메뉴 건너뛰기




Volumn 46, Issue , 2006, Pages 301-315

Functional imaging of tumor proteolysis

Author keywords

Invasion; Migration; Organotypic models; Proteolytic pathways; Tumor microenvironment

Indexed keywords

PROTEINASE;

EID: 33144463387     PISSN: 03621642     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.pharmtox.45.120403.095853     Document Type: Review
Times cited : (60)

References (77)
  • 1
    • 0347383715 scopus 로고    scopus 로고
    • Matrix metalloproteinases and their tissue inhibitors direct cell fate during cancer development
    • Hojilla CV, Mohammed PF, Khokha R. 2003. Matrix metalloproteinases and their tissue inhibitors direct cell fate during cancer development. Br. J. Cancer 89:1817-21
    • (2003) Br. J. Cancer , vol.89 , pp. 1817-1821
    • Hojilla, C.V.1    Mohammed, P.F.2    Khokha, R.3
  • 3
    • 0037688169 scopus 로고    scopus 로고
    • Membrane anchored serine proteases: A rapidly expanding group of cell surface proteolytic enzymes with potential roles in cancer
    • Netzel-Arnett S, Hooper JD, Szabo R, Madison EL, Quigley JP, et al. 2003. Membrane anchored serine proteases: a rapidly expanding group of cell surface proteolytic enzymes with potential roles in cancer. Cancer Metastasis Rev. 22:237-58
    • (2003) Cancer Metastasis Rev. , vol.22 , pp. 237-258
    • Netzel-Arnett, S.1    Hooper, J.D.2    Szabo, R.3    Madison, E.L.4    Quigley, J.P.5
  • 5
    • 10044296973 scopus 로고    scopus 로고
    • Cysteine cathepsins in human cancer
    • Jedeszko C, Sloane BF. 2004. Cysteine cathepsins in human cancer. Biol. Chem. 385:1017-27
    • (2004) Biol. Chem. , vol.385 , pp. 1017-1027
    • Jedeszko, C.1    Sloane, B.F.2
  • 6
    • 11244261160 scopus 로고    scopus 로고
    • ADAMs: Key components in EGFR signalling and development
    • Blobel CP. 2005. ADAMs: key components in EGFR signalling and development. Nat. Rev. Mol. Cell. Biol. 6:32-43
    • (2005) Nat. Rev. Mol. Cell. Biol. , vol.6 , pp. 32-43
    • Blobel, C.P.1
  • 7
    • 0036512208 scopus 로고    scopus 로고
    • New functions for the matrix metalloproteinases in cancer progression
    • Egeblad M, Werb Z. 2002. New functions for the matrix metalloproteinases in cancer progression. Nat. Rev. 2:161-74
    • (2002) Nat. Rev. , vol.2 , pp. 161-174
    • Egeblad, M.1    Werb, Z.2
  • 8
    • 5444219883 scopus 로고    scopus 로고
    • Matrix metalloproteinases in cancer: From new functions to improved inhibition strategies
    • Folgueras AR, Pendas AM, Sanchez LM, Lopez-Otin C. 2004. Matrix metalloproteinases in cancer: from new functions to improved inhibition strategies. Int. J. Dev. Biol. 48:411-24
    • (2004) Int. J. Dev. Biol. , vol.48 , pp. 411-424
    • Folgueras, A.R.1    Pendas, A.M.2    Sanchez, L.M.3    Lopez-Otin, C.4
  • 9
    • 0037320124 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibitors-an emphasis on gastrointestinal malignancies
    • Chau I, Rigg A, Cunningham D. 2003. Matrix metalloproteinase inhibitors-an emphasis on gastrointestinal malignancies. Crit. Rev. Oncol. Hematol. 45:151-76
    • (2003) Crit. Rev. Oncol. Hematol. , vol.45 , pp. 151-176
    • Chau, I.1    Rigg, A.2    Cunningham, D.3
  • 10
    • 0037192458 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibitors and cancer: Trials and tribulations
    • Coussens LM, Fingleton B, Matrisian LM. 2002. Matrix metalloproteinase inhibitors and cancer: trials and tribulations. Science 295:2387-92
    • (2002) Science , vol.295 , pp. 2387-2392
    • Coussens, L.M.1    Fingleton, B.2    Matrisian, L.M.3
  • 11
    • 0036716282 scopus 로고    scopus 로고
    • Strategies for MMP inhibition in cancer: Innovations for the post-trial era
    • Overall CM, Lopez-Otin C. 2002. Strategies for MMP inhibition in cancer: innovations for the post-trial era. Nat. Rev. Cancer 2:657-72
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 657-672
    • Overall, C.M.1    Lopez-Otin, C.2
  • 12
    • 0036661037 scopus 로고    scopus 로고
    • Discovery of chemokine substrates for matrix metalloproteinases by exosite scanning: A new tool for degradomics
    • Overall CM, McQuibban GA, Clark-Lewis I. 2002. Discovery of chemokine substrates for matrix metalloproteinases by exosite scanning: a new tool for degradomics. Biol. Chem. 383:1059-66
    • (2002) Biol. Chem. , vol.383 , pp. 1059-1066
    • Overall, C.M.1    McQuibban, G.A.2    Clark-Lewis, I.3
  • 13
    • 2342460878 scopus 로고    scopus 로고
    • Membrane protease proteomics: Isotope-coded affinity tag MS identification of undescribed MT1-matrix metalloproteinase substrates
    • Tam EM, Morrison CJ, Wu YI, Stack MS, Overall CM. 2004. Membrane protease proteomics: isotope-coded affinity tag MS identification of undescribed MT1-matrix metalloproteinase substrates. Proc. Natl. Acad. Sci. USA 101:6917-22
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 6917-6922
    • Tam, E.M.1    Morrison, C.J.2    Wu, Y.I.3    Stack, M.S.4    Overall, C.M.5
  • 14
    • 3242777139 scopus 로고    scopus 로고
    • Protease degradomics: Mass spectrometry discovery of protease substrates and the CLIP-CHIP, a dedicated DNA microarray of all human proteases and inhibitors
    • Overall CM, Tam EM, Kappelhoff R, Connor A, Ewart T, et al. 2004. Protease degradomics: mass spectrometry discovery of protease substrates and the CLIP-CHIP, a dedicated DNA microarray of all human proteases and inhibitors. Biol. Chem. 385:493-504
    • (2004) Biol. Chem. , vol.385 , pp. 493-504
    • Overall, C.M.1    Tam, E.M.2    Kappelhoff, R.3    Connor, A.4    Ewart, T.5
  • 17
    • 0032746865 scopus 로고    scopus 로고
    • The protease consortium: An alliance to advance the understanding of proteolytic enzymes as therapeutic targets for cancer
    • Girands VL, Matrisian LM. 1999. The protease consortium: an alliance to advance the understanding of proteolytic enzymes as therapeutic targets for cancer. Mol. Carcinog. 26:139-42
    • (1999) Mol. Carcinog. , vol.26 , pp. 139-142
    • Girands, V.L.1    Matrisian, L.M.2
  • 18
    • 0016727321 scopus 로고
    • The use of amino acid derivatives of 4-methoxy-beta-napthylamine for the assay and subcellular localization of tissue proteinases
    • Smith RE, van Frank RM. 1975. The use of amino acid derivatives of 4-methoxy-beta-napthylamine for the assay and subcellular localization of tissue proteinases. Front. Biol. 43:193-249
    • (1975) Front. Biol. , vol.43 , pp. 193-249
    • Smith, R.E.1    Van Frank, R.M.2
  • 19
    • 0022415059 scopus 로고
    • Use of different derivatives of D-Val-Leu-Arg for studying kallikrein activities in cat submandibular glands and saliva
    • Garrett JR, Kidd A, Kyriacou K, Smith RE. 1985. Use of different derivatives of D-Val-Leu-Arg for studying kallikrein activities in cat submandibular glands and saliva. Histochem. J. 17:805-18
    • (1985) Histochem. J. , vol.17 , pp. 805-818
    • Garrett, J.R.1    Kidd, A.2    Kyriacou, K.3    Smith, R.E.4
  • 21
    • 0033556368 scopus 로고    scopus 로고
    • Enhanced production and activation of progelatinase a mediated by membrane-type 1 matrix metalloproteinase in human papillary thyroid carcinomas
    • Nakamura H, Ueno H, Yamashita K, Shimada T, Yamamoto E, et al. 1999. Enhanced production and activation of progelatinase A mediated by membrane-type 1 matrix metalloproteinase in human papillary thyroid carcinomas. Cancer Res. 59:467-73
    • (1999) Cancer Res. , vol.59 , pp. 467-473
    • Nakamura, H.1    Ueno, H.2    Yamashita, K.3    Shimada, T.4    Yamamoto, E.5
  • 22
    • 0028273525 scopus 로고
    • Membrane association of cathepsin B can be induced by transfection of human breast epithelial cells with c-Ha-ras oncogene
    • Sloane BF, Moin K, Sameni M, Tait LR, Rozhin J, Ziegler G. 1994. Membrane association of cathepsin B can be induced by transfection of human breast epithelial cells with c-Ha-ras oncogene. J. Cell Sci. 107:373-84
    • (1994) J. Cell Sci. , vol.107 , pp. 373-384
    • Sloane, B.F.1    Moin, K.2    Sameni, M.3    Tait, L.R.4    Rozhin, J.5    Ziegler, G.6
  • 25
    • 0021027432 scopus 로고
    • Involvement of a cathepsin B-like cysteine proteinase in platelet aggregation induced by tumor cells and their shed membrane vesicles
    • Cavanaugh PG, Sloane BF, Bajkowski AS, Gasic GJ, Gasic TB, Honn KV. 1983. Involvement of a cathepsin B-like cysteine proteinase in platelet aggregation induced by tumor cells and their shed membrane vesicles. Clin. Exp. Metastasis 1:297-308
    • (1983) Clin. Exp. Metastasis , vol.1 , pp. 297-308
    • Cavanaugh, P.G.1    Sloane, B.F.2    Bajkowski, A.S.3    Gasic, G.J.4    Gasic, T.B.5    Honn, K.V.6
  • 26
    • 0028145293 scopus 로고
    • Cathepsin B expression in colorectal carcinomas correlates with tumor progression and shortened patient survival
    • Campo E, Munoz J, Miquel R, Palacin A, Cardesa A, et al. 1994. Cathepsin B expression in colorectal carcinomas correlates with tumor progression and shortened patient survival. Am. J. Pathol. 145:301-9
    • (1994) Am. J. Pathol. , vol.145 , pp. 301-309
    • Campo, E.1    Munoz, J.2    Miquel, R.3    Palacin, A.4    Cardesa, A.5
  • 28
    • 0026575258 scopus 로고
    • Degradation of extracellular-matrix proteins by human cathepsin B from normal and tumour tissues
    • Buck MR, Karustis DG, Day NA, Honn KV, Sloane BF. 1992. Degradation of extracellular-matrix proteins by human cathepsin B from normal and tumour tissues. Biochem. J. 282:273-78
    • (1992) Biochem. J. , vol.282 , pp. 273-278
    • Buck, M.R.1    Karustis, D.G.2    Day, N.A.3    Honn, K.V.4    Sloane, B.F.5
  • 29
    • 0028113717 scopus 로고
    • Increased gelatinase a (MMP-2) and cathepsin B activity in microdissected human colon cancer
    • Emmert-Buck MR, Roth MJ, Zhuang Z, Campo E, Rozhin J, et al. 1994. Increased gelatinase A (MMP-2) and cathepsin B activity in microdissected human colon cancer. Am. J. Pathol. 145:1285-90
    • (1994) Am. J. Pathol. , vol.145 , pp. 1285-1290
    • Emmert-Buck, M.R.1    Roth, M.J.2    Zhuang, Z.3    Campo, E.4    Rozhin, J.5
  • 30
    • 0033802696 scopus 로고    scopus 로고
    • Comparative localization of cathepsin B protein and activity in colorectal cancer
    • Hazen LG, Bleeker FE, Lauritzen B, Bahns S, Song J, et al. 2000. Comparative localization of cathepsin B protein and activity in colorectal cancer. J. Histochem. Cytochem. 48:1421-30
    • (2000) J. Histochem. Cytochem. , vol.48 , pp. 1421-1430
    • Hazen, L.G.1    Bleeker, F.E.2    Lauritzen, B.3    Bahns, S.4    Song, J.5
  • 31
    • 0001071353 scopus 로고    scopus 로고
    • Cancer invasion and tissue remodeling-cooperation of protease systems and cell types
    • Dano K, Romer J, Nielsen BS, Bjorn S, Pyke C, et al. 1999. Cancer invasion and tissue remodeling-cooperation of protease systems and cell types. APMIS 107:120-27
    • (1999) APMIS , vol.107 , pp. 120-127
    • Dano, K.1    Romer, J.2    Nielsen, B.S.3    Bjorn, S.4    Pyke, C.5
  • 33
    • 0034486945 scopus 로고    scopus 로고
    • Imaging proteolysis by living human breast cancer cells
    • Sameni M, Moin K, Sloane BF. 2000. Imaging proteolysis by living human breast cancer cells. Neoplasia 2:496-504
    • (2000) Neoplasia , vol.2 , pp. 496-504
    • Sameni, M.1    Moin, K.2    Sloane, B.F.3
  • 34
    • 0034930565 scopus 로고    scopus 로고
    • Imaging proteolysis by living human glioma cells
    • Sameni M, Dosescu J, Sloane BF. 2001. Imaging proteolysis by living human glioma cells. Biol. Chem. 382:785-88
    • (2001) Biol. Chem. , vol.382 , pp. 785-788
    • Sameni, M.1    Dosescu, J.2    Sloane, B.F.3
  • 35
    • 0034329464 scopus 로고    scopus 로고
    • Rac1-induced endocytosis is associated with intracellular proteolysis during migration through a 3-dimensional matrix
    • Ahram M, Sameni M, Qiu R-G, Linebaugh B, Kirn D, Sloane BF. 2000. Rac1-induced endocytosis is associated with intracellular proteolysis during migration through a 3-dimensional matrix. Exp. Cell Res. 260:292-303
    • (2000) Exp. Cell Res. , vol.260 , pp. 292-303
    • Ahram, M.1    Sameni, M.2    Qiu, R.-G.3    Linebaugh, B.4    Kirn, D.5    Sloane, B.F.6
  • 36
    • 0242577116 scopus 로고    scopus 로고
    • Functional imaging of proteolysis: Stromal and inflammatory cells increase tumor proteolysis
    • Sameni M, Dosescu J, Moin K, Sloane BF. 2003. Functional imaging of proteolysis: stromal and inflammatory cells increase tumor proteolysis. Mol. Imaging 2:159-75
    • (2003) Mol. Imaging , vol.2 , pp. 159-175
    • Sameni, M.1    Dosescu, J.2    Moin, K.3    Sloane, B.F.4
  • 37
    • 15744371624 scopus 로고    scopus 로고
    • Bone microenvironment modulates expression and activity of cathepsin B in prostate cancer
    • Podgorski I, Linebaugh BE, Sameni M, Jedeszko C, Bhagat S, et al. 2005. Bone microenvironment modulates expression and activity of cathepsin B in prostate cancer. Neoplasia 7:207-23
    • (2005) Neoplasia , vol.7 , pp. 207-223
    • Podgorski, I.1    Linebaugh, B.E.2    Sameni, M.3    Jedeszko, C.4    Bhagat, S.5
  • 38
    • 17844362479 scopus 로고    scopus 로고
    • Caveolin-1 mediates expression and localization of cathepsin B, pro-urokinase plasminogen activator and their cell surface receptors in human colorectal carcinoma cells
    • Cavallo-Medved D, Mai J, Dosescu J, Sameni M, Sloane BF. 2005. Caveolin-1 mediates expression and localization of cathepsin B, pro-urokinase plasminogen activator and their cell surface receptors in human colorectal carcinoma cells. J. Cell Sci. 18:1493-503
    • (2005) J. Cell Sci. , vol.18 , pp. 1493-1503
    • Cavallo-Medved, D.1    Mai, J.2    Dosescu, J.3    Sameni, M.4    Sloane, B.F.5
  • 39
    • 0034054576 scopus 로고    scopus 로고
    • Selective targeting of lysosomal cysteine proteases with radiolabeled electrophilic substrate analogs
    • Bogyo M, Verhelst S, Bellingard-Dubouchaud V, Toba S, Greenbaum D. 2000. Selective targeting of lysosomal cysteine proteases with radiolabeled electrophilic substrate analogs. Chem. Biol. 7:27-38
    • (2000) Chem. Biol. , vol.7 , pp. 27-38
    • Bogyo, M.1    Verhelst, S.2    Bellingard-Dubouchaud, V.3    Toba, S.4    Greenbaum, D.5
  • 40
    • 1542495339 scopus 로고    scopus 로고
    • Proteolytic and non-proteolytic migration of tumour cells and leucocytes
    • Friedl P, Wolf K. 2003. Proteolytic and non-proteolytic migration of tumour cells and leucocytes. Biochem. Soc. Symp. 70:277-85
    • (2003) Biochem. Soc. Symp. , vol.70 , pp. 277-285
    • Friedl, P.1    Wolf, K.2
  • 41
    • 12344252751 scopus 로고    scopus 로고
    • Mechanisms of cancer cell invasion
    • Sahai E. 2005. Mechanisms of cancer cell invasion. Curr. Opin. Genet. Dev. 15:87-96
    • (2005) Curr. Opin. Genet. Dev. , vol.15 , pp. 87-96
    • Sahai, E.1
  • 42
    • 0030177259 scopus 로고    scopus 로고
    • Suicidal tumor proteases
    • Sloane BF. 1996. Suicidal tumor proteases. Nat. Biotech. 14:826-27
    • (1996) Nat. Biotech. , vol.14 , pp. 826-827
    • Sloane, B.F.1
  • 43
    • 0021833967 scopus 로고
    • Local degradation of fibronectin at sites of expression of the transforming gene product pp60src
    • Chen WT, Chen JM, Parsons SJ, Parsons JT. 1985. Local degradation of fibronectin at sites of expression of the transforming gene product pp60src. Nature 316:156-58
    • (1985) Nature , vol.316 , pp. 156-158
    • Chen, W.T.1    Chen, J.M.2    Parsons, S.J.3    Parsons, J.T.4
  • 44
    • 1842787815 scopus 로고    scopus 로고
    • The urokinase receptor (uPAR) and the uPAR-associated protein (uPARAP/Endo180): Membrane proteins engaged in matrix turnover during tissue remodeling
    • Behrendt N. 2004. The urokinase receptor (uPAR) and the uPAR-associated protein (uPARAP/Endo180): membrane proteins engaged in matrix turnover during tissue remodeling. Biol. Chem. 385:103-36
    • (2004) Biol. Chem. , vol.385 , pp. 103-136
    • Behrendt, N.1
  • 45
    • 22344436842 scopus 로고    scopus 로고
    • Intracellular collagen degradation mediated by uPARAP/Endo180 is a major pathway of extracellular matrix turnover during malignancy
    • Curino AC, Engelholm LH, Yamada SS, Holmbeck K, Lund LR, et al. 2005. Intracellular collagen degradation mediated by uPARAP/Endo180 is a major pathway of extracellular matrix turnover during malignancy. J. Cell Biol. 169:977-85
    • (2005) J. Cell Biol. , vol.169 , pp. 977-985
    • Curino, A.C.1    Engelholm, L.H.2    Yamada, S.S.3    Holmbeck, K.4    Lund, L.R.5
  • 46
    • 0037484174 scopus 로고    scopus 로고
    • Modeling tissue-specific signaling and organ function in three dimensions
    • Schmeichel KL, Bissell MJ. 2003. Modeling tissue-specific signaling and organ function in three dimensions. J. Cell Sci. 116:2377-88
    • (2003) J. Cell Sci. , vol.116 , pp. 2377-2388
    • Schmeichel, K.L.1    Bissell, M.J.2
  • 47
    • 22944463061 scopus 로고    scopus 로고
    • Use of three-dimensional basement membrane cultures to model oncogene-induced changes in mammary epithelial morphogenesis
    • Shaw KR, Wrobel CN, Brugge JS. 2004. Use of three-dimensional basement membrane cultures to model oncogene-induced changes in mammary epithelial morphogenesis. J. Mammary Gland Blol. Neoplasia 9:297-310
    • (2004) J. Mammary Gland Blol. Neoplasia , vol.9 , pp. 297-310
    • Shaw, K.R.1    Wrobel, C.N.2    Brugge, J.S.3
  • 48
    • 0034725119 scopus 로고    scopus 로고
    • Human procathepsin B interacts with the annexin II tetramer on the surface of tumor cells
    • Mai J, Finley R, Waisman DM, Sloane BF. 2000. Human procathepsin B interacts with the annexin II tetramer on the surface of tumor cells. J. Biol. Chem. 275:12806-12
    • (2000) J. Biol. Chem. , vol.275 , pp. 12806-12812
    • Mai, J.1    Finley, R.2    Waisman, D.M.3    Sloane, B.F.4
  • 49
    • 0034615565 scopus 로고    scopus 로고
    • Cell surface complex of cathepsin B/annexin II tetramer in malignant progression
    • Mai J, Waisman DM, Sloane BF. 2000. Cell surface complex of cathepsin B/annexin II tetramer in malignant progression. Biophys. Biochim. Acta 1477:215-30
    • (2000) Biophys. Biochim. Acta , vol.1477 , pp. 215-230
    • Mai, J.1    Waisman, D.M.2    Sloane, B.F.3
  • 51
    • 13244275005 scopus 로고    scopus 로고
    • Integrin beta1 is required for the invasive behaviour but not proliferation of squamous cell carcinoma cells in vivo
    • Brockbank EC, Bridges J, Marshall CJ, Sahai E. 2005. Integrin beta1 is required for the invasive behaviour but not proliferation of squamous cell carcinoma cells in vivo. Br. J. Cancer 17:102-12
    • (2005) Br. J. Cancer , vol.17 , pp. 102-112
    • Brockbank, E.C.1    Bridges, J.2    Marshall, C.J.3    Sahai, E.4
  • 52
    • 0042354574 scopus 로고    scopus 로고
    • Differing modes of tumour cell invasion have distinct requirements for Rho/ROCK signaling and extracellular proteolysis
    • Sahai E, Marshall CJ. 2003. Differing modes of tumour cell invasion have distinct requirements for Rho/ROCK signaling and extracellular proteolysis. Nat. Cell Biol. 5:690-92
    • (2003) Nat. Cell Biol. , vol.5 , pp. 690-692
    • Sahai, E.1    Marshall, C.J.2
  • 53
    • 15244351837 scopus 로고    scopus 로고
    • Functional imaging of pericellular proteolysis in cancer cell invasion
    • Wolf K, Friedl P. 2005. Functional imaging of pericellular proteolysis in cancer cell invasion. Biochimie 87:315-20
    • (2005) Biochimie , vol.87 , pp. 315-320
    • Wolf, K.1    Friedl, P.2
  • 54
    • 0029894671 scopus 로고    scopus 로고
    • Stromal cell expression of components of matrix-degrading protease systems in human cancer
    • Hewitt R, Dano K. 1996. Stromal cell expression of components of matrix-degrading protease systems in human cancer. Enzyme Protein 49:163-73
    • (1996) Enzyme Protein , vol.49 , pp. 163-173
    • Hewitt, R.1    Dano, K.2
  • 55
    • 0034123653 scopus 로고    scopus 로고
    • Interactions between tumour cells and stromal cells and proteolytic modification of the extracellular matrix by metalloproteinases in cancer
    • DeClerck YA. 2000. Interactions between tumour cells and stromal cells and proteolytic modification of the extracellular matrix by metalloproteinases in cancer. Eur. J. Cancer 36:1258-68
    • (2000) Eur. J. Cancer , vol.36 , pp. 1258-1268
    • Declerck, Y.A.1
  • 56
    • 0035835829 scopus 로고    scopus 로고
    • Heterotypic signaling between epithelial tumor cells and fibroblasts in carcinoma formation
    • Elenbaas B, Weinberg RA. 2001. Heterotypic signaling between epithelial tumor cells and fibroblasts in carcinoma formation. Exp. Cell Res. 264:169-84
    • (2001) Exp. Cell Res. , vol.264 , pp. 169-184
    • Elenbaas, B.1    Weinberg, R.A.2
  • 57
    • 10044261295 scopus 로고    scopus 로고
    • T cell-derived matrix metalloproteinase-9 in breast cancer: Friend or foe?
    • Owen JL, Iragavarapu-Charyulu V, Lopez DM. 2004. T cell-derived matrix metalloproteinase-9 in breast cancer: friend or foe? Breast Dis. 20:143-53
    • (2004) Breast Dis. , vol.20 , pp. 143-153
    • Owen, J.L.1    Iragavarapu-Charyulu, V.2    Lopez, D.M.3
  • 58
    • 0035176717 scopus 로고    scopus 로고
    • Tumor progression: Defining the soil round the tumor seed
    • McCawley LJ, Matrisian LM. 2001. Tumor progression: defining the soil round the tumor seed. Curr. Biol. 11:R25-27
    • (2001) Curr. Biol. , vol.11
    • McCawley, L.J.1    Matrisian, L.M.2
  • 60
    • 0142041935 scopus 로고    scopus 로고
    • Cancer invasion: Watch your neighbourhood!
    • Quaranta V, Giannelli G. 2003. Cancer invasion: watch your neighbourhood! Tumori 89:343-48
    • (2003) Tumori , vol.89 , pp. 343-348
    • Quaranta, V.1    Giannelli, G.2
  • 62
    • 0344438130 scopus 로고    scopus 로고
    • Near-infrared optical imaging of proteases in cancer
    • Mahmood U, Weissleder R. 2003. Near-infrared optical imaging of proteases in cancer. Mol. Cancer Ther. 2:489-96
    • (2003) Mol. Cancer Ther. , vol.2 , pp. 489-496
    • Mahmood, U.1    Weissleder, R.2
  • 64
    • 0036096896 scopus 로고    scopus 로고
    • Cellular activation of the self-quenched fluorescent reporter probe in tumor microenvironment
    • Bogdanov AA Jr, Lin CP, Simonova M, Matuszewski L, Weissleder R. 2002. Cellular activation of the self-quenched fluorescent reporter probe in tumor microenvironment. Neoplasia 4:228-36
    • (2002) Neoplasia , vol.4 , pp. 228-236
    • Bogdanov Jr., A.A.1    Lin, C.P.2    Simonova, M.3    Matuszewski, L.4    Weissleder, R.5
  • 66
    • 0035947634 scopus 로고    scopus 로고
    • Targeting of tumor cells by cell surface urokinase plasminogen activator-dependent anthrax toxin
    • Liu S, Bugge TH, Leppla SH. 2001. Targeting of tumor cells by cell surface urokinase plasminogen activator-dependent anthrax toxin. J. Biol. Chem. 276:17976-84
    • (2001) J. Biol. Chem. , vol.276 , pp. 17976-17984
    • Liu, S.1    Bugge, T.H.2    Leppla, S.H.3
  • 68
    • 0030878999 scopus 로고    scopus 로고
    • Optimal subsite occupany and design of a selective inhibitor of urokinase
    • Ke SH, Coombs GS, Tachias K, Corey DR, Madison EL. 1997. Optimal subsite occupany and design of a selective inhibitor of urokinase. J. Biol. Chem. 272:20456-62
    • (1997) J. Biol. Chem. , vol.272 , pp. 20456-20462
    • Ke, S.H.1    Coombs, G.S.2    Tachias, K.3    Corey, D.R.4    Madison, E.L.5
  • 69
    • 0030997660 scopus 로고    scopus 로고
    • Distinguishing the specificities of closely related proteases. Role of P3 in substrate and inhibitor discrimination between tissue-type plasminogen activator and urokinase
    • Ke SH, Coombs GS, Tachias K, Navre M, Corey DR, Madison EL. 1997. Distinguishing the specificities of closely related proteases. Role of P3 in substrate and inhibitor discrimination between tissue-type plasminogen activator and urokinase. J. Biol. Chem. 272:16603-9
    • (1997) J. Biol. Chem. , vol.272 , pp. 16603-16609
    • Ke, S.H.1    Coombs, G.S.2    Tachias, K.3    Navre, M.4    Corey, D.R.5    Madison, E.L.6
  • 70
    • 1142306153 scopus 로고    scopus 로고
    • Design, synthesis, and characterization of urokinase plasminogen- activator-sensitive near-infrared reporter
    • Law B, Curino A, Bugge TH, Weissleder R, Tung CH. 2004. Design, synthesis, and characterization of urokinase plasminogen-activator-sensitive near-infrared reporter. Chem. Biol. 11:99-106
    • (2004) Chem. Biol. , vol.11 , pp. 99-106
    • Law, B.1    Curino, A.2    Bugge, T.H.3    Weissleder, R.4    Tung, C.H.5
  • 71
    • 13644263240 scopus 로고    scopus 로고
    • Optical zymography for specific detection of urokinase plasminogen activator activity in biological samples
    • Law B, Hsiao JK, Bugge TH, Weissleder R, Tung CH. 2005. Optical zymography for specific detection of urokinase plasminogen activator activity in biological samples. Anal. Biochem. 338:151-58
    • (2005) Anal. Biochem. , vol.338 , pp. 151-158
    • Law, B.1    Hsiao, J.K.2    Bugge, T.H.3    Weissleder, R.4    Tung, C.H.5
  • 72
    • 1242343929 scopus 로고    scopus 로고
    • Development of a novel fluorogenic proteolytic beacon for in vivo detection and imaging of tumour-associated matrix metalloproteinase-7 activity
    • McIntyre JO, Fingleton B, Wells KS, Piston DW, Lynch CC, et al. 2004. Development of a novel fluorogenic proteolytic beacon for in vivo detection and imaging of tumour-associated matrix metalloproteinase-7 activity. Biochem. J. 377:617-28
    • (2004) Biochem. J. , vol.377 , pp. 617-628
    • McIntyre, J.O.1    Fingleton, B.2    Wells, K.S.3    Piston, D.W.4    Lynch, C.C.5
  • 73
  • 74
    • 2342603891 scopus 로고    scopus 로고
    • Cathepsin cysteine proteases are effectors of invasive growth and angiogenesis during multistage tumorigenesis
    • Joyce JA, Baruch A, Chehade K, Meyer-Morse N, Giraudo E, et al. 2004. Cathepsin cysteine proteases are effectors of invasive growth and angiogenesis during multistage tumorigenesis. Cancer Cell 5:443-53
    • (2004) Cancer Cell , vol.5 , pp. 443-453
    • Joyce, J.A.1    Baruch, A.2    Chehade, K.3    Meyer-Morse, N.4    Giraudo, E.5
  • 75
    • 33644825565 scopus 로고    scopus 로고
    • Dynamic imaging of protease activity with fluorescently quenched activity-based probes
    • In press
    • 74a. Blum G, Mullins SR, Keren K, Fonovic M, Jedeszko C, et al. 2005. Dynamic imaging of protease activity with fluorescently quenched activity-based probes. Nat. Chem. Biol. In press
    • (2005) Nat. Chem. Biol.
    • Blum, G.1    Mullins, S.R.2    Keren, K.3    Fonovic, M.4    Jedeszko, C.5
  • 76
    • 0344874727 scopus 로고    scopus 로고
    • Molecular imaging of proteolytic activity in cancer
    • McIntyre JO, Matrisian LM. 2003. Molecular imaging of proteolytic activity in cancer. J. Cell Biochem. 90:1087-97
    • (2003) J. Cell Biochem. , vol.90 , pp. 1087-1097
    • McIntyre, J.O.1    Matrisian, L.M.2
  • 77
    • 0037455576 scopus 로고    scopus 로고
    • Compensation mechanism in tumor cell migration: Mesenchymal-amoeboid transition after blocking of pericellular proteolysis
    • Wolf K, Mazo I, Leung H, Engelke K, von Andrian UH, et al. 2003. Compensation mechanism in tumor cell migration: mesenchymal-amoeboid transition after blocking of pericellular proteolysis. J. Cell Biol. 160:267-77
    • (2003) J. Cell Biol. , vol.160 , pp. 267-277
    • Wolf, K.1    Mazo, I.2    Leung, H.3    Engelke, K.4    Von Andrian, U.H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.