메뉴 건너뛰기




Volumn , Issue , 2012, Pages 315-342

The ADAMTS family of metalloproteinases

Author keywords

[No Author keywords available]

Indexed keywords


EID: 84923243574     PISSN: None     EISSN: None     Source Type: Book    
DOI: None     Document Type: Chapter
Times cited : (4)

References (149)
  • 1
    • 0033551844 scopus 로고    scopus 로고
    • Cloning and characterization of ADAMTS11, an aggrecanase from the ADAMTS family
    • Abbaszade, I., Liu, R. Q., Yang, F., et al. (1999). Cloning and characterization of ADAMTS11, an aggrecanase from the ADAMTS family. J Biol Chem 274, 23443-23450.
    • (1999) J Biol Chem , vol.274 , pp. 23443-23450
    • Abbaszade, I.1    Liu, R.Q.2    Yang, F.3
  • 2
    • 72949104661 scopus 로고    scopus 로고
    • Crystal structures of the noncatalytic domains of ADAMTS13 reveal multiple discontinuous exosites for von Willebrand factor
    • Akiyama, M., Takeda, S., Kokame, K., Takagi, J., and Miyata, T. (2009). Crystal structures of the noncatalytic domains of ADAMTS13 reveal multiple discontinuous exosites for von Willebrand factor. Proc Natl Acad Sci U S A 106, 19274-19279.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 19274-19279
    • Akiyama, M.1    Takeda, S.2    Kokame, K.3    Takagi, J.4    Miyata, T.5
  • 3
    • 4143112912 scopus 로고    scopus 로고
    • A disintegrin-like and metalloprotease (reprolysin type) with thrombospondin type 1 motifs: The ADAMTS family
    • Apte, S. S. (2004). A disintegrin-like and metalloprotease (reprolysin type) with thrombospondin type 1 motifs: the ADAMTS family. Int J Biochem Cell Biol 36, 981-985.
    • (2004) Int J Biochem Cell Biol , vol.36 , pp. 981-985
    • Apte, S.S.1
  • 4
    • 70450253102 scopus 로고    scopus 로고
    • A disintegrin-like and metalloprotease (reprolysin-type) with thrombospondin type 1 motif (ADAMTS) superfamily: Functions and mechanisms
    • Apte, S. S. (2009). A disintegrin-like and metalloprotease (reprolysin-type) with thrombospondin type 1 motif (ADAMTS) superfamily: functions and mechanisms. J Biol Chem 284, 31493-31497.
    • (2009) J Biol Chem , vol.284 , pp. 31493-31497
    • Apte, S.S.1
  • 5
    • 0025171017 scopus 로고
    • Specific inhibition of endothelial cell proliferation by thrombospondin
    • Bagavandoss, P., and Wilks, J. W. (1990). Specific inhibition of endothelial cell proliferation by thrombospondin. Biochem Biophys Res Commun 170, 867-872.
    • (1990) Biochem Biophys Res Commun , vol.170 , pp. 867-872
    • Bagavandoss, P.1    Wilks, J.W.2
  • 6
    • 0036822797 scopus 로고    scopus 로고
    • Relative messenger RNA expression profiling of collagenases and aggrecanases in human articular chondrocytes in vivo and in vitro
    • Bau, B., Gebhard, P. M., Haag, J., Knorr, T., Bartnik, E., and Aigner, T. (2002). Relative messenger RNA expression profiling of collagenases and aggrecanases in human articular chondrocytes in vivo and in vitro. Arthritis Rheum 46, 2648-2657.
    • (2002) Arthritis Rheum , vol.46 , pp. 2648-2657
    • Bau, B.1    Gebhard, P.M.2    Haag, J.3    Knorr, T.4    Bartnik, E.5    Aigner, T.6
  • 7
    • 0028027226 scopus 로고
    • Crystal structure of the 50 kDa metallo protease from Serratia marcescens
    • Baumann, U. (1994). Crystal structure of the 50 kDa metallo protease from Serratia marcescens. J Mol Biol 242, 244-251.
    • (1994) J Mol Biol , vol.242 , pp. 244-251
    • Baumann, U.1
  • 8
    • 0028805811 scopus 로고
    • Stromelysin-1: Three-dimensional structure of the inhibited catalytic domain and of the C-truncated proenzyme
    • Becker, J. W., Marcy, A. I., Rokosz, L. L., et al. (1995). Stromelysin-1: three-dimensional structure of the inhibited catalytic domain and of the C-truncated proenzyme. Protein Sci 4, 1966-1976.
    • (1995) Protein Sci , vol.4 , pp. 1966-1976
    • Becker, J.W.1    Marcy, A.I.2    Rokosz, L.L.3
  • 9
    • 8044257704 scopus 로고    scopus 로고
    • A metalloproteinase disintegrin that releases tumour-necrosis factor-alpha from cells
    • Black, R. A., Rauch, C. T., Kozlosky, C. J., et al. (1997). A metalloproteinase disintegrin that releases tumour-necrosis factor-alpha from cells. Nature 385, 729-733.
    • (1997) Nature , vol.385 , pp. 729-733
    • Black, R.A.1    Rauch, C.T.2    Kozlosky, C.J.3
  • 10
    • 0033542457 scopus 로고    scopus 로고
    • Control of organ shape by a secreted metalloprotease in the nematode Caenorhabditis elegans
    • Blelloch, R., and Kimble, J. (1999). Control of organ shape by a secreted metalloprotease in the nematode Caenorhabditis elegans. Nature 399, 586-590.
    • (1999) Nature , vol.399 , pp. 586-590
    • Blelloch, R.1    Kimble, J.2
  • 11
    • 11244261160 scopus 로고    scopus 로고
    • ADAMs: Key components in EGFR signalling and development
    • Blobel, C. P. (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
  • 12
    • 0027515396 scopus 로고
    • Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc-binding environments (HEXXHXXGXXH and Met-turn) and topologies and should be grouped into a common family, the "metzincins."
    • Bode, W., Gomis-Rüth, F. X., and Stöckler, W. (1993). Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc-binding environments (HEXXHXXGXXH and Met-turn) and topologies and should be grouped into a common family, the "metzincins." FEBS Lett 331, 134-140.
    • (1993) FEBS Lett , vol.331 , pp. 134-140
    • Bode, W.1    Gomis-Rüth, F.X.2    Stöckler, W.3
  • 13
    • 0028324076 scopus 로고
    • The X-ray crystal structure of the catalytic domain of human neutrophil collagenase inhibited by a substrate analogue reveals the essentials for catalysis and specificity
    • Bode, W., Reinemer, P., Huber, R., Kleine, T., Schnierer, S., and Tschesche, H. (1994). The X-ray crystal structure of the catalytic domain of human neutrophil collagenase inhibited by a substrate analogue reveals the essentials for catalysis and specificity. EMBO J 13, 1263-1269.
    • (1994) EMBO J , vol.13 , pp. 1263-1269
    • Bode, W.1    Reinemer, P.2    Huber, R.3    Kleine, T.4    Schnierer, S.5    Tschesche, H.6
  • 14
    • 0035977453 scopus 로고    scopus 로고
    • Characterization of ADAMTS14, a novel member of the ADAMTS metalloproteinase family
    • Bolz, H., Ramirez, A., von Brederlow, B., and Kubisch, C. (2001). Characterization of ADAMTS14, a novel member of the ADAMTS metalloproteinase family. Biochim Biophys Acta 1522, 221-225.
    • (2001) Biochim Biophys Acta , vol.1522 , pp. 221-225
    • Bolz, H.1    Ramirez, A.2    von Brederlow, B.3    Kubisch, C.4
  • 15
    • 0033870003 scopus 로고    scopus 로고
    • Evidence for modulation of genes involved in vascular adaptation by prolonged exposure of endothelial cells to shear stress
    • Bongrazio, M., Baumann, C., Zakrzewicz, A., Pries, A. R., and Gaehtgens, P. (2000). Evidence for modulation of genes involved in vascular adaptation by prolonged exposure of endothelial cells to shear stress. Cardiovasc Res 47, 384-393.
    • (2000) Cardiovasc Res , vol.47 , pp. 384-393
    • Bongrazio, M.1    Baumann, C.2    Zakrzewicz, A.3    Pries, A.R.4    Gaehtgens, P.5
  • 16
    • 77049113770 scopus 로고    scopus 로고
    • The tissue inhibitors of metalloproteinases (TIMPs): An ancient family with structural and functional diversity
    • Brew, K., and Nagase, H. (2010). The tissue inhibitors of metalloproteinases (TIMPs): an ancient family with structural and functional diversity. Biochim Biophys Acta 1803, 55-71.
    • (2010) Biochim Biophys Acta , vol.1803 , pp. 55-71
    • Brew, K.1    Nagase, H.2
  • 17
    • 0036516460 scopus 로고    scopus 로고
    • Matrix metalloproteinases: A tail of a frog that became a prince
    • Brinckerhoff, C. E., and Matrisian, L. M. (2002). Matrix metalloproteinases: a tail of a frog that became a prince. Nat Rev Mol Cell Biol 3, 207-214.
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 207-214
    • Brinckerhoff, C.E.1    Matrisian, L.M.2
  • 18
    • 76149121798 scopus 로고    scopus 로고
    • Proteolytic cleavage of versican during limb joint development
    • Capehart, A. A. (2010). Proteolytic cleavage of versican during limb joint development. Anat Rec 293, 208-214.
    • (2010) Anat Rec , vol.293 , pp. 208-214
    • Capehart, A.A.1
  • 19
    • 0030959540 scopus 로고    scopus 로고
    • CDNA cloning and expression of bovine procollagen I N-proteinase: A new member of the superfamily of zinc-metalloproteinases with binding sites for cells and other matrix components
    • Colige, A., Li, S. W., Sieron, A. L., Nusgens, B. V., Prockop, D. J., and Lapiere, C. M. (1997). cDNA cloning and expression of bovine procollagen I N-proteinase: a new member of the superfamily of zinc-metalloproteinases with binding sites for cells and other matrix components. Proc Natl Acad Sci U S A 94, 2374-2379.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 2374-2379
    • Colige, A.1    Li, S.W.2    Sieron, A.L.3    Nusgens, B.V.4    Prockop, D.J.5    Lapiere, C.M.6
  • 20
    • 0033358540 scopus 로고    scopus 로고
    • Human Ehlers-Danlos syndrome type VII C and bovine dermatosparaxis are caused by mutations in the procollagen I N-proteinase gene
    • Colige, A., Sieron, A. L., Li, S. W., et al. (1999). Human Ehlers-Danlos syndrome type VII C and bovine dermatosparaxis are caused by mutations in the procollagen I N-proteinase gene. Am J Hum Genet 65, 308-317.
    • (1999) Am J Hum Genet , vol.65 , pp. 308-317
    • Colige, A.1    Sieron, A.L.2    Li, S.W.3
  • 21
    • 3543043776 scopus 로고    scopus 로고
    • ADAMTS-8 exhibits aggrecanase activity and is expressed in human articular cartilage
    • Collins-Racie, L. A., Flannery, C. R., Zeng, W., et al. (2004). ADAMTS-8 exhibits aggrecanase activity and is expressed in human articular cartilage. Matrix Biol 23, 219-230.
    • (2004) Matrix Biol , vol.23 , pp. 219-230
    • Collins-Racie, L.A.1    Flannery, C.R.2    Zeng, W.3
  • 22
    • 18644370594 scopus 로고    scopus 로고
    • ADAMTS-9 is synergistically induced by interleukin-1 B and tumor necrosis factor A in OUMS-27 chondrosarcoma cells and in human chondrocytes
    • Demircan, K., Hirohata, S., Nishida, K., et al. (2005). ADAMTS-9 is synergistically induced by interleukin-1 B and tumor necrosis factor A in OUMS-27 chondrosarcoma cells and in human chondrocytes. Arthritis Rheum 52, 1451-1460.
    • (2005) Arthritis Rheum , vol.52 , pp. 1451-1460
    • Demircan, K.1    Hirohata, S.2    Nishida, K.3
  • 23
    • 78651291555 scopus 로고    scopus 로고
    • ADAMTS-2 functions as anti-angiogenic and anti-tumoral molecule independently of its catalytic activity
    • Dubail, J., Kesteloot, F., Deroanne, C., et al. (2010). ADAMTS-2 functions as anti-angiogenic and anti-tumoral molecule independently of its catalytic activity. Cell Mol Life Sci 67, 4213-4232.
    • (2010) Cell Mol Life Sci , vol.67 , pp. 4213-4232
    • Dubail, J.1    Kesteloot, F.2    Deroanne, C.3
  • 24
    • 33846669882 scopus 로고    scopus 로고
    • Palatal fusion - where do the midline cells go. A review on cleft palate, a major human birth defect
    • Dudas, M., Li, W. Y., Kim, J., Yang, A., and Kaartinen, V. (2007). Palatal fusion - where do the midline cells go? A review on cleft palate, a major human birth defect. Acta Histochem 109, 1-14.
    • (2007) Acta Histochem , vol.109 , pp. 1-14
    • Dudas, M.1    Li, W.Y.2    Kim, J.3    Yang, A.4    Kaartinen, V.5
  • 25
    • 80051475089 scopus 로고    scopus 로고
    • Altered versican cleavage in ADAMTS5 deficient mice; a novel etiology of myxomatous valve disease
    • Dupuis, L. E., McCulloch, D. R., McGarity, J. D., et al. (2011). Altered versican cleavage in ADAMTS5 deficient mice; a novel etiology of myxomatous valve disease. Dev Biol 357, 152-164.
    • (2011) Dev Biol , vol.357 , pp. 152-164
    • Dupuis, L.E.1    McCulloch, D.R.2    McGarity, J.D.3
  • 26
    • 50949112558 scopus 로고    scopus 로고
    • Characterization of an ADAMTS-5-mediated cleavage site in aggrecan in OSM-stimulated bovine cartilage
    • Durigova, M., Soucy, P., Fushimi, K., Nagase, H., Mort, J. S., and Roughley, P. J. (2008). Characterization of an ADAMTS-5-mediated cleavage site in aggrecan in OSM-stimulated bovine cartilage. Osteoarthritis Cartilage 16, 1245-1252.
    • (2008) Osteoarthritis Cartilage , vol.16 , pp. 1245-1252
    • Durigova, M.1    Soucy, P.2    Fushimi, K.3    Nagase, H.4    Mort, J.S.5    Roughley, P.J.6
  • 28
    • 78649823007 scopus 로고    scopus 로고
    • Cooperation of two ADAMTS metalloproteases in closure of the mouse palate identifies a requirement for versican proteolysis in regulating palatal mesenchyme proliferation
    • Enomoto, H., Nelson, C. M., Somerville, R. P., et al. (2010). Cooperation of two ADAMTS metalloproteases in closure of the mouse palate identifies a requirement for versican proteolysis in regulating palatal mesenchyme proliferation. Development 137, 4029-4038.
    • (2010) Development , vol.137 , pp. 4029-4038
    • Enomoto, H.1    Nelson, C.M.2    Somerville, R.P.3
  • 29
    • 0035943639 scopus 로고    scopus 로고
    • Procollagen II amino propeptide processing by ADAMTS-3. Insights on dermatosparaxis
    • Fernandes, R. J., Hirohata, S., Engle, J. M., et al. (2001). Procollagen II amino propeptide processing by ADAMTS-3. Insights on dermatosparaxis. J Biol Chem 276, 31502-31509.
    • (2001) J Biol Chem , vol.276 , pp. 31502-31509
    • Fernandes, R.J.1    Hirohata, S.2    Engle, J.M.3
  • 30
    • 79952186875 scopus 로고    scopus 로고
    • C. elegans ADAMTS ADT-2 regulates body size by modulating TGFbeta signaling and cuticle collagen organization
    • Fernando, T., Flibotte, S., Xiong, S., et al. (2011). C. elegans ADAMTS ADT-2 regulates body size by modulating TGFbeta signaling and cuticle collagen organization. Dev Biol 352, 92-103.
    • (2011) Dev Biol , vol.352 , pp. 92-103
    • Fernando, T.1    Flibotte, S.2    Xiong, S.3
  • 32
    • 61449216884 scopus 로고    scopus 로고
    • Cell surface nucleolin antagonist causes endothelial cell apoptosis and normalization of tumor vasculature
    • Fogal, V., Sugahara, K. N., Ruoslahti, E., and Christian, S. (2009). Cell surface nucleolin antagonist causes endothelial cell apoptosis and normalization of tumor vasculature. Angiogenesis 12, 91-100.
    • (2009) Angiogenesis , vol.12 , pp. 91-100
    • Fogal, V.1    Sugahara, K.N.2    Ruoslahti, E.3    Christian, S.4
  • 34
    • 0035885972 scopus 로고    scopus 로고
    • Purification of human von Willebrand factor-cleaving protease and its identification as a new member of the metalloproteinase family
    • Fujikawa, K., Suzuki, H., McMullen, B., and Chung, D. (2001). Purification of human von Willebrand factor-cleaving protease and its identification as a new member of the metalloproteinase family. Blood 98, 1662-1666.
    • (2001) Blood , vol.98 , pp. 1662-1666
    • Fujikawa, K.1    Suzuki, H.2    McMullen, B.3    Chung, D.4
  • 35
    • 43749117128 scopus 로고    scopus 로고
    • Functional differences of the catalytic and non-catalytic domains in human ADAMTS-4 and ADAMTS-5 in aggrecanolytic activity
    • Fushimi, K., Troeberg, L., Nakamura, H., Lim, N. H., and Nagase, H. (2008). Functional differences of the catalytic and non-catalytic domains in human ADAMTS-4 and ADAMTS-5 in aggrecanolytic activity. J Biol Chem 283, 6706-6716.
    • (2008) J Biol Chem , vol.283 , pp. 6706-6716
    • Fushimi, K.1    Troeberg, L.2    Nakamura, H.3    Lim, N.H.4    Nagase, H.5
  • 36
    • 1642354112 scopus 로고    scopus 로고
    • ADAMTS4 (aggrecanase-1) activation on the cell surface involves C-terminal cleavage by glycosylphosphatidyl inositol-anchored membrane type 4-matrix metalloproteinase and binding of the activated proteinase to chondroitin sulfate and heparan sulfate on syndecan-1
    • Gao, G., Plaas, A., Thompson, V. P., Jin, S., Zuo, F., and Sandy, J. D. (2004). ADAMTS4 (aggrecanase-1) activation on the cell surface involves C-terminal cleavage by glycosylphosphatidyl inositol-anchored membrane type 4-matrix metalloproteinase and binding of the activated proteinase to chondroitin sulfate and heparan sulfate on syndecan-1. J Biol Chem 279, 10042-10051.
    • (2004) J Biol Chem , vol.279 , pp. 10042-10051
    • Gao, G.1    Plaas, A.2    Thompson, V.P.3    Jin, S.4    Zuo, F.5    Sandy, J.D.6
  • 37
    • 34247845704 scopus 로고    scopus 로고
    • Exosite interactions contribute to tension-induced cleavage of von Willebrand factor by the antithrombotic ADAMTS13 metalloprotease
    • Gao, W., Anderson, P. J., Majerus, E. M., Tuley, E. A., and Sadler, J. E. (2006). Exosite interactions contribute to tension-induced cleavage of von Willebrand factor by the antithrombotic ADAMTS13 metalloprotease. Proc Natl Acad Sci U S A 103, 19099-19104.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 19099-19104
    • Gao, W.1    Anderson, P.J.2    Majerus, E.M.3    Tuley, E.A.4    Sadler, J.E.5
  • 38
    • 52649182049 scopus 로고    scopus 로고
    • Extensive contacts between ADAMTS13 exosites and von Willebrand factor domain A2 contribute to substrate specificity
    • Gao, W., Anderson, P. J., and Sadler, J. E. (2008). Extensive contacts between ADAMTS13 exosites and von Willebrand factor domain A2 contribute to substrate specificity. Blood 112, 1713-1719.
    • (2008) Blood , vol.112 , pp. 1713-1719
    • Gao, W.1    Anderson, P.J.2    Sadler, J.E.3
  • 39
    • 0345735683 scopus 로고    scopus 로고
    • TIMP-3 inhibits aggrecanase-mediated glycosaminoglycan release from cartilage explants stimulated by catabolic factors
    • Gendron, C., Kashiwagi, M., Hughes, C., Caterson, B., and Nagase, H. (2003). TIMP-3 inhibits aggrecanase-mediated glycosaminoglycan release from cartilage explants stimulated by catabolic factors. FEBS Lett 555, 431-436.
    • (2003) FEBS Lett , vol.555 , pp. 431-436
    • Gendron, C.1    Kashiwagi, M.2    Hughes, C.3    Caterson, B.4    Nagase, H.5
  • 40
    • 34547110152 scopus 로고    scopus 로고
    • Proteolytic activities of human ADAMTS-5: Comparative studies with ADAMTS-4
    • Gendron, C., Kashiwagi, M., Lim, N. H., et al. (2007). Proteolytic activities of human ADAMTS-5: comparative studies with ADAMTS-4. J Biol Chem 282, 18294-18306.
    • (2007) J Biol Chem , vol.282 , pp. 18294-18306
    • Gendron, C.1    Kashiwagi, M.2    Lim, N.H.3
  • 41
    • 34848826829 scopus 로고    scopus 로고
    • Crystal structures of human ADAMTS-1 reveal a conserved catalytic domain and a disintegrin-like domain with a fold homologous to cysteine-rich domains
    • Gerhardt, S., Hassall, G., Hawtin, P., et al. (2007). Crystal structures of human ADAMTS-1 reveal a conserved catalytic domain and a disintegrin-like domain with a fold homologous to cysteine-rich domains. J Mol Biol 373, 891-902.
    • (2007) J Mol Biol , vol.373 , pp. 891-902
    • Gerhardt, S.1    Hassall, G.2    Hawtin, P.3
  • 42
    • 0035885962 scopus 로고    scopus 로고
    • Partial amino acid sequence of purified von Willebrand factor-cleaving protease
    • Gerritsen, H. E., Robles, R., Lammle, B., and Furlan, M. (2001). Partial amino acid sequence of purified von Willebrand factor-cleaving protease. Blood 98, 1654-1661.
    • (2001) Blood , vol.98 , pp. 1654-1661
    • Gerritsen, H.E.1    Robles, R.2    Lammle, B.3    Furlan, M.4
  • 43
    • 0032964167 scopus 로고    scopus 로고
    • The pathobiology of osteoarthritis and the rationale for the use of pentosan polysulfate for its treatment
    • Ghosh, P. (1999). The pathobiology of osteoarthritis and the rationale for the use of pentosan polysulfate for its treatment. Semin Arthritis Rheum 28, 211-267.
    • (1999) Semin Arthritis Rheum , vol.28 , pp. 211-267
    • Ghosh, P.1
  • 44
    • 4043154293 scopus 로고    scopus 로고
    • Characterization of and osteoarthritis susceptibility in ADAMTS-4-knockout mice
    • Glasson, S. S., Askew, R., Sheppard, B., et al. (2004). Characterization of and osteoarthritis susceptibility in ADAMTS-4-knockout mice. Arthritis Rheum 50, 2547-2558.
    • (2004) Arthritis Rheum , vol.50 , pp. 2547-2558
    • Glasson, S.S.1    Askew, R.2    Sheppard, B.3
  • 45
    • 15844413814 scopus 로고    scopus 로고
    • Deletion of active ADAMTS5 prevents cartilage degradation in a murine model of osteoarthritis
    • Glasson, S. S., Askew, R., Sheppard, B., et al. (2005). Deletion of active ADAMTS5 prevents cartilage degradation in a murine model of osteoarthritis. Nature 434, 644-648.
    • (2005) Nature , vol.434 , pp. 644-648
    • Glasson, S.S.1    Askew, R.2    Sheppard, B.3
  • 46
    • 0038019916 scopus 로고    scopus 로고
    • Structural aspects of the metzincin clan of metalloendopeptidases
    • Gomis-Ruth, F. X. (2003). Structural aspects of the metzincin clan of metalloendopeptidases. Mol Biotechnol 24, 157-202.
    • (2003) Mol Biotechnol , vol.24 , pp. 157-202
    • Gomis-Ruth, F.X.1
  • 47
    • 0027386056 scopus 로고
    • First structure of a snake venom metalloproteinase: A prototype for matrix metalloproteinases/collagenases
    • Gomis-Ruth, F. X., Kress, L. F., and Bode, W. (1993). First structure of a snake venom metalloproteinase: a prototype for matrix metalloproteinases/collagenases. EMBO J 12, 4151-4157.
    • (1993) EMBO J , vol.12 , pp. 4151-4157
    • Gomis-Ruth, F.X.1    Kress, L.F.2    Bode, W.3
  • 48
    • 0025147371 scopus 로고
    • A tumor suppressor-dependent inhibitor of angiogenesis is immunologically and functionally indistinguishable from a fragment of thrombospondin
    • Good, D. J., Polverini, P. J., Rastinejad, F., et al. (1990). A tumor suppressor-dependent inhibitor of angiogenesis is immunologically and functionally indistinguishable from a fragment of thrombospondin. Proc Natl Acad Sci U S A 87, 6624-6628.
    • (1990) Proc Natl Acad Sci U S A , vol.87 , pp. 6624-6628
    • Good, D.J.1    Polverini, P.J.2    Rastinejad, F.3
  • 49
    • 0345935809 scopus 로고
    • Collagenolytic activity in amphibian tissues: A tissue culture assay
    • Gross, J., and Lapiere, C. M. (1962). Collagenolytic activity in amphibian tissues: a tissue culture assay. Proc Natl Acad Sci U S A 48, 1014-1022.
    • (1962) Proc Natl Acad Sci U S A , vol.48 , pp. 1014-1022
    • Gross, J.1    Lapiere, C.M.2
  • 50
    • 77954222578 scopus 로고    scopus 로고
    • Granulin-epithelin precursor binds directly to ADAMTS-7 and ADAMTS-12 and inhibits their degradation of cartilage oligomeric matrix protein
    • Guo, F., Lai, Y., Tian, Q., Lin, E. A., Kong, L., and Liu, C. (2010). Granulin-epithelin precursor binds directly to ADAMTS-7 and ADAMTS-12 and inhibits their degradation of cartilage oligomeric matrix protein. Arthritis Rheum 62, 2023-2036.
    • (2010) Arthritis Rheum , vol.62 , pp. 2023-2036
    • Guo, F.1    Lai, Y.2    Tian, Q.3    Lin, E.A.4    Kong, L.5    Liu, C.6
  • 51
    • 67649354791 scopus 로고    scopus 로고
    • Abundance and location of proteoglycans and hyaluronan within normal and myxomatous mitral valves
    • Gupta, V., Barzilla, J. E., Mendez, J. S., et al. (2009). Abundance and location of proteoglycans and hyaluronan within normal and myxomatous mitral valves. Cardiovasc Pathol 18, 191-197.
    • (2009) Cardiovasc Pathol , vol.18 , pp. 191-197
    • Gupta, V.1    Barzilla, J.E.2    Mendez, J.S.3
  • 52
    • 80053205979 scopus 로고    scopus 로고
    • Pericellular versican regulates the fibroblast-myofibroblast transition: A role for ADAMTS5 protease-mediated proteolysis
    • Hattori, N., Carrino, D. A., Lauer, M. E., et al. (2011). Pericellular versican regulates the fibroblast-myofibroblast transition: a role for ADAMTS5 protease-mediated proteolysis. J Biol Chem 286, 34298-34310.
    • (2011) J Biol Chem , vol.286 , pp. 34298-34310
    • Hattori, N.1    Carrino, D.A.2    Lauer, M.E.3
  • 53
    • 0024786458 scopus 로고
    • Pleomorphism in type I collagen fibrils produced by persistence of the procollagen N-propeptide
    • Hulmes, D. J., Kadler, K. E., Mould, A. P., et al. (1989). Pleomorphism in type I collagen fibrils produced by persistence of the procollagen N-propeptide. J Mol Biol 210, 337-345.
    • (1989) J Mol Biol , vol.210 , pp. 337-345
    • Hulmes, D.J.1    Kadler, K.E.2    Mould, A.P.3
  • 54
    • 0033520318 scopus 로고    scopus 로고
    • ADAM-TS5, ADAM-TS6, and ADAM-TS7, novel members of a new family of zinc metalloproteases. General features and genomic distribution of the ADAM-TS family
    • Hurskainen, T. L., Hirohata, S., Seldin, M. F., and Apte, S. S. (1999). ADAM-TS5, ADAM-TS6, and ADAM-TS7, novel members of a new family of zinc metalloproteases. General features and genomic distribution of the ADAM-TS family. J Biol Chem 274, 25555-25563.
    • (1999) J Biol Chem , vol.274 , pp. 25555-25563
    • Hurskainen, T.L.1    Hirohata, S.2    Seldin, M.F.3    Apte, S.S.4
  • 55
    • 21844444108 scopus 로고    scopus 로고
    • The characterisation of six ADAMTS proteases in the basal chordate Ciona intestinalis provides new insights into the vertebrate ADAMTS family
    • Huxley-Jones, J., Apte, S. S., Robertson, D. L., and Boot-Handford, R. P. (2005). The characterisation of six ADAMTS proteases in the basal chordate Ciona intestinalis provides new insights into the vertebrate ADAMTS family. Int J Biochem Cell Biol 37, 1838-1845.
    • (2005) Int J Biochem Cell Biol , vol.37 , pp. 1838-1845
    • Huxley-Jones, J.1    Apte, S.S.2    Robertson, D.L.3    Boot-Handford, R.P.4
  • 56
    • 49349089963 scopus 로고    scopus 로고
    • Stage-specific activation of MIG-17/ADAMTS controls cell migration in Caenorhabditis elegans
    • Ihara, S., and Nishiwaki, K. (2008). Stage-specific activation of MIG-17/ADAMTS controls cell migration in Caenorhabditis elegans. FEBS J 275, 4296-4305.
    • (2008) FEBS J , vol.275 , pp. 4296-4305
    • Ihara, S.1    Nishiwaki, K.2
  • 57
    • 0026533115 scopus 로고
    • Mechanism of catabolism of aggrecan by articular cartilage
    • Ilic, M. Z., Handley, C. J., Robinson, H. C., and Mok, M. T. (1992). Mechanism of catabolism of aggrecan by articular cartilage. Arch Biochem Biophys 294, 115-122.
    • (1992) Arch Biochem Biophys , vol.294 , pp. 115-122
    • Ilic, M.Z.1    Handley, C.J.2    Robinson, H.C.3    Mok, M.T.4
  • 58
    • 0025853349 scopus 로고
    • Thrombospondin exerts an antiangiogenic effect on cord formation by endothelial cells in vitro
    • Iruela-Arispe, M. L., Bornstein, P., and Sage, H. (1991). Thrombospondin exerts an antiangiogenic effect on cord formation by endothelial cells in vitro. Proc Natl Acad Sci U S A 88, 5026-5030.
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 5026-5030
    • Iruela-Arispe, M.L.1    Bornstein, P.2    Sage, H.3
  • 59
    • 26844448800 scopus 로고    scopus 로고
    • Adam meets Eph: An ADAM substrate recognition module acts as a molecular switch for ephrin cleavage in trans
    • Janes, P. W., Saha, N., Barton, W. A., et al. (2005). Adam meets Eph: an ADAM substrate recognition module acts as a molecular switch for ephrin cleavage in trans. Cell 123, 291-304.
    • (2005) Cell , vol.123 , pp. 291-304
    • Janes, P.W.1    Saha, N.2    Barton, W.A.3
  • 60
    • 0033602549 scopus 로고    scopus 로고
    • Isolated noncompaction of the myocardium
    • Jenni, R., Rojas, J., and Oechslin, E. (1999). Isolated noncompaction of the myocardium. N Engl J Med 340, 966-967.
    • (1999) N Engl J Med , vol.340 , pp. 966-967
    • Jenni, R.1    Rojas, J.2    Oechslin, E.3
  • 61
    • 19944429537 scopus 로고    scopus 로고
    • Role of ADAMTS-1 in atherosclerosis: Remodeling of carotid artery, immunohistochemistry, and proteolysis of versican
    • Jonsson-Rylander, A. C., Nilsson, T., Fritsche-Danielson, R., et al. (2005). Role of ADAMTS-1 in atherosclerosis: remodeling of carotid artery, immunohistochemistry, and proteolysis of versican. Arterioscler Thromb Vasc Biol 25, 180-185.
    • (2005) Arterioscler Thromb Vasc Biol , vol.25 , pp. 180-185
    • Jonsson-Rylander, A.C.1    Nilsson, T.2    Fritsche-Danielson, R.3
  • 62
    • 1642280932 scopus 로고    scopus 로고
    • Altered proteolytic activities of ADAMTS-4 expressed by C-terminal processing
    • Kashiwagi, M., Enghild, J. J., Gendron, C., et al. (2004). Altered proteolytic activities of ADAMTS-4 expressed by C-terminal processing. J Biol Chem 279, 10109-10119.
    • (2004) J Biol Chem , vol.279 , pp. 10109-10119
    • Kashiwagi, M.1    Enghild, J.J.2    Gendron, C.3
  • 63
    • 70249130143 scopus 로고    scopus 로고
    • Cell death-associated ADAMTS4 and versican degradation in vascular tissue
    • Kenagy, R. D., Min, S. K., Clowes, A. W., and Sandy, J. D. (2009). Cell death-associated ADAMTS4 and versican degradation in vascular tissue. J Histochem Cytochem 57, 889-897.
    • (2009) J Histochem Cytochem , vol.57 , pp. 889-897
    • Kenagy, R.D.1    Min, S.K.2    Clowes, A.W.3    Sandy, J.D.4
  • 64
    • 33746954594 scopus 로고    scopus 로고
    • Proteolytic cleavage of versican during cardiac cushion morphogenesis
    • Kern, C. B., Twal, W. O., Mjaatvedt, C. H., et al. (2006). Proteolytic cleavage of versican during cardiac cushion morphogenesis. Dev Dyn 235, 2238-2247.
    • (2006) Dev Dyn , vol.235 , pp. 2238-2247
    • Kern, C.B.1    Twal, W.O.2    Mjaatvedt, C.H.3
  • 65
    • 9144230209 scopus 로고    scopus 로고
    • Expression profiling of metalloproteinases and their inhibitors in cartilage
    • Kevorkian, L., Young, D. A., Darrah, C., et al. (2004). Expression profiling of metalloproteinases and their inhibitors in cartilage. Arthritis Rheum 50, 131-141.
    • (2004) Arthritis Rheum , vol.50 , pp. 131-141
    • Kevorkian, L.1    Young, D.A.2    Darrah, C.3
  • 66
    • 77749304050 scopus 로고    scopus 로고
    • ADAMTS9 is a cell-autonomously acting, anti-angiogenic metalloprotease expressed by microvascular endothelial cells
    • Koo, B. H., Coe, D. M., Dixon, L. J., et al. (2010). ADAMTS9 is a cell-autonomously acting, anti-angiogenic metalloprotease expressed by microvascular endothelial cells. Am J Pathol 176, 1494-1504.
    • (2010) Am J Pathol , vol.176 , pp. 1494-1504
    • Koo, B.H.1    Coe, D.M.2    Dixon, L.J.3
  • 69
    • 21244501417 scopus 로고    scopus 로고
    • ADAMTS1 proteinase is up-regulated in wounded skin and regulates migration of fibroblasts and endothelial cells
    • Krampert, M., Kuenzle, S., Thai, S. N., Lee, N., Iruela-Arispe, M. L., and Werner, S. (2005). ADAMTS1 proteinase is up-regulated in wounded skin and regulates migration of fibroblasts and endothelial cells. J Biol Chem 280, 23844-23852.
    • (2005) J Biol Chem , vol.280 , pp. 23844-23852
    • Krampert, M.1    Kuenzle, S.2    Thai, S.N.3    Lee, N.4    Iruela-Arispe, M.L.5    Werner, S.6
  • 70
    • 0037023703 scopus 로고    scopus 로고
    • The Caenorhabditis elegans ADAMTS family gene adt-1 is necessary for morphogenesis of the male copulatory organs
    • Kuno, K., Baba, C., Asaka, A., Matsushima, C., Matsushima, K., and Hosono, R. (2002). The Caenorhabditis elegans ADAMTS family gene adt-1 is necessary for morphogenesis of the male copulatory organs. J Biol Chem 277, 12228-12236.
    • (2002) J Biol Chem , vol.277 , pp. 12228-12236
    • Kuno, K.1    Baba, C.2    Asaka, A.3    Matsushima, C.4    Matsushima, K.5    Hosono, R.6
  • 71
    • 0031036524 scopus 로고    scopus 로고
    • Molecular cloning of a gene encoding a new type of metalloproteinase-disintegrin family protein with thrombospondin motifs as an inflammation associated gene
    • Kuno, K., Kanada, N., Nakashima, E., Fujiki, F., Ichimura, F., and Matsushima, K. (1997). Molecular cloning of a gene encoding a new type of metalloproteinase-disintegrin family protein with thrombospondin motifs as an inflammation associated gene. J Biol Chem 272, 556-562.
    • (1997) J Biol Chem , vol.272 , pp. 556-562
    • Kuno, K.1    Kanada, N.2    Nakashima, E.3    Fujiki, F.4    Ichimura, F.5    Matsushima, K.6
  • 72
    • 18744437369 scopus 로고    scopus 로고
    • Aggrecan degradation in human cartilage - evidence for both matrix metalloproteinase and aggrecanase activity in normal, osteoarthritic, and rheumatoid joints
    • Lark, M. W., Bayne, E. K., Flanagan, J., et al. (1997). Aggrecan degradation in human cartilage - evidence for both matrix metalloproteinase and aggrecanase activity in normal, osteoarthritic, and rheumatoid joints. J Clin Invest 100, 93-106.
    • (1997) J Clin Invest , vol.100 , pp. 93-106
    • Lark, M.W.1    Bayne, E.K.2    Flanagan, J.3
  • 73
    • 33751073396 scopus 로고    scopus 로고
    • ADAMTS1 mediates the release of antiangiogenic polypeptides from TSP1 and 2
    • Lee, N. V., Sato, M., Annis, D. S., et al. (2006). ADAMTS1 mediates the release of antiangiogenic polypeptides from TSP1 and 2. EMBO J 25, 5270-5283.
    • (2006) EMBO J , vol.25 , pp. 5270-5283
    • Lee, N.V.1    Sato, M.2    Annis, D.S.3
  • 74
    • 0035807348 scopus 로고    scopus 로고
    • Mutations in a member of the ADAMTS gene family cause thrombotic thrombocytopenic purpura
    • Levy, G. G., Nichols, W. C., Lian, E. C., et al. (2001). Mutations in a member of the ADAMTS gene family cause thrombotic thrombocytopenic purpura. Nature 413, 488-494.
    • (2001) Nature , vol.413 , pp. 488-494
    • Levy, G.G.1    Nichols, W.C.2    Lian, E.C.3
  • 75
    • 0035870995 scopus 로고    scopus 로고
    • Transgenic mice with inactive alleles for procollagen N-proteinase (ADAMTS-2) develop fragile skin and male sterility
    • Li, S. W., Arita, M., Fertala, A., et al. (2001). Transgenic mice with inactive alleles for procollagen N-proteinase (ADAMTS-2) develop fragile skin and male sterility. Biochem J 355, 271-278.
    • (2001) Biochem J , vol.355 , pp. 271-278
    • Li, S.W.1    Arita, M.2    Fertala, A.3
  • 76
    • 67650386153 scopus 로고    scopus 로고
    • C-terminal ADAMTS-18 fragment induces oxidative platelet fragmentation, dissolves platelet aggregates, and protects against carotid artery occusion and cerebral stroke
    • Li, Z., Nard, M. A., Li, Y. S., et al. (2009). C-terminal ADAMTS-18 fragment induces oxidative platelet fragmentation, dissolves platelet aggregates, and protects against carotid artery occusion and cerebral stroke. Blood 113, 6051-6060.
    • (2009) Blood , vol.113 , pp. 6051-6060
    • Li, Z.1    Nard, M.A.2    Li, Y.S.3
  • 77
    • 85062725461 scopus 로고    scopus 로고
    • ADAMTS-7: A metalloproteinase that directly binds to and degrades cartilage oligomeric matrix protein
    • Liu, C. J., Kong, W., Ilalov, K., et al. (2006a). ADAMTS-7: a metalloproteinase that directly binds to and degrades cartilage oligomeric matrix protein. FASEB J 20, 988-990.
    • (2006) FASEB J , vol.20 , pp. 988-990
    • Liu, C.J.1    Kong, W.2    Ilalov, K.3
  • 78
    • 33744909868 scopus 로고    scopus 로고
    • ADAMTS-12 associates with and degrades cartilage oligomeric matrix protein
    • Liu, C. J., Kong, W., Xu, K., et al. (2006b). ADAMTS-12 associates with and degrades cartilage oligomeric matrix protein. J Biol Chem 281, 15800-15808.
    • (2006) J Biol Chem , vol.281 , pp. 15800-15808
    • Liu, C.J.1    Kong, W.2    Xu, K.3
  • 79
    • 36249015281 scopus 로고    scopus 로고
    • The ADAMTS12 metalloproteinase exhibits anti-tumorigenic properties through modulation of the Ras-dependent ERK signalling pathway
    • Llamazares, M., Obaya, A. J., Moncada-Pazos, A., et al. (2007). The ADAMTS12 metalloproteinase exhibits anti-tumorigenic properties through modulation of the Ras-dependent ERK signalling pathway. J Cell Sci 120, 3544-3552.
    • (2007) J Cell Sci , vol.120 , pp. 3544-3552
    • Llamazares, M.1    Obaya, A.J.2    Moncada-Pazos, A.3
  • 80
    • 77954352573 scopus 로고    scopus 로고
    • Extracellular protease ADAMTS9 suppresses esophageal and nasopharyngeal carcinoma tumor formation by inhibiting angiogenesis
    • Lo, P. H., Lung, H. L., Cheung, A. K., et al. (2010). Extracellular protease ADAMTS9 suppresses esophageal and nasopharyngeal carcinoma tumor formation by inhibiting angiogenesis. Cancer Res 70, 5567-5576.
    • (2010) Cancer Res , vol.70 , pp. 5567-5576
    • Lo, P.H.1    Lung, H.L.2    Cheung, A.K.3
  • 82
    • 4043114232 scopus 로고    scopus 로고
    • Identification of prodomain determinants involved in ADAMTS-1 biosynthesis
    • Longpré, J. M., and Leduc, R. (2004). Identification of prodomain determinants involved in ADAMTS-1 biosynthesis. J Biol Chem 279, 33237-33245.
    • (2004) J Biol Chem , vol.279 , pp. 33237-33245
    • Longpré, J.M.1    Leduc, R.2
  • 84
    • 74049137935 scopus 로고    scopus 로고
    • ADAMTS13 mutations and polymorphisms in congenital thrombotic thrombocytopenic purpura
    • Lotta, L. A., Garagiola, I., Palla, R., Cairo, A., and Peyvandi, F. (2010). ADAMTS13 mutations and polymorphisms in congenital thrombotic thrombocytopenic purpura. Hum Mutat 31, 11-19.
    • (2010) Hum Mutat , vol.31 , pp. 11-19
    • Lotta, L.A.1    Garagiola, I.2    Palla, R.3    Cairo, A.4    Peyvandi, F.5
  • 85
    • 0026771893 scopus 로고
    • N-terminal sequence of proteoglycan fragments isolated from medium of interleukin-1-treated articular-cartilage cultures
    • Loulakis, P., Shrikhande, A., Davis, G., and Maniglia, C. A. (1992). N-terminal sequence of proteoglycan fragments isolated from medium of interleukin-1-treated articular-cartilage cultures. Putative site(s) of enzymic cleavage. Biochem J 284, 589-593.
    • (1992) Putative site(s) of enzymic cleavage. Biochem J , vol.284 , pp. 589-593
    • Loulakis, P.1    Shrikhande, A.2    Davis, G.3    Maniglia, C.A.4
  • 86
    • 0028047686 scopus 로고
    • Structure of the catalytic domain of fibroblast collagenase complexed with an inhibitor
    • Lovejoy, B., Cleasby, A., Hassell, A. M., et al. (1994). Structure of the catalytic domain of fibroblast collagenase complexed with an inhibitor. Science 263, 375-377.
    • (1994) Science , vol.263 , pp. 375-377
    • Lovejoy, B.1    Cleasby, A.2    Hassell, A.M.3
  • 87
    • 33748597666 scopus 로고    scopus 로고
    • Amino acid regions 572-579 and 657-666 of the spacer domain of ADAMTS13 provide a common antigenic core required for binding of antibodies in patients with acquired TTP
    • Luken, B. M., Turenhout, E. A., Kaijen, P. H., et al. (2006). Amino acid regions 572-579 and 657-666 of the spacer domain of ADAMTS13 provide a common antigenic core required for binding of antibodies in patients with acquired TTP. Thromb Haemost 96, 295-301.
    • (2006) Thromb Haemost , vol.96 , pp. 295-301
    • Luken, B.M.1    Turenhout, E.A.2    Kaijen, P.H.3
  • 88
    • 0038109791 scopus 로고    scopus 로고
    • ADAMTS1/METH1 inhibits endothelial cell proliferation by direct binding and sequestration of VEGF165
    • Luque, A., Carpizo, D. R., and Iruela-Arispe, M. L. (2003). ADAMTS1/METH1 inhibits endothelial cell proliferation by direct binding and sequestration of VEGF165. J Biol Chem 278, 23656-23665.
    • (2003) J Biol Chem , vol.278 , pp. 23656-23665
    • Luque, A.1    Carpizo, D.R.2    Iruela-Arispe, M.L.3
  • 89
    • 20444454641 scopus 로고    scopus 로고
    • Binding of ADAMTS13 to von Willebrand factor
    • Majerus, E. M., Anderson, P. J., and Sadler, J. E. (2005). Binding of ADAMTS13 to von Willebrand factor. J Biol Chem 280, 21773-21778.
    • (2005) J Biol Chem , vol.280 , pp. 21773-21778
    • Majerus, E.M.1    Anderson, P.J.2    Sadler, J.E.3
  • 90
    • 67349155506 scopus 로고    scopus 로고
    • Adamts5, the gene encoding a proteoglycan-degrading metalloprotease, is expressed by specific cell lineages during mouse embryonic development and in adult tissues
    • McCulloch, D. R., Le Goff, C., Bhatt, S., Dixon, L. J., Sandy, J. D., and Apte, S. S. (2009). Adamts5, the gene encoding a proteoglycan-degrading metalloprotease, is expressed by specific cell lineages during mouse embryonic development and in adult tissues. Gene Expr Patterns 9, 314-323.
    • (2009) Gene Expr Patterns , vol.9 , pp. 314-323
    • McCulloch, D.R.1    Le Goff, C.2    Bhatt, S.3    Dixon, L.J.4    Sandy, J.D.5    Apte, S.S.6
  • 91
    • 1642341845 scopus 로고    scopus 로고
    • Adamts-1 is essential for the development and function of the urogenital system
    • Mittaz, L., Russell, D. L., Wilson, T., et al. (2004). Adamts-1 is essential for the development and function of the urogenital system. Biol Reprod 70, 1096-1105.
    • (2004) Biol Reprod , vol.70 , pp. 1096-1105
    • Mittaz, L.1    Russell, D.L.2    Wilson, T.3
  • 92
    • 0020428664 scopus 로고
    • Unusually large plasma factor VIII: Von Willebrand factor multimers in chronic relapsing thrombotic thrombocytopenic purpura
    • Moake, J. L., Rudy, C. K., Troll, J. H., et al. (1982). Unusually large plasma factor VIII: von Willebrand factor multimers in chronic relapsing thrombotic thrombocytopenic purpura. N Engl J Med 307, 1432-1435.
    • (1982) N Engl J Med , vol.307 , pp. 1432-1435
    • Moake, J.L.1    Rudy, C.K.2    Troll, J.H.3
  • 93
    • 8044250278 scopus 로고    scopus 로고
    • Cloning of a disintegrin metalloproteinase that processes precursor tumour-necrosis factor-alpha
    • Moss, M. L., Jin, S. L. C., Milla, M. E., et al. (1997). Cloning of a disintegrin metalloproteinase that processes precursor tumour-necrosis factor-alpha. Nature 385, 733-736.
    • (1997) Nature , vol.385 , pp. 733-736
    • Moss, M.L.1    Jin, S.L.C.2    Milla, M.E.3
  • 94
    • 37549037806 scopus 로고    scopus 로고
    • Crystal structures of the two major aggrecan degrading enzymes, ADAMTS4 and ADAMTS5
    • Mosyak, L., Georgiadis, K., Shane, T., et al. (2008). Crystal structures of the two major aggrecan degrading enzymes, ADAMTS4 and ADAMTS5. Protein Sci 17, 16-21.
    • (2008) Protein Sci , vol.17 , pp. 16-21
    • Mosyak, L.1    Georgiadis, K.2    Shane, T.3
  • 95
    • 78650440475 scopus 로고    scopus 로고
    • Localizing matrix metalloproteinase activities in the pericellular environment
    • Murphy, G., and Nagase, H. (2011). Localizing matrix metalloproteinase activities in the pericellular environment. FEBS J 278, 2-15.
    • (2011) FEBS J , vol.278 , pp. 2-15
    • Murphy, G.1    Nagase, H.2
  • 96
    • 0038639763 scopus 로고    scopus 로고
    • Aggrecanases and cartilage matrix degradation
    • Nagase, H., and Kashiwagi, M. (2003). Aggrecanases and cartilage matrix degradation. Arthritis Res Ther 5, 94-103.
    • (2003) Arthritis Res Ther , vol.5 , pp. 94-103
    • Nagase, H.1    Kashiwagi, M.2
  • 97
    • 31344458952 scopus 로고    scopus 로고
    • Structure and function of matrix metalloproteinases and TIMPs
    • Nagase, H., Visse, R., and Murphy, G. (2006). Structure and function of matrix metalloproteinases and TIMPs. Cardiovasc Res 69, 562-573.
    • (2006) Cardiovasc Res , vol.69 , pp. 562-573
    • Nagase, H.1    Visse, R.2    Murphy, G.3
  • 98
    • 28444437398 scopus 로고    scopus 로고
    • Expression of versican and ADAMTS1, 4, and 5 during bone development in the rat mandible and hind limb
    • Nakamura, M., Sone, S., Takahashi, I., Mizoguchi, I., Echigo, S., and Sasano, Y. (2005). Expression of versican and ADAMTS1, 4, and 5 during bone development in the rat mandible and hind limb. J Histochem Cytochem 53, 1553-1562.
    • (2005) J Histochem Cytochem , vol.53 , pp. 1553-1562
    • Nakamura, M.1    Sone, S.2    Takahashi, I.3    Mizoguchi, I.4    Echigo, S.5    Sasano, Y.6
  • 99
    • 2142711672 scopus 로고    scopus 로고
    • Complement-independent Ab-induced peroxide lysis of platelets requires 12-lipoxygenase and a platelet NADPH oxidase pathway
    • Nardi, M., Feinmark, S. J., Hu, L., Li, Z., and Karpatkin, S. (2004). Complement-independent Ab-induced peroxide lysis of platelets requires 12-lipoxygenase and a platelet NADPH oxidase pathway. J Clin Invest 113, 973-980.
    • (2004) J Clin Invest , vol.113 , pp. 973-980
    • Nardi, M.1    Feinmark, S.J.2    Hu, L.3    Li, Z.4    Karpatkin, S.5
  • 100
    • 0035823022 scopus 로고    scopus 로고
    • Complement-independent, peroxide-induced antibody lysis of platelets in HIV-1-related immune thrombocytopenia
    • Nardi, M., Tomlinson, S., Greco, M. A., and Karpatkin, S. (2001). Complement-independent, peroxide-induced antibody lysis of platelets in HIV-1-related immune thrombocytopenia. Cell 106, 551-561.
    • (2001) Cell , vol.106 , pp. 551-561
    • Nardi, M.1    Tomlinson, S.2    Greco, M.A.3    Karpatkin, S.4
  • 101
    • 12844286997 scopus 로고    scopus 로고
    • Dual role of matrix metalloproteinases (matrixins) in intimal thickening and atherosclerotic plaque rupture
    • Newby, A. C. (2005). Dual role of matrix metalloproteinases (matrixins) in intimal thickening and atherosclerotic plaque rupture. Physiol Rev 85, 1-31.
    • (2005) Physiol Rev , vol.85 , pp. 1-31
    • Newby, A.C.1
  • 102
    • 0034705575 scopus 로고    scopus 로고
    • A metalloprotease disintegrin that controls cell migration in Caenorhabditis elegans
    • Nishiwaki, K., Hisamoto, N., and Matsumoto, K. (2000). A metalloprotease disintegrin that controls cell migration in Caenorhabditis elegans. Science 288, 2205-2208.
    • (2000) Science , vol.288 , pp. 2205-2208
    • Nishiwaki, K.1    Hisamoto, N.2    Matsumoto, K.3
  • 103
    • 0026879788 scopus 로고
    • Evidence for a relationship between Ehlers-Danlos type VII C in humans and bovine dermatosparaxis
    • Nusgens, B. V., Verellen-Dumoulin, C., Hermanns-Le, T., et al. (1992). Evidence for a relationship between Ehlers-Danlos type VII C in humans and bovine dermatosparaxis. Nat Genet 1, 214-217.
    • (1992) Nat Genet , vol.1 , pp. 214-217
    • Nusgens, B.V.1    Verellen-Dumoulin, C.2    Hermanns-Le, T.3
  • 104
    • 33847195428 scopus 로고    scopus 로고
    • Matrix metalloproteinases and the regulation of tissue remodelling
    • Page-McCaw, A., Ewald, A. J., and Werb, Z. (2007). Matrix metalloproteinases and the regulation of tissue remodelling. Nat Rev Mol Cell Biol 8, 221-233.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 221-233
    • Page-McCaw, A.1    Ewald, A.J.2    Werb, Z.3
  • 106
    • 17044420401 scopus 로고    scopus 로고
    • Ovulation: New factors that prepare the oocyte for fertilization
    • Richards, J. S. (2005). Ovulation: new factors that prepare the oocyte for fertilization. Mol Cell Endocrinol 234, 75-79.
    • (2005) Mol Cell Endocrinol , vol.234 , pp. 75-79
    • Richards, J.S.1
  • 108
    • 0036295493 scopus 로고    scopus 로고
    • ADAMTS1 cleaves aggrecan at multiple sites and is differentially inhibited by metalloproteinase inhibitors
    • Rodriguez-Manzaneque, J. C., Westling, J., Thai, S. N., et al. (2002). ADAMTS1 cleaves aggrecan at multiple sites and is differentially inhibited by metalloproteinase inhibitors. Biochem Biophys Res Commun 293, 501-508.
    • (2002) Biochem Biophys Res Commun , vol.293 , pp. 501-508
    • Rodriguez-Manzaneque, J.C.1    Westling, J.2    Thai, S.N.3
  • 109
    • 0019442145 scopus 로고
    • The complex multimeric composition of factor VIII/von Willebrand factor
    • Ruggeri, Z. M., and Zimmerman, T. S. (1981). The complex multimeric composition of factor VIII/von Willebrand factor. Blood 57, 1140-1143.
    • (1981) Blood , vol.57 , pp. 1140-1143
    • Ruggeri, Z.M.1    Zimmerman, T.S.2
  • 110
    • 0142211236 scopus 로고    scopus 로고
    • Processing and localization of ADAMTS-1 and proteolytic cleavage of versican during cumulus matrix expansion and ovulation
    • Russell, D. L., Doyle, K. M., Ochsner, S. A., Sandy, J. D., and Richards, J. S. (2003). Processing and localization of ADAMTS-1 and proteolytic cleavage of versican during cumulus matrix expansion and ovulation. J Biol Chem 278, 42330-42339.
    • (2003) J Biol Chem , vol.278 , pp. 42330-42339
    • Russell, D.L.1    Doyle, K.M.2    Ochsner, S.A.3    Sandy, J.D.4    Richards, J.S.5
  • 111
    • 0031686041 scopus 로고    scopus 로고
    • Biochemistry and genetics of von Willebrand factor
    • Sadler, J. E. (1998). Biochemistry and genetics of von Willebrand factor. Annu Rev Biochem 67, 395-424.
    • (1998) Annu Rev Biochem , vol.67 , pp. 395-424
    • Sadler, J.E.1
  • 112
    • 30544436016 scopus 로고    scopus 로고
    • A contentious issue finds some clarity: On the independent and complementary roles of aggrecanase activity and MMP activity in human joint aggrecanolysis
    • Sandy, J. D. (2006). A contentious issue finds some clarity: on the independent and complementary roles of aggrecanase activity and MMP activity in human joint aggrecanolysis. Osteoarthritis Cartilage 14, 95-100.
    • (2006) Osteoarthritis Cartilage , vol.14 , pp. 95-100
    • Sandy, J.D.1
  • 113
    • 0026682509 scopus 로고
    • The structure of aggrecan fragments in human synovial fluid. Evidence for the involvement in osteoarthritis of a novel proteinase which cleaves the Glu 373-Ala 374 bond of the interglobular domain
    • Sandy, J. D., Flannery, C. R., Neame, P. J., and Lohmander, L. S. (1992). The structure of aggrecan fragments in human synovial fluid. Evidence for the involvement in osteoarthritis of a novel proteinase which cleaves the Glu 373-Ala 374 bond of the interglobular domain. J Clin Invest 89, 1512-1516.
    • (1992) J Clin Invest , vol.89 , pp. 1512-1516
    • Sandy, J.D.1    Flannery, C.R.2    Neame, P.J.3    Lohmander, L.S.4
  • 114
    • 0025776382 scopus 로고
    • Catabolism of aggrecan in cartilage explants. Identification of a major cleavage site within the interglobular domain
    • Sandy, J. D., Neame, P. J., Boynton, R. E., and Flannery, C. R. (1991). Catabolism of aggrecan in cartilage explants. Identification of a major cleavage site within the interglobular domain. J Biol Chem 266, 8683-8685.
    • (1991) J Biol Chem , vol.266 , pp. 8683-8685
    • Sandy, J.D.1    Neame, P.J.2    Boynton, R.E.3    Flannery, C.R.4
  • 115
    • 38349112018 scopus 로고    scopus 로고
    • High resolution crystal structure of the catalytic domain of ADAMTS-5 (aggrecanase-2)
    • Shieh, H. S., Mathis, K. J., Williams, J. M., et al. (2008). High resolution crystal structure of the catalytic domain of ADAMTS-5 (aggrecanase-2). J Biol Chem 283, 1501-1507.
    • (2008) J Biol Chem , vol.283 , pp. 1501-1507
    • Shieh, H.S.1    Mathis, K.J.2    Williams, J.M.3
  • 116
    • 0034033973 scopus 로고    scopus 로고
    • ADAMTS-1: A metalloproteinase-disintegrin essential for normal growth, fertility, and organ morphology and function
    • Shindo, T., Kurihara, H., Kuno, K., et al. (2000). ADAMTS-1: a metalloproteinase-disintegrin essential for normal growth, fertility, and organ morphology and function. J Clin Invest 105, 1345-1352.
    • (2000) J Clin Invest , vol.105 , pp. 1345-1352
    • Shindo, T.1    Kurihara, H.2    Kuno, K.3
  • 117
    • 40149083619 scopus 로고    scopus 로고
    • The secreted metalloprotease ADAMTS20 is required for melanoblast survival
    • Silver, D. L., Hou, L., Somerville, R., Young, M. E., Apte, S. S., and Pavan, W. J. (2008). The secreted metalloprotease ADAMTS20 is required for melanoblast survival. PLoS Genet 4, e1000003.
    • (2008) PLoS Genet , vol.4 , pp. e1000003
    • Silver, D.L.1    Hou, L.2    Somerville, R.3    Young, M.E.4    Apte, S.S.5    Pavan, W.J.6
  • 118
    • 0142152440 scopus 로고    scopus 로고
    • ADAMTS-13 cysteine-rich/spacer domains are functionally essential for von Willebrand factor cleavage
    • Soejima, K., Matsumoto, M., Kokame, K., et al. (2003). ADAMTS-13 cysteine-rich/spacer domains are functionally essential for von Willebrand factor cleavage. Blood 102, 3232-3237.
    • (2003) Blood , vol.102 , pp. 3232-3237
    • Soejima, K.1    Matsumoto, M.2    Kokame, K.3
  • 119
    • 0034759807 scopus 로고    scopus 로고
    • A novel human metalloprotease synthesized in the liver and secreted into the blood: Possibly, the von Willebrand factor-cleaving protease
    • Soejima, K., Mimura, N., Hirashima, M., et al. (2001). A novel human metalloprotease synthesized in the liver and secreted into the blood: possibly, the von Willebrand factor-cleaving protease? J Biochem 130, 475-480.
    • (2001) J Biochem , vol.130 , pp. 475-480
    • Soejima, K.1    Mimura, N.2    Hirashima, M.3
  • 120
    • 4143129884 scopus 로고    scopus 로고
    • ADAMTS7B, the full-length product of the ADAMTS7 gene, is a chondroitin sulfate proteoglycan containing a mucin domain
    • Somerville, R. P., Longpre, J. M., Apel, E. D., et al. (2004). ADAMTS7B, the full-length product of the ADAMTS7 gene, is a chondroitin sulfate proteoglycan containing a mucin domain. J Biol Chem 279, 35159-35175.
    • (2004) J Biol Chem , vol.279 , pp. 35159-35175
    • Somerville, R.P.1    Longpre, J.M.2    Apel, E.D.3
  • 121
    • 0038237345 scopus 로고    scopus 로고
    • Characterization of ADAMTS-9 and ADAMTS-20 as a distinct ADAMTS subfamily related to Caenorhabditis elegans GON-1
    • Somerville, R. P., Longpré, J. M., Jungers, K. A., et al. (2003). Characterization of ADAMTS-9 and ADAMTS-20 as a distinct ADAMTS subfamily related to Caenorhabditis elegans GON-1. J Biol Chem 278, 9503-9513.
    • (2003) J Biol Chem , vol.278 , pp. 9503-9513
    • Somerville, R.P.1    Longpré, J.M.2    Jungers, K.A.3
  • 122
    • 38849156394 scopus 로고    scopus 로고
    • Endocardial Brg1 represses ADAMTS1 to maintain the microenvironment for myocardial morphogenesis
    • Stankunas, K., Hang, C. T., Tsun, Z. Y., et al. (2008). Endocardial Brg1 represses ADAMTS1 to maintain the microenvironment for myocardial morphogenesis. Dev Cell 14, 298-311.
    • (2008) Dev Cell , vol.14 , pp. 298-311
    • Stankunas, K.1    Hang, C.T.2    Tsun, Z.Y.3
  • 123
    • 15844384854 scopus 로고    scopus 로고
    • ADAMTS5 is the major aggrecanase in mouse cartilage in vivo and in vitro
    • Stanton, H., Rogerson, F. M., East, C. J., et al. (2005). ADAMTS5 is the major aggrecanase in mouse cartilage in vivo and in vitro. Nature 434, 648-652.
    • (2005) Nature , vol.434 , pp. 648-652
    • Stanton, H.1    Rogerson, F.M.2    East, C.J.3
  • 124
    • 30544448357 scopus 로고    scopus 로고
    • Human osteoarthritis synovial fluid and joint cartilage contain both aggrecanase- and matrix metalloproteinase-generated aggrecan fragments
    • Struglics, A., Larsson, S., Pratta, M. A., Kumar, S., Lark, M. W., and Lohmander, L. S. (2006). Human osteoarthritis synovial fluid and joint cartilage contain both aggrecanase- and matrix metalloproteinase-generated aggrecan fragments. Osteoarthritis Cartilage 14, 101-113.
    • (2006) Osteoarthritis Cartilage , vol.14 , pp. 101-113
    • Struglics, A.1    Larsson, S.2    Pratta, M.A.3    Kumar, S.4    Lark, M.W.5    Lohmander, L.S.6
  • 125
    • 63649149047 scopus 로고    scopus 로고
    • Three-dimensional domain architecture of the ADAM family proteinases
    • Takeda, S. (2009). Three-dimensional domain architecture of the ADAM family proteinases. Semin Cell Dev Biol 20, 146-152.
    • (2009) Semin Cell Dev Biol , vol.20 , pp. 146-152
    • Takeda, S.1
  • 126
    • 33745731954 scopus 로고    scopus 로고
    • Crystal structures of VAP1 reveal ADAMs' MDC domain architecture and its unique C-shaped scaffold
    • Takeda, S., Igarashi, T., Mori, H., and Araki, S. (2006). Crystal structures of VAP1 reveal ADAMs' MDC domain architecture and its unique C-shaped scaffold. EMBO J 25, 2388-2396.
    • (2006) EMBO J , vol.25 , pp. 2388-2396
    • Takeda, S.1    Igarashi, T.2    Mori, H.3    Araki, S.4
  • 127
    • 82755161763 scopus 로고    scopus 로고
    • Snake venom metalloproteinases: Structure, function and relevance to the mammalian ADAM/ADAMTS family proteins
    • Takeda, S., Takeya, H., and Iwanaga, I. (2012). Snake venom metalloproteinases: structure, function and relevance to the mammalian ADAM/ADAMTS family proteins. Biochim Biophys Acta 1824, 164-176.
    • (2012) Biochim Biophys Acta , vol.1824 , pp. 164-176
    • Takeda, S.1    Takeya, H.2    Iwanaga, I.3
  • 128
    • 0037191047 scopus 로고    scopus 로고
    • Crystal structure of the TSP-1 type 1 repeats: A novel layered fold and its biological implication
    • Tan, K., Duquette, M., Liu, J. H., et al. (2002). Crystal structure of the TSP-1 type 1 repeats: a novel layered fold and its biological implication. J Cell Biol 159, 373-382.
    • (2002) J Cell Biol , vol.159 , pp. 373-382
    • Tan, K.1    Duquette, M.2    Liu, J.H.3
  • 129
    • 0027290714 scopus 로고
    • Peptides derived from two separate domains of the matrix protein thrombospondin-1 have anti-angiogenic activity
    • Tolsma, S. S., Volpert, O. V., Good, D. J., Frazier, W. A., Polverini, P. J., and Bouck, N. (1993). Peptides derived from two separate domains of the matrix protein thrombospondin-1 have anti-angiogenic activity. J Cell Biol 122, 497-511.
    • (1993) J Cell Biol , vol.122 , pp. 497-511
    • Tolsma, S.S.1    Volpert, O.V.2    Good, D.J.3    Frazier, W.A.4    Polverini, P.J.5    Bouck, N.6
  • 130
    • 0345211445 scopus 로고    scopus 로고
    • Purification and cloning of aggrecanase-1: A member of the ADAMTS family of proteins
    • Tortorella, M. D., Burn, T. C., Pratta, M. A., et al. (1999). Purification and cloning of aggrecanase-1: a member of the ADAMTS family of proteins. Science 284, 1664-1666.
    • (1999) Science , vol.284 , pp. 1664-1666
    • Tortorella, M.D.1    Burn, T.C.2    Pratta, M.A.3
  • 131
    • 0036775227 scopus 로고    scopus 로고
    • Characterization of human aggrecanase 2 (ADAM-TS5): Substrate specificity studies and comparison with aggrecanase 1 (ADAM-TS4)
    • Tortorella, M. D., Liu, R. Q., Burn, T., Newton, R. C., and Arner, E. (2002). Characterization of human aggrecanase 2 (ADAM-TS5): substrate specificity studies and comparison with aggrecanase 1 (ADAM-TS4). Matrix Biol 21, 499-511.
    • (2002) Matrix Biol , vol.21 , pp. 499-511
    • Tortorella, M.D.1    Liu, R.Q.2    Burn, T.3    Newton, R.C.4    Arner, E.5
  • 132
    • 54049085750 scopus 로고    scopus 로고
    • Calcium pentosan polysulfate is a multifaceted exosite inhibitor of aggrecanases
    • Troeberg, L., Fushimi, K., Khokha, R., Emonard, H., Ghosh, P., and Nagase, H. (2008). Calcium pentosan polysulfate is a multifaceted exosite inhibitor of aggrecanases. FASEB J 22, 3515-3524.
    • (2008) FASEB J , vol.22 , pp. 3515-3524
    • Troeberg, L.1    Fushimi, K.2    Khokha, R.3    Emonard, H.4    Ghosh, P.5    Nagase, H.6
  • 133
    • 84863373517 scopus 로고    scopus 로고
    • Pentosan polysulfate increases affinity between ADAMTS-5 and TIMP-3 through formation of an electrostatically driven trimolecular complex
    • Troeberg, L., Mulloy, B., Ghosh, P., Lee, M. H., Murphy, G., and Nagase, H. (2012). Pentosan polysulfate increases affinity between ADAMTS-5 and TIMP-3 through formation of an electrostatically driven trimolecular complex. Biochem J 443, 307-315.
    • (2012) Biochem J , vol.443 , pp. 307-315
    • Troeberg, L.1    Mulloy, B.2    Ghosh, P.3    Lee, M.H.4    Murphy, G.5    Nagase, H.6
  • 134
    • 0025025442 scopus 로고
    • The cysteine switch: A principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metallo-proteinase gene family
    • Van Wart, H. E., and Birkedal-Hansen, H. (1990). The cysteine switch: a principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metallo-proteinase gene family. Proc Natl Acad Sci U S A 87, 5578-5582.
    • (1990) Proc Natl Acad Sci U S A , vol.87 , pp. 5578-5582
    • Van Wart, H.E.1    Birkedal-Hansen, H.2
  • 135
    • 0038757017 scopus 로고    scopus 로고
    • METH-1, a human ortholog of ADAMTS-1, and METH-2 are members of a new family of proteins with angio-inhibitory activity
    • Vazquez, F., Hastings, G., Ortega, M. A., et al. (1999). METH-1, a human ortholog of ADAMTS-1, and METH-2 are members of a new family of proteins with angio-inhibitory activity. J Biol Chem 274, 23349-23357.
    • (1999) J Biol Chem , vol.274 , pp. 23349-23357
    • Vazquez, F.1    Hastings, G.2    Ortega, M.A.3
  • 136
    • 79960390318 scopus 로고    scopus 로고
    • Adamts5 deletion blocks murine dermal repair through CD44-mediated aggrecan accumulation and modulation of transforming growth factor beta1 (TGFbeta1) signaling
    • Velasco, J., Li, J., DiPietro, L., Stepp, M. A., Sandy, J. D., and Plaas, A. (2011). Adamts5 deletion blocks murine dermal repair through CD44-mediated aggrecan accumulation and modulation of transforming growth factor beta1 (TGFbeta1) signaling. J Biol Chem 286, 26016-26027.
    • (2011) J Biol Chem , vol.286 , pp. 26016-26027
    • Velasco, J.1    Li, J.2    DiPietro, L.3    Stepp, M.A.4    Sandy, J.D.5    Plaas, A.6
  • 137
    • 0037693895 scopus 로고    scopus 로고
    • Matrix metalloproteinases and tissue inhibitors of metallo-proteinases: Structure, function, and biochemistry
    • Visse, R., and Nagase, H. (2003). Matrix metalloproteinases and tissue inhibitors of metallo-proteinases: structure, function, and biochemistry. Circ Res 92, 827-839.
    • (2003) Circ Res , vol.92 , pp. 827-839
    • Visse, R.1    Nagase, H.2
  • 138
    • 0027449459 scopus 로고
    • Modulation of endothelial cell proliferation, adhesion, and motility by recombinant heparin-binding domain and synthetic pep-tides from the type I repeats of thrombospondin
    • Vogel, T., Guo, N. H., Krutzsch, H. C., et al. (1993). Modulation of endothelial cell proliferation, adhesion, and motility by recombinant heparin-binding domain and synthetic pep-tides from the type I repeats of thrombospondin. J Cell Biochem 53, 74-84.
    • (1993) J Cell Biochem , vol.53 , pp. 74-84
    • Vogel, T.1    Guo, N.H.2    Krutzsch, H.C.3
  • 139
    • 63649122439 scopus 로고    scopus 로고
    • ADAMTS-7 mediates vascular smooth muscle cell migration and neointima formation in balloon-injured rat arteries
    • Wang, L., Zheng, J., Bai, X., et al. (2009). ADAMTS-7 mediates vascular smooth muscle cell migration and neointima formation in balloon-injured rat arteries. Circ Res 104, 688-698.
    • (2009) Circ Res , vol.104 , pp. 688-698
    • Wang, L.1    Zheng, J.2    Bai, X.3
  • 140
    • 2442595171 scopus 로고    scopus 로고
    • Proprotein convertase furin interacts with and cleaves pro-ADAMTS4 (Aggrecanase-1) in the trans-Golgi network
    • Wang, P., Tortorella, M., England, K., et al. (2004). Proprotein convertase furin interacts with and cleaves pro-ADAMTS4 (Aggrecanase-1) in the trans-Golgi network. J Biol Chem 279, 15434-15440.
    • (2004) J Biol Chem , vol.279 , pp. 15434-15440
    • Wang, P.1    Tortorella, M.2    England, K.3
  • 141
    • 33748741385 scopus 로고    scopus 로고
    • TIMP-3 inhibits the procollagen N-proteinase ADAMTS-2
    • Wang, W. M., Ge, G., Lim, N. H., Nagase, H., and Greenspan, D. S. (2006). TIMP-3 inhibits the procollagen N-proteinase ADAMTS-2. Biochem J 398, 515-519.
    • (2006) Biochem J , vol.398 , pp. 515-519
    • Wang, W.M.1    Ge, G.2    Lim, N.H.3    Nagase, H.4    Greenspan, D.S.5
  • 142
    • 51349143013 scopus 로고    scopus 로고
    • Type IV collagens regulate BMP signalling in Drosophila
    • Wang, X., Harris, R. E., Bayston, L. J., and Ashe, H. L. (2008). Type IV collagens regulate BMP signalling in Drosophila. Nature 455, 72-77.
    • (2008) Nature , vol.455 , pp. 72-77
    • Wang, X.1    Harris, R.E.2    Bayston, L.J.3    Ashe, H.L.4
  • 144
    • 0016785364 scopus 로고
    • Purification of rheumatoid synovial collagenase and its action on soluble and insoluble collagen
    • Woolley, D. E., Glanville, R. W., Crossley, M. J., and Evanson, J. M. (1975). Purification of rheumatoid synovial collagenase and its action on soluble and insoluble collagen. Eur J Biochem 54, 611-622.
    • (1975) Eur J Biochem , vol.54 , pp. 611-622
    • Woolley, D.E.1    Glanville, R.W.2    Crossley, M.J.3    Evanson, J.M.4
  • 145
    • 33644883338 scopus 로고    scopus 로고
    • Glycosaminoglycan-binding properties and aggrecanase activities of truncated ADAMTSs: Comparative analyses with ADAMTS-5, -9, -16 and -18
    • Zeng, W., Corcoran, C., Collins-Racie, L. A., LaVallie, E. R., Morris, E. A., and Flannery, C. R. (2006). Glycosaminoglycan-binding properties and aggrecanase activities of truncated ADAMTSs: comparative analyses with ADAMTS-5, -9, -16 and -18. Biochim Biophys Acta 1760, 517-524.
    • (2006) Biochim Biophys Acta , vol.1760 , pp. 517-524
    • Zeng, W.1    Corcoran, C.2    Collins-Racie, L.A.3    LaVallie, E.R.4    Morris, E.A.5    Flannery, C.R.6
  • 146
    • 0027964860 scopus 로고
    • Structural interaction of natural and synthetic inhibitors with the venom metalloproteinase, atrolysin C (form d)
    • Zhang, D., Botos, I., Gomis-Ruth, F. X., et al. (1994). Structural interaction of natural and synthetic inhibitors with the venom metalloproteinase, atrolysin C (form d). Proc Natl Acad Sci USA 91, 8447-8451.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 8447-8451
    • Zhang, D.1    Botos, I.2    Gomis-Ruth, F.X.3
  • 147
    • 67249086879 scopus 로고    scopus 로고
    • Structural specializations of A2, a force-sensing domain in the ultralarge vascular protein von Willebrand factor
    • Zhang, Q., Zhou, Y. F., Zhang, C. Z., Zhang, X., Lu, C., and Springer, T. A. (2009a). Structural specializations of A2, a force-sensing domain in the ultralarge vascular protein von Willebrand factor. Proc Natl Acad Sci U S A 106, 9226-9231.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 9226-9231
    • Zhang, Q.1    Zhou, Y.F.2    Zhang, C.Z.3    Zhang, X.4    Lu, C.5    Springer, T.A.6
  • 148
    • 0035798582 scopus 로고    scopus 로고
    • Structure of von Willebrand factor-cleaving protease (ADAMTS13), a metalloprotease involved in thrombotic thrombocytopenic purpura
    • Zheng, X., Chung, D., Takayama, T. K., Majerus, E. M., Sadler, J. E., and Fujikawa, K. (2001). Structure of von Willebrand factor-cleaving protease (ADAMTS13), a metalloprotease involved in thrombotic thrombocytopenic purpura. J Biol Chem 276, 41059-41063.
    • (2001) J Biol Chem , vol.276 , pp. 41059-41063
    • Zheng, X.1    Chung, D.2    Takayama, T.K.3    Majerus, E.M.4    Sadler, J.E.5    Fujikawa, K.6
  • 149
    • 0042530524 scopus 로고    scopus 로고
    • Cleavage of von Willebrand factor requires the spacer domain of the metalloprotease ADAMTS13
    • Zheng, X., Nishio, K., Majerus, E. M., and Sadler, J. E. (2003). Cleavage of von Willebrand factor requires the spacer domain of the metalloprotease ADAMTS13. J Biol Chem 278, 30136-30141.
    • (2003) J Biol Chem , vol.278 , pp. 30136-30141
    • Zheng, X.1    Nishio, K.2    Majerus, E.M.3    Sadler, J.E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.