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

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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

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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

Role of the pulmonary epithelium and inflammatory signals in acute lung injury

Manicone, A. M. (2008) · Expert Review of Clinical Immunology · doi:10.1586/1744666x.5.1.63 · Cited by 142

IL-6–Mediated Induction of Matrix Metalloproteinase-9 Is Modulated by JAK-Dependent IL-10 Expression in Macrophages

Kothari, P., Pestana, R., Mesraoua, R., Elchaki, R., Khan, K. M. F., Dannenberg, A. J., & Falcone, D. J. (2014) · The Journal of Immunology · doi:10.4049/jimmunol.1301906 · Cited by 137

Myelin Formation during Development of the CNS Is Delayed in Matrix Metalloproteinase-9 and -12 Null Mice

Larsen, P. H., DaSilva, A. G., Conant, K. E., & Yong, V. W. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.1880-05.2006 · Cited by 143

Immune Cells and Molecular Networks in Experimentally Induced Pulpitis

Renard, E., Gaudin, A., Bienvenu, G., Amiaud, J., Farges, J., Cuturi, M. C., Moreau, A., & Alliot‐Licht, B. (2015) · Journal of Dental Research · doi:10.1177/0022034515612086 · Cited by 138

Increased expression of MMP-2 and MMP-9 indicates poor prognosis in glioma recurrence

Zhou, W., Yu, X., Sun, S., Zhang, X., Yang, W., Zhang, J., Zhang, X., & Jiang, Z. (2019) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2019.109369 · Cited by 137

Eosinophil-Derived Cationic Proteins Activate the Synthesis of Remodeling Factors by Airway Epithelial Cells

Pégorier, S., Wagner, L. A., Gleich, G. J., & Pretolani, M. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.177.7.4861 · Cited by 134

SARM inhibits both TRIF‐ and MyD88‐mediated AP‐1 activation

Peng, J., Yuan, Q., Lin, B., Panneerselvam, P., Wang, X., Luan, X. L., Lim, S. K., Leung, B. P. L., Ho, B., & Ding, J. L. (2010) · European Journal of Immunology · doi:10.1002/eji.200940034 · Cited by 135

Role of oxidative stress in chemical allergens induced skin cells activation

Corsini, E., Galbiati, V., Nikitovic, D., & Tsatsakis, A. M. (2013) · Food and Chemical Toxicology · doi:10.1016/j.fct.2013.02.038 · Cited by 133

Expression of Smad7 in Mouse Eyes Accelerates Healing of Corneal Tissue after Exposure to Alkali

Saika, S., Ikeda, K., Yamanaka, O., Miyamoto, T. K., Ohnishi, Y., Sato, M., Muragaki, Y., Ooshima, A., Nakajima, Y., Kao, W. W. ‐., et al. (2005) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)62358-9 · Cited by 132

Oncogenic Properties of Apoptotic Tumor Cells in Aggressive B Cell Lymphoma

Ford, C. A., Petrova, S., Pound, J. D., Voss, J. J. L. P., Melville, L. A., Paterson, M., Farnworth, S. L., Gallimore, A., Cuff, S. M., Wheadon, H., et al. (2015) · Current Biology · doi:10.1016/j.cub.2014.12.059 · Cited by 133

Inflammation and matrix metalloproteinase 9 (Mmp‐9) regulate photoreceptor regeneration in adult zebrafish

Silva, N. J., Nagashima, M., Li, J., Kakuk‐Atkins, L., Ashrafzadeh, M., Hyde, D. R., & Hitchcock, P. F. (2020) · Glia · doi:10.1002/glia.23792 · Cited by 119

Myeloperoxidase Inactivates TIMP-1 by Oxidizing Its N-terminal Cysteine Residue

Wang, Y., Rosen, H., Madtes, D. K., Shao, B., Martin, T. R., Heinecke, J. W., & Fu, X. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m704894200 · Cited by 132

Characteristics of the Tumor Microenvironment That Influence Immune Cell Functions: Hypoxia, Oxidative Stress, Metabolic Alterations

Augustin, R. C., Delgoffe, G. M., & Najjar, Y. G. (2020) · Cancers · doi:10.3390/cancers12123802 · Cited by 139

Paneth cell defensins and the regulation of the microbiome

Salzman, N. H. (2010) · Gut Microbes · doi:10.4161/gmic.1.6.14076 · Cited by 140

Relative contribution of matrix metalloprotease and cysteine protease activities to cytokine-stimulated articular cartilage degradation

Søndergaard, B. C., Henriksen, K., Wulf, H., Oestergaard, S., Schurigt, U., Bräuer, R., Danielsen, I., Christiansen, C., Qvist, P., & Karsdal, M. A. (2006) · Osteoarthritis and Cartilage · doi:10.1016/j.joca.2006.01.016 · Cited by 128

Preclinical evaluation of mRNA trimannosylated lipopolyplexes as therapeutic cancer vaccines targeting dendritic cells

Moignic, A. L., Malard, V., Benvegnu, T. J., Lemiègre, L., Berchel, M., Jaffrès, P., Baillou, C., Guillot‐Delost, M., Macedo, R., Rochefort, J., et al. (2018) · Journal of Controlled Release · doi:10.1016/j.jconrel.2018.03.035 · Cited by 129

A ferrobotic system for automated microfluidic logistics

Yu, W., Lin, H., Wang, Y., He, X., Chen, N., Sun, K., Lo, D., Cheng, B., Yeung, C. J., Tan, J., et al. (2020) · Science Robotics · doi:10.1126/scirobotics.aba4411 · Cited by 129

The role of matrix metalloproteinase 9 in fibrosis diseases and its molecular mechanisms

Wang, Y., Jiao, L., Qiang, C., Chen, C., Shen, Z., Ding, F., Lv, L., Zhu, T., Lu, Y., & Cui, X. (2024) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2023.116116 · Cited by 131

Tuberculosis Immunopathology: The Neglected Role of Extracellular Matrix Destruction

Elkington, P. T., D'Armiento, J. M., & Friedland, J. S. (2011) · Science Translational Medicine · doi:10.1126/scitranslmed.3001847 · Cited by 127

The Potential of Minocycline for Neuroprotection in Human Neurologic Disease

Zemke, D., & Majid, A. (2004) · Clinical Neuropharmacology · doi:10.1097/01.wnf.0000150867.98887.3e · Cited by 125

Matrix metalloproteinase: An upcoming therapeutic approach for idiopathic pulmonary fibrosis

Mahalanobish, S., Saha, S., Dutta, S., & Sil, P. C. (2019) · Pharmacological Research · doi:10.1016/j.phrs.2019.104591 · Cited by 131

Host-Directed Therapies for Tuberculosis: Figure 1.Preprint

Tobin, D. M. (2015) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a021196 · Cited by 123

Trachoma: Protective and Pathogenic Ocular Immune Responses to Chlamydia trachomatis

Hu, V. H., Holland, M. J., & Burton, M. J. (2013) · PLoS neglected tropical diseases · doi:10.1371/journal.pntd.0002020 · Cited by 129

Proteoglycans: Key Regulators of Pulmonary Inflammation and the Innate Immune Response to Lung Infection

Gill, S. E., Wight, T. N., & Frevert, C. W. (2010) · The Anatomical Record · doi:10.1002/ar.21094 · Cited by 123

Matrix Metalloproteinase (MMP)-1 and MMP-3 Induce Macrophage MMP-9: Evidence for the Role of TNF-α and Cyclooxygenase-2

Steenport, M. L., Khan, K. M. F., Du, B., Barnhard, S. E., Dannenberg, A. J., & Falcone, D. J. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0901925 · Cited by 121

Specificity of the zebrafish host transcriptome response to acute and chronic mycobacterial infection and the role of innate and adaptive immune components

van der Sar, A. M., Spaink, H. P., Zakrzewska, A., Bitter, W., & Meijer, A. H. (2009) · Molecular Immunology · doi:10.1016/j.molimm.2009.03.024 · Cited by 116

The Role of Macrophages in the Infarcted Myocardium: Orchestrators of ECM Remodeling

O’Rourke, S. A., Dunne, A., & Monaghan, M. G. (2019) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2019.00101 · Cited by 124

The Extracellular Matrix in Pancreatic Cancer: Description of a Complex Network and Promising Therapeutic Options

Ferrara, B., Pignatelli, C., Cossutta, M., Citro, A., Courty, J., & Piemonti, L. (2021) · Cancers · doi:10.3390/cancers13174442 · Cited by 134

Abdominal Aortic Aneurysm as a Complex Multifactorial Disease

Pearce, W. H., & Shively, V. P. (2006) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1383.025 · Cited by 118

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

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

Matrix metalloproteinases as drug targets in ischemia/reperfusion injury

Dejonckheere, E., Vandenbroucke, R. E., & Libert, C. (2011) · Drug Discovery Today · doi:10.1016/j.drudis.2011.06.009 · Cited by 120

Astrocytes in Chronic Pain: Cellular and Molecular Mechanisms

Lu, H.-J., & Gao, Y.-J. (2023) · Neuroscience Bulletin · doi:10.1007/s12264-022-00961-3 · Cited by 118

Matrix Metalloproteinases Promote Inflammation and Fibrosis in Asbestos-Induced Lung Injury in Mice

Tan, R. J., Fattman, C. L., Niehouse, L. M., Tobolewski, J. M., Hanford, L. E., Li, Q., Monzon, F. A., Parks, W. C., & Oury, T. D. (2006) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2005-0471oc · Cited by 117

Proteinase inhibitors and helminth parasite infection

Knox, D. P. (2006) · Parasite Immunology · doi:10.1111/j.1365-3024.2006.00913.x · Cited by 118

Towards extracellular matrix normalization for improved treatment of solid tumors

Abyaneh, H. S., Regenold, M., McKee, T. D., Allen, C. J., & Gauthier, M. A. (2020) · Theranostics · doi:10.7150/thno.39995 · Cited by 120

Molecular Balance of Capillary Tube Formation versus Regression in Wound Repair: Role of Matrix Metalloproteinases and Their Inhibitors

Davis, G. E., & Saunders, W. B. (2006) · Journal of Investigative Dermatology Symposium Proceedings · doi:10.1038/sj.jidsymp.5650008 · Cited by 122

Nanomedicine-based drug delivery towards tumor biological and immunological microenvironment

Li, J., & Burgess, D. J. (2020) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2020.05.008 · Cited by 118

Role of matrix metalloproteinase in wound healing.

Kandhwal, M., Behl, T., Singh, S., Sharma, N., Arora, S., Bhatia, S., Al‐Harrasi, A., Sachdeva, M., & BUNGAU, S. G. (2022) · PubMed Central · Cited by 117

Matrix Metalloprotease 8-Dependent Extracellular Matrix Cleavage at the Blood-CSF Barrier Contributes to Lethality during Systemic Inflammatory Diseases

Vandenbroucke, R. E., Dejonckheere, E., Lint, P. V., Demeestere, D., Wonterghem, E. V., Vanlaere, I., Puimège, L., Hauwermeiren, F. V., Rycke, R. M. D., Guire, C. M., et al. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.0967-12.2012 · Cited by 121

Systems-Level Analysis of Proteolytic Events in Increased Vascular Permeability and Complement Activation in Skin Inflammation

Keller, U. A. D., Prudova, A., Eckhard, U., Fingleton, B., & Overall, C. M. (2013) · Science Signaling · doi:10.1126/scisignal.2003512 · Cited by 115

Endothelial Response to Glucocorticoids in Inflammatory Diseases

Zielińska, K. A., Moortel, L. V., Opdenakker, G., Bosscher, K. D., & den Steen, P. E. V. (2016) · Frontiers in Immunology · doi:10.3389/fimmu.2016.00592 · Cited by 120

Matrix Metalloproteinases in Diabetic Kidney Disease

Garcı́a-Fernández, N., Jacobs-Cachá, C., Mora‐Gutiérrez, J. M., Vergara, A., Orbe, J., & Soler, M. J. (2020) · Journal of Clinical Medicine · doi:10.3390/jcm9020472 · Cited by 115

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

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

Redox-Dependent Anti-Inflammatory Signaling Actions of Unsaturated Fatty Acids

Delmastro-Greenwood, M. M., Freeman, B. Α., & Wendell, S. G. (2013) · Annual Review of Physiology · doi:10.1146/annurev-physiol-021113-170341 · Cited by 117

Multifunctional biophotonic nanostructures inspired by the longtail glasswing butterfly for medical devices

Narasimhan, V., Siddique, R. H., Lee, J. O., Kumar, S., Ndjamen, B., Du, J., Hong, N., Sretavan, D. W., & Choo, H. (2018) · Nature Nanotechnology · doi:10.1038/s41565-018-0111-5 · Cited by 113

Matrix Metalloproteinases in Renal Diseases: A Critical Appraisal

Zakiyanov, O., Kalousová, M., Zima, T., & Tesař, V. (2019) · Kidney & Blood Pressure Research · doi:10.1159/000499876 · Cited by 115

Elastolytic Proteases

Taggart, C. C., Greene, C. M., Carroll, T. P., O'Neill, S. J., & McElvaney, N. G. (2005) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.200407-881pp · Cited by 113

Mycobacterium tuberculosis Up-Regulates Matrix Metalloproteinase-1 Secretion from Human Airway Epithelial Cells via a p38 MAPK Switch

Elkington, P. T., Emerson, J. E., LOPEZ‐PASCUA, L. D. C., O’Kane, C. M., Horncastle, D. E., Boyle, J. J., & Friedland, J. S. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.175.8.5333 · Cited by 112

Roles of NF-κB Signaling in the Regulation of miRNAs Impacting on Inflammation in Cancer

Markopoulos, G. S., Roupakia, E., Tokamani, M., Alabasi, G., Sandaltzopoulos, R., Marcu, K. B., & Kolettas, E. (2018) · Biomedicines · doi:10.3390/biomedicines6020040 · Cited by 116

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

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

Emerging roles of activating transcription factor (ATF) family members in tumourigenesis and immunity: Implications in cancer immunotherapy

Chen, M., Liu, Y., Yang, Y., Qiu, Y., Wang, Z., Li, X., & Zhang, W. (2021) · Genes & Diseases · doi:10.1016/j.gendis.2021.04.008 · Cited by 114

Exploring the Role of Soluble Factors Associated with Immune Regulatory Properties of Mesenchymal Stem Cells

Bassi, Ê. J., de Almeida, D. C., Moraes‐Vieira, P. M., & Câmara, N. O. S. (2011) · Stem Cell Reviews and Reports · doi:10.1007/s12015-011-9311-1 · Cited by 107

Biological characteristics and pathogenicity of Acanthamoeba

Wang, Y., Jiang, L., Zhao, Y., Ju, X., Wang, L., Jin, L., Fine, R. D., & Li, M. (2023) · Frontiers in Microbiology · doi:10.3389/fmicb.2023.1147077 · Cited by 108

Divergent functions for airway epithelial matrix metalloproteinase 7 and retinoic acid in experimental asthma

Goswami, S., Angkasekwinai, P., Shan, M., Greenlee, K. J., Barranco, W. T., Polikepahad, S., Seryshev, A. B., Song, L., Redding, D., Singh, B., et al. (2009) · Nature Immunology · doi:10.1038/ni.1719 · Cited by 109

Interplay of extracellular matrix and leukocytes in lung inflammation

Wight, T. N., Frevert, C. W., Debley, J. S., Reeves, S. R., Parks, W. C., & Ziegler, S. F. (2016) · Cellular Immunology · doi:10.1016/j.cellimm.2016.12.003 · Cited by 105

Proline metabolism and cancer

James, M. A. (2011) · Frontiers in bioscience · doi:10.2741/4022 · Cited by 109

Matrix Metalloproteinase 9 Activity Enhances Host Susceptibility to Pulmonary Infection with Type A and B Strains of Francisella tularensis

Malik, M., Bakshi, C. S., McCabe, K., Catlett, S. V., Shah, A., Singh, R. P., Jackson, P. L., Gaggar, A., Metzger, D. W., Melendez, J. A., et al. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.178.2.1013 · Cited by 107

Matrix metalloproteinases as therapeutic targets in protozoan parasitic infections

Geurts, N., Opdenakker, G., & den Steen, P. E. V. (2011) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2011.11.008 · Cited by 105

Matrix Metalloproteinases as Potential Targets in the Venous Dilation Associated with Varicose Veins

Küçükgüven, A., & Khalil, R. A. (2013) · Current Drug Targets · doi:10.2174/138945013804998972 · Cited by 109

NF-κB-iNOS-COX2-TNF α inflammatory signaling pathway plays an important role in methotrexate induced small intestinal injury in rats

Natarajan, K., Abraham, P., Kota, R., & Isaac, B. (2018) · Food and Chemical Toxicology · doi:10.1016/j.fct.2018.06.040 · Cited by 106

Pathogenesis of Neisseria gonorrhoeae and the Host Defense in Ascending Infections of Human Fallopian Tube

Lenz, J. D., & Dillard, J. P. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.02710 · Cited by 103

Colonization of experimental murine breast tumours by Escherichia coli K-12 significantly alters the tumour microenvironment

Weibel, S., Stritzker, J., Eck, M., Goebel, W., & Szalay, A. A. (2008) · Cellular Microbiology · doi:10.1111/j.1462-5822.2008.01122.x · Cited by 103

MMP-10 Regulates Collagenolytic Activity of Alternatively Activated Resident Macrophages

Rohani, M. G., McMahan, R. S., Razumova, M. V., Hertz, A. L., Cieslewicz, M., Pun, S. H., Regnier, M., Wang, Y., Birkland, T. P., & Parks, W. C. (2015) · Journal of Investigative Dermatology · doi:10.1038/jid.2015.167 · Cited by 101

Neutrophils in Tuberculosis: Heterogeneity Shapes the Way?

Lyadova, I. V. (2017) · Mediators of Inflammation · doi:10.1155/2017/8619307 · Cited by 110

Matrix metalloproteases from chondrocytes generate an antiangiogenic 16 kDa prolactin

Macotela, Y., Aguilar, M. B., Guzmán‐Morales, J., Rivera, J. C., Zermeño, C., López-Barrera, F., Nava, G., Lavalle, C. M., de la Escalera, G. M., & Clapp, C. (2006) · Journal of Cell Science · doi:10.1242/jcs.02887 · Cited by 103

Biochemistry of human tear film: A review

Masoudi, S. (2022) · Experimental Eye Research · doi:10.1016/j.exer.2022.109101 · Cited by 109

Mycobacterium tuberculosis , but Not Vaccine BCG, Specifically Upregulates Matrix Metalloproteinase-1

Elkington, P. T., Nuttall, R. K., Boyle, J. J., O’Kane, C. M., Horncastle, D. E., Edwards, D. R., & Friedland, J. S. (2005) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.200505-753oc · Cited by 102

Invited review: Breaking barriers — attack on innate immune defences by omptin surface proteases of enterobacterial pathogens

Haiko, J., Suomalainen, M., Ojala, T., Lähteenmäki, K., & Korhonen, T. (2009) · Innate Immunity · doi:10.1177/1753425909102559 · Cited by 102

Matrix metalloproteinase inhibitor properties of tetracyclines: Therapeutic potential in cardiovascular diseases

de Castro, M. M., Kandasamy, A. D., Youssef, N., & Schulz, R. (2011) · Pharmacological Research · doi:10.1016/j.phrs.2011.05.005 · Cited by 102

The therapeutic potential of targeting the endothelial-to-mesenchymal transition

Man, S., Sánchez‐Duffhues, G., ten Dijke, P., & Baker, D. A. (2018) · Angiogenesis · doi:10.1007/s10456-018-9639-0 · Cited by 99

Recklessness as a hallmark of aggressive cancer

Noda, M., & Takahashi, C. (2007) · Cancer Science · doi:10.1111/j.1349-7006.2007.00588.x · Cited by 101

Matrix metalloproteinase8 has a central role in inflammatory disorders and cancer progression

Dejonckheere, E., Vandenbroucke, R. E., & Libert, C. (2011) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2011.02.002 · Cited by 100

Metal-Enhanced Fluorescence by Bifunctional Au Nanoparticles for Highly Sensitive and Simple Detection of Proteolytic Enzyme

Choi, J., & Choi, J.-W. (2020) · Nano Letters · doi:10.1021/acs.nanolett.0c02343 · Cited by 101

IL-21 Is Highly Produced in Helicobacter pylori -Infected Gastric Mucosa and Promotes Gelatinases Synthesis

Caruso, R., Fina, D., Peluso, I., Fantini, M. C., Tosti, C., Blanco, G. D. V., Paoluzi, O. A., Caprioli, F., Andrei, F., Stolfi, C., et al. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.178.9.5957 · Cited by 100

Kaposi's Sarcoma-Associated Herpesvirus Infection Promotes Invasion of Primary Human Umbilical Vein Endothelial Cells by Inducing Matrix Metalloproteinases

Qian, L., Xie, J., Ye, F., & Gao, S. (2007) · Journal of Virology · doi:10.1128/jvi.00016-07 · Cited by 99

Molecular and Cellular Mechanisms of Syndecans in Tissue Injury and Inflammation

Bartlett, A. H., Hayashida, K., & Park, P. W. (2007) · Molecules and Cells · doi:10.1016/s1016-8478(23)07324-7 · Cited by 102

Matrix Metalloproteinase Processing of CXCL11/I-TAC Results in Loss of Chemoattractant Activity and Altered Glycosaminoglycan Binding

Cox, J. H., Dean, R. A., Roberts, C. R., & Overall, C. M. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m800266200 · Cited by 99

Anti-inflammatory effects of anethole in lipopolysaccharide-induced acute lung injury in mice

Kang, P., Kim, K. Y., Lee, H. S., Min, S. S., & Seol, G. H. (2013) · Life Sciences · doi:10.1016/j.lfs.2013.10.014 · Cited by 99

Rac1-mediated Mitochondrial H2O2 Generation Regulates MMP-9 Gene Expression in Macrophages via Inhibition of SP-1 and AP-1

Murthy, S., Ryan, A. J., He, C., Mallampalli, R. K., & Carter, A. B. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.099655 · Cited by 100

Matrix Metalloproteinase-12 and Cathepsin D Expression in Pulmonary Macrophages and Dendritic Cells of Cigarette Smoke-Exposed Mice

Bracke, K. R., Cataldo, D. D., Maes, T., Gueders, M. M., Noël, A., Foidart, J., Brusselle, G., & PAUWELS, R. A. (2005) · International Archives of Allergy and Immunology · doi:10.1159/000088439 · Cited by 99

Matrix Metalloproteinase 12 Overexpression in Lung Epithelial Cells Plays a Key Role in Emphysema to Lung Bronchioalveolar Adenocarcinoma Transition

Qu, P., Du, H., Wang, X., & Yan, C. (2009) · Cancer Research · doi:10.1158/0008-5472.can-09-0577 · Cited by 99

Overview of the mechanisms regulating chemokine activity and availability

Mortier, A., Damme, J. V., & Proost, P. (2012) · Immunology Letters · doi:10.1016/j.imlet.2012.04.015 · Cited by 98

Stromelysin-2 (MMP10) Moderates Inflammation by Controlling Macrophage Activation

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Proteases and the gut barrier

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