메뉴 건너뛰기




Volumn , Issue , 2006, Pages 37-59

Regulation of TGF-ß family activity by proprotein processing

Author keywords

[No Author keywords available]

Indexed keywords


EID: 85056652904     PISSN: None     EISSN: None     Source Type: Book    
DOI: None     Document Type: Chapter
Times cited : (2)

References (72)
  • 1
    • 0038461962 scopus 로고    scopus 로고
    • Curbing activation: Proprotein convertases in homeostasis and pathology
    • Taylor, N. A., Van De Ven, W. J., Creemers, J. W., Curbing activation: proprotein convertases in homeostasis and pathology. Faseb, 17, 1215-27, 2003.
    • (2003) Faseb , vol.17 , pp. 1215-1227
    • Taylor, N.A.1    Van De Ven, W.J.2    Creemers, J.W.3
  • 2
    • 0038682002 scopus 로고    scopus 로고
    • Mechanisms of TGF-beta signaling from cell membrane to the nucleus
    • Shi, Y., Massague, J., Mechanisms of TGF-beta signaling from cell membrane to the nucleus. Cell, 113, 685-700, 2003.
    • (2003) Cell , vol.113 , pp. 685-700
    • Shi, Y.1    Massague, J.2
  • 3
    • 0029737070 scopus 로고    scopus 로고
    • Bone morphogenetic proteins: Multifunctional regulators of vertebrate development
    • Hogan, B. L., Bone morphogenetic proteins: multifunctional regulators of vertebrate development. Genes Dev, 10, 1580-94, 1996.
    • (1996) Genes Dev , vol.10 , pp. 1580-1594
    • Hogan, B.L.1
  • 4
    • 0029148342 scopus 로고
    • Ventral mesodermal patterning in Xenopus embryos: Expression patterns and activities of BMP-2 and BMP-4
    • Hemmati-Brivanlou, A., Thomsen, G. H., Ventral mesodermal patterning in Xenopus embryos: expression patterns and activities of BMP-2 and BMP-4. Dev Gene, 17, 78-89, 1995.
    • (1995) Dev Gene , vol.17 , pp. 78-89
    • Hemmati-Brivanlou, A.1    Thomsen, G.H.2
  • 5
    • 0029143953 scopus 로고
    • Bone morphogenetic protein 2 in the early development of Xenopus laevis
    • Clement, J. H., Fettes, P., Knochel, S., Lef, J., Knochel, W., Bone morphogenetic protein 2 in the early development of Xenopus laevis. Mech Dev, 52, 357-70, 1995.
    • (1995) Mech Dev , vol.52 , pp. 357-370
    • Clement, J.H.1    Fettes, P.2    Knochel, S.3    Lef, J.4    Knochel, W.5
  • 6
    • 0033625428 scopus 로고    scopus 로고
    • Endogenous patterns of TGFbeta superfamily signaling during early Xenopus development
    • Faure, S., Lee, M. A., Keller, T., ten Dijke, P., Whitman, M., Endogenous patterns of TGFbeta superfamily signaling during early Xenopus development. Development, 127, 2917-31, 2000.
    • (2000) Development , vol.127 , pp. 2917-2931
    • Faure, S.1    Lee, M.A.2    Keller, T.3    ten Dijke, P.4    Whitman, M.5
  • 7
    • 0035141275 scopus 로고    scopus 로고
    • Visualization of endogenous BMP signaling during Xenopus development
    • Kurata, T., Nakabayashi, J., Yamamoto, T., Mochii, M., Ueno, N., Visualization of endogenous BMP signaling during Xenopus development. Differentiation, 67, 33-30, 2000.
    • (2000) Differentiation , vol.67 , pp. 33-30
    • Kurata, T.1    Nakabayashi, J.2    Yamamoto, T.3    Mochii, M.4    Ueno, N.5
  • 8
    • 0035498979 scopus 로고    scopus 로고
    • The activity and signaling range of mature BMP-4 is regulated by sequential cleavage at two sites within the prodomain of the precursor
    • Cui, Y., Hackenmiller, R., Berg, L., Jean, F., Nakayama, T., Thomas, G., Christian, J. L., The activity and signaling range of mature BMP-4 is regulated by sequential cleavage at two sites within the prodomain of the precursor. Genes Dev, 15, 2797-802, 2001.
    • (2001) Genes Dev , vol.15 , pp. 2797-2802
    • Cui, Y.1    Hackenmiller, R.2    Berg, L.3    Jean, F.4    Nakayama, T.5    Thomas, G.6    Christian, J.L.7
  • 10
    • 20744448964 scopus 로고    scopus 로고
    • Proprotein convertase genes in Xenopus development
    • Nelsen, S., Berg, L., Wong, C., Christian, J. L., Proprotein convertase genes in Xenopus development. Dev Dyn, 233, 1038-14, 2005.
    • (2005) Dev Dyn , vol.233 , pp. 1038-1014
    • Nelsen, S.1    Berg, L.2    Wong, C.3    Christian, J.L.4
  • 11
    • 0032541405 scopus 로고    scopus 로고
    • BMP-4 is proteolytically activated by furin and/or PC6 during vertebrate embryonic development
    • Cui, Y., Jean, F., Thomas, G., Christian, J. L., BMP-4 is proteolytically activated by furin and/or PC6 during vertebrate embryonic development. Embo J, 17, 4735-13, 1998.
    • (1998) Embo J , vol.17 , pp. 4735-4713
    • Cui, Y.1    Jean, F.2    Thomas, G.3    Christian, J.L.4
  • 12
    • 6344272882 scopus 로고    scopus 로고
    • Cleavages within the prodomain direct intracellular trafficking and degradation of mature BMP-4
    • Degnin, C., Jean, F., Thomas, G., Christian, J. L., Cleavages within the prodomain direct intracellular trafficking and degradation of mature BMP-4. Mol Biol Cell, 11, 5012-20, 2004.
    • (2004) Mol Biol Cell , vol.11 , pp. 5012-5020
    • Degnin, C.1    Jean, F.2    Thomas, G.3    Christian, J.L.4
  • 13
    • 33745094372 scopus 로고    scopus 로고
    • Mutation of an upstream cleavage site in the BMP4 prodomain leads to tissue-specific loss of activity
    • Goldman, D., Hackenmiller, R., Nakayama, T., Sopory, S., Wong, C., Kulessa, H., and Christian, J. L, Mutation of an upstream cleavage site in the BMP4 prodomain leads to tissue-specific loss of activity. Development, 133, 1933-12.
    • Development , vol.133 , pp. 1933-1912
    • Goldman, D.1    Hackenmiller, R.2    Nakayama, T.3    Sopory, S.4    Wong, C.5    Kulessa, H.6    Christian, J.L.7
  • 14
    • 0035512155 scopus 로고    scopus 로고
    • Nodal signaling in early vertebrate embryos: Themes and variations
    • Whitman, M., Nodal signaling in early vertebrate embryos: themes and variations. Dev Cell, 1, 605-17, 2001.
    • (2001) Dev Cell , vol.1 , pp. 605-617
    • Whitman, M.1
  • 15
    • 0025373853 scopus 로고
    • Requirement for activin A and transforming growth factor-beta 1 pro-regions in homodimer assembly
    • Gray, A. M., Mason, A. J., Requirement for activin A and transforming growth factor-beta 1 pro-regions in homodimer assembly. Science, 247, 1328-30, 1990.
    • (1990) Science , vol.247 , pp. 1328-1330
    • Gray, A.M.1    Mason, A.J.2
  • 18
    • 0036791359 scopus 로고    scopus 로고
    • Furin at the cutting edge: From protein traffic to embryogenesis and disease
    • Thomas, G., Furin at the cutting edge: from protein traffic to embryogenesis and disease. Nat Rev Mol Cell Biol, 3, 753-66, 2002.
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 753-766
    • Thomas, G.1
  • 19
    • 0037066315 scopus 로고    scopus 로고
    • The ordered and compartment-specific autoproteolytic removal of the furin intramolecular chaperone is required for enzyme activation
    • Anderson, E. D., Molloy, S. S., Jean, F., Fei, H., Shimamura, S., Thomas, G., The ordered and compartment-specific autoproteolytic removal of the furin intramolecular chaperone is required for enzyme activation. J Biol Chem, 277, 12879-90, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 12879-12890
    • Anderson, E.D.1    Molloy, S.S.2    Jean, F.3    Fei, H.4    Shimamura, S.5    Thomas, G.6
  • 20
    • 0032560533 scopus 로고    scopus 로고
    • A model for the structure of the P domains in the subtilisin-like prohormone convertases
    • Lipkind, G. M., Zhou, A., Steiner, D. F., A model for the structure of the P domains in the subtilisin-like prohormone convertases. Proc Natl Acad Sci U S A, 95, 7310-15, 1998.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 7310-7315
    • Lipkind, G.M.1    Zhou, A.2    Steiner, D.F.3
  • 21
    • 0032080254 scopus 로고    scopus 로고
    • Regulatory roles of the P domain of the subtilisin-like prohormone convertases
    • Zhou, A., Martin, S., Lipkind, G., LaMendola, J., Steiner, D. F., Regulatory roles of the P domain of the subtilisin-like prohormone convertases. J Biol Chem, 273, (18), 11107-14, 1998.
    • (1998) J Biol Chem , vol.273 , Issue.18 , pp. 11107-11114
    • Zhou, A.1    Martin, S.2    Lipkind, G.3    LaMendola, J.4    Steiner, D.F.5
  • 22
    • 0026801571 scopus 로고
    • Cloning and functional expression of Dfurin2, a subtilisin-like proprotein processing enzyme of Drosophila melanogaster with multiple repeats of a cysteine motif
    • Roebroek, A. J., Creemers, J. W., Pauli, I. G., Kurzik-Dumke, U., Rentrop, M., Gateff, E. A., Leunissen, J. A., Van de Ven, W. J., Cloning and functional expression of Dfurin2, a subtilisin-like proprotein processing enzyme of Drosophila melanogaster with multiple repeats of a cysteine motif. J Biol Chem, 267, 17208-15, 1992.
    • (1992) J Biol Chem , vol.267 , pp. 17208-17215
    • Roebroek, A.J.1    Creemers, J.W.2    Pauli, I.G.3    Kurzik-Dumke, U.4    Rentrop, M.5    Gateff, E.A.6    Leunissen, J.A.7    Van de Ven, W.J.8
  • 24
    • 0034077580 scopus 로고    scopus 로고
    • The PC6B cytoplasmic domain contains two acidic clusters that direct sorting to distinct trans-Golgi network/endosomal compartments
    • Xiang, Y., Molloy, S. S., Thomas, L., Thomas, G., The PC6B cytoplasmic domain contains two acidic clusters that direct sorting to distinct trans-Golgi network/endosomal compartments. Mol Biol Cell, 11, 1257-73, 2000.
    • (2000) Mol Biol Cell , vol.11 , pp. 1257-1273
    • Xiang, Y.1    Molloy, S.S.2    Thomas, L.3    Thomas, G.4
  • 26
    • 0026785385 scopus 로고
    • Testicular expression of PC4 in the rat: Molecular diversity of a novel germ cell-specific Kex2/subtilisin-like proprotein convertase
    • Seidah, N. G., Day, R., Hamelin, J., Gaspar, A., Collard, M. W., Chretien, M., Testicular expression of PC4 in the rat: molecular diversity of a novel germ cell-specific Kex2/subtilisin-like proprotein convertase. Mol Endocrinol, 6, 1559-70, 1992.
    • (1992) Mol Endocrinol , vol.6 , pp. 1559-1570
    • Seidah, N.G.1    Day, R.2    Hamelin, J.3    Gaspar, A.4    Collard, M.W.5    Chretien, M.6
  • 27
    • 0026660354 scopus 로고
    • Identification of the fourth member of the mammalian endoprotease family homologous to the yeast Kex2 protease. Its testis-specific expression
    • Nakayama, K., Kim, W. S., Torii, S., Hosaka, M., Nakagawa, T., Ikemizu, J., Baba, T., Murakami, K., Identification of the fourth member of the mammalian endoprotease family homologous to the yeast Kex2 protease. Its testis-specific expression. J Biol Chem, 267, 5897-900, 1992.
    • (1992) J Biol Chem , vol.267 , pp. 5897-5900
    • Nakayama, K.1    Kim, W.S.2    Torii, S.3    Hosaka, M.4    Nakagawa, T.5    Ikemizu, J.6    Baba, T.7    Murakami, K.8
  • 28
    • 0030048594 scopus 로고    scopus 로고
    • Furin/PACE/SPC1: A convertase involved in exocytic and endocytic processing of precursor proteins
    • Denault, J. B., Leduc, R., Furin/PACE/SPC1: a convertase involved in exocytic and endocytic processing of precursor proteins. FEBS Lett, 379, 113-16, 1996.
    • (1996) FEBS Lett , vol.379 , pp. 113-116
    • Denault, J.B.1    Leduc, R.2
  • 29
    • 0033597852 scopus 로고    scopus 로고
    • Proteolytic processing in the secretory pathway
    • Zhou, A., Webb, G., Zhu, X., Steiner, D. F., Proteolytic processing in the secretory pathway. J Biol Chem, 274, 20745-48, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 20745-20748
    • Zhou, A.1    Webb, G.2    Zhu, X.3    Steiner, D.F.4
  • 30
    • 0027295514 scopus 로고
    • Characterization of a secreted form of human furin endoprotease
    • Vidricaire, G., Denault, J. B., Leduc, R., Characterization of a secreted form of human furin endoprotease. Biochem Biophys Res Commun, 195, 1011-18, 1993.
    • (1993) Biochem Biophys Res Commun , vol.195 , pp. 1011-1018
    • Vidricaire, G.1    Denault, J.B.2    Leduc, R.3
  • 31
    • 0030605010 scopus 로고    scopus 로고
    • Functional analysis of human PACE4-A and PACE4-C isoforms: Identification of a new PACE4-CS isoform
    • Zhong, M., Benjannet, S., Lazure, C., Munzer, S., Seidah, N. G., Functional analysis of human PACE4-A and PACE4-C isoforms: identification of a new PACE4-CS isoform. FEBS Lett, 396, 31-36, 1996.
    • (1996) FEBS Lett , vol.396 , pp. 31-36
    • Zhong, M.1    Benjannet, S.2    Lazure, C.3    Munzer, S.4    Seidah, N.G.5
  • 32
    • 0037474206 scopus 로고    scopus 로고
    • Secretory proprotein convertases PACE4 and PC6A are heparin-binding proteins which are localized in the extracellular matrix. Potential role of PACE4 in the activation of proproteins in the extracellular matrix
    • Tsuji, A., Sakurai, K., Kiyokage, E., Yamazaki, T., Koide, S., Toida, K., Ishimura, K., Matsuda, Y., Secretory proprotein convertases PACE4 and PC6A are heparin-binding proteins which are localized in the extracellular matrix. Potential role of PACE4 in the activation of proproteins in the extracellular matrix. Biochim Biophys Acta, 1645, 95-104, 2003.
    • (2003) Biochim Biophys Acta , vol.1645 , pp. 95-104
    • Tsuji, A.1    Sakurai, K.2    Kiyokage, E.3    Yamazaki, T.4    Koide, S.5    Toida, K.6    Ishimura, K.7    Matsuda, Y.8
  • 33
    • 0035877007 scopus 로고    scopus 로고
    • Processing of immunosuppressive pro-TGF-beta 1,2 by human glioblastoma cells involves cytoplasmic and secreted furin-like proteases
    • Leitlein, J., Aulwurm, S., Waltereit, R., Naumann, U., Wagenknecht, B., Garten, W., Weller, M., Platten, M., Processing of immunosuppressive pro-TGF-beta 1,2 by human glioblastoma cells involves cytoplasmic and secreted furin-like proteases. J Immunol, 166, 7238-43, 2001.
    • (2001) J Immunol , vol.166 , pp. 7238-7243
    • Leitlein, J.1    Aulwurm, S.2    Waltereit, R.3    Naumann, U.4    Wagenknecht, B.5    Garten, W.6    Weller, M.7    Platten, M.8
  • 34
    • 0033545215 scopus 로고    scopus 로고
    • Regulation of bone morphogenetic protein activity by pro domains and proprotein convertases
    • Constam, D. B., Robertson, E. J., Regulation of bone morphogenetic protein activity by pro domains and proprotein convertases. J Cell Biol, 144, 139-49, 1999.
    • (1999) J Cell Biol , vol.144 , pp. 139-149
    • Constam, D.B.1    Robertson, E.J.2
  • 35
    • 0026775916 scopus 로고
    • Human furin is a calcium-dependent serine endoprotease that recognizes the sequence Arg-X-X-Arg and efficiently cleaves anthrax toxin protective antigen
    • Molloy, S. S., Bresnahan, P. A., Leppla, S. H., Klimpel, K. R., Thomas, G., Human furin is a calcium-dependent serine endoprotease that recognizes the sequence Arg-X-X-Arg and efficiently cleaves anthrax toxin protective antigen. J Biol Chem, 267, 16396-402, 1992.
    • (1992) J Biol Chem , vol.267 , pp. 16396-16402
    • Molloy, S.S.1    Bresnahan, P.A.2    Leppla, S.H.3    Klimpel, K.R.4    Thomas, G.5
  • 36
    • 0028157148 scopus 로고
    • Sequence specificity of furin, a proprotein-processing endoprotease, for the hemagglutinin of a virulent avian influenza virus
    • Walker, J. A., Molloy, S. S., Thomas, G., Sakaguchi, T., Yoshida, T., Chambers, T. M., Kawaoka, Y., Sequence specificity of furin, a proprotein-processing endoprotease, for the hemagglutinin of a virulent avian influenza virus. J Virol, 68, 1213-18, 1994.
    • (1994) J Virol , vol.68 , pp. 1213-1218
    • Walker, J.A.1    Molloy, S.S.2    Thomas, G.3    Sakaguchi, T.4    Yoshida, T.5    Chambers, T.M.6    Kawaoka, Y.7
  • 37
    • 0033551805 scopus 로고    scopus 로고
    • Quantitative characterization of furin specificity. Energetics of substrate discrimination using an internally consistent set of hexapeptidyl methylcoumarinamides
    • Krysan, D. J., Rockwell, N. C., Fuller, R. S., Quantitative characterization of furin specificity. Energetics of substrate discrimination using an internally consistent set of hexapeptidyl methylcoumarinamides. J Biol Chem, 274, 23229-34, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 23229-23234
    • Krysan, D.J.1    Rockwell, N.C.2    Fuller, R.S.3
  • 39
    • 9644281041 scopus 로고    scopus 로고
    • Proprotein convertase models based on the crystal structures of furin and kexin: Explanation of their specificity
    • Henrich, S., Lindberg, I., Bode, W., Than, M. E., Proprotein convertase models based on the crystal structures of furin and kexin: explanation of their specificity. J Mol Biol, 345, 211-27, 2005.
    • (2005) J Mol Biol , vol.345 , pp. 211-227
    • Henrich, S.1    Lindberg, I.2    Bode, W.3    Than, M.E.4
  • 40
    • 0030808665 scopus 로고    scopus 로고
    • Biosynthesis, distinct post-translational modifications, and functional characterization of lymphoma proprotein convertase
    • van de Loo, J. W., Creemers, J. W., Bright, N. A., Young, B. D., Roebroek, A. J., Van de Ven, W. J., Biosynthesis, distinct post-translational modifications, and functional characterization of lymphoma proprotein convertase. J Biol Chem, 272, 27116-23, 1997.
    • (1997) J Biol Chem , vol.272 , pp. 27116-27123
    • van de Loo, J.W.1    Creemers, J.W.2    Bright, N.A.3    Young, B.D.4    Roebroek, A.J.5    Van de Ven, W.J.6
  • 41
    • 0029946619 scopus 로고    scopus 로고
    • SPC4, SPC6, and the novel protease SPC7 are coexpressed with bone morphogenetic proteins at distinct sites during embryogenesis
    • Constam, D. B., Calfon, M., Robertson, E. J., SPC4, SPC6, and the novel protease SPC7 are coexpressed with bone morphogenetic proteins at distinct sites during embryogenesis. J Cell Biol, 134, 181-91, 1996.
    • (1996) J Cell Biol , vol.134 , pp. 181-191
    • Constam, D.B.1    Calfon, M.2    Robertson, E.J.3
  • 43
    • 0028124241 scopus 로고
    • The developmental expression in rat of proteases furin, PC1, PC2, and carboxypeptidase E: Implications for early maturation of proteolytic processing capacity
    • Zheng, M., Streck, R. D., Scott, R. E., Seidah, N. G., Pintar, J. E., The developmental expression in rat of proteases furin, PC1, PC2, and carboxypeptidase E: implications for early maturation of proteolytic processing capacity. J Neurosci, 14, 4656-73, 1994.
    • (1994) J Neurosci , vol.14 , pp. 4656-4673
    • Zheng, M.1    Streck, R.D.2    Scott, R.E.3    Seidah, N.G.4    Pintar, J.E.5
  • 44
    • 0027968515 scopus 로고
    • The tissue distribution of mRNAs for the PACE4 isoforms, kexin-like processing protease: PACE4C and PACE4D mRNAs are major transcripts among PACE4 isoforms
    • Tsuji, A., Mori, K., Hine, C., Tamai, Y., Nagamune, H., Matsuda, Y., The tissue distribution of mRNAs for the PACE4 isoforms, kexin-like processing protease: PACE4C and PACE4D mRNAs are major transcripts among PACE4 isoforms. Biochem Biophys Res Commun, 202, 1215-21, 1994.
    • (1994) Biochem Biophys Res Commun , vol.202 , pp. 1215-1221
    • Tsuji, A.1    Mori, K.2    Hine, C.3    Tamai, Y.4    Nagamune, H.5    Matsuda, Y.6
  • 45
    • 0030920027 scopus 로고    scopus 로고
    • A novel human PACE4 isoform, PACE4E is an active processing protease containing a hydrophobic cluster at the carboxy terminus
    • Mori, K., Kii, S., Tsuji, A., Nagahama, M., Imamaki, A., Hayashi, K., Akamatsu, T., Nagamune, H., Matsuda, Y., A novel human PACE4 isoform, PACE4E is an active processing protease containing a hydrophobic cluster at the carboxy terminus. J Biochem (Tokyo), 121, 941-48, 1997.
    • (1997) J Biochem (Tokyo) , vol.121 , pp. 941-948
    • Mori, K.1    Kii, S.2    Tsuji, A.3    Nagahama, M.4    Imamaki, A.5    Hayashi, K.6    Akamatsu, T.7    Nagamune, H.8    Matsuda, Y.9
  • 46
    • 14044273683 scopus 로고    scopus 로고
    • XPACE4 is a localized pro-protein convertase required for mesoderm induction and the cleavage of specific TGF-B proteins in Xenopus development
    • Birsoy, B., Berg, L., Williams, P. H., Smith, J. C., Wylie, C. C., Christian, J. L., Heasman, J., XPACE4 is a localized pro-protein convertase required for mesoderm induction and the cleavage of specific TGF-B proteins in Xenopus development. Development, 132, 591-602, 2005.
    • (2005) Development , vol.132 , pp. 591-602
    • Birsoy, B.1    Berg, L.2    Williams, P.H.3    Smith, J.C.4    Wylie, C.C.5    Christian, J.L.6    Heasman, J.7
  • 47
    • 0027296764 scopus 로고
    • Identification of an isoform with an extremely large Cys-rich region of PC6, a Kex2-like processing endoprotease
    • Nakagawa, T., Murakami, K., Nakayama, K., Identification of an isoform with an extremely large Cys-rich region of PC6, a Kex2-like processing endoprotease. FEBS Lett, 327, 165-71, 1993.
    • (1993) FEBS Lett , vol.327 , pp. 165-171
    • Nakagawa, T.1    Murakami, K.2    Nakayama, K.3
  • 48
    • 0027274628 scopus 로고
    • CDNA structure of the mouse and rat subtilisin/kexin-like PC5: A candidate proprotein convertase expressed in endocrine and nonendocrine cells
    • Lusson, J., Vieau, D., Hamelin, J., Day, R., Chretien, M., Seidah, N. G., cDNA structure of the mouse and rat subtilisin/kexin-like PC5: a candidate proprotein convertase expressed in endocrine and nonendocrine cells. Proc Natl Acad Sci U S A, 90, 6691-95, 1993.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 6691-6695
    • Lusson, J.1    Vieau, D.2    Hamelin, J.3    Day, R.4    Chretien, M.5    Seidah, N.G.6
  • 49
    • 0027965348 scopus 로고
    • The family of subtilisin/kexin like pro-protein and pro-hormone convertases: Divergent or shared functions
    • Seidah, N. G., Chretien, M., Day, R., The family of subtilisin/kexin like pro-protein and pro-hormone convertases: divergent or shared functions. Biochimie, 76, 197-209, 1994.
    • (1994) Biochimie , vol.76 , pp. 197-209
    • Seidah, N.G.1    Chretien, M.2    Day, R.3
  • 50
    • 0029135124 scopus 로고
    • Fluorescent peptidyl substrates as an aid in studying the substrate specificity of human prohormone convertase PC1 and human furin and designing a potent irreversible inhibitor
    • Jean, F., Boudreault, A., Basak, A., Seidah, N. G., Lazure, C., Fluorescent peptidyl substrates as an aid in studying the substrate specificity of human prohormone convertase PC1 and human furin and designing a potent irreversible inhibitor. J Biol Chem, 270, 19225-31, 1995.
    • (1995) J Biol Chem , vol.270 , pp. 19225-19231
    • Jean, F.1    Boudreault, A.2    Basak, A.3    Seidah, N.G.4    Lazure, C.5
  • 51
    • 0018388950 scopus 로고
    • Intramolecularly quenched fluorogenic substrates for hydrolytic enzymes
    • Yaron, A., Carmel, A., Katchalski-Katzir, E., Intramolecularly quenched fluorogenic substrates for hydrolytic enzymes. Anal Biochem, 95, 228-35, 1979.
    • (1979) Anal Biochem , vol.95 , pp. 228-235
    • Yaron, A.1    Carmel, A.2    Katchalski-Katzir, E.3
  • 53
    • 0032560449 scopus 로고    scopus 로고
    • Alpha1-Antitrypsin Portland, a bioengineered serpin highly selective for furin: Application as an antipathogenic agent
    • Jean, F., Stella, K., Thomas, L., Liu, G., Xiang, Y., Reason, A. J., Thomas, G., Alpha1-Antitrypsin Portland, a bioengineered serpin highly selective for furin: application as an antipathogenic agent. Proc Natl Acad Sci U S A, 95, 7293-98, 1998.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 7293-7298
    • Jean, F.1    Stella, K.2    Thomas, L.3    Liu, G.4    Xiang, Y.5    Reason, A.J.6    Thomas, G.7
  • 54
    • 0035253151 scopus 로고    scopus 로고
    • Implication of the proprotein convertases furin, PC5 and PC7 in the cleavage of surface glycoproteins of Hong Kong, Ebola and respiratory syncytial viruses: A comparative analysis with fluorogenic peptides
    • Basak, A., Zhong, M., Munzer, J. S., Chretien, M., Seidah, N. G., Implication of the proprotein convertases furin, PC5 and PC7 in the cleavage of surface glycoproteins of Hong Kong, Ebola and respiratory syncytial viruses: a comparative analysis with fluorogenic peptides. Biochem J, 353, 537-15, 2001.
    • (2001) Biochem J , vol.353 , pp. 537-515
    • Basak, A.1    Zhong, M.2    Munzer, J.S.3    Chretien, M.4    Seidah, N.G.5
  • 55
    • 0030725756 scopus 로고    scopus 로고
    • Furin: A mammalian subtilisin/Kex2p-like endoprotease involved in processing of a wide variety of precursor proteins
    • Nakayama, K., Furin: a mammalian subtilisin/Kex2p-like endoprotease involved in processing of a wide variety of precursor proteins. Biochem. J., 327, 625-35, 1997.
    • (1997) Biochem. J , vol.327 , pp. 625-635
    • Nakayama, K.1
  • 57
    • 10744224233 scopus 로고    scopus 로고
    • Endoproteolytic activation of alpha(v) integrin by proprotein convertase PC5 is required for vascular smooth muscle cell adhesion to vitronectin and integrin-dependent signaling
    • Stawowy, P., Kallisch, H., Veinot, J. P., Kilimnik, A., Prichett, W., Goetze, S., Seidah, N. G., Chretien, M., Fleck, E., Graf, K., Endoproteolytic activation of alpha(v) integrin by proprotein convertase PC5 is required for vascular smooth muscle cell adhesion to vitronectin and integrin-dependent signaling. Circulation, 109, 770-76, 2004.
    • (2004) Circulation , vol.109 , pp. 770-776
    • Stawowy, P.1    Kallisch, H.2    Veinot, J.P.3    Kilimnik, A.4    Prichett, W.5    Goetze, S.6    Seidah, N.G.7    Chretien, M.8    Fleck, E.9    Graf, K.10
  • 59
    • 0033952923 scopus 로고    scopus 로고
    • Tissue-specific requirements for the proprotein convertase furin/SPC1 during embryonic turning and heart looping
    • Constam, D. B., Robertson, E. J., Tissue-specific requirements for the proprotein convertase furin/SPC1 during embryonic turning and heart looping. Development, 127, 245-54, 2000.
    • (2000) Development , vol.127 , pp. 245-254
    • Constam, D.B.1    Robertson, E.J.2
  • 62
    • 0027429771 scopus 로고
    • Inhibition of HIV-1 gp160-dependent membrane fusion by a furin-directed alpha 1-antitrypsin variant
    • Anderson, E. D., Thomas, L., Hayflick, J. S., Thomas, G., Inhibition of HIV-1 gp160-dependent membrane fusion by a furin-directed alpha 1-antitrypsin variant. J Biol Chem, 268, 24887-91, 1993.
    • (1993) J Biol Chem , vol.268 , pp. 24887-24891
    • Anderson, E.D.1    Thomas, L.2    Hayflick, J.S.3    Thomas, G.4
  • 63
    • 0036010133 scopus 로고    scopus 로고
    • Development of selectivity of alpha1-antitrypsin variant by mutagenesis in its reactive site loop against proprotein convertase. A crucial role of the P4 arginine in PACE4 inhibition
    • Tsuji, A., Ikoma, T., Hashimoto, E., Matsuda, Y., Development of selectivity of alpha1-antitrypsin variant by mutagenesis in its reactive site loop against proprotein convertase. A crucial role of the P4 arginine in PACE4 inhibition. Protein Eng, 15, 123-30, 2002.
    • (2002) Protein Eng , vol.15 , pp. 123-130
    • Tsuji, A.1    Ikoma, T.2    Hashimoto, E.3    Matsuda, Y.4
  • 64
    • 3042639565 scopus 로고    scopus 로고
    • Drosophila serpin 4 functions as a neuroserpin-like inhibitor of subtilisin-like proprotein convertases
    • Osterwalder, T., Kuhnen, A., Leiserson, W. M., Kim, Y. S., Keshishian, H., Drosophila serpin 4 functions as a neuroserpin-like inhibitor of subtilisin-like proprotein convertases. J Neurosci, 24, 5482-91, 2004.
    • (2004) J Neurosci , vol.24 , pp. 5482-5491
    • Osterwalder, T.1    Kuhnen, A.2    Leiserson, W.M.3    Kim, Y.S.4    Keshishian, H.5
  • 66
    • 0026289508 scopus 로고
    • Fertilization of cultured Xenopus oocytes and use in studies of maternally inherited molecules
    • Heasman, J., Holwill, S., Wylie, C. C., Fertilization of cultured Xenopus oocytes and use in studies of maternally inherited molecules. Methods Cell Biol, 36, 213-30, 1991.
    • (1991) Methods Cell Biol , vol.36 , pp. 213-230
    • Heasman, J.1    Holwill, S.2    Wylie, C.C.3
  • 68
    • 0028787260 scopus 로고
    • Nodal-related signals induce axial mesoderm and dorsalize mesoderm during gastrulation
    • Jones, C. M., Kuehn, M. R., Hogan, B. L. M., Smith, J. C., Wright, C. V. E., Nodal-related signals induce axial mesoderm and dorsalize mesoderm during gastrulation. Development, 121, 3651-62, 1995.
    • (1995) Development , vol.121 , pp. 3651-3662
    • Jones, C.M.1    Kuehn, M.R.2    Hogan, B.L.M.3    Smith, J.C.4    Wright, C.V.E.5
  • 69
    • 0032773058 scopus 로고    scopus 로고
    • Xenopus nodal-related signaling is essential for mesendodermal patterning during early embryogenesis
    • Osada, S. I., Wright, C. V., Xenopus nodal-related signaling is essential for mesendodermal patterning during early embryogenesis. Development, 126, 3229-40, 1999.
    • (1999) Development , vol.126 , pp. 3229-3240
    • Osada, S.I.1    Wright, C.V.2
  • 70
    • 0034642235 scopus 로고    scopus 로고
    • Engineered eglin c variants inhibit yeast and human proprotein processing proteases, Kex2 and furin
    • Komiyama, T., Fuller, R. S., Engineered eglin c variants inhibit yeast and human proprotein processing proteases, Kex2 and furin. Biochemistry, 39, 15156-65, 2000.
    • (2000) Biochemistry , vol.39 , pp. 15156-15165
    • Komiyama, T.1    Fuller, R.S.2
  • 71
    • 0036515170 scopus 로고    scopus 로고
    • Production, purification, and characterization of recombinant prohormone convertase 5 from baculovirus-infected insect cells
    • Cain, B. M., Vishnuvardhan, D., Wang, W., Foulon, T., Cadel, S., Cohen, P., Beinfeld, M. C., Production, purification, and characterization of recombinant prohormone convertase 5 from baculovirus-infected insect cells. Protein Expr Purif, 24, 227-33, 2002.
    • (2002) Protein Expr Purif , vol.24 , pp. 227-233
    • Cain, B.M.1    Vishnuvardhan, D.2    Wang, W.3    Foulon, T.4    Cadel, S.5    Cohen, P.6    Beinfeld, M.C.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.