메뉴 건너뛰기




Volumn 5, Issue 9, 2014, Pages 2736-2749

Tumor cell-produced matrix metalloproteinase 9 (MMP-9) drives malignant progression and metastasis of basal-like triple negative breast cancer

Author keywords

Basal like breast cancer; Bioluminescence imaging; Invasion; Matrix metalloproteinases; Metastasis; Mouse orthotopic tumor models; Triple negative breast cancer

Indexed keywords

GELATINASE B; MESSENGER RNA; MMP9 PROTEIN, HUMAN; SMALL INTERFERING RNA; TUMOR MARKER;

EID: 84901191680     PISSN: None     EISSN: 19492553     Source Type: Journal    
DOI: 10.18632/oncotarget.1932     Document Type: Article
Times cited : (296)

References (94)
  • 6
    • 84876968058 scopus 로고    scopus 로고
    • The development of endocrine therapy for women with breast cancer
    • Sainsbury R. The development of endocrine therapy for women with breast cancer. Cancer Treat Rev. 2013; 39(5):507-517.
    • (2013) Cancer Treat Rev. , vol.39 , Issue.5 , pp. 507-517
    • Sainsbury, R.1
  • 8
    • 84867128714 scopus 로고    scopus 로고
    • Optimal strategies for the treatment of metastatic triple-negative breast cancer with currently approved agents
    • Andre F and Zielinski CC. Optimal strategies for the treatment of metastatic triple-negative breast cancer with currently approved agents. Ann Oncol. 2012; 23 Suppl 6:vi46-51.
    • (2012) Ann Oncol , vol.23 , Issue.SUPPL. 6
    • Andre, F.1    Zielinski, C.C.2
  • 9
    • 84874653875 scopus 로고    scopus 로고
    • Molecularly targeted therapies for metastatic triple-negative breast cancer
    • Bayraktar S and Gluck S. Molecularly targeted therapies for metastatic triple-negative breast cancer. Breast Cancer Res Treat. 2013; 138(1):21-35.
    • (2013) Breast Cancer Res Treat. , vol.138 , Issue.1 , pp. 21-35
    • Bayraktar, S.1    Gluck, S.2
  • 10
    • 83455236666 scopus 로고    scopus 로고
    • Basal breast cancer: a complex and deadly molecular subtype
    • Bertucci F, Finetti P and Birnbaum D. Basal breast cancer: a complex and deadly molecular subtype. Current Molecular Medicine. 2012; 12(1):96-110.
    • (2012) Current Molecular Medicine. , vol.12 , Issue.1 , pp. 96-110
    • Bertucci, F.1    Finetti, P.2    Birnbaum, D.3
  • 12
    • 0038575443 scopus 로고    scopus 로고
    • Extracellular matrix remodelling: the role of matrix metalloproteinases
    • Stamenkovic I. Extracellular matrix remodelling: the role of matrix metalloproteinases. J Pathol. 2003; 200(4):448-464.
    • (2003) J Pathol. , vol.200 , Issue.4 , pp. 448-464
    • Stamenkovic, I.1
  • 13
    • 3543134126 scopus 로고    scopus 로고
    • Matrix metalloproteinases as modulators of inflammation and innate immunity
    • Parks WC, Wilson CL and Lopez-Boado YS. Matrix metalloproteinases as modulators of inflammation and innate immunity. Nat Rev Immunol. 2004; 4(8):617-629.
    • (2004) Nat Rev Immunol. , vol.4 , Issue.8 , pp. 617-629
    • Parks, W.C.1    Wilson, C.L.2    Lopez-Boado, Y.S.3
  • 14
    • 77950931419 scopus 로고    scopus 로고
    • Matrix metalloproteinases: regulators of the tumor microenvironment
    • Kessenbrock K, Plaks V and Werb Z. Matrix metalloproteinases: regulators of the tumor microenvironment. Cell. 2010; 141(1):52-67.
    • (2010) Cell. , vol.141 , Issue.1 , pp. 52-67
    • Kessenbrock, K.1    Plaks, V.2    Werb, Z.3
  • 15
    • 78650424066 scopus 로고    scopus 로고
    • Roles of matrix metalloproteinases in cancer progression and their pharmacological targeting
    • Gialeli C, Theocharis AD and Karamanos NK. Roles of matrix metalloproteinases in cancer progression and their pharmacological targeting. FEBS Journal. 2011; 278(1):16-27.
    • (2011) FEBS Journal. , vol.278 , Issue.1 , pp. 16-27
    • Gialeli, C.1    Theocharis, A.D.2    Karamanos, N.K.3
  • 16
    • 77954861244 scopus 로고    scopus 로고
    • Matrix metalloproteinase-induced epithelial-mesenchymal transition in breast cancer
    • Radisky ES and Radisky DC. Matrix metalloproteinase-induced epithelial-mesenchymal transition in breast cancer. J Mammary Gland Biol Neoplasia. 2010; 15(2):201-212.
    • (2010) J Mammary Gland Biol Neoplasia. , vol.15 , Issue.2 , pp. 201-212
    • Radisky, E.S.1    Radisky, D.C.2
  • 17
    • 34948884579 scopus 로고    scopus 로고
    • Stromal induction of breast cancer: inflammation and invasion
    • Radisky ES and Radisky DC. Stromal induction of breast cancer: inflammation and invasion. Rev Endocr Metab Disord. 2007; 8(3):279-287.
    • (2007) Rev Endocr Metab Disord. , vol.8 , Issue.3 , pp. 279-287
    • Radisky, E.S.1    Radisky, D.C.2
  • 19
    • 50849134800 scopus 로고    scopus 로고
    • Matrix metalloproteinase expression and outcome in patients with breast cancer: analysis of a published database
    • McGowan PM and Duffy MJ. Matrix metalloproteinase expression and outcome in patients with breast cancer: analysis of a published database. Ann Oncol. 2008; 19(9):1566-1572.
    • (2008) Ann Oncol. , vol.19 , Issue.9 , pp. 1566-1572
    • McGowan, P.M.1    Duffy, M.J.2
  • 20
    • 33748055761 scopus 로고    scopus 로고
    • Analysis of host- and tumor-derived proteinases using a custom dual species microarray reveals a protective role for stromal matrix metalloproteinase-12 in non-small cell lung cancer
    • Acuff HB, Sinnamon M, Fingleton B, Boone B, Levy SE, Chen X, Pozzi A, Carbone DP, Schwartz DR, Moin K, Sloane BF and Matrisian LM. Analysis of host- and tumor-derived proteinases using a custom dual species microarray reveals a protective role for stromal matrix metalloproteinase-12 in non-small cell lung cancer. Cancer Res. 2006; 66(16):7968-7975.
    • (2006) Cancer Res. , vol.66 , Issue.16 , pp. 7968-7975
    • Acuff, H.B.1    Sinnamon, M.2    Fingleton, B.3    Boone, B.4    Levy, S.E.5    Chen, X.6    Pozzi, A.7    Carbone, D.P.8    Schwartz, D.R.9    Moin, K.10    Sloane, B.F.11    Matrisian, L.M.12
  • 22
    • 51049100625 scopus 로고    scopus 로고
    • Effect of ablation or inhibition of stromal matrix metalloproteinase-9 on lung metastasis in a breast cancer model is dependent on genetic background
    • Martin MD, Carter KJ, Jean-Philippe SR, Chang M, Mobashery S, Thiolloy S, Lynch CC, Matrisian LM and Fingleton B. Effect of ablation or inhibition of stromal matrix metalloproteinase-9 on lung metastasis in a breast cancer model is dependent on genetic background. Cancer Res. 2008; 68(15):6251-6259.
    • (2008) Cancer Res. , vol.68 , Issue.15 , pp. 6251-6259
    • Martin, M.D.1    Carter, K.J.2    Jean-Philippe, S.R.3    Chang, M.4    Mobashery, S.5    Thiolloy, S.6    Lynch, C.C.7    Matrisian, L.M.8    Fingleton, B.9
  • 24
    • 9344271530 scopus 로고    scopus 로고
    • Expression of matrix metalloproteinase (MMP)-2 and MMP-9 in breast cancer with a special reference to activator protein-2, HER2, and prognosis
    • Pellikainen JM, Ropponen KM, Kataja VV, Kellokoski JK, Eskelinen MJ and Kosma VM. Expression of matrix metalloproteinase (MMP)-2 and MMP-9 in breast cancer with a special reference to activator protein-2, HER2, and prognosis. Clin Cancer Res. 2004; 10(22):7621-7628.
    • (2004) Clin Cancer Res. , vol.10 , Issue.22 , pp. 7621-7628
    • Pellikainen, J.M.1    Ropponen, K.M.2    Kataja, V.V.3    Kellokoski, J.K.4    Eskelinen, M.J.5    Kosma, V.M.6
  • 26
    • 0035362633 scopus 로고    scopus 로고
    • Overexpression of matrix-metalloproteinase-9 in human breast cancer: a potential favourable indicator in node-negative patients
    • Scorilas A, Karameris A, Arnogiannaki N, Ardavanis A, Bassilopoulos P, Trangas T and Talieri M. Overexpression of matrix-metalloproteinase-9 in human breast cancer: a potential favourable indicator in node-negative patients. Br J Cancer. 2001; 84(11):1488-1496.
    • (2001) Br J Cancer. , vol.84 , Issue.11 , pp. 1488-1496
    • Scorilas, A.1    Karameris, A.2    Arnogiannaki, N.3    Ardavanis, A.4    Bassilopoulos, P.5    Trangas, T.6    Talieri, M.7
  • 27
    • 34250004027 scopus 로고    scopus 로고
    • Recombination of CXCR4, VEGF, and MMP-9 predicting lymph node metastasis in human breast cancer
    • Hao L, Zhang C, Qiu Y, Wang L, Luo Y, Jin M, Zhang Y, Guo TB and Matsushima K. Recombination of CXCR4, VEGF, and MMP-9 predicting lymph node metastasis in human breast cancer. Cancer Lett. 2007; 253(1):34-42.
    • (2007) Cancer Lett. , vol.253 , Issue.1 , pp. 34-42
    • Hao, L.1    Zhang, C.2    Qiu, Y.3    Wang, L.4    Luo, Y.5    Jin, M.6    Zhang, Y.7    Guo, T.B.8    Matsushima, K.9
  • 28
    • 40749099079 scopus 로고    scopus 로고
    • Prognostic significance of MMP-9 and TIMP-1 serum and tissue expression in breast cancer
    • Wu ZS, Wu Q, Yang JH, Wang HQ, Ding XD, Yang F and Xu XC. Prognostic significance of MMP-9 and TIMP-1 serum and tissue expression in breast cancer. Int J Cancer. 2008; 122(9):2050-2056.
    • (2008) Int J Cancer. , vol.122 , Issue.9 , pp. 2050-2056
    • Wu, Z.S.1    Wu, Q.2    Yang, J.H.3    Wang, H.Q.4    Ding, X.D.5    Yang, F.6    Xu, X.C.7
  • 29
    • 84869789997 scopus 로고    scopus 로고
    • PEGylation extends circulation half-life while preserving in vitro and in vivo activity of tissue inhibitor of metalloproteinases-1 (TIMP-1)
    • Batra J, Robinson J, Mehner C, Hockla A, Miller E, Radisky DC and Radisky ES. PEGylation extends circulation half-life while preserving in vitro and in vivo activity of tissue inhibitor of metalloproteinases-1 (TIMP-1). PloS One. 2012; 7(11):e50028.
    • (2012) PloS One. , vol.7 , Issue.11
    • Batra, J.1    Robinson, J.2    Mehner, C.3    Hockla, A.4    Miller, E.5    Radisky, D.C.6    Radisky, E.S.7
  • 33
    • 39849100541 scopus 로고    scopus 로고
    • Matrix metalloproteinase-9 is required for tumor vasculogenesis but not for angiogenesis: role of bone marrow-derived myelomonocytic cells
    • Ahn GO and Brown JM. Matrix metalloproteinase-9 is required for tumor vasculogenesis but not for angiogenesis: role of bone marrow-derived myelomonocytic cells. Cancer Cell. 2008; 13(3):193-205.
    • (2008) Cancer Cell. , vol.13 , Issue.3 , pp. 193-205
    • Ahn, G.O.1    Brown, J.M.2
  • 35
    • 79952819724 scopus 로고    scopus 로고
    • GOBO: Gene Expression-Based Outcome for Breast Cancer Online
    • Ringnér M, Fredlund E, Häkkinen J, Borg Å and Staaf J. GOBO: Gene Expression-Based Outcome for Breast Cancer Online. PLoS One. 2011; 6(3):e17911.
    • (2011) PLoS One. , vol.6 , Issue.3
    • Ringnér, M.1    Fredlund, E.2    Häkkinen, J.3    Borg Å4    Staaf, J.5
  • 40
    • 0032926177 scopus 로고    scopus 로고
    • Localization of matrix metalloproteinase 9 to the cell surface provides a mechanism for CD44-mediated tumor invasion
    • Yu Q and Stamenkovic I. Localization of matrix metalloproteinase 9 to the cell surface provides a mechanism for CD44-mediated tumor invasion. Genes Dev. 1999; 13(1):35-48.
    • (1999) Genes Dev. , vol.13 , Issue.1 , pp. 35-48
    • Yu, Q.1    Stamenkovic, I.2
  • 41
    • 0031808063 scopus 로고    scopus 로고
    • CD44v(3,8-10) is involved in cytoskeleton-mediated tumor cell migration and matrix metalloproteinase (MMP-9) association in metastatic breast cancer cells
    • Bourguignon LY, Gunja-Smith Z, Iida N, Zhu HB, Young LJ, Muller WJ and Cardiff RD. CD44v(3,8-10) is involved in cytoskeleton-mediated tumor cell migration and matrix metalloproteinase (MMP-9) association in metastatic breast cancer cells. J Cell Physiol. 1998; 176(1):206-215.
    • (1998) J Cell Physiol. , vol.176 , Issue.1 , pp. 206-215
    • Bourguignon, L.Y.1    Gunja-Smith, Z.2    Iida, N.3    Zhu, H.B.4    Young, L.J.5    Muller, W.J.6    Cardiff, R.D.7
  • 42
    • 0034650486 scopus 로고    scopus 로고
    • Cell surface-localized matrix metalloproteinase-9 proteolytically activates TGF-beta and promotes tumor invasion and angiogenesis
    • Yu Q and Stamenkovic I. Cell surface-localized matrix metalloproteinase-9 proteolytically activates TGF-beta and promotes tumor invasion and angiogenesis. Genes Dev. 2000; 14(2):163-176.
    • (2000) Genes Dev. , vol.14 , Issue.2 , pp. 163-176
    • Yu, Q.1    Stamenkovic, I.2
  • 43
    • 54049107708 scopus 로고    scopus 로고
    • Role of the hemopexin domain of matrix metalloproteinases in cell migration
    • Dufour A, Sampson NS, Zucker S and Cao J. Role of the hemopexin domain of matrix metalloproteinases in cell migration. J Cell Physiol. 2008; 217(3):643-651.
    • (2008) J Cell Physiol. , vol.217 , Issue.3 , pp. 643-651
    • Dufour, A.1    Sampson, N.S.2    Zucker, S.3    Cao, J.4
  • 44
    • 0141817946 scopus 로고    scopus 로고
    • Identification of a negatively charged peptide motif within the catalytic domain of progelatinases that mediates binding to leukocyte beta 2 integrins
    • Stefanidakis M, Bjorklund M, Ihanus E, Gahmberg CG and Koivunen E. Identification of a negatively charged peptide motif within the catalytic domain of progelatinases that mediates binding to leukocyte beta 2 integrins. J Biol Chem. 2003; 278(36):34674-34684.
    • (2003) J Biol Chem. , vol.278 , Issue.36 , pp. 34674-34684
    • Stefanidakis, M.1    Bjorklund, M.2    Ihanus, E.3    Gahmberg, C.G.4    Koivunen, E.5
  • 45
    • 3142698646 scopus 로고    scopus 로고
    • Peptide inhibition of catalytic and noncatalytic activities of matrix metalloproteinase-9 blocks tumor cell migration and invasion
    • Bjorklund M, Heikkila P and Koivunen E. Peptide inhibition of catalytic and noncatalytic activities of matrix metalloproteinase-9 blocks tumor cell migration and invasion. J Biol Chem. 2004; 279(28):29589-29597.
    • (2004) J Biol Chem. , vol.279 , Issue.28 , pp. 29589-29597
    • Bjorklund, M.1    Heikkila, P.2    Koivunen, E.3
  • 46
    • 79951849322 scopus 로고    scopus 로고
    • Forkhead transcription factor foxq1 promotes epithelial-mesenchymal transition and breast cancer metastasis
    • Zhang H, Meng F, Liu G, Zhang B, Zhu J, Wu F, Ethier SP, Miller F and Wu G. Forkhead transcription factor foxq1 promotes epithelial-mesenchymal transition and breast cancer metastasis. Cancer Res. 2011; 71(4):1292-1301.
    • (2011) Cancer Res. , vol.71 , Issue.4 , pp. 1292-1301
    • Zhang, H.1    Meng, F.2    Liu, G.3    Zhang, B.4    Zhu, J.5    Wu, F.6    Ethier, S.P.7    Miller, F.8    Wu, G.9
  • 49
    • 80054997801 scopus 로고    scopus 로고
    • New facets of matrix metalloproteinases MMP-2 and MMP-9 as cell surface transducers: outside-in signaling and relationship to tumor progression
    • Bauvois B. New facets of matrix metalloproteinases MMP-2 and MMP-9 as cell surface transducers: outside-in signaling and relationship to tumor progression. Biochim Biophys Acta. 2012; 1825(1):29-36.
    • (2012) Biochim Biophys Acta. , vol.1825 , Issue.1 , pp. 29-36
    • Bauvois, B.1
  • 50
    • 84867120285 scopus 로고    scopus 로고
    • Pathological and molecular diagnosis of triple-negative breast cancer: a clinical perspective
    • Penault-Llorca F and Viale G. Pathological and molecular diagnosis of triple-negative breast cancer: a clinical perspective. Ann Oncol. 2012; 23 Suppl 6:vi19-22.
    • (2012) Ann Oncol , vol.23 , Issue.SUPPL. 6
    • Penault-Llorca, F.1    Viale, G.2
  • 51
    • 0037192458 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibitors and cancer: trials and tribulations
    • Coussens LM, Fingleton B and Matrisian LM. Matrix metalloproteinase inhibitors and cancer: trials and tribulations. Science. 2002; 295(5564):2387-2392.
    • (2002) Science. , vol.295 , Issue.5564 , pp. 2387-2392
    • Coussens, L.M.1    Fingleton, B.2    Matrisian, L.M.3
  • 52
    • 36849073658 scopus 로고    scopus 로고
    • MMPs as therapeutic targets-Still a viable option?
    • Fingleton B. MMPs as therapeutic targets-Still a viable option? Semin Cell Dev Biol. 2008; 19(1):61-68.
    • (2008) Semin Cell Dev Biol. , vol.19 , Issue.1 , pp. 61-68
    • Fingleton, B.1
  • 53
    • 16544372352 scopus 로고    scopus 로고
    • Randomized phase III trial of marimastat versus placebo in patients with metastatic breast cancer who have responding or stable disease after first-line chemotherapy: Eastern Cooperative Oncology Group trial E2196
    • Sparano JA, Bernardo P, Stephenson P, Gradishar WJ, Ingle JN, Zucker S and Davidson NE. Randomized phase III trial of marimastat versus placebo in patients with metastatic breast cancer who have responding or stable disease after first-line chemotherapy: Eastern Cooperative Oncology Group trial E2196. J Clin Oncol. 2004; 22(23):4683-4690.
    • (2004) J Clin Oncol. , vol.22 , Issue.23 , pp. 4683-4690
    • Sparano, J.A.1    Bernardo, P.2    Stephenson, P.3    Gradishar, W.J.4    Ingle, J.N.5    Zucker, S.6    Davidson, N.E.7
  • 56
    • 33645738383 scopus 로고    scopus 로고
    • Towards third generation matrix metalloproteinase inhibitors for cancer therapy
    • Overall CM and Kleifeld O. Towards third generation matrix metalloproteinase inhibitors for cancer therapy. Br J Cancer. 2006; 94(7):941-946.
    • (2006) Br J Cancer. , vol.94 , Issue.7 , pp. 941-946
    • Overall, C.M.1    Kleifeld, O.2
  • 57
    • 33646584823 scopus 로고    scopus 로고
    • Recent advances in MMP inhibitor design
    • Fisher JF and Mobashery S. Recent advances in MMP inhibitor design. Cancer Metastasis Rev. 2006; 25(1):115-136.
    • (2006) Cancer Metastasis Rev. , vol.25 , Issue.1 , pp. 115-136
    • Fisher, J.F.1    Mobashery, S.2
  • 58
    • 32944459251 scopus 로고    scopus 로고
    • Matrix metalloproteinases: roles in cancer and metastasis
    • Fingleton B. Matrix metalloproteinases: roles in cancer and metastasis. Front Biosci. 2006; 11:479-491.
    • (2006) Front Biosci. , vol.11 , pp. 479-491
    • Fingleton, B.1
  • 59
    • 36148994693 scopus 로고    scopus 로고
    • The other side of MMPs: protective roles in tumor progression
    • Martin MD and Matrisian LM. The other side of MMPs: protective roles in tumor progression. Cancer Metastasis Rev. 2007; 26(3-4):717-724.
    • (2007) Cancer Metastasis Rev. , vol.26 , Issue.3-4 , pp. 717-724
    • Martin, M.D.1    Matrisian, L.M.2
  • 60
    • 33644545381 scopus 로고    scopus 로고
    • Tumour microenvironment - opinion: validating matrix metalloproteinases as drug targets and anti-targets for cancer therapy
    • Overall CM and Kleifeld O. Tumour microenvironment - opinion: validating matrix metalloproteinases as drug targets and anti-targets for cancer therapy. Nat Rev Cancer. 2006; 6(3):227-239.
    • (2006) Nat Rev Cancer. , vol.6 , Issue.3 , pp. 227-239
    • Overall, C.M.1    Kleifeld, O.2
  • 64
    • 50649119519 scopus 로고    scopus 로고
    • Selective modulation of matrix metalloproteinase 9 (MMP-9) functions via exosite inhibition
    • Lauer-Fields JL, Whitehead JK, Li S, Hammer RP, Brew K and Fields GB. Selective modulation of matrix metalloproteinase 9 (MMP-9) functions via exosite inhibition. J Biol Chem. 2008; 283(29):20087-20095.
    • (2008) J Biol Chem. , vol.283 , Issue.29 , pp. 20087-20095
    • Lauer-Fields, J.L.1    Whitehead, J.K.2    Li, S.3    Hammer, R.P.4    Brew, K.5    Fields, G.B.6
  • 65
    • 78149231567 scopus 로고    scopus 로고
    • Role of matrix metalloproteinase-9 dimers in cell migration: design of inhibitory peptides
    • Dufour A, Zucker S, Sampson NS, Kuscu C and Cao J. Role of matrix metalloproteinase-9 dimers in cell migration: design of inhibitory peptides. J Biol Chem. 2010; 285(46):35944-35956.
    • (2010) J Biol Chem. , vol.285 , Issue.46 , pp. 35944-35956
    • Dufour, A.1    Zucker, S.2    Sampson, N.S.3    Kuscu, C.4    Cao, J.5
  • 66
    • 84864967480 scopus 로고    scopus 로고
    • A 17-residue sequence from the matrix metalloproteinase-9 (MMP-9) hemopexin domain binds alpha4beta1 integrin and inhibits MMP-9-induced functions in chronic lymphocytic leukemia B cells
    • Ugarte-Berzal E, Bailon E, Amigo-Jimenez I, Vituri CL, del Cerro MH, Terol MJ, Albar JP, Rivas G, Garcia-Marco JA and Garcia-Pardo A. A 17-residue sequence from the matrix metalloproteinase-9 (MMP-9) hemopexin domain binds alpha4beta1 integrin and inhibits MMP-9-induced functions in chronic lymphocytic leukemia B cells. J Biol Chem. 2012; 287(33):27601-27613.
    • (2012) J Biol Chem. , vol.287 , Issue.33 , pp. 27601-27613
    • Ugarte-Berzal, E.1    Bailon, E.2    Amigo-Jimenez, I.3    Vituri, C.L.4    del Cerro, M.H.5    Terol, M.J.6    Albar, J.P.7    Rivas, G.8    Garcia-Marco, J.A.9    Garcia-Pardo, A.10
  • 69
    • 34548436604 scopus 로고    scopus 로고
    • Constraining specificity in the N-domain of tissue inhibitor of metalloproteinases-1; gelatinase-selective inhibitors
    • Hamze AB, Wei S, Bahudhanapati H, Kota S, Acharya KR and Brew K. Constraining specificity in the N-domain of tissue inhibitor of metalloproteinases-1; gelatinase-selective inhibitors. Protein Sci. 2007; 16(9):1905-1913.
    • (2007) Protein Sci. , vol.16 , Issue.9 , pp. 1905-1913
    • Hamze, A.B.1    Wei, S.2    Bahudhanapati, H.3    Kota, S.4    Acharya, K.R.5    Brew, K.6
  • 70
    • 77149171184 scopus 로고    scopus 로고
    • Structural and functional bases for allosteric control of MMP activities: can it pave the path for selective inhibition?
    • Sela-Passwell N, Rosenblum G, Shoham T and Sagi I. Structural and functional bases for allosteric control of MMP activities: can it pave the path for selective inhibition? Biochim Biophys Acta. 2010; 1803(1):29-38.
    • (2010) Biochim Biophys Acta. , vol.1803 , Issue.1 , pp. 29-38
    • Sela-Passwell, N.1    Rosenblum, G.2    Shoham, T.3    Sagi, I.4
  • 71
    • 84860868139 scopus 로고    scopus 로고
    • Matrix metalloproteinase-10 (MMP-10) interaction with tissue inhibitors of metalloproteinases TIMP-1 and TIMP-2: binding studies and crystal structure
    • Batra J, Robinson J, Soares AS, Fields AP, Radisky DC and Radisky ES. Matrix metalloproteinase-10 (MMP-10) interaction with tissue inhibitors of metalloproteinases TIMP-1 and TIMP-2: binding studies and crystal structure. J Biol Chem. 2012; 287(19):15935-15946.
    • (2012) J Biol Chem. , vol.287 , Issue.19 , pp. 15935-15946
    • Batra, J.1    Robinson, J.2    Soares, A.S.3    Fields, A.P.4    Radisky, D.C.5    Radisky, E.S.6
  • 72
    • 84884490364 scopus 로고    scopus 로고
    • Matrix Metalloproteinase-10/TIMP-2 Structure and Analyses Define Conserved Core Interactions and Diverse Exosite Interactions in MMP/TIMP Complexes
    • Batra J, Soares AS, Mehner C and Radisky ES. Matrix Metalloproteinase-10/TIMP-2 Structure and Analyses Define Conserved Core Interactions and Diverse Exosite Interactions in MMP/TIMP Complexes. PLoS One. 2013; 8(9):e75836.
    • (2013) PLoS One. , vol.8 , Issue.9
    • Batra, J.1    Soares, A.S.2    Mehner, C.3    Radisky, E.S.4
  • 74
    • 84929214664 scopus 로고    scopus 로고
    • Tissue inhibitors of metalloproteinases (TIMPs): inhibition of Zn-dependent metallopeptidases
    • (in press)), In: Scott RA, ed,: John Wiley&Sons
    • Batra J and Radisky ES. (2013 (in press)). Tissue inhibitors of metalloproteinases (TIMPs): inhibition of Zn-dependent metallopeptidases. In: Scott RA, ed. Encyclopedia of Inorganic and Bioinorganic Chemistry: John Wiley&Sons.
    • (2013) Encyclopedia of Inorganic and Bioinorganic Chemistry
    • Batra, J.1    Radisky, E.S.2
  • 76
    • 65449155176 scopus 로고    scopus 로고
    • Homology with vesicle fusion mediator syntaxin-1a predicts determinants of epimorphin/syntaxin-2 function in mammary epithelial morphogenesis
    • Chen CS, Nelson CM, Khauv D, Bennett S, Radisky ES, Hirai Y, Bissell MJ and Radisky DC. Homology with vesicle fusion mediator syntaxin-1a predicts determinants of epimorphin/syntaxin-2 function in mammary epithelial morphogenesis. J Biol Chem. 2009; 284(11):6877-6884.
    • (2009) J Biol Chem. , vol.284 , Issue.11 , pp. 6877-6884
    • Chen, C.S.1    Nelson, C.M.2    Khauv, D.3    Bennett, S.4    Radisky, E.S.5    Hirai, Y.6    Bissell, M.J.7    Radisky, D.C.8
  • 77
    • 84859142802 scopus 로고    scopus 로고
    • Growth of lung cancer cells in three-dimensional microenvironments reveals key features of tumor malignancy
    • Cichon MA, Gainullin VG, Zhang Y and Radisky DC. Growth of lung cancer cells in three-dimensional microenvironments reveals key features of tumor malignancy. Integrative Biology. 2012; 4(4):440-448.
    • (2012) Integrative Biology. , vol.4 , Issue.4 , pp. 440-448
    • Cichon, M.A.1    Gainullin, V.G.2    Zhang, Y.3    Radisky, D.C.4
  • 82
    • 67249120052 scopus 로고    scopus 로고
    • Efficient acquisition of dual metastasis organotropism to bone and lung through stable spontaneous fusion between MDA-MB-231 variants
    • Lu X and Kang Y. Efficient acquisition of dual metastasis organotropism to bone and lung through stable spontaneous fusion between MDA-MB-231 variants. Proc Natl Acad Sci U S A. 2009; 106(23):9385-9390.
    • (2009) Proc Natl Acad Sci U S A. , vol.106 , Issue.23 , pp. 9385-9390
    • Lu, X.1    Kang, Y.2
  • 91
    • 58549104080 scopus 로고    scopus 로고
    • The expO project (Expression Project for Oncology)
    • The International Genomics Consortium (IGC)
    • The International Genomics Consortium (IGC). The expO project (Expression Project for Oncology).
  • 93
    • 84856002018 scopus 로고    scopus 로고
    • TP53 genomics predict higher clinical and pathologic tumor response in operable early-stage breast cancer treated with docetaxel-capecitabine +/- trastuzumab
    • Gluck S, Ross JS, Royce M, McKenna EF, Jr., Perou CM, Avisar E and Wu L. TP53 genomics predict higher clinical and pathologic tumor response in operable early-stage breast cancer treated with docetaxel-capecitabine +/- trastuzumab. Breast Cancer Res Treat. 2012; 132(3):781-791.
    • (2012) Breast Cancer Res Treat. , vol.132 , Issue.3 , pp. 781-791
    • Gluck, S.1    Ross, J.S.2    Royce, M.3    McKenna, E.F.4    Perou, C.M.5    Avisar, E.6    Wu, L.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.