Matrix Metalloproteinase-9 (MMP-9) as a Cancer Biomarker and MMP-9 Biosensors: Recent Advances
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Klein, 2011, Physiology and pathophysiology of matrix metalloproteases, Amino Acids, 41, 271, 10.1007/s00726-010-0689-x
Nagase, 2006, Structure and function of matrix metalloproteinases and timps, Cardiovasc. Res., 69, 562, 10.1016/j.cardiores.2005.12.002
Vandooren, 2013, Biochemistry and molecular biology of gelatinase B or matrix metalloproteinase-9 (MMP-9): The next decade, Crit. Rev. Biochem. Mol. Biol., 48, 222, 10.3109/10409238.2013.770819
Bruschi, 2013, The significance of matrix metalloproteinases in parasitic infections involving the central nervous system, Pathogens, 2, 105, 10.3390/pathogens2010105
Dubois, 2002, Biochemistry and molecular biology of gelatinase B or matrix metalloproteinase-9 (MMP-9), Crit. Rev. Biochem. Mol. Biol., 37, 375, 10.1080/10409230290771546
Agrawal, 2008, Zinc-binding groups modulate selective inhibition of MMPs, ChemMedChem, 3, 812, 10.1002/cmdc.200700290
Santos, 2004, Inhibition of human pulpal gelatinases (MMP-2 and MMP-9) by zinc oxide cements, J. Oral Rehabil., 31, 660, 10.1111/j.1365-2842.2004.01297.x
Opdenakker, 2001, Gelatinase B functions as regulator and effector in leukocyte biology, J. Leukoc. Biol., 69, 851, 10.1189/jlb.69.6.851
Rosenblum, 2007, Insights into the structure and domain flexibility of full-length pro-matrix metalloproteinase-9/gelatinase B, Structure, 15, 1227, 10.1016/j.str.2007.07.019
Overall, 2007, Protease yoga: Extreme flexibility of a matrix metalloproteinase, Structure, 15, 1159, 10.1016/j.str.2007.10.001
Shipley, 1996, The structural basis for the elastolytic activity of the 92-kDa and 72-kDa gelatinases. Role of the fibronectin type ii-like repeats, J. Biol. Chem., 271, 4335, 10.1074/jbc.271.8.4335
Pourmotabbed, 1998, The fibronectin-like domain is required for the type V and XI collagenolytic activity of gelatinase B, Arch. Biochem. Biophys., 354, 24, 10.1006/abbi.1998.0662
Whitehead, 2008, Selective modulation of matrix metalloproteinase 9 (MMP-9) functions via exosite inhibition, J. Biol. Chem., 283, 20087, 10.1074/jbc.M801438200
Roeb, 2002, The matrix metalloproteinase 9 (MMP-9) hemopexin domain is a novel gelatin binding domain and acts as an antagonist, J. Biol. Chem., 277, 50326, 10.1074/jbc.M207446200
Ethell, 2007, Matrix metalloproteinases in brain development and remodeling: Synaptic functions and targets, J. Neurosci. Res., 85, 2813, 10.1002/jnr.21273
Roderfeld, 2007, Latent MMP-9 is bound to TIMP-1 before secretion, Biol. Chem., 388, 1227, 10.1515/BC.2007.123
Yabluchanskiy, 2013, Matrix metalloproteinase-9: Many shades of function in cardiovascular disease, Physiology, 28, 391, 10.1152/physiol.00029.2013
Massova, 1998, Matrix metalloproteinases: Structures, evolution, and diversification, FASEB J., 12, 1075, 10.1096/fasebj.12.12.1075
Dufour, 2011, Small-molecule anticancer compounds selectively target the hemopexin domain of matrix metalloproteinase-9, Cancer Res., 71, 4977, 10.1158/0008-5472.CAN-10-4552
Reinhard, 2015, A delicate balance: Role of MMP-9 in brain development and pathophysiology of neurodevelopmental disorders, Front. Cell. Neurosci., 9, 280, 10.3389/fncel.2015.00280
Ogata, 1992, Matrix metalloproteinase 3 (stromelysin) activates the precursor for the human matrix metalloproteinase 9, J. Biol. Chem., 267, 3581, 10.1016/S0021-9258(19)50563-4
Fridman, 1995, Activation of progelatinase b (MMP-9) by gelatinase a (MMP-2), Cancer Res., 55, 2548
Imai, 1995, Matrix metalloproteinase 7 (matrilysin) from human rectal carcinoma cells. Activation of the precursor, interaction with other matrix metalloproteinases and enzymic properties, J. Biol. Chem., 270, 6691, 10.1074/jbc.270.12.6691
Knauper, 1997, Activation of progelatinase B (proMMP-9) by active collagenase-3 (MMP-13), Eur. J. Biochem., 248, 369, 10.1111/j.1432-1033.1997.00369.x
Rajagopalan, 1996, Reactive oxygen species produced by macrophage-derived foam cells regulate the activity of vascular matrix metalloproteinases in vitro. Implications for atherosclerotic plaque stability, J. Clin. Investig., 98, 2572, 10.1172/JCI119076
Gu, 2002, S-nitrosylation of matrix metalloproteinases: Signaling pathway to neuronal cell death, Science, 297, 1186, 10.1126/science.1073634
Paquette, 2003, Activation of matrix metalloproteinase-2 and -9 by 2- and 4-hydroxyestradiol, J. Steroid Biochem. Mol. Biol., 87, 65, 10.1016/S0960-0760(03)00386-8
Manabe, 2005, Activation of matrix metalloproteinase-9 via neuronal nitric oxide synthase contributes to NMDA-induced retinal ganglion cell death, Investig. Ophthalmol. Vis. Sci., 46, 4747, 10.1167/iovs.05-0128
Ridnour, 2007, Nitric oxide regulates matrix metalloproteinase-9 activity by guanylyl-cyclase-dependent and -independent pathways, Proc. Natl. Acad. Sci. USA, 104, 16898, 10.1073/pnas.0702761104
Kridel, 2001, Substrate hydrolysis by matrix metalloproteinase-9, J. Biol. Chem., 276, 20572, 10.1074/jbc.M100900200
Prudova, 2010, Multiplex n-terminome analysis of MMP-2 and MMP-9 substrate degradomes by itraq-tails quantitative proteomics, Mol. Cell. Proteom., 9, 894, 10.1074/mcp.M000050-MCP201
Fan, 2016, Microrna-183 functions as the tumor suppressor via inhibiting cellular invasion and metastasis by targeting MMP-9 in cervical cancer, Gynecol. Oncol., 141, 166, 10.1016/j.ygyno.2016.02.006
Aung, 2015, MMP-9 expression is increased in b lymphocytes during multiple sclerosis exacerbation and is regulated by microrna-320a, J. Neuroimmunol., 278, 185, 10.1016/j.jneuroim.2014.11.004
Jiang, 2002, Regulation of matrix metalloproteinase-9 (MMP-9) by translational efficiency in murine prostate carcinoma cells, Cancer Res., 62, 1910
Melamed, 2006, Modulation of matrix metalloproteinase-9 (MMP-9) secretion in B lymphopoiesis, Int. Immunol., 18, 1355, 10.1093/intimm/dxl068
Ong, 2017, Complex regulation of neutrophil-derived MMP-9 secretion in central nervous system tuberculosis, J. Neuroinflamm., 14, 31, 10.1186/s12974-017-0801-1
Li, 2013, Role of microrna-mediated MMP regulation in the treatment and diagnosis of malignant tumors, Cancer Biol. Ther., 14, 796, 10.4161/cbt.25936
Zariffard, M.R., Anastos, K., French, A.L., Munyazesa, E., Cohen, M., Landay, A.L., and Spear, G.T. (2015). Cleavage/alteration of interleukin-8 by matrix metalloproteinase-9 in the female lower genital tract. PLoS ONE, 10.
Backstrom, 1996, Matrix metalloproteinase-9 (MMP-9) is synthesized in neurons of the human hippocampus and is capable of degrading the amyloid-beta peptide (1–40), J. Neurosci., 16, 7910, 10.1523/JNEUROSCI.16-24-07910.1996
Mohan, 2002, Matrix metalloproteinase gelatinase b (MMP-9) coordinates and effects epithelial regeneration, J. Biol. Chem., 277, 2065, 10.1074/jbc.M107611200
Armant, 2011, Regulation of proteinases during mouse peri-implantation development: Urokinase-type plasminogen activator expression and cross talk with matrix metalloproteinase 9, Reproduction, 141, 227, 10.1530/REP-10-0334
Dziembowska, 2012, MMP9: A novel function in synaptic plasticity, Int. J. Biochem. Cell Biol., 44, 709, 10.1016/j.biocel.2012.01.023
Agrawal, 2008, MMPs in the central nervous system: Where the good guys go bad, Semin. Cell Dev. Biol., 19, 42, 10.1016/j.semcdb.2007.06.003
Stamenkovic, 2003, Extracellular matrix remodelling: The role of matrix metalloproteinases, J. Pathol., 200, 448, 10.1002/path.1400
Farina, 2014, Gelatinase b/MMP-9 in tumour pathogenesis and progression, Cancers, 6, 240, 10.3390/cancers6010240
Fiore, 2002, Matrix metalloproteinase 9 (MMP-9/gelatinase B) proteolytically cleaves ICAM-1 and participates in tumor cell resistance to natural killer cell-mediated cytotoxicity, Oncogene, 21, 5213, 10.1038/sj.onc.1205684
Vaisar, 2009, MMP-9 sheds the beta2 integrin subunit (CD18) from macrophages, Mol. Cell. Proteom. MCP, 8, 1044, 10.1074/mcp.M800449-MCP200
Cauwe, 2010, Intracellular substrate cleavage: A novel dimension in the biochemistry, biology and pathology of matrix metalloproteinases, Crit. Rev. Biochem. Mol. Biol., 45, 351, 10.3109/10409238.2010.501783
Jobin, 2017, New intracellular activities of matrix metalloproteinases shine in the moonlight, Biochim. Biophys. Acta, 1864, 2043, 10.1016/j.bbamcr.2017.05.013
Zhang, 2015, Proteolytic cleavage of ampkalpha and intracellular MMP9 expression are both required for tlr4-mediated mtorc1 activation and hif-1alpha expression in leukocytes, J. Immunol., 195, 2452, 10.4049/jimmunol.1500944
Nguyen, 1998, Active and tissue inhibitor of matrix metalloproteinase-free gelatinase b accumulates within human microvascular endothelial vesicles, J. Biol. Chem., 273, 5400, 10.1074/jbc.273.9.5400
Zhao, 2003, Activation of pro-gelatinase b by endometase/matrilysin-2 promotes invasion of human prostate cancer cells, J. Biol. Chem., 278, 15056, 10.1074/jbc.M210975200
Kowluru, 2011, Abrogation of MMP-9 gene protects against the development of retinopathy in diabetic mice by preventing mitochondrial damage, Diabetes, 60, 3023, 10.2337/db11-0816
Hill, 2012, Intranuclear matrix metalloproteinases promote DNA damage and apoptosis induced by oxygen-glucose deprivation in neurons, Neuroscience, 220, 277, 10.1016/j.neuroscience.2012.06.019
Yang, 2010, Increased intranuclear matrix metalloproteinase activity in neurons interferes with oxidative DNA repair in focal cerebral ischemia, J. Neurochem., 112, 134, 10.1111/j.1471-4159.2009.06433.x
Hou, 2014, High matrix metalloproteinase-9 expression induces angiogenesis and basement membrane degradation in stroke-prone spontaneously hypertensive rats after cerebral infarction, Neural Regen. Res., 9, 1154, 10.4103/1673-5374.135318
Misko, 2002, Matrix metalloproteinase mediated degradation of basement membrane proteins in trembler j neuropathy nerves, J. Neurochem., 83, 885, 10.1046/j.1471-4159.2002.01200.x
Ozdemir, 1999, Role of matrix metalloproteinase-9 in the basement membrane destruction of superficial urothelial carcinomas, J. Urol., 161, 1359, 10.1016/S0022-5347(01)61684-7
Hsu, C.C., Huang, S.F., Wang, J.S., Chu, W.K., Nien, J.E., Chen, W.S., and Chow, S.E. (2016). Interplay of n-cadherin and matrix metalloproteinase 9 enhances human nasopharyngeal carcinoma cell invasion. BMC Cancer, 16.
Kim, 2012, Matrix metalloproteinase 9 (MMP-9)-dependent processing of betaig-h3 protein regulates cell migration, invasion, and adhesion, J. Biol. Chem., 287, 38957, 10.1074/jbc.M112.357863
Dwivedi, 2009, MMP-9 and -12 cause n-cadherin shedding and thereby beta-catenin signalling and vascular smooth muscle cell proliferation, Cardiovasc. Res., 81, 178, 10.1093/cvr/cvn278
Ortega, 2005, Galectin-3 is a downstream regulator of matrix metalloproteinase-9 function during endochondral bone formation, Mol. Biol. Cell, 16, 3028, 10.1091/mbc.e04-12-1119
Gialeli, 2011, Roles of matrix metalloproteinases in cancer progression and their pharmacological targeting, FEBS J., 278, 16, 10.1111/j.1742-4658.2010.07919.x
Mehner, 2014, Tumor cell-produced matrix metalloproteinase 9 (MMP-9) drives malignant progression and metastasis of basal-like triple negative breast cancer, Oncotarget, 5, 2736, 10.18632/oncotarget.1932
Xu, 2010, Matrix metalloproteinase-9 regulates tumor cell invasion through cleavage of protease nexin-1, Cancer Res., 70, 6988, 10.1158/0008-5472.CAN-10-0242
Pego, 2018, Molecular basis of the effect of MMP-9 on the prostate bone metastasis: A review, Urol. Oncol., 36, 272, 10.1016/j.urolonc.2018.03.009
Itoh, 1999, Experimental metastasis is suppressed in MMP-9-deficient mice, Clin. Exp. Metast., 17, 177, 10.1023/A:1006603723759
Wang, 2010, Inhibition of MMP-9 transcription and suppression of tumor metastasis by pyrrole-imidazole polyamide, Cancer Sci., 101, 759, 10.1111/j.1349-7006.2009.01435.x
Chou, 2012, MMP-9 from sublethally irradiated tumor promotes lewis lung carcinoma cell invasiveness and pulmonary metastasis, Oncogene, 31, 458, 10.1038/onc.2011.240
Hawinkels, 2008, VEGF release by MMP-9 mediated heparan sulphate cleavage induces colorectal cancer angiogenesis, Eur. J. Cancer, 44, 1904, 10.1016/j.ejca.2008.06.031
Leifler, 2013, Inflammation induced by MMP-9 enhances tumor regression of experimental breast cancer, J. Immunol., 190, 4420, 10.4049/jimmunol.1202610
Zhang, 2017, Relationship between matrix metalloproteinases and the occurrence and development of ovarian cancer, Braz. J. Med. Biol. Res., 50, e6104, 10.1590/1414-431x20176104
Kessenbrock, 2010, Matrix metalloproteinases: Regulators of the tumor microenvironment, Cell, 141, 52, 10.1016/j.cell.2010.03.015
Johnson, 2010, Osteoclast-derived matrix metalloproteinase-9 directly affects angiogenesis in the prostate tumor-bone microenvironment, Mol. Cancer Res., 8, 459, 10.1158/1541-7786.MCR-09-0445
Candido, 2016, Roles of ngal and MMP-9 in the tumor microenvironment and sensitivity to targeted therapy, Biochim. Biophys. Acta, 1863, 438, 10.1016/j.bbamcr.2015.08.010
Garg, 2010, Matrix metalloproteinase-9 functions as a tumor suppressor in colitis-associated cancer, Cancer Res., 70, 792, 10.1158/0008-5472.CAN-09-3166
Pujada, 2017, Matrix metalloproteinase MMP9 maintains epithelial barrier function and preserves mucosal lining in colitis associated cancer, Oncotarget, 8, 94650, 10.18632/oncotarget.21841
Walter, 2017, Epithelial derived-matrix metalloproteinase (MMP9) exhibits a novel defensive role of tumor suppressor in colitis associated cancer by activating MMP9-Notch1-ARF-p53 axis, Oncotarget, 8, 364, 10.18632/oncotarget.13406
Rahimi, 2016, Functional promoter polymorphisms of MMP-2 C-735T and MMP-9 C-1562T and their synergism with MMP-7 A-181G in multiple sclerosis, Immunol. Investig., 45, 543, 10.1080/08820139.2016.1180303
Ram, 2006, Matrix metalloproteinase-9 and autoimmune diseases, J. Clin. Immunol., 26, 299, 10.1007/s10875-006-9022-6
Zhernakova, 2014, A genetic variant in the region of MMP-9 is associated with serum levels and progression of joint damage in rheumatoid arthritis, Ann. Rheum. Dis., 73, 1163, 10.1136/annrheumdis-2013-203375
Xue, 2014, Endogenous MMP-9 and not MMP-2 promotes rheumatoid synovial fibroblast survival, inflammation and cartilage degradation, Rheumatology, 53, 2270, 10.1093/rheumatology/keu254
Naouali, 2015, Association of MMP-9 gene polymorphisms with behcet’s disease risk, Immunol. Lett., 164, 18, 10.1016/j.imlet.2015.01.005
Liang, 2018, Serum matrix metalloproteinase-9 level as a biomarker for colorectal cancer: A diagnostic meta-analysis, Biomark. Med., 12, 393, 10.2217/bmm-2017-0206
Shao, 2011, Prognostic impact of MMP-2 and MMP-9 expression in pathologic stage ia non-small cell lung cancer, J. Surg. Oncol., 104, 841, 10.1002/jso.22001
Roy, 2009, Matrix metalloproteinases as novel biomarkers and potential therapeutic targets in human cancer, J. Clin. Oncol., 27, 5287, 10.1200/JCO.2009.23.5556
Li, 2013, Prognostic value of MMP-9 in ovarian cancer: A meta-analysis, Asian Pac. J. Cancer Prev., 14, 4107, 10.7314/APJCP.2013.14.7.4107
Hu, 2012, Matrix metalloproteinase-9 expression correlates with prognosis and involved in ovarian cancer cell invasion, Arch. Gynecol. Obstet., 286, 1537, 10.1007/s00404-012-2456-6
Chen, 2018, Matrix metalloproteinase-9 expression of gctsc in peripheral tissue and central tissue of gctb, J. Cell. Biochem., 119, 5805, 10.1002/jcb.26766
Burotto, 2014, Biomarkers in early-stage non-small-cell lung cancer: Current concepts and future directions, J. Thorac. Oncol., 9, 1609, 10.1097/JTO.0000000000000302
Korpanty, 2014, Biomarkers that currently affect clinical practice in lung cancer: Egfr, alk, met, ros-1, and kras, Front. Oncol., 4, 204, 10.3389/fonc.2014.00204
Blanco-Prieto, S., Barcia-Castro, L., Paez de la Cadena, M., Rodriguez-Berrocal, F.J., Vazquez-Iglesias, L., Botana-Rial, M.I., Fernandez-Villar, A., and De Chiara, L. (2017). Relevance of matrix metalloproteases in non-small cell lung cancer diagnosis. BMC Cancer, 17.
Li, 2012, Matrix metalloproteinase-9 is a prognostic marker for patients with cervical cancer, Med. Oncol., 29, 3394, 10.1007/s12032-012-0283-z
Zajkowska, M., Zbucka-Kretowska, M., Sidorkiewicz, I., Lubowicka, E., Bedkowska, G.E., Gacuta, E., Szmitkowski, M., and Lawicki, S. (2018). Human Plasma Levels of Vascular Endothelial Growth Factor, Matrix Metalloproteinase 9, and Tissue Inhibitor of Matrix Metalloproteinase 1 and Their Applicability as Tumor Markers in Diagnoses of Cervical Cancer Based on ROC Analysis. Cancer Control J. Moffitt Cancer Cent., 25.
Zajkowska, M., Zbucka-Kretowska, M., Sidorkiewicz, I., Lubowicka, E., Gacuta, E., Szmitkowski, M., Chrostek, L., and Lawicki, S. (2018). Plasma levels and diagnostic utility of macrophage-colony stimulating factor, matrix metalloproteinase-9 and tissue inhibitor of metalloproteinase-1 as tumor markers in cervical cancer patients. Tumour Biol. J. Int. Soc. Oncodev. Biol. Med., 40.
Lubowicka, 2017, [The plasma levels and diagnostic utility of matrix metalloproteinase-9 and CA 125 in cervical cancer patients], Pol. Merkur. Lekarski, 43, 10
Reid, 2017, Epidemiology of ovarian cancer: A review, Cancer Biol. Med., 14, 9, 10.20892/j.issn.2095-3941.2016.0084
Reiner, 2017, Ev-associated MMP9 in high-grade serous ovarian cancer is preferentially localized to annexin v-binding evs, Dis. Mark., 2017, 9653194
Tian, M., Cui, Y.Z., Song, G.H., Zong, M.J., Zhou, X.Y., Chen, Y., and Han, J.X. (2008). Proteomic analysis identifies MMP-9, DJ-1 and A1BG as overexpressed proteins in pancreatic juice from pancreatic ductal adenocarcinoma patients. BMC Cancer, 8.
Wang, 2014, Matrix metalloproteinase 9 (MMP-9) in osteosarcoma: Review and meta-analysis, Clin. Chim. Acta Int. J. Clin. Chem., 433, 225, 10.1016/j.cca.2014.03.023
Liu, 2017, Matrix metalloproteinase 9 expression and survival of patients with osteosarcoma: A meta-analysis, Eur. J. Cancer Care, 26, e12364, 10.1111/ecc.12364
Yousef, E.M., Tahir, M.R., St-Pierre, Y., and Gaboury, L.A. (2014). MMP-9 expression varies according to molecular subtypes of breast cancer. BMC Cancer, 14.
Cao, 2008, Serial analysis of gene expression of lobular carcinoma in situ identifies down regulation of claudin 4 and overexpression of matrix metalloproteinase 9, Breast Cancer Res., 10, R91, 10.1186/bcr2189
Roomi, 2009, Distinct patterns of matrix metalloproteinase-2 and -9 expression in normal human cell lines, Oncol. Rep., 21, 821
Li, 2017, The relationship between MMP-2 and MMP-9 expression levels with breast cancer incidence and prognosis, Oncol. Lett., 14, 5865
Golubnitschaja, 2017, Breast cancer risk assessment: A non-invasive multiparametric approach to stratify patients by MMP-9 serum activity and RhoA expression patterns in circulating leucocytes, Amino Acids, 49, 273, 10.1007/s00726-016-2357-2
Darlix, 2016, Serum NSE, MMP-9 and HER2 extracellular domain are associated with brain metastases in metastatic breast cancer patients: Predictive biomarkers for brain metastases?, Int. J. Cancer, 139, 2299, 10.1002/ijc.30290
Yeh, 2010, Evaluation of serum matrix metalloproteinase (MMP)-9 to MMP-2 ratio as a biomarker in hepatocellular carcinoma, Hepato-Gastroenterology, 57, 98
Yan, 2001, The high molecular weight urinary matrix metalloproteinase (MMP) activity is a complex of gelatinase B/MMP-9 and neutrophil gelatinase-associated lipocalin (NGAL). Modulation of MMP-9 activity by NGAL, J. Biol. Chem., 276, 37258, 10.1074/jbc.M106089200
Chakraborty, 2012, The multifaceted roles of neutrophil gelatinase associated lipocalin (NGAL) in inflammation and cancer, Biochim. Biophys. Acta, 1826, 129
Haase, 2009, Accuracy of neutrophil gelatinase-associated lipocalin (NGAL) in diagnosis and prognosis in acute kidney injury: A systematic review and meta-analysis, Am. J. Kidney Dis., 54, 1012, 10.1053/j.ajkd.2009.07.020
Devarajan, 2010, Review: Neutrophil gelatinase-associated lipocalin: A troponin-like biomarker for human acute kidney injury, Nephrology, 15, 419, 10.1111/j.1440-1797.2010.01317.x
Shemin, 2011, Neutrophil gelatinase-associated lipocalin (NGAL) as a biomarker for early acute kidney injury, Crit. Care Clin., 27, 379, 10.1016/j.ccc.2010.12.003
Mitsnefes, 2007, Serum neutrophil gelatinase-associated lipocalin as a marker of renal function in children with chronic kidney disease, Pediatr. Nephrol., 22, 101, 10.1007/s00467-006-0244-x
Fernandez, 2005, The matrix metalloproteinase-9/neutrophil gelatinase-associated lipocalin complex plays a role in breast tumor growth and is present in the urine of breast cancer patients, Clin. Cancer Res., 11, 5390, 10.1158/1078-0432.CCR-04-2391
Liu, 2015, Matrix metalloproteinase-9/neutrophil gelatinase-associated lipocalin complex activity in human glioma samples predicts tumor presence and clinical prognosis, Dis. Mark., 2015, 138974
Shimura, 2015, Urinary adam12 and MMP-9/NGAL complex detect the presence of gastric cancer, Cancer Prev. Res., 8, 240, 10.1158/1940-6207.CAPR-14-0229
Lee, 2017, A reference electrode-free electrochemical biosensor for detecting MMP-9 using a concentric electrode device, Sens. Actuators B Chem., 240, 735, 10.1016/j.snb.2016.09.026
Biela, 2015, Disposable MMP-9 sensor based on the degradation of peptide cross-linked hydrogel films using electrochemical impedance spectroscopy, Biosens. Bioelectron., 68, 660, 10.1016/j.bios.2015.01.060
Stawarski, 2014, Genetically encoded fret-based biosensor for imaging MMP-9 activity, Biomaterials, 35, 1402, 10.1016/j.biomaterials.2013.11.033
Nguyen, 2017, Fabrication of peptide stabilized fluorescent gold nanocluster/graphene oxide nanocomplex and its application in turn-on detection of metalloproteinase-9, Biosens. Bioelectron., 89, 666, 10.1016/j.bios.2015.12.031
Wang, 2018, Stimuli-responsive nanodiamond-based biosensor for enhanced metastatic tumor site detection, SLAS Technol., 23, 44, 10.1177/2472630317735497
Pasamar, 2018, Detection of plasma MMP-9 within minutes. Unveiling some of the clues to develop fast and simple electrochemical magneto-immunosensors, Biosens. Bioelectron., 115, 45, 10.1016/j.bios.2018.05.020
Scarano, 2015, Design of a dual aptamer-based recognition strategy for human matrix metalloproteinase 9 protein by piezoelectric biosensors, Anal. Chim. Acta, 897, 1, 10.1016/j.aca.2015.07.009