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Volumn 430, Issue 1, 2010, Pages 87-95

Proteolytic processing of the serine protease matriptase-2: Identification of the cleavage sites required for its autocatalytic release from the cell surface

Author keywords

Autocatalysis; Cell surface shedding; Cleavage site determination; Matriptase 2; Proteolytic processing; Type II transmembrane serine protease (TTSP)

Indexed keywords

AUTOCATALYSIS; CELL SURFACE SHEDDING; CLEAVAGE SITE DETERMINATION; MATRIPTASE-2; PROTEOLYTIC PROCESSING; TYPE II TRANSMEMBRANE SERINE PROTEASE;

EID: 77955496853     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20091565     Document Type: Article
Times cited : (55)

References (51)
  • 1
    • 0037020169 scopus 로고    scopus 로고
    • Matriptase-2, a membrane-bound mosaic serine proteinase predominantly expressed in human liver and showing degrading activity against extracellular matrix proteins
    • Velasco, G., Cal, S., Quesada, V., Sánchez, L. M. and López-Otín, C. (2002) Matriptase-2, a membrane-bound mosaic serine proteinase predominantly expressed in human liver and showing degrading activity against extracellular matrix proteins. J. Biol. Chem. 277, 37637-37646
    • (2002) J. Biol. Chem. , vol.277 , pp. 37637-37646
    • Velasco, G.1    Cal, S.2    Quesada, V.3    Sánchez, L.M.4    López-Otín, C.5
  • 2
    • 0023850048 scopus 로고
    • A novel trypsin-like serine protease (hepsin) with a putative transmembrane domain expressed by human liver and hepatoma cells
    • Leytus, S. P., Loeb, K. R., Hagen, F. S., Kurachi, K. and Dayie, E. W. (1988) A novel trypsin-like serine protease (hepsin) with a putative transmembrane domain expressed by human liver and hepatoma cells. Biochemistry 27, 1067-1074
    • (1988) Biochemistry , vol.27 , pp. 1067-1074
    • Leytus, S.P.1    Loeb, K.R.2    Hagen, F.S.3    Kurachi, K.4    Dayie, E.W.5
  • 3
    • 0027474797 scopus 로고
    • Identification and characterization of a novel matrix-degrading protease from hormone-dependent human breast cancer cells
    • Shi, Y. E., Torri, J., Yieh, L., Wellstein, A., Lippman, M. E. and Dickson, R. B. (1993) Identification and characterization of a novel matrix-degrading protease from hormone-dependent human breast cancer cells. Cancer Res. 53, 1409-1415
    • (1993) Cancer Res. , vol.53 , pp. 1409-1415
    • Shi, Y.E.1    Torri, J.2    Yieh, L.3    Wellstein, A.4    Lippman, M.E.5    Dickson, R.B.6
  • 4
    • 0028903750 scopus 로고
    • cDNA sequence and chromosomal localization of human enterokinase, the proteolytic activator of trypsinogen
    • Kitamoto, Y., Veile, R. A., Donis-Keller, H. and Sadler, J. E. (1995) cDNA sequence and chromosomal localization of human enterokinase, the proteolytic activator of trypsinogen. Biochemistry 34, 4562-4568
    • (1995) Biochemistry , vol.34 , pp. 4562-4568
    • Kitamoto, Y.1    Veile, R.A.2    Donis-Keller, H.3    Sadler, J.E.4
  • 5
    • 0032496275 scopus 로고    scopus 로고
    • Cloning and characterization of the cDNA for human airway trypsin-like protease
    • Yamaoka, K., Masuda, K., Ogawa, H., Takagi, K., Umemoto, N. and Yasuoka, S. (1998) Cloning and characterization of the cDNA for human airway trypsin-like protease. J. Biol. Chem. 273, 11895-11901
    • (1998) J. Biol. Chem. , vol.273 , pp. 11895-11901
    • Yamaoka, K.1    Masuda, K.2    Ogawa, H.3    Takagi, K.4    Umemoto, N.5    Yasuoka, S.6
  • 6
    • 0033591253 scopus 로고    scopus 로고
    • Corin, a mosaic transmembrane serine protease encoded by a novel cDNA from human heart
    • Yan, W., Sheng, N., Seto, M., Morser, J. and Wu, Q. (1999) Corin, a mosaic transmembrane serine protease encoded by a novel cDNA from human heart. J. Biol. Chem. 274, 14926-14935
    • (1999) J. Biol. Chem. , vol.274 , pp. 14926-14935
    • Yan, W.1    Sheng, N.2    Seto, M.3    Morser, J.4    Wu, Q.5
  • 7
    • 0036510530 scopus 로고    scopus 로고
    • Spinesin/TMPRSS5, a novel transmembrane serine protease, cloned from human spinal cord
    • Yamaguchi, N., Okui, A., Yamada, T., Nakazaot, H. and Mitsui, S. (2002) Spinesin/TMPRSS5, a novel transmembrane serine protease, cloned from human spinal cord. J. Biol. Chem. 277, 6806-6812
    • (2002) J. Biol. Chem. , vol.277 , pp. 6806-6812
    • Yamaguchi, N.1    Okui, A.2    Yamada, T.3    Nakazaot, H.4    Mitsui, S.5
  • 8
    • 23944450595 scopus 로고    scopus 로고
    • Matriptase-3 is a novel phylogenetically preserved membrane-anchored serine protease with broad serpin reactivity
    • Szabo, R., Netzel-Arnett, S., Hobson, J. P., Antalis, T. M. and Bugge, T. H. (2005) Matriptase-3 is a novel phylogenetically preserved membrane-anchored serine protease with broad serpin reactivity. Biochem. J. 390, 231-242
    • (2005) Biochem. J. , vol.390 , pp. 231-242
    • Szabo, R.1    Netzel-Arnett, S.2    Hobson, J.P.3    Antalis, T.M.4    Bugge, T.H.5
  • 9
    • 0033603574 scopus 로고    scopus 로고
    • Molecular cloning of cDNA for matriptase, a matrix-degrading serine protease with trypsin-like activity
    • Lin, C. Y., Anders, J., Johnson, M., Sang, Q. A. and Dickson, R. B. (1999) Molecular cloning of cDNA for matriptase, a matrix-degrading serine protease with trypsin-like activity. J. Biol. Chem. 274, 18231-18236
    • (1999) J. Biol. Chem. , vol.274 , pp. 18231-18236
    • Lin, C.Y.1    Anders, J.2    Johnson, M.3    Sang, Q.A.4    Dickson, R.B.5
  • 10
    • 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., Tam, E. M., Kappelhoff, R., Connor, A., Ewart, T., Morrison, C. J., Puente, X., López-Otín, C. and Seth, A. (2004) Protease degradomics: mass spectrometry discovery of protease substrates and the CLIP-CHIP, a dedicated DNA microarray of all human proteases and inhibitors. Biol. Chem. 385, 493-504
    • (2004) Biol. Chem. , vol.385 , pp. 493-504
    • Overall, C.M.1    Tam, E.M.2    Kappelhoff, R.3    Connor, A.4    Ewart, T.5    Morrison, C.J.6    Puente, X.7    López-Otín, C.8    Seth, A.9
  • 11
    • 33846076709 scopus 로고    scopus 로고
    • Genetic reduction of matriptase-1 expression is associated with a reduction in the aggressive phenotype of prostate cancer cells in vitroand in vivo
    • Sanders, A. J., Parr, C., Davies, G., Martin, T. A., Lane, J., Mason, M. D. and Jiang, W. G. (2006) Genetic reduction of matriptase-1 expression is associated with a reduction in the aggressive phenotype of prostate cancer cells in vitroand in vivo. J. Exp. Ther. Oncol. 6, 39-48
    • (2006) J. Exp. Ther. Oncol. , vol.6 , pp. 39-48
    • Sanders, A.J.1    Parr, C.2    Davies, G.3    Martin, T.A.4    Lane, J.5    Mason, M.D.6    Jiang, W.G.7
  • 12
    • 34250777391 scopus 로고    scopus 로고
    • Matriptase-2 inhibits breast tumor growth and invasion and correlates with favorable prognosis for breast cancer patients
    • Parr, C., Sanders, A. J., Davies, G., Martin, T., Lane, J., Mason, M. D., Mansel, R. E. and Jiang, W. G. (2007) Matriptase-2 inhibits breast tumor growth and invasion and correlates with favorable prognosis for breast cancer patients. Clin. Cancer Res. 13, 3568-3576
    • (2007) Clin. Cancer Res. , vol.13 , pp. 3568-3576
    • Parr, C.1    Sanders, A.J.2    Davies, G.3    Martin, T.4    Lane, J.5    Mason, M.D.6    Mansel, R.E.7    Jiang, W.G.8
  • 13
    • 48749092358 scopus 로고    scopus 로고
    • Genetic upregulation of matriptase-2 reduces the aggressiveness of prostate cancer cells in vitroand in vivoand affects FAK and paxillin localisation
    • Sanders, A. J., Parr, C., Martin, T. A., Lane, J., Mason, M. D. and Jiang, W. G. (2008) Genetic upregulation of matriptase-2 reduces the aggressiveness of prostate cancer cells in vitroand in vivoand affects FAK and paxillin localisation. J. Cell. Physiol. 6, 780-789
    • (2008) J. Cell. Physiol. , vol.6 , pp. 780-789
    • Sanders, A.J.1    Parr, C.2    Martin, T.A.3    Lane, J.4    Mason, M.D.5    Jiang, W.G.6
  • 14
    • 0034711244 scopus 로고    scopus 로고
    • Activation of hepatocyte growth factor and urokinase/plasminogen activator by matriptase, an epithelial membrane serine protease
    • Lee, S. L., Dickson, R. B. and Lin, C. Y. (2000) Activation of hepatocyte growth factor and urokinase/plasminogen activator by matriptase, an epithelial membrane serine protease. J. Biol. Chem. 275, 36720-36725
    • (2000) J. Biol. Chem. , vol.275 , pp. 36720-36725
    • Lee, S.L.1    Dickson, R.B.2    Lin, C.Y.3
  • 15
    • 0034714379 scopus 로고    scopus 로고
    • Cellular localization of membrane-type serine protease 1 and identification of protease-activated receptor-2 and single-chain urokinase-type plasminogen activator as substrates
    • Takeuchi, T., Harris, J. L., Huang, W., Yan, K. W., Coughlin, S. R. and Craik, C. S. (2000) Cellular localization of membrane-type serine protease 1 and identification of protease-activated receptor-2 and single-chain urokinase-type plasminogen activator as substrates. J. Biol. Chem. 275, 26333-26342
    • (2000) J. Biol. Chem. , vol.275 , pp. 26333-26342
    • Takeuchi, T.1    Harris, J.L.2    Huang, W.3    Yan, K.W.4    Coughlin, S.R.5    Craik, C.S.6
  • 17
    • 33846072965 scopus 로고    scopus 로고
    • Matriptase and its putative role in cancer
    • Uhland, K. (2006) Matriptase and its putative role in cancer. Cell. Mol. Life Sci. 63, 2968-2978
    • (2006) Cell. Mol. Life Sci. , vol.63 , pp. 2968-2978
    • Uhland, K.1
  • 21
    • 56449096622 scopus 로고    scopus 로고
    • The serine protease matriptase-2 (TMPRSS6) inhibits hepcidin activation by cleaving membrane hemojuvelin
    • Silvestri, L., Pagani, A., Nai, A., De Domenico, I., Kaplan, J. and Camaschella, C. (2008) The serine protease matriptase-2 (TMPRSS6) inhibits hepcidin activation by cleaving membrane hemojuvelin. Cell Metabol. 8, 502-511
    • (2008) Cell Metabol. , vol.8 , pp. 502-511
    • Silvestri, L.1    Pagani, A.2    Nai, A.3    De Domenico, I.4    Kaplan, J.5    Camaschella, C.6
  • 22
    • 0035081038 scopus 로고    scopus 로고
    • Regulation of the activity of matriptase on epithelial cell surfaces by a blood-derived factor
    • Benaud, C., Dickson, R. B. and Lin, C. Y. (2001) Regulation of the activity of matriptase on epithelial cell surfaces by a blood-derived factor. Eur. J. Biochem. 168, 1439-1447
    • (2001) Eur. J. Biochem. , vol.168 , pp. 1439-1447
    • Benaud, C.1    Dickson, R.B.2    Lin, C.Y.3
  • 23
    • 0038035877 scopus 로고    scopus 로고
    • The activation of matriptase requires its noncatalytic domains, serine protease domain, and its cognate inhibitor
    • Oberst, M. D., Williams, C. A., Dickson, R. B., Johnson, M. D. and Lin, C. Y. (2003) The activation of matriptase requires its noncatalytic domains, serine protease domain, and its cognate inhibitor. J. Biol. Chem. 278, 26773-26779
    • (2003) J. Biol. Chem. , vol.278 , pp. 26773-26779
    • Oberst, M.D.1    Williams, C.A.2    Dickson, R.B.3    Johnson, M.D.4    Lin, C.Y.5
  • 25
    • 20544441281 scopus 로고    scopus 로고
    • Evidence for the occurrence of membrane-type serine protease 1/matriptase on the basolateral sides of enterocytes
    • Tsuzuki, S., Murai, N., Miyake, Y., Inouye, K., Hirayasu, H., Iwanaga, T. and Fushiki, T. (2005) Evidence for the occurrence of membrane-type serine protease 1/matriptase on the basolateral sides of enterocytes. Biochem. J. 388, 679-687
    • (2005) Biochem. J. , vol.388 , pp. 679-687
    • Tsuzuki, S.1    Murai, N.2    Miyake, Y.3    Inouye, K.4    Hirayasu, H.5    Iwanaga, T.6    Fushiki, T.7
  • 26
    • 33750614146 scopus 로고    scopus 로고
    • Initiation of plasminogen activation on the surface of monocytes expressing the type II transmembrane serine protease matriptase
    • Kilpatrick, L. M., Harris, R. L., Owen, K. A., Bass, R., Ghorayeb, C., Bar-Or, A. and Ellis, V. (2006) Initiation of plasminogen activation on the surface of monocytes expressing the type II transmembrane serine protease matriptase. Blood 108, 2616-2623
    • (2006) Blood , vol.108 , pp. 2616-2623
    • Kilpatrick, L.M.1    Harris, R.L.2    Owen, K.A.3    Bass, R.4    Ghorayeb, C.5    Bar-Or, A.6    Ellis, V.7
  • 27
    • 15444372149 scopus 로고    scopus 로고
    • Simultaneous activation and hepatocyte growth factor activator inhibitor 1-mediated inhibition of matriptase induced at activation foci in human mammary epithelial cells
    • Lee, M. S., Kiyomiya, K., Benaud, C., Dickson, R. B. and Lin, C. Y. (2005) Simultaneous activation and hepatocyte growth factor activator inhibitor 1-mediated inhibition of matriptase induced at activation foci in human mammary epithelial cells. Am. J. Physiol. Cell Physiol. 288, C932-C941
    • (2005) Am. J. Physiol. Cell Physiol. , vol.288
    • Lee, M.S.1    Kiyomiya, K.2    Benaud, C.3    Dickson, R.B.4    Lin, C.Y.5
  • 28
    • 0038463745 scopus 로고    scopus 로고
    • Type II transmembrane serine proteases
    • Wu, Q. (2003) Type II transmembrane serine proteases. Curr. Top. Dev. Biol. 54, 167-206
    • (2003) Curr. Top. Dev. Biol. , vol.54 , pp. 167-206
    • Wu, Q.1
  • 29
    • 43049128477 scopus 로고    scopus 로고
    • Type II transmembrane serine proteases in development and disease
    • Szabo, R. and Bugge, T. H. (2008) Type II transmembrane serine proteases in development and disease. Int. J. Biochem. Cell Biol. 40, 1297-1316
    • (2008) Int. J. Biochem. Cell Biol. , vol.40 , pp. 1297-1316
    • Szabo, R.1    Bugge, T.H.2
  • 30
    • 0035846933 scopus 로고    scopus 로고
    • Type II transmembrane serine proteases: Insights into an emerging class of cell surface proteolytic enzymes
    • Hooper, J. D., Clements, J. A., Quigley, J. P. and Antalis, T. M. (2001) Type II transmembrane serine proteases: insights into an emerging class of cell surface proteolytic enzymes. J. Biol. Chem. 276, 857-860
    • (2001) J. Biol. Chem. , vol.276 , pp. 857-860
    • Hooper, J.D.1    Clements, J.A.2    Quigley, J.P.3    Antalis, T.M.4
  • 31
    • 0033603547 scopus 로고    scopus 로고
    • Purification and characterization of a complex containing matriptase and a Kunitz-type serine protease inhibitor from human milk
    • Lin, C. Y., Anders, J., Johnson, M. and Dickson, R. B. (1999) Purification and characterization of a complex containing matriptase and a Kunitz-type serine protease inhibitor from human milk. J. Biol. Chem. 274, 18237-18242
    • (1999) J. Biol. Chem. , vol.274 , pp. 18237-18242
    • Lin, C.Y.1    Anders, J.2    Johnson, M.3    Dickson, R.B.4
  • 33
    • 70449467280 scopus 로고    scopus 로고
    • Haematologic data, iron parameters and molecular findings in two new cases of iron-refractory iron deficiency anaemia
    • Tchou, I., Diepold, M., Pilotto, P. A., Swinkels, D., Neerman-Arbez, M. and Beris, P. (2009) Haematologic data, iron parameters and molecular findings in two new cases of iron-refractory iron deficiency anaemia. Eur. J. Haematol. 83, 595-602
    • (2009) Eur. J. Haematol. , vol.83 , pp. 595-602
    • Tchou, I.1    Diepold, M.2    Pilotto, P.A.3    Swinkels, D.4    Neerman-Arbez, M.5    Beris, P.6
  • 36
    • 0017710978 scopus 로고
    • Characteristics of a human cell line transformed by DNA from human adenovirus type 5
    • Graham, F. L., Smiley, J., Russell, W. C. and Nairn, R. (1977) Characteristics of a human cell line transformed by DNA from human adenovirus type 5. J. Gen. Virol. 36, 59-74
    • (1977) J. Gen. Virol. , vol.36 , pp. 59-74
    • Graham, F.L.1    Smiley, J.2    Russell, W.C.3    Nairn, R.4
  • 37
    • 0022340978 scopus 로고
    • Isolation of monoclonal antibodies specific for human c-myc proto-oncogene product
    • Evan, G. I., Lewis, G. K., Ramsay, G. and Bishop, J. M. (1985) Isolation of monoclonal antibodies specific for human c-myc proto-oncogene product. Mol. Cell. Biol. 5, 3610-3616
    • (1985) Mol. Cell. Biol. , vol.5 , pp. 3610-3616
    • Evan, G.I.1    Lewis, G.K.2    Ramsay, G.3    Bishop, J.M.4
  • 38
    • 33746083974 scopus 로고    scopus 로고
    • Compatible solutes as protectants for zymogens against proteolysis
    • Kolp, S., Pietsch, M., Galinski, E. A. and Gütschow, M. (2006) Compatible solutes as protectants for zymogens against proteolysis. Biochim. Biophys. Acta 1764, 1234-1242
    • (2006) Biochim. Biophys. Acta , vol.1764 , pp. 1234-1242
    • Kolp, S.1    Pietsch, M.2    Galinski, E.A.3    Gütschow, M.4
  • 39
    • 63049086099 scopus 로고    scopus 로고
    • Probing the substrate specificities of matriptase, matriptase-2, hepsin and DESC1 with internally quenched fluorescent peptides
    • Béliveau, F., Désilets, A. and Leduc, R. (2009) Probing the substrate specificities of matriptase, matriptase-2, hepsin and DESC1 with internally quenched fluorescent peptides. FEBS J. 276, 2213-2226
    • (2009) FEBS J. , vol.276 , pp. 2213-2226
    • Béliveau, F.1    Désilets, A.2    Leduc, R.3
  • 40
    • 0041567036 scopus 로고    scopus 로고
    • Mouse matriptase-2: Identification, characterization and comparative mRNA expression analysis with mouse hepsin in adult and embryonic tissues
    • DOI 10.1042/BJ20030390
    • Hooper, J. D., Campagnolo, L., Goodarzi, G., Truong, T. N., Stuhlmann, H. and Quigley, J. P. (2003) Mouse matriptase-2: identification, characterization and comparative mRNA expression analysis with mouse hepsin in adult and embryonic tissues. Biochem. J. 373, 689-702 (Pubitemid 36981079)
    • (2003) Biochemical Journal , vol.373 , Issue.3 , pp. 689-702
    • Hooper, J.D.1    Campagnolo, L.2    Goodarzi, G.3    Truong, T.N.4    Stuhlmann, H.5    Quigley, J.P.6
  • 41
    • 57649183234 scopus 로고    scopus 로고
    • Potent inhibition and global co-localization implicate the transmembrane Kunitz-type serine protease inhibitor hepatocyte growth factor activator inhibitor-2 in the regulation of epithelial matriptase activity
    • Szabo, R., Hobson, J. P., List, K., Molinolo, A., Lin, C. Y. and Bugge, T. H. (2008) Potent inhibition and global co-localization implicate the transmembrane Kunitz-type serine protease inhibitor hepatocyte growth factor activator inhibitor-2 in the regulation of epithelial matriptase activity. J. Biol. Chem. 283, 29495-29504
    • (2008) J. Biol. Chem. , vol.283 , pp. 29495-29504
    • Szabo, R.1    Hobson, J.P.2    List, K.3    Molinolo, A.4    Lin, C.Y.5    Bugge, T.H.6
  • 44
    • 0033613123 scopus 로고    scopus 로고
    • Reverse biochemistry: Use of macromolecular protease inhibitors to dissect complex biological processes and identify a membrane-type serine protease in epithelial cancer and normal tissue
    • Takeuchi, T., Shuman, M. A. and Craik, C. S. (1999) Reverse biochemistry: use of macromolecular protease inhibitors to dissect complex biological processes and identify a membrane-type serine protease in epithelial cancer and normal tissue. Proc. Natl. Acad. Sci. U.S.A. 96, 11054-11061
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 11054-11061
    • Takeuchi, T.1    Shuman, M.A.2    Craik, C.S.3
  • 45
    • 0028111631 scopus 로고
    • Enterokinase, the initiator of intestinal digestion, is a mosaic protease composed of a distinctive assortment of domains
    • Kitamoto, Y., Yuan, X., Wu, Q., McCourt, D. W. and Sadler, J. E. (1994) Enterokinase, the initiator of intestinal digestion, is a mosaic protease composed of a distinctive assortment of domains. Proc. Natl. Acad. Sci. U.S.A. 91, 7588-7592
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 7588-7592
    • Kitamoto, Y.1    Yuan, X.2    Wu, Q.3    McCourt, D.W.4    Sadler, J.E.5
  • 46
    • 44849133938 scopus 로고    scopus 로고
    • Mutation G827R in matriptase causing autosomal recessive ichthyosis with hypotrichosis yields an inactive protease
    • Désilets, A., Béliveau, F., Vandal., G., McDuff, F. O., Lavigne, P. and Leduc, R. (2008) Mutation G827R in matriptase causing autosomal recessive ichthyosis with hypotrichosis yields an inactive protease. J. Biol. Chem. 283, 10535-10542
    • (2008) J. Biol. Chem. , vol.283 , pp. 10535-10542
    • Désilets, A.1    Béliveau, F.2    Vandal, G.3    McDuff, F.O.4    Lavigne, P.5    Leduc, R.6
  • 47
    • 68649110529 scopus 로고    scopus 로고
    • Activation of a membrane-bound serine protease matriptase on the cell surface
    • Miyake, Y., Yasumoto, M., Tsuzuki, S., Fushiki, T. and Inouye, K. (2009) Activation of a membrane-bound serine protease matriptase on the cell surface. J. Biochem. 146, 273-282
    • (2009) J. Biochem. , vol.146 , pp. 273-282
    • Miyake, Y.1    Yasumoto, M.2    Tsuzuki, S.3    Fushiki, T.4    Inouye, K.5
  • 48
    • 0015847599 scopus 로고
    • On the distribution of enterokinase in porcine intestine and on its subcellular localization
    • Louvard, D., Maroux, S., Baratti, J. and Desnuelle, P. (1973) On the distribution of enterokinase in porcine intestine and on its subcellular localization. Biochim. Biophys. Acta 309, 127-137
    • (1973) Biochim. Biophys. Acta , vol.309 , pp. 127-137
    • Louvard, D.1    Maroux, S.2    Baratti, J.3    Desnuelle, P.4
  • 49
    • 0021099291 scopus 로고
    • Incorporation of bovine enterokinase in reconstituted soybean phospholipid vesicles
    • Fonseca, P. and Light, A. (1983) Incorporation of bovine enterokinase in reconstituted soybean phospholipid vesicles. J. Biol. Chem. 258, 3069-3074
    • (1983) J. Biol. Chem. , vol.258 , pp. 3069-3074
    • Fonseca, P.1    Light, A.2
  • 51
    • 0346732305 scopus 로고    scopus 로고
    • Functional analysis of the transmembrane domain and activation cleavage of human corin: Design and characterization of a soluble corin
    • Knappe, S., Wu, F., Masikat, M. R., Morser, J. and Wu, Q. (2003) Functional analysis of the transmembrane domain and activation cleavage of human corin: design and characterization of a soluble corin. J. Biol. Chem. 278, 52363-52370
    • (2003) J. Biol. Chem. , vol.278 , pp. 52363-52370
    • Knappe, S.1    Wu, F.2    Masikat, M.R.3    Morser, J.4    Wu, Q.5


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