Metalloproteinases and their natural inhibitors in inflammation and 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

Structure and function of matrix metalloproteinases and TIMPs

Nagase, H., Visse, R., & MURPHY, G. (2006) · Cardiovascular Research · doi:10.1016/j.cardiores.2005.12.002 · Cited by 3,507

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

Defensins: antimicrobial peptides of innate immunity

Ganz, T. (2003) · Nature Reviews Immunology · doi:10.1038/nri1180 · Cited by 3,066

Inflammasomes in health and disease

Strowig, T., Henao-Mejia, J., Elinav, E., & Flavell, R. (2012) · Nature · doi:10.1038/nature10759 · Cited by 2,230

Tumour-derived soluble MIC ligands impair expression of NKG2D and T-cell activation

Groh, V., Wu, J. D., Yee, C., & Spies, T. (2002) · Nature · doi:10.1038/nature01112 · Cited by 1,674

An Essential Role for Ectodomain Shedding in Mammalian Development

Peschon, J. J., Slack, J. L., Reddy, P., Stocking, K. L., Sunnarborg, S. W., Lee, D. C., Russell, W. E., Castner, B. J., Johnson, R. S., Fitzner, J. N., et al. (1998) · Science · doi:10.1126/science.282.5392.1281 · Cited by 1,622

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

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

The transmembrane form of tumor necrosis factor is the prime activating ligand of the 80 kDa tumor necrosis factor receptor

Grell, M., Douni, E. K., Wajant, H., Löhden, M., Clauss, M. A., Maxeiner, B., Georgopoulos, S., Lesslauer, W., Kollias, G. A., Pfizenmaier, K., et al. (1995) · Cell · doi:10.1016/0092-8674(95)90192-2 · Cited by 1,328

Innate lymphoid cells promote lung-tissue homeostasis after infection with influenza virus

Monticelli, L. A., Sonnenberg, G. F., Abt, M. C., Alenghat, T., Ziegler, C. G. K., Doering, T. A., Angelosanto, J., Laidlaw, B. J., Yang, C. Y., Sathaliyawala, T., et al. (2011) · Nature Immunology · doi:10.1038/ni.2131 · Cited by 1,327

Remodelling the extracellular matrix in development and disease

Bonnans, C., Chou, J., & Werb, Z. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3904 · Cited by 4,367

The history and advances in cancer immunotherapy: understanding the characteristics of tumor-infiltrating immune cells and their therapeutic implications

Zhang, Y., & Zhang, Z. (2020) · Cellular and Molecular Immunology · doi:10.1038/s41423-020-0488-6 · Cited by 2,906

Is there new hope for therapeutic matrix metalloproteinase inhibition?

Vandenbroucke, R. E., & Libert, C. (2014) · Nature Reviews Drug Discovery · doi:10.1038/nrd4390 · Cited by 856

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 753

Resveratrol regulates neuro-inflammation and induces adaptive immunity in Alzheimer’s disease

Moussa, C., Hebron, M. L., Huang, X., Ahn, J., Rissman, R. A., Aisen, P. S. S., & Turner, R. S. (2017) · Journal of Neuroinflammation · doi:10.1186/s12974-016-0779-0 · Cited by 712

Functions of ROS in Macrophages and Antimicrobial Immunity

Herb, M., & Schramm, M. (2021) · Antioxidants · doi:10.3390/antiox10020313 · Cited by 633

Matrix Metalloproteinases: From Molecular Mechanisms to Physiology, Pathophysiology, and Pharmacology

de Almeida, L. G. N., Thode, H., Eslambolchi, Y., Chopra, S., Young, D. W., Gill, S. E., Devel, L., & Dufour, A. (2022) · Pharmacological Reviews · doi:10.1124/pharmrev.121.000349 · Cited by 572

Inflammation and fibrosis

Mack, M. (2017) · Matrix Biology · doi:10.1016/j.matbio.2017.11.010 · Cited by 535

TIMPs: versatile extracellular regulators in cancer

Jackson, H. W., Defamie, V., Waterhouse, P. D., & Khokha, R. (2016) · Nature reviews. Cancer · doi:10.1038/nrc.2016.115 · Cited by 454

Immune mechanisms in medium and large-vessel vasculitis

Weyand, C. M., & Goronzy, J. J. (2013) · Nature Reviews Rheumatology · doi:10.1038/nrrheum.2013.161 · Cited by 412

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

Modulating extracellular matrix stiffness: A strategic approach to boost cancer immunotherapy

Mai, Z., Lin, Y., Lin, P., Zhao, X., & Cui, L. (2024) · Cell Death & Disease · doi:10.1038/s41419-024-06697-4 · Cited by 398

MMP ‐9 in translation: from molecule to brain physiology, pathology, and therapy

Vafadari, B., Salamian, A., & Kaczmarek, L. (2015) · Journal of Neurochemistry · doi:10.1111/jnc.13415 · Cited by 393

Annexin A1–containing extracellular vesicles and polymeric nanoparticles promote epithelial wound repair

Leoni, G., Neumann, P., Kamaly, N., Quirós, M., Nishio, H., Jones, H. R., Sumagin, R., Hilgarth, R., Alam, A. M., Fredman, G., et al. (2015) · Journal of Clinical Investigation · doi:10.1172/jci76693 · Cited by 362

Resolution of organ fibrosis

Jun, J.-I., & Lau, L. F. (2018) · Journal of Clinical Investigation · doi:10.1172/jci93563 · Cited by 358

Angiogenesis and Inflammation Crosstalk in Diabetic Retinopathy

Capitão, M., & Soares, R. A. (2016) · Journal of Cellular Biochemistry · doi:10.1002/jcb.25575 · Cited by 314

Interleukin-6: from basic biology to selective blockade of pro-inflammatory activities

Scheller, J., Garbers, C., & Rose-John, S. (2014) · Seminars in Immunology · doi:10.1016/j.smim.2013.11.002 · Cited by 308

Re-Emergence of Dendritic Cell Vaccines for Cancer Treatment

Saxena, M., & Bhardwaj, N. (2018) · Trends in cancer · doi:10.1016/j.trecan.2017.12.007 · Cited by 307

Origin and function of stress-induced IL-6 in murine models

Qing, H., Desrouleaux, R., Israni-Winger, K., Mineur, Y. S., Fogelman, N., Zhang, C., Rashed, S., Palm, N. W., Sinha, R., Picciotto, M. R., et al. (2020) · Cell · doi:10.1016/j.cell.2020.05.054 · Cited by 303

The Rebirth of Matrix Metalloproteinase Inhibitors: Moving Beyond the Dogma

Fields, G. B. (2019) · Cells · doi:10.3390/cells8090984 · Cited by 304

Chimeric antigen receptor macrophage therapy for breast tumours mediated by targeting the tumour extracellular matrix

Zhang, W., Liu, L., Su, H., Liu, Q., Shen, J., Dai, H., Zheng, W., Lu, Y., Zhang, W., Bei, Y., et al. (2019) · British Journal of Cancer · doi:10.1038/s41416-019-0578-3 · Cited by 310

Fibroblast activation in cancer: when seed fertilizes soil

Kužet, S.-E., & Gaggioli, C. (2016) · Cell and Tissue Research · doi:10.1007/s00441-016-2467-x · Cited by 301

Ciliary Hedgehog Signaling Restricts Injury-Induced Adipogenesis

Kopinke, D., Roberson, E. C., & Reiter, J. F. (2017) · Cell · doi:10.1016/j.cell.2017.06.035 · Cited by 260

Leukaemogenic effects of Ptpn11 activating mutations in the stem cell microenvironment

Dong, L., Yu, W., Zheng, H., Loh, M. L., Bunting, S. T., Pauly, M. G., Huang, G., Zhou, M., Broxmeyer, H. E., Scadden, D. T., et al. (2016) · Nature · doi:10.1038/nature20131 · Cited by 260

Monocyte and macrophage immunometabolism in atherosclerosis

Groh, L. A., Keating, S. T., Joosten, L. A. B., Netea, M. G., & Riksen, N. P. (2017) · Seminars in Immunopathology · doi:10.1007/s00281-017-0656-7 · Cited by 258

Tuberculosis, Pulmonary Cavitation, and Matrix Metalloproteinases

Ong, C. W. M., Elkington, P. T., & Friedland, J. S. (2014) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.201311-2106pp · Cited by 240

Proteolytic Cleavage—Mechanisms, Function, and “Omic” Approaches for a Near-Ubiquitous Posttranslational Modification

Klein, T., Eckhard, U., Dufour, A., Solis, N., & Overall, C. M. (2017) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00120 · Cited by 237

Metalloproteinases in atherosclerosis

Johnson, J. L. (2017) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2017.09.007 · Cited by 227

Matrix metalloproteinases in arthritis: towards precision medicine

Grillet, B. A. M., Pereira, R. V. S., Damme, J. V., El‐Asrar, A. M. A., Proost, P., & Opdenakker, G. (2023) · Nature Reviews Rheumatology · doi:10.1038/s41584-023-00966-w · Cited by 217

Janus Kinase Inhibitors in the Treatment of Vitiligo: A Review

Qi, F., Liu, F., & Gao, L. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.790125 · Cited by 203

Loss of the Timp gene family is sufficient for the acquisition of the CAF-like cell state

Shimoda, M., Principe, S., Jackson, H. W., Luga, V., Fang, H., Molyneux, S. D., Shao, Y. W., Aiken, A., Waterhouse, P. D., Karamboulas, C., et al. (2014) · Nature Cell Biology · doi:10.1038/ncb3021 · Cited by 209

The impact of cancer-associated fibroblasts on major hallmarks of pancreatic cancer

Sun, Q., Zhang, B., Hu, Q., Qin, Y., Xu, W., Liu, W., Yu, X., & Xu, J. (2018) · Theranostics · doi:10.7150/thno.26546 · Cited by 201

From Structure to Phenotype: Impact of Collagen Alterations on Human Health

Arseni, L., Lombardi, A., & Orioli, D. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19051407 · Cited by 186

Targeting inflammation in diabetes: Newer therapeutic options

Agrawal, N. K. (2014) · World Journal of Diabetes · doi:10.4239/wjd.v5.i5.697 · Cited by 189

New intracellular activities of matrix metalloproteinases shine in the moonlight

Jobin, P. G., Butler, G. S., & Overall, C. M. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2017.05.013 · Cited by 184

Susceptibility of low-density lipoprotein particles to aggregate depends on particle lipidome, is modifiable, and associates with future cardiovascular deaths

Ruuth, M., Nguyen, S. D., Vihervaara, T., Hilvo, M., Laajala, T. D., Kondadi, P. K., Gisterå, A., Lähteenmäki, H., Kittilä, T., Huusko, J., et al. (2018) · European Heart Journal · doi:10.1093/eurheartj/ehy319 · Cited by 180

The Extracellular Matrix: Its Composition, Function, Remodeling, and Role in Tumorigenesis

Dzobo, K., & Dandara, C. (2023) · Biomimetics · doi:10.3390/biomimetics8020146 · Cited by 228

Metalloproteinases in extracellular vesicles

Shimoda, M., & Khokha, R. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2017.05.027 · Cited by 171

Stimuli-Responsive Polymeric Nanoplatforms for Cancer Therapy

Chang, D., Ma, Y., Xu, X., Xie, J., & Ju, S. (2021) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2021.707319 · Cited by 171

Metalloproteinase production from macrophages – a perfect storm leading to atherosclerotic plaque rupture and myocardial infarction

Newby, A. C. (2016) · Experimental Physiology · doi:10.1113/ep085567 · Cited by 159

Shedding of Endogenous Interleukin-6 Receptor (IL-6R) Is Governed by A Disintegrin and Metalloproteinase (ADAM) Proteases while a Full-length IL-6R Isoform Localizes to Circulating Microvesicles

Schumacher, N., Meyer, D., Mauermann, A., von der Heyde, J., Wolf, J., Schwarz, J., Knittler, K., Murphy, G., Michalek, M., Garbers, C., et al. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.649509 · Cited by 152

Stanford-A acute aortic dissection, inflammation, and metalloproteinases: A review

Cifani, N., Proietta, M., Tritapepe, L., Gioia, C. R. T. D., Ferri, L., Taurino, M., & Porto, F. D. (2015) · Annals of Medicine · doi:10.3109/07853890.2015.1073346 · Cited by 146

The Dynamic Interplay Between Cardiac Inflammation and Fibrosis

Thomas, T. P., & Grisanti, L. A. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.529075 · Cited by 153

A novel function of artesunate on inhibiting migration and invasion of fibroblast-like synoviocytes from rheumatoid arthritis patients

Ma, J., Jing, J., Jun-wei, W., Yan, T., Li, Q., Mo, Y., Zheng, D.-H., Gao, J., Nguyen, K.-A. T., & Dai, L. (2019) · Arthritis Research & Therapy · doi:10.1186/s13075-019-1935-6 · Cited by 144

The immunomodulatory role of matrix metalloproteinases in colitis-associated cancer

He, L., Kang, Q., Chan, K. I., Zhang, Y., Zhong, Z., & Tan, W. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2022.1093990 · Cited by 151

Squalene targets pro- and anti-inflammatory mediators and pathways to modulate over-activation of neutrophils, monocytes and macrophages

Cárdeno, A., Aparicio‐Soto, M., la Paz, S. M., Bermúdez, B., Muriana, F. J. G., & Alarcón‐de‐la‐Lastra, C. (2015) · Journal of Functional Foods · doi:10.1016/j.jff.2015.03.009 · Cited by 148

Biology of Tissue Inhibitor of Metalloproteinase 3 (TIMP3), and Its Therapeutic Implications in Cardiovascular Pathology

Dong, F., & Kassiri, Z. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.00661 · Cited by 147

ADAM-family metalloproteinases in lung inflammation: potential therapeutic targets

Yildiz, D., Uhlig, S., & Ludwig, A. (2014) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00294.2014 · Cited by 145

Proteolytic Cleavage Governs Interleukin-11 Trans-signaling

Lokau, J., Nitz, R., Agthe, M., Monhasery, N., Aparicio-Siegmund, S., Schumacher, N., Wolf, J., Möller‐Hackbarth, K., Waetzig, G. H., Grötzinger, J., et al. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.01.053 · Cited by 135

Immunomodulatory biomaterials and their application in therapies for chronic inflammation-related diseases

Nakkala, J. R., Li, Z., Ahmad, W., Wang, K., & Gao, C. (2021) · Acta Biomaterialia · doi:10.1016/j.actbio.2021.01.025 · Cited by 136

Cerebral Malaria in Mouse and Man

Ghazanfari, N., Mueller, S. N., & Heath, W. R. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.02016 · Cited by 134

Perturbations of the cerebrovascular matrisome: A convergent mechanism in small vessel disease of the brain?

Joutel, A., Haddad, I., Ratelade, J., & Nelson, M. T. (2015) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/jcbfm.2015.62 · Cited by 137

Role of Matrix Metalloproteinases in the Pathogenesis of Traumatic Brain Injury

Muneer, P. M. A., Pfister, B. J., Haorah, J., & Chandra, N. (2015) · Molecular Neurobiology · doi:10.1007/s12035-015-9520-8 · Cited by 132

Regulation of A disintegrin and metalloproteinase (ADAM) family sheddases ADAM10 and ADAM17: The emerging role of tetraspanins and rhomboids

Matthews, A. L., Noy, P. J., Reyat, J. S., & Tomlinson, M. G. (2016) · Platelets · doi:10.1080/09537104.2016.1184751 · Cited by 122

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

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 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

Activation of cell-surface proteases promotes necroptosis, inflammation and cell migration

Cai, Z., Zhang, A., Choksi, S., Li, W., Li, T., Zhang, X.-M., & Liu, Z.-G. (2016) · Cell Research · doi:10.1038/cr.2016.87 · Cited by 103

Intratumoral fate of functional nanoparticles in response to microenvironment factor: Implications on cancer diagnosis and therapy

Peng, J., Yang, Q., Shi, K., Xiao, Y., Wei, X., & Qian, Z. (2019) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2019.06.007 · Cited by 105

Harnessing the antitumor potential of macrophages for cancer immunotherapy

Long, K. B., & Beatty, G. L. (2013) · OncoImmunology · doi:10.4161/onci.26860 · Cited by 103

Matrix Metalloproteinases in Non-Neoplastic Disorders

Tokito, A., & Jougasaki, M. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17071178 · Cited by 98

Polysialylation and lipopolysaccharide‐induced shedding of E‐selectin ligand‐1 and neuropilin‐2 by microglia and THP‐1 macrophages

Werneburg, S., Buettner, F. F. R., Erben, L., Mathews, M., Neumann, H., Mühlenhoff, M., & Hildebrandt, H. (2016) · Glia · doi:10.1002/glia.23004 · Cited by 91

Roles of Matrix Metalloproteinases and Their Natural Inhibitors in Metabolism: Insights into Health and Disease

Molière, S., Jaulin, A., Tomasetto, C., & Dali‐Youcef, N. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241310649 · Cited by 98

Matrix metalloproteinases: Expression, regulation and role in the immunopathology of tuberculosis

Sabir, N., Hussain, T. A., Mangi, M. H., Zhao, D., & Zhou, X. (2019) · Cell Proliferation · doi:10.1111/cpr.12649 · Cited by 100

A novel regulation of PD-1 ligands on mesenchymal stromal cells through MMP-mediated proteolytic cleavage

Dezutter‐Dambuyant, C., Durand, I., Alberti, L., Bendriss‐Vermare, N., Valladeau‐Guilemond, J., Duc, A., Magron, A., Morel, A., Sisirak, V., Rodriguez, C., et al. (2015) · OncoImmunology · doi:10.1080/2162402x.2015.1091146 · Cited by 96

Antifibrotic, Antioxidant, and Immunomodulatory Effects of Mesenchymal Stem Cells in HOCl‐Induced Systemic Sclerosis

Maria, A. T. J., Toupet, K., Bony, C., Pirot, N., Vozenin, M., Petit, B., Roger, P., Batteux, F., Quellec, A. L., Jørgensen, C., et al. (2015) · Arthritis & Rheumatology · doi:10.1002/art.39477 · Cited by 90

Matrix metalloproteinase-9 activity and a downregulated Hedgehog pathway impair blood-brain barrier function in an in vitro model of CNS tuberculosis

Brilha, S., Ong, C. W. M., Weksler, B. B., Romero, N., Couraud, P., & Friedland, J. S. (2017) · Scientific Reports · doi:10.1038/s41598-017-16250-3 · Cited by 86

Innate immune system and tissue regeneration in planarians: An area ripe for exploration

Peiris, T. H., Hoyer, K. K., & Oviedo, N. J. (2014) · Seminars in Immunology · doi:10.1016/j.smim.2014.06.005 · Cited by 93

Matrix metalloproteinases and inhibitors in dentistry

Boelen, G., Boute, L., d’Hoop, J., EzEldeen, M., Lambrichts, I., & Opdenakker, G. (2019) · Clinical Oral Investigations · doi:10.1007/s00784-019-02915-y · Cited by 89

Augmented Th17 differentiation in Trim21 deficiency promotes a stable phenotype of atherosclerotic plaques with high collagen content

Brauner, S., Jiang, X., Thorlacius, G. E., Lundberg, A. M., Östberg, T., Yan, Z.-Q., Kuchroo, V. K., Hansson, G. K., & Wahren‐Herlenius, M. (2017) · Cardiovascular Research · doi:10.1093/cvr/cvx181 · Cited by 86

Matrix Metalloproteases as Influencers of the Cells’ Social Media

Young, D. W., Das, N., Anowai, A., & Dufour, A. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20163847 · Cited by 86

Transcriptome of American Oysters, Crassostrea virginica, in Response to Bacterial Challenge: Insights into Potential Mechanisms of Disease Resistance

McDowell, I. C., Nikapitiya, C., Aguiar, D., Lane, C. E., Istrail, S., & Marta Gómez-chiarri, G. (2014) · PLoS ONE · doi:10.1371/journal.pone.0105097 · Cited by 87

Metalloproteinases and their roles in human cancer

Roy, R., Morad, G., Jedinak, A., & Moses, M. A. (2019) · The Anatomical Record · doi:10.1002/ar.24188 · Cited by 84

Matrix metalloproteinase contribution in management of cancer proliferation, metastasis and drug targeting

Abdel‐Hamid, N. M., & Abass, S. A. (2021) · Molecular Biology Reports · doi:10.1007/s11033-021-06635-z · Cited by 86

Matrix Metalloproteinase-19 Promotes Metastatic Behavior In Vitro and is Associated with Increased Mortality in Non–Small Cell Lung Cancer

Yu, G., Herazo‐Maya, J. D., Nukui, T., Romkes, M., Parwani, A. V., Juan-Guardela, B. M., Robertson, J. V., Gauldie, J., Siegfried, J. M., Kaminski, N., et al. (2014) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.201310-1903oc · Cited by 85

Mechanisms of receptor shedding in platelets

Montague, S. J., Andrews, R. K., & Gardiner, E. E. (2018) · Blood · doi:10.1182/blood-2018-03-742668 · Cited by 82

Type-1 cytokines regulate MMP-9 production and E-cadherin disruption to promote melanocyte loss in vitiligo

Boukhedouni, N., Martins, C. P., Darrigade, A. ‐., Drullion, C., Rambert, J., Barrault, C., Garnier, J., Jacquemin, C., Thiolat, D., Lucchese, F., et al. (2020) · JCI Insight · doi:10.1172/jci.insight.133772 · Cited by 82

Matrix metalloproteinases in impaired wound healing

Keller, U. A. D., & Sabino, F. (2015) · Metalloproteinases In Medicine · doi:10.2147/mnm.s68420 · Cited by 85

Next-Generation Sequencing Reveals Low-Dose Effects of Cationic Dendrimers in Primary Human Bronchial Epithelial Cells

Feliu, N., Kohonen, P. J., Ji, J., Zhang, Y., Karlsson, H. L., Palmberg, L., Nyström, A. M., & Fadeel, B. (2014) · ACS Nano · doi:10.1021/nn5061783 · Cited by 79

Immunomodulatory roles of metalloproteinases in rheumatoid arthritis

Bian, Y., Xiang, Z., Wang, Y., Ren, Q., Chen, G., Xiang, B., Wang, J., Zhang, C., Pei, S., Guo, S., et al. (2023) · Frontiers in Pharmacology · doi:10.3389/fphar.2023.1285455 · Cited by 88

Matrix Metalloproteinases and Protein Tyrosine Kinases

Aschner, Y., Zemans, R. L., Yamashita, C. M., & Downey, G. P. (2014) · CHEST Journal · doi:10.1378/chest.14-0397 · Cited by 76

Matrix metalloproteinase inhibitors enhance the efficacy of frontline drugs against Mycobacterium tuberculosis

Xu, Y., Wang, L., Zimmerman, M. D., Chen, K., Huang, L., Fu, D., Kaya, F., Rakhilin, N., Nazarova, E. V., Bu, P., et al. (2018) · PLoS Pathogens · doi:10.1371/journal.ppat.1006974 · Cited by 75

ADAM Proteases and Gastrointestinal Function

Jones, J. C., Rustagi, S., & Dempsey, P. J. (2015) · Annual Review of Physiology · doi:10.1146/annurev-physiol-021014-071720 · Cited by 77

Salvianolic acid A attenuates ischemia reperfusion induced rat brain damage by protecting the blood brain barrier through MMP-9 inhibition and anti-inflammation

Zhang, W., Jun-Ke, S. O. N. G., Zhang, X., Zhou, Q., He, G., Xu, X., Rong, Y., Zhou, W., & Du, G. (2018) · Chinese Journal of Natural Medicines · doi:10.1016/s1875-5364(18)30046-3 · Cited by 74

TGFβ-induced switch from adipogenic to osteogenic differentiation of human mesenchymal stem cells: identification of drug targets for prevention of fat cell differentiation

van Zoelen, E. J. J., Duarte, I., Hendriks, J. M. A., & van der Woning, S. P. (2016) · Stem Cell Research & Therapy · doi:10.1186/s13287-016-0375-3 · Cited by 72

A novel indomethacin/methotrexate/MMP-9 siRNA in situ hydrogel with dual effects of anti-inflammatory activity and reversal of cartilage disruption for the synergistic treatment of rheumatoid arthritis

Yin, N., Tan, X., Liu, H., He, F., Ding, N., Gou, J., Yin, T., He, H., Zhang, Y. X., & Tang, X. (2020) · Nanoscale · doi:10.1039/d0nr00454e · Cited by 71

Functional peptide-based drug delivery systems

Lian, Z., & Ji, T. (2020) · Journal of Materials Chemistry B · doi:10.1039/d0tb00713g · Cited by 71

Scissor sisters: regulation of ADAM10 by the TspanC8 tetraspanins

Matthews, A. L., Szyroka, J., Collier, R., Noy, P. J., & Tomlinson, M. G. (2017) · Biochemical Society Transactions · doi:10.1042/bst20160290 · 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

Molecular pathogenesis of genetic and sporadic aortic aneurysms and dissections

Shen, Y. H., & LeMaire, S. A. (2017) · Current Problems in Surgery · doi:10.1067/j.cpsurg.2017.01.001 · Cited by 72

The human brain NGF metabolic pathway is impaired in the pre-clinical and clinical continuum of Alzheimers disease

Pentz, R., Iulita, M. F., Ducatenzeiler, A., Bennett, D. A., & Cuello, A. C. (2021) · Molecular Psychiatry · doi:10.1038/s41380-020-0797-2 · Cited by 68

Mechanistic insights into a TIMP3-sensitive pathway constitutively engaged in the regulation of cerebral hemodynamics

Capone, C., Dabertrand, F., Baron‐Menguy, C., Chalaris, A., Ghezali, L., Domenga, V., Schmidt, S., Huneau, C., Rose‐John, S., Nelson, M. T., et al. (2016) · eLife · doi:10.7554/elife.17536 · Cited by 72

Genetic Polymorphisms and Sepsis in Premature Neonates

Esposito, S., Zampiero, A., Pugni, L., Tabano, S. M., Pelucchi, C., Ghirardi, B., Terranova, L., Miozzo, M. R., Mosca, F., & Principi, N. (2014) · PLoS ONE · doi:10.1371/journal.pone.0101248 · Cited by 67

Activity and components of the granulocyte colony‐stimulating factor pathway in hidradenitis suppurativa*

Wolk, K., Brembach, T.-C., Šimaitė, D., Bartnik, E., Cucinotta, S., Pokrywka, A., Irmer, M. L., Triebus, J., Witte‐Händel, E., Salinas, G., et al. (2021) · British Journal of Dermatology · doi:10.1111/bjd.19795 · Cited by 66

Research Progress on the Pathogenesis of Aortic Dissection

Yin, Z., Han, H., Yan, X., & Zheng, Q. (2022) · Current Problems in Cardiology · doi:10.1016/j.cpcardiol.2022.101249 · Cited by 66

Endothelial Glycocalyx Turnover in Vascular Health and Disease: Rethinking Endothelial Dysfunction

Toledo, A. G., Golden, G. J., Cummings, R. D., Malmström, J. A., & Esko, J. D. (2025) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-032620-104745 · Cited by 71

ADAM17 controls IL‐6 signaling by cleavage of the murine IL‐6Rα from the cell surface of leukocytes during inflammatory responses

Yan, I., Schwarz, J., Lücke, K., Schumacher, N., Schumacher, V., Schmidt, S., Rabe, B., Saftig, P., Donners, M., Rose-John, S., et al. (2016) · Journal of Leukocyte Biology · doi:10.1189/jlb.3a0515-207r · Cited by 67

Semaphorin 4D inhibits neutrophil activation and is involved in the pathogenesis of neutrophil-mediated autoimmune vasculitis

Nishide, M., Nojima, S., Ito, D., Takamatsu, H., Koyama, S., Kang, S., Kimura, T., Morimoto, K., Hosokawa, T., Hayama, Y., et al. (2017) · Annals of the Rheumatic Diseases · doi:10.1136/annrheumdis-2016-210706 · Cited by 66

Ectodomain Shedding by ADAM17: Its Role in Neutrophil Recruitment and the Impairment of This Process during Sepsis

Mishra, H. K., Ma, J., & Walcheck, B. K. (2017) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2017.00138 · Cited by 66

Matrix metalloproteinases as modulators of inflammation and innate immunity

Parks, W. C., Wilson, C. L., & López-Boado, Y. S. (2004) · Nature Reviews Immunology · doi:10.1038/nri1418 · Cited by 1,929

Metalloproteinases and their inhibitors in matrix remodeling

Matrisian, L. M. (1990) · Trends in Genetics · doi:10.1016/0168-9525(90)90126-q · Cited by 1,626

Metalloproteinases: a Functional Pathway for Myeloid Cells

Chou, J., Chan, M. F., & Werb, Z. (2016) · Microbiology Spectrum · doi:10.1128/microbiolspec.mchd-0002-2015 · Cited by 35

Metalloproteinases and Their Inhibitors: Potential for the Development of New Therapeutics

Raeeszadeh‐Sarmazdeh, M., Do, L., & Hritz, B. (2020) · Cells · doi:10.3390/cells9051313 · Cited by 341

Tissue inhibitors of metalloproteinases

Murphy, G. (2011) · Genome biology · doi:10.1186/gb-2011-12-11-233 · Cited by 472