Matrix Metalloproteinases

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

Molecular basis of sun-induced premature skin ageing and retinoid antagonism

Fisher, G. J., Datta, S. C., Talwar, H. S., Wang, Z.-Q., Varani, J., Kang, S., & Voorhees, J. J. (1996) · Nature · doi:10.1038/379335a0 · Cited by 1,410

Mechanism of inhibition of the human matrix metalloproteinase stromelysin-1 by TIMP-1.

Gomis-R¨th, F.-X., Maskos, K., Betz, M., Bergner, A., Huber, R., Suzuki, K., Yoshida, N., Nagase, H., Brew, K., Bourenkov, G. P., et al. (1997) · Nature · doi:10.1038/37995 · Cited by 619

Retinoic acid inhibits induction of c-Jun protein by ultraviolet radiation that occurs subsequent to activation of mitogen-activated protein kinase pathways in human skin in vivo

Fisher, G. J., Talwar, H. S., Lin, J., Lin, P., McPhillips, F., Wang, Z., Li, X., Wan, Y., Kang, S., & Voorhees, J. J. (1998) · Journal of Clinical Investigation · doi:10.1172/jci2153 · Cited by 392

Neuronal matrix metalloproteinase-2 degrades and inactivates a neurite-inhibiting chondroitin sulfate proteoglycan

Zuo, J., Ferguson, T. A., Hernandez, Y. J., Stetler-Stevenson, W. G., & Muir, D. (1998) · The Journal of Neuroscience · doi:10.1523/jneurosci.18-14-05203.1998 · Cited by 270

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

Extracellular Matrix Degradation and Remodeling in Development and Disease

Lu, P., Takai, K., Weaver, V. M., & Werb, Z. (2011) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a005058 · Cited by 2,265

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

Pathophysiology of polytrauma

Keel, M., & Trentz, O. (2005) · Injury · doi:10.1016/j.injury.2004.12.037 · Cited by 885

IL-22 Inhibits Epidermal Differentiation and Induces Proinflammatory Gene Expression and Migration of Human Keratinocytes

Boniface, K., Bernard, F.-X., Garcia, M., Gurney, A. L., Lecron, J.-C., & Morel, F. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.174.6.3695 · Cited by 864

Dual Role of Matrix Metalloproteinases (Matrixins) in Intimal Thickening and Atherosclerotic Plaque Rupture

Newby, A. C. (2005) · Physiological Reviews · doi:10.1152/physrev.00048.2003 · Cited by 817

Transcriptional regulation of collagenase (MMP-1, MMP-13) genes in arthritis: integration of complex signaling pathways for the recruitment of gene-specific transcription factors

Vincenti, M. P., & Brinckerhoff, C. E. (2002) · Arthritis Research & Therapy · doi:10.1186/ar401 · Cited by 796

The ADAMTS metalloproteinases

PORTER, S., CLARK, I. M., KEVORKIAN, L., & EDWARDS, D. R. (2005) · Biochemical Journal · doi:10.1042/bj20040424 · Cited by 779

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

Gelatinase B functions as regulator and effector in leukocyte biology

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

Propranolol for infantile haemangiomas: insights into the molecular mechanisms of action: Propranolol in haemangiomas

Storch, C. H., & Hoeger, P. H. (2010) · British Journal of Dermatology · doi:10.1111/j.1365-2133.2010.09848.x · Cited by 526

Matrix metalloproteinase-9 is required for hippocampal late-phase long-term potentiation and memory

Nagy, V., Bozdagi, O., Matynia, A., Balcerzyk, M., Okulski, P., Dzwonek, J., Costa, R. M., Silva, A. J., Kaczmarek, L., & Huntley, G. W. (2006) · The Journal of Neuroscience · doi:10.1523/jneurosci.4359-05.2006 · Cited by 499

The role of matrix metalloproteinases (MMPs) in human caries

Chaussain-Miller, C., Fioretti, F., Goldberg, M., & Menashi, S. (2006) · Journal of Dental Research · doi:10.1177/154405910608500104 · Cited by 481

Matrix Metalloproteinase-9 Undergoes Expression and Activation during Dendritic Remodeling in Adult Hippocampus

Szklarczyk, A., Lapinska, J., Rylski, M., McKay, R. D. G., & Kaczmarek, L. (2002) · The Journal of Neuroscience · doi:10.1523/jneurosci.22-03-00920.2002 · Cited by 392

The role of chondrocyte senescence in osteoarthritis

Price, J. S., Waters, J. G., Darrah, C., Pennington, C., Edwards, D. R., Donell, S. T., & Clark, I. M. (2002) · Aging Cell · doi:10.1046/j.1474-9728.2002.00008.x · Cited by 386

Matrix Metalloproteinase-9 Degrades Amyloid-β Fibrils in Vitro and Compact Plaques in Situ

Yan, P., Hu, X., Song, H., Yin, K., Bateman, R. J., Cirrito, J. R., Xiao, Q., Hsu, F. F., Turk, J. W., Xu, J., et al. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602440200 · Cited by 380

Oxidative stress, neurodegeneration, and the balance of protein degradation and protein synthesis

Dasuri, K., Zhang, L., & Keller, J. N. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.09.016 · Cited by 371

TIMP-3 Binds to Sulfated Glycosaminoglycans of the Extracellular Matrix

Yu, W.-H., Yu, S.-S. C., Meng, Q., Brew, K., & Woessner, J. F. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000907200 · Cited by 328

Anticancer Activity of Chitosan, Chitosan Derivatives, and Their Mechanism of Action

Adhikari, H. S., & Yadav, P. N. (2018) · International Journal of Biomaterials · doi:10.1155/2018/2952085 · Cited by 313

CD44 directs membrane-type 1 matrix metalloproteinase to lamellipodia by associating with its hemopexin-like domain.

Mori, H., Tomari, T., Koshikawa, N., Kajita, M., Itoh, Y., Sato, H., Tojo, H., Yana, I., & Seiki, M. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf411 · Cited by 296

Interleukin-1 beta promotes matrix metalloproteinase expression and cell proliferation in calcific aortic valve stenosis

Kaden, J. J., Dempfle, C.-E., Grobholz, R., Tran, H.-T., Kılıç, R., Sarıkoç, A., Brueckmann, M., Vahl, C., Hagl, S., Haase, K. K., et al. (2003) · Atherosclerosis · doi:10.1016/s0021-9150(03)00284-3 · Cited by 272

Modulation of Adipose Tissue Expression of Murine Matrix Metalloproteinases and Their Tissue Inhibitors With Obesity

Maquoi, E., Munaut, C., Colige, A., Collen, D., & Lijnen, H. R. (2002) · Diabetes · doi:10.2337/diabetes.51.4.1093 · Cited by 271

Autophagy Regulates TGF-β Expression and Suppresses Kidney Fibrosis Induced by Unilateral Ureteral Obstruction

Ding, Y., Kim, S. L., Lee, S.-Y., Koo, J. K., Wang, Z., & Choi, M. E. (2014) · Journal of the American Society of Nephrology · doi:10.1681/asn.2013101068 · Cited by 264

Topically Applied Vitamin C Enhances the mRNA Level of Collagens I and III, Their Processing Enzymes and Tissue Inhibitor of Matrix Metalloproteinase 1 in the Human Dermis11Part of this work was presented in poster form at the American Academy of Dermatology, San Francisco, CA, March 10–15, 2000.

Nusgens, B. V., Colige, A. C., Lambert, C. A., Lapière, C. M., Humbert, P., Rougier, A., Haftek, M., Richard, A., & Creidi, P. (2001) · Journal of Investigative Dermatology · doi:10.1046/j.0022-202x.2001.01362.x · Cited by 262

Nanoparticles for modulating tumor microenvironment to improve drug delivery and tumor therapy

Yang, S., & Gao, H. (2017) · Pharmacological Research · doi:10.1016/j.phrs.2017.05.004 · Cited by 256

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

Tam, E. M., Morrison, C. J., Wu, Y. I., Stack, M. S., & Overall, C. M. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0305862101 · Cited by 244

Extracellular matrix signaling in morphogenesis and repair

Clause, K. C., & Barker, T. H. (2013) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2013.04.011 · Cited by 230

Hypoxia stimulates breast carcinoma cell invasion through MT1-MMP and MMP-2 activation

Muñoz-Nájar, U. M., Neurath, K. M., Vumbaca, F., & Claffey, K. P. (2006) · Oncogene · doi:10.1038/sj.onc.1209273 · Cited by 209

Transcriptional characterizations of differences between eutopic and ectopic endometrium

Wu, Y., Kajdacsy-Balla, A., Strawn, E., Basir, Z., Halverson, G., Jailwala, P., Wang, Y., Wang, X., Ghosh, S., & Guo, S.-W. (2006) · Endocrinology · doi:10.1210/en.2005-0426 · Cited by 208

White matter damage is associated with matrix metalloproteinases in vascular dementia

Rosenberg, G. A., Sullivan, N., & Esiri, M. M. (2001) · Stroke · doi:10.1161/01.str.32.5.1162 · Cited by 207

Friends or foes: matrix metalloproteinases and their multifaceted roles in neurodegenerative diseases

Brkic, M., Balusu, S., Libert, C., & Vandenbroucke, R. E. (2015) · Mediators of Inflammation · doi:10.1155/2015/620581 · Cited by 205

Peroxynitrite-induced myocardial injury is mediated through matrix metalloproteinase-2

Wang, W. (2002) · Cardiovascular Research · doi:10.1016/s0008-6363(01)00445-x · Cited by 191

Tissue inhibitors of metalloproteinases and programmed cell death: Conundrums, controversies and potential implications

Mannello, F., & Gazzanelli, G. (2001) · Apoptosis · doi:10.1023/a:1012493808790 · Cited by 185

In vivo roles for matrix metalloproteinase-9 in mature hippocampal synaptic physiology and plasticity

Bozdagi, O., Nagy, V., Kwei, K. T., & Huntley, G. W. (2007) · Journal of Neurophysiology · doi:10.1152/jn.00202.2007 · Cited by 182

Matrix metalloproteinase-2 and -9 are induced differently by doxorubicin in H9c2 cells: The role of MAP kinases and NAD(P)H oxidase

SPALLAROSSA, P., ALTIERI, P., GARIBALDI, S., GHIGLIOTTI, G., BARISIONE, C., MANCA, V, FABBI, P., BALLESTRERO, A., BRUNELLI, C., & BARSOTTI, A. (2006) · Cardiovascular Research · doi:10.1016/j.cardiores.2005.08.009 · Cited by 182

Differences in the Fibrogenic Response after Transfer of Active Transforming Growth Factor- β 1 Gene to Lungs of “Fibrosis-prone” and “Fibrosis-resistant” Mouse Strains

Kolb, M., Bonniaud, P., Galt, T., Sime, P. J., Kelly, M. M., Margetts, P. J., & Gauldie, J. (2002) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/ajrcmb.27.2.4674 · Cited by 168

Matrix metalloproteinases and cellular fibrinolytic activity

Lijnen, H. R. (2002) · Biochemistry (Moscow) · doi:10.1023/a:1013908332232 · Cited by 167

Requirement of STAT3 activation for maximal collagenase-1 (MMP-1) induction by epidermal growth factor and malignant characteristics in T24 bladder cancer cells

Itoh, M., Murata, T., Suzuki, T., Shindoh, M., Nakajima, K., Imai, K., & Yoshida, K. (2006) · Oncogene · doi:10.1038/sj.onc.1209149 · Cited by 166

Fucoidan a sulfated polysaccharide from brown algae is a potent modulator of connective tissue proteolysis

Senni, K., Gueniche, F., Foucault-Bertaud, A., Igondjo-Tchen, S., Fioretti, F., Colliec-Jouault, S., Durand, P., Guezennec, J., Godeau, G., & Letourneur, D. (2006) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2005.11.001 · Cited by 163

Characterization of the Distinct Collagen Binding, Helicase and Cleavage Mechanisms of Matrix Metalloproteinase 2 and 14 (Gelatinase A and MT1-MMP)

Tam, E. M., Moore, T. R., Butler, G. S., & Overall, C. M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m407186200 · Cited by 142

The Low Density Lipoprotein Receptor-related Protein LRP Is Regulated by Membrane Type-1 Matrix Metalloproteinase (MT1-MMP) Proteolysis in Malignant Cells

Rozanov, D. V., Hahn-Dantona, E., Strickland, D. K., & Strongin, A. Y. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m311569200 · Cited by 130

Omega-3 fatty acids and the regulation of expression of endothelial pro-atherogenic and pro-inflammatory genes

De Caterina, R., & Massaro, M. (2005) · Journal of Membrane Biology · doi:10.1007/s00232-005-0783-2 · Cited by 130

Downregulation of Matrix Metalloproteinase-9 and Attenuation of Edema via Inhibition of ERK Mitogen Activated Protein Kinase in Traumatic Brain Injury

Mori, T., Wang, X., Aoki, T., & Lo, E. H. (2002) · Journal of Neurotrauma · doi:10.1089/089771502320914642 · Cited by 129

Evaluation of metalloproteinase 2 and 9 levels and their inhibitors in diabetic and healthy subjects

Derosa, G., D’Angelo, A., Tinelli, C., Devangelio, E., Consoli, A., Miccoli, R., Penno, G., Del Prato, S., Paniga, S., & Cicero, A. F. G. (2007) · Diabetes & Metabolism · doi:10.1016/j.diabet.2006.11.008 · Cited by 129

Role of matrix metalloproteinases in dental caries, pulp and periapical inflammation: an overview

Jain, A., & Bahuguna, R. (2015) · Journal of Oral Biology and Craniofacial Research · doi:10.1016/j.jobcr.2015.06.015 · Cited by 122

Cardiac remodeling and failure

Fedak, P. W. M., Verma, S., Weisel, R. D., & Li, R.-K. (2005) · Cardiovascular Pathology · doi:10.1016/j.carpath.2005.01.005 · Cited by 120

Matrix-metalloproteinase-14 deficiency in bone-marrow-derived cells promotes collagen accumulation in mouse atherosclerotic plaques.

Schneider, F., Sukhova, G. K., Aikawa, M., Canner, J., Gerdes, N., Tang, S.-M. T., Shi, G.-P., Apte, S. S., & Libby, P. (2008) · Circulation · doi:10.1161/circulationaha.107.707448 · Cited by 119

Suppression of matrix metalloproteinase-9 transcription by transforming growth factor-β is mediated by a nuclear factor-κB site

OGAWA, K., CHEN, F., KUANG, C., & CHEN, Y. (2004) · Biochemical Journal · doi:10.1042/bj20040058 · Cited by 116

Tumor-associated Trypsinogen-2 (Trypsinogen-2) activates procollagenases (MMP-1, -8, -13) and Stromelysin-1 (MMP-3) and degrades type I collagen

Moilanen, M., Sorsa, T., Stenman, M., Nyberg, P., Lindy, O., Vesterinen, J., Paju, A., Konttinen, Y. T., Stenman, U.-H., & Salo, T. (2003) · Biochemistry · doi:10.1021/bi020582s · Cited by 111

The extracellular protease matrix metalloproteinase-9 is activated by inhibitory avoidance learning and required for long-term memory

Nagy, V., Bozdagi, O., & Huntley, G. W. (2007) · Learning & Memory · doi:10.1101/lm.678307 · Cited by 107

Recent computational advances in the identification of allosteric sites in proteins

Lu, S., Huang, W., & Zhang, J. (2014) · Drug Discovery Today · doi:10.1016/j.drudis.2014.07.012 · Cited by 102

The Genetic Basis of Peyronie Disease: A Review

Herati, A. S., & Pastuszak, A. W. (2016) · Sexual Medicine Reviews · doi:10.1016/j.sxmr.2015.10.002 · Cited by 104

Structural and Enzymatic Characterization of Drosophila Dm2-MMP, a Membrane-bound Matrix Metalloproteinase with Tissue-specific Expression

Llano, E., Adam, G., Pendás, A. M., Quesada, V., Sánchez, L. M., Santamarı́a, I., Noselli, S., & López-Otı́n, C. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m200121200 · Cited by 100

Protease-Responsive Prodrug with Aggregation-Induced Emission Probe for Controlled Drug Delivery and Drug Release Tracking in Living Cells

Cheng, Y., Huang, F., Min, X., Gao, P., Zhang, T., Li, X., Liu, B., Hong, Y., Lou, X., & Xia, F. (2016) · Analytical Chemistry · doi:10.1021/acs.analchem.6b02833 · Cited by 94

ECM in brain aging and dementia

Morawski, M., Filippov, M., Tzinia, A., Tsilibary, E., & Vargova, L. (2014) · Progress in Brain Research · doi:10.1016/b978-0-444-63486-3.00010-4 · Cited by 84

Synaptically released matrix metalloproteinase activity in control of structural plasticity and the cell surface distribution of GluA1-AMPA receptors

Szepesi, Z., Hosy, E., Ruszczycki, B., Bijata, M., Pyskaty, M., Bikbaev, A., Heine, M., Choquet, D., Kaczmarek, L., & Wlodarczyk, J. (2014) · PLoS ONE · doi:10.1371/journal.pone.0098274 · Cited by 83

The Role of the Skeletal Muscle Secretome in Mediating Endurance and Resistance Training Adaptations

Leuchtmann, A. B., Adak, V., Dilbaz, S., & Handschin, C. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2021.709807 · Cited by 84

Cleavage of Amyloid-β Precursor Protein (APP) by Membrane-Type Matrix Metalloproteinases

Ahmad, M., Takino, T., Miyamori, H., Yoshizaki, T., Furukawa, M., & Sato, H. (2006) · The Journal of Biochemistry · doi:10.1093/jb/mvj054 · Cited by 82

Chemokine-protease interactions in cancer

Van Damme, J., Struyf, S., & Opdenakker, G. (2004) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2003.10.007 · Cited by 71

New approaches to selectively target cancer-associated matrix metalloproteinase activity

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

Epigenetic regulation of matrix metalloproteinases and their collagen substrates in cancer

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

Differential Calcium Independent Regulation of Matrix Metalloproteinases and Tissue Inhibitors of Matrix Metalloproteinases by Interleukin-1β and Transforming Growth Factor-β in Peyronie's Plaque Fibroblasts

Del Carlo, M., Cole, A. A., & Levine, L. A. (2008) · Journal of Urology · doi:10.1016/j.juro.2008.01.093 · Cited by 69

Non-antibiotic properties of tetracyclines and their clinical application in dermatology

Perret, L. J., & Tait, C. P. (2014) · Australasian Journal of Dermatology · doi:10.1111/ajd.12075 · Cited by 68

The intrinsic protein flexibility of endogenous protease inhibitor TIMP-1 controls its binding interface and affects its function.

Grossman, M., Tworowski, D., Dym, O., Lee, M.-H., Levy, Y., Murphy, G., & Sagi, I. (2010) · Biochemistry · doi:10.1021/bi902141x · Cited by 68

Degradation of the extracellular matrix components by bacterial-derived metalloproteases: Implications for inflammatory bowel diseases

Pruteanu, M., Hyland, N. P., Clarke, D. J., Kiely, B., & Shanahan, F. (2011) · Inflammatory Bowel Diseases · doi:10.1002/ibd.21475 · Cited by 67

Aberrant, persistent inclusion into lipid rafts limits the tumorigenic function of membrane type-1 matrix metalloproteinase in malignant cells.

Rozanov, D. V., Deryugina, E. I., Monosov, E. Z., Marchenko, N. D., & Strongin, A. Y. (2004) · Experimental Cell Research · doi:10.1016/j.yexcr.2003.10.006 · Cited by 64

Sorsby fundus dystrophy—A review of pathology and disease mechanisms

Christensen, D. R. G., Brown, F. E., Cree, A. J., Ratnayaka, J. A., & Lotery, A. J. (2017) · Experimental Eye Research · doi:10.1016/j.exer.2017.08.014 · Cited by 60

Matrix metalloproteinase-9 activity increased by two different types of epileptic seizures that do not induce neuronal death: A possible role in homeostatic synaptic plasticity

Takács, E., Nyilas, R., Szepesi, Z., Baracskay, P., Karlsen, B., Røsvold, T., Bjørkum, A. A., Czurkó, A., Kovács, Z., Kékesi, A. K., et al. (2010) · Neurochemistry International · doi:10.1016/j.neuint.2010.03.003 · Cited by 63

Butyrate upregulates stromelysin-1 production by intestinal mesenchymal cells

Pender, S. L. F., Quinn, J. J., Sanderson, I. R., & MacDonald, T. T. (2000) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.2000.279.5.g918 · Cited by 55

Tricyclic Antidepressant Amitriptyline Activates Fibroblast Growth Factor Receptor Signaling in Glial Cells

Hisaoka, K., Tsuchioka, M., Yano, R., Maeda, N., Kajitani, N., Morioka, N., Nakata, Y., & Takebayashi, M. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.224683 · Cited by 57

Mutations in the Interglobular Domain of Aggrecan Alter Matrix Metalloproteinase and Aggrecanase Cleavage Patterns

Mercuri, F. A., Maciewicz, R. A., Tart, J., Last, K., & Fosang, A. J. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.42.33038 · Cited by 52

Membrane Type-1 Matrix Metalloproteinase Functions as a Proprotein Self-convertase

Rozanov, D. V., & Strongin, A. Y. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m213246200 · Cited by 49

Clinical investigation of matrix metalloproteinases, tissue inhibitors of matrix metalloproteinases, and matrix metalloproteinase/tissue inhibitors of matrix metalloproteinase complexes and their networks in apical periodontitis

Martinho, F. C., Teixeira, F. F. C., Cardoso, F. G. R., Ferreira, N. S., Nascimento, G. G., Carvalho, C. A. T., & Valera, M. C. (2016) · Journal of Endodontics · doi:10.1016/j.joen.2016.04.001 · Cited by 48

Activity of matrix metallo proteinases (MMPs) and the tissue inhibitor of MMP (TIMP)-1 in electromagnetic field-exposed THP-1 cells

Patruno, A., Pesce, M., Marrone, A., Speranza, L., Grilli, A., De Lutiis, M. A., Felaco, M., & Reale, M. (2012) · Journal of Cellular Physiology · doi:10.1002/jcp.23024 · Cited by 42

Crystal structure of the catalytic domain of MMP-16/MT3-MMP: Characterization of MT-MMP specific features.

Lang, R., Braun, M., Sounni, N. E., Noel, A., Frankenne, F., Foidart, J.-M., Bode, W., & Maskos, K. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2003.12.022 · Cited by 42

Suppression of fibroblast metalloproteinases by ajulemic acid, a nonpsychoactive cannabinoid acid

Johnson, D. R., Stebulis, J. A., Rossetti, R. G., Burstein, S. H., & Zurier, R. B. (2007) · Journal of Cellular Biochemistry · doi:10.1002/jcb.21046 · Cited by 41

Mitochondrial matrix RTN4IP1/OPA10 is an oxidoreductase for coenzyme Q synthesis

Park, I., Kim, K.-E., Kim, J., Kim, A.-K., Bae, S., Jung, M., Choi, J., Mishra, P. K., Kim, T.-M., Kwak, C., et al. (2024) · Nature Chemical Biology · doi:10.1038/s41589-023-01452-w · Cited by 39

Monocyte/Macrophage MMP-14 Modulates Cell Infiltration and T-Cell Attraction in Contact Dermatitis But Not in Murine Wound Healing

Klose, A., Zigrino, P., & Mauch, C. (2013) · The American Journal of Pathology · doi:10.1016/j.ajpath.2012.11.028 · Cited by 38

Gastroprotective effect of kefir on ulcer induced in irradiated rats

Fahmy, H. A., & Ismail, A. F. M. (2015) · Journal of Photochemistry and Photobiology B: Biology · doi:10.1016/j.jphotobiol.2015.02.009 · Cited by 35

Oxidative Remodeling in Pressure Overload Induced Chronic Heart Failure

Henderson, B. C., Tyagi, N., Ovechkin, A., Kartha, G. K., Moshal, K. S., & Tyagi, S. C. (2007) · European Journal of Heart Failure · doi:10.1016/j.ejheart.2006.12.008 · Cited by 32

Matrix Metalloproteinase-14 Is a Negative Prognostic Marker for Patients with Gastric Cancer

He, L., Chu, D., Li, X., Zheng, J., Liu, S., Li, J., Zhao, Q., & Ji, G. (2013) · Digestive Diseases and Sciences · doi:10.1007/s10620-012-2513-9 · Cited by 28

Modulation of matrix metalloproteinases activity in the ventral horn of the spinal cord re-stores neuroglial synaptic homeostasis and neurotrophic support following peripheral nerve injury.

Cirillo, G., Colangelo, A. M., De Luca, C., Savarese, L., Barillari, M. R., Alberghina, L., & Papa, M. (2016) · PLoS ONE · doi:10.1371/journal.pone.0152750 · Cited by 27

Wnt activation disturbs cell competition and causes diffuse invasion of transformed cells through NF-κB-MMP21 pathway

Nakai, K., Lin, H., Yamano, S., Tanaka, S., Kitamoto, S., Saitoh, H., Sakuma, K., Kurauchi, J., Akter, E., Konno, M., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-42774-6 · Cited by 14

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