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Volumn 10, Issue 9, 2011, Pages

Proteomic analyses reveal an acidic prime side specificity for the astacin metalloprotease family reflected by physiological substrates

Author keywords

[No Author keywords available]

Indexed keywords

ASTACIN; FIBROBLAST GROWTH FACTOR 19; INTERLEUKIN 1BETA; MEPRIN; MEPRIN ALPHA; MEPRIN BETA; PREKALLIKREIN; PREKALLIKREIN 7; PROCOLLAGEN; PROLINE; PROTEINASE; UNCLASSIFIED DRUG; VASCULOTROPIN A; ENZYME PRECURSOR; KALLIKREIN; KLK7 PROTEIN, HUMAN; METALLOPROTEINASE; PEPTIDE; RECOMBINANT PROTEIN; TIOPRONIN;

EID: 80052734691     PISSN: 15359476     EISSN: 15359484     Source Type: Journal    
DOI: 10.1074/mcp.M111.009233     Document Type: Article
Times cited : (122)

References (70)
  • 1
    • 0037803570 scopus 로고    scopus 로고
    • Human and mouse proteases: A comparative genomic approach
    • DOI 10.1038/nrg1111
    • Puente, X. S., Sánchez, L. M., Overall, C. M., and López-Otin, C. (2003) Human and mouse proteases: a comparative genomic approach. Nat. Rev. Genet. 4, 544-558 (Pubitemid 36781345)
    • (2003) Nature Reviews Genetics , vol.4 , Issue.7 , pp. 544-558
    • Puente, X.S.1    Sanchez, L.M.2    Overall, C.M.3    Lopez-Otin, C.4
  • 2
    • 33644545381 scopus 로고    scopus 로고
    • Validating matrix metalloproteinases as drug targets and anti-targets for cancer therapy
    • DOI 10.1038/nrc1821, PII N1821
    • Overall, C. M., and Kleifeld, O. (2006) Tumour microenvironment - opinion: validating matrix metalloproteinases as drug targets and anti-targets for cancer therapy. Nat. Rev. Cancer 6, 227-239 (Pubitemid 43292566)
    • (2006) Nature Reviews Cancer , vol.6 , Issue.3 , pp. 227-239
    • Overall, C.M.1    Kleifeld, O.2
  • 3
    • 33748308883 scopus 로고    scopus 로고
    • Targeting proteases: Successes, failures and future prospects
    • Turk, B. (2006) Targeting proteases: successes, failures and future prospects. Nat. Rev. Drug Discov. 5, 785-799
    • (2006) Nat. Rev. Drug Discov. , vol.5 , pp. 785-799
    • Turk, B.1
  • 4
    • 28444438511 scopus 로고    scopus 로고
    • Mapping of the active site of proteases in the 1960s and rational design of inhibitors/drugs in the 1990s
    • Schechter, I. (2005) Mapping of the active site of proteases in the 1960s and rational design of inhibitors/drugs in the 1990s. Curr. Protein Pept. Sci. 6, 501-512
    • (2005) Curr. Protein Pept. Sci. , vol.6 , pp. 501-512
    • Schechter, I.1
  • 5
    • 0038019916 scopus 로고    scopus 로고
    • Structural aspects of the metzincin clan of metalloendopeptidases
    • Gomis-Rüth, 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-Rüth, F.X.1
  • 6
    • 0029016839 scopus 로고
    • The astacin family of metalloendopeptidases
    • Bond, J. S., and Beynon, R. J. (1995) The astacin family of metalloendopeptidases. Protein Sci. 4, 1247-1261
    • (1995) Protein Sci. , vol.4 , pp. 1247-1261
    • Bond, J.S.1    Beynon, R.J.2
  • 7
    • 0020032479 scopus 로고
    • Non-pancreatic hydrolysis of N-benzoyl-L-tyrosyl-p-aminobenzoic acid (PABA-peptide) in the human small intestine
    • Sterchi, E. E., Green, J. R., and Lentze, M. J. (1982) Non-pancreatic hydrolysis of N-benzoyl-l-tyrosyl-p-aminobenzoic acid (PABA-peptide) in the human small intestine. Clin. Sci. 62, 557-560 (Pubitemid 12127238)
    • (1982) Clinical Science , vol.62 , Issue.5 , pp. 557-560
    • Sterchi, E.E.1    Green, J.R.2    Lentze, M.J.3
  • 8
    • 35348923714 scopus 로고    scopus 로고
    • The bone morphogenetic protein 1/Tolloid-like metalloproteinases
    • DOI 10.1016/j.matbio.2007.05.004, PII S0945053X07000649
    • Hopkins, D. R., Keles, S., and Greenspan, D. S. (2007) The bone morphogenetic protein 1/Tolloid-like metalloproteinases. Matrix Biol. 26, 508-523 (Pubitemid 47575882)
    • (2007) Matrix Biology , vol.26 , Issue.7 , pp. 508-523
    • Hopkins, D.R.1    Keles, S.2    Greenspan, D.S.3
  • 9
    • 2942754000 scopus 로고    scopus 로고
    • Identification and characterization of human and mouse ovastacin: A novel metalloproteinase similar to hatching enzymes from arthropods, birds, amphibians, and fish
    • DOI 10.1074/jbc.M401588200
    • Quesada, V., Sánchez, L. M., Alvarez, J., and López-Otin, C. (2004) Identification and characterization of human and mouse ovastacin: a novel metalloproteinase similar to hatching enzymes from arthropods, birds, amphibians, and fish. J. Biol. Chem. 279, 26627-26634 (Pubitemid 38798820)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.25 , pp. 26627-26634
    • Quesada, V.1    Sanchez, L.M.2    Alvarez, J.3    Lopez-Otin, C.4
  • 10
    • 21244454923 scopus 로고    scopus 로고
    • Substrate-specific modulation of a multisubstrate proteinase: C-terminal processing of fibrillar procollagens is the only BMP-1-dependent activity to be enhanced by PCPE-1
    • DOI 10.1074/jbc.M501486200
    • Moali, C., Font, B., Ruggiero, F., Eichenberger, D., Rousselle, P., François, V., Oldberg, A., Bruckner-Tuderman, L., and Hulmes, D. J. (2005) Substrate-specific modulation of a multisubstrate proteinase. C-terminal processing of fibrillar procollagens is the only BMP-1-dependent activity to be enhanced by PCPE-1. J. Biol. Chem. 280, 24188-24194 (Pubitemid 40884908)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.25 , pp. 24188-24194
    • Moali, C.1    Font, B.2    Ruggiero, F.3    Eichenberger, D.4    Rousselle, P.5    Francois, V.6    Oldberg, A.7    Bruckner-Tuderman, L.8    Hulmes, D.J.S.9
  • 12
    • 34247257873 scopus 로고    scopus 로고
    • The alpha and beta subunits of the metalloprotease meprin are expressed in separate layers of human epidermis, revealing different functions in keratinocyte proliferation and differentiation
    • DOI 10.1038/sj.jid.5700675, PII 5700675
    • Becker-Pauly, C., Höwel, M., Walker, T., Vlad, A., Aufenvenne, K., Oji, V., Lottaz, D., Sterchi, E. E., Debela, M., Magdolen, V., Traupe, H., and Stöcker, W. (2007) The alpha and beta subunits of the metalloprotease meprin are expressed in separate layers of human epidermis, revealing different functions in keratinocyte proliferation and differentiation. J. Invest. Dermatol. 127, 1115-1125 (Pubitemid 46625146)
    • (2007) Journal of Investigative Dermatology , vol.127 , Issue.5 , pp. 1115-1125
    • Becker-Pauly, C.1    Howel, M.2    Walker, T.3    Vlad, A.4    Aufenvenne, K.5    Oji, V.6    Lottaz, D.7    Sterchi, E.E.8    Debela, M.9    Magdolen, V.10    Traupe, H.11    Stocker, W.12
  • 13
    • 0025991743 scopus 로고
    • Meprin-A and -B: Cell surface endopeptidases of the mouse kidney
    • Kounnas, M. Z., Wolz, R. L., Gorbea, C. M., and Bond, J. S. (1991) Meprin-A and -B. Cell surface endopeptidases of the mouse kidney. J. Biol. Chem. 266, 17350-17357 (Pubitemid 21907946)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.26 , pp. 17350-17357
    • Kounnas, M.Z.1    Wolz, R.L.2    Gorbea, C.M.3    Bond, J.S.4
  • 14
    • 52949132216 scopus 로고    scopus 로고
    • Meprins, membrane-bound and secreted astacin metalloproteinases
    • Sterchi, E. E., Stöcker, W., and Bond, J. S. (2008) Meprins, membrane-bound and secreted astacin metalloproteinases. Mol. Aspects Med. 29, 309-328
    • (2008) Mol. Aspects Med. , vol.29 , pp. 309-328
    • Sterchi, E.E.1    Stöcker, W.2    Bond, J.S.3
  • 16
    • 0037462760 scopus 로고    scopus 로고
    • Structure of homo- and hetero-oligomeric meprin metalloproteases: Dimers, tetramers, and high molecular mass multimers
    • DOI 10.1074/jbc.M208808200
    • Bertenshaw, G. P., Norcum, M. T., and Bond, J. S. (2003) Structure of homo- and hetero-oligomeric meprin metalloproteases. Dimers, tetramers, and high molecular mass multimers. J. Biol. Chem. 278, 2522-2532 (Pubitemid 36801329)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.4 , pp. 2522-2532
    • Bertenshaw, G.P.1    Norcum, M.T.2    Bond, J.S.3
  • 17
    • 1642362446 scopus 로고    scopus 로고
    • Human meprin alpha and beta homo-oligomers: Cleavage of basement membrane proteins and sensitivity to metalloprotease inhibitors
    • DOI 10.1042/BJ20031163
    • Kruse, M. N., Becker, C., Lottaz, D., Köhler, D., Yiallouros, I., Krell, H. W., Sterchi, E. E., and Stöcker, W. (2004) Human meprin alpha and beta homo-oligomers: cleavage of basement membrane proteins and sensitivity to metalloprotease inhibitors. Biochem. J. 378, 383-389 (Pubitemid 38367229)
    • (2004) Biochemical Journal , vol.378 , Issue.2 , pp. 383-389
    • Kruse, M.-N.1    Becker, C.2    Lottaz, D.3    Kohler, D.4    Yiallouros, I.5    Krell, H.-W.6    Sterchi, E.E.7    Stocker, W.8
  • 18
    • 77952485887 scopus 로고    scopus 로고
    • Let it flow: Morpholino knockdown in zebrafish embryos reveals a pro-angiogenic effect of the metalloprotease meprin alpha2
    • Schütte, A., Hedrich, J., Stöcker, W., and Becker-Pauly, C. (2010) Let it flow: Morpholino knockdown in zebrafish embryos reveals a pro-angiogenic effect of the metalloprotease meprin alpha2. PloS One 5, e8835
    • (2010) PloS One , vol.5
    • Schütte, A.1    Hedrich, J.2    Stöcker, W.3    Becker-Pauly, C.4
  • 19
    • 23944491189 scopus 로고    scopus 로고
    • Generation of biologically active interleukin-1beta by meprin B
    • DOI 10.1016/j.cyto.2005.06.012, PII S1043466605002152
    • Herzog, C., Kaushal, G. P., and Haun, R. S. (2005) Generation of biologically active interleukin-1beta by meprin B. Cytokine 31, 394-403 (Pubitemid 41188061)
    • (2005) Cytokine , vol.31 , Issue.5 , pp. 394-403
    • Herzog, C.1    Kaushal, G.P.2    Haun, R.S.3
  • 20
    • 57649123150 scopus 로고    scopus 로고
    • Prointerleukin-18 is activated by meprin beta in vitro and in vivo in intestinal inflammation
    • Banerjee, S., and Bond, J. S. (2008) Prointerleukin-18 is activated by meprin beta in vitro and in vivo in intestinal inflammation. J. Biol. Chem. 283, 31371-31377
    • (2008) J. Biol. Chem. , vol.283 , pp. 31371-31377
    • Banerjee, S.1    Bond, J.S.2
  • 24
    • 34249066698 scopus 로고    scopus 로고
    • Two alpha subunits and one beta subunit of meprin zinc-endopeptidases are differentially expressed in the zebrafish Danio rerio
    • DOI 10.1515/BC.2007.060
    • Schütte, A., Lottaz, D., Sterchi, E. E., Stöcker, W., and Becker-Pauly, C. (2007) Two alpha subunits and one beta subunit of meprin zinc-endopeptidases are differentially expressed in the zebrafish Danio rerio. Biol. Chem. 388, 523-531 (Pubitemid 46800265)
    • (2007) Biological Chemistry , vol.388 , Issue.5 , pp. 523-531
    • Schutte, A.1    Lottaz, D.2    Sterchi, E.E.3    Stocker, W.4    Becker-Pauly, C.5
  • 25
    • 44949142150 scopus 로고    scopus 로고
    • Proteome-derived, database-searchable peptide libraries for identifying protease cleavage sites
    • DOI 10.1038/nbt1408, PII NBT1408
    • Schilling, O., and Overall, C. M. (2008) Proteome-derived, database-searchable peptide libraries for identifying protease cleavage sites. Nat. Biotechnol. 26, 685-694 (Pubitemid 351809596)
    • (2008) Nature Biotechnology , vol.26 , Issue.6 , pp. 685-694
    • Schilling, O.1    Overall, C.M.2
  • 26
    • 77951134556 scopus 로고    scopus 로고
    • Multiplex N-terminome analysis of MMP-2 and MMP-9 substrate degradomes by iTRAQ-TAILS quantitative proteomics
    • Prudova, A., auf dem Keller, U., Butler, G. S., and Overall, C. M. (2010) Multiplex N-terminome analysis of MMP-2 and MMP-9 substrate degradomes by iTRAQ-TAILS quantitative proteomics. Mol. Cell Proteomics 9, 894-911
    • (2010) Mol. Cell Proteomics , vol.9 , pp. 894-911
    • Prudova, A.1    Auf Dem Keller, U.2    Butler, G.S.3    Overall, C.M.4
  • 29
    • 0026736225 scopus 로고
    • Structure of astacin and implications for activation of astacins and zincligation of collagenases
    • Bode, W., Gomis-Rüth, F. X., Huber, R., Zwilling, R., and Stöcker, W. (1992) Structure of astacin and implications for activation of astacins and zincligation of collagenases. Nature 358, 164-167
    • (1992) Nature , vol.358 , pp. 164-167
    • Bode, W.1    Gomis-Rüth, F.X.2    Huber, R.3    Zwilling, R.4    Stöcker, W.5
  • 30
    • 3142702204 scopus 로고    scopus 로고
    • TANDEM: Matching proteins with tandem mass spectra
    • DOI 10.1093/bioinformatics/bth092
    • Craig, R., and Beavis, R. C. (2004) TANDEM: matching proteins with tandem mass spectra. Bioinformatics 20, 1466-1467 (Pubitemid 38931421)
    • (2004) Bioinformatics , vol.20 , Issue.9 , pp. 1466-1467
    • Craig, R.1    Beavis, R.C.2
  • 31
    • 0037108887 scopus 로고    scopus 로고
    • Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search
    • DOI 10.1021/ac025747h
    • Keller, A., Nesvizhskii, A. I., Kolker, E., and Aebersold, R. (2002) Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search. Anal. Chem. 74, 5383-5392 (Pubitemid 35215372)
    • (2002) Analytical Chemistry , vol.74 , Issue.20 , pp. 5383-5392
    • Keller, A.1    Nesvizhskii, A.I.2    Kolker, E.3    Aebersold, R.4
  • 32
    • 3042818018 scopus 로고    scopus 로고
    • The international protein index: An integrated database for proteomics experiments
    • DOI 10.1002/pmic.200300721
    • Kersey, P. J., Duarte, J., Williams, A., Karavidopoulou, Y., Birney, E., and Apweiler, R. (2004) The International Protein Index: an integrated database for proteomics experiments. Proteomics 4, 1985-1988 (Pubitemid 38880363)
    • (2004) Proteomics , vol.4 , Issue.7 , pp. 1985-1988
    • Kersey, P.J.1    Duarte, J.2    Williams, A.3    Karavidopoulou, Y.4    Birney, E.5    Apweiler, R.6
  • 33
    • 78651069641 scopus 로고    scopus 로고
    • Characterization of the prime and non-prime active site specificities of proteases by proteome-derived peptide libraries and tandem mass spectrometry
    • Schilling, O., Huesgen, P. F., Barre, O., Auf dem Keller, U., and Overall, C. M. (2011) Characterization of the prime and non-prime active site specificities of proteases by proteome-derived peptide libraries and tandem mass spectrometry. Nat. Protoc. 6, 111-120
    • (2011) Nat. Protoc. , vol.6 , pp. 111-120
    • Schilling, O.1    Huesgen, P.F.2    Barre, O.3    Auf Dem Keller, U.4    Overall, C.M.5
  • 34
    • 0029939026 scopus 로고    scopus 로고
    • Human immunodeficiency virus, type 1 protease substrate specificity is limited by interactions between substrate amino acids bound in adjacent enzyme subsites
    • DOI 10.1074/jbc.271.9.4709
    • Ridky, T. W., Cameron, C. E., Cameron, J., Leis, J., Copeland, T., Wlodawer, A., Weber, I. T., and Harrison, R. W. (1996) Human immunodeficiency virus, type 1 protease substrate specificity is limited by interactions between substrate amino acids bound in adjacent enzyme subsites. J. Biol. Chem. 271, 4709-4717 (Pubitemid 26074952)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.9 , pp. 4709-4717
    • Ridky, T.W.1    Cameron, C.E.2    Cameron, J.3    Leis, J.4    Copeland, T.5    Wlodawer, A.6    Weber, I.T.7    Harrison, R.W.8
  • 35
    • 77449122863 scopus 로고    scopus 로고
    • Trans-proteomic pipeline: A pipeline for proteomic analysis
    • Pedrioli, P. G. (2010) Trans-proteomic pipeline: a pipeline for proteomic analysis. Methods Mol. Biol. 604, 213-238
    • (2010) Methods Mol. Biol. , vol.604 , pp. 213-238
    • Pedrioli, P.G.1
  • 38
    • 0031473030 scopus 로고    scopus 로고
    • Displaying the information contents of structural RNA alignments: The structure logos
    • Gorodkin, J., Heyer, L. J., Brunak, S., and Stormo, G. D. (1997) Displaying the information contents of structural RNA alignments: the structure logos. Comput. Appl. Biosci. 13, 583-586 (Pubitemid 28039651)
    • (1997) Computer Applications in the Biosciences , vol.13 , Issue.6 , pp. 583-586
    • Gorodkin, J.1    Heyer, L.J.2    Brunak, S.3    Stormo, G.D.4
  • 39
    • 0348062818 scopus 로고    scopus 로고
    • The SWISS-MODEL repository of annotated three-dimensional protein structure homology models
    • Kopp, J., and Schwede, T. (2004) The SWISS-MODEL Repository of annotated three-dimensional protein structure homology models. Nucleic Acids Res. 32, D230-234 (Pubitemid 38081645)
    • (2004) Nucleic Acids Research , vol.32 , Issue.DATABASE ISS.
    • Kopp, J.1    Schwede, T.2
  • 40
  • 44
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • DOI 10.1093/nar/25.24.4876
    • Thompson, J. D., Gibson, T. J., Plewniak, F., Jeanmougin, F., and Higgins, D. G. (1997) The CLUSTAL X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res. 25, 4876-4882 (Pubitemid 28022245)
    • (1997) Nucleic Acids Research , vol.25 , Issue.24 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 46
    • 0041386108 scopus 로고    scopus 로고
    • MrBayes 3: Bayesian phylogenetic inference under mixed models
    • DOI 10.1093/bioinformatics/btg180
    • Ronquist, F., and Huelsenbeck, J. P. (2003) MrBayes 3: Bayesian phylogenetic inference under mixed models. Bioinformatics 19, 1572-1574 (Pubitemid 37038874)
    • (2003) Bioinformatics , vol.19 , Issue.12 , pp. 1572-1574
    • Ronquist, F.1    Huelsenbeck, J.P.2
  • 47
    • 0030203863 scopus 로고    scopus 로고
    • TreeView: An application to display phylogenetic trees on personal computers
    • Page, R. D. (1996) TreeView: an application to display phylogenetic trees on personal computers. Comput. Appl. Biosci. 12, 357-358
    • (1996) Comput. Appl. Biosci. , vol.12 , pp. 357-358
    • Page, R.D.1
  • 48
    • 77951848689 scopus 로고    scopus 로고
    • A statistics-based platform for quantitative N-terminome analysis and identification of protease cleavage products
    • Auf dem Keller, U., Prudova, A., Gioia, M., Butler, G. S., and Overall, C. M. (2010) A statistics-based platform for quantitative N-terminome analysis and identification of protease cleavage products. Mol. Cell Proteomics 9, 912-927
    • (2010) Mol. Cell Proteomics , vol.9 , pp. 912-927
    • Auf Dem Keller, U.1    Prudova, A.2    Gioia, M.3    Butler, G.S.4    Overall, C.M.5
  • 49
    • 0014211618 scopus 로고
    • On the size of the active site in proteases. I. Papain
    • Schechter, I., and Berger, A. (1967) On the size of the active site in proteases. I. Papain. Biochem. Biophys. Res. Commun. 27, 157-162
    • (1967) Biochem. Biophys. Res. Commun. , vol.27 , pp. 157-162
    • Schechter, I.1    Berger, A.2
  • 50
    • 33846821908 scopus 로고    scopus 로고
    • Proteomic discovery of protease substrates
    • DOI 10.1016/j.cbpa.2006.11.037, PII S1367593106001943
    • Schilling, O., and Overall, C. M. (2007) Proteomic discovery of protease substrates. Curr. Opin. Chem. Biol. 11, 36-45 (Pubitemid 46216133)
    • (2007) Current Opinion in Chemical Biology , vol.11 , Issue.1 , pp. 36-45
    • Schilling, O.1    Overall, C.M.2
  • 52
    • 3142701399 scopus 로고    scopus 로고
    • Biosynthetic processing of the pro-alpha1(V)pro-alpha2(V)pro- alpha3(V) procollagen heterotrimer
    • DOI 10.1074/jbc.M402252200
    • Gopalakrishnan, B., Wang, W. M., and Greenspan, D. S. (2004) Biosynthetic processing of the Pro-alpha1(V)Pro-alpha2(V)Pro-alpha3(V) procollagen heterotrimer. J. Biol. Chem. 279, 30904-30912 (Pubitemid 38938027)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.29 , pp. 30904-30912
    • Gopalakrishnan, B.1    Wang, W.-M.2    Greenspan, D.S.3
  • 55
    • 57749105419 scopus 로고    scopus 로고
    • Dentin matrix protein-1 isoforms promote differential cell attachment and migration
    • Von Marschall, Z., and Fisher, L. W. (2008) Dentin matrix protein-1 isoforms promote differential cell attachment and migration. J. Biol. Chem. 283, 32730-32740
    • (2008) J. Biol. Chem. , vol.283 , pp. 32730-32740
    • Von Marschall, Z.1    Fisher, L.W.2
  • 56
    • 78650935427 scopus 로고    scopus 로고
    • Astacin proteases cleave dentin sialophosphoprotein (Dspp) to generate dentin phosphoprotein (Dpp)
    • Tsuchiya, S., Simmer, J. P., Hu, J. C., Richardson, A. S., Yamakoshi, F., and Yamakoshi, Y. (2011) Astacin proteases cleave dentin sialophosphoprotein (Dspp) to generate dentin phosphoprotein (Dpp). J. Bone Mineral Res. 26, 220-228
    • (2011) J. Bone Mineral Res. , vol.26 , pp. 220-228
    • Tsuchiya, S.1    Simmer, J.P.2    Hu, J.C.3    Richardson, A.S.4    Yamakoshi, F.5    Yamakoshi, Y.6
  • 59
    • 77951479269 scopus 로고    scopus 로고
    • Analyzing the protease web in skin: Meprin metalloproteases are activated specifically by KLK4, 5 and 8 vice versa leading to processing of proKLK7 thereby triggering its activation
    • Ohler, A., Debela, M., Wagner, S., Magdolen, V., and Becker-Pauly, C. (2010) Analyzing the protease web in skin: meprin metalloproteases are activated specifically by KLK4, 5 and 8 vice versa leading to processing of proKLK7 thereby triggering its activation. Biol. Chem. 391, 455-460
    • (2010) Biol. Chem. , vol.391 , pp. 455-460
    • Ohler, A.1    Debela, M.2    Wagner, S.3    Magdolen, V.4    Becker-Pauly, C.5
  • 60
    • 70350668613 scopus 로고    scopus 로고
    • Active-site determinants of substrate recognition by the metalloproteinases TACE and ADAM10
    • Caescu, C. I., Jeschke, G. R., and Turk, B. E. (2009) Active-site determinants of substrate recognition by the metalloproteinases TACE and ADAM10. Biochem. J. 424, 79-88
    • (2009) Biochem. J. , vol.424 , pp. 79-88
    • Caescu, C.I.1    Jeschke, G.R.2    Turk, B.E.3
  • 62
    • 0038343128 scopus 로고    scopus 로고
    • 1 specificity for acidic residues and cleaves peptides derived from fibroblast growth factor-23 and matrix extracellular phosphoglycoprotein
    • DOI 10.1042/BJ20030287
    • Campos, M., Couture, C., Hirata, I. Y., Juliano, M. A., Loisel, T. P., Crine, P., Juliano, L., Boileau, G., and Carmona, A. K. (2003) Human recombinant endopeptidase PHEX has a strict S1′ specificity for acidic residues and cleaves peptides derived from fibroblast growth factor-23 and matrix extracellular phosphoglycoprotein. Biochem. J. 373, 271-279 (Pubitemid 36819521)
    • (2003) Biochemical Journal , vol.373 , Issue.1 , pp. 271-279
    • Campos, M.1    Couture, C.2    Hirata, I.Y.3    Juliano, M.A.4    Loisel, T.P.5    Crine, P.6    Juliano, L.7    Boileau, G.8    Carmona, A.K.9
  • 63
    • 0037085233 scopus 로고    scopus 로고
    • Mapping the active site of endothelin-converting enzyme-1 through subsite specificity and mutagenesis studies: A comparison with neprilysin
    • DOI 10.1006/abbi.2001.2708
    • Johnson, G. D., Swenson, H. R., Ramage, R., and Ahn, K. (2002) Mapping the active site of endothelin-converting enzyme-1 through subsite specificity and mutagenesis studies: a comparison with neprilysin. Arch. Biochem. Biophys. 398, 240-248 (Pubitemid 34848591)
    • (2002) Archives of Biochemistry and Biophysics , vol.398 , Issue.2 , pp. 240-248
    • Johnson, G.D.1    Swenson, H.R.2    Ramage, R.3    Ahn, K.4
  • 64
    • 0020008195 scopus 로고
    • A protease from Astacus fluviatilis as an aid in protein sequencing
    • Krauhs, E., Dörsam, H., Little, M., Zwilling, R., and Ponstingl, H. (1982) A protease from Astacus fluviatilis as an aid in protein sequencing. Anal. Biochem. 119, 153-157
    • (1982) Anal. Biochem. , vol.119 , pp. 153-157
    • Krauhs, E.1    Dörsam, H.2    Little, M.3    Zwilling, R.4    Ponstingl, H.5
  • 65
    • 0024996696 scopus 로고
    • Fluorescent oligopeptide substrates for kinetic characterization of the specificity of Astacus protease
    • Stöcker, W., Ng, M., and Auld, D. S. (1990) Fluorescent oligopeptide substrates for kinetic characterization of the specificity of Astacus protease. Biochemistry 29, 10418-10425 (Pubitemid 20384553)
    • (1990) Biochemistry , vol.29 , Issue.45 , pp. 10418-10425
    • Stocker, W.1    Ng, M.2    Auld, D.S.3
  • 66
    • 0032731204 scopus 로고    scopus 로고
    • Purification and characterization of a novel isoform of myosinase from spear squid liver
    • Tamori, J., Kanzawa, N., Tajima, T., Tamiya, T., and Tsuchiya, T. (1999) Purification and characterization of a novel isoform of myosinase from spear squid liver. J Biochem. 126, 969-974
    • (1999) J Biochem. , vol.126 , pp. 969-974
    • Tamori, J.1    Kanzawa, N.2    Tajima, T.3    Tamiya, T.4    Tsuchiya, T.5
  • 67
    • 55949128787 scopus 로고    scopus 로고
    • Purification and characterization of zebrafish hatching enzyme - An evolutionary aspect of the mechanism of egg envelope digestion
    • Sano, K., Inohaya, K., Kawaguchi, M., Yoshizaki, N., Iuchi, I., and Yasumasu, S. (2008) Purification and characterization of zebrafish hatching enzyme - an evolutionary aspect of the mechanism of egg envelope digestion. Febs J. 275, 5934-5946
    • (2008) Febs J. , vol.275 , pp. 5934-5946
    • Sano, K.1    Inohaya, K.2    Kawaguchi, M.3    Yoshizaki, N.4    Iuchi, I.5    Yasumasu, S.6
  • 70
    • 2142738304 scopus 로고    scopus 로고
    • WebLogo: A sequence logo generator
    • DOI 10.1101/gr.849004
    • Crooks, G. E., Hon, G., Chandonia, J. M., and Brenner, S. E. (2004) WebLogo: a sequence logo generator. Genome Res. 14, 1188-1190 (Pubitemid 38811555)
    • (2004) Genome Research , vol.14 , Issue.6 , pp. 1188-1190
    • Crooks, G.E.1    Hon, G.2    Chandonia, J.-M.3    Brenner, S.E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.