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Volumn 270, Issue 24, 2003, Pages 4909-4920

The astacin protein family in Caenorhabditis elegans

Author keywords

Astacin family; Astacus astacus; Caenorhabditis elegans; Metalloproteases; Protein evolution

Indexed keywords

ASTACIN; BONE MORPHOGENETIC PROTEIN; METALLOPROTEINASE;

EID: 17444450739     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1033.2003.03891.x     Document Type: Article
Times cited : (75)

References (66)
  • 1
    • 0014139615 scopus 로고
    • On the evolution of endopeptidases, 3: A protease of molecular weight 11,000 and a trypsin-like fraction from Astacus fluviatilis fabr. Hoppe Seylers
    • Pfleiderer, G., Zwilling, R. & Sonneborn, H.H. (1967) On the evolution of endopeptidases, 3: a protease of molecular weight 11,000 and a trypsin-like fraction from Astacus fluviatilis fabr. Hoppe Seylers. Z. Physiol. Chem. 348, 1319-1331.
    • (1967) Z. Physiol. Chem. , vol.348 , pp. 1319-1331
    • Pfleiderer, G.1    Zwilling, R.2    Sonneborn, H.H.3
  • 2
    • 84945734881 scopus 로고
    • Evolution of endopeptidases. X. Cleavage specificity of low molecular weight protease from Astacus leptodactylus Esch. Hoppe Seylers
    • Sonneborn, H.H., Zwilling, R. & Pfleiderer, G. (1969) Evolution of endopeptidases. X. Cleavage specificity of low molecular weight protease from Astacus leptodactylus Esch. Hoppe Seylers. Z. Physiol. Chem. 350, 1097-1102.
    • (1969) Z. Physiol. Chem. , vol.350 , pp. 1097-1102
    • Sonneborn, H.H.1    Zwilling, R.2    Pfleiderer, G.3
  • 3
    • 0020008195 scopus 로고
    • A protease from Astacus fluviatilis as an aid in protein sequencing
    • Krauhs, E., Dörsam, H., Little, M., Zwilling, R. & 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
  • 4
    • 0019873249 scopus 로고
    • Low molecular mass protease: Evidence for a new family of proteolytic enzymes
    • Zwilling, R., Dörsam, H., Torff, H.-J. & Rödl, J. (1981) Low molecular mass protease: evidence for a new family of proteolytic enzymes. FEBS Lett. 127, 75-78.
    • (1981) FEBS Lett. , vol.127 , pp. 75-78
    • Zwilling, R.1    Dörsam, H.2    Torff, H.-J.3    Rödl, J.4
  • 6
    • 0026736225 scopus 로고
    • Structure of astacin and implications for activation of astacins and zinc-ligation of collagenases
    • Bode, W., Gomis-Rüth, F., Huber, R., Zwilling, R. & Stöcker, W. (1992) Structure of astacin and implications for activation of astacins and zinc-ligation of collagenases. Nature 358, 164-167.
    • (1992) Nature , vol.358 , pp. 164-167
    • Bode, W.1    Gomis-Rüth, F.2    Huber, R.3    Zwilling, R.4    Stöcker, W.5
  • 7
    • 0027418428 scopus 로고
    • Refined 1.8 Å X-ray crystal structure of astacin, a zinc-endopeptidase from the crayfish Astacus astacus L. Structure determination, refinement, molecular structure and comparison with thermolysin
    • Gomis-Rüth, F., Stöcker, W., Huber, R., Zwilling, R. & Bode, W. (1993) Refined 1.8 Å X-ray crystal structure of astacin, a zinc-endopeptidase from the crayfish Astacus astacus L. Structure determination, refinement, molecular structure and comparison with thermolysin. J. Mol. Biol. 229, 945-968.
    • (1993) J. Mol. Biol. , vol.229 , pp. 945-968
    • Gomis-Rüth, F.1    Stöcker, W.2    Huber, R.3    Zwilling, R.4    Bode, W.5
  • 8
    • 0024526399 scopus 로고
    • Biosynthesis of Astacus protease, a digestive enzyme from crayfish
    • Vogt, G., Stöcker, W., Storch, V. & Zwilling, R. (1989) Biosynthesis of Astacus protease, a digestive enzyme from crayfish. Histochemistry 91, 373-381.
    • (1989) Histochemistry , vol.91 , pp. 373-381
    • Vogt, G.1    Stöcker, W.2    Storch, V.3    Zwilling, R.4
  • 10
    • 0034849042 scopus 로고    scopus 로고
    • Activation of pro-astacin: Immunological and model peptide studies on the processing of immature astacin, a zinc-endopeptidase from the crayfish Astacus astacus
    • Möhrlen, F., Baus, S., Gruber, A., Rackwitz, H.R., Schnölzer, M., Vogt, G. & Zwilling, R. (2001) Activation of pro-astacin: immunological and model peptide studies on the processing of immature astacin, a zinc-endopeptidase from the crayfish Astacus astacus. Eur. J. Biochem. 268, 2540-2546.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 2540-2546
    • Möhrlen, F.1    Baus, S.2    Gruber, A.3    Rackwitz, H.R.4    Schnölzer, M.5    Vogt, G.6    Zwilling, R.7
  • 14
    • 0029051493 scopus 로고
    • Molecular cloning and sequence analysis of flavastacin: An O-glycosylated prokaryotic zinc metalloendopeptidase
    • Tarentino, A.L., Quinones, G., Grimwood, B.G., Hauer, C.R. & Plummer, T.H. J. (1995) Molecular cloning and sequence analysis of flavastacin: an O-glycosylated prokaryotic zinc metalloendopeptidase. Arch. Biochem. Biophys. 319, 281-285.
    • (1995) Arch. Biochem. Biophys. , vol.319 , pp. 281-285
    • Tarentino, A.L.1    Quinones, G.2    Grimwood, B.G.3    Hauer, C.R.4    Plummer, T.H.J.5
  • 16
    • 0032079907 scopus 로고    scopus 로고
    • Cloning and characterization of a cDNA coding for Astacus embryonic astacin, a member of the astacin family of metalloproteases from the crayfish Astacus astacus
    • Geier, G. & Zwilling, R. (1998) Cloning and characterization of a cDNA coding for Astacus embryonic astacin, a member of the astacin family of metalloproteases from the crayfish Astacus astacus. Eur. J. Biochem. 253, 796-803.
    • (1998) Eur. J. Biochem. , vol.253 , pp. 796-803
    • Geier, G.1    Zwilling, R.2
  • 19
    • 0001234053 scopus 로고    scopus 로고
    • Aspartyl proteases in Caenorhabditis elegans. Isolation, identification and characterization by a combined use of affinity chromatography, two-dimensional gel electrophoresis, microsequencing and databank analysis
    • Geier, G., Banaj, H.J., Heid, H., Bini, L., Pallini, V. & Zwilling, R. (1999) Aspartyl proteases in Caenorhabditis elegans. Isolation, identification and characterization by a combined use of affinity chromatography, two-dimensional gel electrophoresis, microsequencing and databank analysis. Eur. J. Biochem. 264, 872-879.
    • (1999) Eur. J. Biochem. , vol.264 , pp. 872-879
    • Geier, G.1    Banaj, H.J.2    Heid, H.3    Bini, L.4    Pallini, V.5    Zwilling, R.6
  • 21
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski, P. & Sacchi, N. (1987) Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162, 156-159.
    • (1987) Anal. Biochem. , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 24
    • 0346789754 scopus 로고    scopus 로고
    • 7 March 2003
    • Anonymous (2003) WormBase, release WS 97, 7 March 2003; http://www.wormbase.org
    • (2003) WormBase, Release WS 97
  • 25
    • 0041898654 scopus 로고    scopus 로고
    • Oxford University Press, New York
    • Hope, I.A. (1999) C. Elegans. Oxford University Press, New York.
    • (1999) C. Elegans
    • Hope, I.A.1
  • 29
    • 0029889221 scopus 로고    scopus 로고
    • Local alignment statistics
    • Altschul, S.F. & Gish, W. (1996) Local alignment statistics. Methods Enzymol. 266, 460-480.
    • (1996) Methods Enzymol. , vol.266 , pp. 460-480
    • Altschul, S.F.1    Gish, W.2
  • 31
    • 0033977575 scopus 로고    scopus 로고
    • The intronerator: Exploring introns and alternative splicing in Caenorhabditis elegans
    • Kent, W.J. & Zahler, A.M. (2000) The intronerator: exploring introns and alternative splicing in Caenorhabditis elegans. Nucleic Acids Res. 28, 91-93.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 91-93
    • Kent, W.J.1    Zahler, A.M.2
  • 32
  • 33
    • 0346159157 scopus 로고    scopus 로고
    • 21 March
    • SMART, Version 3.5, 21 March 2001. http://smart.embl-heidel berg.de.
    • (2001) SMART, Version 3.5
  • 37
    • 0346159164 scopus 로고    scopus 로고
    • PHYLIP package 3.5; http://evolution.genetics.washington.edu/ phylip.html.
    • PHYLIP Package 3.5
  • 38
    • 0036806280 scopus 로고    scopus 로고
    • Potential applications and pitfalls of Bayesian inference of phylogeny
    • Huelsenbeck, J.P., Larget, B., Miller, R.E. & Ronquist, F. (2002) Potential applications and pitfalls of Bayesian inference of phylogeny. Syst. Biol. 51, 673-688.
    • (2002) Syst. Biol. , vol.51 , pp. 673-688
    • Huelsenbeck, J.P.1    Larget, B.2    Miller, R.E.3    Ronquist, F.4
  • 39
    • 0035861456 scopus 로고    scopus 로고
    • Bayesian inference of phylogeny and its impact on evolutionary biology
    • Huelsenbeck, J.P., Ronquist, F., Nielsen, R. & Bollback, J.P. (2001) Bayesian inference of phylogeny and its impact on evolutionary biology. Science 294, 2310-2314.
    • (2001) Science , vol.294 , pp. 2310-2314
    • Huelsenbeck, J.P.1    Ronquist, F.2    Nielsen, R.3    Bollback, J.P.4
  • 40
    • 0034849408 scopus 로고    scopus 로고
    • MRBAYES: Bayesian inference of phylogenetic trees
    • Huelsenbeck, J.P. & Ronquist, F. (2001) MRBAYES: Bayesian inference of phylogenetic trees. Bioinformatics 17, 754-755.
    • (2001) Bioinformatics , vol.17 , pp. 754-755
    • Huelsenbeck, J.P.1    Ronquist, F.2
  • 41
    • 0035031966 scopus 로고    scopus 로고
    • A general empirical model of protein evolution derived from multiple protein families using a maximum-likelihood approach
    • Whelan, S. & Goldman, N. (2001) A general empirical model of protein evolution derived from multiple protein families using a maximum-likelihood approach. Mol. Biol. Evol. 18, 691-699.
    • (2001) Mol. Biol. Evol. , vol.18 , pp. 691-699
    • Whelan, S.1    Goldman, N.2
  • 42
    • 0346159162 scopus 로고    scopus 로고
    • TreeView 1.6.6; http://taxonomy.zoology.gla.ac.uk/rod/rod.html.
    • TreeView 1.6.6
  • 43
    • 0032509302 scopus 로고    scopus 로고
    • The C. elegans Sequencing Consortium genome sequence of the nematode C. elegans: A platform for investigating biology
    • C. elegans Sequencing Consortium (1998) The C. elegans Sequencing Consortium genome sequence of the nematode C. elegans: a platform for investigating biology. Science 282, 2012-2018.
    • (1998) Science , vol.282 , pp. 2012-2018
  • 45
    • 0029763234 scopus 로고    scopus 로고
    • hch-1, a gene required for normal hatching and normal migration of a neuroblast in C. elegans, encodes a protein related to TOLLOID and BMP-1
    • Hishida, R., Ishihara, T., Kondo, K. & Katsura, I. (1996) hch-1, a gene required for normal hatching and normal migration of a neuroblast in C. elegans, encodes a protein related to TOLLOID and BMP-1. EMBO J. 15, 4111-4122.
    • (1996) EMBO J. , vol.15 , pp. 4111-4122
    • Hishida, R.1    Ishihara, T.2    Kondo, K.3    Katsura, I.4
  • 49
    • 0037350760 scopus 로고    scopus 로고
    • Composition and dynamics of the Caenorhabditis elegans early embryonic transcriptome
    • Baugh, L.R., Hill, A.A., Slonim, D.K., Brown, E.L. & Hunter, C.P. (2003) Composition and dynamics of the Caenorhabditis elegans early embryonic transcriptome. Development 130, 889-900.
    • (2003) Development , vol.130 , pp. 889-900
    • Baugh, L.R.1    Hill, A.A.2    Slonim, D.K.3    Brown, E.L.4    Hunter, C.P.5
  • 51
    • 0035793050 scopus 로고    scopus 로고
    • Genome-wide analysis of developmental and sex-regulated gene expression profiles in Caenorhabditis elegans
    • Jiang, M., Ryu, J., Kiraly, M., Duke, K., Reinke, V. & Kim, S.K. (2001) Genome-wide analysis of developmental and sex-regulated gene expression profiles in Caenorhabditis elegans. Proc. Natl Acad. Sci. USA 98, 218-223.
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 218-223
    • Jiang, M.1    Ryu, J.2    Kiraly, M.3    Duke, K.4    Reinke, V.5    Kim, S.K.6
  • 54
    • 0035128859 scopus 로고    scopus 로고
    • Large-scale analysis of gene function in Caenorhabditis elegans by high-throughput RNAi
    • Maeda, I., Kohara, Y., Yamamoto, M. & Sugimoto, A. (2001) Large-scale analysis of gene function in Caenorhabditis elegans by high-throughput RNAi. Curr. Biol. 11, 171-176.
    • (2001) Curr. Biol. , vol.11 , pp. 171-176
    • Maeda, I.1    Kohara, Y.2    Yamamoto, M.3    Sugimoto, A.4
  • 55
    • 0035229245 scopus 로고    scopus 로고
    • Effectiveness of specific RNA-mediated interference through ingested double-stranded RNA in Caenorhabditis elegans
    • RESEARCH0002
    • Kamath, R.S., Martinez-Campos, M., Zipperlen, P., Fraser, A.G. & Ahringer, J. (2001) Effectiveness of specific RNA-mediated interference through ingested double-stranded RNA in Caenorhabditis elegans. Genome Biol. 2, RESEARCH0002.
    • (2001) Genome Biol. , vol.2
    • Kamath, R.S.1    Martinez-Campos, M.2    Zipperlen, P.3    Fraser, A.G.4    Ahringer, J.5
  • 58
    • 0037228016 scopus 로고    scopus 로고
    • A systematic RNAi screen identifies a critical role for mitochondria in C. elegans longevity
    • Lee, S.S., Lee, R.Y., Fraser, A.G., Kamath, R.S., Ahringer, J. & Ruvkun, G. (2003) A systematic RNAi screen identifies a critical role for mitochondria in C. elegans longevity. Nat. Genet. 33, 40-48.
    • (2003) Nat. Genet. , vol.33 , pp. 40-48
    • Lee, S.S.1    Lee, R.Y.2    Fraser, A.G.3    Kamath, R.S.4    Ahringer, J.5    Ruvkun, G.6
  • 60
    • 0027287308 scopus 로고
    • Implications of the three-dimensional structure of astacin for the structure and function of the astacin family of zinc-endopeptidases
    • Stöcker, W., Gomis-Rüth, F., Bode, W. & Zwilling, R. (1993) Implications of the three-dimensional structure of astacin for the structure and function of the astacin family of zinc-endopeptidases. Eur. J. Biochem. 214, 215-231.
    • (1993) Eur. J. Biochem. , vol.214 , pp. 215-231
    • Stöcker, W.1    Gomis-Rüth, F.2    Bode, W.3    Zwilling, R.4
  • 61
    • 0034634473 scopus 로고    scopus 로고
    • The roles of Glu93 and Tyr149 in astacin-like zinc peptidases
    • Yiallouros, I., Grosse-Berkhoff, E. & Stöcker, W. (2000) The roles of Glu93 and Tyr149 in astacin-like zinc peptidases. FEBS Lett. 484, 224-228.
    • (2000) FEBS Lett. , vol.484 , pp. 224-228
    • Yiallouros, I.1    Grosse-Berkhoff, E.2    Stöcker, W.3
  • 62
    • 0027190974 scopus 로고
    • The CUB domain: A widespread module in developmentally regulated proteins
    • Bork, P. & Beckmann, G. (1993) The CUB domain: a widespread module in developmentally regulated proteins. J. Mol. Biol. 231, 539-545.
    • (1993) J. Mol. Biol. , vol.231 , pp. 539-545
    • Bork, P.1    Beckmann, G.2
  • 63
    • 0034724260 scopus 로고    scopus 로고
    • Structure and function of procollagen C-proteinase (mTolloid) domains determined by protease digestion, circular dichroism, binding to procollagen type I, and computer modeling
    • Sieron, A.L., Tretiakova, A., Jameson, B.A., Segall, M.L., Lund, K.S., Khan, M.T., Li, S. & Stöcker, W. (2000) Structure and function of procollagen C-proteinase (mTolloid) domains determined by protease digestion, circular dichroism, binding to procollagen type I, and computer modeling. Biochemistry 39, 3231-3239.
    • (2000) Biochemistry , vol.39 , pp. 3231-3239
    • Sieron, A.L.1    Tretiakova, A.2    Jameson, B.A.3    Segall, M.L.4    Lund, K.S.5    Khan, M.T.6    Li, S.7    Stöcker, W.8
  • 64
    • 0029150195 scopus 로고
    • An abundant, trans-spliced mRNA from Toxocara canis infective larvae encodes a 26-kDa protein with homology to phosphatidylethanolamine-binding proteins
    • Gems, D., Ferguson, C.J., Robertson, B.D., Nieves, R., Page, A.P., Blaxter, M.L. & Maizels, R.M. (1995) An abundant, trans-spliced mRNA from Toxocara canis infective larvae encodes a 26-kDa protein with homology to phosphatidylethanolamine-binding proteins. J. Biol. Chem. 270, 18517-18522.
    • (1995) J. Biol. Chem. , vol.270 , pp. 18517-18522
    • Gems, D.1    Ferguson, C.J.2    Robertson, B.D.3    Nieves, R.4    Page, A.P.5    Blaxter, M.L.6    Maizels, R.M.7
  • 65
    • 0032509180 scopus 로고    scopus 로고
    • Caenorhabditis elegans is a nematode
    • Blaxter, M. (1998) Caenorhabditis elegans is a nematode. Science 282, 2041-2046.
    • (1998) Science , vol.282 , pp. 2041-2046
    • Blaxter, M.1


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