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

Etiopathogenetic factors of wound healing in chronic post-intubation cicatricial stenosis of the larynx and trachea

Валерьевич, В. В., Kuznetsova, D. A., Нажмудинов, И. И., & Давудов, Х. Ш. (2020) · Russian Bulletin of Otorhinolaryngology · doi:10.17116/otorino20208502178 · Cited by 5

Gene expression profile in newborn rat lungs after two days of recovery of mechanical ventilation

Dénervaud, V., Gremlich, S., Trummer‐Menzi, E., Schittny, J. C., & Roth‐Kleiner, M. (2015) · Pediatric Research · doi:10.1038/pr.2015.155 · Cited by 5

The protease systems and their pathogenic role in juvenile idiopathic arthritis

Margheri, F., Laurenzana, A., Giani, T., Maggi, L., Cosmi, L., Annunziato, F., Cimaz, R., & Rosso, M. D. (2019) · Autoimmunity Reviews · doi:10.1016/j.autrev.2019.06.010 · Cited by 5

Extracellular Matrix: Immunity and Inflammation

Cataldi, A., & di Giacomo, V. (2018) · Stem cell biology and regenerative medicine · doi:10.1007/978-3-319-77023-9_4 · Cited by 5

Understanding and treating intrauterine adhesions: Insights into molecular mechanisms and innovative therapies

Gou, D., Cai, X., He, H., & Chi, Y. (2025) · International Journal of Gynecology & Obstetrics · doi:10.1002/ijgo.70755 · Cited by 7

MMP3 overexpression enhances CAR-T cell infiltration and antitumor activity in a CAF-enriched solid tumor model

Zhu, Y., Jiaxin, T., Li, S. X., Xiao, B., Zhou, X., Teng, X., Zhang, G., Xie, H., Sun, K., Li, X., et al. (2026) · Journal for ImmunoTherapy of Cancer · doi:10.1136/jitc-2025-013211 · Cited by 4

Exploring causal correlations of inflammatory biomarkers in idiopathic normal-pressure hydrocephalus: insights from bidirectional Mendelian randomization analysis

Lu, J., Wang, X., Xu, F., Rao, C., Guo, Y., Su, Z., Chen, S., & Li, Q. (2024) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2024.1412434 · Cited by 4

Fibrosis regression is induced by AdhMMP8 in a murine model of chronic kidney injury

Contreras-Salinas, H., Meza-Ríos, A., Garcia-Bañuelos, J. J., Sandoval-Rodriguez, A. S., Sánchez-Orozco, L. V., García‐Benavides, L., la Rosa-Bibiano, R. D., Monroy-Ramírez, H. C., Gutiérrez‐Cuevas, J., Santos, A., et al. (2020) · PLoS ONE · doi:10.1371/journal.pone.0243307 · Cited by 4

Abnormal B-cell development in TIMP-deficient bone marrow

Weiss, A., Saw, S., Aiken, A., Aliar, K., Shao, Y. W., Fang, H., Narala, S., Shetty, R. K., Waterhouse, P. D., & Khokha, R. (2021) · Blood Advances · doi:10.1182/bloodadvances.2020004101 · Cited by 4

AdhMMP8 Vector Administration in Muscle: An Alternate Strategy to Regress Hepatic Fibrosis

Garcia-Bañuelos, J. J., Oceguera-Contreras, E., Sandoval-Rodriguez, A. S., Bastidas‐Ramírez, B. E., Lucano‐Landeros, S., Gordillo‐Bastidas, D., Gómez‐Meda, B. C., Santos, A., Reyes, E. C., & Armendáriz‐Borunda, J. (2023) · Cells · doi:10.3390/cells12172127 · Cited by 4

Snake Venom Metalloproteinases

Fox, J. W., & Gutiérrez, J. M. (2017) · MDPI eBooks · doi:10.3390/books978-3-03842-427-7 · Cited by 40

Human pluripotent stem cell-derived skin organoids enabled pathophysiological model of Mycobacterium tuberculosis infection

Yue, L., Liang, Y., Zhong, P., Fang, L., Yun, Z., Su, Q., Li, C., Xiang, M., Zhang, J., Wang, J., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-65848-z · Cited by 4

An Overview of Major Clinical Predictive Factors and Prognostic Biomarkers of Diabetic Kidney Disease in Children and Adolescents

Gosai, S. A., Qadree, A. K., Singh, A. P., Chavan, M., & Oso, B. I. (2023) · Clinical Medicine And Health Research Journal · doi:10.18535/cmhrj.v3i3.170 · Cited by 3

Matrix metalloproteases

Trabocchi, A., & Lenci, E. (2023) · Elsevier eBooks · doi:10.1016/b978-0-12-823974-2.00033-4 · Cited by 3

Gallbladder cancer-associated genetic variants rs1003349 and rs1004030 regulate MMP14 expression by altering SOX10- and MYB-binding sites

Vinay, J., Palo, A., Besra, K., & Dixit, M. (2023) · Human Molecular Genetics · doi:10.1093/hmg/ddad077 · Cited by 3

Bioinformatics analysis of MMP14+ myeloid cells affecting endothelial-mesenchymal transformation and immune microenvironment in glioma

Luo, W., Quan, Q., Xu, Z., Lei, J.-J., & Peng, R. (2024) · Heliyon · doi:10.1016/j.heliyon.2024.e26859 · Cited by 4

Effects of the nerve growth factor and its carrier protein on the inflammatory response from human monocytes

Verrès, Y., Bodin, A., Chevret, S., Victoni, T., Gicquel, T., Barreto, E., Freund‐Michel, V., & Lagente, V. (2024) · Fundamental and Clinical Pharmacology · doi:10.1111/fcp.13006 · Cited by 3

Potential Roles of Matrix Metalloproteinases in Malignant Mesothelioma

Ying, S., Wang, Y., & Lyu, L. (2020) · IntechOpen eBooks · doi:10.5772/intechopen.88783 · Cited by 3

Polymorphisms of the Matrix Metalloproteinase Genes are Associated with Acute Ischemic Stroke in Chinese Han Population

Li, A., Han, T., Li, Y., Yang, G., Zhang, Y., Huang, Y., Zhou, B., Song, G., & He, Y. (2023) · International Journal of General Medicine · doi:10.2147/ijgm.s395416 · Cited by 3

Noninvasive Detection and Imaging of Matrix Metalloproteinases for Cancer Diagnosis

Hong, J., Chen, Y., Shen, J., & Ding, Y. (2017) · Journal of Analysis and Testing · doi:10.1007/s41664-017-0036-2 · Cited by 3

RNA-sequencing transcriptomic analysis of scrapie-exposed ovine mesenchymal stem cells

Hernaiz, A., Marín, B., Vázquez, F. J., Badiola, J. J., Zaragoza, P., Bolea, R., & Martín‐Burriel, I. (2024) · Research in Veterinary Science · doi:10.1016/j.rvsc.2024.105423 · Cited by 2

Neutrophils in BCR::ABL1 negative MPN: Contributors or bystanders of fibrosis?

Vermeersch, G., Gouwy, M., Proost, P., Struyf, S., & Devos, T. (2025) · Blood Reviews · doi:10.1016/j.blre.2025.101285 · Cited by 3

Relevant biomarkers in acute graft-versus-host disease secondary to transplantation of hematopoietic stem cells

Manosalva, J.-P., Quimbaya, P., Bustos, R., Perdomo-Arciniegas, A. M., Bonilla, X., & Oliveros, H. (2025) · Hematology/Oncology and Stem Cell Therapy · doi:10.4103/hemoncstem.hemoncstem-d-24-00003 · Cited by 2

Combined effects of glutamine dipeptide, plant essential oils, and Astragalus polysaccharide on growth performance, antioxidant capacity, immune function, and intestinal health in large yellow croaker (Larimichthys crocea)

Zhu, X., Zhan, Y., Chen, Y., Hang, Y., Wang, C., Mi, S., Zhang, J., Sun, M., Yuan, L., Lin, M., et al. (2025) · Aquaculture Reports · doi:10.1016/j.aqrep.2025.103283 · Cited by 2

Emerging functionalized artificial periostea: Diverse origins, multifaceted roles and therapeutic frontiers

Luo, Y., Jiang, W., Wu, H., Zhao, C., Wei, H., & Wang, X. (2026) · Biomaterials · doi:10.1016/j.biomaterials.2026.124066 · Cited by 2

Ancient and Emerging Nanostructures for Innovations to Fight Head and Neck Cancer

Kummer, N., Acet, Ö., Acet, B. Ö., Blueggel, M., Khamis, A., Gül, D., Knauer, S. K., & Stauber, R. H. (2026) · Cells · doi:10.3390/cells15040339 · Cited by 3

Novel Plasma Proteomic Markers and Risk of Venous Thromboembolism

Tang, W., Li, A., Austin, T. R., Brækkan, S. K., Nøst, T. H., Li, X., Deo, R., Dubin, R. F., Ganz, P., Guan, W., et al. (2026) · Circulation · doi:10.1161/circulationaha.125.074493 · Cited by 3

Coral larvae have unique transcriptomic responses to pathogenic and probiotic bacteria

Borbee, E., Changsut, I., Bernabe, K., Schickle, A., Nelson, D. C., Sharp, K., & Fuess, L. (2026) · Coral reefs · doi:10.1007/s00338-026-02830-1 · Cited by 1

Morphofunctional features of the cardiovascular system in extreme specialists of the navy (depending on the polymorphism of the genes of the matrix metalloprotheinase 1 (MMP-1) and collagen 1 (COL1A1)

Nikashin, A. N., Cherkashin, D. V., Andrianov, V. P., & Fisun, A. Y. (2020) · Translational Medicine · doi:10.18705/2311-4495-2020-7-4-32-43 · Cited by 2

Spatially Resolved Tagging of Proteolytic Neo-N termini with Subtiligase-TM

Weeks, A. M. (2021) · The Journal of Membrane Biology · doi:10.1007/s00232-021-00171-4 · Cited by 2

CD11b-Based Pre-Targeted SPECT/CT Imaging Allows for the Detection of Inflammation in Aortic Aneurysm

Zhou, X., Zhu, K., Zhang, Y., Yang, M., Shi, D., Tan, H., Xiang, B., Zhu, S., Cheng, D., Lai, H., et al. (2022) · Journal of Inflammation Research · doi:10.2147/jir.s350593 · Cited by 2

Assessment of tissue expression of matrix metalloproteinase-9 level in patients with vitiligo and its relation to disease pattern, activity, and severity

Mohammed, S. M., Eyada, M., Elokda, M., & Mohammed, G. F. (2022) · Egyptian Journal of Dermatology and Venerology · doi:10.4103/ejdv.ejdv_37_21 · Cited by 2

Chronic respiratory failure correction in cicatricial laryngeal and tracheal stenosis using helium-oxygen mixture

Анатольевна, К. Е., Frolkina, E. A., Rybalchenko, I. E., & Tyutina, S. I. (2022) · Russian Bulletin of Otorhinolaryngology · doi:10.17116/otorino20228704163 · Cited by 2

Effects of Kojic Acid-mediated Sonodynamic Therapy as a Matrix Metalloprotease-9 Inhibitor against Oral Squamous Cell Carcinoma: A Bioinformatics Screening and In Vitro Analysis

Pourhajibagher, M., Alaeddini, M., Etemad‐Moghadam, S., Parker, S. P. A., & Bahador, A. (2023) · Current Drug Discovery Technologies · doi:10.2174/0115701638266082231124055825 · Cited by 2

Discovery of TP0628103: A Highly Potent and Selective MMP-7 Inhibitor with Reduced OATP-Mediated Clearance Designed by Shifting Isoelectric Points

Oka, Y., Abe-Sato, K., Tabuse, H., Yasukawa, Y., Yahara, T., Nishimoto, T., Kamitani, M., Fukunaga, T., Ochiai, N., Abe-Kumasaka, T., et al. (2024) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.3c01967 · Cited by 2

Distinct structural basis and catalytic classification of matrix metalloproteinases and their endogenous tissue inhibitors with glycosylation issue in cellular and tissue regulation

Kim, H.-D., Choi, H., Park, J.-Y., & Kim, C. (2025) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2025.110436 · Cited by 2

LEKTI, A Physiological Inhibitor of Multiple Serine Proteinases, Suppresses Perineural and Lymphovascular Invasion of Human Head and Neck Cancer Cells in A Mouse Orthotopic Model

Jayakumar, A. (2014) · MOJ Proteomics & Bioinformatics · doi:10.15406/mojpb.2014.01.00029 · Cited by 2

Evolving Perspectives in Orthobiologic Approaches to Articular Cartilage Regeneration

Brambilla, L., Scotti, C., Gobbi, A. W., & Peretti, G. M. (2017) · Springer eBooks · doi:10.1007/978-3-662-54181-4_50 · Cited by 2

Polarized Membrane Trafficking in Development and Disease

Linklater, E. S., Jewett, C. E., & Prekeris, R. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-802438-6.00005-x · Cited by 2

Structural and Functional Properties of the Extracellular Matrix

CENAN, R. S., Ergin, E., Ekici, Y., & Ataç, F. B. (2018) · Journal of Literature Pharmacy Sciences · doi:10.5336/pharmsci.2018-60599 · Cited by 2

DAMP-Promoted Efferent Innate Immune Responses in Human Diseases: Fibrosis

Land, W. G. (2020) · Springer eBooks · doi:10.1007/978-3-030-53868-2_6 · Cited by 2

Predictors of Pulmonary Cavitation among Tuberculosis Patients

Balogun, O. O., Fawole, A., Osemwinyen, E., & Busola, B. (2021) · Journal of Infectious Diseases and Epidemiology · doi:10.23937/2474-3658/1510231 · Cited by 2

Effect of the p38 MAPK Inhibitor on the Expression of Metalloproteinases and Their Inhibitors during the Formation of Abdominal Adhesions

Александровна, Ш. И., Родионова, Л. В., Ayushinova, N., Чепурных, Е., Сергеевна, Т. И., & Шурыгин, М. Г. (2021) · International Journal of Biomedicine · doi:10.21103/article11(4)_oa9 · Cited by 2

Human Polyomaviruses and Papillomaviruses

Moens, U. L. (2018) · MDPI eBooks · doi:10.3390/books978-3-03897-221-1 · Cited by 2

Hyaluronic acid suppresses the effect of di-(2-ethylhexyl) phthalate in HaCaT keratinocytes

Kim, J. H. (2022) · Molecular & Cellular Toxicology · doi:10.1007/s13273-022-00227-z · Cited by 2

Biological Activity and Implications of the Metalloproteinases in Diabetic Foot Ulcers

la Rosa, C. C.-D., Veloz, I. G., Cardenas‐Vargas, E., Castañeda-Miranda, R., Solís-Sánchez, L. O., Ortiz-Rodriguez, J. M., Vega-Carrillo, H. R., Martínez-Blanco, M. D. R., Flores‐Morales, V., Hernandez-Delgadillo, G. P., et al. (2017) · InTech eBooks · doi:10.5772/intechopen.71725 · Cited by 2

Analysis of CERK1 ectodomain shedding and the role of XLG2 in cerk1-4 cell death execution

Meusel, C. (2016) · doi:10.53846/goediss-5647 · Cited by 2

Matrix Metalloproteinases

Swarnakar, S., & Jana, S. (2017) · Springer eBooks · doi:10.1007/978-3-319-67199-4_101814 · Cited by 2

Macrophage Metalloprotease (MMP)-12 as a Cardiovascular Biomarker

Porto, F. D., Cifani, N., Ferri, L., Proietta, M., Tritapepe, L., Gioia, C. R. T. D., & Taurino, M. (2016) · Springer eBooks · doi:10.1007/978-94-007-7678-4_29 · Cited by 1

Myocardial Tissue Repair and Regeneration

Wang, K., Wang, S., Miao, Y., Lu, Y., Zheng, H., Deng, K., Song, L., Li, S., Zhu, Y., & Gao, C. (2023) · Springer eBooks · doi:10.1007/978-981-99-6948-7_12 · Cited by 1

The level of serum matrix metalloproteinase-1 and tissue inhibitor of matrix metalloproteinase-1 in newborns from mothers with undifferentiated connective tissue dysplasia

Chumak, O. Y., & Volokha, A. P. (2024) · Ukrainian journal of Perinatology and Pediatrics · doi:10.15574/pp.2024.97.64 · Cited by 1

Decoding the gut microbiota metabolite–matrix metalloproteinase-3 axis in breast cancer: a multi-omics and network pharmacology study

Yuan, T., Xing, J., & Liu, P. (2025) · Molecular Diversity · doi:10.1007/s11030-025-11351-y · Cited by 1

Association of MMP7 (−181A > G) promoter polymorphism with endometriosis in Eastern Indian women

Chatterjee, K., Jana, S., DasMahapatra, P., & Swarnakar, S. (2025) · Journal of Endometriosis and Pelvic Pain Disorders · doi:10.1177/22840265251377971 · Cited by 1

Insulin modulates MMP-2 and 9 activities through the control of oxidative stress in the heart of diabetic rats

Martins, B. T., de Deus, I. J., Gutierres, V. V., Souza, M. V., da Silva, T. C. A., Fagundes, M. M. D. A., das Mercês, A. C., de Lima, W. G., Ceron, C. S., & Paula-Gomes, S. (2025) · Canadian Journal of Physiology and Pharmacology · doi:10.1139/cjpp-2025-0037 · Cited by 1

Metalloproteinase imbalance in HIV-1: Subtype comparison in CSF and serum

de Almeida, S. M., Rotta, I., Liao, A., Tang, B., Vaida, F., Letendre, S. L., & Ellis, R. J. (2026) · Journal of Neuroimmunology · doi:10.1016/j.jneuroim.2026.578935 · Cited by 1

Cervical Glycosaminoglycans and Extracellular Matrix Remodeling: New Insights and the Therapeutic Promise of Tafoxiparin

Flis, W., Wartęga, M., Sowińska, J., & Socha, M. W. (2025) · Cells · doi:10.3390/cells14241934 · Cited by 1

Guidelines for the Design of Custom Affinity-Based Probes for Metalloproteases

Launay, M., Berthy, L., Rizo, S. L., Balachouti, M. A., Georgiadis, D., & Devel, L. (2026) · Methods in molecular biology · doi:10.1007/978-1-0716-5092-9_11 · Cited by 1

Blood MMP-7 and TNF-α levels as potential prognostic biomarkers for adult pulmonary Langerhans cell histiocytosis

Benattia, A., Porcher, R., Terry, S., Andrieu, M., Lorillon, G., & Tazi, A. (2026) · Scientific Reports · doi:10.1038/s41598-026-40540-4 · Cited by 1

The Potential of A Disintegrin and Metalloproteinase (ADAM) Proteins as Clinically Relevant Biomarkers in Colorectal Cancer: A Comprehensive Analysis

Romanowicz, A., Łukaszewicz‐Zając, M., & Mroczko, B. (2026) · Cancers · doi:10.3390/cancers18071127 · Cited by 1

Human immunoglobulin G suppresses the production of matrix metalloproteinase‐9 in peripheral blood mononuclear cells of patients with multiple sclerosis

Okada, K., & Adachi, H. (2015) · Clinical and Experimental Neuroimmunology · doi:10.1111/cen3.12214 · Cited by 1

Development of in-cell imaging assay systems for MMP-2 and MMP-9 based on trans-localizing molecular beacon proteins

Lee, M. J., Cho, Y., Hwang, H. J., & Kim, J. H. (2015) · Archives of Pharmacal Research · doi:10.1007/s12272-014-0546-7 · Cited by 1

Chemical, microbial, and host‐related factors: effects on the integrity of dentin and the dentin–biomaterial interface

Carrilho, M. T., Piveta, F., & Tjäderhane, L. (2015) · Endodontic Topics · doi:10.1111/etp.12087 · Cited by 1

PROTEOLYTIC SYSTEM CONDITION AS IN THE CASE OF NEUTROPHIL ELASTASE IN PATIENTS WITH TROPHIC ULCERS ON THE BACKGROUND OF DIABETES MELLITUS

Nikolaienko, A. S. (2020) · Eastern Ukrainian Medical Journal · doi:10.21272/eumj.2020;8(4):346-350 · Cited by 1

Metalloproteinases: a Functional Pathway for Myeloid Cells

Chou, J., Chan, M. F., & Werb, Z. (2017) · ASM Press eBooks · doi:10.1128/9781555819194.ch36 · Cited by 1

Gain of function of a metalloproteinase associated with multiple myeloma, bicuspid aortic valve, and Von Hippel–Lindau syndrome

Snipas, S. J., Jappelli, R., Torkamani, A., Paternostro, G., & Salvesen, G. S. (2022) · Biochemical Journal · doi:10.1042/bcj20220166 · Cited by 1

Regulation of Matrix Metalloproteinase-2 and Matrix Metalloproteinase-9 in Abdominal Aortic Aneurysm

Wang, S., Liu, D., Zhang, X., & Tian, X. (2023) · Cardiology Discovery · doi:10.1097/cd9.0000000000000097 · Cited by 1

Matrix gla protein, a potential marker of tissue remodelling and physiological ageing of the gut in crohn’s disease

Vieujean, S., Gillard, R., Delanaye, P., Seidel, L., Bequet, É., Salée, C., Meuwis, M., Massot, C., Pierre, N., Meunier, P., et al. (2023) · Scandinavian Journal of Gastroenterology · doi:10.1080/00365521.2023.2286913 · Cited by 2

Matrix metalloproteases as diagnostic and prognostic biomarkers in cancer

Maurya, S., Swati, K., Ghosh, M., & Yadav, P. K. (2024) · Elsevier eBooks · doi:10.1016/b978-0-443-30098-1.00013-6 · Cited by 1

The role of the enzyme systems of the organism in the development of chronic liver diseases

Прищепенко, В. А., Yupatov, G. I., & Окулич, В. К. (2018) · Russian Journal of Evidence-Based Gastroenterology · doi:10.17116/dokgastro20187235 · Cited by 1

Association of polymorphisms in the promoter regions of MMP2, MMP3 and MMP9 genes with cardiovascular risk factors in patients with rheumatoid arthritis

Omelchenko, V. O., Алексеевна, Л. Е., Shevchenko, A. V., Konenkov, V. I., Pospelova, T. I., & Korolev, M. A. (2019) · JOURNAL of SIBERIAN MEDICAL SCIENCES · doi:10.31549/2542-1174-2019-1-109-118 · Cited by 1

Immunoxpression of MMPs -9, -13 and TIMP-3 after Using Etch-and-rinse Adhesive

Costa, L. M., Rizuto, A. V., de Mendonça, L. S., Carvalho, M. D. V., da Silveira, M. M. F., & Sobral, A. P. V. (2021) · Research Society and Development · doi:10.33448/rsd-v10i9.17315 · Cited by 1

Modulation of inflammatory responses by Sutherlandia frutescens

Lei, W. (2015) · doi:10.32469/10355/50153 · Cited by 1

iRhom2 serves as a facilitator in obesity by enhancing adipose inflammation and insulin resistancePreprint

Xu, M., Ge, C., Qin, Y., Deshuai, L., Qiang, L., Feng, J., Wu, Y., Hu, L., Huang, P., & Jun, T. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/600460 · Cited by 1

Activity‐Based Probes for Profiling Protein Activities

Ruddraraju, K. V., & Zhang, Z. (2019) · doi:10.1002/9781118970195.ch4 · Cited by 1

Tissue Inhibitor of Metalloproteinase

Masciantonio, M. G., & Gill, S. E. (2017) · Springer eBooks · doi:10.1007/978-1-4614-6438-9_101950-1 · Cited by 1

Live imaging epidermal cell metabolism during inflammation: a new immunometabolic role for epidermal keratinocytes?

(2014) · Inflammation and Cell Signaling · doi:10.14800/ics.318

mAbs Targeting Apoptosis, Angiogenesis Inhibitors, and Other mAbs in Phase 1 and 2 Clinical Studies for Immunological Disorders

Brennan, F. R. (2014) · Wiley eBooks · doi:10.1002/9783527682423.ch38

MMPs: From Genomics to Degradomics

Grünwald, B. T., Schlage, P., Krüger, A., & Keller, U. A. D. (2015) · doi:10.1002/9781118772287.ch9

Secrets of the Cutaneous Basement Membrane

Kárpáti, S. (2014) · Journal of Investigative Dermatology · doi:10.1038/jid.2013.452

Hydrogen peroxide modulation of angiogenic factors in tumor cells

de Sousa, A. M. J. G. (2013) · Portuguese National Funding Agency for Science, Research and Technology (RCAAP Project by FCT)

Influence of Periostin on Synovial Fibroblasts in Knee

Yoshida, N., Yamasaki, E. M., Hisamitsu, T., & Ishikawa, S. (2015)

Expression of LEKTI Correlates With PNI and LVI In SCC of the Oral Tongue and Mechanism of LEKTI Loss in HNSCC

Jayakumar, A. (2015) · MOJ Proteomics & Bioinformatics · doi:10.15406/mojpb.2015.02.00060

Expression of CD13/Aminopeptidase N by Synovial Fibroblasts: Novel Roles in the Pathogenesis of Rheumatoid Arthritis.

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