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Volumn 33, Issue 4, 2014, Pages 1043-1057

New approaches to selectively target cancer-associated matrix metalloproteinase activity

Author keywords

Activity based protein probes; Cancer progression and metastasis; Extracellular matrix; Matrix metalloproteinase; Tumor microenvironment

Indexed keywords

ANTINEOPLASTIC AGENT; MATRIX METALLOPROTEINASE; MATRIX METALLOPROTEINASE INHIBITOR; MONOCLONAL ANTIBODY; NATURAL PRODUCT;

EID: 84914163554     PISSN: 01677659     EISSN: 15737233     Source Type: Journal    
DOI: 10.1007/s10555-014-9530-4     Document Type: Article
Times cited : (66)

References (111)
  • 1
    • 0036716282 scopus 로고    scopus 로고
    • Strategies for MMP inhibition in cancer: Innovations for the post-trial era
    • COI: 1:CAS:528:DC%2BD38Xmslamsro%3D, PID: 12209155
    • Overall, C. M., & Lopez-Otin, C. (2002). Strategies for MMP inhibition in cancer: Innovations for the post-trial era. Nature Reviews Cancer, 2(9), 657–72. doi:10.1038/nrc884.
    • (2002) Nature Reviews Cancer , vol.2 , Issue.9 , pp. 657-672
    • Overall, C.M.1    Lopez-Otin, C.2
  • 2
    • 0036512208 scopus 로고    scopus 로고
    • New functions for the matrix metalloproteinases in cancer progression
    • COI: 1:CAS:528:DC%2BD38Xis1KktL8%3D, PID: 11990853
    • Egeblad, M., & Werb, Z. (2002). New functions for the matrix metalloproteinases in cancer progression. Nature Reviews Cancer, 2(3), 161–74.
    • (2002) Nature Reviews Cancer , vol.2 , Issue.3 , pp. 161-174
    • Egeblad, M.1    Werb, Z.2
  • 3
    • 0033618337 scopus 로고    scopus 로고
    • Matrix metalloproteinases
    • COI: 1:CAS:528:DyaK1MXltVynu7s%3D
    • Nagase, H., & Woessner, J. F., Jr. (1999). Matrix metalloproteinases. Journal Biological Chemistry, 274(31), 21491–4.
    • (1999) Journal Biological Chemistry , vol.274 , Issue.31 , pp. 21491-21494
    • Nagase, H.1    Woessner, J.F.2
  • 4
    • 84883143934 scopus 로고    scopus 로고
    • Metalloproteinases and their natural inhibitors in inflammation and immunity
    • COI: 1:CAS:528:DC%2BC3sXhtlWktLzE, PID: 23969736
    • Khokha, R., Murthy, A., & Weiss, A. (2013). Metalloproteinases and their natural inhibitors in inflammation and immunity. Nature Reviews Immunology, 13(9), 649–65. doi:10.1038/nri3499.
    • (2013) Nature Reviews Immunology , vol.13 , Issue.9 , pp. 649-665
    • Khokha, R.1    Murthy, A.2    Weiss, A.3
  • 5
    • 0019195010 scopus 로고
    • Metastatic potential correlates with enzymatic degradation of basement membrane collagen
    • COI: 1:CAS:528:DyaL3cXktVGmsbw%3D, PID: 6243750
    • Liotta, L. A., Tryggvason, K., Garbisa, S., Hart, I., Foltz, C. M., & Shafie, S. (1980). Metastatic potential correlates with enzymatic degradation of basement membrane collagen. Nature, 284(5751), 67–8.
    • (1980) Nature , vol.284 , Issue.5751 , pp. 67-68
    • Liotta, L.A.1    Tryggvason, K.2    Garbisa, S.3    Hart, I.4    Foltz, C.M.5    Shafie, S.6
  • 6
    • 78149361406 scopus 로고    scopus 로고
    • Third generation of matrix metalloprotease inhibitors: Gain in selectivity by targeting the depth of the S1′ cavity
    • COI: 1:CAS:528:DC%2BC3cXhtl2isLrE, PID: 20696203
    • Devel, L., Czarny, B., Beau, F., Georgiadis, D., Stura, E., & Dive, V. (2010). Third generation of matrix metalloprotease inhibitors: Gain in selectivity by targeting the depth of the S1′ cavity. Biochimie, 92(11), 1501–8. doi:10.1016/j.biochi.2010.07.017.
    • (2010) Biochimie , vol.92 , Issue.11 , pp. 1501-1508
    • Devel, L.1    Czarny, B.2    Beau, F.3    Georgiadis, D.4    Stura, E.5    Dive, V.6
  • 7
    • 0037192458 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibitors and cancer: Trials and tribulations
    • COI: 1:CAS:528:DC%2BD38XisFSmtb0%3D, PID: 11923519
    • Coussens, L. M., Fingleton, B., & Matrisian, L. M. (2002). Matrix metalloproteinase inhibitors and cancer: Trials and tribulations. Science, 295(5564), 2387–92.
    • (2002) Science , vol.295 , Issue.5564 , pp. 2387-2392
    • Coussens, L.M.1    Fingleton, B.2    Matrisian, L.M.3
  • 8
    • 33846120591 scopus 로고    scopus 로고
    • Matrix metalloproteinases as valid clinical targets
    • COI: 1:CAS:528:DC%2BD2sXjtlWhsLo%3D, PID: 17313364
    • Fingleton, B. (2007). Matrix metalloproteinases as valid clinical targets. Current Pharmaceutical Design, 13(3), 333–46.
    • (2007) Current Pharmaceutical Design , vol.13 , Issue.3 , pp. 333-346
    • Fingleton, B.1
  • 9
    • 0036302814 scopus 로고    scopus 로고
    • Protease degradomics: a new challenge for proteomics
    • COI: 1:CAS:528:DC%2BD38XkvFKmtbc%3D, PID: 12094217
    • Lopez-Otin, C., & Overall, C. M. (2002). Protease degradomics: a new challenge for proteomics. Nature Reviews Molecular Cell Biology, 3(7), 509–19. doi:10.1038/nrm858.
    • (2002) Nature Reviews Molecular Cell Biology , vol.3 , Issue.7 , pp. 509-519
    • Lopez-Otin, C.1    Overall, C.M.2
  • 10
    • 75749157368 scopus 로고    scopus 로고
    • Selective matrix metalloproteinase (MMP) inhibitors in cancer therapy: Ready for prime time?
    • COI: 1:CAS:528:DC%2BC3cXpsFKhurY%3D, PID: 19959934
    • Zucker, S., & Cao, J. (2009). Selective matrix metalloproteinase (MMP) inhibitors in cancer therapy: Ready for prime time? Cancer Biology and Therapy, 8(24), 2371–3.
    • (2009) Cancer Biology and Therapy , vol.8 , Issue.24 , pp. 2371-2373
    • Zucker, S.1    Cao, J.2
  • 11
    • 70449732503 scopus 로고    scopus 로고
    • Matrix metalloproteinases as novel biomarkers and potential therapeutic targets in human cancer
    • COI: 1:CAS:528:DC%2BD1MXhsFahsLnP, PID: 19738110
    • Roy, R., Yang, J., & Moses, M. A. (2009). Matrix metalloproteinases as novel biomarkers and potential therapeutic targets in human cancer. Journal of Clinical Oncology, 27(31), 5287–97. doi:10.1200/JCO.2009.23.5556.
    • (2009) Journal of Clinical Oncology , vol.27 , Issue.31 , pp. 5287-5297
    • Roy, R.1    Yang, J.2    Moses, M.A.3
  • 12
    • 77149164774 scopus 로고    scopus 로고
    • Matrix metalloproteinases: what do they not do? New substrates and biological roles identified by murine models and proteomics
    • COI: 1:CAS:528:DC%2BC3cXitVKitL8%3D, PID: 19800373
    • Rodriguez, D., Morrison, C. J., & Overall, C. M. (2010). Matrix metalloproteinases: what do they not do? New substrates and biological roles identified by murine models and proteomics. Biochimica et Biophysica Acta, 1803(1), 39–54. doi:10.1016/j.bbamcr.2009.09.015.
    • (2010) Biochimica et Biophysica Acta , vol.1803 , Issue.1 , pp. 39-54
    • Rodriguez, D.1    Morrison, C.J.2    Overall, C.M.3
  • 13
    • 33847276695 scopus 로고    scopus 로고
    • In search of partners: Linking extracellular proteases to substrates
    • COI: 1:CAS:528:DC%2BD2sXitVGrsrs%3D, PID: 17299501
    • Overall, C. M., & Blobel, C. P. (2007). In search of partners: Linking extracellular proteases to substrates. Nature Reviews Molecular Cell Biology, 8(3), 245–57. doi:10.1038/nrm2120.
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.3 , pp. 245-257
    • Overall, C.M.1    Blobel, C.P.2
  • 14
    • 34648815810 scopus 로고    scopus 로고
    • Emerging roles of proteases in tumour suppression
    • COI: 1:CAS:528:DC%2BD2sXhtVOnsr3I, PID: 17851543
    • Lopez-Otin, C., & Matrisian, L. M. (2007). Emerging roles of proteases in tumour suppression. Nature Reviews Cancer, 7(10), 800–8. doi:10.1038/nrc2228.
    • (2007) Nature Reviews Cancer , vol.7 , Issue.10 , pp. 800-808
    • Lopez-Otin, C.1    Matrisian, L.M.2
  • 15
    • 74049088595 scopus 로고    scopus 로고
    • MT1-MMP is required for myeloid cell fusion via regulation of Rac1 signaling
    • COI: 1:CAS:528:DC%2BC3cXkvVWhs7g%3D, PID: 20152179
    • Gonzalo, P., Guadamillas, M. C., Hernandez-Riquer, M. V., Pollan, A., Grande-Garcia, A., Bartolome, R. A., et al. (2010). MT1-MMP is required for myeloid cell fusion via regulation of Rac1 signaling. Developmental Cell, 18(1), 77–89. doi:10.1016/j.devcel.2009.11.012.
    • (2010) Developmental Cell , vol.18 , Issue.1 , pp. 77-89
    • Gonzalo, P.1    Guadamillas, M.C.2    Hernandez-Riquer, M.V.3    Pollan, A.4    Grande-Garcia, A.5    Bartolome, R.A.6
  • 16
    • 84876245148 scopus 로고    scopus 로고
    • The hemopexin domain of MMP3 is responsible for mammary epithelial invasion and morphogenesis through extracellular interaction with HSP90beta
    • COI: 1:CAS:528:DC%2BC3sXnt1Wkt74%3D, PID: 23592797
    • Correia, A. L., Mori, H., Chen, E. I., Schmitt, F. C., & Bissell, M. J. (2013). The hemopexin domain of MMP3 is responsible for mammary epithelial invasion and morphogenesis through extracellular interaction with HSP90beta. Genes and Development, 27(7), 805–17. doi:10.1101/gad.211383.112.
    • (2013) Genes and Development , vol.27 , Issue.7 , pp. 805-817
    • Correia, A.L.1    Mori, H.2    Chen, E.I.3    Schmitt, F.C.4    Bissell, M.J.5
  • 18
    • 0029030448 scopus 로고
    • Matrilysin-inhibitor complexes: Common themes among metalloproteases
    • COI: 1:CAS:528:DyaK2MXls1yluro%3D, PID: 7756291
    • Browner, M. F., Smith, W. W., & Castelhano, A. L. (1995). Matrilysin-inhibitor complexes: Common themes among metalloproteases. Biochemistry, 34(20), 6602–10.
    • (1995) Biochemistry , vol.34 , Issue.20 , pp. 6602-6610
    • Browner, M.F.1    Smith, W.W.2    Castelhano, A.L.3
  • 19
    • 3142738143 scopus 로고    scopus 로고
    • New beginnings for matrix metalloproteinase inhibitors: Identification of high-affinity zinc-binding groups
    • COI: 1:CAS:528:DC%2BD2cXkvFyit7Y%3D, PID: 15237990
    • Puerta, D. T., Lewis, J. A., & Cohen, S. M. (2004). New beginnings for matrix metalloproteinase inhibitors: Identification of high-affinity zinc-binding groups. Journal of the American Chemical Society, 126(27), 8388–9. doi:10.1021/ja0485513.
    • (2004) Journal of the American Chemical Society , vol.126 , Issue.27 , pp. 8388-8389
    • Puerta, D.T.1    Lewis, J.A.2    Cohen, S.M.3
  • 20
    • 0024318368 scopus 로고
    • Pump-1 cDNA codes for a protein with characteristics similar to those of classical collagenase family members
    • COI: 1:CAS:528:DyaL1MXktFymu70%3D, PID: 2550050
    • Quantin, B., Murphy, G., & Breathnach, R. (1989). Pump-1 cDNA codes for a protein with characteristics similar to those of classical collagenase family members. Biochemistry, 28(13), 5327–34.
    • (1989) Biochemistry , vol.28 , Issue.13 , pp. 5327-5334
    • Quantin, B.1    Murphy, G.2    Breathnach, R.3
  • 21
    • 0030581634 scopus 로고    scopus 로고
    • Macrophage metalloelastase degrades matrix and myelin proteins and processes a tumour necrosis factor-alpha fusion protein
    • COI: 1:CAS:528:DyaK28XmvVOrs7k%3D, PID: 8920930
    • Chandler, S., Cossins, J., Lury, J., & Wells, G. (1996). Macrophage metalloelastase degrades matrix and myelin proteins and processes a tumour necrosis factor-alpha fusion protein. Biochemical and Biophysical Research Communications, 228(2), 421–9. doi:10.1006/bbrc.1996.1677.
    • (1996) Biochemical and Biophysical Research Communications , vol.228 , Issue.2 , pp. 421-429
    • Chandler, S.1    Cossins, J.2    Lury, J.3    Wells, G.4
  • 22
    • 34548670257 scopus 로고    scopus 로고
    • Crystal structures of MMP-9 complexes with five inhibitors: Contribution of the flexible Arg424 side-chain to selectivity
    • COI: 1:CAS:528:DC%2BD2sXot12rur4%3D, PID: 17599356
    • Tochowicz, A., Maskos, K., Huber, R., Oltenfreiter, R., Dive, V., Yiotakis, A., et al. (2007). Crystal structures of MMP-9 complexes with five inhibitors: Contribution of the flexible Arg424 side-chain to selectivity. Journal of Molecular Biology, 371(4), 989–1006. doi:10.1016/j.jmb.2007.05.068.
    • (2007) Journal of Molecular Biology , vol.371 , Issue.4 , pp. 989-1006
    • Tochowicz, A.1    Maskos, K.2    Huber, R.3    Oltenfreiter, R.4    Dive, V.5    Yiotakis, A.6
  • 23
    • 67149115144 scopus 로고    scopus 로고
    • DFT studies of the ring-opening mechanism of SB-3CT, a potent inhibitor of matrix metalloproteinase 2
    • COI: 1:CAS:528:DC%2BD1MXlvFWntL8%3D, PID: 19445474
    • Tao, P., Fisher, J. F., Mobashery, S., & Schlegel, H. B. (2009). DFT studies of the ring-opening mechanism of SB-3CT, a potent inhibitor of matrix metalloproteinase 2. Organic Letters, 11(12), 2559–62. doi:10.1021/ol9008393.
    • (2009) Organic Letters , vol.11 , Issue.12 , pp. 2559-2562
    • Tao, P.1    Fisher, J.F.2    Mobashery, S.3    Schlegel, H.B.4
  • 24
    • 0035907387 scopus 로고    scopus 로고
    • X-ray absorption studies of human matrix metalloproteinase-2 (MMP-2) bound to a highly selective mechanism-based inhibitor. Comparison with the latent and active forms of the enzyme
    • COI: 1:CAS:528:DC%2BD3MXjvFGitrY%3D, PID: 11278946
    • Kleifeld, O., Kotra, L. P., Gervasi, D. C., Brown, S., Bernardo, M. M., Fridman, R., et al. (2001). X-ray absorption studies of human matrix metalloproteinase-2 (MMP-2) bound to a highly selective mechanism-based inhibitor. Comparison with the latent and active forms of the enzyme. Journal of Biological Chemistry, 276(20), 17125–31.
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.20 , pp. 17125-17131
    • Kleifeld, O.1    Kotra, L.P.2    Gervasi, D.C.3    Brown, S.4    Bernardo, M.M.5    Fridman, R.6
  • 25
    • 84894947633 scopus 로고    scopus 로고
    • Role of L1 cell adhesion molecule (L1CAM) in the metastatic cascade: Promotion of dissemination, colonization, and metastatic growth
    • COI: 1:CAS:528:DC%2BC2cXhtVOmsbY%3D, PID: 24002299
    • Weinspach, D., Seubert, B., Schaten, S., Honert, K., Sebens, S., Altevogt, P., et al. (2014). Role of L1 cell adhesion molecule (L1CAM) in the metastatic cascade: Promotion of dissemination, colonization, and metastatic growth. Clinical and Experimental Metastasis, 31(1), 87–100. doi:10.1007/s10585-013-9613-6.
    • (2014) Clinical and Experimental Metastasis , vol.31 , Issue.1 , pp. 87-100
    • Weinspach, D.1    Seubert, B.2    Schaten, S.3    Honert, K.4    Sebens, S.5    Altevogt, P.6
  • 26
    • 33646352955 scopus 로고    scopus 로고
    • Inhibition of human prostate cancer growth, osteolysis and angiogenesis in a bone metastasis model by a novel mechanism-based selective gelatinase inhibitor
    • COI: 1:CAS:528:DC%2BD28Xks1Sis7s%3D
    • Bonfil, R. D., Sabbota, A., Nabha, S., Bernardo, M. M., Dong, Z., Meng, H., et al. (2006). Inhibition of human prostate cancer growth, osteolysis and angiogenesis in a bone metastasis model by a novel mechanism-based selective gelatinase inhibitor. International Journal of Cancer, 118(11), 2721–6.
    • (2006) International Journal of Cancer , vol.118 , Issue.11 , pp. 2721-2726
    • Bonfil, R.D.1    Sabbota, A.2    Nabha, S.3    Bernardo, M.M.4    Dong, Z.5    Meng, H.6
  • 27
    • 84886547274 scopus 로고    scopus 로고
    • O-phenyl carbamate and phenyl urea thiiranes as selective matrix metalloproteinase-2 inhibitors that cross the blood–brain barrier
    • COI: 1:CAS:528:DC%2BC3sXhsVeksbrF, PID: 24028490
    • Gooyit, M., Song, W., Mahasenan, K. V., Lichtenwalter, K., Suckow, M. A., Schroeder, V. A., et al. (2013). O-phenyl carbamate and phenyl urea thiiranes as selective matrix metalloproteinase-2 inhibitors that cross the blood–brain barrier. Journal of Medicinal Chemistry, 56(20), 8139–50. doi:10.1021/jm401217d.
    • (2013) Journal of Medicinal Chemistry , vol.56 , Issue.20 , pp. 8139-8150
    • Gooyit, M.1    Song, W.2    Mahasenan, K.V.3    Lichtenwalter, K.4    Suckow, M.A.5    Schroeder, V.A.6
  • 29
    • 79959748552 scopus 로고    scopus 로고
    • Biphenyl sulfonylamino methyl bisphosphonic acids as inhibitors of matrix metalloproteinases and bone resorption
    • COI: 1:CAS:528:DC%2BC3MXotVCmurg%3D, PID: 21714093
    • Rubino, M. T., Agamennone, M., Campestre, C., Campiglia, P., Cremasco, V., Faccio, R., et al. (2011). Biphenyl sulfonylamino methyl bisphosphonic acids as inhibitors of matrix metalloproteinases and bone resorption. ChemMedChem, 6(7), 1258–68. doi:10.1002/cmdc.201000540.
    • (2011) ChemMedChem , vol.6 , Issue.7 , pp. 1258-1268
    • Rubino, M.T.1    Agamennone, M.2    Campestre, C.3    Campiglia, P.4    Cremasco, V.5    Faccio, R.6
  • 30
    • 84855392626 scopus 로고    scopus 로고
    • An osteoblast-derived proteinase controls tumor cell survival via TGF-beta activation in the bone microenvironment
    • COI: 1:CAS:528:DC%2BC38XptF2qtw%3D%3D, PID: 22238668
    • Thiolloy, S., Edwards, J. R., Fingleton, B., Rifkin, D. B., Matrisian, L. M., & Lynch, C. C. (2012). An osteoblast-derived proteinase controls tumor cell survival via TGF-beta activation in the bone microenvironment. PloS One, 7(1), e29862. doi:10.1371/journal.pone.0029862PONE-D-11-14696.
    • (2012) PloS One , vol.7 , Issue.1 , pp. e29862
    • Thiolloy, S.1    Edwards, J.R.2    Fingleton, B.3    Rifkin, D.B.4    Matrisian, L.M.5    Lynch, C.C.6
  • 32
    • 0348109450 scopus 로고    scopus 로고
    • The growing impact of click chemistry on drug discovery
    • COI: 1:CAS:528:DC%2BD3sXpvVWkuro%3D, PID: 14678739
    • Kolb, H. C., & Sharpless, K. B. (2003). The growing impact of click chemistry on drug discovery. Drug Discovery Today, 8(24), 1128–37.
    • (2003) Drug Discovery Today , vol.8 , Issue.24 , pp. 1128-1137
    • Kolb, H.C.1    Sharpless, K.B.2
  • 33
    • 0037087516 scopus 로고    scopus 로고
    • Click chemistry in situ: acetylcholinesterase as a reaction vessel for the selective assembly of a femtomolar inhibitor from an array of building blocks
    • COI: 1:CAS:528:DC%2BD38XisVeisbo%3D, PID: 12491310
    • Lewis, W. G., Green, L. G., Grynszpan, F., Radic, Z., Carlier, P. R., Taylor, P., et al. (2002). Click chemistry in situ: acetylcholinesterase as a reaction vessel for the selective assembly of a femtomolar inhibitor from an array of building blocks. Angewandte Chemie, 41(6), 1053–7.
    • (2002) Angewandte Chemie , vol.41 , Issue.6 , pp. 1053-1057
    • Lewis, W.G.1    Green, L.G.2    Grynszpan, F.3    Radic, Z.4    Carlier, P.R.5    Taylor, P.6
  • 34
    • 60949098929 scopus 로고    scopus 로고
    • In situ “click” assembly of small molecule matrix metalloprotease inhibitors containing zinc-chelating groups
    • COI: 1:CAS:528:DC%2BD1cXhsVWks7%2FE, PID: 19053720
    • Hu, M., Li, J., & Yao, S. Q. (2008). In situ “click” assembly of small molecule matrix metalloprotease inhibitors containing zinc-chelating groups. Organic Letters, 10(24), 5529–31. doi:10.1021/ol802286g.
    • (2008) Organic Letters , vol.10 , Issue.24 , pp. 5529-5531
    • Hu, M.1    Li, J.2    Yao, S.Q.3
  • 35
    • 52549108229 scopus 로고    scopus 로고
    • Imaging matrix metalloproteinases in cancer
    • PID: 18465089
    • Scherer, R. L., McIntyre, J. O., & Matrisian, L. M. (2008). Imaging matrix metalloproteinases in cancer. Cancer and Metastasis Reviews, 27(4), 679–90. doi:10.1007/s10555-008-9152-9.
    • (2008) Cancer and Metastasis Reviews , vol.27 , Issue.4 , pp. 679-690
    • Scherer, R.L.1    McIntyre, J.O.2    Matrisian, L.M.3
  • 36
    • 84897856218 scopus 로고    scopus 로고
    • Paclitaxel: Biosynthesis, production and future prospects
    • COI: 1:CAS:528:DC%2BC2cXntVequr0%3D, PID: 24614567
    • Howat, S., Park, B., Oh, I. S., Jin, Y. W., Lee, E. K., & Loake, G. J. (2014). Paclitaxel: Biosynthesis, production and future prospects. New Biotechnology, 31(3), 242–5. doi:10.1016/j.nbt.2014.02.010.
    • (2014) New Biotechnology , vol.31 , Issue.3 , pp. 242-245
    • Howat, S.1    Park, B.2    Oh, I.S.3    Jin, Y.W.4    Lee, E.K.5    Loake, G.J.6
  • 37
    • 79251609692 scopus 로고    scopus 로고
    • Using tetracyclines to treat osteoporotic/osteopenic bone loss: from the basic science laboratory to the clinic
    • COI: 1:CAS:528:DC%2BC3MXht1yntLc%3D
    • Payne, J. B., & Golub, L. M. (2011). Using tetracyclines to treat osteoporotic/osteopenic bone loss: from the basic science laboratory to the clinic. Pharmacological Research: The Official Journal of the Italian Pharmacological Society, 63(2), 121–9. doi:10.1016/j.phrs.2010.10.006.
    • (2011) Pharmacological Research: The Official Journal of the Italian Pharmacological Society , vol.63 , Issue.2 , pp. 121-129
    • Payne, J.B.1    Golub, L.M.2
  • 38
    • 1642515727 scopus 로고    scopus 로고
    • CMT-3. CollaGenex
    • COI: 1:CAS:528:DC%2BD2cXht1eqtb0%3D, PID: 14763133
    • Fingleton, B. (2003). CMT-3. CollaGenex. Current Opinion in Investigational Drugs, 4(12), 1460–7.
    • (2003) Current Opinion in Investigational Drugs , vol.4 , Issue.12 , pp. 1460-1467
    • Fingleton, B.1
  • 39
    • 33744718737 scopus 로고    scopus 로고
    • COL-3 benefits patients with AIDS-related Kaposi’s sarcoma
    • PID: 16696161
    • Furlow, B. (2006). COL-3 benefits patients with AIDS-related Kaposi’s sarcoma. The Lancet Oncology, 7(5), 368.
    • (2006) The Lancet Oncology , vol.7 , Issue.5 , pp. 368
    • Furlow, B.1
  • 40
    • 84863183193 scopus 로고    scopus 로고
    • Antimetastasis effect of anthraquinones from marine fungus, Microsporum sp
    • PID: 22361203
    • Zhang, C., & Kim, S. K. (2012). Antimetastasis effect of anthraquinones from marine fungus, Microsporum sp. Advances in Food and Nutrition Research, 65, 415–21. doi:10.1016/B978-0-12-416003-3.00027-5.
    • (2012) Advances in Food and Nutrition Research , vol.65 , pp. 415-421
    • Zhang, C.1    Kim, S.K.2
  • 41
    • 4444331025 scopus 로고    scopus 로고
    • Activation of protein kinase C betaII/epsilon-c-Jun NH2-terminal kinase pathway and inhibition of mitogen-activated protein/extracellular signal-regulated kinase 1/2 phosphorylation in antitumor invasive activity induced by the polymethoxy flavonoid, nobiletin
    • COI: 1:CAS:528:DC%2BD2cXls1amsrs%3D, PID: 15252145
    • Miyata, Y., Sato, T., Yano, M., & Ito, A. (2004). Activation of protein kinase C betaII/epsilon-c-Jun NH2-terminal kinase pathway and inhibition of mitogen-activated protein/extracellular signal-regulated kinase 1/2 phosphorylation in antitumor invasive activity induced by the polymethoxy flavonoid, nobiletin. Molecular Cancer Therapeutics, 3(7), 839–47.
    • (2004) Molecular Cancer Therapeutics , vol.3 , Issue.7 , pp. 839-847
    • Miyata, Y.1    Sato, T.2    Yano, M.3    Ito, A.4
  • 42
    • 0035070354 scopus 로고    scopus 로고
    • Evaluation of the effects of swainsonine, captopril, tangeretin and nobiletin on the biological behaviour of brain tumour cells in vitro
    • COI: 1:CAS:528:DC%2BD3MXjtFKnurY%3D, PID: 11299000
    • Rooprai, H. K., Kandanearatchi, A., Maidment, S. L., Christidou, M., Trillo-Pazos, G., Dexter, D. T., et al. (2001). Evaluation of the effects of swainsonine, captopril, tangeretin and nobiletin on the biological behaviour of brain tumour cells in vitro. Neuropathology and Applied Neurobiology, 27(1), 29–39.
    • (2001) Neuropathology and Applied Neurobiology , vol.27 , Issue.1 , pp. 29-39
    • Rooprai, H.K.1    Kandanearatchi, A.2    Maidment, S.L.3    Christidou, M.4    Trillo-Pazos, G.5    Dexter, D.T.6
  • 43
    • 33748803350 scopus 로고    scopus 로고
    • Citrus auraptene targets translation of MMP-7 (matrilysin) via ERK1/2-dependent and mTOR-independent mechanism
    • COI: 1:CAS:528:DC%2BD28XpvFGntLc%3D, PID: 16979634
    • Kawabata, K., Murakami, A., & Ohigashi, H. (2006). Citrus auraptene targets translation of MMP-7 (matrilysin) via ERK1/2-dependent and mTOR-independent mechanism. FEBS Letters, 580(22), 5288–94. doi:10.1016/j.febslet.2006.08.072.
    • (2006) FEBS Letters , vol.580 , Issue.22 , pp. 5288-5294
    • Kawabata, K.1    Murakami, A.2    Ohigashi, H.3
  • 44
    • 0035673312 scopus 로고    scopus 로고
    • The citrus flavonoid, nobiletin, inhibits peritoneal dissemination of human gastric carcinoma in SCID mice
    • COI: 1:CAS:528:DC%2BD38XhtV2jtLw%3D, PID: 11749698
    • Minagawa, A., Otani, Y., Kubota, T., Wada, N., Furukawa, T., Kumai, K., et al. (2001). The citrus flavonoid, nobiletin, inhibits peritoneal dissemination of human gastric carcinoma in SCID mice. Japanese Journal of Cancer Research: Gann, 92(12), 1322–8.
    • (2001) Japanese Journal of Cancer Research: Gann , vol.92 , Issue.12 , pp. 1322-1328
    • Minagawa, A.1    Otani, Y.2    Kubota, T.3    Wada, N.4    Furukawa, T.5    Kumai, K.6
  • 45
    • 0031855920 scopus 로고    scopus 로고
    • Genistein inhibits both constitutive and EGF-stimulated invasion in ER-negative human breast carcinoma cell lines
    • COI: 1:CAS:528:DyaK1cXltF2ks7Y%3D, PID: 9673352
    • Shao, Z. M., Wu, J., Shen, Z. Z., & Barsky, S. H. (1998). Genistein inhibits both constitutive and EGF-stimulated invasion in ER-negative human breast carcinoma cell lines. Anticancer Research, 18(3A), 1435–9.
    • (1998) Anticancer Research , vol.18 , Issue.3A , pp. 1435-1439
    • Shao, Z.M.1    Wu, J.2    Shen, Z.Z.3    Barsky, S.H.4
  • 46
    • 22844432461 scopus 로고    scopus 로고
    • Genistein suppresses the invasive potential of human breast cancer cells through transcriptional regulation of metalloproteinases and their tissue inhibitors
    • COI: 1:CAS:528:DC%2BD2MXjtFeltrg%3D, PID: 15754008
    • Kousidou, O. C., Mitropoulou, T. N., Roussidis, A. E., Kletsas, D., Theocharis, A. D., & Karamanos, N. K. (2005). Genistein suppresses the invasive potential of human breast cancer cells through transcriptional regulation of metalloproteinases and their tissue inhibitors. International Journal of Oncology, 26(4), 1101–9.
    • (2005) International Journal of Oncology , vol.26 , Issue.4 , pp. 1101-1109
    • Kousidou, O.C.1    Mitropoulou, T.N.2    Roussidis, A.E.3    Kletsas, D.4    Theocharis, A.D.5    Karamanos, N.K.6
  • 47
    • 34547829030 scopus 로고    scopus 로고
    • Silibinin inhibits constitutive activation of Stat3, and causes caspase activation and apoptotic death of human prostate carcinoma DU145 cells
    • COI: 1:CAS:528:DC%2BD2sXos12itr8%3D, PID: 17341659
    • Agarwal, C., Tyagi, A., Kaur, M., & Agarwal, R. (2007). Silibinin inhibits constitutive activation of Stat3, and causes caspase activation and apoptotic death of human prostate carcinoma DU145 cells. Carcinogenesis, 28(7), 1463–70. doi:10.1093/carcin/bgm042.
    • (2007) Carcinogenesis , vol.28 , Issue.7 , pp. 1463-1470
    • Agarwal, C.1    Tyagi, A.2    Kaur, M.3    Agarwal, R.4
  • 48
    • 33845941617 scopus 로고    scopus 로고
    • Anticancer potential of silymarin: from bench to bed side
    • COI: 1:CAS:528:DC%2BD2sXpslGjtQ%3D%3D, PID: 17201169
    • Agarwal, R., Agarwal, C., Ichikawa, H., Singh, R. P., & Aggarwal, B. B. (2006). Anticancer potential of silymarin: from bench to bed side. Anticancer Research, 26(6B), 4457–98.
    • (2006) Anticancer Research , vol.26 , Issue.6B , pp. 4457-4498
    • Agarwal, R.1    Agarwal, C.2    Ichikawa, H.3    Singh, R.P.4    Aggarwal, B.B.5
  • 49
    • 34248173053 scopus 로고    scopus 로고
    • Matrix proteases, green tea, and St. John’s wort: biomedical research catches up with folk medicine
    • PID: 17382921
    • Dell’Aica, I., Caniato, R., Biggin, S., & Garbisa, S. (2007). Matrix proteases, green tea, and St. John’s wort: biomedical research catches up with folk medicine. Clinica Chimica Acta; International Journal of Clinical Chemistry, 381(1), 69–77. doi:10.1016/j.cca.2007.02.022.
    • (2007) Clinica Chimica Acta; International Journal of Clinical Chemistry , vol.381 , Issue.1 , pp. 69-77
    • Dell’Aica, I.1    Caniato, R.2    Biggin, S.3    Garbisa, S.4
  • 50
    • 2542421799 scopus 로고    scopus 로고
    • (−)-Epigallocatechin gallate inhibits membrane-type 1 matrix metalloproteinase, MT1-MMP, and tumor angiogenesis
    • COI: 1:CAS:528:DC%2BD2cXksVCisLY%3D, PID: 15172120
    • Yamakawa, S., Asai, T., Uchida, T., Matsukawa, M., Akizawa, T., & Oku, N. (2004). (−)-Epigallocatechin gallate inhibits membrane-type 1 matrix metalloproteinase, MT1-MMP, and tumor angiogenesis. Cancer Letters, 210(1), 47–55. doi:10.1016/j.canlet.2004.03.008.
    • (2004) Cancer Letters , vol.210 , Issue.1 , pp. 47-55
    • Yamakawa, S.1    Asai, T.2    Uchida, T.3    Matsukawa, M.4    Akizawa, T.5    Oku, N.6
  • 51
    • 12344318082 scopus 로고    scopus 로고
    • Anti-angiogenic activity of resveratrol, a natural compound from medicinal plants
    • COI: 1:CAS:528:DC%2BD2cXhtFCqtbnI, PID: 15621628
    • Cao, Y., Fu, Z. D., Wang, F., Liu, H. Y., & Han, R. (2005). Anti-angiogenic activity of resveratrol, a natural compound from medicinal plants. Journal of Asian Natural Products Research, 7(3), 205–13. doi:10.1080/10286020410001690190.
    • (2005) Journal of Asian Natural Products Research , vol.7 , Issue.3 , pp. 205-213
    • Cao, Y.1    Fu, Z.D.2    Wang, F.3    Liu, H.Y.4    Han, R.5
  • 53
    • 1842482424 scopus 로고    scopus 로고
    • Resveratrol inhibits phorbol myristate acetate-induced matrix metalloproteinase-9 expression by inhibiting JNK and PKC delta signal transduction
    • COI: 1:CAS:528:DC%2BD2cXhvFOiu78%3D, PID: 14661062
    • Woo, J. H., Lim, J. H., Kim, Y. H., Suh, S. I., Min, D. S., Chang, J. S., et al. (2004). Resveratrol inhibits phorbol myristate acetate-induced matrix metalloproteinase-9 expression by inhibiting JNK and PKC delta signal transduction. Oncogene, 23(10), 1845–53. doi:10.1038/sj.onc.1207307.
    • (2004) Oncogene , vol.23 , Issue.10 , pp. 1845-1853
    • Woo, J.H.1    Lim, J.H.2    Kim, Y.H.3    Suh, S.I.4    Min, D.S.5    Chang, J.S.6
  • 54
    • 3042778748 scopus 로고    scopus 로고
    • Proanthocyanidins from grape seeds inhibit expression of matrix metalloproteinases in human prostate carcinoma cells, which is associated with the inhibition of activation of MAPK and NF kappa B
    • COI: 1:CAS:528:DC%2BD2cXksVahtL4%3D, PID: 14742313
    • Vayalil, P. K., Mittal, A., & Katiyar, S. K. (2004). Proanthocyanidins from grape seeds inhibit expression of matrix metalloproteinases in human prostate carcinoma cells, which is associated with the inhibition of activation of MAPK and NF kappa B. Carcinogenesis, 25(6), 987–95. doi:10.1093/carcin/bgh095.
    • (2004) Carcinogenesis , vol.25 , Issue.6 , pp. 987-995
    • Vayalil, P.K.1    Mittal, A.2    Katiyar, S.K.3
  • 55
    • 33847045962 scopus 로고    scopus 로고
    • Inhibition of host extracellular matrix destructive enzyme production and activity by a high-molecular-weight cranberry fraction
    • COI: 1:CAS:528:DC%2BD2sXksFKmtbg%3D, PID: 17305875
    • Bodet, C., Chandad, F., & Grenier, D. (2007). Inhibition of host extracellular matrix destructive enzyme production and activity by a high-molecular-weight cranberry fraction. Journal of Periodontal Research, 42(2), 159–68. doi:10.1111/j.1600-0765.2006.00929.x.
    • (2007) Journal of Periodontal Research , vol.42 , Issue.2 , pp. 159-168
    • Bodet, C.1    Chandad, F.2    Grenier, D.3
  • 56
    • 3042558087 scopus 로고    scopus 로고
    • Effect of curcumin on gelatinase A (MMP-2) activity in B16F10 melanoma cells
    • COI: 1:CAS:528:DC%2BD2cXlt1Wgtbc%3D, PID: 15219947
    • Banerji, A., Chakrabarti, J., Mitra, A., & Chatterjee, A. (2004). Effect of curcumin on gelatinase A (MMP-2) activity in B16F10 melanoma cells. Cancer Letters, 211(2), 235–42. doi:10.1016/j.canlet.2004.02.007.
    • (2004) Cancer Letters , vol.211 , Issue.2 , pp. 235-242
    • Banerji, A.1    Chakrabarti, J.2    Mitra, A.3    Chatterjee, A.4
  • 57
    • 0031813252 scopus 로고    scopus 로고
    • Curcumin inhibits SK-Hep-1 hepatocellular carcinoma cell invasion in vitro and suppresses matrix metalloproteinase-9 secretion
    • COI: 1:CAS:528:DyaK1cXktVejs7w%3D
    • Lin, L. I., Ke, Y. F., Ko, Y. C., & Lin, J. K. (1998). Curcumin inhibits SK-Hep-1 hepatocellular carcinoma cell invasion in vitro and suppresses matrix metalloproteinase-9 secretion. Oncology (Williston Park), 55(4), 349–53.
    • (1998) Oncology (Williston Park) , vol.55 , Issue.4 , pp. 349-353
    • Lin, L.I.1    Ke, Y.F.2    Ko, Y.C.3    Lin, J.K.4
  • 58
    • 9144231812 scopus 로고    scopus 로고
    • Anti-invasive gene expression profile of curcumin in lung adenocarcinoma based on a high throughput microarray analysis
    • COI: 1:CAS:528:DC%2BD2cXivVChsr0%3D, PID: 14722241
    • Chen, H. W., Yu, S. L., Chen, J. J., Li, H. N., Lin, Y. C., Yao, P. L., et al. (2004). Anti-invasive gene expression profile of curcumin in lung adenocarcinoma based on a high throughput microarray analysis. Molecular Pharmacology, 65(1), 99–110. doi:10.1124/mol.65.1.99.
    • (2004) Molecular Pharmacology , vol.65 , Issue.1 , pp. 99-110
    • Chen, H.W.1    Yu, S.L.2    Chen, J.J.3    Li, H.N.4    Lin, Y.C.5    Yao, P.L.6
  • 59
    • 34548312355 scopus 로고    scopus 로고
    • Depolymerized products of lambda-carrageenan as a potent angiogenesis inhibitor
    • COI: 1:CAS:528:DC%2BD2sXot1Gksrc%3D, PID: 17661479
    • Chen, H., Yan, X., Lin, J., Wang, F., & Xu, W. (2007). Depolymerized products of lambda-carrageenan as a potent angiogenesis inhibitor. Journal of Agricultural and Food Chemistry, 55(17), 6910–7. doi:10.1021/jf070183+.
    • (2007) Journal of Agricultural and Food Chemistry , vol.55 , Issue.17 , pp. 6910-6917
    • Chen, H.1    Yan, X.2    Lin, J.3    Wang, F.4    Xu, W.5
  • 60
  • 61
    • 34047252538 scopus 로고    scopus 로고
    • Natural bio-drugs as matrix metalloproteinase inhibitors: New perspectives on the horizon?
    • COI: 1:CAS:528:DC%2BD28XhsFWrtrk%3D, PID: 18221029
    • Mannello, F. (2006). Natural bio-drugs as matrix metalloproteinase inhibitors: New perspectives on the horizon? Recent Patents on Anti-Cancer Drug Discovery, 1(1), 91–103.
    • (2006) Recent Patents on Anti-Cancer Drug Discovery , vol.1 , Issue.1 , pp. 91-103
    • Mannello, F.1
  • 62
    • 4043116451 scopus 로고    scopus 로고
    • AE-941 (AEterna)
    • COI: 1:CAS:528:DC%2BD2cXnt1Srsbg%3D, PID: 15242256
    • Dredge, K. (2004). AE-941 (AEterna). Current Opinion in Investigational Drugs, 5(6), 668–77.
    • (2004) Current Opinion in Investigational Drugs , vol.5 , Issue.6 , pp. 668-677
    • Dredge, K.1
  • 63
    • 79952066487 scopus 로고    scopus 로고
    • Chemistry and biochemistry of dietary polyphenols
    • COI: 1:CAS:528:DC%2BC3cXhs1WiurfP, PID: 22254006
    • Tsao, R. (2010). Chemistry and biochemistry of dietary polyphenols. Nutrients, 2(12), 1231–46. doi:10.3390/nu2121231.
    • (2010) Nutrients , vol.2 , Issue.12 , pp. 1231-1246
    • Tsao, R.1
  • 64
    • 52049116999 scopus 로고    scopus 로고
    • Green tea catechins and cardiovascular health: an update
    • COI: 1:CAS:528:DC%2BD1cXovFWnsbg%3D, PID: 18691042
    • Babu, P. V., & Liu, D. (2008). Green tea catechins and cardiovascular health: an update. Current Medicinal Chemistry, 15(18), 1840–50.
    • (2008) Current Medicinal Chemistry , vol.15 , Issue.18 , pp. 1840-1850
    • Babu, P.V.1    Liu, D.2
  • 65
    • 0037196553 scopus 로고    scopus 로고
    • Green tea polyphenol (−)-epigallocatechin 3-gallate inhibits MMP-2 secretion and MT1-MMP-driven migration in glioblastoma cells
    • COI: 1:CAS:528:DC%2BD38Xhtlertr8%3D, PID: 11853893
    • Annabi, B., Lachambre, M. P., Bousquet-Gagnon, N., Page, M., Gingras, D., & Beliveau, R. (2002). Green tea polyphenol (−)-epigallocatechin 3-gallate inhibits MMP-2 secretion and MT1-MMP-driven migration in glioblastoma cells. Biochimica et Biophysica Acta, 1542(1–3), 209–20.
    • (2002) Biochimica et Biophysica Acta , vol.1542 , Issue.1-3 , pp. 209-220
    • Annabi, B.1    Lachambre, M.P.2    Bousquet-Gagnon, N.3    Page, M.4    Gingras, D.5    Beliveau, R.6
  • 66
    • 0034673682 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibition by green tea catechins
    • COI: 1:CAS:528:DC%2BD3cXhslalsrk%3D, PID: 10719174
    • Demeule, M., Brossard, M., Page, M., Gingras, D., & Beliveau, R. (2000). Matrix metalloproteinase inhibition by green tea catechins. Biochimica et Biophysica Acta, 1478(1), 51–60.
    • (2000) Biochimica et Biophysica Acta , vol.1478 , Issue.1 , pp. 51-60
    • Demeule, M.1    Brossard, M.2    Page, M.3    Gingras, D.4    Beliveau, R.5
  • 67
    • 0345733986 scopus 로고    scopus 로고
    • Ageladine A: an antiangiogenic matrixmetalloproteinase inhibitor from the marine sponge Agelas nakamurai
    • COI: 1:CAS:528:DC%2BD3sXptlOmu7g%3D, PID: 14677933
    • Fujita, M., Nakao, Y., Matsunaga, S., Seiki, M., Itoh, Y., Yamashita, J., et al. (2003). Ageladine A: an antiangiogenic matrixmetalloproteinase inhibitor from the marine sponge Agelas nakamurai. Journal of the American Chemical Society, 125(51), 15700–1. doi:10.1021/ja038025w.
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.51 , pp. 15700-15701
    • Fujita, M.1    Nakao, Y.2    Matsunaga, S.3    Seiki, M.4    Itoh, Y.5    Yamashita, J.6
  • 68
    • 79953767989 scopus 로고    scopus 로고
    • A one-pot synthesis and biological activity of ageladine A and analogues
    • COI: 1:CAS:528:DC%2BC3MXjsVClt7o%3D, PID: 21413800
    • Shengule, S. R., Loa-Kum-Cheung, W. L., Parish, C. R., Blairvacq, M., Meijer, L., Nakao, Y., et al. (2011). A one-pot synthesis and biological activity of ageladine A and analogues. Journal of Medicinal Chemistry, 54(7), 2492–503. doi:10.1021/jm200039m.
    • (2011) Journal of Medicinal Chemistry , vol.54 , Issue.7 , pp. 2492-2503
    • Shengule, S.R.1    Loa-Kum-Cheung, W.L.2    Parish, C.R.3    Blairvacq, M.4    Meijer, L.5    Nakao, Y.6
  • 69
    • 0035207897 scopus 로고    scopus 로고
    • Neovastat, a naturally occurring multifunctional antiangiogenic drug, in phase III clinical trials
    • COI: 1:CAS:528:DC%2BD38XjvVSmug%3D%3D, PID: 11740820
    • Falardeau, P., Champagne, P., Poyet, P., Hariton, C., & Dupont, E. (2001). Neovastat, a naturally occurring multifunctional antiangiogenic drug, in phase III clinical trials. Seminars in Oncology, 28(6), 620–5.
    • (2001) Seminars in Oncology , vol.28 , Issue.6 , pp. 620-625
    • Falardeau, P.1    Champagne, P.2    Poyet, P.3    Hariton, C.4    Dupont, E.5
  • 70
    • 77953695968 scopus 로고    scopus 로고
    • Chemoradiotherapy with or without AE-941 in stage III non-small cell lung cancer: a randomized phase III trial
    • COI: 1:CAS:528:DC%2BC3cXnvVyju7s%3D, PID: 20505152
    • Lu, C., Lee, J. J., Komaki, R., Herbst, R. S., Feng, L., Evans, W. K., et al. (2010). Chemoradiotherapy with or without AE-941 in stage III non-small cell lung cancer: a randomized phase III trial. Journal of the National Cancer Institute, 102(12), 859–65. doi:10.1093/jnci/djq179.
    • (2010) Journal of the National Cancer Institute , vol.102 , Issue.12 , pp. 859-865
    • Lu, C.1    Lee, J.J.2    Komaki, R.3    Herbst, R.S.4    Feng, L.5    Evans, W.K.6
  • 71
    • 20544458580 scopus 로고    scopus 로고
    • Evaluation of shark cartilage in patients with advanced cancer: a north central cancer treatment group trial
    • PID: 15912493
    • Loprinzi, C. L., Levitt, R., Barton, D. L., Sloan, J. A., Atherton, P. J., Smith, D. J., et al. (2005). Evaluation of shark cartilage in patients with advanced cancer: a north central cancer treatment group trial. Cancer, 104(1), 176–82. doi:10.1002/cncr.21107.
    • (2005) Cancer , vol.104 , Issue.1 , pp. 176-182
    • Loprinzi, C.L.1    Levitt, R.2    Barton, D.L.3    Sloan, J.A.4    Atherton, P.J.5    Smith, D.J.6
  • 72
    • 84899115962 scopus 로고    scopus 로고
    • Trial watch: Tumor-targeting monoclonal antibodies in cancer therapy
    • PID: 24605265
    • Vacchelli, E., Aranda, F., Eggermont, A., Galon, J., Sautes-Fridman, C., Zitvogel, L., et al. (2014). Trial watch: Tumor-targeting monoclonal antibodies in cancer therapy. Oncoimmunology, 3(1), e27048. doi:10.4161/onci.27048.
    • (2014) Oncoimmunology , vol.3 , Issue.1 , pp. e27048
    • Vacchelli, E.1    Aranda, F.2    Eggermont, A.3    Galon, J.4    Sautes-Fridman, C.5    Zitvogel, L.6
  • 74
    • 84861326986 scopus 로고    scopus 로고
    • Bevacizumab: Overview of the literature
    • COI: 1:CAS:528:DC%2BC38XntFOgsro%3D, PID: 22594892
    • Braghiroli, M. I., Sabbaga, J., & Hoff, P. M. (2012). Bevacizumab: Overview of the literature. Expert Review of Anticancer Therapy, 12(5), 567–80. doi:10.1586/era.12.13.
    • (2012) Expert Review of Anticancer Therapy , vol.12 , Issue.5 , pp. 567-580
    • Braghiroli, M.I.1    Sabbaga, J.2    Hoff, P.M.3
  • 75
    • 60649108677 scopus 로고    scopus 로고
    • Selective inhibition of matrix metalloproteinase-14 blocks tumor growth, invasion, and angiogenesis
    • COI: 1:CAS:528:DC%2BD1MXhslynsLg%3D, PID: 19208838
    • Devy, L., Huang, L., Naa, L., Yanamandra, N., Pieters, H., Frans, N., et al. (2009). Selective inhibition of matrix metalloproteinase-14 blocks tumor growth, invasion, and angiogenesis. Cancer Research, 69(4), 1517–26. doi:10.1158/0008-5472.CAN-08-3255.
    • (2009) Cancer Research , vol.69 , Issue.4 , pp. 1517-1526
    • Devy, L.1    Huang, L.2    Naa, L.3    Yanamandra, N.4    Pieters, H.5    Frans, N.6
  • 76
    • 84868596491 scopus 로고    scopus 로고
    • Development of a neutralizing antibody specific for the active form of matrix metalloproteinase-13
    • COI: 1:CAS:528:DC%2BC38XhsVyltbjJ, PID: 23050690
    • Naito, S., Takahashi, T., Onoda, J., Yamauchi, A., Kawai, T., Kishino, J., et al. (2012). Development of a neutralizing antibody specific for the active form of matrix metalloproteinase-13. Biochemistry, 51(44), 8877–84. doi:10.1021/bi301228d.
    • (2012) Biochemistry , vol.51 , Issue.44 , pp. 8877-8884
    • Naito, S.1    Takahashi, T.2    Onoda, J.3    Yamauchi, A.4    Kawai, T.5    Kishino, J.6
  • 77
    • 84890402516 scopus 로고    scopus 로고
    • A monoclonal antibody interferes with TIMP-2 binding and incapacitates the MMP-2-activating function of multifunctional, pro-tumorigenic MMP-14/MT1-MMP
    • COI: 1:CAS:528:DC%2BC3sXhvVyktbfE, PID: 24296749
    • Shiryaev, S. A., Remacle, A. G., Golubkov, V. S., Ingvarsen, S., Porse, A., Behrendt, N., et al. (2013). A monoclonal antibody interferes with TIMP-2 binding and incapacitates the MMP-2-activating function of multifunctional, pro-tumorigenic MMP-14/MT1-MMP. Oncogenesis, 2, e80. doi:10.1038/oncsis.2013.44.
    • (2013) Oncogenesis , vol.2 , pp. e80
    • Shiryaev, S.A.1    Remacle, A.G.2    Golubkov, V.S.3    Ingvarsen, S.4    Porse, A.5    Behrendt, N.6
  • 78
    • 33847171983 scopus 로고    scopus 로고
    • A rat monoclonal antibody that recognizes pro- and active MMP-7 indicates polarized expression in vivo
    • COI: 1:CAS:528:DC%2BD2sXhvF2iu7o%3D
    • Fingleton, B., Powell, W. C., Crawford, H. C., Couchman, J. R., & Matrisian, L. M. (2007). A rat monoclonal antibody that recognizes pro- and active MMP-7 indicates polarized expression in vivo. Hybridoma (Larchmt), 26(1), 22–7. doi:10.1089/hyb.2006.028.
    • (2007) Hybridoma (Larchmt) , vol.26 , Issue.1 , pp. 22-27
    • Fingleton, B.1    Powell, W.C.2    Crawford, H.C.3    Couchman, J.R.4    Matrisian, L.M.5
  • 79
    • 65549151760 scopus 로고    scopus 로고
    • Inflammatory and alternatively activated human macrophages attract vessel-associated stem cells, relying on separate HMGB1- and MMP-9-dependent pathways
    • COI: 1:CAS:528:DC%2BD1MXlvVCksrg%3D, PID: 19197071
    • Lolmede, K., Campana, L., Vezzoli, M., Bosurgi, L., Tonlorenzi, R., Clementi, E., et al. (2009). Inflammatory and alternatively activated human macrophages attract vessel-associated stem cells, relying on separate HMGB1- and MMP-9-dependent pathways. Journal of Leukocyte Biology, 85(5), 779–87. doi:10.1189/jlb.0908579.
    • (2009) Journal of Leukocyte Biology , vol.85 , Issue.5 , pp. 779-787
    • Lolmede, K.1    Campana, L.2    Vezzoli, M.3    Bosurgi, L.4    Tonlorenzi, R.5    Clementi, E.6
  • 80
    • 84855536559 scopus 로고    scopus 로고
    • Antibodies targeting the catalytic zinc complex of activated matrix metalloproteinases show therapeutic potential
    • COI: 1:CAS:528:DC%2BC3MXhs1OltbnN
    • Sela-Passwell, N., Kikkeri, R., Dym, O., Rozenberg, H., Margalit, R., Arad-Yellin, R., et al. (2012). Antibodies targeting the catalytic zinc complex of activated matrix metalloproteinases show therapeutic potential. Nature Medicine, 18(1), 143–7. doi:10.1038/nm.2582.
    • (2012) Nature Medicine , vol.18 , Issue.1 , pp. 143-147
    • Sela-Passwell, N.1    Kikkeri, R.2    Dym, O.3    Rozenberg, H.4    Margalit, R.5    Arad-Yellin, R.6
  • 81
    • 0034721850 scopus 로고    scopus 로고
    • Cysteine array matrix metalloproteinase (CA-MMP)/MMP-23 is a type II transmembrane matrix metalloproteinase regulated by a single cleavage for both secretion and activation
    • COI: 1:CAS:528:DC%2BD3cXnvVyjtb0%3D, PID: 10945999
    • Pei, D., Kang, T., & Qi, H. (2000). Cysteine array matrix metalloproteinase (CA-MMP)/MMP-23 is a type II transmembrane matrix metalloproteinase regulated by a single cleavage for both secretion and activation. The Journal of Biological Chemistry, 275(43), 33988–97. doi:10.1074/jbc.M006493200.
    • (2000) The Journal of Biological Chemistry , vol.275 , Issue.43 , pp. 33988-33997
    • Pei, D.1    Kang, T.2    Qi, H.3
  • 82
    • 0030756920 scopus 로고    scopus 로고
    • Membrane-type matrix metalloproteinases (MT-MMPs) in cell invasion
    • COI: 1:CAS:528:DyaK2sXktFeltLo%3D, PID: 9198203
    • Sato, H., Okada, Y., & Seiki, M. (1997). Membrane-type matrix metalloproteinases (MT-MMPs) in cell invasion. Thrombosis and Haemostasis, 78(1), 497–500.
    • (1997) Thrombosis and Haemostasis , vol.78 , Issue.1 , pp. 497-500
    • Sato, H.1    Okada, Y.2    Seiki, M.3
  • 83
    • 28444454893 scopus 로고    scopus 로고
    • MT1-MMP: a potent modifier of pericellular microenvironment
    • COI: 1:CAS:528:DC%2BD2MXht12gsLzF, PID: 15920734
    • Itoh, Y., & Seiki, M. (2006). MT1-MMP: a potent modifier of pericellular microenvironment. Journal of Cellular Physiology, 206(1), 1–8. doi:10.1002/jcp.20431.
    • (2006) Journal of Cellular Physiology , vol.206 , Issue.1 , pp. 1-8
    • Itoh, Y.1    Seiki, M.2
  • 84
    • 73949087260 scopus 로고    scopus 로고
    • Induction of a MT1-MMP and MT2-MMP-dependent basement membrane transmigration program in cancer cells by Snail1
    • COI: 1:CAS:528:DC%2BC3cXjtFSqsg%3D%3D, PID: 19915148
    • Ota, I., Li, X. Y., Hu, Y., & Weiss, S. J. (2009). Induction of a MT1-MMP and MT2-MMP-dependent basement membrane transmigration program in cancer cells by Snail1. Proceedings of the National Academy of Sciences of the United States of America, 106(48), 20318–23. doi:10.1073/pnas.0910962106.
    • (2009) Proceedings of the National Academy of Sciences of the United States of America , vol.106 , Issue.48 , pp. 20318-20323
    • Ota, I.1    Li, X.Y.2    Hu, Y.3    Weiss, S.J.4
  • 85
    • 84855428544 scopus 로고    scopus 로고
    • New approaches for dissecting protease functions to improve probe development and drug discovery
    • COI: 1:CAS:528:DC%2BC38XivFagtQ%3D%3D
    • Deu, E., Verdoes, M., & Bogyo, M. (2012). New approaches for dissecting protease functions to improve probe development and drug discovery. Nature Structural & Molecular Biology, 19(1), 9–16. doi:10.1038/nsmb.2203.
    • (2012) Nature Structural & Molecular Biology , vol.19 , Issue.1 , pp. 9-16
    • Deu, E.1    Verdoes, M.2    Bogyo, M.3
  • 86
    • 77749297971 scopus 로고    scopus 로고
    • Activatable cell penetrating peptides linked to nanoparticles as dual probes for in vivo fluorescence and MR imaging of proteases
    • COI: 1:CAS:528:DC%2BC3cXjsFWiurw%3D, PID: 20160077
    • Olson, E. S., Jiang, T., Aguilera, T. A., Nguyen, Q. T., Ellies, L. G., Scadeng, M., et al. (2010). Activatable cell penetrating peptides linked to nanoparticles as dual probes for in vivo fluorescence and MR imaging of proteases. Proceedings of the National Academy of Sciences of the United States of America, 107(9), 4311–6. doi:10.1073/pnas.0910283107.
    • (2010) Proceedings of the National Academy of Sciences of the United States of America , vol.107 , Issue.9 , pp. 4311-4316
    • Olson, E.S.1    Jiang, T.2    Aguilera, T.A.3    Nguyen, Q.T.4    Ellies, L.G.5    Scadeng, M.6
  • 87
    • 84863378692 scopus 로고    scopus 로고
    • Detection of MMP-2 and MMP-9 activity in vivo with a triple-helical peptide optical probe
    • COI: 1:CAS:528:DC%2BC38XhvVWjs7s%3D, PID: 22309692
    • Akers, W. J., Xu, B., Lee, H., Sudlow, G. P., Fields, G. B., Achilefu, S., et al. (2012). Detection of MMP-2 and MMP-9 activity in vivo with a triple-helical peptide optical probe. Bioconjugate Chemistry, 23(3), 656–63. doi:10.1021/bc300027y.
    • (2012) Bioconjugate Chemistry , vol.23 , Issue.3 , pp. 656-663
    • Akers, W.J.1    Xu, B.2    Lee, H.3    Sudlow, G.P.4    Fields, G.B.5    Achilefu, S.6
  • 88
    • 0034946412 scopus 로고    scopus 로고
    • Determination of protease cleavage site motifs using mixture-based oriented peptide libraries
    • COI: 1:CAS:528:DC%2BD3MXkvFGju74%3D, PID: 11433279
    • Turk, B. E., Huang, L. L., Piro, E. T., & Cantley, L. C. (2001). Determination of protease cleavage site motifs using mixture-based oriented peptide libraries. Nature Biotechnology, 19(7), 661–7. doi:10.1038/90273.
    • (2001) Nature Biotechnology , vol.19 , Issue.7 , pp. 661-667
    • Turk, B.E.1    Huang, L.L.2    Piro, E.T.3    Cantley, L.C.4
  • 89
    • 61749094550 scopus 로고    scopus 로고
    • Optical imaging of matrix metalloproteinase-7 activity in vivo using a proteolytic nanobeacon
    • COI: 1:CAS:528:DC%2BD1cXhsFWrt7vI, PID: 19123982
    • Scherer, R. L., VanSaun, M. N., McIntyre, J. O., & Matrisian, L. M. (2008). Optical imaging of matrix metalloproteinase-7 activity in vivo using a proteolytic nanobeacon. Molecular Imaging, 7(3), 118–31.
    • (2008) Molecular Imaging , vol.7 , Issue.3 , pp. 118-131
    • Scherer, R.L.1    VanSaun, M.N.2    McIntyre, J.O.3    Matrisian, L.M.4
  • 90
    • 84914103549 scopus 로고    scopus 로고
    • Zhang, H. (2004). Pyro-Gly-Pro-Leu-Gly-Leu-Ala-Arg-Lys (BHQ3). Molecular Imaging and Contrast Agent Database (MICAD). Bethesda (MD)
    • Zhang, H. (2004). Pyro-Gly-Pro-Leu-Gly-Leu-Ala-Arg-Lys (BHQ3). Molecular Imaging and Contrast Agent Database (MICAD). Bethesda (MD).
  • 91
    • 84914103548 scopus 로고    scopus 로고
    • Fudala R, Rich R, Mukerjee A, Ranjan AP, Vishwanatha JK, Kurdowska AK, et al. (2012). Fluorescence detection of MMP-9.II. Ratiometric FRET-based sensing with dually labeled specific peptide. Current Pharmaceutical Biotechnology
    • Fudala R, Rich R, Mukerjee A, Ranjan AP, Vishwanatha JK, Kurdowska AK, et al. (2012). Fluorescence detection of MMP-9.II. Ratiometric FRET-based sensing with dually labeled specific peptide. Current Pharmaceutical Biotechnology.
  • 92
    • 77952473782 scopus 로고    scopus 로고
    • Peptides and peptide hormones for molecular imaging and disease diagnosis
    • COI: 1:CAS:528:DC%2BC3cXjtFOqs78%3D, PID: 20225899
    • Lee, S., Xie, J., & Chen, X. (2010). Peptides and peptide hormones for molecular imaging and disease diagnosis. Chemical Reviews, 110(5), 3087–111. doi:10.1021/cr900361p.
    • (2010) Chemical Reviews , vol.110 , Issue.5 , pp. 3087-3111
    • Lee, S.1    Xie, J.2    Chen, X.3
  • 93
    • 84868314908 scopus 로고    scopus 로고
    • Extra- and intracellular imaging of human matrix metalloprotease 11 (hMMP-11) with a cell-penetrating FRET substrate
    • COI: 1:CAS:528:DC%2BC38Xhs1WjtLnO, PID: 22927434
    • Meyer, B. S., & Rademann, J. (2012). Extra- and intracellular imaging of human matrix metalloprotease 11 (hMMP-11) with a cell-penetrating FRET substrate. Journal of Biological Chemistry, 287(45), 37857–67. doi:10.1074/jbc.M112.371500.
    • (2012) Journal of Biological Chemistry , vol.287 , Issue.45 , pp. 37857-37867
    • Meyer, B.S.1    Rademann, J.2
  • 94
    • 79953064715 scopus 로고    scopus 로고
    • Directed evolution of protease beacons that enable sensitive detection of endogenous MT1-MMP activity in tumor cell lines
    • COI: 1:CAS:528:DC%2BC3MXjvFSrt74%3D
    • Jabaiah, A., & Daugherty, P. S. (2011). Directed evolution of protease beacons that enable sensitive detection of endogenous MT1-MMP activity in tumor cell lines. Chemistry & Biology, 18(3), 392–401. doi:10.1016/j.chembiol.2010.12.017.
    • (2011) Chemistry & Biology , vol.18 , Issue.3 , pp. 392-401
    • Jabaiah, A.1    Daugherty, P.S.2
  • 95
    • 84896710015 scopus 로고    scopus 로고
    • Rational design of matrix metalloproteinase-13 activatable probes for enhanced specificity
    • Zhu, L., Ma, Y., Kiesewetter, D. O., Wang, Y., Lang, L., Lee, S., et al. (2013). Rational design of matrix metalloproteinase-13 activatable probes for enhanced specificity. ACS Chemical Biology. doi:10.1021/cb400698s.
    • (2013) ACS Chemical Biology
    • Zhu, L.1    Ma, Y.2    Kiesewetter, D.O.3    Wang, Y.4    Lang, L.5    Lee, S.6
  • 96
    • 84890656032 scopus 로고    scopus 로고
    • Enzyme-directed assembly of nanoparticles in tumors monitored by in vivo whole animal imaging and ex vivo super-resolution fluorescence imaging
    • PID: 24308273
    • Chien, M. P., Carlini, A. S., Hu, D., Barback, C. V., Rush, A. M., Hall, D. J., et al. (2013). Enzyme-directed assembly of nanoparticles in tumors monitored by in vivo whole animal imaging and ex vivo super-resolution fluorescence imaging. Journal of the American Chemical Society. doi:10.1021/ja408182p.
    • (2013) Journal of the American Chemical Society
    • Chien, M.P.1    Carlini, A.S.2    Hu, D.3    Barback, C.V.4    Rush, A.M.5    Hall, D.J.6
  • 97
    • 84880047527 scopus 로고    scopus 로고
    • Non-destructive and selective imaging of the functionally active, pro-invasive membrane type-1 matrix metalloproteinase (MT1-MMP) enzyme in cancer cells
    • COI: 1:CAS:528:DC%2BC3sXhtV2rt7vJ, PID: 23733191
    • Remacle, A. G., Shiryaev, S. A., Golubkov, V. S., Freskos, J. N., Brown, M. A., Karwa, A. S., et al. (2013). Non-destructive and selective imaging of the functionally active, pro-invasive membrane type-1 matrix metalloproteinase (MT1-MMP) enzyme in cancer cells. Journal of Biological Chemistry, 288(28), 20568–80. doi:10.1074/jbc.M113.471508.
    • (2013) Journal of Biological Chemistry , vol.288 , Issue.28 , pp. 20568-20580
    • Remacle, A.G.1    Shiryaev, S.A.2    Golubkov, V.S.3    Freskos, J.N.4    Brown, M.A.5    Karwa, A.S.6
  • 98
    • 84862327507 scopus 로고    scopus 로고
    • Size- and charge-dependent non-specific uptake of PEGylated nanoparticles by macrophages
    • COI: 1:CAS:528:DC%2BC38XjvFWrsrc%3D, PID: 22359457
    • Yu, S. S., Lau, C. M., Thomas, S. N., Jerome, W. G., Maron, D. J., Dickerson, J. H., et al. (2012). Size- and charge-dependent non-specific uptake of PEGylated nanoparticles by macrophages. International Journal of Nanomedicine, 7, 799–813. doi:10.2147/IJN.S28531.
    • (2012) International Journal of Nanomedicine , vol.7 , pp. 799-813
    • Yu, S.S.1    Lau, C.M.2    Thomas, S.N.3    Jerome, W.G.4    Maron, D.J.5    Dickerson, J.H.6
  • 99
    • 84887479739 scopus 로고    scopus 로고
    • Quantitative imaging of disease signatures through radioactive decay signal conversion
    • COI: 1:CAS:528:DC%2BC3sXhtl2ks7jO, PID: 24013701
    • Thorek, D. L., Ogirala, A., Beattie, B. J., & Grimm, J. (2013). Quantitative imaging of disease signatures through radioactive decay signal conversion. Nature Medicine, 19(10), 1345–50. doi:10.1038/nm.3323.
    • (2013) Nature Medicine , vol.19 , Issue.10 , pp. 1345-1350
    • Thorek, D.L.1    Ogirala, A.2    Beattie, B.J.3    Grimm, J.4
  • 100
    • 72149096051 scopus 로고    scopus 로고
    • Bioluminescent nanosensors for protease detection based upon gold nanoparticle-luciferase conjugates
    • COI: 1:CAS:528:DC%2BD1MXhsFektrnL
    • Kim, Y. P., Daniel, W. L., Xia, Z., Xie, H., Mirkin, C. A., & Rao, J. (2010). Bioluminescent nanosensors for protease detection based upon gold nanoparticle-luciferase conjugates. Chemical communications (Cambridge), 46(1), 76–8. doi:10.1039/b915612g.
    • (2010) Chemical communications (Cambridge) , vol.46 , Issue.1 , pp. 76-78
    • Kim, Y.P.1    Daniel, W.L.2    Xia, Z.3    Xie, H.4    Mirkin, C.A.5    Rao, J.6
  • 101
    • 84881337237 scopus 로고    scopus 로고
    • Synthesis and in vitro efficacy of MMP9-activated NanoDendrons
    • COI: 1:CAS:528:DC%2BC3sXptFSgtLk%3D, PID: 23750801
    • Samuelson, L. E., Scherer, R. L., Matrisian, L. M., McIntyre, J. O., & Bornhop, D. J. (2013). Synthesis and in vitro efficacy of MMP9-activated NanoDendrons. Molecular Pharmaceutics, 10(8), 3164–74. doi:10.1021/mp4002206.
    • (2013) Molecular Pharmaceutics , vol.10 , Issue.8 , pp. 3164-3174
    • Samuelson, L.E.1    Scherer, R.L.2    Matrisian, L.M.3    McIntyre, J.O.4    Bornhop, D.J.5
  • 102
    • 84866528463 scopus 로고    scopus 로고
    • Enhancing cellular uptake of activable cell-penetrating peptide-doxorubicin conjugate by enzymatic cleavage
    • COI: 1:CAS:528:DC%2BC38XlsFyrsb8%3D, PID: 22619516
    • Shi, N. Q., Gao, W., Xiang, B., & Qi, X. R. (2012). Enhancing cellular uptake of activable cell-penetrating peptide-doxorubicin conjugate by enzymatic cleavage. International Journal of Nanomedicine, 7, 1613–21. doi:10.2147/IJN.S30104.
    • (2012) International Journal of Nanomedicine , vol.7 , pp. 1613-1621
    • Shi, N.Q.1    Gao, W.2    Xiang, B.3    Qi, X.R.4
  • 103
    • 84880771922 scopus 로고    scopus 로고
    • Intelligently targeted drug delivery and enhanced antitumor effect by gelatinase-responsive nanoparticles
    • COI: 1:CAS:528:DC%2BC3sXht1yqtb%2FJ, PID: 23936062
    • Li, R., Wu, W., Liu, Q., Wu, P., Xie, L., Zhu, Z., et al. (2013). Intelligently targeted drug delivery and enhanced antitumor effect by gelatinase-responsive nanoparticles. PloS One, 8(7), e69643. doi:10.1371/journal.pone.0069643.
    • (2013) PloS One , vol.8 , Issue.7 , pp. e69643
    • Li, R.1    Wu, W.2    Liu, Q.3    Wu, P.4    Xie, L.5    Zhu, Z.6
  • 104
    • 35148881028 scopus 로고    scopus 로고
    • Drug resistance and the solid tumor microenvironment
    • COI: 1:CAS:528:DC%2BD2sXht1yltbrO, PID: 17895480
    • Tredan, O., Galmarini, C. M., Patel, K., & Tannock, I. F. (2007). Drug resistance and the solid tumor microenvironment. Journal of the National Cancer Institute, 99(19), 1441–54. doi:10.1093/jnci/djm135.
    • (2007) Journal of the National Cancer Institute , vol.99 , Issue.19 , pp. 1441-1454
    • Tredan, O.1    Galmarini, C.M.2    Patel, K.3    Tannock, I.F.4
  • 105
    • 78649315943 scopus 로고    scopus 로고
    • To exploit the tumor microenvironment: Passive and active tumor targeting of nanocarriers for anti-cancer drug delivery
    • COI: 1:CAS:528:DC%2BC3cXhsVCmsrzF
    • Danhier, F., Feron, O., & Preat, V. (2010). To exploit the tumor microenvironment: Passive and active tumor targeting of nanocarriers for anti-cancer drug delivery. Journal of Controlled Release: Official Journal of the Controlled Release Society, 148(2), 135–46. doi:10.1016/j.jconrel.2010.08.027.
    • (2010) Journal of Controlled Release: Official Journal of the Controlled Release Society , vol.148 , Issue.2 , pp. 135-146
    • Danhier, F.1    Feron, O.2    Preat, V.3
  • 106
    • 80054989315 scopus 로고    scopus 로고
    • Trastuzumab emtansine (T-DM1): a novel agent for targeting HER2+ breast cancer
    • COI: 1:CAS:528:DC%2BC3MXhsVOhtL%2FF, PID: 21729661
    • Burris, H. A., 3rd, Tibbitts, J., Holden, S. N., Sliwkowski, M. X., & Lewis Phillips, G. D. (2011). Trastuzumab emtansine (T-DM1): a novel agent for targeting HER2+ breast cancer. Clinical Breast Cancer, 11(5), 275–82. doi:10.1016/j.clbc.2011.03.018.
    • (2011) Clinical Breast Cancer , vol.11 , Issue.5 , pp. 275-282
    • Burris, H.A.1    Tibbitts, J.2    Holden, S.N.3    Sliwkowski, M.X.4    Lewis Phillips, G.D.5
  • 107
    • 84868121994 scopus 로고    scopus 로고
    • PEG-co-PCL nanoparticles modified with MMP-2/9 activatable low molecular weight protamine for enhanced targeted glioblastoma therapy
    • PID: 23069707
    • Gu, G., Xia, H., Hu, Q., Liu, Z., Jiang, M., Kang, T., et al. (2013). PEG-co-PCL nanoparticles modified with MMP-2/9 activatable low molecular weight protamine for enhanced targeted glioblastoma therapy. Biomaterials, 34(1), 196–208. doi:10.1016/j.biomaterials.2012.09.044.
    • (2013) Biomaterials , vol.34 , Issue.1 , pp. 196-208
    • Gu, G.1    Xia, H.2    Hu, Q.3    Liu, Z.4    Jiang, M.5    Kang, T.6
  • 108
    • 0347382317 scopus 로고    scopus 로고
    • Anti-neovascular therapy by liposomal drug targeted to membrane type-1 matrix metalloproteinase
    • COI: 1:CAS:528:DC%2BD3sXhtVWgu7rN
    • Kondo, M., Asai, T., Katanasaka, Y., Sadzuka, Y., Tsukada, H., Ogino, K., et al. (2004). Anti-neovascular therapy by liposomal drug targeted to membrane type-1 matrix metalloproteinase. International Journal of Cancer, 108(2), 301–6. doi:10.1002/ijc.11526.
    • (2004) International Journal of Cancer , vol.108 , Issue.2 , pp. 301-306
    • Kondo, M.1    Asai, T.2    Katanasaka, Y.3    Sadzuka, Y.4    Tsukada, H.5    Ogino, K.6
  • 109
    • 26944443171 scopus 로고    scopus 로고
    • Targeting an MMP-9-activated prodrug to multiple myeloma-diseased bone marrow: a proof of principle in the 5T33MM mouse model
    • PID: 16015389
    • Van Valckenborgh, E., Mincher, D., Di Salvo, A., Van Riet, I., Young, L., Van Camp, B., et al. (2005). Targeting an MMP-9-activated prodrug to multiple myeloma-diseased bone marrow: a proof of principle in the 5T33MM mouse model. Leukemia, 19(9), 1628–33. doi:10.1038/sj.leu.2403866.
    • (2005) Leukemia , vol.19 , Issue.9 , pp. 1628-1633
    • Van Valckenborgh, E.1    Mincher, D.2    Di Salvo, A.3    Van Riet, I.4    Young, L.5    Van Camp, B.6
  • 110
    • 84893463349 scopus 로고    scopus 로고
    • Development of novel tumor-targeted theranostic nanoparticles activated by membrane-type matrix metalloproteinases for combined cancer magnetic resonance imaging and therapy
    • COI: 1:CAS:528:DC%2BC3sXhtlCns7zK, PID: 24038954
    • Ansari, C., Tikhomirov, G. A., Hong, S. H., Falconer, R. A., Loadman, P. M., Gill, J. H., et al. (2014). Development of novel tumor-targeted theranostic nanoparticles activated by membrane-type matrix metalloproteinases for combined cancer magnetic resonance imaging and therapy. Small, 10(3), 566–75. doi:10.1002/smll.201301456.
    • (2014) Small , vol.10 , Issue.3 , pp. 566-575
    • Ansari, C.1    Tikhomirov, G.A.2    Hong, S.H.3    Falconer, R.A.4    Loadman, P.M.5    Gill, J.H.6
  • 111
    • 84879325210 scopus 로고    scopus 로고
    • Coupling protein engineering with probe design to inhibit and image matrix metalloproteinases with controlled specificity
    • COI: 1:CAS:528:DC%2BC3sXotV2rtb4%3D, PID: 23701445
    • Morell, M., Nguyen Duc, T., Willis, A. L., Syed, S., Lee, J., Deu, E., et al. (2013). Coupling protein engineering with probe design to inhibit and image matrix metalloproteinases with controlled specificity. Journal of the American Chemical Society, 135(24), 9139–48. doi:10.1021/ja403523p.
    • (2013) Journal of the American Chemical Society , vol.135 , Issue.24 , pp. 9139-9148
    • Morell, M.1    Nguyen Duc, T.2    Willis, A.L.3    Syed, S.4    Lee, J.5    Deu, E.6


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