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Volumn 40, Issue 6-7, 2008, Pages 1297-1316

Type II transmembrane serine proteases in development and disease

Author keywords

Cancer; Cell surface proteolysis; Mammalian development

Indexed keywords

CELL SURFACE PROTEIN; CORIN PROTEASE; ENTEROPEPTIDASE; HEPSIN; HUMAN AIRWAY TRYPSIN LIKE PROTEASE; MATRIPTASE; PROTEINASE; SCATTER FACTOR; SERINE PROTEINASE; TYPE II TRANSMEMBRANE SERINE PROTEASE;

EID: 43049128477     PISSN: 13572725     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biocel.2007.11.013     Document Type: Review
Times cited : (164)

References (181)
  • 1
    • 0035866379 scopus 로고    scopus 로고
    • Catalytic cleavage of the androgen regulated TMPRSS2 protease results in its secretion by prostate and prostate cancer epithelia
    • Afar D.E.H., Vivanco I., Hubert R.S., Kuo J., Chen E., Saffran D.C., et al. Catalytic cleavage of the androgen regulated TMPRSS2 protease results in its secretion by prostate and prostate cancer epithelia. Cancer Research 61 (2001) 1686-1692
    • (2001) Cancer Research , vol.61 , pp. 1686-1692
    • Afar, D.E.H.1    Vivanco, I.2    Hubert, R.S.3    Kuo, J.4    Chen, E.5    Saffran, D.C.6
  • 2
    • 26444617226 scopus 로고    scopus 로고
    • Characterization of a new full length TMPRSS3 isoform and identification of mutant alleles responsible for nonsyndromic recessive deafness in Newfoundland and Pakistan
    • Ahmed Z.M., Li X.C., Powell S.D., Riazuddin S., Young T.L., Ramzan K., et al. Characterization of a new full length TMPRSS3 isoform and identification of mutant alleles responsible for nonsyndromic recessive deafness in Newfoundland and Pakistan. BMC Medical Genetics 5 (2004) 24
    • (2004) BMC Medical Genetics , vol.5 , pp. 24
    • Ahmed, Z.M.1    Li, X.C.2    Powell, S.D.3    Riazuddin, S.4    Young, T.L.5    Ramzan, K.6
  • 4
    • 33645465530 scopus 로고    scopus 로고
    • Activation of epithelial sodium channels by mouse channel activating proteases (mCAP) expressed in Xenopus oocytes requires catalytic activity of mCAP3 and mCAP2 but not mCAP1
    • Andreasen D., Vuagniaux G., Fowler-Jaeger N., Hummler E., and Rossier B.C. Activation of epithelial sodium channels by mouse channel activating proteases (mCAP) expressed in Xenopus oocytes requires catalytic activity of mCAP3 and mCAP2 but not mCAP1. Journal of the American Society of Nephrology 17 (2006) 968-976
    • (2006) Journal of the American Society of Nephrology , vol.17 , pp. 968-976
    • Andreasen, D.1    Vuagniaux, G.2    Fowler-Jaeger, N.3    Hummler, E.4    Rossier, B.C.5
  • 5
    • 33847225554 scopus 로고    scopus 로고
    • Autosomal recessive ichthyosis with hypotrichosis caused by a mutation in ST14, encoding type II transmembrane serine protease matriptase
    • Basel-Vanagaite L., Attia R., Ishida-Yamamoto A., Rainshtein L., Ben Amitai D., Lurie R., et al. Autosomal recessive ichthyosis with hypotrichosis caused by a mutation in ST14, encoding type II transmembrane serine protease matriptase. American Journal of Human Genetics 80 (2007) 467-477
    • (2007) American Journal of Human Genetics , vol.80 , pp. 467-477
    • Basel-Vanagaite, L.1    Attia, R.2    Ishida-Yamamoto, A.3    Rainshtein, L.4    Ben Amitai, D.5    Lurie, R.6
  • 7
    • 11244259136 scopus 로고    scopus 로고
    • Molecular cloning and characterisation of DESC4, a new transmembrane serine protease
    • Behrens M., Bufe B., Schmale H., and Meyerhof W. Molecular cloning and characterisation of DESC4, a new transmembrane serine protease. Cellular and Molecular Life Sciences 61 (2004) 2866-2877
    • (2004) Cellular and Molecular Life Sciences , vol.61 , pp. 2866-2877
    • Behrens, M.1    Bufe, B.2    Schmale, H.3    Meyerhof, W.4
  • 9
    • 34147123126 scopus 로고    scopus 로고
    • Clinical relevance of hepsin and hepatocyte growth factor activator inhibitor type 2 expression in renal cell carcinoma
    • Betsunoh H., Mukai S., Akiyama Y., Fukushima T., Minamiguchi N., Hasui Y., et al. Clinical relevance of hepsin and hepatocyte growth factor activator inhibitor type 2 expression in renal cell carcinoma. Cancer Science 98 (2007) 491-498
    • (2007) Cancer Science , vol.98 , pp. 491-498
    • Betsunoh, H.1    Mukai, S.2    Akiyama, Y.3    Fukushima, T.4    Minamiguchi, N.5    Hasui, Y.6
  • 12
    • 0035967874 scopus 로고    scopus 로고
    • Characterization of a serine protease that cleaves pro-gamma-melanotropin at the adrenal to stimulate growth
    • Bicknell A.B., Lomthaisong K., Woods R.J., Hutchinson E.G., Bennett H.P.J., Gladwell R.T., et al. Characterization of a serine protease that cleaves pro-gamma-melanotropin at the adrenal to stimulate growth. Cell 105 (2001) 903-912
    • (2001) Cell , vol.105 , pp. 903-912
    • Bicknell, A.B.1    Lomthaisong, K.2    Woods, R.J.3    Hutchinson, E.G.4    Bennett, H.P.J.5    Gladwell, R.T.6
  • 14
    • 33748950305 scopus 로고    scopus 로고
    • Proteolytic activation of influenza viruses by serine proteases TMPRSS2 and HAT from human airway epithelium
    • Bottcher E., Matrosovich T., Beyerle M., Klenk H.D., Garten W., and Matrosovich M. Proteolytic activation of influenza viruses by serine proteases TMPRSS2 and HAT from human airway epithelium. Journal of Virology 80 (2006) 9896-9898
    • (2006) Journal of Virology , vol.80 , pp. 9896-9898
    • Bottcher, E.1    Matrosovich, T.2    Beyerle, M.3    Klenk, H.D.4    Garten, W.5    Matrosovich, M.6
  • 15
    • 33645800829 scopus 로고    scopus 로고
    • Identification and characterization of human polyserase-3, a novel protein with tandem serine-protease domains in the same polypeptide chain
    • Cal S., Peinado J.R., Llamazares M., Quesada V., Moncada-Pazos A., Garabaya C., et al. Identification and characterization of human polyserase-3, a novel protein with tandem serine-protease domains in the same polypeptide chain. BMC Biochemistry 7 (2006) 9
    • (2006) BMC Biochemistry , vol.7 , pp. 9
    • Cal, S.1    Peinado, J.R.2    Llamazares, M.3    Quesada, V.4    Moncada-Pazos, A.5    Garabaya, C.6
  • 18
    • 33644831171 scopus 로고    scopus 로고
    • Cluster analysis of S100 gene expression and genes correlating to psoriasin (S100A7) expression at different stages of breast cancer development
    • Carlsson H., Petersson S., and Enerback C. Cluster analysis of S100 gene expression and genes correlating to psoriasin (S100A7) expression at different stages of breast cancer development. International Journal of Oncology 27 (2005) 1473-1481
    • (2005) International Journal of Oncology , vol.27 , pp. 1473-1481
    • Carlsson, H.1    Petersson, S.2    Enerback, C.3
  • 19
    • 35648960787 scopus 로고    scopus 로고
    • Inactivation of serine protease Matriptase1a by its inhibitor Hai1 is required for epithelial integrity of the zebrafish epidermis
    • Carney T.J., Von Der Hardt S., Sonntag C., Amsterdam A., Topczewski J., Hopkins N., et al. Inactivation of serine protease Matriptase1a by its inhibitor Hai1 is required for epithelial integrity of the zebrafish epidermis. Development 134 (2007) 3461-3471
    • (2007) Development , vol.134 , pp. 3461-3471
    • Carney, T.J.1    Von Der Hardt, S.2    Sonntag, C.3    Amsterdam, A.4    Topczewski, J.5    Hopkins, N.6
  • 21
    • 13344295074 scopus 로고    scopus 로고
    • Mutations in subunits of the epithelial sodium channel cause salt wasting with hyperkalaemic acidosis, pseudohypoaldosteronism type 1
    • Chang S.S., Grunder S., Hanukoglu A., Rosler A., Mathew P.M., Hanukoglu I., et al. Mutations in subunits of the epithelial sodium channel cause salt wasting with hyperkalaemic acidosis, pseudohypoaldosteronism type 1. Nature Genetics 12 (1996) 248-253
    • (1996) Nature Genetics , vol.12 , pp. 248-253
    • Chang, S.S.1    Grunder, S.2    Hanukoglu, A.3    Rosler, A.4    Mathew, P.M.5    Hanukoglu, I.6
  • 23
    • 0037376293 scopus 로고    scopus 로고
    • Hepsin and maspin are inversely expressed in laser capture microdissectioned prostate cancer
    • Chen Z.X., Fan Z.B., Mcneal J.E., Nolley R., Caldwell M.C., Mahadevappa M., et al. Hepsin and maspin are inversely expressed in laser capture microdissectioned prostate cancer. Journal of Urology 169 (2003) 1316-1319
    • (2003) Journal of Urology , vol.169 , pp. 1316-1319
    • Chen, Z.X.1    Fan, Z.B.2    Mcneal, J.E.3    Nolley, R.4    Caldwell, M.C.5    Mahadevappa, M.6
  • 24
    • 0035976996 scopus 로고    scopus 로고
    • N-terminal processing is essential for release of epithin, a mouse type II membrane serine protease
    • Cho E.G., Kim M.G., Kim C., Kim S.R., Seong I.S., Chung C., et al. N-terminal processing is essential for release of epithin, a mouse type II membrane serine protease. Journal of Biological Chemistry 276 (2001) 44581-44589
    • (2001) Journal of Biological Chemistry , vol.276 , pp. 44581-44589
    • Cho, E.G.1    Kim, M.G.2    Kim, C.3    Kim, S.R.4    Seong, I.S.5    Chung, C.6
  • 27
    • 27144449108 scopus 로고    scopus 로고
    • Corin gene minor allele defined by 2 missense mutations is common in blacks and associated with high blood pressure and hypertension
    • Dries D.L., Victor R.G., Rame J.E., Cooper R.S., Wu X.D., Zhu X.F., et al. Corin gene minor allele defined by 2 missense mutations is common in blacks and associated with high blood pressure and hypertension. Circulation 112 (2005) 2403-2410
    • (2005) Circulation , vol.112 , pp. 2403-2410
    • Dries, D.L.1    Victor, R.G.2    Rame, J.E.3    Cooper, R.S.4    Wu, X.D.5    Zhu, X.F.6
  • 29
    • 34250807826 scopus 로고    scopus 로고
    • Autosomal recessive postlingual hearing loss (DFNB8): Compound heterozygosity for two novel TMPRSS3 mutations in German siblings
    • Elbracht M., Senderek J., Eggermann T., Thurmer C., Park J., Westhofen M., et al. Autosomal recessive postlingual hearing loss (DFNB8): Compound heterozygosity for two novel TMPRSS3 mutations in German siblings. Journal of Medical Genetics 44 (2007) e81
    • (2007) Journal of Medical Genetics , vol.44
    • Elbracht, M.1    Senderek, J.2    Eggermann, T.3    Thurmer, C.4    Park, J.5    Westhofen, M.6
  • 30
    • 0025821769 scopus 로고
    • Epidermal barrier function-Intercellular lamellar lipid structures, origin, composition and metabolism
    • Elias P.M. Epidermal barrier function-Intercellular lamellar lipid structures, origin, composition and metabolism. Journal of Controlled Release 15 (1991) 199-208
    • (1991) Journal of Controlled Release , vol.15 , pp. 199-208
    • Elias, P.M.1
  • 32
    • 33846917477 scopus 로고    scopus 로고
    • Hepatocyte growth factor activator inhibitor-1 (HAI-1) is essential for the integrity of basement membranes in the developing placental labyrinth
    • Fan B., Brennan J., Grant D., Peale F., Rangell L., and Kirchhofer D. Hepatocyte growth factor activator inhibitor-1 (HAI-1) is essential for the integrity of basement membranes in the developing placental labyrinth. Developmental Biology 303 (2007) 222-230
    • (2007) Developmental Biology , vol.303 , pp. 222-230
    • Fan, B.1    Brennan, J.2    Grant, D.3    Peale, F.4    Rangell, L.5    Kirchhofer, D.6
  • 33
    • 0021100321 scopus 로고
    • The purification and characterization of bovine enterokinase from membrane fragments in the duodenal mucosal fluid
    • Fonseca P., and Light A. The purification and characterization of bovine enterokinase from membrane fragments in the duodenal mucosal fluid. Journal of Biological Chemistry 258 (1983) 14516-14520
    • (1983) Journal of Biological Chemistry , vol.258 , pp. 14516-14520
    • Fonseca, P.1    Light, A.2
  • 34
    • 33646347137 scopus 로고    scopus 로고
    • Protein interaction analysis of ST14 domains and their point and deletion mutants
    • Ge W.T., Hu H.G., Ding K.F., Sun L.F., and Zheng S. Protein interaction analysis of ST14 domains and their point and deletion mutants. Journal of Biological Chemistry 281 (2006) 7406-7412
    • (2006) Journal of Biological Chemistry , vol.281 , pp. 7406-7412
    • Ge, W.T.1    Hu, H.G.2    Ding, K.F.3    Sun, L.F.4    Zheng, S.5
  • 36
    • 0022896194 scopus 로고
    • Acute necrotising pancreatitis-A role for enterokinase
    • Grant D. Acute necrotising pancreatitis-A role for enterokinase. International Journal of Pancreatology 1 (1986) 167-183
    • (1986) International Journal of Pancreatology , vol.1 , pp. 167-183
    • Grant, D.1
  • 38
    • 34548321253 scopus 로고    scopus 로고
    • Mice deficient for the type II transmembrane serine protease, TMPRSS1/hepsin, exhibit profound hearing loss
    • Guipponi M., Tan J., Cannon P.Z., Donley L., Crewther P., Clarke M., et al. Mice deficient for the type II transmembrane serine protease, TMPRSS1/hepsin, exhibit profound hearing loss. American Journal of Pathology 171 (2007) 608-616
    • (2007) American Journal of Pathology , vol.171 , pp. 608-616
    • Guipponi, M.1    Tan, J.2    Cannon, P.Z.3    Donley, L.4    Crewther, P.5    Clarke, M.6
  • 39
    • 0036849378 scopus 로고    scopus 로고
    • The transmembrane serine protease (TMPRSS3) mutated in deafness DFNB8/10 activates the epithelial sodium channel (ENaC) in vitro
    • Guipponi M., Vuagniaux G., Wattenhofer M., Shibuya K., Vazquez M., Dougherty L., et al. The transmembrane serine protease (TMPRSS3) mutated in deafness DFNB8/10 activates the epithelial sodium channel (ENaC) in vitro. Human Molecular Genetics 11 (2002) 2829-2836
    • (2002) Human Molecular Genetics , vol.11 , pp. 2829-2836
    • Guipponi, M.1    Vuagniaux, G.2    Wattenhofer, M.3    Shibuya, K.4    Vazquez, M.5    Dougherty, L.6
  • 40
    • 13244252559 scopus 로고    scopus 로고
    • Evidence against a role of human airway trypsin-like protease - The human analogue of the growth-promoting rat adrenal secretory protease - In adrenal tumourigenesis
    • Hahner S., Fassnacht M., Hammer F., Schammann M., Weismann D., Hansen I.A., et al. Evidence against a role of human airway trypsin-like protease - The human analogue of the growth-promoting rat adrenal secretory protease - In adrenal tumourigenesis. European Journal of Endocrinology 152 (2005) 143-153
    • (2005) European Journal of Endocrinology , vol.152 , pp. 143-153
    • Hahner, S.1    Fassnacht, M.2    Hammer, F.3    Schammann, M.4    Weismann, D.5    Hansen, I.A.6
  • 41
    • 1642423649 scopus 로고    scopus 로고
    • The adrenal secretory serine protease AsP is a short secretory isoform of the transmembrane airway trypsin-like protease
    • Hansen I.A., Fassnacht M., Hahner S., Hammer F., Schammann M., Meyer S.R., et al. The adrenal secretory serine protease AsP is a short secretory isoform of the transmembrane airway trypsin-like protease. Endocrinology 145 (2004) 1898-1905
    • (2004) Endocrinology , vol.145 , pp. 1898-1905
    • Hansen, I.A.1    Fassnacht, M.2    Hahner, S.3    Hammer, F.4    Schammann, M.5    Meyer, S.R.6
  • 42
    • 33645053497 scopus 로고    scopus 로고
    • Refinement of the 22q12-q13 breast cancer-associated region: Evidence of TMPRSS6 as a candidate gene in an eastern Finnish population
    • Hartikainen J.M., Tuhkanen H., Kataja V., Eskelinen M., Uusitupa M., Kosma V.M., et al. Refinement of the 22q12-q13 breast cancer-associated region: Evidence of TMPRSS6 as a candidate gene in an eastern Finnish population. Clinical Cancer Research 12 (2006) 1454-1462
    • (2006) Clinical Cancer Research , vol.12 , pp. 1454-1462
    • Hartikainen, J.M.1    Tuhkanen, H.2    Kataja, V.3    Eskelinen, M.4    Uusitupa, M.5    Kosma, V.M.6
  • 43
    • 0016691190 scopus 로고
    • Intestinal enterokinase deficiency-Occurrence in 2 sibs and age dependency of clinical expression
    • Haworth J.C., Hadorn B., Gourley B., Prasad A., and Troesch V. Intestinal enterokinase deficiency-Occurrence in 2 sibs and age dependency of clinical expression. Archives of Disease in Childhood 50 (1975) 277-282
    • (1975) Archives of Disease in Childhood , vol.50 , pp. 277-282
    • Haworth, J.C.1    Hadorn, B.2    Gourley, B.3    Prasad, A.4    Troesch, V.5
  • 45
    • 0037477788 scopus 로고    scopus 로고
    • Mice with targeted disruption of the fatty acid transport protein 4 (Fatp 4, SlC27a4) gene show features of lethal restrictive dermopathy
    • Herrmann T., Van Der Hoeven F., Grone H.J., Stewart A.F., Langbein L., Kaiser I., et al. Mice with targeted disruption of the fatty acid transport protein 4 (Fatp 4, SlC27a4) gene show features of lethal restrictive dermopathy. Journal of Cell Biology 161 (2003) 1105-1115
    • (2003) Journal of Cell Biology , vol.161 , pp. 1105-1115
    • Herrmann, T.1    Van Der Hoeven, F.2    Grone, H.J.3    Stewart, A.F.4    Langbein, L.5    Kaiser, I.6
  • 46
    • 21244448682 scopus 로고    scopus 로고
    • Hepatocyte growth factor is a preferred in vitro substrate for human hepsin, a membrane-anchored serine protease implicated in prostate and ovarian cancers
    • Herter S., Piper D.E., Aaron W., Gabriele T., Cutler G., Cao P., et al. Hepatocyte growth factor is a preferred in vitro substrate for human hepsin, a membrane-anchored serine protease implicated in prostate and ovarian cancers. Biochemical Journal 390 (2005) 125-136
    • (2005) Biochemical Journal , vol.390 , pp. 125-136
    • Herter, S.1    Piper, D.E.2    Aaron, W.3    Gabriele, T.4    Cutler, G.5    Cao, P.6
  • 47
    • 2442432225 scopus 로고    scopus 로고
    • Gene expression profiling identifies matriptase overexpression in malignant mesothelioma
    • Hoang C.D., D'cunha J., Kratzke M.G., Casmey C.E., Frizelle S.P., Maddaus M.A., et al. Gene expression profiling identifies matriptase overexpression in malignant mesothelioma. Chest 125 (2004) 1843-1852
    • (2004) Chest , vol.125 , pp. 1843-1852
    • Hoang, C.D.1    D'cunha, J.2    Kratzke, M.G.3    Casmey, C.E.4    Frizelle, S.P.5    Maddaus, M.A.6
  • 48
    • 8744227027 scopus 로고    scopus 로고
    • Mouse DESC1 is located within a cluster of seven DESC1-like genes and encodes a type II transmembrane serine protease that forms serpin inhibitory complexes
    • Hobson J.P., Netzel-Arnett S., Szabo R., Rehault S.M., Church F.C., Strickland D.K., et al. Mouse DESC1 is located within a cluster of seven DESC1-like genes and encodes a type II transmembrane serine protease that forms serpin inhibitory complexes. Journal of Biological Chemistry 279 (2004) 46981-46994
    • (2004) Journal of Biological Chemistry , vol.279 , pp. 46981-46994
    • Hobson, J.P.1    Netzel-Arnett, S.2    Szabo, R.3    Rehault, S.M.4    Church, F.C.5    Strickland, D.K.6
  • 50
    • 0041567036 scopus 로고    scopus 로고
    • Mouse matriptase-2: Identification, characterization and comparative mRNA expression analysis with mouse hepsin in adult and embryonic tissues
    • Hooper J.D., Campagnolo L., Goodarzi G., Truong T.N., Stuhlmann H., and Quigley J.P. Mouse matriptase-2: Identification, characterization and comparative mRNA expression analysis with mouse hepsin in adult and embryonic tissues. Biochemical Journal 373 (2003) 689-702
    • (2003) Biochemical Journal , vol.373 , pp. 689-702
    • Hooper, J.D.1    Campagnolo, L.2    Goodarzi, G.3    Truong, T.N.4    Stuhlmann, H.5    Quigley, J.P.6
  • 51
    • 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. Type II transmembrane serine proteases-Insights into an emerging class of cell surface proteolytic enzymes. Journal of Biological Chemistry 276 (2001) 857-860
    • (2001) Journal of Biological Chemistry , vol.276 , pp. 857-860
    • Hooper, J.D.1    Clements, J.A.2    Quigley, J.P.3    Antalis, T.M.4
  • 54
    • 0344925815 scopus 로고    scopus 로고
    • Expression of enteropeptidase in differentiated enterocytes, goblet cells, and the tumor cells in human duodenum
    • Imamura T., and Kitamoto Y. Expression of enteropeptidase in differentiated enterocytes, goblet cells, and the tumor cells in human duodenum. American Journal of Physiology-Gastrointestinal and Liver Physiology 285 (2003) G1235-G1241
    • (2003) American Journal of Physiology-Gastrointestinal and Liver Physiology , vol.285
    • Imamura, T.1    Kitamoto, Y.2
  • 58
    • 0029347803 scopus 로고
    • Mucosal enterokinase activity in cow's milk protein sensitive enteropathy
    • Iyngkaran N., Yadav M., and Boey C.G. Mucosal enterokinase activity in cow's milk protein sensitive enteropathy. Singapore Medical Journal 36 (1995) 393-396
    • (1995) Singapore Medical Journal , vol.36 , pp. 393-396
    • Iyngkaran, N.1    Yadav, M.2    Boey, C.G.3
  • 59
    • 0033970075 scopus 로고    scopus 로고
    • Cloning, genomic organization, chromosomal assignment and expression of a novel mosaic serine proteinase: Epitheliasin
    • Jacquinet E., Rao N.V., Rao G.V., and Hoidal J.R. Cloning, genomic organization, chromosomal assignment and expression of a novel mosaic serine proteinase: Epitheliasin. FEBS Letters 468 (2000) 93-100
    • (2000) FEBS Letters , vol.468 , pp. 93-100
    • Jacquinet, E.1    Rao, N.V.2    Rao, G.V.3    Hoidal, J.R.4
  • 61
    • 33846325108 scopus 로고    scopus 로고
    • Expression of the serine protease, matriptase, in breast ductal carcinoma of Chinese women: Correlation with clinicopathological parameters
    • Jin J.S., Cheng T.F., Tsai W.C., Sheu L.F., Chiang H., and Yu C.P. Expression of the serine protease, matriptase, in breast ductal carcinoma of Chinese women: Correlation with clinicopathological parameters. Histology and Histopathology 22 (2007) 305-309
    • (2007) Histology and Histopathology , vol.22 , pp. 305-309
    • Jin, J.S.1    Cheng, T.F.2    Tsai, W.C.3    Sheu, L.F.4    Chiang, H.5    Yu, C.P.6
  • 62
    • 33244487758 scopus 로고    scopus 로고
    • Increasing expression of serine protease matriptase in ovarian tumors: Tissue microarray analysis of immunostaining score with clinicopathological parameters
    • Jin J.S., Hsieh D.S., Loh S.H., Chen A., Yao C.W., and Yen C.Y. Increasing expression of serine protease matriptase in ovarian tumors: Tissue microarray analysis of immunostaining score with clinicopathological parameters. Modern Pathology 19 (2006) 447-452
    • (2006) Modern Pathology , vol.19 , pp. 447-452
    • Jin, J.S.1    Hsieh, D.S.2    Loh, S.H.3    Chen, A.4    Yao, C.W.5    Yen, C.Y.6
  • 63
    • 18244388249 scopus 로고    scopus 로고
    • Lipoxygenase-3 (ALOXE3) and 12(R)-lipoxygenase (ALOX12B) are mutated in non-bullous congenital ichthyosiform erythroderma (NCIE) linked to chromosome 17p13.1
    • Jobard F., Lefevre C., Karaduman A., Blanchet-Bardon C., Emre S., Weissenbach J., et al. Lipoxygenase-3 (ALOXE3) and 12(R)-lipoxygenase (ALOX12B) are mutated in non-bullous congenital ichthyosiform erythroderma (NCIE) linked to chromosome 17p13.1. Human Molecular Genetics 11 (2002) 107-113
    • (2002) Human Molecular Genetics , vol.11 , pp. 107-113
    • Jobard, F.1    Lefevre, C.2    Karaduman, A.3    Blanchet-Bardon, C.4    Emre, S.5    Weissenbach, J.6
  • 64
    • 0037374303 scopus 로고    scopus 로고
    • Tissue microarray analysis of hepatocyte growth factor/Met pathway components reveals a role for Met, matriptase, and hepatocyte growth factor activator inhibitor 1 in the progression of node-negative breast cancer
    • Kang J.Y., Dolled-Filhart M., Ocal I.T., Singh B., Lin C.Y., Dickson R.B., et al. Tissue microarray analysis of hepatocyte growth factor/Met pathway components reveals a role for Met, matriptase, and hepatocyte growth factor activator inhibitor 1 in the progression of node-negative breast cancer. Cancer Research 63 (2003) 1101-1105
    • (2003) Cancer Research , vol.63 , pp. 1101-1105
    • Kang, J.Y.1    Dolled-Filhart, M.2    Ocal, I.T.3    Singh, B.4    Lin, C.Y.5    Dickson, R.B.6
  • 65
    • 0028804679 scopus 로고
    • Hepsin, a putative membrane-associated serine-protease, activates human factor-VII and initiates a pathway of blood-coagulation on the cell-surface leading to thrombin formation
    • Kazama Y., Hamamoto T., Foster D.C., and Kisiel W. Hepsin, a putative membrane-associated serine-protease, activates human factor-VII and initiates a pathway of blood-coagulation on the cell-surface leading to thrombin formation. Journal of Biological Chemistry 270 (1995) 66-72
    • (1995) Journal of Biological Chemistry , vol.270 , pp. 66-72
    • Kazama, Y.1    Hamamoto, T.2    Foster, D.C.3    Kisiel, W.4
  • 66
    • 24944513216 scopus 로고    scopus 로고
    • ECM1 and TMPRSS4 are diagnostic markers of malignant thyroid neoplasms and improve the accuracy of fine needle aspiration biopsy
    • Kebebew E., Peng M., Reiff E., Duh Q.Y., Clark O.H., and Mcmillan A. ECM1 and TMPRSS4 are diagnostic markers of malignant thyroid neoplasms and improve the accuracy of fine needle aspiration biopsy. Annals of Surgery 242 (2005) 353-363
    • (2005) Annals of Surgery , vol.242 , pp. 353-363
    • Kebebew, E.1    Peng, M.2    Reiff, E.3    Duh, Q.Y.4    Clark, O.H.5    Mcmillan, A.6
  • 67
    • 33745186955 scopus 로고    scopus 로고
    • Diagnostic and extent of disease multigene assay for malignant thyroid neoplasms
    • Kebebew E., Peng M., Reiff E., and Mcmillan A. Diagnostic and extent of disease multigene assay for malignant thyroid neoplasms. Cancer 106 (2006) 2592-2597
    • (2006) Cancer , vol.106 , pp. 2592-2597
    • Kebebew, E.1    Peng, M.2    Reiff, E.3    Mcmillan, A.4
  • 69
    • 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., et al. Initiation of plasminogen activation on the surface of monocytes expressing the type II transmembrane serine protease matriptase. Blood 108 (2006) 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
  • 70
    • 0035911646 scopus 로고    scopus 로고
    • Cloning and expression of novel mosaic serine proteases with and without a transmembrane domain from human lung
    • Kim D.R., Sharmin S., Inoue M., and Kido H. Cloning and expression of novel mosaic serine proteases with and without a transmembrane domain from human lung. Biochimica Et Biophysica Acta-Gene Structure and Expression 1518 (2001) 204-209
    • (2001) Biochimica Et Biophysica Acta-Gene Structure and Expression , vol.1518 , pp. 204-209
    • Kim, D.R.1    Sharmin, S.2    Inoue, M.3    Kido, H.4
  • 71
    • 0032923230 scopus 로고    scopus 로고
    • Cloning and chromosomal mapping of a gene isolated from thymic stromal cells encoding a new mouse type II membrane serine protease, epithin, containing four LDL receptor modules and two CUB domains
    • Kim M.G., Chen C., Lyu M.S., Cho E.G., Park D., Kozak C., et al. Cloning and chromosomal mapping of a gene isolated from thymic stromal cells encoding a new mouse type II membrane serine protease, epithin, containing four LDL receptor modules and two CUB domains. Immunogenetics 49 (1999) 420-428
    • (1999) Immunogenetics , vol.49 , pp. 420-428
    • Kim, M.G.1    Chen, C.2    Lyu, M.S.3    Cho, E.G.4    Park, D.5    Kozak, C.6
  • 73
    • 0141815667 scopus 로고    scopus 로고
    • Tissue expression, protease specificity, and Kunitz domain functions of hepatocyte growth factor activator Inhibitor-1B (HAI-1B), a new splice variant of HAI-1
    • Kirchhofer D., Peek M., Li W., Stamos J., Eigenbrot C., Kadkhodayan S., et al. Tissue expression, protease specificity, and Kunitz domain functions of hepatocyte growth factor activator Inhibitor-1B (HAI-1B), a new splice variant of HAI-1. Journal of Biological Chemistry 278 (2003) 36341-36349
    • (2003) Journal of Biological Chemistry , vol.278 , pp. 36341-36349
    • Kirchhofer, D.1    Peek, M.2    Li, W.3    Stamos, J.4    Eigenbrot, C.5    Kadkhodayan, S.6
  • 74
    • 15544386767 scopus 로고    scopus 로고
    • Hepsin activates pro-hepatocyte growth factor and is inhibited by hepatocyte growth factor activator inhibitor-1B (HAI-1B) and HAI-2
    • Kirchhofer D., Peek M., Lipari M.T., Billeci K., Fan B., and Moran P. Hepsin activates pro-hepatocyte growth factor and is inhibited by hepatocyte growth factor activator inhibitor-1B (HAI-1B) and HAI-2. FEBS Letters 579 (2005) 1945-1950
    • (2005) FEBS Letters , vol.579 , pp. 1945-1950
    • Kirchhofer, D.1    Peek, M.2    Lipari, M.T.3    Billeci, K.4    Fan, B.5    Moran, P.6
  • 75
    • 0034848571 scopus 로고    scopus 로고
    • Characterization of a membrane-bound arginine-specific serine protease from rat intestinal mucosa
    • Kishi K., Yamazaki K., Yasuda I., Yahagi N., Ichinose M., Tsuchiya Y., et al. Characterization of a membrane-bound arginine-specific serine protease from rat intestinal mucosa. Journal of Biochemistry 130 (2001) 425-430
    • (2001) Journal of Biochemistry , vol.130 , pp. 425-430
    • Kishi, K.1    Yamazaki, K.2    Yasuda, I.3    Yahagi, N.4    Ichinose, M.5    Tsuchiya, Y.6
  • 78
    • 4544273338 scopus 로고    scopus 로고
    • Identification of domain structures in the propeptide of corin essential for the processing of proatrial natriuretic peptide
    • Knappe S., Wu F., Madlansacay M.R., and Wu Q. Identification of domain structures in the propeptide of corin essential for the processing of proatrial natriuretic peptide. The Journal of Biological Chemistry 279 (2004) 34464-34471
    • (2004) The Journal of Biological Chemistry , vol.279 , pp. 34464-34471
    • Knappe, S.1    Wu, F.2    Madlansacay, M.R.3    Wu, Q.4
  • 79
    • 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. Functional analysis of the transmembrane domain and activation cleavage of human corin: Design and characterization of a soluble corin. The Journal of Biological Chemistry 278 (2003) 52363-52370
    • (2003) The Journal of Biological Chemistry , vol.278 , pp. 52363-52370
    • Knappe, S.1    Wu, F.2    Masikat, M.R.3    Morser, J.4    Wu, Q.5
  • 80
    • 0035147418 scopus 로고    scopus 로고
    • Differential expression of a novel serine protease homologue in squamous cell carcinoma of the head and neck
    • Lang J.C., and Schuller D.E. Differential expression of a novel serine protease homologue in squamous cell carcinoma of the head and neck. British Journal of Cancer 84 (2001) 237-243
    • (2001) British Journal of Cancer , vol.84 , pp. 237-243
    • Lang, J.C.1    Schuller, D.E.2
  • 81
    • 0017280813 scopus 로고
    • Enterokinase and trypsin activities in pancreatic insufficiency and diseases of the small intestine
    • Lebenthal E., Antonowicz I., and Shwachman H. Enterokinase and trypsin activities in pancreatic insufficiency and diseases of the small intestine. Gastroenterology 70 (1976) 508-512
    • (1976) Gastroenterology , vol.70 , pp. 508-512
    • Lebenthal, E.1    Antonowicz, I.2    Shwachman, H.3
  • 82
    • 21544452009 scopus 로고    scopus 로고
    • Increased expression of matriptase is associated with histopathologic grades of cervical neoplasia
    • Lee J.W., Song S.Y., Choi J.J., Lee S.J., Kim B.G., Park C.S., et al. Increased expression of matriptase is associated with histopathologic grades of cervical neoplasia. Human Pathology 36 (2005) 626-633
    • (2005) Human Pathology , vol.36 , pp. 626-633
    • Lee, J.W.1    Song, S.Y.2    Choi, J.J.3    Lee, S.J.4    Kim, B.G.5    Park, C.S.6
  • 83
    • 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. Activation of hepatocyte growth factor and urokinase/plasminogen activator by matriptase, an epithelial membrane serine protease. Journal of Biological Chemistry 275 (2000) 36720-36725
    • (2000) Journal of Biological Chemistry , vol.275 , pp. 36720-36725
    • Lee, S.L.1    Dickson, R.B.2    Lin, C.Y.3
  • 85
    • 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 Davie E.W. A novel trypsin-like serine protease (hepsin) with a putative transmembrane domain expressed by human-liver and hepatoma-cells. Biochemistry 27 (1988) 1067-1074
    • (1988) Biochemistry , vol.27 , pp. 1067-1074
    • Leytus, S.P.1    Loeb, K.R.2    Hagen, F.S.3    Kurachi, K.4    Davie, E.W.5
  • 87
    • 0033198498 scopus 로고    scopus 로고
    • Prostate-localized and androgen-regulated expression of the membrane-bound serine protease TMPRSS2
    • Lin B.Y., Ferguson C., White J.T., Wang S.Y., Vessella R., True L.D., et al. Prostate-localized and androgen-regulated expression of the membrane-bound serine protease TMPRSS2. Cancer Research 59 (1999) 4180-4184
    • (1999) Cancer Research , vol.59 , pp. 4180-4184
    • Lin, B.Y.1    Ferguson, C.2    White, J.T.3    Wang, S.Y.4    Vessella, R.5    True, L.D.6
  • 88
    • 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. Purification and characterization of a complex containing matriptase and a Kunitz-type serine protease inhibitor from human milk. Journal of Biological Chemistry 274 (1999) 18237-18242
    • (1999) Journal of Biological Chemistry , vol.274 , pp. 18237-18242
    • Lin, C.Y.1    Anders, J.2    Johnson, M.3    Dickson, R.B.4
  • 89
    • 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. Molecular cloning of cDNA for matriptase, a matrix-degrading serine protease with trypsin-like activity. Journal of Biological Chemistry 274 (1999) 18231-18236
    • (1999) Journal of Biological Chemistry , vol.274 , pp. 18231-18236
    • Lin, C.Y.1    Anders, J.2    Johnson, M.3    Sang, Q.A.4    Dickson, R.B.5
  • 90
    • 0030910387 scopus 로고    scopus 로고
    • Characterization of a novel, membrane-bound, 80-kDa matrix-degrading protease from human breast cancer cells - Monoclonal antibody production, isolation, and localization
    • Lin C.Y., Wang J.K., Torri J., Dou L., Sang Q.X.A., and Dickson R.B. Characterization of a novel, membrane-bound, 80-kDa matrix-degrading protease from human breast cancer cells - Monoclonal antibody production, isolation, and localization. Journal of Biological Chemistry 272 (1997) 9147-9152
    • (1997) Journal of Biological Chemistry , vol.272 , pp. 9147-9152
    • Lin, C.Y.1    Wang, J.K.2    Torri, J.3    Dou, L.4    Sang, Q.X.A.5    Dickson, R.B.6
  • 91
    • 37549057380 scopus 로고    scopus 로고
    • Autosomal Ichthyosis with hypotrichosis syndrome displays low matriptase proteolytic activity and is phenocopied in ST14 hypomorphic mice
    • List K., Currie B., Scharschmidt T.C., Szabo R., Shireman J., Molinolo A., et al. Autosomal Ichthyosis with hypotrichosis syndrome displays low matriptase proteolytic activity and is phenocopied in ST14 hypomorphic mice. Journal of Biological Chemistry 282 (2007) 36714-36723
    • (2007) Journal of Biological Chemistry , vol.282 , pp. 36714-36723
    • List, K.1    Currie, B.2    Scharschmidt, T.C.3    Szabo, R.4    Shireman, J.5    Molinolo, A.6
  • 92
    • 0037161955 scopus 로고    scopus 로고
    • Matriptase/MT-SP1 is required for postnatal survival, epidermal barrier function, hair follicle development, and thymic homeostasis
    • List K., Haudenschild C.C., Szabo R., Chen W.J., Wahl S.M., Swaim W., et al. Matriptase/MT-SP1 is required for postnatal survival, epidermal barrier function, hair follicle development, and thymic homeostasis. Oncogene 21 (2002) 3765-3779
    • (2002) Oncogene , vol.21 , pp. 3765-3779
    • List, K.1    Haudenschild, C.C.2    Szabo, R.3    Chen, W.J.4    Wahl, S.M.5    Swaim, W.6
  • 93
    • 34548505485 scopus 로고    scopus 로고
    • Co-localization of the channel activating protease prostasin/(CAP1/PRSS8) with its candidate activator, matriptase
    • List K., Hobson J.P., Molinolo A., and Bugge T.H. Co-localization of the channel activating protease prostasin/(CAP1/PRSS8) with its candidate activator, matriptase. Journal of Cell Physiology 213 (2007) 237-245
    • (2007) Journal of Cell Physiology , vol.213 , pp. 237-245
    • List, K.1    Hobson, J.P.2    Molinolo, A.3    Bugge, T.H.4
  • 94
    • 33646514271 scopus 로고    scopus 로고
    • Delineation of matriptase protein expression by enzymatic gene trapping suggests diverging roles in barrier function, hair formation, and squamous cell carcinogenesis
    • List K., Szabo R., Molinolo A., Nielsen B.S., and Bugge T.H. Delineation of matriptase protein expression by enzymatic gene trapping suggests diverging roles in barrier function, hair formation, and squamous cell carcinogenesis. American Journal of Pathology 168 (2006) 1513-1525
    • (2006) American Journal of Pathology , vol.168 , pp. 1513-1525
    • List, K.1    Szabo, R.2    Molinolo, A.3    Nielsen, B.S.4    Bugge, T.H.5
  • 95
    • 23944489424 scopus 로고    scopus 로고
    • Deregulated matriptase causes ras-independent multistage carcinogenesis and promotes ras-mediated malignant transformation
    • List K., Szabo R., Molinolo A., Sriuranpong V., Redeye V., Murdock T., et al. Deregulated matriptase causes ras-independent multistage carcinogenesis and promotes ras-mediated malignant transformation. Genes & Development 19 (2005) 1934-1950
    • (2005) Genes & Development , vol.19 , pp. 1934-1950
    • List, K.1    Szabo, R.2    Molinolo, A.3    Sriuranpong, V.4    Redeye, V.5    Murdock, T.6
  • 96
    • 0345166962 scopus 로고    scopus 로고
    • Loss of proteolytically processed filaggrin caused by epidermal deletion of matriptase/MT-SP1
    • List K., Szabo R., Wertz P.W., Segre J., Haudenschild C.C., Kim S.Y., et al. Loss of proteolytically processed filaggrin caused by epidermal deletion of matriptase/MT-SP1. Journal of Cell Biology 163 (2003) 901-910
    • (2003) Journal of Cell Biology , vol.163 , pp. 901-910
    • List, K.1    Szabo, R.2    Wertz, P.W.3    Segre, J.4    Haudenschild, C.C.5    Kim, S.Y.6
  • 97
    • 0015847599 scopus 로고
    • Distribution of enterokinase in porcine intestine and on its subcellular localization
    • Louvard D., Maroux S., Baratti J., and Desnuell P. Distribution of enterokinase in porcine intestine and on its subcellular localization. Biochimica Et Biophysica Acta 309 (1973) 127-137
    • (1973) Biochimica Et Biophysica Acta , vol.309 , pp. 127-137
    • Louvard, D.1    Maroux, S.2    Baratti, J.3    Desnuell, P.4
  • 98
    • 0031466897 scopus 로고    scopus 로고
    • Bovine proenteropeptidase is activated by trypsin, and the specificity of enteropeptidase depends on the heavy chain
    • Lu D.S., Yuan X., Zheng X.L., and Sadler J.E. Bovine proenteropeptidase is activated by trypsin, and the specificity of enteropeptidase depends on the heavy chain. Journal of Biological Chemistry 272 (1997) 31293-31300
    • (1997) Journal of Biological Chemistry , vol.272 , pp. 31293-31300
    • Lu, D.S.1    Yuan, X.2    Zheng, X.L.3    Sadler, J.E.4
  • 99
    • 0035874995 scopus 로고    scopus 로고
    • Human prostate cancer and benign prostatic hyperplasia: Molecular dissection by gene expression profiling
    • Luo J., Duggan D.J., Chen Y.D., Sauvageot J., Ewing C.M., Bittner M.L., et al. Human prostate cancer and benign prostatic hyperplasia: Molecular dissection by gene expression profiling. Cancer Research 61 (2001) 4683-4688
    • (2001) Cancer Research , vol.61 , pp. 4683-4688
    • Luo, J.1    Duggan, D.J.2    Chen, Y.D.3    Sauvageot, J.4    Ewing, C.M.5    Bittner, M.L.6
  • 100
    • 30044448792 scopus 로고    scopus 로고
    • Autoproteolysis coupled to protein folding in the SEA domain of the membrane-bound MUC1 mucin
    • Macao B., Johansson D.G., Hansson G.C., and Hard T. Autoproteolysis coupled to protein folding in the SEA domain of the membrane-bound MUC1 mucin. Nature Structural & Molecular Biology 13 (2006) 71-76
    • (2006) Nature Structural & Molecular Biology , vol.13 , pp. 71-76
    • Macao, B.1    Johansson, D.G.2    Hansson, G.C.3    Hard, T.4
  • 101
  • 104
    • 0034910275 scopus 로고    scopus 로고
    • Novel missense mutations of TMPRSS3 in two consanguineous Tunisian families with non-syndromic autosomal recessive deafness
    • Masmoudi S., Antonarakis S.E., Schwede T., Ghorbel A.M., Gratri M., Pappasavas M.P., et al. Novel missense mutations of TMPRSS3 in two consanguineous Tunisian families with non-syndromic autosomal recessive deafness. Human Mutation 18 (2001) 101-108
    • (2001) Human Mutation , vol.18 , pp. 101-108
    • Masmoudi, S.1    Antonarakis, S.E.2    Schwede, T.3    Ghorbel, A.M.4    Gratri, M.5    Pappasavas, M.P.6
  • 107
    • 33847334356 scopus 로고    scopus 로고
    • Retinal pathology and skin barrier defect in mice carrying a Stargardt disease-3 mutation in elongase of very long chain fatty acids-4
    • McMahon A., Butovich I.A., Mata N.L., Klein M., Ritter III R., Richardson J., et al. Retinal pathology and skin barrier defect in mice carrying a Stargardt disease-3 mutation in elongase of very long chain fatty acids-4. Molecular Vision 13 (2007) 258-272
    • (2007) Molecular Vision , vol.13 , pp. 258-272
    • McMahon, A.1    Butovich, I.A.2    Mata, N.L.3    Klein, M.4    Ritter III, R.5    Richardson, J.6
  • 108
    • 0038777217 scopus 로고    scopus 로고
    • Effect of human airway trypsin-like protease on intracellular free Ca2+ concentration in human bronchial epithelial cells
    • Miki M., Nakamura Y., Takahashi A., Nakaya Y., Eguchi H., Masegi T., et al. Effect of human airway trypsin-like protease on intracellular free Ca2+ concentration in human bronchial epithelial cells. The Journal of Medical Investigation 50 (2003) 95-107
    • (2003) The Journal of Medical Investigation , vol.50 , pp. 95-107
    • Miki, M.1    Nakamura, Y.2    Takahashi, A.3    Nakaya, Y.4    Eguchi, H.5    Masegi, T.6
  • 110
    • 0034938583 scopus 로고    scopus 로고
    • Celiac disease in a patient with a congenital deficiency of intestinal enteropeptidase
    • Moroz S.P., Hadorn B., Rossi T.M., and Haworth J.C. Celiac disease in a patient with a congenital deficiency of intestinal enteropeptidase. American Journal of Gastroenterology 96 (2001) 2251-2254
    • (2001) American Journal of Gastroenterology , vol.96 , pp. 2251-2254
    • Moroz, S.P.1    Hadorn, B.2    Rossi, T.M.3    Haworth, J.C.4
  • 111
    • 33845945142 scopus 로고    scopus 로고
    • Evidence for a matriptase-prostasin proteolytic cascade regulating terminal epidermal differentiation
    • Netzel-Arnett S., Currie B.M., Szabo R., Lin C.Y., Chen L.M., Chai K.X., et al. Evidence for a matriptase-prostasin proteolytic cascade regulating terminal epidermal differentiation. Journal of Biological Chemistry 281 (2006) 32941-32945
    • (2006) Journal of Biological Chemistry , vol.281 , pp. 32941-32945
    • Netzel-Arnett, S.1    Currie, B.M.2    Szabo, R.3    Lin, C.Y.4    Chen, L.M.5    Chai, K.X.6
  • 112
    • 0037688169 scopus 로고    scopus 로고
    • Membrane anchored serine proteases: A rapidly expanding group of cell surface proteolytic enzymes with potential roles in cancer
    • Netzel-Arnett S., Hooper J.D., Szabo R., Madison E.L., Quigley J.P., Bugge T.H., et al. Membrane anchored serine proteases: A rapidly expanding group of cell surface proteolytic enzymes with potential roles in cancer. Cancer and Metastasis Reviews 22 (2003) 237-258
    • (2003) Cancer and Metastasis Reviews , vol.22 , pp. 237-258
    • Netzel-Arnett, S.1    Hooper, J.D.2    Szabo, R.3    Madison, E.L.4    Quigley, J.P.5    Bugge, T.H.6
  • 113
    • 0015527691 scopus 로고
    • Localization of human enterokinase
    • Nordstro C., and Dahlqvis A. Localization of human enterokinase. Lancet 2 (1972) 933
    • (1972) Lancet , vol.2 , pp. 933
    • Nordstro, C.1    Dahlqvis, A.2
  • 114
    • 0035069846 scopus 로고    scopus 로고
    • Matriptase and HAI-1 are expressed by normal and malignant epithelial cells in vitro and in vivo
    • Oberst M., Anders J., Xie B., Singh B., Ossandon M., Johnson M., et al. Matriptase and HAI-1 are expressed by normal and malignant epithelial cells in vitro and in vivo. American Journal of Pathology 158 (2001) 1301-1311
    • (2001) American Journal of Pathology , vol.158 , pp. 1301-1311
    • Oberst, M.1    Anders, J.2    Xie, B.3    Singh, B.4    Ossandon, M.5    Johnson, M.6
  • 115
    • 0036554846 scopus 로고    scopus 로고
    • Expression of the serine protease matriptase and its inhibitor HAI-1 in epithelial ovarian cancer: Correlation with clinical outcome and tumor clinicopathological parameters
    • Oberst M.D., Johnson M.D., Dickson R.B., Lin C.Y., Singh B., Stewart M., et al. Expression of the serine protease matriptase and its inhibitor HAI-1 in epithelial ovarian cancer: Correlation with clinical outcome and tumor clinicopathological parameters. Clinical Cancer Research 8 (2002) 1101-1107
    • (2002) Clinical Cancer Research , vol.8 , pp. 1101-1107
    • Oberst, M.D.1    Johnson, M.D.2    Dickson, R.B.3    Lin, C.Y.4    Singh, B.5    Stewart, M.6
  • 117
    • 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. The activation of matriptase requires its noncatalytic domains, serine protease domain, and its cognate inhibitor. Journal of Biological Chemistry 278 (2003) 26773-26779
    • (2003) Journal of Biological Chemistry , 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
  • 118
    • 33845807406 scopus 로고    scopus 로고
    • Serase-1B, a new splice variant of polyserase-1/TMPRSS9, activates urokinase-type plasminogen activator and the proteolytic activation is negatively regulated by glycosaminoglycans
    • Okumura Y., Hayama M., Takahashi E., Fujiuchi M., Shimabukuro A., Yano M., et al. Serase-1B, a new splice variant of polyserase-1/TMPRSS9, activates urokinase-type plasminogen activator and the proteolytic activation is negatively regulated by glycosaminoglycans. Biochemical Journal 400 (2006) 551-561
    • (2006) Biochemical Journal , vol.400 , pp. 551-561
    • Okumura, Y.1    Hayama, M.2    Takahashi, E.3    Fujiuchi, M.4    Shimabukuro, A.5    Yano, M.6
  • 119
    • 0036932848 scopus 로고    scopus 로고
    • Identification of two alternate splice variants of a novel serine protease expressed in steroidogenic tissues
    • Omer S., Lomthaisong K., and Bicknell A.B. Identification of two alternate splice variants of a novel serine protease expressed in steroidogenic tissues. Endocrine Research 28 (2002) 339-348
    • (2002) Endocrine Research , vol.28 , pp. 339-348
    • Omer, S.1    Lomthaisong, K.2    Bicknell, A.B.3
  • 120
    • 33747016828 scopus 로고    scopus 로고
    • Variants in the HEPSIN gene are associated with prostate cancer in men of European origin
    • Pal P., Xi H., Kaushal R., Sun G., Jin C.H., Jin L., et al. Variants in the HEPSIN gene are associated with prostate cancer in men of European origin. Human Genetics 120 (2006) 187-192
    • (2006) Human Genetics , vol.120 , pp. 187-192
    • Pal, P.1    Xi, H.2    Kaushal, R.3    Sun, G.4    Jin, C.H.5    Jin, L.6
  • 121
    • 0031572305 scopus 로고    scopus 로고
    • Cloning of the TMPRSS2 gene, which encodes a novel serine protease with transmembrane, LDLRA, and SRCR domains and maps to 21q22.3
    • Paoloni-Giacobino A., Chen H.M., Peitsch M.C., Rossier C., and Antonarakis S.E. Cloning of the TMPRSS2 gene, which encodes a novel serine protease with transmembrane, LDLRA, and SRCR domains and maps to 21q22.3. Genomics 44 (1997) 309-320
    • (1997) Genomics , vol.44 , pp. 309-320
    • Paoloni-Giacobino, A.1    Chen, H.M.2    Peitsch, M.C.3    Rossier, C.4    Antonarakis, S.E.5
  • 123
    • 20444493600 scopus 로고    scopus 로고
    • Frequent overexpression of ETS-related gene-1 (ERG1) in prostate cancer transcriptome
    • Petrovics G., Liu A.J., Shaheduzzaman S., Furasato B., Sun C., Chen Y.M., et al. Frequent overexpression of ETS-related gene-1 (ERG1) in prostate cancer transcriptome. Oncogene 24 (2005) 3847-3852
    • (2005) Oncogene , vol.24 , pp. 3847-3852
    • Petrovics, G.1    Liu, A.J.2    Shaheduzzaman, S.3    Furasato, B.4    Sun, C.5    Chen, Y.M.6
  • 128
    • 22044445706 scopus 로고    scopus 로고
    • Identification of degradome components associated with prostate cancer progression by expression analysis of human prostatic tissues
    • Riddick A.C.P., Shukla C.J., Pennington C.J., Bass R., Nuttall R.K., Hogan A., et al. Identification of degradome components associated with prostate cancer progression by expression analysis of human prostatic tissues. British Journal of Cancer 92 (2005) 2171-2180
    • (2005) British Journal of Cancer , vol.92 , pp. 2171-2180
    • Riddick, A.C.P.1    Shukla, C.J.2    Pennington, C.J.3    Bass, R.4    Nuttall, R.K.5    Hogan, A.6
  • 129
    • 0018101424 scopus 로고
    • Enteropeptidase Levels in Duodenal Juice of Normal Subjects and Patients with Gastrointestinal-Disease
    • Rinderknecht H., Nagaraja M.R., and Adham N.F. Enteropeptidase Levels in Duodenal Juice of Normal Subjects and Patients with Gastrointestinal-Disease. American Journal of Digestive Diseases 23 (1978) 327-331
    • (1978) American Journal of Digestive Diseases , vol.23 , pp. 327-331
    • Rinderknecht, H.1    Nagaraja, M.R.2    Adham, N.F.3
  • 130
    • 8644289994 scopus 로고    scopus 로고
    • The membrane proteases ADAMS and hepsin are differentially expressed in renal cell carcinoma. Are they potential tumor markers?
    • Roemer A., Schwettmann L., Jung M., Stephan C., Roigas J., Kristiansen G., et al. The membrane proteases ADAMS and hepsin are differentially expressed in renal cell carcinoma. Are they potential tumor markers?. Journal of Urology 172 (2004) 2162-2166
    • (2004) Journal of Urology , vol.172 , pp. 2162-2166
    • Roemer, A.1    Schwettmann, L.2    Jung, M.3    Stephan, C.4    Roigas, J.5    Kristiansen, G.6
  • 132
    • 33644784579 scopus 로고    scopus 로고
    • A novel biomarker for staging human prostate adenocarcinoma: Overexpression of matriptase with concomitant loss of its inhibitor, hepatocyte growth factor activator inhibitor-1
    • Saleem M., Adhami V.M., Zhong W.X., Longley B.J., Lin C.Y., Dickson R.B., et al. A novel biomarker for staging human prostate adenocarcinoma: Overexpression of matriptase with concomitant loss of its inhibitor, hepatocyte growth factor activator inhibitor-1. Cancer Epidemiology Biomarkers & Prevention 15 (2006) 217-227
    • (2006) Cancer Epidemiology Biomarkers & Prevention , vol.15 , pp. 217-227
    • Saleem, M.1    Adhami, V.M.2    Zhong, W.X.3    Longley, B.J.4    Lin, C.Y.5    Dickson, R.B.6
  • 133
    • 4544224142 scopus 로고    scopus 로고
    • Gene expression profiles in primary ovarian serous papillary tumors and normal ovarian epithelium: Identification of candidate molecular markers for ovarian cancer diagnosis and therapy
    • Santin A.D., Zhan F.H., Bellone S., Palmieri M., Cane S., Bignotti E., et al. Gene expression profiles in primary ovarian serous papillary tumors and normal ovarian epithelium: Identification of candidate molecular markers for ovarian cancer diagnosis and therapy. International Journal of Cancer 112 (2004) 14-25
    • (2004) International Journal of Cancer , vol.112 , pp. 14-25
    • Santin, A.D.1    Zhan, F.H.2    Bellone, S.3    Palmieri, M.4    Cane, S.5    Bignotti, E.6
  • 135
    • 4644309151 scopus 로고    scopus 로고
    • The transmembrane protease serine (TMPRSS3/TADG-12) D variant: A potential candidate for diagnosis and therapeutic intervention in ovarian cancer
    • Sawasaki T., Shigemasa K., Gu L.J., Beard J.B., and O'brien T.J. The transmembrane protease serine (TMPRSS3/TADG-12) D variant: A potential candidate for diagnosis and therapeutic intervention in ovarian cancer. Tumor Biology 25 (2004) 141-148
    • (2004) Tumor Biology , vol.25 , pp. 141-148
    • Sawasaki, T.1    Shigemasa, K.2    Gu, L.J.3    Beard, J.B.4    O'brien, T.J.5
  • 137
    • 0035167046 scopus 로고    scopus 로고
    • Insertion of beta-satellite repeats identifies a transmembrane protease causing both congenital and childhood onset autosomal recessive deafness
    • Scott H.S., Kudoh J., Wattenhofer M., Shibuya K., Berry A., Chrast R., et al. Insertion of beta-satellite repeats identifies a transmembrane protease causing both congenital and childhood onset autosomal recessive deafness. Nature Genetics 27 (2001) 59-63
    • (2001) Nature Genetics , vol.27 , pp. 59-63
    • Scott, H.S.1    Kudoh, J.2    Wattenhofer, M.3    Shibuya, K.4    Berry, A.5    Chrast, R.6
  • 139
    • 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. Identification and characterization of a novel matrix-degrading protease from hormone-dependent human breast-cancer cells. Cancer Research 53 (1993) 1409-1415
    • (1993) Cancer Research , 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
  • 141
    • 33646580105 scopus 로고    scopus 로고
    • Confirmation of the high frequency of the TMPRSS2/ERG fusion gene in prostate cancer
    • Soller M.J., Elfving P., Lundgren R., and Panagopols I. Confirmation of the high frequency of the TMPRSS2/ERG fusion gene in prostate cancer. Genes Chromosomes & Cancer 45 (2006) 717-719
    • (2006) Genes Chromosomes & Cancer , vol.45 , pp. 717-719
    • Soller, M.J.1    Elfving, P.2    Lundgren, R.3    Panagopols, I.4
  • 142
    • 0035174607 scopus 로고    scopus 로고
    • Molecular genetic profiling of gleason grade 4/5 prostate cancers compared to benign prostatic hyperplasia
    • Stamey T.A., Warrington J.A., Caldwell M.C., Chen Z.X., Fan Z.B., Mahadevappa M., et al. Molecular genetic profiling of gleason grade 4/5 prostate cancers compared to benign prostatic hyperplasia. Journal of Urology 166 (2001) 2171-2177
    • (2001) Journal of Urology , vol.166 , pp. 2171-2177
    • Stamey, T.A.1    Warrington, J.A.2    Caldwell, M.C.3    Chen, Z.X.4    Fan, Z.B.5    Mahadevappa, M.6
  • 143
    • 10744220367 scopus 로고    scopus 로고
    • Hepsin is highly over expressed in and a new candidate for a prognostic indicator in prostate cancer
    • Stephan C., Yousef G.M., Scorilas A., Jung K., Jung M., Kristiansen G., et al. Hepsin is highly over expressed in and a new candidate for a prognostic indicator in prostate cancer. Journal of Urology 171 (2004) 187-191
    • (2004) Journal of Urology , vol.171 , pp. 187-191
    • Stephan, C.1    Yousef, G.M.2    Scorilas, A.3    Jung, K.4    Jung, M.5    Kristiansen, G.6
  • 144
    • 33947164004 scopus 로고    scopus 로고
    • Matriptase inhibition by hepatocyte growth factor activator inhibitor-1 is essential for placental development
    • Szabo R., Molinolo A., List K., and Bugge T.H. Matriptase inhibition by hepatocyte growth factor activator inhibitor-1 is essential for placental development. Oncogene 26 (2007) 1546-1556
    • (2007) Oncogene , vol.26 , pp. 1546-1556
    • Szabo, R.1    Molinolo, A.2    List, K.3    Bugge, T.H.4
  • 145
    • 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. Matriptase-3 is a novel phylogenetically preserved membrane-anchored serine protease with broad serpin reactivity. Biochemical Journal 390 (2005) 231-242
    • (2005) Biochemical Journal , vol.390 , pp. 231-242
    • Szabo, R.1    Netzel-Arnett, S.2    Hobson, J.P.3    Antalis, T.M.4    Bugge, T.H.5
  • 148
    • 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. Cellular localization of membrane-type serine protease 1 and identification of protease-activated receptor-2 and single-chain urokinase-type plasminogen activator as substrates. Journal of Biological Chemistry 275 (2000) 26333-26342
    • (2000) Journal of Biological Chemistry , 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
  • 149
    • 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. 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. Proceedings of the National Academy of Sciences of the United States of America 96 (1999) 11054-11061
    • (1999) Proceedings of the National Academy of Sciences of the United States of America , vol.96 , pp. 11054-11061
    • Takeuchi, T.1    Shuman, M.A.2    Craik, C.S.3
  • 150
    • 20744448360 scopus 로고    scopus 로고
    • Hepatocyte growth factor activator inhibitor type 1 (HAI-1) is required for branching morphogenesis in the chorioallantoic placenta
    • Tanaka H., Nagaike K., Takeda N., Itoh H., Kohama K., Fukushima T., et al. Hepatocyte growth factor activator inhibitor type 1 (HAI-1) is required for branching morphogenesis in the chorioallantoic placenta. Molecular and Cellular Biology 25 (2005) 5687-5698
    • (2005) Molecular and Cellular Biology , vol.25 , pp. 5687-5698
    • Tanaka, H.1    Nagaike, K.2    Takeda, N.3    Itoh, H.4    Kohama, K.5    Fukushima, T.6
  • 151
    • 0030850099 scopus 로고    scopus 로고
    • Hepsin, a cell surface serine protease identified in hepatoma cells, is overexpressed in ovarian cancer
    • Tanimoto H., Yan Y., Clarke J., Korourian S., Shigemasa K., Parmley T.H., et al. Hepsin, a cell surface serine protease identified in hepatoma cells, is overexpressed in ovarian cancer. Cancer Research 57 (1997) 2884-2887
    • (1997) Cancer Research , vol.57 , pp. 2884-2887
    • Tanimoto, H.1    Yan, Y.2    Clarke, J.3    Korourian, S.4    Shigemasa, K.5    Parmley, T.H.6
  • 153
    • 27344451557 scopus 로고    scopus 로고
    • Recurrent fusion of TMPRSS2 and ETS transcription factor genes in prostate cancer
    • Tomlins S.A., Rhodes D.R., Perner S., Dhanasekaran S.M., Mehra R., Sun X.W., et al. Recurrent fusion of TMPRSS2 and ETS transcription factor genes in prostate cancer. Science 310 (2005) 644-648
    • (2005) Science , vol.310 , pp. 644-648
    • Tomlins, S.A.1    Rhodes, D.R.2    Perner, S.3    Dhanasekaran, S.M.4    Mehra, R.5    Sun, X.W.6
  • 154
    • 33846815516 scopus 로고    scopus 로고
    • Identification of novel genes that co-cluster with estrogen receptor alpha in breast tumor biopsy specimens, using a large-scale real-time reverse transcription-PCR approach
    • Tozlu S., Girault I., Vacher S., Vendrell J., Andrieu C., Spyratos F., et al. Identification of novel genes that co-cluster with estrogen receptor alpha in breast tumor biopsy specimens, using a large-scale real-time reverse transcription-PCR approach. Endocrine-Related Cancer 13 (2006) 1109-1120
    • (2006) Endocrine-Related Cancer , vol.13 , pp. 1109-1120
    • Tozlu, S.1    Girault, I.2    Vacher, S.3    Vendrell, J.4    Andrieu, C.5    Spyratos, F.6
  • 156
    • 0025951220 scopus 로고
    • Hepsin, a cell membrane-associated protease-Characterization, tissue distribution, and gene localization
    • Tsuji A., Torresrosado A., Arai T., Lebeau M.M., Lemons R.S., Chou S.H., et al. Hepsin, a cell membrane-associated protease-Characterization, tissue distribution, and gene localization. Journal of Biological Chemistry 266 (1991) 16948-16953
    • (1991) Journal of Biological Chemistry , vol.266 , pp. 16948-16953
    • Tsuji, A.1    Torresrosado, A.2    Arai, T.3    Lebeau, M.M.4    Lemons, R.S.5    Chou, S.H.6
  • 157
    • 33846072965 scopus 로고    scopus 로고
    • Matriptase and its putative role in cancer
    • Uhland K. Matriptase and its putative role in cancer. Cellular and Molecular Life Sciences 63 (2006) 2968-2978
    • (2006) Cellular and Molecular Life Sciences , vol.63 , pp. 2968-2978
    • Uhland, K.1
  • 158
    • 0035545817 scopus 로고    scopus 로고
    • The TMPRSS2 gene encoding transmembrane serine protease is overexpressed in a majority of prostate cancer patients: Detection of mutated TMPRSS2 form in a case of aggressive disease
    • Vaarala M.H., Porvari K., Kyllonen A., Lukkarinen O., and Vihko P. The TMPRSS2 gene encoding transmembrane serine protease is overexpressed in a majority of prostate cancer patients: Detection of mutated TMPRSS2 form in a case of aggressive disease. International Journal of Cancer 94 (2001) 705-710
    • (2001) International Journal of Cancer , vol.94 , pp. 705-710
    • Vaarala, M.H.1    Porvari, K.2    Kyllonen, A.3    Lukkarinen, O.4    Vihko, P.5
  • 160
    • 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., Sanchez L.M., and Lopez-Otin C. Matriptase-2, a membrane-bound mosaic serine proteinase predominantly expressed in human liver and showing degrading activity against extracellular matrix proteins. Journal of Biological Chemistry 277 (2002) 37637-37646
    • (2002) Journal of Biological Chemistry , vol.277 , pp. 37637-37646
    • Velasco, G.1    Cal, S.2    Quesada, V.3    Sanchez, L.M.4    Lopez-Otin, C.5
  • 161
    • 33746604484 scopus 로고    scopus 로고
    • The ratio of Matriptase/HAI-l mRNA is higher in colorectal cancer adenomas and carcinomas than corresponding tissue from control individuals
    • Vogel L.K., Saebo M., Skjelbred C.F., Abell K., Pedersen E.D.K., Vogel U., et al. The ratio of Matriptase/HAI-l mRNA is higher in colorectal cancer adenomas and carcinomas than corresponding tissue from control individuals. Bmc Cancer 6 (2006)
    • (2006) Bmc Cancer , vol.6
    • Vogel, L.K.1    Saebo, M.2    Skjelbred, C.F.3    Abell, K.4    Pedersen, E.D.K.5    Vogel, U.6
  • 162
    • 0031465168 scopus 로고    scopus 로고
    • Identification and cloning of the membrane-associated serine protease, hepsin, from mouse preimplantation embryos
    • Vu T.K.H., Liu R.W., Haaksma C.J., Tomasek J.J., and Howard E.W. Identification and cloning of the membrane-associated serine protease, hepsin, from mouse preimplantation embryos. Journal of Biological Chemistry 272 (1997) 31315-31320
    • (1997) Journal of Biological Chemistry , vol.272 , pp. 31315-31320
    • Vu, T.K.H.1    Liu, R.W.2    Haaksma, C.J.3    Tomasek, J.J.4    Howard, E.W.5
  • 166
    • 27544455732 scopus 로고    scopus 로고
    • A novel TMPRSS3 missense mutation in a DFNB8/10 family prevents proteolytic activation of the protein
    • Wattenhofer M., Sahin-Calapoglu N., Andreasen D., Kalay E., Caylan R., Braillard B., et al. A novel TMPRSS3 missense mutation in a DFNB8/10 family prevents proteolytic activation of the protein. Human Genetics 117 (2005) 528-535
    • (2005) Human Genetics , vol.117 , pp. 528-535
    • Wattenhofer, M.1    Sahin-Calapoglu, N.2    Andreasen, D.3    Kalay, E.4    Caylan, R.5    Braillard, B.6
  • 167
    • 0038463745 scopus 로고    scopus 로고
    • Type II transmembrane serine proteases
    • Wu Q.Y. Type II transmembrane serine proteases. Cell Surface Proteases 54 (2003) 167-206
    • (2003) Cell Surface Proteases , vol.54 , pp. 167-206
    • Wu, Q.Y.1
  • 168
    • 34347220108 scopus 로고    scopus 로고
    • The serine protease corin in cardiovascular biology and disease
    • Wu Q.Y. The serine protease corin in cardiovascular biology and disease. Frontiers in Biosciences 12 (2007) 4179-4190
    • (2007) Frontiers in Biosciences , vol.12 , pp. 4179-4190
    • Wu, Q.Y.1
  • 170
    • 0036510530 scopus 로고    scopus 로고
    • Spinesin/TMPRSS5, a novel transmembrane serine protease, cloned from human spinal cord
    • Yamaguchi N., Okui A., Yamada T., Nakazato H., and Mitsui S. Spinesin/TMPRSS5, a novel transmembrane serine protease, cloned from human spinal cord. Journal of Biological Chemistry 277 (2002) 6806-6812
    • (2002) Journal of Biological Chemistry , vol.277 , pp. 6806-6812
    • Yamaguchi, N.1    Okui, A.2    Yamada, T.3    Nakazato, H.4    Mitsui, S.5
  • 172
    • 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.Y. Corin, a mosaic transmembrane serine protease encoded by a novel cDNA from human heart. Journal of Biological Chemistry 274 (1999) 14926-14935
    • (1999) Journal of Biological Chemistry , vol.274 , pp. 14926-14935
    • Yan, W.1    Sheng, N.2    Seto, M.3    Morser, J.4    Wu, Q.Y.5
  • 175
    • 0032130759 scopus 로고    scopus 로고
    • Fibrinogenolytic activity of a novel trypsin-like enzyme found in human airway
    • Yoshinaga S., Nakahori Y., and Yasuoka S. Fibrinogenolytic activity of a novel trypsin-like enzyme found in human airway. The Journal of Medical Investigation 45 (1998) 77-86
    • (1998) The Journal of Medical Investigation , vol.45 , pp. 77-86
    • Yoshinaga, S.1    Nakahori, Y.2    Yasuoka, S.3
  • 176
    • 0033724609 scopus 로고    scopus 로고
    • Mice deficient in hepsin, a serine protease, exhibit normal embryogenesis and unchanged hepatocyte regeneration ability
    • Yu I.S., Chen H.J., Lee Y.S.E., Huang P.H., Lin S.R., Tsai T.W., et al. Mice deficient in hepsin, a serine protease, exhibit normal embryogenesis and unchanged hepatocyte regeneration ability. Thrombosis and Haemostasis 84 (2000) 865-870
    • (2000) Thrombosis and Haemostasis , vol.84 , pp. 865-870
    • Yu, I.S.1    Chen, H.J.2    Lee, Y.S.E.3    Huang, P.H.4    Lin, S.R.5    Tsai, T.W.6
  • 180
    • 30644459109 scopus 로고    scopus 로고
    • Expression of serine protease SNC19/matriptase and its inhibitor hepatocyte growth factor activator inhibitor type 1 in normal and malignant tissues of gastrointestinal tract
    • Zeng L., Cao J., and Zhang X. Expression of serine protease SNC19/matriptase and its inhibitor hepatocyte growth factor activator inhibitor type 1 in normal and malignant tissues of gastrointestinal tract. World Journal of Gastroenterology 11 (2005) 6202-6207
    • (2005) World Journal of Gastroenterology , vol.11 , pp. 6202-6207
    • Zeng, L.1    Cao, J.2    Zhang, X.3
  • 181
    • 33750477010 scopus 로고    scopus 로고
    • Comparative analysis of serine protease-related genes in the honey bee genome: Possible involvement in embryonic development and innate immunity
    • Zou Z., Lopez D.L., Kanost M.R., Evans J.D., and Jiang H.B. Comparative analysis of serine protease-related genes in the honey bee genome: Possible involvement in embryonic development and innate immunity. Insect Molecular Biology 15 (2006) 603-614
    • (2006) Insect Molecular Biology , vol.15 , pp. 603-614
    • Zou, Z.1    Lopez, D.L.2    Kanost, M.R.3    Evans, J.D.4    Jiang, H.B.5


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