Structure and function of matrix metalloproteinases and TIMPs

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

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

Molecular Mechanisms of Stress-Responsive Changes in Collagen and Elastin Networks in Skin

Aziz, J., Shezali, H., Radzi, Z., Yahya, N. A., Abu Kassim, N. H., Czernuszka, J., & Rahman, M. T. (2016) · Skin Pharmacology and Physiology · doi:10.1159/000447017 · Cited by 7,323

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

An overview of tissue and whole organ decellularization processes

Crapo, P. M., Gilbert, T. W., & Badylak, S. F. (2011) · Biomaterials · doi:10.1016/j.biomaterials.2011.01.057 · Cited by 3,591

Extracellular matrix structure

Theocharis, A. D., Skandalis, S. S., Gialeli, C., & Karamanos, N. K. (2016) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2015.11.001 · Cited by 2,598

Mechanotransduction and extracellular matrix homeostasis

Humphrey, J. D., Dufresne, E. R., & Schwartz, M. A. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3896 · Cited by 2,124

The Roles of Matrix Metalloproteinases and Their Inhibitors in Human Diseases

Cabral-Pacheco, G. A., Garza-Veloz, I., Castruita-De la Rosa, C., Ramirez-Acuña, J. M., Perez-Romero, B. A., Guerrero-Rodriguez, J. F., Martinez-Avila, N., & Martinez-Fierro, M. L. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21249739 · Cited by 1,820

Extracellular Matrix Reorganization During Wound Healing and Its Impact on Abnormal Scarring

Xue, M., & Jackson, C. J. (2015) · Advances in Wound Care · doi:10.1089/wound.2013.0485 · Cited by 1,468

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

Acute Exacerbations of Idiopathic Pulmonary Fibrosis

Collard, H. R., Moore, B. B., Flaherty, K. R., Brown, K. K., Kaner, R. J., King, T. E., Lasky, J. A., Loyd, J. E., Noth, I., Olman, M. A., et al. (2007) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.200703-463pp · Cited by 1,130

Matrix metalloproteinases (MMPs), the main extracellular matrix (ECM) enzymes in collagen degradation, as a target for anticancer drugs

Jabłońska-Trypuć, A., Matejczyk, M., & Rosochacki, S. (2016) · Journal of Enzyme Inhibition and Medicinal Chemistry · doi:10.3109/14756366.2016.1161620 · Cited by 1,042

Molecular Mechanisms of Dermal Aging and Antiaging Approaches

Shin, J.-W., Kwon, S.-H., Choi, J.-Y., Na, J.-I., Huh, C.-H., Choi, H.-R., & Park, K.-C. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20092126 · Cited by 875

Matrix metalloproteinases in the brain and blood–brain barrier: Versatile breakers and makers

Rempe, R. G., Hartz, A. M., & Bauer, B. (2016) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1177/0271678x16655551 · Cited by 721

The extracellular matrix in tumor progression and metastasis

Eble, J. A., & Niland, S. (2019) · Clinical & Experimental Metastasis · doi:10.1007/s10585-019-09966-1 · Cited by 613

Structure and Function of Human Matrix Metalloproteinases

Laronha, H., & Caldeira, J. (2020) · Cells · doi:10.3390/cells9051076 · Cited by 609

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

Metalloproteinase Expression in Monocytes and Macrophages and its Relationship to Atherosclerotic Plaque Instability

Newby, A. C. (2008) · Arteriosclerosis, Thrombosis, and Vascular Biology · doi:10.1161/atvbaha.108.173898 · Cited by 496

The ADAMs: signalling scissors in the tumour microenvironment

Murphy, G. (2008) · Nature Reviews Cancer · doi:10.1038/nrc2459 · Cited by 451

Comprehensive review of mechanisms of pathogenesis involved in Alzheimer’s disease and potential therapeutic strategies

Sharma, P., Srivastava, P., Seth, A., Tripathi, P. N., Banerjee, A. G., & Shrivastava, S. K. (2019) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2018.12.006 · Cited by 331

Amyloid-Beta Protein Clearance and Degradation (ABCD) Pathways and their Role in Alzheimer’s Disease

Baranello, R., Bharani, K., Padmaraju, V., Chopra, N., Lahiri, D., Greig, N., Pappolla, M., & Sambamurti, K. (2015) · Current Alzheimer Research · doi:10.2174/1567205012666141218140953 · Cited by 331

Hyaluronidases in cancer biology

Stern, R. (2008) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2008.03.017 · Cited by 261

Extracellular matrix, regional heterogeneity of the aorta, and aortic aneurysm

Jana, S., Hu, M., Shen, M., & Kassiri, Z. (2019) · Experimental & Molecular Medicine · doi:10.1038/s12276-019-0286-3 · Cited by 226

Multiphasic roles for matrix metalloproteinases after stroke

ROSELL, A., & LO, E. (2008) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2007.12.001 · Cited by 215

Active site specificity profiling of the matrix metalloproteinase family: Proteomic identification of 4300 cleavage sites by nine MMPs explored with structural and synthetic peptide cleavage analyses.

Eckhard, U., Huesgen, P. F., Schilling, O., Bellac, C. L., Butler, G. S., Cox, J. H., Dufour, A., Goebeler, V., Kappelhoff, R., Keller, U. A. D., et al. (2016) · Matrix Biology · doi:10.1016/j.matbio.2015.09.003 · Cited by 212

Senescence Reprogramming by TIMP1 Deficiency Promotes Prostate Cancer Metastasis

Guccini, I., Revandkar, A., D'Ambrosio, M., Colucci, M., Pasquini, E., Mosole, S., Troiani, M., Brina, D., Sheibani-Tezerji, R., Elia, A. R., et al. (2021) · Cancer Cell · doi:10.1016/j.ccell.2020.10.012 · Cited by 185

Recent advances in stimuli‐responsive theranostic systems with aggregation‐induced emission characteristics

Hu, J., Jiang, W., Yuan, L., Duan, C., Yuan, Q., Long, Z., Lou, X., & Xia, F. (2021) · Aggregate · doi:10.1002/agt2.10 · Cited by 172

Role of Gelatinases MMP-2 and MMP-9 in Healthy and Complicated Pregnancy and Their Future Potential as Preeclampsia Biomarkers

Nikolov, A., & Popovski, N. (2021) · Diagnostics · doi:10.3390/diagnostics11030480 · Cited by 141

Sequential Amyloid-β Degradation by the Matrix Metalloproteases MMP-2 and MMP-9

Hernandez-Guillamon, M., Mawhirt, S., Blais, S., Montaner, J., Neubert, T. A., Rostagno, A., & Ghiso, J. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.610931 · Cited by 137

The Design of Inhibitors for Medicinally Relevant Metalloproteins

Jacobsen, F. E., Lewis, J. A., & Cohen, S. M. (2007) · ChemMedChem · doi:10.1002/cmdc.200600204 · Cited by 132

Inflammation and cortisol response in coronary artery disease

Nijm, J., & Jonasson, L. (2009) · Annals of Medicine · doi:10.1080/07853890802508934 · Cited by 128

Matrix metalloproteinases and their inhibitors in the foreign body reaction on biomaterials

Jones, J. A., McNally, A. K., Chang, D. T., Qin, L. A., Meyerson, H., Colton, E., Kwon, I. L. K., Matsuda, T., & Anderson, J. M. (2008) · Journal of Biomedical Materials Research Part A · doi:10.1002/jbm.a.31220 · Cited by 121

Matrix metalloproteinases as input and output signals for post-myocardial infarction remodeling

Lindsey, M. L., Iyer, R. P., Jung, M., DeLeon-Pennell, K. Y., & Ma, Y. (2016) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2015.12.018 · Cited by 113

Lymphocyte/macrophage interactions: biomaterial surface-dependent cytokine, chemokine, and matrix protein production

Chang, D. T., Jones, J. A., Meyerson, H., Colton, E., Kwon, I. K., Matsuda, T., & Anderson, J. M. (2008) · Journal of Biomedical Materials Research Part A · doi:10.1002/jbm.a.31630 · Cited by 114

Macrophages and the Regulation of Adipose Tissue Remodeling

Martinez-Santibañez, G., & Nien-Kai Lumeng, C. (2014) · Annual Review of Nutrition · doi:10.1146/annurev-nutr-071812-161113 · Cited by 111

Membrane-type MMPs enable extracellular matrix permissiveness and mesenchymal cell proliferation during embryogenesis

Shi, J., Son, M.-Y., Yamada, S., Szabova, L., Kahan, S., Chrysovergis, K., Wolf, L., Surmak, A., & Holmbeck, K. (2008) · Developmental Biology · doi:10.1016/j.ydbio.2007.10.017 · Cited by 107

Matrix Metalloproteinases on Skin Photoaging

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

Matrix Metalloproteinases as New Targets in Alzheimer’s Disease: Opportunities and Challenges

Zipfel, P., Rochais, C., Baranger, K., Rivera, S., & Dallemagne, P. (2020) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.0c00352 · Cited by 94

Propolis Modifies Collagen Types I and III Accumulation in the Matrix of Burnt Tissue

Olczyk, P., Wisowski, G., Komosinska-Vassev, K., Stojko, J., Klimek, K., Olczyk, M., & Kozma, E. M. (2013) · Evidence-Based Complementary and Alternative Medicine · doi:10.1155/2013/423809 · Cited by 92

MMP14 in sarcoma: a regulator of tumor microenvironment communication in connective tissues

Gonzalez-Molina, J., Gramolelli, S., Liao, Z., Carlson, J. W., Ojala, P. M., & Lehti, K. (2019) · Cells · doi:10.3390/cells8090991 · Cited by 89

Decellularized xenogeneic scaffolds in transplantation and tissue engineering: Immunogenicity versus positive cell stimulation

Massaro, M. S., Pálek, R., Rosendorf, J., Červenková, L., Liška, V., & Moulisová, V. (2021) · Materials Science and Engineering: C · doi:10.1016/j.msec.2021.112203 · Cited by 82

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

Omega-3 fatty acids in prevention of diabetic retinopathy

Behl, T., & Kotwani, A. (2017) · Journal of Pharmacy and Pharmacology · doi:10.1111/jphp.12744 · Cited by 49

Anti-Photoaging Effect of Plant Extract Fermented with Lactobacillus buchneri on CCD-986sk Fibroblasts and HaCaT Keratinocytes

Kang, Y.-M., Hong, C.-H., Kang, S.-H., Seo, D.-S., Kim, S.-O., Lee, H.-Y., Sim, H.-J., & An, H.-J. (2020) · Journal of Functional Biomaterials · doi:10.3390/jfb11010003 · Cited by 45

Stroma in normal and cancer wound healing

Huet, E., Jaroz, C., Nguyen, H. Q., Belkacemi, Y., de la Taille, A., Stavrinides, V., & Whitaker, H. (2019) · The FEBS Journal · doi:10.1111/febs.14842 · Cited by 42

Increased Circulating MMP-2 Levels in Infertile Patients With Moderate and Severe Pelvic Endometriosis

Malvezzi, H., Aguiar, V. G., Paz, C. C. P. D., Tanus-Santos, J. E., Penna, I. A. D. A., & Navarro, P. A. (2013) · Reproductive Sciences · doi:10.1177/1933719112459234 · Cited by 41

Loss of epidermal MMP-14 expression interferes with angiogenesis but not with re-epithelialization

Zigrino, P., Ayachi, O., Schild, A., Kaltenberg, J., Zamek, J., Nischt, R., Koch, M., & Mauch, C. (2012) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2012.05.003 · Cited by 38

Multifaced Roles of the αvβ3 Integrin in Ehlers–Danlos and Arterial Tortuosity Syndromes’ Dermal Fibroblasts

Zoppi, N., Chiarelli, N., Ritelli, M., & Colombi, M. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19040982 · Cited by 37

Incretin drugs as modulators of atherosclerosis

Gallego-Colon, E., Wojakowski, W., & Francuz, T. (2018) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2018.09.011 · Cited by 35

Effects of Macelignan Isolated from Myristica fragrans (Nutmeg) on Expression of Matrix Metalloproteinase-1 and Type I Procollagen in UVB-Irradiated Human Skin Fibroblasts

Lee, K.-E., Mun, S., Pyun, H.-B., Kim, M.-S., & Hwang, J.-K. (2012) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.b12-00037 · Cited by 33

Effects of GHK-Cu on MMP and TIMP Expression, Collagen and Elastin Production, and Facial Wrinkle Parameters

Badenhorst, T., Svirskis, D., & Merrilees, M. (2016) · Journal of Aging Science · doi:10.4172/2329-8847.1000166 · Cited by 31

Differential temporal expression of matrix metalloproteinases following sciatic nerve crush

Yi, S., Qin, J., Zha, G.-B., Yu, J., & Zhang, H.-H. (2016) · Neural Regeneration Research · doi:10.4103/1673-5374.187059 · Cited by 30

Cardiomyopathy in the dystrophin/utrophin-deficient mouse model of severe muscular dystrophy is characterized by dysregulation of matrix metalloproteinases

Delfín, D. A., Zang, K. E., Schill, K. E., Patel, N. T., Janssen, P. M. L., Raman, S. V., & Rafael-Fortney, J. A. (2012) · Neuromuscular Disorders · doi:10.1016/j.nmd.2012.05.002 · Cited by 27

Collagenase Clostridium histolyticum for the Treatment of Peyronie's Disease: The Development of This Novel Pharmacologic Approach

Gelbard, M. K., Chagan, L., & Tursi, J. P. (2015) · The Journal of Sexual Medicine · doi:10.1111/jsm.12904 · Cited by 26

Blood assessment of the expression levels of matrix metalloproteinase 9 (MMP9) and its natural inhibitor, TIMP1 genes in Iranian schizophrenic patients.

Rahimi, S., Sayad, A., Moslemi, E., Ghafouri-Fard, S., & Taheri, M. (2017) · Metabolic Brain Disease · doi:10.1007/s11011-017-0043-z · Cited by 24

Asiaticoside delays senescence and attenuate generation of ROS in UV‑exposure cells through regulates TGF‑β1/Smad pathway

Jiang, H., Zhou, X., & Chen, L. (2022) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2022.11603 · Cited by 27

Matrix metalloproteinase 7 promoted Schwann cell migration and myelination after rat sciatic nerve injury

Wang, H., Zhang, P., Yu, J., Zhang, F., Dai, W., & Yi, S. (2019) · Molecular Brain · doi:10.1186/s13041-019-0516-6 · Cited by 25

Targeting tumor extracellular matrix with nanoparticles to circumvent therapeutic resistance

Ding, X., Liang, Y., Zhou, S., Wu, Y., Sałata, P., Mikolajczk-Martinez, A., Khosrawipour, V., & Zhang, Z. (2025) · Journal of Controlled Release · doi:10.1016/j.jconrel.2025.113786 · Cited by 20

Immunoreactivity of Kisspeptin and Kisspeptin Receptor in Eutopic and Ectopic Endometrial Tissue of Women With and Without Endometriosis

Abdelkareem, A. O., Alotaibi, F. T., AlKusayer, G. M., Ait-Allah, A. S., Rasheed, S. M., Helmy, Y. A., Allaire, C., Peng, B., Yong, P. J., & Bedaiwy, M. A. (2020) · Reproductive Sciences · doi:10.1007/s43032-020-00167-w · Cited by 15

The role of matrix metalloproteinases in liver function and disease

Mitropoulou, G., Kompoura, V., Saffioti, F., & Mavroeidis, V. K. (2025) · Frontiers in Bioscience-Landmark · doi:10.31083/fbl27127 · Cited by 14

Preventing obesity, insulin resistance and type 2 diabetes by targeting MT1-MMP

Asthana, P., & Wong, H. L. X. (2024) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2024.167081 · Cited by 13

Combinational Treatment Involving Decellularized Extracellular Matrix Hydrogels With Mesenchymal Stem Cells Increased the Efficacy of Cell Therapy in Pancreatitis

Kojima, H., Kushige, H., Yagi, H., Nishijima, T., Moritoki, N., Nagoshi, N., Nakano, Y., Tanaka, M., Hori, S., Hasegawa, Y., et al. (2023) · Cell Transplantation · doi:10.1177/09636897231170437 · Cited by 12

Drugs of the future for Peyronie’s disease

Gur, S., Kadowitz, P. J., & Hellstrom, W. J. G. (2012) · Medical Hypotheses · doi:10.1016/j.mehy.2011.11.008 · Cited by 10