메뉴 건너뛰기




Volumn 8, Issue 3, 2007, Pages 245-257

In search of partners: Linking extracellular proteases to substrates

Author keywords

[No Author keywords available]

Indexed keywords

ADAM PROTEIN; DNA; PROTEINASE; TUMOR NECROSIS FACTOR ALPHA;

EID: 33847276695     PISSN: 14710072     EISSN: 14710080     Source Type: Journal    
DOI: 10.1038/nrm2120     Document Type: Review
Times cited : (297)

References (122)
  • 1
    • 37049044629 scopus 로고
    • An enzyme cascade in the blood clotting mechanism, and its function as a biochemical amplifier
    • Macfarlane, R. G. An enzyme cascade in the blood clotting mechanism, and its function as a biochemical amplifier. Nature 202, 498-499 (1964).
    • (1964) Nature , vol.202 , pp. 498-499
    • Macfarlane, R.G.1
  • 2
    • 37049242417 scopus 로고
    • Waterfall sequence for intrinsic blood clotting
    • Davie, E. W. & Ratnoff, O. D. Waterfall sequence for intrinsic blood clotting. Science 145, 1310-1312 (1964).
    • (1964) Science , vol.145 , pp. 1310-1312
    • Davie, E.W.1    Ratnoff, O.D.2
  • 3
    • 0001490840 scopus 로고
    • Identification of a peptide released during autocatalytic activation of trypsinogen
    • Davie, E. W. & Neurath, H. Identification of a peptide released during autocatalytic activation of trypsinogen. J. Biol. Chem. 212, 515-529 (1955).
    • (1955) J. Biol. Chem , vol.212 , pp. 515-529
    • Davie, E.W.1    Neurath, H.2
  • 4
    • 8044257704 scopus 로고    scopus 로고
    • A metalloprotease disintegrin that releases tumour-necrosis factor-α from cells
    • Black, R. et al. A metalloprotease disintegrin that releases tumour-necrosis factor-α from cells. Nature 385, 729-733 (1997).
    • (1997) Nature , vol.385 , pp. 729-733
    • Black, R.1
  • 5
    • 8044250278 scopus 로고    scopus 로고
    • Cloning of a disintegrin metalloproteinase that processes precursor tumour-necrosis factor-α
    • Moss, M. L. et al. Cloning of a disintegrin metalloproteinase that processes precursor tumour-necrosis factor-α. Nature 385, 733-736 (1997).
    • (1997) Nature , vol.385 , pp. 733-736
    • Moss, M.L.1
  • 6
    • 0032515018 scopus 로고    scopus 로고
    • Peschon, J. J. et al. An essential role for ectodomain shedding in mammalian development. Science 282, 1281-1284 (1998). An excellent example of linking an enzyme, ADAM17, to several substrates, including TGFα, through the analysis of Adam17-knockout mice and cell-based assays in cells lacking ADAM17, derived from these mice.
    • Peschon, J. J. et al. An essential role for ectodomain shedding in mammalian development. Science 282, 1281-1284 (1998). An excellent example of linking an enzyme, ADAM17, to several substrates, including TGFα, through the analysis of Adam17-knockout mice and cell-based assays in cells lacking ADAM17, derived from these mice.
  • 7
    • 0034682885 scopus 로고    scopus 로고
    • Inflammation dampened by gelatinase A cleavage of monocyte chemoattractant protein-3
    • McQuibban, G. A. et al. Inflammation dampened by gelatinase A cleavage of monocyte chemoattractant protein-3. Science 289, 1202-1206 (2000).
    • (2000) Science , vol.289 , pp. 1202-1206
    • McQuibban, G.A.1
  • 8
    • 3543134126 scopus 로고    scopus 로고
    • Matrix metalloproteinases as modulators of inflammation and innate immunity
    • Parks, W. C., Wilson, C. L. & López-Boado. Matrix metalloproteinases as modulators of inflammation and innate immunity. Nature Rev. Immunol. 4, 617-629 (2004).
    • (2004) Nature Rev. Immunol , vol.4 , pp. 617-629
    • Parks, W.C.1    Wilson, C.L.2    López-Boado3
  • 9
    • 3042749811 scopus 로고    scopus 로고
    • Epithelial cell motility on laminin-5: Regulation by matrix assembly, proteolysis, integrins and erbB receptors
    • Hintermann, E. & Quaranta, V. Epithelial cell motility on laminin-5: regulation by matrix assembly, proteolysis, integrins and erbB receptors. Matrix Biol. 23, 75-85 (2004).
    • (2004) Matrix Biol , vol.23 , pp. 75-85
    • Hintermann, E.1    Quaranta, V.2
  • 10
    • 0029944122 scopus 로고    scopus 로고
    • Angiostatin induces and sustains dormancy of human primary tumors in mice
    • O'Reilly, M. S., Holmgren, L., Chen, C. & Folkman, J. Angiostatin induces and sustains dormancy of human primary tumors in mice. Nature Med. 2, 689-692 (1996).
    • (1996) Nature Med , vol.2 , pp. 689-692
    • O'Reilly, M.S.1    Holmgren, L.2    Chen, C.3    Folkman, J.4
  • 11
    • 0033617532 scopus 로고    scopus 로고
    • Effects of angiogenesis inhibitors on multistage carcinogenesis in mice
    • Bergers, G., Javaherian, K., Lo, K. M., Folkman, J. & Hanahan, D. Effects of angiogenesis inhibitors on multistage carcinogenesis in mice. Science 284, 808-812 (1999).
    • (1999) Science , vol.284 , pp. 808-812
    • Bergers, G.1    Javaherian, K.2    Lo, K.M.3    Folkman, J.4    Hanahan, D.5
  • 12
    • 21644489724 scopus 로고    scopus 로고
    • Dilating the degradome: Matrix metalloproteinase-2 cuts to the heart of the matter
    • Overall, C. M. Dilating the degradome: matrix metalloproteinase-2 cuts to the heart of the matter. Biochem. J. 383, e5-e7 (2004).
    • (2004) Biochem. J , vol.383
    • Overall, C.M.1
  • 13
    • 33644545381 scopus 로고    scopus 로고
    • Validating MMPs as drug targets and anti-targets for cancer therapy
    • Overall, C. M. & Kleifeld, O. Validating MMPs as drug targets and anti-targets for cancer therapy. Nature Rev. Cancer 6, 227-239 (2006).
    • (2006) Nature Rev. Cancer , vol.6 , pp. 227-239
    • Overall, C.M.1    Kleifeld, O.2
  • 14
    • 33748308883 scopus 로고    scopus 로고
    • Targeting proteases: Successes, failures and future prospects
    • Turk, B. Targeting proteases: successes, failures and future prospects. Nature Rev. Drug Discov. 5, 785-799 (2006).
    • (2006) Nature Rev. Drug Discov , vol.5 , pp. 785-799
    • Turk, B.1
  • 15
    • 0036302814 scopus 로고    scopus 로고
    • Protease degradomics: A new challenge for proteomics
    • López-Otin, C. & Overall, C. M. Protease degradomics: a new challenge for proteomics. Nature Rev. Mol. Cell Biol. 3, 509-519 (2002).
    • (2002) Nature Rev. Mol. Cell Biol , vol.3 , pp. 509-519
    • López-Otin, C.1    Overall, C.M.2
  • 16
    • 9844253890 scopus 로고    scopus 로고
    • Identification and characterization of a pro-tumor necrosis factor-α-processing enzyme from the ADAM family of zinc metalloproteases
    • Rosendahl, M. S. et al. Identification and characterization of a pro-tumor necrosis factor-α-processing enzyme from the ADAM family of zinc metalloproteases. J. Biol. Chem. 272, 24588-24593 (1997).
    • (1997) J. Biol. Chem , vol.272 , pp. 24588-24593
    • Rosendahl, M.S.1
  • 17
    • 5644290647 scopus 로고    scopus 로고
    • Evaluation of the contribution of different ADAMs to TNF? shedding and of the function of the TNFα ectodomain in ensuring selective stimulated shedding by the TNFα convertase (TACE/ADAM17)
    • Zheng, Y., Saftig, P., Hartmann, D. & Blobel, C. Evaluation of the contribution of different ADAMs to TNF? shedding and of the function of the TNFα ectodomain in ensuring selective stimulated shedding by the TNFα convertase (TACE/ADAM17). J. Biol. Chem. 279, 42898-42906 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 42898-42906
    • Zheng, Y.1    Saftig, P.2    Hartmann, D.3    Blobel, C.4
  • 18
    • 0033966350 scopus 로고    scopus 로고
    • Matrix metalloproteinase-7-dependent release of tumor necrosis factor-α in a model of herniated disc resorption
    • Haro, H. et al. Matrix metalloproteinase-7-dependent release of tumor necrosis factor-α in a model of herniated disc resorption. J. Clin. Invest. 105, 143-150 (2000).
    • (2000) J. Clin. Invest , vol.105 , pp. 143-150
    • Haro, H.1
  • 19
    • 2342460878 scopus 로고    scopus 로고
    • Tam, E. M., Morrison, C. J., Wu, Y. I., Stack, M. S. & Overall, C. M. Membrane protease proteomics: isotope-coded affinity tag MS identification of undescribed MT1-matrix metalloproteinase substrates. Proc. Natl Acad. Sci. USA 101, 6917-6922 (2004). A key paper describing the use of isotope mass tags and liquid-chromatography-based massspectrometric identification of cleaved products of native substrates in the cellular context.
    • Tam, E. M., Morrison, C. J., Wu, Y. I., Stack, M. S. & Overall, C. M. Membrane protease proteomics: isotope-coded affinity tag MS identification of undescribed MT1-matrix metalloproteinase substrates. Proc. Natl Acad. Sci. USA 101, 6917-6922 (2004). A key paper describing the use of isotope mass tags and liquid-chromatography-based massspectrometric identification of cleaved products of native substrates in the cellular context.
  • 20
    • 0141653868 scopus 로고    scopus 로고
    • Metalloproteinase cleavage of the chemokine SDF-1α induces neuronal apoptosis in HIV encephalitis
    • Zhang, K. et al. Metalloproteinase cleavage of the chemokine SDF-1α induces neuronal apoptosis in HIV encephalitis. Nature Neurosci. 6, 1064-1071 (2003).
    • (2003) Nature Neurosci , vol.6 , pp. 1064-1071
    • Zhang, K.1
  • 21
    • 33846821908 scopus 로고    scopus 로고
    • Proteomic discovery of protease substrates
    • Shilling, O. & Overall, C. M. Proteomic discovery of protease substrates. Curr. Opin. Chem. Biol. 11, 1-10 (2007).
    • (2007) Curr. Opin. Chem. Biol , vol.11 , pp. 1-10
    • Shilling, O.1    Overall, C.M.2
  • 22
    • 0033525037 scopus 로고    scopus 로고
    • Metalloprotease-disintegrin MDC9: Intracellular maturation and catalytic activity
    • Roghani, M. et al. Metalloprotease-disintegrin MDC9: intracellular maturation and catalytic activity. J. Biol. Chem. 274, 3531-3540 (1999).
    • (1999) J. Biol. Chem , vol.274 , pp. 3531-3540
    • Roghani, M.1
  • 24
    • 12144290186 scopus 로고    scopus 로고
    • Catalytic activity of human ADAM33
    • Zou, J. et al. Catalytic activity of human ADAM33. J. Biol. Chem. 279, 9818-9830 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 9818-9830
    • Zou, J.1
  • 25
    • 0028918852 scopus 로고
    • Rapid identification of highly active and selective substrates for stromelysin and matrilysin using bacteriophage peptide display libraries
    • Smith, M. M., Shi, L. & Navre, M. Rapid identification of highly active and selective substrates for stromelysin and matrilysin using bacteriophage peptide display libraries. J. Biol. Chem. 270, 6440-6449 (1995).
    • (1995) J. Biol. Chem , vol.270 , pp. 6440-6449
    • Smith, M.M.1    Shi, L.2    Navre, M.3
  • 26
    • 0027316004 scopus 로고    scopus 로고
    • Matthews, D. J. & Wells, J. A. Substrate phage: selection of protease substrates by monovalent phage display. Science 260, 1113-1117 (1993). A classic paper on the development of phage display to screen for protease-cleavage sites.
    • Matthews, D. J. & Wells, J. A. Substrate phage: selection of protease substrates by monovalent phage display. Science 260, 1113-1117 (1993). A classic paper on the development of phage display to screen for protease-cleavage sites.
  • 27
    • 0034263761 scopus 로고    scopus 로고
    • Rapid identification of substrates for novel proteases using a combinatorial peptide library
    • Rosse, G. et al. Rapid identification of substrates for novel proteases using a combinatorial peptide library. J. Comb. Chem. 2, 461-466 (2000).
    • (2000) J. Comb. Chem , vol.2 , pp. 461-466
    • Rosse, G.1
  • 28
    • 1542315414 scopus 로고    scopus 로고
    • Using peptide libraries to identify optimal cleavage motifs for proteolytic enzymes
    • Turk, B. E. & Cantley, L. C. Using peptide libraries to identify optimal cleavage motifs for proteolytic enzymes. Methods 32, 398-405 (2004).
    • (2004) Methods , vol.32 , pp. 398-405
    • Turk, B.E.1    Cantley, L.C.2
  • 29
    • 0025214021 scopus 로고
    • Engineering human prolactin to bind to the human growth hormone receptor
    • Cunningham, B. C., Henner, D. J. & Wells, J. A. Engineering human prolactin to bind to the human growth hormone receptor. Science 247, 1461-1465 (1990).
    • (1990) Science , vol.247 , pp. 1461-1465
    • Cunningham, B.C.1    Henner, D.J.2    Wells, J.A.3
  • 30
    • 0037928769 scopus 로고    scopus 로고
    • The role of dipeptidyl peptidase IV in the cleavage of glucagon family peptides: In vivo metabolism of pituitary adenylate cyclase activating polypeptide-(1-38)
    • Zhu, L. et al. The role of dipeptidyl peptidase IV in the cleavage of glucagon family peptides: in vivo metabolism of pituitary adenylate cyclase activating polypeptide-(1-38). J. Biol. Chem. 278, 22418-22423 (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 22418-22423
    • Zhu, L.1
  • 31
    • 0030849093 scopus 로고    scopus 로고
    • Thornberry, N. A. et al. A combinatorial approach defines specificities of members of the caspase family and granzyme B. Functional relationships established for key mediators of apoptosis. J. Biol. Chem. 272, 17907-17911 (1997). Describes the development of a now widely used technique for characterizing the active sites of proteases and for defining cleavage-site specificities.
    • Thornberry, N. A. et al. A combinatorial approach defines specificities of members of the caspase family and granzyme B. Functional relationships established for key mediators of apoptosis. J. Biol. Chem. 272, 17907-17911 (1997). Describes the development of a now widely used technique for characterizing the active sites of proteases and for defining cleavage-site specificities.
  • 32
    • 0037132625 scopus 로고    scopus 로고
    • Peptide microarrays for the determination of protease substrate specificity
    • Salisbury, C. M., Maly, D. J. & Ellman, J. A. Peptide microarrays for the determination of protease substrate specificity. J. Am. Chem. Soc. 124, 14868-14870 (2002).
    • (2002) J. Am. Chem. Soc , vol.124 , pp. 14868-14870
    • Salisbury, C.M.1    Maly, D.J.2    Ellman, J.A.3
  • 33
    • 4043081164 scopus 로고    scopus 로고
    • High density peptide microarrays. In situ synthesis and applications
    • Gao, X. et al. High density peptide microarrays. In situ synthesis and applications. Mol. Divers. 8, 177-187 (2004).
    • (2004) Mol. Divers , vol.8 , pp. 177-187
    • Gao, X.1
  • 34
    • 2342650688 scopus 로고    scopus 로고
    • Communication between the active sites and dimer interface of a herpesvirus protease revealed by a transition-state inhibitor
    • Marnett, A. B., Nomura, A. M., Shimba, N., Ortiz de Montellano, P. R. & Craik, C. S. Communication between the active sites and dimer interface of a herpesvirus protease revealed by a transition-state inhibitor. Proc. Natl Acad. Sci. USA 101, 6870-6875 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 6870-6875
    • Marnett, A.B.1    Nomura, A.M.2    Shimba, N.3    Ortiz de Montellano, P.R.4    Craik, C.S.5
  • 35
    • 0036775883 scopus 로고    scopus 로고
    • Greenbaum, D. C. et al. Small molecule affinity fingerprinting. A tool for enzyme family subclassification, target identification, and inhibitor design. Chem. Biol. 9, 1085-1094 (2002). A comprehensive analysis of the development and use of activity-based probes that launched recent in vivo imaging studies, inhibitor design and active-site characterization.
    • Greenbaum, D. C. et al. Small molecule affinity fingerprinting. A tool for enzyme family subclassification, target identification, and inhibitor design. Chem. Biol. 9, 1085-1094 (2002). A comprehensive analysis of the development and use of activity-based probes that launched recent in vivo imaging studies, inhibitor design and active-site characterization.
  • 36
    • 0036890336 scopus 로고    scopus 로고
    • Scanning the prime-site substrate specificity of proteolytic enzymes: A novel assay based on ligand-enhanced lanthanide ion fluorescence
    • Barrios, A. M. & Craik, C. S. Scanning the prime-site substrate specificity of proteolytic enzymes: a novel assay based on ligand-enhanced lanthanide ion fluorescence. Bioorg. Med. Chem. Lett. 12, 3619-3623 (2002).
    • (2002) Bioorg. Med. Chem. Lett , vol.12 , pp. 3619-3623
    • Barrios, A.M.1    Craik, C.S.2
  • 37
    • 0034946412 scopus 로고    scopus 로고
    • Determination of protease cleavage site motifs using mixture-based oriented peptide libraries
    • Turk, B. E., Huang, L. L., Piro, E. T. & Cantley, L. C. Determination of protease cleavage site motifs using mixture-based oriented peptide libraries. Nature Biotechnol. 19, 661-667 (2001).
    • (2001) Nature Biotechnol , vol.19 , pp. 661-667
    • Turk, B.E.1    Huang, L.L.2    Piro, E.T.3    Cantley, L.C.4
  • 38
    • 0043272529 scopus 로고    scopus 로고
    • Biochemical properties and functions of membrane-anchored metalloprotease-disintegrin proteins (ADAMs)
    • Becherer, J. D. & Blobel, C. P. Biochemical properties and functions of membrane-anchored metalloprotease-disintegrin proteins (ADAMs). Curr. Top. Dev. Biol. 54, 101-123 (2003).
    • (2003) Curr. Top. Dev. Biol , vol.54 , pp. 101-123
    • Becherer, J.D.1    Blobel, C.P.2
  • 39
    • 0038019916 scopus 로고    scopus 로고
    • Structural aspects of the metzincin clan of metalloendopeptidases
    • Gomis-Ruth, F. X. Structural aspects of the metzincin clan of metalloendopeptidases. Mol. Biotechnol. 24, 157-202 (2003).
    • (2003) Mol. Biotechnol , vol.24 , pp. 157-202
    • Gomis-Ruth, F.X.1
  • 40
    • 0036741135 scopus 로고    scopus 로고
    • Molecular determinants of metalloproteinase substrate specificity: Matrix metalloproteinase substrate binding domains, modules, and exosites
    • Overall, C. M. Molecular determinants of metalloproteinase substrate specificity: matrix metalloproteinase substrate binding domains, modules, and exosites. Mol. Biotechnol. 22, 51-86 (2002).
    • (2002) Mol. Biotechnol , vol.22 , pp. 51-86
    • Overall, C.M.1
  • 41
    • 0034682773 scopus 로고    scopus 로고
    • The thrombospondin motif of aggrecanase-1 (ADAMTS-4) is critical for aggrecan substrate recognition and cleavage
    • Tortorella, M. et al. The thrombospondin motif of aggrecanase-1 (ADAMTS-4) is critical for aggrecan substrate recognition and cleavage. J. Biol. Chem. 275, 25791-25797 (2000).
    • (2000) J. Biol. Chem , vol.275 , pp. 25791-25797
    • Tortorella, M.1
  • 42
    • 0026333465 scopus 로고
    • A model for interstitial collagen catabolism by mammalian collagenases
    • Fields, G. B. A model for interstitial collagen catabolism by mammalian collagenases. J. Theor. Biol. 153, 585-602 (1991).
    • (1991) J. Theor. Biol , vol.153 , pp. 585-602
    • Fields, G.B.1
  • 44
    • 0026556560 scopus 로고
    • Rapid optimization of enzyme substrates using defined substrate mixtures
    • Berman, J. et al. Rapid optimization of enzyme substrates using defined substrate mixtures. J. Biol. Chem. 267, 1434-1437 (1992).
    • (1992) J. Biol. Chem , vol.267 , pp. 1434-1437
    • Berman, J.1
  • 45
    • 0036661037 scopus 로고    scopus 로고
    • Discovery of chemokine substrates for matrix metalloproteinases by exosite scanning: A new tool for degradomics
    • Overall, C. M., McQuibban, G. A. & Clark-Lewis, I. Discovery of chemokine substrates for matrix metalloproteinases by exosite scanning: a new tool for degradomics. Biol. Chem. 383, 1059-1066 (2002).
    • (2002) Biol. Chem , vol.383 , pp. 1059-1066
    • Overall, C.M.1    McQuibban, G.A.2    Clark-Lewis, I.3
  • 46
    • 4644293845 scopus 로고    scopus 로고
    • The Lin12-notch repeats of pregnancy-associated plasma protein-A bind calcium and determine its proteolytic specificity
    • Boldt, H. B. et al. The Lin12-notch repeats of pregnancy-associated plasma protein-A bind calcium and determine its proteolytic specificity. J. Biol. Chem. 279, 38525-38531 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 38525-38531
    • Boldt, H.B.1
  • 47
    • 33745812768 scopus 로고    scopus 로고
    • ADAMTS1 interacts with, cleaves, and modifies the extracellular location of the matrix inhibitor tissue factor pathway inhibitor-2
    • Torres-Collado, A. X., Kisiel, W., Iruela-Arispe, M. L. & Rodriguez-Manzaneque, J. C. ADAMTS1 interacts with, cleaves, and modifies the extracellular location of the matrix inhibitor tissue factor pathway inhibitor-2. J. Biol. Chem. 281, 17827-17837 (2006).
    • (2006) J. Biol. Chem , vol.281 , pp. 17827-17837
    • Torres-Collado, A.X.1    Kisiel, W.2    Iruela-Arispe, M.L.3    Rodriguez-Manzaneque, J.C.4
  • 48
    • 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, C. M. et al. 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).
    • (2004) Biol. Chem , vol.385 , pp. 493-504
    • Overall, C.M.1
  • 49
    • 33747736649 scopus 로고    scopus 로고
    • A basolateral sorting signal directs ADAM10 to adherens junctions and is required for its function in cell migration
    • Wild-Bode, C., Fellerer, K., Kugler, J., Haass, C. & Capell, A. A basolateral sorting signal directs ADAM10 to adherens junctions and is required for its function in cell migration. J. Biol. Chem. 281, 23824-23829 (2006).
    • (2006) J. Biol. Chem , vol.281 , pp. 23824-23829
    • Wild-Bode, C.1    Fellerer, K.2    Kugler, J.3    Haass, C.4    Capell, A.5
  • 50
    • 0033532144 scopus 로고    scopus 로고
    • Regulation of human ADAM 12 protease by the prodomain. Evidence for a functional cysteine switch
    • Loechel, F., Overgaard, M. T., Oxvig, C., Albrechtsen, R. & Wewer, U. M. Regulation of human ADAM 12 protease by the prodomain. Evidence for a functional cysteine switch. J. Biol. Chem. 274, 13427-13433 (1999).
    • (1999) J. Biol. Chem , vol.274 , pp. 13427-13433
    • Loechel, F.1    Overgaard, M.T.2    Oxvig, C.3    Albrechtsen, R.4    Wewer, U.M.5
  • 51
    • 0029014101 scopus 로고
    • Furin-dependent intracellular activation of the human stromelysin-3 zymogen
    • Pei, D. & Weiss, S. J. Furin-dependent intracellular activation of the human stromelysin-3 zymogen. Nature 375, 244-247 (1995).
    • (1995) Nature , vol.375 , pp. 244-247
    • Pei, D.1    Weiss, S.J.2
  • 52
    • 15744388309 scopus 로고    scopus 로고
    • A key role for mast cell chymase in the activation of pro-matrix metalloprotease-9 and pro-matrix metalloprotease-2
    • Tchougounova, E. et al. A key role for mast cell chymase in the activation of pro-matrix metalloprotease-9 and pro-matrix metalloprotease-2. J. Biol. Chem. 280, 9291-9296 (2005).
    • (2005) J. Biol. Chem , vol.280 , pp. 9291-9296
    • Tchougounova, E.1
  • 53
    • 3543030410 scopus 로고    scopus 로고
    • Cooperation between mast cell carboxypeptidase A and the chymase mouse mast cell protease 4 in the formation and degradation of angiotensin II
    • Lundequist, A., Tchougounova, E., Abrink, M. & Pejler, G. Cooperation between mast cell carboxypeptidase A and the chymase mouse mast cell protease 4 in the formation and degradation of angiotensin II. J. Biol. Chem. 279, 32339-32344 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 32339-32344
    • Lundequist, A.1    Tchougounova, E.2    Abrink, M.3    Pejler, G.4
  • 54
    • 1442358746 scopus 로고    scopus 로고
    • Sahin, U. et al. Distinct roles for ADAM10 and ADAM17 in ectodomain shedding of six EGFR-ligands. J. Cell Biol. 164, 769-779 (2004). Mouse embryonic fibroblasts from different Adam- knockout mice were used in cell-based assays to identify which ADAM is required for processing of individual epidermal-growth-factor-receptor ligands.
    • Sahin, U. et al. Distinct roles for ADAM10 and ADAM17 in ectodomain shedding of six EGFR-ligands. J. Cell Biol. 164, 769-779 (2004). Mouse embryonic fibroblasts from different Adam- knockout mice were used in cell-based assays to identify which ADAM is required for processing of individual epidermal-growth-factor-receptor ligands.
  • 55
    • 33846056925 scopus 로고    scopus 로고
    • Substrate selectivity and regulation of EGF-receptor ligand sheddases by phorbol esters and calcium influx
    • Horiuchi, K. et al. Substrate selectivity and regulation of EGF-receptor ligand sheddases by phorbol esters and calcium influx. Mol. Biol. Cell 18, 176-188 (2007).
    • (2007) Mol. Biol. Cell , vol.18 , pp. 176-188
    • Horiuchi, K.1
  • 56
    • 0036796421 scopus 로고    scopus 로고
    • The disintegrin/metalloprotease ADAM 10 is essential for Notch signalling but not for α-secretase activity in fibroblasts
    • Hartmann, D. et al. The disintegrin/metalloprotease ADAM 10 is essential for Notch signalling but not for α-secretase activity in fibroblasts. Hum. Mol. Genet. 11, 2615-2624 (2002).
    • (2002) Hum. Mol. Genet , vol.11 , pp. 2615-2624
    • Hartmann, D.1
  • 57
    • 2642541715 scopus 로고    scopus 로고
    • Selective roles for tumor necrosis factor α-converting enzyme/ADAM17 in the shedding of the epidermal growth factor receptor ligand family: The juxtamembrane stalk determines cleavage efficiency
    • Hinkle, C. L. et al. Selective roles for tumor necrosis factor α-converting enzyme/ADAM17 in the shedding of the epidermal growth factor receptor ligand family: the juxtamembrane stalk determines cleavage efficiency. J. Biol. Chem. 279, 24179-24188 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 24179-24188
    • Hinkle, C.L.1
  • 58
    • 0030891983 scopus 로고    scopus 로고
    • Enhanced cleavage of type II collagen by collagenases in osteoarthritic articular cartilage
    • Billinghurst, R. C. et al. Enhanced cleavage of type II collagen by collagenases in osteoarthritic articular cartilage. J. Clin. Invest. 99, 1534-1545 (1997).
    • (1997) J. Clin. Invest , vol.99 , pp. 1534-1545
    • Billinghurst, R.C.1
  • 59
    • 0038581051 scopus 로고    scopus 로고
    • TACE cleavage of proamphiregulin regulates GPCR-induced proliferation and motility of cancer cells
    • Gschwind, A., Hart, S., Fischer, O. M. & Ullrich, A. TACE cleavage of proamphiregulin regulates GPCR-induced proliferation and motility of cancer cells. EMBO J. 22, 2411-2421 (2003).
    • (2003) EMBO J , vol.22 , pp. 2411-2421
    • Gschwind, A.1    Hart, S.2    Fischer, O.M.3    Ullrich, A.4
  • 60
    • 33846171956 scopus 로고    scopus 로고
    • Proteomic validation of protease drug targets: Pharmacoproteomics of matrix metalloproteinase inhibitor drugs using isotope-coded affinity tag labelling and tandem mass spectrometry
    • Butler, G. S. & Overall, C. M. Proteomic validation of protease drug targets: Pharmacoproteomics of matrix metalloproteinase inhibitor drugs using isotope-coded affinity tag labelling and tandem mass spectrometry. Curr. Pharm. Des.13, 263-270 (2007).
    • (2007) Curr. Pharm. Des , vol.13 , pp. 263-270
    • Butler, G.S.1    Overall, C.M.2
  • 61
    • 3042554386 scopus 로고    scopus 로고
    • 2+ influx and PKC activation
    • 2+ influx and PKC activation. J. Cell Biol. 165, 893-902 (2004).
    • (2004) J. Cell Biol , vol.165 , pp. 893-902
    • Nagano, O.1
  • 62
    • 0033599039 scopus 로고    scopus 로고
    • EGF receptor transactivation by G-protein-coupled receptors requires metalloproteinase cleavage of proHB-EGF
    • Prenzel, N. et al. EGF receptor transactivation by G-protein-coupled receptors requires metalloproteinase cleavage of proHB-EGF. Nature 402, 884-888 (1999).
    • (1999) Nature , vol.402 , pp. 884-888
    • Prenzel, N.1
  • 63
    • 0033573049 scopus 로고    scopus 로고
    • Ectodomain shedding of TGF-α and other transmembrane proteins is induced by receptor tyrosine kinase activation and MAP kinase signaling cascades
    • Fan, H. & Derynck, R. Ectodomain shedding of TGF-α and other transmembrane proteins is induced by receptor tyrosine kinase activation and MAP kinase signaling cascades. EMBO J. 18, 6962-6972 (1999).
    • (1999) EMBO J , vol.18 , pp. 6962-6972
    • Fan, H.1    Derynck, R.2
  • 64
    • 4644232719 scopus 로고    scopus 로고
    • A proteomic approach to identify substrates of matrix metalloproteinase-14 in human plasma
    • Hwang, I. K., Park, S. M., Kim, S. Y. & Lee, S. T. A proteomic approach to identify substrates of matrix metalloproteinase-14 in human plasma. Biochim. Biophys. Acta 1702, 79-87 (2004).
    • (2004) Biochim. Biophys. Acta , vol.1702 , pp. 79-87
    • Hwang, I.K.1    Park, S.M.2    Kim, S.Y.3    Lee, S.T.4
  • 65
    • 8744269434 scopus 로고    scopus 로고
    • Identification of caspase-3 degradome by two-dimensional gel electrophoresis and matrix-assisted laser desorption/ionization-time of flight analysis
    • Lee, A. Y. et al. Identification of caspase-3 degradome by two-dimensional gel electrophoresis and matrix-assisted laser desorption/ionization-time of flight analysis. Proteomics 4, 3429-3436 (2004).
    • (2004) Proteomics , vol.4 , pp. 3429-3436
    • Lee, A.Y.1
  • 66
    • 2442690776 scopus 로고    scopus 로고
    • Proteomic analysis of cleavage events reveals a dynamic two-step mechanism for proteolysis of a key parasite adhesive complex
    • Zhou, X. W., Blackman, M. J., Howell, S. A. & Carruthers, V. B. Proteomic analysis of cleavage events reveals a dynamic two-step mechanism for proteolysis of a key parasite adhesive complex. Mol. Cell. Proteomics 3, 565-576 (2004).
    • (2004) Mol. Cell. Proteomics , vol.3 , pp. 565-576
    • Zhou, X.W.1    Blackman, M.J.2    Howell, S.A.3    Carruthers, V.B.4
  • 67
    • 4143101424 scopus 로고    scopus 로고
    • Bredemeyer, A. J. et al. A proteomic approach for the discovery of protease substrates. Proc. Natl Acad. Sci. USA 101, 11785-11790 (2004). Describes the successful application of DIGE to identify substrates for granzyme A and B.
    • Bredemeyer, A. J. et al. A proteomic approach for the discovery of protease substrates. Proc. Natl Acad. Sci. USA 101, 11785-11790 (2004). Describes the successful application of DIGE to identify substrates for granzyme A and B.
  • 68
    • 33745477470 scopus 로고    scopus 로고
    • Bech-Serra, J. J. et al. Proteomic identification of desmoglein 2 and activated leukocyte cell adhesion molecule as substrates of ADAM17 and ADAM10 by difference gel electrophoresis. Mol. Cell. Biol. 26, 5086-5095 (2006). DIGE is used to identify substrates for ADAM10 and ADAM17, and the role of these ADAMs in cleaving the newly identified substrates (desmoglein-2 and activated leukocyte cell-adhesion molecule (ALCAM)) was corroborated with cells from ADAM10- or ADAM17-deficient mice.
    • Bech-Serra, J. J. et al. Proteomic identification of desmoglein 2 and activated leukocyte cell adhesion molecule as substrates of ADAM17 and ADAM10 by difference gel electrophoresis. Mol. Cell. Biol. 26, 5086-5095 (2006). DIGE is used to identify substrates for ADAM10 and ADAM17, and the role of these ADAMs in cleaving the newly identified substrates (desmoglein-2 and activated leukocyte cell-adhesion molecule (ALCAM)) was corroborated with cells from ADAM10- or ADAM17-deficient mice.
  • 69
    • 0035106351 scopus 로고    scopus 로고
    • Washburn, M. P., Wolters, D. & Yates, J. R. 3rd. Large-scale analysis of the yeast proteome by multidimensional protein identification technology. Nature Biotechnol. 19, 242-247 (2001).
    • Washburn, M. P., Wolters, D. & Yates, J. R. 3rd. Large-scale analysis of the yeast proteome by multidimensional protein identification technology. Nature Biotechnol. 19, 242-247 (2001).
  • 71
    • 0036052092 scopus 로고    scopus 로고
    • A proteomic approach for the identification of cell-surface proteins shed by metalloproteases
    • Guo, L. et al. A proteomic approach for the identification of cell-surface proteins shed by metalloproteases. Mol. Cell. Proteomics 1, 30-36 (2002).
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 30-36
    • Guo, L.1
  • 72
    • 34247341829 scopus 로고    scopus 로고
    • Proteomic discovery of metalloproteinase substrates in the cellular context by iTRAQ™ labeling reveals a diverse MMP-2 substrate degradome
    • in the press
    • Dean, R. A. & Overall, C. M. Proteomic discovery of metalloproteinase substrates in the cellular context by iTRAQ™ labeling reveals a diverse MMP-2 substrate degradome. Mol. Cell. Proteomics (in the press).
    • Mol. Cell. Proteomics
    • Dean, R.A.1    Overall, C.M.2
  • 73
    • 0042671326 scopus 로고    scopus 로고
    • Intramembrane proteolysis by presenilin and presenilin-like proteases
    • Xia, W. & Wolfe, M. S. Intramembrane proteolysis by presenilin and presenilin-like proteases. J. Cell Sci. 116, 2839-2844 (2003).
    • (2003) J. Cell Sci , vol.116 , pp. 2839-2844
    • Xia, W.1    Wolfe, M.S.2
  • 74
    • 29144504045 scopus 로고    scopus 로고
    • Ji, C., Guo, N. & Li, L. Differential dimethyl labeling of N-termini of peptides after guanidination for proteome analysis. J. Proteome Res. 4, 2099-2108 (2005). Clever use of chemical guanidination of Lys side chains to mask these from the free N terminus of proteins, potentially including cleaved substrates, which can be adopted for degradomics analysis of substrate cleavage.
    • Ji, C., Guo, N. & Li, L. Differential dimethyl labeling of N-termini of peptides after guanidination for proteome analysis. J. Proteome Res. 4, 2099-2108 (2005). Clever use of chemical guanidination of Lys side chains to mask these from the free N terminus of proteins, potentially including cleaved substrates, which can be adopted for degradomics analysis of substrate cleavage.
  • 75
    • 27144473929 scopus 로고    scopus 로고
    • Van Damme, P. et al. Caspase-specific and nonspecific in vivo protein processing during Fas-induced apoptosis. Nature Methods 2, 771-777 (2005). The first comprehensive and working method for N-terminone analysis of proteolysis.
    • Van Damme, P. et al. Caspase-specific and nonspecific in vivo protein processing during Fas-induced apoptosis. Nature Methods 2, 771-777 (2005). The first comprehensive and working method for N-terminone analysis of proteolysis.
  • 76
    • 30944438540 scopus 로고    scopus 로고
    • Positional proteomics: Selective recovery and analysis of N-terminal proteolytic peptides
    • McDonald, L., Robertson, D. H., Hurst, J. L. & Beynon, R. J. Positional proteomics: selective recovery and analysis of N-terminal proteolytic peptides. Nature Methods 2, 955-957 (2005).
    • (2005) Nature Methods , vol.2 , pp. 955-957
    • McDonald, L.1    Robertson, D.H.2    Hurst, J.L.3    Beynon, R.J.4
  • 77
    • 0035047188 scopus 로고    scopus 로고
    • Peptidomics: The comprehensive analysis of peptides in complex biological mixtures
    • Schulz-Knappe, P. et al. Peptidomics: the comprehensive analysis of peptides in complex biological mixtures. Comb. Chem. High Throughput Screen. 4, 207-217 (2001).
    • (2001) Comb. Chem. High Throughput Screen , vol.4 , pp. 207-217
    • Schulz-Knappe, P.1
  • 78
    • 9244220099 scopus 로고    scopus 로고
    • Exploiting natural peptide diversity: Novel research tools and drug leads
    • Adermann, K., John, H., Standker, L. & Forssmann, W. G. Exploiting natural peptide diversity: novel research tools and drug leads. Curr. Opin. Biotechnol. 15, 599-606 (2004).
    • (2004) Curr. Opin. Biotechnol , vol.15 , pp. 599-606
    • Adermann, K.1    John, H.2    Standker, L.3    Forssmann, W.G.4
  • 79
    • 1542617944 scopus 로고    scopus 로고
    • Serum peptide profiling by magnetic particle-assisted, automated sample processing and MALDI-TOF mass spectrometry
    • Villanueva, J. et al. Serum peptide profiling by magnetic particle-assisted, automated sample processing and MALDI-TOF mass spectrometry. Anal. Chem. 76, 1560-1570 (2004).
    • (2004) Anal. Chem , vol.76 , pp. 1560-1570
    • Villanueva, J.1
  • 80
    • 33748051433 scopus 로고    scopus 로고
    • Pan, H. et al. The role of prohormone convertase-2 in hypothalamic neuropeptide processing: a quantitative neuropeptidomic study. J. Neurochem. 98, 1763-1777 (2006). Peptidomic analysis of protease-knockout and wildtype mice focusing on neuropeptide products that result from prohormone convertase-2 activity.
    • Pan, H. et al. The role of prohormone convertase-2 in hypothalamic neuropeptide processing: a quantitative neuropeptidomic study. J. Neurochem. 98, 1763-1777 (2006). Peptidomic analysis of protease-knockout and wildtype mice focusing on neuropeptide products that result from prohormone convertase-2 activity.
  • 81
    • 0036512208 scopus 로고    scopus 로고
    • New functions for the matrix metalloproteinases in cancer progression
    • Egeblad, M., & Werb, Z. New functions for the matrix metalloproteinases in cancer progression. Nature Rev. Cancer 2, 161-174 (2002).
    • (2002) Nature Rev. Cancer , vol.2 , pp. 161-174
    • Egeblad, M.1    Werb, Z.2
  • 82
    • 33644784910 scopus 로고    scopus 로고
    • Distinct roles for cysteine cathepsin genes in multistage tumorigenesis
    • Gocheva, V. et al. Distinct roles for cysteine cathepsin genes in multistage tumorigenesis. Genes Dev. 20, 543-556 (2006).
    • (2006) Genes Dev , vol.20 , pp. 543-556
    • Gocheva, V.1
  • 83
    • 2342603891 scopus 로고    scopus 로고
    • Cathepsin cysteine proteases are effectors of invasive growth and angiogenesis during multistage tumorigenesis
    • Joyce, J. A. et al. Cathepsin cysteine proteases are effectors of invasive growth and angiogenesis during multistage tumorigenesis. Cancer Cell 5, 443-453 (2004).
    • (2004) Cancer Cell , vol.5 , pp. 443-453
    • Joyce, J.A.1
  • 84
    • 21144438505 scopus 로고    scopus 로고
    • Lynch, C. C. et al. MMP-7 promotes prostate cancer-induced osteolysis via the solubilization of RANKL. Cancer Cell 7, 485-496 (2005). Microarray analysis of a rodent prostate cancer model, which metastasizes to bone, showed upregulation of MMP7 in osteoclasts at the tumour-bone interface, and demonstrated a requirement for MMP7 in receptor activator of NF-κB ligand (RANKL).
    • Lynch, C. C. et al. MMP-7 promotes prostate cancer-induced osteolysis via the solubilization of RANKL. Cancer Cell 7, 485-496 (2005). Microarray analysis of a rodent prostate cancer model, which metastasizes to bone, showed upregulation of MMP7 in osteoclasts at the tumour-bone interface, and demonstrated a requirement for MMP7 in receptor activator of NF-κB ligand (RANKL).
  • 85
    • 33750455150 scopus 로고    scopus 로고
    • Willem, M. et al. Control of peripheral nerve myelination by the β-secretase BACE1. Science 314, 664-666 (2006). Expression analysis revealed high amounts of BACE in peripheral nerves during myelination, and BACE-deficient mice were found to display hypomyelination and defects in processing of neuregulin, an ErbB-ligand that is crucial for myelination.
    • Willem, M. et al. Control of peripheral nerve myelination by the β-secretase BACE1. Science 314, 664-666 (2006). Expression analysis revealed high amounts of BACE in peripheral nerves during myelination, and BACE-deficient mice were found to display hypomyelination and defects in processing of neuregulin, an ErbB-ligand that is crucial for myelination.
  • 86
    • 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, H. B. et al. 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. 66, 7968-7975 (2006).
    • (2006) Cancer Res , vol.66 , pp. 7968-7975
    • Acuff, H.B.1
  • 87
    • 33748331284 scopus 로고    scopus 로고
    • ADAM12 is highly expressed in carcinoma-associated stroma and is required for mouse prostate tumor progression
    • Peduto, L. et al. ADAM12 is highly expressed in carcinoma-associated stroma and is required for mouse prostate tumor progression. Oncogene 25, 5462-5466 (2006).
    • (2006) Oncogene , vol.25 , pp. 5462-5466
    • Peduto, L.1
  • 88
    • 0041631044 scopus 로고    scopus 로고
    • Potential role for ADAM15 in pathological neovascularization in mice
    • Horiuchi, K. et al. Potential role for ADAM15 in pathological neovascularization in mice. Mol. Cell. Biol. 23, 5614-5624 (2003).
    • (2003) Mol. Cell. Biol , vol.23 , pp. 5614-5624
    • Horiuchi, K.1
  • 90
    • 15844384854 scopus 로고    scopus 로고
    • ADAMTS5 is the major aggrecanase in mouse cartilage in vivo and in vitro
    • Stanton, H. et al. ADAMTS5 is the major aggrecanase in mouse cartilage in vivo and in vitro. Nature 434, 648-652 (2005).
    • (2005) Nature , vol.434 , pp. 648-652
    • Stanton, H.1
  • 91
    • 15844413814 scopus 로고    scopus 로고
    • Glasson, S. S. et al. Deletion of active ADAMTS5 prevents cartilage degradation in a murine model of osteoarthritis. Nature 434, 644-648 (2005). In references 90 and 91, Adamts4- and Adamts5-knockout mice were used to test which of these is the relevant aggrecanase in vitro and in a mouse model for osteo arthritis. ADAMTS5 emerged as the principal enzyme.
    • Glasson, S. S. et al. Deletion of active ADAMTS5 prevents cartilage degradation in a murine model of osteoarthritis. Nature 434, 644-648 (2005). In references 90 and 91, Adamts4- and Adamts5-knockout mice were used to test which of these is the relevant aggrecanase in vitro and in a mouse model for osteo arthritis. ADAMTS5 emerged as the principal enzyme.
  • 92
    • 10744230888 scopus 로고    scopus 로고
    • Mice with defects in HB-EGF ectodomain shedding show severe developmental abnormalities
    • Yamazaki, S. et al. Mice with defects in HB-EGF ectodomain shedding show severe developmental abnormalities. J. Cell Biol. 163, 469-475 (2003).
    • (2003) J. Cell Biol , vol.163 , pp. 469-475
    • Yamazaki, S.1
  • 93
    • 17944381638 scopus 로고    scopus 로고
    • Membrane-bound TNF supports secondary lymphoid organ structure but is subservient to secreted TNF in driving autoimmune inflammation
    • Ruuls, S. R. et al. Membrane-bound TNF supports secondary lymphoid organ structure but is subservient to secreted TNF in driving autoimmune inflammation. Immunity 15, 533-543 (2001).
    • (2001) Immunity , vol.15 , pp. 533-543
    • Ruuls, S.R.1
  • 94
    • 33749538647 scopus 로고    scopus 로고
    • BMP1 controls TGF?1 activation via cleavage of latent TGF?-binding protein
    • Ge, G. & Greenspan, D. BMP1 controls TGF?1 activation via cleavage of latent TGF?-binding protein. J. Cell Biol. 175, 111-120 (2006).
    • (2006) J. Cell Biol , vol.175 , pp. 111-120
    • Ge, G.1    Greenspan, D.2
  • 95
    • 0035877683 scopus 로고    scopus 로고
    • A point mutation in the juxtamembrane stalk of human angiotensin I-converting enzyme invokes the action of a distinct secretase
    • Alfalah, M. et al. A point mutation in the juxtamembrane stalk of human angiotensin I-converting enzyme invokes the action of a distinct secretase. J. Biol. Chem. 276, 21105-21109 (2001).
    • (2001) J. Biol. Chem , vol.276 , pp. 21105-21109
    • Alfalah, M.1
  • 96
    • 0037507267 scopus 로고    scopus 로고
    • Defective valvulogenesis in HB-EGF and TACE-null mice is associated with aberrant BMP signaling
    • Jackson, L. F. et al. Defective valvulogenesis in HB-EGF and TACE-null mice is associated with aberrant BMP signaling. EMBO J. 22, 2704-2716 (2003).
    • (2003) EMBO J , vol.22 , pp. 2704-2716
    • Jackson, L.F.1
  • 97
    • 26244464287 scopus 로고    scopus 로고
    • Mammary ductal morphogenesis requires paracrine activation of stromal EGFR via ADAM17-dependent shedding of epithelial amphiregulin
    • Sternlicht, M. D. et al. Mammary ductal morphogenesis requires paracrine activation of stromal EGFR via ADAM17-dependent shedding of epithelial amphiregulin. Development 132, 3923-3933 (2005).
    • (2005) Development , vol.132 , pp. 3923-3933
    • Sternlicht, M.D.1
  • 98
    • 19344365408 scopus 로고    scopus 로고
    • De novo carcinogenesis promoted by chronic inflammation is B lymphocyte dependent
    • de Visser, K. E., Korets, L. V. & Coussens, L. M. De novo carcinogenesis promoted by chronic inflammation is B lymphocyte dependent. Cancer Cell 7, 411-423 (2005).
    • (2005) Cancer Cell , vol.7 , pp. 411-423
    • de Visser, K.E.1    Korets, L.V.2    Coussens, L.M.3
  • 99
    • 0033616716 scopus 로고    scopus 로고
    • Constitutive and regulated α-secretase cleavage of Alzheimer's amyloid precursor protein by a disintegrin metalloprotease
    • Lammich, S. et al. Constitutive and regulated α-secretase cleavage of Alzheimer's amyloid precursor protein by a disintegrin metalloprotease. Proc. Natl Acad. Sci. USA 96, 3922-3927 (1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 3922-3927
    • Lammich, S.1
  • 100
    • 0035805620 scopus 로고    scopus 로고
    • Biochemical and pharmacological criteria define two shedding activities for TRANCE/OPGL that are distinct from the TNF? convertase (TACE)
    • Schlöndorff, J. S., Lum, L. & Blobel, C. P. Biochemical and pharmacological criteria define two shedding activities for TRANCE/OPGL that are distinct from the TNF? convertase (TACE). J. Biol. Chem. 276, 14665-14674 (2001).
    • (2001) J. Biol. Chem , vol.276 , pp. 14665-14674
    • Schlöndorff, J.S.1    Lum, L.2    Blobel, C.P.3
  • 101
    • 33845994375 scopus 로고    scopus 로고
    • Negative regulation of osteoclastogenesis by ectodomain shedding of receptor activator of NF-κB ligand
    • Hikita, A. et al. Negative regulation of osteoclastogenesis by ectodomain shedding of receptor activator of NF-κB ligand. J. Biol. Chem. 281, 36846-36855 (2006).
    • (2006) J. Biol. Chem , vol.281 , pp. 36846-36855
    • Hikita, A.1
  • 102
    • 0033597726 scopus 로고    scopus 로고
    • The stromal proteinase MMP3/stromelysin-1 promotes mammary carcinogenesis
    • Sternlicht, M. D. et al. The stromal proteinase MMP3/stromelysin-1 promotes mammary carcinogenesis. Cell 98, 137-146 (1999).
    • (1999) Cell , vol.98 , pp. 137-146
    • Sternlicht, M.D.1
  • 103
    • 0031470904 scopus 로고    scopus 로고
    • SUP-17, a Caenorhabditis elegans ADAM protein related to Drosophila KUZBANIAN, and its role in LIN-12/NOTCH signaling
    • Wen, C., Metzstein, M. M. & Greenwald, I. SUP-17, a Caenorhabditis elegans ADAM protein related to Drosophila KUZBANIAN, and its role in LIN-12/NOTCH signaling. Development 124, 4759-4767 (1997).
    • (1997) Development , vol.124 , pp. 4759-4767
    • Wen, C.1    Metzstein, M.M.2    Greenwald, I.3
  • 104
    • 0343196671 scopus 로고    scopus 로고
    • KUZBANIAN controls proteolytic processing of NOTCH and mediates lateral inhibition during Drosophila and vertebrate neurogenesis
    • Pan, D. & Rubin, J. KUZBANIAN controls proteolytic processing of NOTCH and mediates lateral inhibition during Drosophila and vertebrate neurogenesis. Cell 90, 271-280 (1997).
    • (1997) Cell , vol.90 , pp. 271-280
    • Pan, D.1    Rubin, J.2
  • 105
    • 18744383614 scopus 로고    scopus 로고
    • Li, Q., Park, P. W., Wilson, C. L. & Parks, W. C. Matrilysin shedding of syndecan-1 regulates chemokine mobilization and transepithelial efflux of neutrophils in acute lung injury. Cell 111, 635-646 (2002). An elegant analysis of the role of matrilysin (also known as MMP7) in shedding syndecan-1 with an attached CXC chemokine, and the requirement of this process in neutrophil efflux to sites of lung injury in mice.
    • Li, Q., Park, P. W., Wilson, C. L. & Parks, W. C. Matrilysin shedding of syndecan-1 regulates chemokine mobilization and transepithelial efflux of neutrophils in acute lung injury. Cell 111, 635-646 (2002). An elegant analysis of the role of matrilysin (also known as MMP7) in shedding syndecan-1 with an attached CXC chemokine, and the requirement of this process in neutrophil efflux to sites of lung injury in mice.
  • 106
    • 0033595706 scopus 로고    scopus 로고
    • β-secretase cleavage of Alzheimer's amyloid precursor protein by the transmembrane aspartic protease BACE
    • Vassar, R. et al. β-secretase cleavage of Alzheimer's amyloid precursor protein by the transmembrane aspartic protease BACE. Science 286, 735-741 (1999).
    • (1999) Science , vol.286 , pp. 735-741
    • Vassar, R.1
  • 107
    • 17344388652 scopus 로고    scopus 로고
    • BACE knockout mice are healthy despite lacking the primary β-secretase activity in brain: Implications for Alzheimer's disease therapeutics
    • Roberds, S. L. et al. BACE knockout mice are healthy despite lacking the primary β-secretase activity in brain: implications for Alzheimer's disease therapeutics. Hum. Mol. Genet. 10, 1317-1324 (2001).
    • (2001) Hum. Mol. Genet , vol.10 , pp. 1317-1324
    • Roberds, S.L.1
  • 108
    • 14444272986 scopus 로고    scopus 로고
    • Evidence that tumor necrosis factor α converting enzyme is involved in regulated α-secretase cleavage of the Alzheimer amyloid protein precursor
    • Buxbaum, J. D. et al. Evidence that tumor necrosis factor α converting enzyme is involved in regulated α-secretase cleavage of the Alzheimer amyloid protein precursor. J. Biol. Chem. 273, 27765-27767 (1998).
    • (1998) J. Biol. Chem , vol.273 , pp. 27765-27767
    • Buxbaum, J.D.1
  • 109
    • 33846285347 scopus 로고    scopus 로고
    • Weskamp, G. et al. ADAM10 is a principal 'sheddase' of the low-affinity immunoglobulin E receptor CD23. Nature Immunology 7, 1393-1398 (2006). Gain- and loss-of-function studies with mouse cells, in vivo shedding studies in mice and use of a selective pharmacological inhibitor on mouse and human B cells identified ADAM10 as the major sheddase for CD23, a target for the treatment of allergic disease and rheumatoid arthritis.
    • Weskamp, G. et al. ADAM10 is a principal 'sheddase' of the low-affinity immunoglobulin E receptor CD23. Nature Immunology 7, 1393-1398 (2006). Gain- and loss-of-function studies with mouse cells, in vivo shedding studies in mice and use of a selective pharmacological inhibitor on mouse and human B cells identified ADAM10 as the major sheddase for CD23, a target for the treatment of allergic disease and rheumatoid arthritis.
  • 110
    • 0037803570 scopus 로고    scopus 로고
    • Puente, X. S., Sanchez, L. M., Overall, C. M. & Lopez-Otin, C. Human and mouse proteases: a comparative genomic approach. Nature Rev. Genet. 4, 544-558 (2003). An excellent review on the identification and classification of all proteases in the human genome as well as diseases of proteolysis.
    • Puente, X. S., Sanchez, L. M., Overall, C. M. & Lopez-Otin, C. Human and mouse proteases: a comparative genomic approach. Nature Rev. Genet. 4, 544-558 (2003). An excellent review on the identification and classification of all proteases in the human genome as well as diseases of proteolysis.
  • 111
    • 0033515520 scopus 로고    scopus 로고
    • Germline mutations in the extracellular domains of the 55 kDa TNF receptor, TNFR1, define a family of dominantly inherited autoinflammatory syndromes
    • McDermott, M. F. et al. Germline mutations in the extracellular domains of the 55 kDa TNF receptor, TNFR1, define a family of dominantly inherited autoinflammatory syndromes. Cell 97, 133-144 (1999).
    • (1999) Cell , vol.97 , pp. 133-144
    • McDermott, M.F.1
  • 112
    • 0032211830 scopus 로고    scopus 로고
    • The cell biology of β-amyloid precursor protein and presenilin in Alzheimer's disease
    • Selkoe, D. J. The cell biology of β-amyloid precursor protein and presenilin in Alzheimer's disease. Trends Cell Biol. 8, 447-453 (1998).
    • (1998) Trends Cell Biol , vol.8 , pp. 447-453
    • Selkoe, D.J.1
  • 113
    • 0032724176 scopus 로고    scopus 로고
    • Specific sequence elements are required for the expression of functional tumor necrosis factor-α-converting enzyme (TACE)
    • Milla, M. E. et al. Specific sequence elements are required for the expression of functional tumor necrosis factor-α-converting enzyme (TACE). J. Biol. Chem. 274, 30563-30570 (1999).
    • (1999) J. Biol. Chem , vol.274 , pp. 30563-30570
    • Milla, M.E.1
  • 114
    • 0028915695 scopus 로고
    • X-ray structures of human neutrophil collagenase complexed with peptide hydroxamate and peptide thiol inhibitors. Implications for substrate binding and rational drug design
    • Grams, F. et al. X-ray structures of human neutrophil collagenase complexed with peptide hydroxamate and peptide thiol inhibitors. Implications for substrate binding and rational drug design. Eur. J. Biochem. 228, 830-841 (1995).
    • (1995) Eur. J. Biochem , vol.228 , pp. 830-841
    • Grams, F.1
  • 115
    • 0035940971 scopus 로고    scopus 로고
    • Inhibitory antibodies against endopeptidase activity of human adamalysin 19
    • Zhao, Y. G., Wei, P. & Sang, Q. X. Inhibitory antibodies against endopeptidase activity of human adamalysin 19. Biochem. Biophys. Res. Commun. 289, 288-294 (2001).
    • (2001) Biochem. Biophys. Res. Commun , vol.289 , pp. 288-294
    • Zhao, Y.G.1    Wei, P.2    Sang, Q.X.3
  • 116
    • 16644386010 scopus 로고    scopus 로고
    • Production of antibodies against degradative neoepitopes in aggrecan
    • Mort, J. S. & Roughley, P. J. Production of antibodies against degradative neoepitopes in aggrecan. Methods Mol. Med. 100, 237-250 (2004).
    • (2004) Methods Mol. Med , vol.100 , pp. 237-250
    • Mort, J.S.1    Roughley, P.J.2
  • 117
    • 0037117753 scopus 로고    scopus 로고
    • Structure-activity relationship of hydroxamate-based inhibitors on the secretases that cleave the amyloid precursor protein, angiotensin converting enzyme, CD23, and pro-tumor necrosis factor-α
    • Parkin, E. T. et al. Structure-activity relationship of hydroxamate-based inhibitors on the secretases that cleave the amyloid precursor protein, angiotensin converting enzyme, CD23, and pro-tumor necrosis factor-α. Biochemistry 41, 4972-4981 (2002).
    • (2002) Biochemistry , vol.41 , pp. 4972-4981
    • Parkin, E.T.1
  • 118
    • 1542390484 scopus 로고    scopus 로고
    • Role of TIMPs (tissue inhibitors of metalloproteinases) in pericellular proteolysis: The specificity is in the detail
    • Murphy, G. et al. Role of TIMPs (tissue inhibitors of metalloproteinases) in pericellular proteolysis: the specificity is in the detail. Biochem. Soc. Symp., 65-80 (2003).
    • (2003) Biochem. Soc. Symp , vol.65-80
    • Murphy, G.1
  • 119
    • 3843096112 scopus 로고    scopus 로고
    • Inhibition of the TNFα converting enzyme (TACE) by its Pro domain
    • Gonzales, P. E. et al. Inhibition of the TNFα converting enzyme (TACE) by its Pro domain. J. Biol. Chem. 279, 31638-31645 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 31638-31645
    • Gonzales, P.E.1
  • 120
    • 0037103183 scopus 로고    scopus 로고
    • Matrix metalloproteinase processing of monocyte chemoattractant proteins generates CC chemokine receptor antagonists with anti-inflammatory properties in vivo
    • McQuibban, G. A. et al. Matrix metalloproteinase processing of monocyte chemoattractant proteins generates CC chemokine receptor antagonists with anti-inflammatory properties in vivo. Blood 100, 1160-1167 (2002).
    • (2002) Blood , vol.100 , pp. 1160-1167
    • McQuibban, G.A.1
  • 121
    • 22544477581 scopus 로고    scopus 로고
    • Aptamers as tools for target validation
    • Blank, M. & Blind, M. Aptamers as tools for target validation. Curr. Opin. Chem. Biol. 9, 336-342 (2005).
    • (2005) Curr. Opin. Chem. Biol , vol.9 , pp. 336-342
    • Blank, M.1    Blind, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.