu, E., Mazi�res, B., Valat, J., Loyau, G., Lo�t, X. L., Bourgeois, P., Grouin, J., & Rozenberg, S. (1998) · Arthritis & Rheumatism · doi:10.1002/1529-0131(199801)41:1 · Cited by 207 · see citing works

An Adverse Role for Matrix Metalloproteinase 12 after Spinal Cord Injury in Mice

Wells, J. E. A., Rice, T. K., Nuttall, R. K., Edwards, D. R., Zekki, H., Rivest, S., & Yong, V. W. (2003) · Journal of Neuroscience · doi:10.1523/jneurosci.23-31-10107.2003 · Cited by 203 · see citing works

Gelatinase B is required for alveolar bronchiolization after intratracheal bleomycin.

Betsuyaku, T., Fukuda, Y., Parks, W. C., Shipley, J., & Senior, R. M. (2000) · American Journal of Pathology · doi:10.1016/s0002-9440(10)64563-4 · Cited by 203 · see citing works

The Τumor Necrosis Factor-α Converting Enzyme (TACE): A Unique Metalloproteinase with Highly Defined Substrate Selectivity

Mohan, M. J., Seaton, T., Mitchell, J. L., Howe, A., Blackburn, K., Burkhart, W., Moyer, M. B., Patel, I., Waitt, G. M., Becherer, J. D., et al. (2002) · Biochemistry · doi:10.1021/bi0260132 · Cited by 199 · see citing works

MMP‐2 and MMP‐9 synergize in promoting choroidal neovascularization

Lambert, V., Wielockx, B., Munaut, C., Galopin, C., Jost, M., Itoh, T., Werb, Z., Baker, A. H., Libert, C., Krell, H., et al. (2003) · The FASEB Journal · doi:10.1096/fj.03-0113fje · Cited by 189 · see citing works

Matrix Metalloproteinase-9 Deficiency Results in Enhanced Allergen-Induced Airway Inflammation

McMillan, S. J., Kearley, J., Campbell, J. D., Zhu, X., Larbi, K. Y., Shipley, J. M., Senior, R. M., Nourshargh, S., & Lloyd, C. M. (2004) · The Journal of Immunology · doi:10.4049/jimmunol.172.4.2586 · Cited by 185 · see citing works

Matrix Metalloproteinase-9 Is Required for Adequate Angiogenic Revascularization of Ischemic Tissues

Johnson, C., Sung, H., Lessner, S. M., Fini, M. E., & Galis, Z. S. (2003) · Circulation Research · doi:10.1161/01.res.0000111527.42357.62 · Cited by 184 · see citing works

Matrix metalloproteinase-3–dependent generation of a macrophage chemoattractant in a model of herniated disc resorption

Haro, H., Crawford, H. C., Fingleton, B., MacDougall, J. R., Shinomiya, K., Spengler, D. M., & Matrisian, L. M. (2000) · Journal of Clinical Investigation · doi:10.1172/jci7090 · Cited by 183 · see citing works

Bacterial Exposure Induces and Activates Matrilysin in Mucosal Epithelial Cells

López-Boado, Y. S., Wilson, C. L., Hooper, L. V., Gordon, J. I., Hultgren, S. J., & Parks, W. C. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.148.6.1305 · Cited by 179 · see citing works

Matrix Metalloproteinase Matrilysin Is Constitutively Expressed in Adult Human Exocrine Epithelium

Saarialho‐Kere, U., Crouch, E. C., & Parks, W. C. (1995) · Journal of Investigative Dermatology · doi:10.1111/1523-1747.ep12317104 · Cited by 169 · see citing works

Matrix Metalloproteinase-9 Deficiency Impairs Cellular Infiltration and Bronchial Hyperresponsiveness during Allergen-Induced Airway Inflammation

Cataldo, D. D., Tournoy, K. G., Vermaelen, K. Y., Munaut, C., Foidart, J., Louis, R. E., Noël, A., & PAUWELS, R. A. (2002) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)64205-8 · Cited by 163 · see citing works

Role of Stromelysin 1 and Gelatinase B in Experimental Acute Lung Injury

Warner, R. L., Beltrán, L., Younkin, E. M., Lewis, C. S., Weiss, S. J., Varani, J., & Johnson, K. J. (2001) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/ajrcmb.24.5.4160 · Cited by 156 · see citing works

Hypochlorous Acid Generated by Myeloperoxidase Modifies Adjacent Tryptophan and Glycine Residues in the Catalytic Domain of Matrix Metalloproteinase-7 (Matrilysin)

Fu, X., Kassim, S. Y., Parks, W. C., & Heinecke, J. W. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304739200 · Cited by 152 · see citing works

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

Lee, H., Ciancio, S. G., Tüter, G., RYAN, M. E., Komaroff, E., & Golub, L. M. (2004) · Journal of Periodontology · doi:10.1902/jop.2004.75.3.453 · Cited by 150 · see citing works

Inactivating Mutation of the Mouse Tissue Inhibitor of Metalloproteinases-2(Timp-2) Gene Alters ProMMP-2 Activation

Caterina, J. J., Yamada, S. S., Caterina, N. C. M., Longenecker, G., Holmbäck, K., Shi, J., Yermovsky-Kammerer, A. E., Engler, J. A., & Birkedal‐Hansen, H. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m001271200 · Cited by 149 · see citing works

Identification and characterization of a novel collagenase in Xenopus laevis: possible roles during frog development.

Stolow, M. A., Bauzon, D. D., Li, J., Sedgwick, T., Liang, V. C.-T., Sang, Q. A., & Shi, Y. (1996) · Molecular Biology of the Cell · doi:10.1091/mbc.7.10.1471 · Cited by 140 · see citing works

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

Lelongt, B., Bengatta, S., Delauche, M., Lund, L. R., Werb, Z., & Ronco, P. M. (2001) · The Journal of Experimental Medicine · doi:10.1084/jem.193.7.793 · Cited by 140 · see citing works

Diminished corneal angiogenesis in gelatinase A‐deficient mice

Kato, T., Kure, T., Chang, J.-H., Gabison, E. E., Itoh, T., Itohara, S., & Azar, D. T. (2001) · FEBS Letters · doi:10.1016/s0014-5793(01)02897-6 · Cited by 134 · 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

The First Stage of Transforming Growth Factor β1 Activation is Release of the Large Latent Complex from the Extracellular Matrix of Growth Plate Chondrocytes by Matrix Vesicle Stromelysin-1 (MMP-3)

Maeda, S., Dean, D. D., Gómez, R., Schwartz, Z., & Boyan, B. D. (2002) · Calcified Tissue International · doi:10.1007/s002230010032 · Cited by 131 · see citing works

Post-translational Proteolytic Processing of Procollagen C-terminal Proteinase Enhancer Releases a Metalloproteinase Inhibitor

Mott, J. D., Thomas‐Virnig, C. L., Rosenbach, M. T., Takahara, K., Greenspan, D. S., & Banda, M. J. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.2.1384 · Cited by 131 · see citing works

Collagenase-3 Binds to a Specific Receptor and Requires the Low Density Lipoprotein Receptor-related Protein for Internalization

Barmina, O. Y., Walling, H. W., Fiacco, G. J., Freije, J. M. P., López-Otı́n, C., Jeffrey, J. J., & Partridge, N. C. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.42.30087 · Cited by 124 · see citing works

Identification of MMP-18, a Putative Novel Human Matrix Metalloproteinase

Cossins, J., Dudgeon, T. J., Catlin, G., Gearing, A. J. H., & Clements, J. M. (1996) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1996.1688 · Cited by 122 · see citing works

Studies on the ability of 65-kDa and 92-kDa tumor cell gelatinases to degrade type IV collagen.

Mackay, A. R., Hartzler, J. L., Pelina, M. D., & Thorgeirsson, U. P. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)45827-9 · Cited by 113 · see citing works

Reduced Choroidal Neovascular Membrane Formation in Matrix Metalloproteinase-2–Deficient Mice

Berglin, L., Sarman, S., van der Ploeg, I., Steén, B., Ming, Y., Itohara, S., Seregard, S., & Kvanta, A. (2003) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.02-0180 · Cited by 109 · see citing works

Metalloproteinases Are Involved in Lipopolysaccharide– and Tumor Necrosis Factor-–Mediated Regulation of CXCR1 and CXCR2 Chemokine Receptor Expression

Khandaker, M. H., Mitchell, G. B., Xu, L., Andrews, J. D., Singh, R., Leung, H. C. H., Madrenas, J., Ferguson, S. S. G., Feldman, R. D., & Kelvin, D. J. (1999) · Blood · doi:10.1182/blood.v93.7.2173 · Cited by 100 · see citing works

Gelatinase B/matrix metalloproteinase‐9 cleaves interferon‐β and is a target for immunotherapy

Nelissen, I., Martens, E., den Steen, P. E. V., Proost, P., Ronsse, I., & Opdenakker, G. (2003) · Brain · doi:10.1093/brain/awg129 · Cited by 100 · see citing works

A Proteomic Approach for the Identification of Cell-surface Proteins Shed by Metalloproteases

Guo, L., Eisenman, J. R., Mahimkar, R., Peschon, J. J., Paxton, R. J., Black, R. A., & Johnson, R. S. (2002) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m100020-mcp200 · Cited by 96 · see citing works

Reduced Retinal Angiogenesis in MMP-2–Deficient Mice

Ohno‐Matsui, K., Uetama, T., Yoshida, T., Hayano, M., Itoh, T., Morita, I., & Mochizuki, M. (2003) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.03-0249 · Cited by 90 · see citing works

Proteolytic processing of laminin‐5 by MT1‐MMP in tissues and its effects on epithelial cell morphology

Koshikawa, N., Schenk, S., Moeckel, G. W., Sharabi, A. B., Miyazaki, K., Gardner, H., Zent, R., & Quaranta, V. (2003) · The FASEB Journal · doi:10.1096/fj.03-0584fje · Cited by 87 · see citing works

The Role of Tumor Necrosis Factor in Increased Airspace Epithelial Permeability in Acute Lung Inflammation

Li, X. Y., Donaldson, K., Brown, D. M., & MacNee, W. (1995) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/ajrcmb.13.2.7626286 · Cited by 87 · see citing works

Regulation of Matrilysin Expression in Airway Epithelial Cells by Pseudomonas aeruginosa Flagellin

López-Boado, Y. S., Wilson, C. L., & Parks, W. C. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m107121200 · Cited by 81 · see citing works

The Role of Metalloelastase in Immune Complex-Induced Acute Lung Injury

Warner, R. L., Lewis, C. S., Beltrán, L., Younkin, E. M., Varani, J., & Johnson, K. J. (2001) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)64685-8 · Cited by 79 · see citing works

Structural Analysis of the α2 Integrin I Domain/Procollagenase-1 (Matrix Metalloproteinase-1) Interaction

Stricker, T. P., Dumin, J. A., Dickeson, S. K., Chung, L., Nagase, H., Parks, W. C., & Santoro, S. A. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m102217200 · Cited by 73 · see citing works

Matrilysin-dependent Elastolysis by Human Macrophages

Filippov, S. I., Caras, I. W., Murray, R. M., Matrisian, L. M., Chapman, H. A., Shapiro, S. D., & Weiss, S. J. (2003) · The Journal of Experimental Medicine · doi:10.1084/jem.20030626 · Cited by 66 · see citing works

Detection of collagenase-induced damage of collagen by 9A4, a monoclonal C-terminal neoepitope antibody

Otterness, I. G., Downs, J. T., Lane, C. L., Bliven, M. L., Stukenbrok, H., Scampoli, D. N., Milici, A. J., & Mézeš, P. (1999) · Matrix Biology · doi:10.1016/s0945-053x(99)00026-8 · Cited by 65 · see citing works

Matrix Metalloproteinases: A Therapeutic Target in Cardiovascular Disease

Sierevogel, M. J., Pasterkamp, G., de Kleijn, D. P. V., & Strauss, B. H. (2003) · Current Pharmaceutical Design · doi:10.2174/1381612033455099 · Cited by 55 · see citing works

Corneal Neovascularization after Excimer Keratectomy Wounds in Matrilysin-Deficient Mice

Kure, T., Chang, J.-H., Kato, T., Hernández-Quíntela, E., Ye, H., Lu, P. C.-S., Matrisian, L. M., Gatinel, D., Shapiro, S. D., Ghosheh, F. R., et al. (2003) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.01-1058 · Cited by 48 · see citing works

Metalloprotease inhibitors as anti-inflammatory agents: an evolving target?

Whelan, C. J. (2004) · PubMed · Cited by 14 · see citing works

Macrophage Elastase Prevents Gemella morbillorum Infection and Improves Outcome Following Murine Bone Marrow Transplantation

Hartzell, W. O., & Shapiro, S. D. (1999) · CHEST Journal · doi:10.1378/chest.116.suppl_1.31s-a · Cited by 12 · see citing works

Phenotypic analysis of the murine CD4-related glycoprotein, CD223 (LAG-3)

(2002) · doi:10.1002/1521-4141(200208)32:8

Matrix Metalloproteinases: Regulators of the Tumor Microenvironment

Kessenbrock, K., Plaks, V., & Werb, Z. (2010) · Cell · doi:10.1016/j.cell.2010.03.015 · Cited by 5,151 · see citing works

Matrix metalloproteinases and the regulation of tissue remodelling

Page, A. W., Ewald, A. J., & Werb, Z. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2125 · Cited by 3,011 · see citing works

Cytokines in Atherosclerosis: Pathogenic and Regulatory Pathways

Tedgui, A., & Mallat, Z. (2006) · Physiological Reviews · doi:10.1152/physrev.00024.2005 · Cited by 1,701 · see citing works

Roles of matrix metalloproteinases in cancer progression and their pharmacological targeting

Gialeli, C., Theocharis, A. D., & Karamanos, N. K. (2010) · FEBS Journal · doi:10.1111/j.1742-4658.2010.07919.x · Cited by 1,611 · see citing works

Bioresponsive materials

Lü, Y., Aimetti, A. A., Langer, R., & Gu, Z. (2016) · Nature Reviews Materials · doi:10.1038/natrevmats.2016.75 · Cited by 1,432 · see citing works

Biochemical and Biological Attributes of Matrix Metalloproteinases

Cui, N., Hu, M., & Khalil, R. A. (2017) · Progress in Molecular Biology and Translational Science · doi:10.1016/bs.pmbts.2017.02.005 · Cited by 1,359 · see citing works

Validating matrix metalloproteinases as drug targets and anti-targets for cancer therapy

Overall, C. M., & Kleifeld, O. (2006) · Nature reviews. Cancer · doi:10.1038/nrc1821 · Cited by 1,212 · 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

Immunological hallmarks of stromal cells in the tumour microenvironment

Turley, S. J., Cremasco, V., & Astarita, J. L. (2015) · Nature Reviews Immunology · doi:10.1038/nri3902 · Cited by 1,140 · see citing works

Metalloproteinases and Wound Healing

Caley, M. P., Martins, V., & O’Toole, E. A. (2015) · Advances in Wound Care · doi:10.1089/wound.2014.0581 · Cited by 1,003 · see citing works

Extracellular matrix and its therapeutic potential for cancer treatment

Huang, J., Zhang, L., Wan, D., Zhou, L., Zheng, S., Lin, S., & Qiao, Y. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00544-0 · Cited by 962 · see citing works

Matrix Metalloproteinases As Novel Biomarker s and Potential Therapeutic Targets in Human Cancer

Roy, R., Yang, J., & Moses, M. A. (2009) · Journal of Clinical Oncology · doi:10.1200/jco.2009.23.5556 · Cited by 857 · see citing works

Chemokine:Receptor Structure, Interactions, and Antagonism

Allen, S. J., Crown, S. E., & Handel, T. M. (2007) · Annual Review of Immunology · doi:10.1146/annurev.immunol.24.021605.090529 · Cited by 842 · see citing works

Matrix metalloproteinase inhibitors as therapy for inflammatory and vascular diseases

Hu, J., den Steen, P. E. V., Sang, Q. A., & Opdenakker, G. (2007) · Nature Reviews Drug Discovery · doi:10.1038/nrd2308 · Cited by 798 · see citing works

Platelets, inflammation and tissue regeneration

Nurden, A. T. (2011) · Thrombosis and Haemostasis · doi:10.1160/ths10-11-0720 · Cited by 793 · see citing works

The blood–brain and the blood–cerebrospinal fluid barriers: function and dysfunction

Engelhardt, B., & Sorokin, L. M. (2009) · Seminars in Immunopathology · doi:10.1007/s00281-009-0177-0 · Cited by 792 · see citing works

Biochemistry and molecular biology of gelatinase B or matrix metalloproteinase-9 (MMP-9): The next decade

Vandooren, J., den Steen, P. E. V., & Opdenakker, G. (2013) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2013.770819 · Cited by 767 · see citing works

Role of Inflammation in Diabetic Retinopathy

Rübsam, A., Parikh, S., & Fort, P. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19040942 · Cited by 750 · see citing works

Progress in matrix metalloproteinase research

MURPHY, G., & Nagase, H. (2008) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2008.05.002 · Cited by 755 · see citing works

Distinct roles of matrix metalloproteases in the early- and late-phase development of neuropathic pain

Kawasaki, Y., Xu, Z., Wang, X., Park, J. Y., Zhuang, Z., Tan, P.-H., Gao, Y., Roy, K., Corfas, G., Lo, E. H., et al. (2008) · Nature Medicine · doi:10.1038/nm1723 · Cited by 759 · see citing works

Metalloproteinases and their inhibitors: Regulators of wound healing

Gill, S. E., & Parks, W. C. (2008) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2007.10.024 · Cited by 742 · 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

Multitargeting by curcumin as revealed by molecular interaction studies

Gupta, S. C., Prasad, S., Kim, J. H., Patchva, S., Webb, L. J., Priyadarsini, K. I., & Aggarwal, B. B. (2011) · Natural Product Reports · doi:10.1039/c1np00051a · Cited by 671 · see citing works

Control of matrix metalloproteinase catalytic activity

Ra, H.-J., & Parks, W. C. (2007) · Matrix Biology · doi:10.1016/j.matbio.2007.07.001 · Cited by 645 · see citing works

Resolution of Inflammation: What Controls Its Onset?

Sugimoto, M. A., Sousa, L. P., Pinho, V., Perretti, M., & Teixeira, M. M. (2016) · Frontiers in Immunology · doi:10.3389/fimmu.2016.00160 · Cited by 638 · see citing works

Matrix Metalloproteinases as Modulators of Inflammation

MANICONE, A., & MCGUIRE, J. (2008) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2007.07.003 · Cited by 617 · see citing works

Neutrophils and Wound Repair: Positive Actions and Negative Reactions

Wilgus, T. A., Roy, S., & McDaniel, J. C. (2013) · Advances in Wound Care · doi:10.1089/wound.2012.0383 · Cited by 616 · see citing works

Collagen as a double-edged sword in tumor progression

Fang, M., Yuan, J., Peng, C., & Li, Y. (2014) · Tumor Biology · doi:10.1007/s13277-013-1511-7 · Cited by 580 · see citing works

Activated macrophages are an adaptive element of the colonic epithelial progenitor niche necessary for regenerative responses to injury

Pull, S. L., Doherty, J. M., Mills, J. C., Gordon, J. I., & Stappenbeck, T. S. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0405979102 · Cited by 605 · see citing works

Human neutrophils uniquely release TIMP-free MMP-9 to provide a potent catalytic stimulator of angiogenesis

Ardi, V. C., Kupriyanova, T. A., Deryugina, E. I., & Quigley, J. P. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0706438104 · Cited by 603 · see citing works

Chemokine and cytokine processing by matrix metalloproteinases and its effect on leukocyte migration and inflammation

Lint, P. V., & Libert, C. (2007) · Journal of Leukocyte Biology · doi:10.1189/jlb.0607338 · Cited by 564 · see citing works

Matrix metalloproteinases: What do they not do? New substrates and biological roles identified by murine models and proteomics

Rodrı́guez, D., Morrison, C., & Overall, C. M. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2009.09.015 · Cited by 560 · see citing works

Dystroglycan is selectively cleaved at the parenchymal basement membrane at sites of leukocyte extravasation in experimental autoimmune encephalomyelitis

Agrawal, S., Anderson, P., Durbeej, M., van Rooijen, N., Ivars, F., Opdenakker, G., & Sorokin, L. M. (2006) · The Journal of Experimental Medicine · doi:10.1084/jem.20051342 · Cited by 559 · see citing works

Diverse functions of matrix metalloproteinases during fibrosis

Giannandrea, M., & Parks, W. C. (2014) · Disease Models & Mechanisms · doi:10.1242/dmm.012062 · Cited by 543 · see citing works

Ovulation: Parallels With Inflammatory Processes

Duffy, D. M., Ko, C. J., Jo, M., Brännström, M., & Curry, T. E. (2018) · Endocrine Reviews · doi:10.1210/er.2018-00075 · Cited by 530 · see citing works

Metalloproteinases: Mediators of Pathology and Regeneration in the CNS

Yong, V. W. (2005) · Nature Reviews Neuroscience · doi:10.1038/nrn1807 · Cited by 582 · see citing works

Beyond the margins: real-time detection of cancer using targeted fluorophores

Zhang, R. R., Schroeder, A. B., Grudzinski, J. J., Rosenthal, E. L., Warram, J. M., Pinchuk, A. N., Eliceiri, K. W., Kuo, J. S., & Weichert, J. P. (2017) · Nature Reviews Clinical Oncology · doi:10.1038/nrclinonc.2016.212 · Cited by 485 · see citing works

Matrix metalloproteinases in liver injury, repair and fibrosis

Duarte, S. M., Baber, J. T., Fujii, T., & Coito, A. J. (2015) · Matrix Biology · doi:10.1016/j.matbio.2015.01.004 · Cited by 481 · see citing works

Matrix Metalloproteinases in Lung: Multiple, Multifarious, and Multifaceted

Greenlee, K. J., Werb, Z., & Kheradmand, F. (2007) · Physiological Reviews · doi:10.1152/physrev.00022.2006 · Cited by 474 · see citing works

Pregnancy-associated breast cancer and metastasis

Schedin, P. S. (2006) · Nature reviews. Cancer · doi:10.1038/nrc1839 · Cited by 467 · see citing works

Matrix Metalloproteinases: Inflammatory Regulators of Cell Behaviors in Vascular Formation and Remodeling

Chen, Q., Jin, M., Yang, F., Zhu, J., Xiao, Q., & Zhang, L. (2013) · Mediators of Inflammation · doi:10.1155/2013/928315 · Cited by 444 · see citing works

Matrix metalloproteinases in inflammation

Nissinen, L. M., & Kähäri, V. (2014) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2014.03.007 · Cited by 446 · see citing works

Oxidative Stress in Pulmonary Fibrosis

Kinnula, V. L., Fattman, C. L., Tan, R. J., & Oury, T. D. (2005) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.200501-017pp · Cited by 437 · see citing works

Targeting Astrocyte Signaling for Chronic Pain

Gao, Y., & Ji, R. (2010) · Neurotherapeutics · doi:10.1016/j.nurt.2010.05.016 · Cited by 424 · 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

How do immune cells overcome the blood-brain barrier in multiple sclerosis?

Larochelle, C., Alvarez, J. I., & Prat, A. (2011) · FEBS Letters · doi:10.1016/j.febslet.2011.04.066 · Cited by 405 · see citing works

The tumor microenvironment in hepatocellular carcinoma: Current status and therapeutic targets

Yang, J. D., Nakamura, I., & Roberts, L. R. (2010) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2010.10.007 · Cited by 389 · see citing works

Inflammatory Molecules Associated with Ultraviolet Radiation-Mediated Skin Aging

Ansary, T. M., Hossain, M. R., Kamiya, K., Komine, M., & Ohtsuki, M. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22083974 · Cited by 393 · see citing works

The Biochemical, Biological, and Pathological Kaleidoscope of Cell Surface Substrates Processed by Matrix Metalloproteinases

Cauwe, B., den Steen, P. E. V., & Opdenakker, G. (2007) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409230701340019 · Cited by 384 · see citing works

Matrix metalloproteinases in brain development and remodeling: Synaptic functions and targets

Ethell, I. M., & Ethell, D. W. (2007) · Journal of Neuroscience Research · doi:10.1002/jnr.21273 · Cited by 378 · see citing works

Omega-3 fatty acids and metabolic syndrome: Effects and emerging mechanisms of action

Poudyal, H., Panchal, S. K., Diwan, V., & Brown, L. (2011) · Progress in Lipid Research · doi:10.1016/j.plipres.2011.06.003 · Cited by 373 · see citing works

Mesenchymal cell targeting by TNF as a common pathogenic principle in chronic inflammatory joint and intestinal diseases

Armaka, M., Apostolaki, M., Jacques, P., Kontoyiannis, D. L., Elewaut, D. S., & Kollias, G. A. (2008) · The Journal of Experimental Medicine · doi:10.1084/jem.20070906 · Cited by 371 · see citing works

Tumor cell-produced matrix metalloproteinase 9 (MMP-9) drives malignant progression and metastasis of basal-like triple negative breast cancer

Mehner, C., Hockla, A., Miller, E. E., Ran, S., Radisky, D. C., & Radisky, E. S. (2014) · Oncotarget · doi:10.18632/oncotarget.1932 · Cited by 369 · see citing works

In search of partners: linking extracellular proteases to substrates

Overall, C. M., & Blobel, C. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2120 · Cited by 350 · see citing works

Towards third generation matrix metalloproteinase inhibitors for cancer therapy

Overall, C. M., & Kleifeld, O. (2006) · British Journal of Cancer · doi:10.1038/sj.bjc.6603043 · Cited by 344 · see citing works

The paradox of matrix metalloproteinases in infectious disease

Elkington, P. T., O’Kane, C. M., & Friedland, J. S. (2005) · Clinical & Experimental Immunology · doi:10.1111/j.1365-2249.2005.02840.x · Cited by 343 · see citing works

Matrix metalloproteinases in destructive pulmonary pathology

Elkington, P. T. (2005) · Thorax · doi:10.1136/thx.2005.051979 · Cited by 331 · see citing works

Collagenases in cancer

Ala‐aho, R., & Kähäri, V. (2005) · Biochimie · doi:10.1016/j.biochi.2004.12.009 · Cited by 328 · see citing works

Chemokines Regulate the Migration of Neural Progenitors to Sites of Neuroinflammation

Belmadani, A. A., Tran, P. B., Ren, D., & Miller, R. J. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.0156-06.2006 · Cited by 322 · see citing works

Neuroprotection by inhibition of matrix metalloproteinases in a mouse model of intracerebral haemorrhage

Wang, J., & Tsirka, S. E. (2005) · Brain · doi:10.1093/brain/awh489 · Cited by 321 · see citing works

Mechanisms of cigarette smoke-induced COPD: insights from animal models

Churg, A., Cosío, M. G., & Wright, J. L. (2008) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00390.2007 · Cited by 320 · see citing works

Reappraising metalloproteinases in rheumatoid arthritis and osteoarthritis: destruction or repair?

Murphy, G., & Nagase, H. (2008) · Nature Clinical Practice Rheumatology · doi:10.1038/ncprheum0727 · Cited by 316 · see citing works

Missing the target: matrix metalloproteinase antitargets in inflammation and cancer

Dufour, A., & Overall, C. M. (2013) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2013.02.004 · Cited by 313 · 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

Proline Metabolism and Microenvironmental Stress

Phang, J. M., Liu, W., & Zabirnyk, O. (2010) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.012809.104638 · Cited by 303 · see citing works

Cancer invasion and metastasis: changing views

Duffy, M. J., McGowan, P. M., & Gallagher, W. M. (2007) · The Journal of Pathology · doi:10.1002/path.2282 · Cited by 300 · 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

Gene expression associated with white syndromes in a reef building coral, Acropora hyacinthus

Wright, R. M., Aglyamova, G. V., Meyer, E., & Matz, M. V. (2015) · BMC Genomics · doi:10.1186/s12864-015-1540-2 · Cited by 299 · see citing works

Intracellular substrate cleavage: a novel dimension in the biochemistry, biology and pathology of matrix metalloproteinases

Cauwe, B., & Opdenakker, G. (2010) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2010.501783 · Cited by 296 · see citing works

Extracellular matrix in lung development, homeostasis and disease

Zhou, Y., Horowitz, J. C., Naba, A., Ambalavanan, N., Atabai, K., Balestrini, J. L., Bitterman, P. B., CORLEY, R. A., Ding, B., Engler, A. J., et al. (2018) · Matrix Biology · doi:10.1016/j.matbio.2018.03.005 · Cited by 285 · see citing works

Mesenchymal Stem Cells Prevent the Rejection of Fully Allogenic Islet Grafts by the Immunosuppressive Activity of Matrix Metalloproteinase-2 and -9

Ding, Y., Xu, D., Feng, G. L., Bushell, A., Muschel, R. J., & Wood, K. J. (2009) · Diabetes · doi:10.2337/db09-0317 · Cited by 285 · see citing works

Multiplex N-terminome Analysis of MMP-2 and MMP-9 Substrate Degradomes by iTRAQ-TAILS Quantitative Proteomics

Prudova, A., Keller, U. A. D., Butler, G. S., & Overall, C. M. (2010) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m000050-mcp201 · Cited by 284 · see citing works

Pulmonary Fibrosis as a Result of Acute Lung Inflammation: Molecular Mechanisms, Relevant In Vivo Models, Prognostic and Therapeutic Approaches

Savin, I. A., Аркадьевна, З. М., & Васильевна, С. А. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232314959 · Cited by 288 · see citing works

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

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

Minocycline as a Neuroprotective Agent

Stirling, D. P., Koochesfahani, K. M., Steeves, J. D., & Tetzlaff, W. (2005) · The Neuroscientist · doi:10.1177/1073858405275175 · Cited by 280 · see citing works

COVID-19 and Oxidative Stress

Chernyak, B. V., Popova, E. N., Prikhodko, A. S., Grebenchikov, O. A., Zinovkina, L. A., & Zinovkin, R. A. (2020) · Biochemistry (Moscow) · doi:10.1134/s0006297920120068 · Cited by 283 · see citing works

Wnt/β-catenin signaling and kidney fibrosis

Tan, R. J., Zhou, D. F., Zhou, L., & Liu, Y. (2014) · Kidney International Supplements · doi:10.1038/kisup.2014.16 · Cited by 279 · see citing works

Matrix metalloproteinases: roles in cancer and metastasis

Fingleton, B. (2006) · Frontiers in bioscience · doi:10.2741/1811 · Cited by 272 · see citing works

Targeted Deletion of Metalloproteinase 9 Attenuates Experimental Colitis in Mice: Central Role of Epithelial-Derived MMP

Castaneda, F. E., Walia, B., Vijay–Kumar, M., Patel, N. R., Roser, S., Kolachala, V. L., Rojas, M., Wang, L., Oprea, G. M., Garg, P., et al. (2005) · Gastroenterology · doi:10.1053/j.gastro.2005.09.017 · Cited by 267 · see citing works

The Prostanoid EP4 Receptor and Its Signaling Pathway

Yokoyama, U., Iwatsubo, K., Umemura, M., Fujita, T., & Ishikawa, Y. (2013) · Pharmacological Reviews · doi:10.1124/pr.112.007195 · Cited by 266 · see citing works

Matrix metalloproteinases in kidney homeostasis and diseases

Tan, R. J., & Liu, Y. (2012) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00037.2012 · Cited by 261 · see citing works

A new transcriptional role for matrix metalloproteinase-12 in antiviral immunity

Marchant, D., Bellac, C. L., Moraes, T. J., Wadsworth, S. J., Dufour, A., Butler, G. S., Bilawchuk, L. M., Hendry, R. G., Robertson, A. G., Cheung, C., et al. (2014) · Nature Medicine · doi:10.1038/nm.3508 · Cited by 265 · see citing works

Matrix metalloproteinases as regulators of inflammatory processes

Fingleton, B. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2017.05.010 · Cited by 263 · see citing works

Anti‐inflammatory Effect of Rosmarinic Acid and an Extract ofRosmarinus officinalisin Rat Models of Local and Systemic Inflammation

Rocha, J. P., Figueira, M. E., Barateiro, A. P., Fernandes, A. M. A., Brites, D. M. T. O., Bronze, M. R., Duarte, C. M. M., Serra, T., Pinto, R. M. A., Freitas, M., et al. (2014) · Basic & Clinical Pharmacology & Toxicology · doi:10.1111/bcpt.12335 · Cited by 259 · 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

Neutrophil-Derived Matrix Metalloproteinase 9 Triggers Acute Aortic Dissection

Kurihara, T., Shimizu‐Hirota, R., Shimoda, M., Adachi, T. K., Shimizu, H., Weiss, S. J., Itoh, H., Hori, S., Aikawa, N., & Okada, Y. (2012) · Circulation · doi:10.1161/circulationaha.112.097097 · Cited by 257 · see citing works

Recent advances in MMP inhibitor design

Fisher, J. F., & Mobashery, S. (2006) · Cancer and Metastasis Reviews · doi:10.1007/s10555-006-7894-9 · Cited by 255 · see citing works

The metabolism of proline, a stress substrate, modulates carcinogenic pathways

Phang, J. M., Donald, S. P., Pandhare, J., & Liu, Y. (2008) · Amino Acids · doi:10.1007/s00726-008-0063-4 · Cited by 252 · see citing works

Amino Acid Catabolism in <i>Staphylococcus aureus</i> and the Function of Carbon Catabolite Repression

Halsey, C. R., Lei, S., Wax, J. K., Lehman, M. K., Nuxoll, A. S., Steinke, L., Sadykov, M., Powers, R., & Fey, P. D. (2017) · mBio · doi:10.1128/mbio.01434-16 · Cited by 233 · see citing works

Stroke Biomarkers: Progress and Challenges for Diagnosis, Prognosis, Differentiation, and Treatment

Saenger, A. K., & Christenson, R. H. (2009) · Clinical Chemistry · doi:10.1373/clinchem.2009.133801 · Cited by 254 · see citing works

The Role of the Mediators of Inflammation in Cancer Development

Fernandes, J. V., Cobucci, R. N., Jatobá, C. A. N., Fernandes, T. A. A. D. M., de Azevedo, J. W. V., & de Araújo, J. M. G. (2015) · Pathology & Oncology Research · doi:10.1007/s12253-015-9913-z · Cited by 252 · see citing works

Matrix metalloproteinases and epidermal wound repair

Martins, V., Caley, M. P., & O’Toole, E. A. (2012) · Cell and Tissue Research · doi:10.1007/s00441-012-1410-z · Cited by 251 · see citing works

Host-Pathogen Interactions Made Transparent with the Zebrafish Model

Meijer, A. H., & Spaink, H. P. (2011) · Current Drug Targets · doi:10.2174/138945011795677809 · Cited by 253 · see citing works

Matrix metalloproteinases in acute lung injury: mediators of injury and drivers of repair

Davey, A., McAuley, D. F., & O’Kane, C. M. (2011) · European Respiratory Journal · doi:10.1183/09031936.00032111 · Cited by 249 · see citing works

Mechanisms of immune-mediated skin diseases: an overview.

Filippucci, E., Iagnocco, A., Meenagh, G., Riente, L., Sedie, A. D., Bombardieri, S., Valesini, G., & Grassi, W. (2006) · PubMed · Cited by 248 · see citing works

Bacterial metastasis: the host plasminogen system in bacterial invasion

Lähteenmäki, K., Edelman, S., & Korhonen, T. (2004) · Trends in Microbiology · doi:10.1016/j.tim.2004.12.003 · Cited by 242 · see citing works

Inflammasome-Independent NLRP3 Augments TGF-β Signaling in Kidney Epithelium

Wang, W., Wang, X., Chun, J., Vilaysane, A., Clark, S. A., French, G., Bracey, N. A., Trpkov, K., Bonni, S., Duff, H. J., et al. (2012) · The Journal of Immunology · doi:10.4049/jimmunol.1201959 · Cited by 239 · see citing works

Pleiotropic roles of matrix metalloproteinases in tumor angiogenesis: Contrasting, overlapping and compensatory functions

Deryugina, E. I., & Quigley, J. P. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2009.09.017 · Cited by 234 · see citing works

Kaempferol acts through mitogen‐activated protein kinases and protein kinase B/AKT to elicit protection in a model of neuroinflammation in BV2 microglial cells

Park, S. E., Sapkota, K., Kim, S. H., Kim, H., & Kim, S. (2011) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2011.01389.x · Cited by 235 · see citing works

Matrix metalloproteinases as regulators of inflammatory processes

Fingleton, B. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2017.05.010 · Cited by 263 · see citing works

Metalloproteinases and their natural inhibitors in inflammation and immunity

Khokha, R., Murthy, A., & Weiss, A. (2013) · Nature reviews. Immunology · doi:10.1038/nri3499 · Cited by 552 · see citing works

РЕГУЛЯТОРНА ФУНКЦІЯ МАТРИКСНИХ МЕТАЛОПРОТЕЇНАЗ ТА ЇХНІХ ІНГІБІТОРІВ (ОГЛЯД ЛІТЕРАТУРИ)

Волошин, О. М., Savchenko, I. I., Осичнюк, Л. М., & Богданець, О. А. (2025) · Український журнал екстремальної медицини ім Г О Можаєва · doi:10.32782/3083-7324/2025.1.1

Matrix metalloproteinases in tissue remodelling and inflammation

Lagente, V. (2008) · Cited by 2 · see citing works

Matrix Metalloproteinases as Modulators of Inflammation

MANICONE, A., & MCGUIRE, J. (2008) · Seminars in Cell &amp; Developmental Biology · doi:10.1016/j.semcdb.2007.07.003 · Cited by 617 · see citing works