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

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

Targeted disruption of the mouse transforming growth factor-β1 gene results in multifocal inflammatory disease

Shull, M. M., Ormsby, I., Kier, A. B., Pawlowski, S., Diebold, R. J., Yin, M., Allen, R., Sidman, C., Proetzel, G., Calvin, D., et al. (1992) · Nature · doi:10.1038/359693a0 · Cited by 2,985

Matrix metalloproteinase-9 triggers the angiogenic switch during carcinogenesis

Bergers, G., Brekken, R., McMahon, G., Vu, T. H., Itoh, T., Tamaki, K., Tanzawa, K., Thorpe, P., Itohara, S., Werb, Z., et al. (2000) · Nature Cell Biology · doi:10.1038/35036374 · Cited by 2,797

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

Matrix Metalloproteinase-2 (MMP-2) Gene Deletion Enhances MMP-9 Activity, Impairs PARP-1 Degradation, and Exacerbates Hepatic Ischemia and Reperfusion Injury in Mice

Kato, H., Duarte, S. M., Liu, D., Busuttil, R. W., & Coito, A. J. (2015) · PLoS ONE · doi:10.1371/journal.pone.0137642 · Cited by 30

A novel immunomodulatory function of neutrophils on rhinovirus-activated monocytes in vitro

Tang, F., Hansbro, P. M., Burgess, J. K., Ammit, A. J., Baines, K. J., & Oliver, B. G. G. (2016) · Thorax · doi:10.1136/thoraxjnl-2015-207781 · Cited by 29

Effects of exercise training on renal interstitial fibrosis and renin–angiotensin system in rats with chronic renal failure

Yamakoshi, S., Nakamura, T., Mori, N., Suda, C., Kohzuki, M., & Ito, O. (2020) · Journal of Hypertension · doi:10.1097/hjh.0000000000002605 · Cited by 30

SAR studies of non-zinc-chelating MMP-13 inhibitors: Improving selectivity and metabolic stability

Gao, D. A., Xiong, Z., Heim‐Riether, A., Amodeo, L., August, E. M., Cao, X., Ciccarelli, L., Collins, B., Harrington, K. E., Haverty, K., et al. (2010) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2010.07.036 · Cited by 30

Liver immunolocalization and plasma levels of MMP-9 in non-alcoholic steatohepatitis (NASH) and hepatitis C infection

D’Amico, F., Consolo, M., Amoroso, A., Skarmoutsou, E., Mauceri, B., Stivala, F., Malaponte, G., Bertino, G., Neri, S., & Mazzarino, M. C. (2009) · Acta Histochemica · doi:10.1016/j.acthis.2009.05.005 · Cited by 30

Role of matrix metalloproteinases 2 and 9 in ex vivo Trypanosoma cruzi infection of human placental chorionic villi

Castillo, C., López‐Muñoz, R., Duaso, J., Galanti, N., Jaña, F., Ferreira, J., Cabrera, G., Maya, J. D., & Kemmerling, U. (2012) · Placenta · doi:10.1016/j.placenta.2012.10.004 · Cited by 30

MMP9 deficiency does not decrease blood–brain barrier disruption, but increases astrocyte MMP3 expression during viral encephalomyelitis

Savarin, C., Stohlman, S. A., Rietsch, A. M., Butchi, N. B., Ransohoff, R. M., & Bergmann, C. C. (2011) · Glia · doi:10.1002/glia.21222 · Cited by 31

Terminalia Chebulanin Attenuates Psoriatic Skin Lesion via Regulation of Heme Oxygenase-1

An, J., Li, T. X., Dong, Y., Li, Z., & Huo, J. (2016) · Cellular Physiology and Biochemistry · doi:10.1159/000445645 · Cited by 30

Exploiting biological activities of brown seaweed Ishige okamurae Yendo for potential industrial applications: a review

Sanjeewa, K. K. A., Lee, W., Kim, J., & Jeon, Y. (2017) · Journal of Applied Phycology · doi:10.1007/s10811-017-1213-4 · Cited by 30

Upregulation of matrix metalloproteinase-9/2 in the wounded tissue, dorsal root ganglia, and spinal cord is involved in the development of postoperative pain

Gu, H., Xing, F., Jiang, M., Wang, Y., Bai, L., Zhang, J., Li, T.-T., Zhang, W., & Xu, J. (2019) · Brain Research · doi:10.1016/j.brainres.2019.05.007 · Cited by 30

A neurokinin‐1 receptor antagonist that reduces intraabdominal adhesion formation increases peritoneal matrix metalloproteinase activity

Cohen, P. A., Gower, A. C., Stucchi, A. F., Leeman, S. E., Becker, J. M., & Reed, K. L. (2007) · Wound Repair and Regeneration · doi:10.1111/j.1524-475x.2007.00291.x · Cited by 30

Halogen Bonding Controls Selectivity of FRET Substrate Probes for MMP-9

Tranchant, I., Vera, L., Czarny, B., Amoura, M., Lajeunesse, E. C., Beau, F., Stura, E. A., & Dive, V. (2014) · Chemistry & Biology · doi:10.1016/j.chembiol.2014.01.008 · Cited by 30

Antiproteases as Therapeutics to Target Inflammation in Cystic Fibrosis

Quinn, D. J., Weldon, S., & Taggart, C. C. (2010) · The Open Respiratory Medicine Journal · doi:10.2174/1874306401004020020 · Cited by 30

Inhibition of matrix metalloproteinase‐9 by interferons and TGF‐β1 through distinct signalings accounts for reduced monocyte invasiveness

Nguyen, J., Knapnougel, P., Lesavre, P., & Bauvois, B. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.09.012 · Cited by 30

Extracellular Matrix and Tissue Regeneration

Konttinen, Y. T., Kaivosoja, E., Stegaev, V., Wagner, H. D., Levón, J., Tiainen, V., & Mackiewicz, Z. (2010) · Springer eBooks · doi:10.1007/978-90-481-9075-1_2 · Cited by 29

Alleviation of atopic dermatitis-related symptoms by Perilla frutescens Britton

Lee, S. (2011) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2011.763 · Cited by 29

Matrix metalloproteinases as biomarkers and therapeutic targets in colitis-associated cancer

Moura, N. S., Schledwitz, A., Alizadeh, M. A., Patil, S. A., & Raufman, J. (2024) · Frontiers in Oncology · doi:10.3389/fonc.2023.1325095 · Cited by 29

Biosimulation of acute phonotrauma: An extended model

Li‐Jessen, N. Y. K., Yoram Vodovotz, B., Kim, K. H., Mi, Q., Hebda, P. A., & Abbott, K. V. (2011) · The Laryngoscope · doi:10.1002/lary.22226 · Cited by 29

Role of N-acetylcysteine and GSH redox system on total and active MMP-2 in intestinal myofibroblasts of Crohn's disease patients

Romagnoli, C., Marcucci, T., Picariello, L., Tonelli, F., VINCENZINI, M. T., & Iantomasi, T. (2012) · International Journal of Colorectal Disease · doi:10.1007/s00384-012-1632-2 · Cited by 29

Mmp23b Promotes Liver Development and Hepatocyte Proliferation Through the Tumor Necrosis Factor Pathway in Zebrafish

Qi, F., Song, J., Yang, H., Gao, W., Liu, N., Zhang, B., & Lin, S. (2010) · Hepatology · doi:10.1002/hep.23945 · Cited by 29

Genetic association between polymorphisms in the BTG1 gene and multiple sclerosis

Camiña-Tato, M., Morcillo-Suárez, C., Navarro, A., Fernández, M., Horga, A., Montalbán, X., & Comabella, M. (2009) · Journal of Neuroimmunology · doi:10.1016/j.jneuroim.2009.05.010 · Cited by 31

ATP induced microglial cell migration through non-transcriptional activation of matrix metalloproteinase-9

Choi, M. S., Cho, K. S., Shin, S. M., Ko, H. M., Kwon, K. J., Shin, C. Y., & Ko, K. H. (2010) · Archives of Pharmacal Research · doi:10.1007/s12272-010-0211-8 · Cited by 29

The effect of gender and genetic polymorphisms on matrix metalloprotease (MMP) and tissue inhibitor (TIMP) plasma levels in different infectious and non-infectious conditions

Collazos, J., Asensi, V., Martin, G., Montes, A. H., Suárez‐Zarracina, T., & Valle-Garay, E. (2015) · Clinical & Experimental Immunology · doi:10.1111/cei.12686 · Cited by 29

Interleukin‐17A Stimulates Migration of Periodontal Ligament Fibroblasts Via p38 MAPK/NF‐κB ‐Dependent MMP‐1 Expression

Wu, Y. R., Zhu, L., Liu, L., Zhang, J., & Peng, B. (2013) · Journal of Cellular Physiology · doi:10.1002/jcp.24444 · Cited by 29

A Review of the Use of Melatonin in Ulcerative Colitis

Jena, G., & Trivedi, P. P. (2013) · Inflammatory Bowel Diseases · doi:10.1097/01.mib.0000436962.32164.6e · Cited by 31

Matrix Metalloproteinase Expression in the Rat Myometrium During Pregnancy, Term Labor, and Postpartum

Nguyen, T. T.-T. N., Shynlova, O. P., & Lye, S. J. (2016) · Biology of Reproduction · doi:10.1095/biolreprod.115.138248 · Cited by 29

The influence of surface modified poly( l -lactic acid) films on the differentiation of human monocytes into macrophages

Correia, C. R., Gaifem, J., Oliveira, M. B., Silvestre, R., & Mano, J. F. (2017) · Biomaterials Science · doi:10.1039/c6bm00920d · Cited by 29

Probiotic intervention influences the salivary levels of Matrix Metalloproteinase (MMP)-9 and Tissue Inhibitor of metalloproteinases (TIMP)-1 in healthy adults

Jäsberg, H., Tervahartiala, T. I., Sorsa, T. A., Söderling, E. M., & Haukioja, A. L. (2017) · Archives of Oral Biology · doi:10.1016/j.archoralbio.2017.10.003 · Cited by 29

Impact of Surface-Engineered ZnO Nanoparticles on Protein Corona Configuration and Their Interactions With Biological System

Srivastav, A. K., Dhiman, N., Khan, H., Srivastav, A. K., Yadav, S. K., Prakash, J., Arjaria, N., Singh, D., Yadav, S., Patnaik, S., et al. (2019) · Journal of Pharmaceutical Sciences · doi:10.1016/j.xphs.2018.12.021 · Cited by 30

Evaluation of a Recombinant Flavobacterium columnare DnaK Protein Vaccine as a Means of Protection Against Columnaris Disease in Channel Catfish (Ictalurus punctatus)

Lange, M. D., Abernathy, J. W., & Farmer, B. D. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.01175 · Cited by 29

Evaluation of cartilage damage by measuring collagen degradation products in joint extracts in a traumatic model of osteoarthritis

Nielsen, R. H., Stoop, R., Leeming, D. J., Stolina, M., Qvist, P., Christiansen, C., & Karsdal, M. A. (2008) · Biomarkers · doi:10.1080/13547500701615108 · Cited by 29

Enhanced early vascular permeability in gelatinase B (MMP-9)-deficient mice: putative contribution of COX-1-derived PGE2 of macrophage origin

Kołaczkowska, E., Ścisłowska‐Czarnecka, A., Chadzińska, M., Płytycz, B., van Rooijen, N., Opdenakker, G., & Arnold, B. (2006) · Journal of Leukocyte Biology · doi:10.1189/jlb.0106013 · Cited by 29

MMP-2, TNF-α and NLRP1 polymorphisms in Chinese patients with ankylosing spondylitis and rheumatoid arthritis

Sun, R., Huang, Y., Zhang, H., & Liu, R. (2013) · Molecular Biology Reports · doi:10.1007/s11033-013-2743-8 · Cited by 30

Matrix metalloproteinases contribute to the regulation of chemokine expression and pulmonary inflammation in Cryptococcus infection

Supasorn, O., Sringkarin, N., Srimanote, P., & Angkasekwinai, P. (2015) · Clinical & Experimental Immunology · doi:10.1111/cei.12725 · Cited by 28

Protease activity sensors noninvasively classify bacterial infections and antibiotic responses

Buss, C. G., Dudani, J. S., Akana, R., Fleming, H. E., & Bhatia, S. N. (2018) · EBioMedicine · doi:10.1016/j.ebiom.2018.11.031 · Cited by 29

Serum Matrix Metalloproteinase 7 Is a Diagnostic Biomarker of Biliary Injury and Fibrosis in Pediatric Autoimmune Liver Disease

Lam, S., Singh, R., Dillman, J. R., Trout, A. T., Serai, S. D., Sharma, D., Sheridan, R. M., Su, W., Fei, L., Karns, R. A., et al. (2020) · Hepatology Communications · doi:10.1002/hep4.1589 · Cited by 28

Impact of inflammation and immunotherapy in renal cell carcinoma (Review)

Shi, J., Wang, K., Xiong, Z., Yuan, C., Wang, C., Cao, Q., Huang, Y., Meng, X., Xie, K., Cheng, Z., et al. (2020) · Oncology Letters · doi:10.3892/ol.2020.12135 · Cited by 28

Antiretroviral protease inhibitors induce features of cellular senescence that are reversible upon drug removal

Kuehnemann, C., Hughes, J. B., Desprez, P., Melov, S., Wiley, C. D., & Campisi, J. (2022) · Aging Cell · doi:10.1111/acel.13750 · Cited by 27

Novel gene expression responses in the ovine abomasal mucosa to infection with the gastric nematode Teladorsagia circumcincta

Knight, P. A., Griffith, S. E., Pemberton, A. D., Pate, J. M., Guarneri, L., Anderson, K., Talbot, R., Smith, S. E., Waddington, D., Fell, M., et al. (2011) · Veterinary Research · doi:10.1186/1297-9716-42-78 · Cited by 28

MMP Inhibitor Clinical Trials – The Past, Present, and Future

Fingleton, B. (2008) · Springer eBooks · doi:10.1007/978-0-387-69057-5_36 · Cited by 28

Tackling the EGFR in pathological tissue remodelling

Chan, H., Smith, N. J., Hannan, R. D., & Thomas, W. G. (2005) · Pulmonary Pharmacology & Therapeutics · doi:10.1016/j.pupt.2005.04.005 · Cited by 28

Therapeutic inhibition of matrix metalloproteinases for the treatment of chronic obstructive pulmonary disease (COPD)

Daheshia, M. (2005) · Current Medical Research and Opinion · doi:10.1185/030079905x41417 · Cited by 28

Matrix metalloproteinases and their inhibitors in non-neoplastic otorhinolaryngological disease

De, S., Fenton, J. E., & Jones, A. S. (2005) · The Journal of Laryngology & Otology · doi:10.1258/0022215054273269 · Cited by 28

Tissue Inhibitor of Metalloproteinase-1 Deficiency Abrogates Obliterative Airway Disease after Heterotopic Tracheal Transplantation

Chen, P., Farivar, A. S., Mulligan, M. S., & Madtes, D. K. (2005) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2005-0344oc · Cited by 28

Improving acne keloidalis nuchae with targeted ultraviolet B treatment: a prospective, randomized, split‐scalp comparison study

Okoye, G. A., Rainer, B. M., Leung, S. G., Suh, H. S., Kim, J. H., Nelson, A. M., Garza, L. A., Chien, A. L.-L., & Kang, S. (2014) · British Journal of Dermatology · doi:10.1111/bjd.13119 · Cited by 28

Factors Controlling the Role of Zn and Reactivity of Zn‐bound Cysteines in Proteins: Application to Drug Target Discovery

Lee, Y., Lin, Y., & Lim, C. (2013) · Journal of the Chinese Chemical Society · doi:10.1002/jccs.201300392 · Cited by 27

Regulation of matrix metalloproteinase‐1, ‐3, and ‐9 in Mycobacterium tuberculosis‐dependent respiratory networks by the rapamycin‐sensitive PI3K/p70 S6K cascade

Singh, S., Saraiva, L., Elkington, P. T., & Friedland, J. S. (2013) · The FASEB Journal · doi:10.1096/fj.13-235507 · Cited by 27

Silencing of WNK2 is associated with upregulation of MMP2 and JNK in gliomas

Costa, Â. M., Pinto, F., Martinho, O., Oliveira, M. J., Jordan, P., & Reis, R. M. (2014) · Oncotarget · doi:10.18632/oncotarget.2805 · Cited by 28

Gambogic Acid and Its Role in Chronic Diseases

Pandey, M. K., Karelia, D. N., & Amin, S. (2016) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-41334-1_15 · Cited by 26

Pulmonary Remodeling in Equine Asthma: What Do We Know about Mediators of Inflammation in the Horse?

Barton, A. K., & Gehlen, H. (2016) · Mediators of Inflammation · doi:10.1155/2016/5693205 · Cited by 27

Pulmonary toxicity and global gene expression changes in response to sub-chronic inhalation exposure to crystalline silica in rats

Umbright, C., Sellamuthu, R., Roberts, J. R., Young, S., Richardson, D. L., Schwegler‐Berry, D., McKinney, W., Chen, B. T., Gu, J. K., Kashon, M. L., et al. (2017) · Journal of Toxicology and Environmental Health · doi:10.1080/15287394.2017.1384773 · Cited by 27

Serum MMP-9: a novel biomarker for prediction of clinical relapse in patients with quiescent Crohn’s disease, a post hoc analysis

Yablecovitch, D., Kopylov, U., Lahat, A., Amitai, M., Klang, E., Shor, D. B., Neuman, S., Levhar, N., Fudim, E., Avidan, B., et al. (2019) · Therapeutic Advances in Gastroenterology · doi:10.1177/1756284819881590 · Cited by 27

Blood-brain barrier dysfunction significantly correlates with serum matrix metalloproteinase-7 (MMP-7) following traumatic brain injury

Nichols, P., Urriola, J., Miller, S., Bjorkman, T., Mahady, K., Vegh, V., Nasrallah, F., & Winter, C. (2021) · NeuroImage: Clinical · doi:10.1016/j.nicl.2021.102741 · Cited by 26

Extracellular matrix remodeling and inflammatory pathway in human endometrium: insights from uterine leiomyomas

Governini, L., Marrocco, C., Semplici, B., Pavone, V., Belmonte, G., Luisi, S. V., Petraglia, F., Luddi, A., & Piomboni, P. (2021) · Fertility and Sterility · doi:10.1016/j.fertnstert.2021.06.023 · Cited by 27

The 7-Hydroxyflavone attenuates chemotherapy-induced neuropathic pain by targeting inflammatory pathway

Ullah, R., Ali, G., Rasheed, A., Subhan, F., Khan, A., Halim, S. A., & Al‐Harrasi, A. (2022) · International Immunopharmacology · doi:10.1016/j.intimp.2022.108674 · Cited by 28

Metalloelastase (MMP-12) is upregulated in the gut of pediatric patients with potential celiac disease and in type 1 diabetes

Bister, V., Kolho, K., Karikoski, R., Westerholm‐Ormio, M., Savilahti, E., & Saarialho‐Kere, U. (2005) · Scandinavian Journal of Gastroenterology · doi:10.1080/00365520510023918 · Cited by 27

Matrix metalloproteinase (MMP)‐2 and MMP‐9 as inflammation markers of Trichinella spiralis and Trichinella pseudospiralis infections in mice

Bruschi, F., Bianchi, C., Fornaro, M., Naccarato, A. G., Menicagli, M., Gómez-Morales, M. Á., Pozio, E., & Pinto, B. (2014) · Parasite Immunology · doi:10.1111/pim.12138 · Cited by 27

MMP expression in rheumatoid inflammation: the rs11568818 polymorphism is associated with MMP-7 expression at an extra-articular site

Kazantseva, M., Hung, N. A., Highton, J., & Hessian, P. A. (2013) · Genes and Immunity · doi:10.1038/gene.2012.65 · Cited by 27

Comparison of matrix metalloproteinase 9 and brain natriuretic peptide as clinical biomarkers in chronic heart failure

Vorovich, E., Chuai, S., Li, M., Averna, J. F., Marwin, V. M., Wolfe, D. J., Reilly, M. P., & Cappola, T. P. (2008) · American Heart Journal · doi:10.1016/j.ahj.2008.01.007 · Cited by 27

Addressing the Inflammatory Response to Clinically Relevant Polymers by Manipulating the Host Response Using ITIM Domain-Containing Receptors

Slee, J. B., Christian, A. J., Levy, R. J., & Stachelek, S. J. (2014) · Polymers · doi:10.3390/polym6102526 · Cited by 29

Chronic inflammation in asthma: a contest of persistence vs resolution

Hove, C. L. V., Maes, T., Joos, G., & Tournoy, K. G. (2008) · Allergy · doi:10.1111/j.1398-9995.2008.01772.x · Cited by 28

Comparative analysis of septic injury-inducible genes in phylogenetically distant model organisms of regeneration and stem cell research, the planarian Schmidtea mediterranea and the cnidarian Hydra vulgaris

Altincicek, B., & Vilcinskas, A. (2008) · Frontiers in Zoology · doi:10.1186/1742-9994-5-6 · Cited by 29

Involvement of matrix metalloproteinases (MMP-2, -7, -9) and their tissue inhibitors (TIMP-2, -3) in the chicken oviduct regression and recrudescence

Leśniak-Walentyn, A., & Hrabia, A. (2016) · Cell and Tissue Research · doi:10.1007/s00441-016-2442-6 · Cited by 27

Understanding molecular mechanism of diabetic wound healing: addressing recent advancements in therapeutic managements

Porel, P., Kaur, M., Sharma, V., & Aran, K. R. (2025) · Journal of Diabetes & Metabolic Disorders · doi:10.1007/s40200-025-01588-7 · Cited by 28

Therapeutic potential of matrix metalloprotease inhibitors in neuropathic pain

Dev, R., Srivastava, P. K., Iyer, J. P., Dastidar, S. G., & Ray, A. (2010) · Expert Opinion on Investigational Drugs · doi:10.1517/13543781003643486 · Cited by 26

Omega-3 fatty acid concentrate from Dunaliella salina possesses anti-inflammatory properties including blockade of NF- κ B nuclear translocation

Chitranjali, T., Anoop Chandran, P., & Kurup, G. M. (2014) · Immunopharmacology and Immunotoxicology · doi:10.3109/08923973.2014.981639 · Cited by 26

Integrative pathway genomics of lung function and airflow obstruction

Gharib, S. A., Loth, D. W., Artigas, M. S., Birkland, T. P., Wilk, J. B., Wain, L. V., Brody, J. A., Obeidat, M., Hancock, D. B., Tang, W., et al. (2015) · Human Molecular Genetics · doi:10.1093/hmg/ddv378 · Cited by 26

Immunomodulation of endothelial differentiated mesenchymal stromal cells: impact on T and NK cells

Omar, R. E., Xiong, Y., Dostert, G., Louis, H., Gentils, M., Menu, P., Stoltz, J., Velot, É., & Decot, V. (2015) · Immunology and Cell Biology · doi:10.1038/icb.2015.94 · Cited by 26

Women report higher pain intensity at a lower level of inflammation after knee surgery compared with men

Solheim, N., Östlund, S., Gordh, T., & Rosseland, L. A. (2017) · PAIN Reports · doi:10.1097/pr9.0000000000000595 · Cited by 26

Dissecting the Role of the Extracellular Matrix in Heart Disease: Lessons from the Drosophila Genetic Model

Hughes, C. J. R., & Jacobs, J. R. (2017) · Veterinary Sciences · doi:10.3390/vetsci4020024 · Cited by 24

ERK1/ATF-2 signaling axis contributes to interleukin-1β-induced MMP-3 expression in dermal fibroblasts

Kitanaka, N., Nakano, R., Sakai, M., Kitanaka, T., Namba, S., Konno, T., Nakayama, T., & Sugiya, H. (2019) · PLoS ONE · doi:10.1371/journal.pone.0222869 · Cited by 29

Role of various imbalances centered on alveolar epithelial cell/fibroblast apoptosis imbalance in the pathogenesis of idiopathic pulmonary fibrosis

Wang, Q., Xie, Z., Wu, Q., Jin, Z., Yang, C., & Feng, J. (2021) · Chinese Medical Journal · doi:10.1097/cm9.0000000000001288 · Cited by 26

Emerging technologies provide insights on cancer extracellular matrix biology and therapeutics

Cruz‐Acuña, R., Vunjak‐Novakovic, G., Burdick, J. A., & Rustgi, A. K. (2021) · iScience · doi:10.1016/j.isci.2021.102475 · Cited by 26

Role of Matrix Metalloproteinases in Myelin Abnormalities and Mechanical Allodynia in Rodents with Diabetic Neuropathy

Deng, X., Ma, P., Wu, M., Liao, H., & Song, X. (2021) · Aging and Disease · doi:10.14336/ad.2021.0126 · Cited by 26

Genomic deciphering of sex determination and unique immune system of a potential model species rare minnow ( Gobiocypris rarus )

Hu, X., Li, H., Lin, Y., Wang, Z., Feng, H., Zhou, M., Shi, L., Cao, H., & Ren, Y. (2022) · Science Advances · doi:10.1126/sciadv.abl7253 · Cited by 27

Current knowledge on the role of extracellular vesicles in endometrial receptivity

Sui, C., Liao, Z., Bai, J., Hu, D., Yue, J., & Yang, S. (2023) · European journal of medical research · doi:10.1186/s40001-023-01459-y · Cited by 29

PPARγ and Proline Oxidase in Cancer

Phang, J. M., Pandhare, J., Zabirnyk, O., & Liu, Y. (2008) · PPAR Research · doi:10.1155/2008/542694 · Cited by 26

Altered apoptosis of inflammatory neutrophils in MMP-9-deficient mice is due to lower expression and activity of caspase-3

Kołaczkowska, E., Kozioł, A., Płytycz, B., Arnold, B., & Opdenakker, G. (2009) · Immunology Letters · doi:10.1016/j.imlet.2009.08.002 · Cited by 26

Cp G inclusion in feed reduces sea lice, L epeophtheirus salmonis, numbers following re‐infection

Purcell, S. L., Friend, S. E., Covello, J. M., Donkin, A. W., Groman, D. B., Poley, J. D., & Fast, M. D. (2012) · Journal of Fish Diseases · doi:10.1111/jfd.12024 · Cited by 26

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