Cited by 1,929Protease and Inhibitor MechanismsBlood Coagulation and Thrombosis MechanismsNeutrophil, Myeloperoxidase and Oxidative Mechanisms

The DOI matches its Crossref record; 148 of the 149 references it cites were found in a registry or an index.

Matrix metalloproteinases as modulators of inflammation and innate immunity

Parks, William C., Wilson, Carole L., López-Boado, Yolanda S.·2004·Nature Reviews Immunology

DOI 10.1038/nri1418

Open this paper in CoChat — free account

Integrity signals

Registry

Crossref · 10.1038/nri1418

Cites

148 of 148 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

We couldn’t retrieve this paper’s full text, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

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

Flagged first, then by citations

Show all 149 references

1 of the 149 references couldn’t be matched to a known paper.

Research works printed but not linked: 1

Hotary, K. B. et al. Matrix metalloproteinases (MMPs) regulate fibrin-invasive activity via MT1-MMP-dependent and -independent processes. J. Exp. Med. 195, 295–308 (2002). · DOI

Sorted by citations

Items 501–600 of 1,001

Ambidextrous binding of cell and membrane bilayers by soluble matrix metalloproteinase-12
Koppisetti, R. K., Fulcher, Y. G., Jurkevich, A., Prior, S. H., Xu, J., Lenoir, M., Overduin, M., & Doren, S. R. V. (2014) · Nature Communications · doi:10.1038/ncomms6552 · Cited by 55
Matrix Metalloproteinases 2 and 9 Are Differentially Expressed in Patients with Indeterminate and Cardiac Clinical Forms of Chagas Disease
Fares‐Gusmao, R., Gomes, J. D. A. S., Garzoni, L. R., Waghabi, M. C., Saraiva, R. M., Medeiros, N. I., Oliveira-Prado, R., Sangenis, L. H. C., Chambela, M. D. C., de Araújo, F. F., et al. (2013) · Infection and Immunity · doi:10.1128/iai.00153-13 · Cited by 55
Optimization of a Protease Activated Probe for Optical Surgical Navigation
Yim, J. J., Tholen, M., Klaassen, A., Sorger, J., & Bogyo, M. S. (2017) · Molecular Pharmaceutics · doi:10.1021/acs.molpharmaceut.7b00822 · Cited by 55
MMP2/MMP9-mediated CD100 shedding is crucial for inducing intrahepatic anti-HBV CD8 T cell responses and HBV clearance.
Yang, S.-Q., Wang, L., Pan, W.-M., Bayer, W., Thoens, C., Heim, K., Dittmer, U., Timm, J., Wang, Q., Yu, Q., et al. (2019) · Journal of Hepatology · doi:10.1016/j.jhep.2019.05.013 · Cited by 45
Protective Role of Matrix Metalloproteinase-9 in Ozone-Induced Airway Inflammation
Yoon, H. K., Cho, H., & Kleeberger, S. R. (2007) · Environmental Health Perspectives · doi:10.1289/ehp.10289 · Cited by 55
Collagen fragments modulate innate immunity.
Thomas, A. H., Edelman, E. R., & Stultz, C. M. (2007) · PubMed · Cited by 56
The Balance Between Metalloproteinases and TIMPs
Masciantonio, M. G., Lee, C. K. S., Arpino, V., Mehta, S., & Gill, S. E. (2017) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2017.01.001 · Cited by 56
Capturing dynamic biological signals via bio-mimicking hydrogel for precise remodeling of soft tissue
Cai, Z., Saiding, Q., Cheng, L., Zhang, L., Wang, Z., Wang, F., Chen, X., Chen, G., Deng, L., & Cui, W. (2021) · Bioactive Materials · doi:10.1016/j.bioactmat.2021.04.039 · Cited by 54
Molecular profiling of the hippocampus of children with autism spectrum disorder
Rexrode, L., Hartley, J., Showmaker, K. C., Challagundla, L., Vandewege, M. W., Martin, B. E., Blair, E., Bollavarapu, R., Antonyraj, R. B., Hilton, K., et al. (2024) · Molecular Psychiatry · doi:10.1038/s41380-024-02441-8 · Cited by 73
Quercetin and sulforaphane in combination suppress the progression of melanoma through the down-regulation of matrix metalloproteinase-9
Pradhan, S. J., Mishra, R., Sharma, P., & Kundu, G. C. (2010) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2010.144 · Cited by 55
Gelatinase B/matrix metalloproteinase-9 contributes to cellular infiltration in a murine model of zymosan peritonitis
Kołaczkowska, E., Chadzińska, M., Ścisłowska‐Czarnecka, A., Płytycz, B., Opdenakker, G., & Arnold, B. (2006) · Immunobiology · doi:10.1016/j.imbio.2005.08.004 · Cited by 54
The Significance of Matrix Metalloproteinases in Parasitic Infections Involving the Central Nervous System
Bruschi, F., & Pinto, B. (2013) · Pathogens · doi:10.3390/pathogens2010105 · Cited by 56
MMP ‐13 deletion decreases profibrogenic molecules and attenuates N ‐nitrosodimethylamine‐induced liver injury and fibrosis in mice
George, J., Tsutsumi, M., & Tsuchishima, M. (2017) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.13304 · Cited by 54
Proteoglycans as Immunomodulators of the Innate Immune Response to Lung Infection
Kang, I., Chang, M. Y., Wight, T. N., & Frevert, C. W. (2018) · Journal of Histochemistry & Cytochemistry · doi:10.1369/0022155417751880 · Cited by 53
Matrix metalloproteinases and their inhibitors in bone: an overview of regulation and functions
Varghese, S. (2006) · Frontiers in bioscience · doi:10.2741/2024 · Cited by 54
An MMP liberates the Ninjurin A ectodomain to signal a lossof cell adhesionPreprint
Zhang, S., Dailey, G. M., Kwan, E., Glasheen, B. M., Sroga, G. E., & Page, A. W. (2006) · Genes & Development · doi:10.1101/gad.1426906 · Cited by 54
Neutrophil activation signature in juvenile idiopathic arthritis indicates the presence of low-density granulocytes
Ramanathan, K., Glaser, A., Lythgoe, H., Ong, J., Beresford, M. W., Midgley, A., & Wright, H. L. (2017) · Lara D. Veeken · doi:10.1093/rheumatology/kex441 · Cited by 53
ADAM8 signaling drives neutrophil migration and ARDS severity
Conrad, C., Yildiz, D., Cleary, S. J., Margraf, A., Cook, L., Schlomann, U., Panaretou, B., Bowser, J. L., Karmouty‐Quintana, H., Li, J., et al. (2022) · JCI Insight · doi:10.1172/jci.insight.149870 · Cited by 55
A subset of anti-rotavirus antibodies directed against the viral protein VP7 predicts the onset of celiac disease and induces typical features of the disease in the intestinal epithelial cell line T84
Dolcino, M., Zanoni, G., Bason, C., Tinazzi, E., Boccola, E., Valletta, E. A., Contreas, G., Lunardi, C., & Puccetti, A. (2013) · Immunologic Research · doi:10.1007/s12026-013-8420-0 · Cited by 53
Persistent Helicobacter pylori Specific Th17 Responses in Patients with Past H. pylori Infection Are Associated with Elevated Gastric Mucosal IL-1β
Serelli-Lee, V., Ling, K. L., Ho, C. S. L., Yeong, L. H., Lim, G. K., Ho, B., & Wong, S. B. J. (2012) · PLoS ONE · doi:10.1371/journal.pone.0039199 · Cited by 57
ADAM8: a new therapeutic target for asthma
Knolle, M. D., & Owen, C. A. (2009) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728220902889788 · Cited by 53
Effective Therapy with Anti‐TNF‐α in Patients with Psoriatic Arthritis Is Associated with Decreased Levels of Metalloproteinases and Angiogenic Cytokines in the Sera and Skin Lesions
Cordiali‐Fei, P., Trento, E., D’Agosto, G., Bordignon, V., Mussi, A., Ardigò, M., Mastroianni, A., Vento, A., Solivetti, F. M., Berardesca, E., et al. (2007) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1423.062 · Cited by 53
Matrix metalloproteinases in the cervical mucus plug in relation to gestational age, plug compartment, and preterm labor
Becher, N., Hein, M., Danielsen, C. C., & Uldbjerg, N. (2010) · Reproductive Biology and Endocrinology · doi:10.1186/1477-7827-8-113 · Cited by 53
Helicobacter pylori Activates Matrix Metalloproteinase 10 in Gastric Epithelial Cells via EGFR and ERK-mediated Pathways
Costa, Â. M., Ferreira, R. M., Pinto-Ribeiro, I., Sougleri, I. S., Oliveira, M. J., Carreto, L. C., Santos, M. A. S., Sgouras, D. N., Carneiro, F., Leite, M., et al. (2016) · The Journal of Infectious Diseases · doi:10.1093/infdis/jiw031 · Cited by 53
MicroRNA 744-3p promotes MMP-9-mediated metastasis by simultaneously suppressing PDCD4 and PTEN in laryngeal squamous cell carcinoma
Li, Z.-H., Gao, W., Lei, W.-B., Zhao, J., Chan, J. Y. W., Wei, W., Ho, W.-K., & Wong, T. (2016) · Oncotarget · doi:10.18632/oncotarget.11280 · Cited by 53
Tissue inhibitor of metalloproteinase-1 exacerbated renal interstitial fibrosis through enhancing inflammation
Cai, G., Zhang, X., Hong, Q., Shao, F., Shang, X., Fu, B., Feng, Z., Lin, H., Wang, J., Shi, S., et al. (2008) · Nephrology Dialysis Transplantation · doi:10.1093/ndt/gfm666 · Cited by 53
Differential Responses to Targeting Matrix Metalloproteinase 9 in Idiopathic Pulmonary Fibrosis
Espíndola, M. S., Habiel, D. M., Coelho, A. L., Stripp, B. R., Parks, W. C., Oldham, J. M., Martínez, F. J., Noth, I., Lopez, D., Mikels, A. J., et al. (2020) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.201910-1977oc · Cited by 52
Self-citation
The Nrf2 transcription factor: A multifaceted regulator of the extracellular matrix
Hiebert, P. (2021) · Matrix Biology Plus · doi:10.1016/j.mbplus.2021.100057 · Cited by 54
Matrix metalloproteinases and tissue damage in HIV ‐tuberculosis immune reconstitution inflammatory syndrome
Tadokera, R., Meintjes, G., Wilkinson, K. A., Skolimowska, K. H., Walker, N. F., Friedland, J. S., Maartens, G., Elkington, P. T., & Wilkinson, R. J. (2013) · European Journal of Immunology · doi:10.1002/eji.201343593 · Cited by 52
PET Radioligands for In Vivo Visualization of Neuroinflammation
Ory, D., Celen, S., Verbruggen, A., & Bormans, G. M. (2014) · Current Pharmaceutical Design · doi:10.2174/1381612820666140613120212 · Cited by 53
Structure-Based Design and Synthesis of Potent and Selective Matrix Metalloproteinase 13 Inhibitors
Choi, J. Y., Fuerst, R., Knapinska, A. M., Taylor, A. B., Smith, L., Cao, X., Hart, P. J., Fields, G., & Roush, W. R. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.7b00514 · Cited by 53
Comparative analysis of angiogenic gene expression in normal and impaired wound healing in diabetic mice: effects of extracorporeal shock wave therapy
Zins, S. R., Amare, M. F., Tadaki, D. K., Elster, E. A., & Davis, T. A. (2010) · Angiogenesis · doi:10.1007/s10456-010-9186-9 · Cited by 51
Matrix metalloproteinase-9 deletion is associated with decreased mid-term vein wall fibrosis in experimental stasis DVT
Deatrick, K. B., Andrea, T., Luke, C. E., Elfline, M. A., Sood, V., Upchurch, G. R., Jaffer, F. A., Wakefield, T. W., & Henke, P. K. (2013) · Thrombosis Research · doi:10.1016/j.thromres.2013.06.027 · Cited by 49
Matrix metalloproteinase-12 contributes to neuroinflammation in the aged brain
Liu, Y., Zhang, M., Hao, W., Mihaljevic, I., Liu, X., Xie, K., Walter, S., & Fassbender, K. C. (2012) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2012.10.015 · Cited by 50
Ascaris lumbricoides: An Overview of Therapeutic Targets
Hagel, I., & Giusti, T. (2010) · Infectious Disorders - Drug Targets · doi:10.2174/187152610793180876 · Cited by 53
The effect of matrix metalloproteinase 2 and matrix metalloproteinase 2/9 deletion in experimental post-thrombotic vein wall remodeling
Deatrick, K. B., Luke, C. E., Elfline, M. A., Sood, V., Baldwin, J., Upchurch, G. R., Jaffer, F. A., Wakefield, T. W., & Henke, P. K. (2013) · Journal of Vascular Surgery · doi:10.1016/j.jvs.2012.11.088 · Cited by 52
Spirulina maxima derived marine pectin promotes the in vitro and in vivo regeneration and wound healing in zebrafish
Edirisinghe, S. L., Rajapaksha, D. C., Nikapitiya, C., Oh, C., Lee, K.-A., Kang, D.-H., & Zoysa, M. D. (2020) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2020.10.008 · Cited by 53
Matrix Metalloproteinase-1 Is Regulated in Tuberculosis by a p38 MAPK-Dependent, p -Aminosalicylic Acid-Sensitive Signaling Cascade
Rand, L., Green, J. A., Saraiva, L., Friedland, J. S., & Elkington, P. T. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0801935 · Cited by 51
Diagnostic Cytokines and Comparative Analysis Secreted from Exfoliated Deciduous Teeth, Dental Pulp, and Bone Marrow Derived Mesenchymal Stem Cells for Functional Cell-Based Therapy
Yamada, Y., Nakamura-Yamada, S., Umemura-Kubota, E., & Baba, S. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20235900 · Cited by 49
Metalloproteinases and Their Associated Genes Contribute to the Functional Integrity and Noise-Induced Damage in the Cochlear Sensory Epithelium
Hu, B. H., Cai, Q., Hu, Z., Patel, M. B., Bard, J., Jamison, J. L., & Coling, D. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.1588-12.2012 · Cited by 50
FRET‐based and other fluorescent proteinase probes
Hu, H., Gehrig, S. M., Reither, G., Subramanian, D., Mall, M. A., Plettenburg, O., & Schultz, C. (2014) · Biotechnology Journal · doi:10.1002/biot.201300201 · Cited by 49
The Role of Matrix Metalloproteinase Polymorphisms in Ischemic Stroke
Chang, J. J., Stanfill, A. G., & Pourmotabbed, T. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17081323 · Cited by 50
Evolution in chronic cold: varied loss of cellular response to heat in Antarctic notothenioid fish
Bilyk, K. T., Vargas‐Chacoff, L., & Cheng, C. ‐. C. (2018) · BMC Evolutionary Biology · doi:10.1186/s12862-018-1254-6 · Cited by 51
Role of Mitochondria-Derived Danger Signals Released After Injury in Systemic Inflammation and Sepsis
Itagaki, K., Riça, I. G., Konečná, B., Kim, H. I., Park, J. B., Kaczmarek, E., & Hauser, C. J. (2021) · Antioxidants and Redox Signaling · doi:10.1089/ars.2021.0052 · Cited by 50
Dual Inhibitors of Matrix Metalloproteinases and Carbonic Anhydrases: Iminodiacetyl-Based Hydroxamate−Benzenesulfonamide Conjugates
Marques, S. M., Nuti, E., Rossello, A., Supuran, C. T., Tuccinardi, T., Martinelli, A., & Santos, M. A. (2008) · Journal of Medicinal Chemistry · doi:10.1021/jm800964f · Cited by 49
Gelatinase B/MMP-9 as an inflammatory marker enzyme in mouse zymosan peritonitis: Comparison of phase-specific and cell-specific production by mast cells, macrophages and neutrophils
Kołaczkowska, E., Arnold, B., & Opdenakker, G. (2007) · Immunobiology · doi:10.1016/j.imbio.2007.07.005 · Cited by 50
Decorin overexpression reduces atherosclerosis development in apolipoprotein E-deficient mice
Zen, A. A. H., Caligiuri, G., Sainz, J., Lemitre, M., Demerens, C., & Lafont, A. M. (2005) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2005.08.023 · Cited by 50
Decreased levels of metalloproteinase-9 and angiogenic factors in skin lesions of patients with psoriatic arthritis after therapy with anti-TNF-α
Cordiali‐Fei, P., Trento, E., D’Agosto, G., Bordignon, V., Mussi, A., Ardigò, M., Mastroianni, A., Vento, A., Solivetti, F. M., Berardesca, E., et al. (2006) · Journal of Autoimmune Diseases · doi:10.1186/1740-2557-3-5 · Cited by 50
Inflammation Regulates the Multi-Step Process of Retinal Regeneration in Zebrafish
Nagashima, M., & Hitchcock, P. F. (2021) · Cells · doi:10.3390/cells10040783 · Cited by 49
Host-directed therapies in pulmonary tuberculosis: Updates on anti-inflammatory drugs
Cubillos-Angulo, J. M., Nogueira, B. M. F., Arriaga, M. B., Barreto‐Duarte, B., Araújo‐Pereira, M., Fernandes, C. D., Vinhaes, C. L., Villalva-Serra, K., Nunes, V. M., Miguez-Pinto, J. P., et al. (2022) · Frontiers in Medicine · doi:10.3389/fmed.2022.970408 · Cited by 48
Cord immunoproteins as predictors of respiratory outcome in preterm infants
Kaukola, T., Tuimala, J., Herva, R., Kingsmore, S. F., & Hallman, M. (2008) · American Journal of Obstetrics and Gynecology · doi:10.1016/j.ajog.2008.07.070 · Cited by 49
Differential Expression of Matrix Metalloproteinases 2, 9 and Cytokines by Neutrophils and Monocytes in the Clinical Forms of Chagas Disease
Medeiros, N. I., Fares‐Gusmao, R., Franco, E. P., Sousa, G. R., de Mattos, R. T., Chaves, A. T., Nunes, M. C. P., Dutra, W. O., Corrêa‐Oliveira, R., Rocha, M. O. D. C., et al. (2017) · PLoS neglected tropical diseases · doi:10.1371/journal.pntd.0005284 · Cited by 49
Matrix metalloproteinase-9 expression and release from skin fibroblasts interacting with keratinocytes: Upregulation in response to sulphur mustard
Ries, C., Popp, T., Egea, V., Kehe, K., & Jochum, M. (2008) · Toxicology · doi:10.1016/j.tox.2008.08.011 · Cited by 49
Identification of a lepidopteran matrix metalloproteinase with dual roles in metamorphosis and innate immunity
Altincicek, B., & Vilcinskas, A. (2007) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2007.08.001 · Cited by 49
TACE-dependent EGF receptor activation in angiotensin-II-induced kidney disease
Shah, B. H., & Catt, K. J. (2006) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2006.03.010 · Cited by 49
Molt-dependent transcriptomic analysis of cement proteins in the barnacle Amphibalanus amphitrite
Wang, Z., Leary, D. H., Liu, J., Settlage, R. E., Fears, K. P., North, S. H., Mostaghim, A., Essock‐Burns, T., Haynes, S. E., Wahl, K. J., et al. (2015) · BMC Genomics · doi:10.1186/s12864-015-2076-1 · Cited by 48
Regeneration of Soft Tissues Is Promoted by MMP1 Treatment after Digit Amputation in Mice
Mu, X., Bellayr, I. H., Pan, H., Choi, Y., & Li, Y. (2013) · PLoS ONE · doi:10.1371/journal.pone.0059105 · Cited by 48
Functional Genomics Reveals the Induction of Inflammatory Response and Metalloproteinase Gene Expression during Lethal Ebola Virus Infection
Cillóniz, C., Ebihara, H., Ni, C., Neumann, G., Korth, M. J., Kelly, S. M., Kawaoka, Y., Feldmann, H., & Katze, M. G. (2011) · Journal of Virology · doi:10.1128/jvi.00659-11 · Cited by 47
Matrix metalloproteinase-9 deficiency leads to prolonged foreign body response in the brain associated with increased IL-1β levels and leakage of the blood-brain barrier
Tian, W., & Kyriakides, T. R. (2009) · Matrix Biology · doi:10.1016/j.matbio.2009.02.002 · Cited by 49
The potential role of DNA methylation in the pathogenesis of abdominal aortic aneurysm
Toghill, B. J., Saratzis, A. N., Harrison, S. C., Verissimo, A. R., Mallon, E. B., & Bown, M. J. (2015) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2015.05.001 · Cited by 50
Translating Koch’s Postulates to Identify Matrix Metalloproteinase Roles in Postmyocardial Infarction Remodeling
Iyer, R. P., Brás, L. E. D. C., Jin, Y.-F., & Lindsey, M. L. (2014) · Circulation Research · doi:10.1161/circresaha.114.301673 · Cited by 48
Matrix Metalloproteinases in Tuberculosis-Immune Reconstitution Inflammatory Syndrome and Impaired Lung Function Among Advanced HIV/TB Co-infected Patients Initiating Antiretroviral Therapy
Ravimohan, S., Tamuhla, N., Kung, S., Nfanyana, K., Steenhoff, A. P., Gross, R., Weissman, D., & Bisson, G. P. (2015) · EBioMedicine · doi:10.1016/j.ebiom.2015.11.040 · Cited by 48
Mechanism and Inhibition of Matrix Metalloproteinases
Cerofolini, L., Fragai, M., & Luchinat, C. (2018) · Current Medicinal Chemistry · doi:10.2174/0929867325666180326163523 · Cited by 51
Elevated levels of matrix metalloproteinases reflect severity and extent of disease in tuberculosis-diabetes co-morbidity and are predominantly reversed following standard anti-tuberculosis or metformin treatment
Kumar, N. P., Moideen, K., Viswanathan, V., Shruthi, B. S., Sivakumar, S., Menon, P. A., Kornfeld, H., & Babu, S. (2018) · BMC Infectious Diseases · doi:10.1186/s12879-018-3246-y · Cited by 49
Expression of gelatinases (MMP-2 and MMP-9) and tissue inhibitors of metalloproteinases (TIMP-2 and TIMP-3) in the chicken ovary in relation to follicle development and atresia
Hrabia, A., Wolak, D., Kwaśniewska, M., Kieronska‐Rudek, A., Socha, J. K., & Sechman, A. (2018) · Theriogenology · doi:10.1016/j.theriogenology.2018.11.017 · Cited by 48
Molecular Determinants of a Selective Matrix Metalloprotease-12 Inhibitor: Insights from Crystallography and Thermodynamic Studies
Czarny, B., Stura, E. A., Devel, L., Vera, L., Lajeunesse, E. C., Beau, F., Calderone, V., Fragai, M., Luchinat, C., & Dive, V. (2013) · Journal of Medicinal Chemistry · doi:10.1021/jm301574d · Cited by 48
Bone Morphogenetic Proteins Stimulate Mammary Fibroblasts to Promote Mammary Carcinoma Cell Invasion
Owens, P., Polikowsky, H. G., Pickup, M. W., Gorska, A. E., Jovanović, B., Shaw, A. K., Novitskiy, S. V., Hong, C. C., & Moses, H. L. (2013) · PLoS ONE · doi:10.1371/journal.pone.0067533 · Cited by 47
Topical Brazilian propolis improves corneal wound healing and inflammation in rats following alkali burns
Martin, L. F. T., Rocha, E. M., Garcia, S. B., & Paula, J. S. (2013) · BMC Complementary and Alternative Medicine · doi:10.1186/1472-6882-13-337 · Cited by 47
Novel n-3 PUFA monoacylglycerides of pharmacological and medicinal interest: Anti-inflammatory and anti-proliferative effects
Khaddaj‐Mallat, R., Morin, C., & Rousseau, É. (2016) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2016.10.038 · Cited by 48
Conserved gene expression in sperm reservoirs between birds and mammals in response to mating
Atikuzzaman, M., Álvarez‐Rodríguez, M., Vicente‐Carrillo, A., Johnsson, M., Wright, D., & Rodríguez‐Martínez, H. (2017) · BMC Genomics · doi:10.1186/s12864-017-3488-x · Cited by 47
MicroRNA-140-5p inhibits cell proliferation and invasion by regulating VEGFA/MMP2 signaling in glioma
Hu, Y., Li, Y., Wu, C., Zhou, L., Han, X., Wang, Q., Xie, X., Zhou, Y., & Du, Z. (2017) · Tumor Biology · doi:10.1177/1010428317697558 · Cited by 47
Potential roles of metalloproteinases of endometrium‐derived exosomes in embryo‐maternal crosstalk during implantation
Latifi, Z., Fattahi, A., Ranjbaran, A., Nejabati, H. R., & Imakawa, K. (2017) · Journal of Cellular Physiology · doi:10.1002/jcp.26259 · Cited by 47
Immunomodulation as Rescue for Chronic Atonic Skin Wounds
Opdenakker, G., Damme, J. V., & Vranckx, J. J. (2018) · Trends in Immunology · doi:10.1016/j.it.2018.01.010 · Cited by 50
Effects of Resistance Training on Matrix Metalloproteinase Activity in Skeletal Muscles and Blood Circulation During Aging
Neto, I. V. D. S., Durigan, J. L. Q., Guzzoni, V., Tibana, R. A., Prestes, J., Selistre-de-Araújo, H. S., & Marqueti, R. D. C. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.00190 · Cited by 47
Effects of IL-1β on MMP-9 Expression in Cementoblast-Derived Cell Line and MMP-Mediated Degradation of Type I Collagen
Du, M., Wang, Y., Liu, Z., Wang, L., Cao, Z., Zhang, C., Hao, Y., & He, H. (2019) · Inflammation · doi:10.1007/s10753-018-00951-6 · Cited by 47
Matrix Metalloproteinase–7 Coordinates Airway Epithelial Injury Response and Differentiation of Ciliated Cells
Gharib, S. A., Altemeier, W. A., Winkle, L. S. V., Plopper, C. G., Schlesinger, S. Y., Buell, C. A., Brauer, R., Lee, V. S., Parks, W. C., & Chen, P. (2012) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2012-0083oc · Cited by 47
Self-citation
Loss of IL-7R and IL-15R Expression Is Associated with Disappearance of Memory T Cells in Respiratory Tract following Influenza Infection1
Shen, C.-H., Ge, Q., Talay, O., Eisen, H., García-Sastre, A., & Chen, J.-Z. (2008) · Journal of Immunology · doi:10.4049/jimmunol.180.1.171 · Cited by 56
An Introduction to Analytical Challenges, Approaches, and Applications in Mass Spectrometry–Based Secretomics
Knecht, S., Eberl, H. C., Kreisz, N., Ugwu, U. J., Starikova, T., Küster, B., & Wilhelm, S. (2023) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2023.100636 · Cited by 49
Hitting the Target! Challenges and Opportunities for TGF-β Inhibition for the Treatment of Cardiac fibrosis
Vistnes, M. (2024) · Pharmaceuticals · doi:10.3390/ph17030267 · Cited by 49
Matrix Metalloproteinase-10/TIMP-2 Structure and Analyses Define Conserved Core Interactions and Diverse Exosite Interactions in MMP/TIMP Complexes
Batra, J., Soares, A. S., Mehner, C., & Radisky, E. S. (2013) · PLoS ONE · doi:10.1371/journal.pone.0075836 · Cited by 45
Repeated exposure of mouse dermal fibroblasts at a sub-cytotoxic dose of UVB leads to premature senescence: A robust model of cellular photoaging
Zeng, J.-P., Bi, B., Chen, L., Yang, P. C., Guo, Y., Zhou, Y.-Q., & Liu, T. (2013) · Journal of Dermatological Science · doi:10.1016/j.jdermsci.2013.08.013 · Cited by 50
Matrix metalloproteinase-10 plays an active role in microvascular complications in type 1 diabetic patients
Toni, M., Hermida, J., Goñi, M. J., Fernández, P., Parks, W. C., Toledo, E., Montes, R., & Díez, N. (2013) · Diabetologia · doi:10.1007/s00125-013-3052-4 · Cited by 46
Self-citation
Persistence of cirrhosis is maintained by intrahepatic regulatory T cells that inhibit fibrosis resolution by regulating the balance of tissue inhibitors of metalloproteinases and matrix metalloproteinases
Zhang, X., Feng, M., Liu, X., Bai, L., Kong, M., Chen, Y., Zheng, S., Liu, S., Wan, Y. Y., Duan, Z., et al. (2015) · Translational research · doi:10.1016/j.trsl.2015.10.008 · Cited by 46
Lung remodeling associated with recovery from acute lung injury
Gill, S. E., Yamashita, C. M., & Veldhuizen, R. A. W. (2016) · Cell and Tissue Research · doi:10.1007/s00441-016-2521-8 · Cited by 46
The multifaceted roles of tumor-associated proteases and harnessing their activity for prodrug activation
Vasiljeva, O. S., Hostetter, D. R., Moore, S. J., & Winter, M. B. (2019) · Biological Chemistry · doi:10.1515/hsz-2018-0451 · Cited by 46
Biomarkers in urinary tract infections – which ones are suitable for diagnostics and follow-up?
Horváth, J., Wullt, B., Naber, K. G., & Köves, B. (2020) · PubMed Central · doi:10.3205/id000068 · Cited by 45
Extracellular matrix and dermal nerve growth factor dysregulation in prurigo nodularis compared to atopic dermatitis
Deng, J., Parthasarathy, V., Marani, M., Bordeaux, Z. A., Lee, K. K., Trinh, C., Cornman, H. L., Kambala, A., Pritchard, T., Chen, S., et al. (2022) · Frontiers in Medicine · doi:10.3389/fmed.2022.1022889 · Cited by 45
The contribution of matrix metalloproteinases and their inhibitors to the development, progression, and rupture of abdominal aortic aneurysms
Atkinson, G., Bianco, R., Gregoli, K. D., & Johnson, J. L. (2023) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2023.1248561 · Cited by 45
Understanding the matrix: collagen modifications in tumors and their implications for immunotherapy
Borst, R., Meyaard, L., & Ramos, M. I. P. (2024) · Journal of Translational Medicine · doi:10.1186/s12967-024-05199-3 · Cited by 53
Significance of Circulating and Crevicular Matrix Metalloproteinase-9 in Rheumatoid Arthritis-Chronic Periodontitis Association
Siloşi, I., Cojocaru, M., Foia, L. G., Boldeanu, M. V., Petrescu, F., Șurlin, P., & Biciuşcă, V. (2015) · Journal of Immunology Research · doi:10.1155/2015/218060 · Cited by 45
The ORF3 Protein of Hepatitis E Virus Interacts with Hemopexin by Means of Its 26 Amino Acid N-Terminal Hydrophobic Domain II
Ratra, R., Kar-Roy, A., & Lal, S. K. (2008) · Biochemistry · doi:10.1021/bi7016552 · Cited by 45
AUY954, a selective S1P1 modulator, prevents experimental autoimmune neuritis
Zhang, Z., Zhang, Z., Zug, C., Nuesslein‐Hildesheim, B., Leppert, D., & Schluesener, H. J. (2009) · Journal of Neuroimmunology · doi:10.1016/j.jneuroim.2009.09.010 · Cited by 46
Matrix metalloproteinases 1, 2, 3 and 9 functional single-nucleotide polymorphisms in idiopathic recurrent spontaneous abortion
Pereza, N., Ostojić, S., Volk, M., Kapović, M., & Peterlin, B. (2012) · Reproductive BioMedicine Online · doi:10.1016/j.rbmo.2012.01.008 · Cited by 45
Knockdown of ribosomal protein S7 causes developmental abnormalities via p53 dependent and independent pathways in zebrafish
Duan, J., Ba, Q., Wang, Z., Hao, M., Li, X., Hu, P., Zhang, D., Zhang, R., & Wang, H. (2011) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2011.04.015 · Cited by 45
Compartment-Specific Remodeling of Splenic Micro-Architecture during Experimental Visceral Leishmaniasis
Yurdakul, P., Dalton, J. E., Beattie, L., Brown, N., Ergüven, S., Maroof, A., & Kaye, P. M. (2011) · American Journal Of Pathology · doi:10.1016/j.ajpath.2011.03.009 · Cited by 45
Elucidating the Function of Non catalytic Domains of Collagenases and Aggrecanases
Nagase, H., & Fushimi, K. (2008) · Connective Tissue Research · doi:10.1080/03008200802151698 · Cited by 45
Effects of verbascoside biotechnologically produced by Syringa vulgaris plant cell cultures in a rodent model of colitis
Mazzon, E., Esposito, E., Paola, R. D., Riccardi, L., Caminiti, R., Toso, R. D., Pressi, G., & Cuzzocrea, S. (2009) · Naunyn-Schmiedeberg s Archives of Pharmacology · doi:10.1007/s00210-009-0400-5 · Cited by 45
Protein tyrosine kinase and p38 MAP kinase pathways are involved in stimulation of matrix metalloproteinase-9 by TNF-α in human monocytes
Nguyen, J., Gogusev, J., Knapnougel, P., & Bauvois, B. (2006) · Immunology Letters · doi:10.1016/j.imlet.2006.04.003 · Cited by 45
Modified synthetic siRNA targeting tissue inhibitor of metalloproteinase‐2 inhibits hepatic fibrogenesis in rats
Hu, Y., Li, D., & Lu, H. (2007) · The Journal of Gene Medicine · doi:10.1002/jgm.1009 · Cited by 45
Expression and regulation of matrix metalloproteinase-12 in experimental autoimmune encephalomyelitis and by bone marrow derived macrophages in vitro
DaSilva, A. G., & Yong, V. W. (2008) · Journal of Neuroimmunology · doi:10.1016/j.jneuroim.2008.04.034 · Cited by 45

Authors: Parks, W. C., Wilson, C. L., & López-Boado, Y. S.
Affiliations: University of Washington (US)
Wake Forest University Health Sciences (US)
Corresponding author: Parks, William C.
ORCID: Wilson, Carole L.
Venue: Nature Reviews Immunology
Publisher: Springer Science and Business Media LLC
Published: 2004-08
Volume: 4
Issue: 8
Pages: 617-629
ISSN: 1474-1733 (ISSN-L)
1474-1741
DOI: 10.1038/nri1418
OpenAlex: W1987825791
Cited by: 1,929
References: 149
Citations by year: 2026: 48 · 2025: 47 · 2024: 86 · 2023: 72 · 2022: 68 · 2021: 93 · 2020: 89 · 2019: 97 · 2018: 90 · 2017: 134 · 2016: 87 · 2015: 116 · 2014: 109 · 2013: 102 · 2012: 113
FWCI: 4.82
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
Locations: Nature reviews. Immunology (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
Health Sciences › Medicine › Hematology › Blood Coagulation and Thrombosis Mechanisms
Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
Keywords: matrix metalloproteinases, inflammation, innate immunity, extracellular matrix degradation, inflammatory cytokines, chemokines, protein processing, proteolysis
MeSH terms: Animals, Extracellular Matrix, Humans, Immunity, Innate, Inflammation, Chemokines, Matrix Metalloproteinases

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Matrix metalloproteinases as modulators of inflammation and innate immunity

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks