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Volumn 364, Issue 4, 2006, Pages 625-636

Serpin1 of Arabidopsis thaliana is a Suicide Inhibitor for Metacaspase 9

Author keywords

Arabidopsis thaliana; cysteine protease; metacaspase; positional scanning peptide substrate libraries; serpin

Indexed keywords

ARGININE; CASPASE 9 INHIBITOR; ISOLEUCINE; LEUCINE; LYSINE; SERINE PROTEINASE INHIBITOR; TETRAPEPTIDE;

EID: 33750942499     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2006.09.010     Document Type: Article
Times cited : (157)

References (66)
  • 1
    • 0033638182 scopus 로고    scopus 로고
    • Identification of paracaspases and metacaspases: two ancient families of caspase-like proteins, one of which plays a key role in MALT lymphoma
    • Uren A.G., O'Rourke K., Aravind L., Pisabarro M.T., Seshagiri S., Koonin E.V., and Dixit V.M. Identification of paracaspases and metacaspases: two ancient families of caspase-like proteins, one of which plays a key role in MALT lymphoma. Mol. Cell 6 (2000) 961-967
    • (2000) Mol. Cell , vol.6 , pp. 961-967
    • Uren, A.G.1    O'Rourke, K.2    Aravind, L.3    Pisabarro, M.T.4    Seshagiri, S.5    Koonin, E.V.6    Dixit, V.M.7
  • 2
    • 28644443666 scopus 로고    scopus 로고
    • Introduction: the clans and families of cysteine peptidases
    • Barrett A.J., Rawlings N.D., and Woessner J.F. (Eds), Elsevier, London
    • Rawlings N.D., and Barrett A.J. Introduction: the clans and families of cysteine peptidases. In: Barrett A.J., Rawlings N.D., and Woessner J.F. (Eds). Handbook of Proteolytic Enzymes. 2nd edit. (2004), Elsevier, London 1051-1071
    • (2004) Handbook of Proteolytic Enzymes. 2nd edit. , pp. 1051-1071
    • Rawlings, N.D.1    Barrett, A.J.2
  • 3
    • 0032885388 scopus 로고    scopus 로고
    • Mammalian caspases: structure, activation, substrates, and functions during apoptosis
    • Earnshaw W.C., Martins L.M., and Kauffmann S.H. Mammalian caspases: structure, activation, substrates, and functions during apoptosis. Annu. Rev. Biochem. 68 (1999) 383-424
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 383-424
    • Earnshaw, W.C.1    Martins, L.M.2    Kauffmann, S.H.3
  • 4
    • 10644282148 scopus 로고    scopus 로고
    • The protein structures that shape caspase activity, specificity, activation and inhibition
    • Fuentes-Prior P., and Salvesen G.S. The protein structures that shape caspase activity, specificity, activation and inhibition. Biochem. J. 384 (2004) 201-232
    • (2004) Biochem. J. , vol.384 , pp. 201-232
    • Fuentes-Prior, P.1    Salvesen, G.S.2
  • 5
    • 0001612653 scopus 로고
    • Vacuolar processing enzyme responsible for maturation of seed proteins
    • Hara-Nishimura I., Shimada T., Hiraiwa N., and Nishimura M. Vacuolar processing enzyme responsible for maturation of seed proteins. J. Plant Physiol. 145 (1995) 632-640
    • (1995) J. Plant Physiol. , vol.145 , pp. 632-640
    • Hara-Nishimura, I.1    Shimada, T.2    Hiraiwa, N.3    Nishimura, M.4
  • 6
    • 25444522319 scopus 로고    scopus 로고
    • Vacuolar processing enzyme is essential for mycotoxin-induced cell death in Arabidopsis thaliana
    • Kuroyanagi M., Yamada K., Hatsugai N., Kondo M., Nishimura M., and Hara-Nishimura I. Vacuolar processing enzyme is essential for mycotoxin-induced cell death in Arabidopsis thaliana. J. Biol. Chem. 280 (2005) 32914-32920
    • (2005) J. Biol. Chem. , vol.280 , pp. 32914-32920
    • Kuroyanagi, M.1    Yamada, K.2    Hatsugai, N.3    Kondo, M.4    Nishimura, M.5    Hara-Nishimura, I.6
  • 7
    • 0033168496 scopus 로고    scopus 로고
    • Sister-chromatid separation at anaphase onset is promoted by cleavage of the cohesin subunit Scc1
    • Uhlmann F., Lottspeich F., and Nasmyth K. Sister-chromatid separation at anaphase onset is promoted by cleavage of the cohesin subunit Scc1. Nature 400 (1999) 37-42
    • (1999) Nature , vol.400 , pp. 37-42
    • Uhlmann, F.1    Lottspeich, F.2    Nasmyth, K.3
  • 8
    • 2342629277 scopus 로고    scopus 로고
    • The TRAF6 ubiquitin ligase and TAK1 kinase mediate IKK activation by BCL10 and MALT1 in T lymphocytes
    • Sun L., Deng L., Ea C.-K., Xia Z.-P., and Chen Z.J. The TRAF6 ubiquitin ligase and TAK1 kinase mediate IKK activation by BCL10 and MALT1 in T lymphocytes. Mol. Cell 14 (2004) 289-301
    • (2004) Mol. Cell , vol.14 , pp. 289-301
    • Sun, L.1    Deng, L.2    Ea, C.-K.3    Xia, Z.-P.4    Chen, Z.J.5
  • 10
    • 8544235061 scopus 로고    scopus 로고
    • Type II metacaspases Atmc4 and Atmc9 of Arabidopsis thaliana cleave substrates after arginine and lysine
    • Vercammen D., van de Cotte B., De Jaeger G., Eeckhout D., Casteels P., Vandepoele K., et al. Type II metacaspases Atmc4 and Atmc9 of Arabidopsis thaliana cleave substrates after arginine and lysine. J. Biol. Chem. 279 (2004) 45329-45336
    • (2004) J. Biol. Chem. , vol.279 , pp. 45329-45336
    • Vercammen, D.1    van de Cotte, B.2    De Jaeger, G.3    Eeckhout, D.4    Casteels, P.5    Vandepoele, K.6
  • 11
    • 17644412048 scopus 로고    scopus 로고
    • Two Arabidopsis metacaspases AtMCP1b and AtMCP2b are arginine/lysine-specific cysteine proteases and activate apoptosis-like cell death in yeast
    • Watanabe N., and Lam E. Two Arabidopsis metacaspases AtMCP1b and AtMCP2b are arginine/lysine-specific cysteine proteases and activate apoptosis-like cell death in yeast. J. Biol. Chem. 280 (2005) 14691-14699
    • (2005) J. Biol. Chem. , vol.280 , pp. 14691-14699
    • Watanabe, N.1    Lam, E.2
  • 13
    • 0041709197 scopus 로고    scopus 로고
    • A tomato metacaspase gene is upregulated during programmed cell death in Botrytis cinerea-infected leaves
    • Hoeberichts F.A., ten Have A., and Woltering E.J. A tomato metacaspase gene is upregulated during programmed cell death in Botrytis cinerea-infected leaves. Planta 217 (2003) 517-522
    • (2003) Planta , vol.217 , pp. 517-522
    • Hoeberichts, F.A.1    ten Have, A.2    Woltering, E.J.3
  • 16
    • 0242432345 scopus 로고    scopus 로고
    • Many cuts to ruin: a comprehensive update of caspase substrates
    • Fischer U., Jänicke R.U., and Schulze-Osthoff K. Many cuts to ruin: a comprehensive update of caspase substrates. Cell Death Differ. 10 (2003) 76-100
    • (2003) Cell Death Differ. , vol.10 , pp. 76-100
    • Fischer, U.1    Jänicke, R.U.2    Schulze-Osthoff, K.3
  • 18
    • 0030849093 scopus 로고    scopus 로고
    • A combinatorial approach defines specificities of members of the caspase family and granzyme B. Functional relationships established for key mediators of apoptosis
    • Thornberry N.A., Rano T.A., Peterson E.P., Rasper D.M., Timkey T., Garcia-Calvo M., et al. A combinatorial approach defines specificities of members of the caspase family and granzyme B. Functional relationships established for key mediators of apoptosis. J. Biol. Chem. 272 (1997) 17907-17911
    • (1997) J. Biol. Chem. , vol.272 , pp. 17907-17911
    • Thornberry, N.A.1    Rano, T.A.2    Peterson, E.P.3    Rasper, D.M.4    Timkey, T.5    Garcia-Calvo, M.6
  • 22
    • 0035860703 scopus 로고    scopus 로고
    • Definition of the extended substrate specificity determinants for β-tryptases I and II
    • Harris J.L., Niles A., Burdick K., Maffitt M., Backes B.J., Ellman J.A., et al. Definition of the extended substrate specificity determinants for β-tryptases I and II. J. Biol. Chem. 276 (2001) 34941-34947
    • (2001) J. Biol. Chem. , vol.276 , pp. 34941-34947
    • Harris, J.L.1    Niles, A.2    Burdick, K.3    Maffitt, M.4    Backes, B.J.5    Ellman, J.A.6
  • 23
    • 23344446921 scopus 로고    scopus 로고
    • Functional profiling of recombinant NS3 proteases from all four serotypes of dengue virus using tetrapeptide and octapeptide substrate libraries
    • Li J., Lim S.P., Beer D., Patel V., Wen D., Tumanut C., et al. Functional profiling of recombinant NS3 proteases from all four serotypes of dengue virus using tetrapeptide and octapeptide substrate libraries. J. Biol. Chem. 280 (2005) 28766-28774
    • (2005) J. Biol. Chem. , vol.280 , pp. 28766-28774
    • Li, J.1    Lim, S.P.2    Beer, D.3    Patel, V.4    Wen, D.5    Tumanut, C.6
  • 24
    • 0034608931 scopus 로고    scopus 로고
    • Rapid and general profiling of protease specificity by using combinatorial fluorogenic substrate libraries
    • Harris J.L., Backes B.J., Leonetti F., Mahrus S., Ellman J.A., and Craik C.S. Rapid and general profiling of protease specificity by using combinatorial fluorogenic substrate libraries. Proc. Natl Acad. Sci. USA 97 (2000) 7754-7759
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 7754-7759
    • Harris, J.L.1    Backes, B.J.2    Leonetti, F.3    Mahrus, S.4    Ellman, J.A.5    Craik, C.S.6
  • 25
    • 20944437268 scopus 로고    scopus 로고
    • High throughput substrate specificity profiling of serine and cysteine proteases using solution-phase fluorogenic peptide microarrays
    • Gosalia D.N., Salisbury C.M., Ellman J.A., and Diamond S.L. High throughput substrate specificity profiling of serine and cysteine proteases using solution-phase fluorogenic peptide microarrays. Mol. Cell. Proteomics 4 (2005) 626-636
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 626-636
    • Gosalia, D.N.1    Salisbury, C.M.2    Ellman, J.A.3    Diamond, S.L.4
  • 27
    • 0033937332 scopus 로고    scopus 로고
    • Serpins and other serine protease inhibitors
    • Patston P.A. Serpins and other serine protease inhibitors. Immunol. Today 21 (2000) 354
    • (2000) Immunol. Today , vol.21 , pp. 354
    • Patston, P.A.1
  • 29
    • 0028955325 scopus 로고
    • Granzyme B is inhibited by the cowpox virus serpin cytokine response modified A
    • Quan L.T., Caputo A., Bleackley R.C., Pickup D.J., and Salvesen G. Granzyme B is inhibited by the cowpox virus serpin cytokine response modified A. J. Biol. Chem. 270 (1995) 10377-10379
    • (1995) J. Biol. Chem. , vol.270 , pp. 10377-10379
    • Quan, L.T.1    Caputo, A.2    Bleackley, R.C.3    Pickup, D.J.4    Salvesen, G.5
  • 30
    • 0028168514 scopus 로고
    • Inhibition of interleukin-1β converting enzyme by the cowpox virus serpin CrmA. An example of cross-class inhibition
    • Komiyama T., Ray C.A., Pickup D.J., Howard A.D., Thornberry N.A., Peterson E.P., and Salvesen G. Inhibition of interleukin-1β converting enzyme by the cowpox virus serpin CrmA. An example of cross-class inhibition. J. Biol. Chem. 269 (1994) 19331-19337
    • (1994) J. Biol. Chem. , vol.269 , pp. 19331-19337
    • Komiyama, T.1    Ray, C.A.2    Pickup, D.J.3    Howard, A.D.4    Thornberry, N.A.5    Peterson, E.P.6    Salvesen, G.7
  • 31
    • 0030977847 scopus 로고    scopus 로고
    • Target protease specificity of the viral serpin CrmA. Analysis of five caspases
    • Zhou Q., Snipas S., Orth K., Muzio M., Dixit V.M., and Salvesen G. Target protease specificity of the viral serpin CrmA. Analysis of five caspases. J. Biol. Chem. 272 (1997) 7797-7800
    • (1997) J. Biol. Chem. , vol.272 , pp. 7797-7800
    • Zhou, Q.1    Snipas, S.2    Orth, K.3    Muzio, M.4    Dixit, V.M.5    Salvesen, G.6
  • 33
    • 0034526511 scopus 로고    scopus 로고
    • Keeping the serpin machine running smoothly
    • Gettins P.G.W. Keeping the serpin machine running smoothly. Genome Res. 10 (2000) 1833-1835
    • (2000) Genome Res. , vol.10 , pp. 1833-1835
    • Gettins, P.G.W.1
  • 34
    • 0034687422 scopus 로고    scopus 로고
    • Structure of a serpin-protease complex shows inhibition by deformation
    • Huntington J.A., Read R.J., and Carrell R.W. Structure of a serpin-protease complex shows inhibition by deformation. Nature 407 (2000) 923-926
    • (2000) Nature , vol.407 , pp. 923-926
    • Huntington, J.A.1    Read, R.J.2    Carrell, R.W.3
  • 35
  • 36
    • 0034523345 scopus 로고    scopus 로고
    • Phylogeny of the serpin superfamily: implications of patterns of amino acid conservation for structure and function
    • Irving J.A., Pike R.N., Lesk A.M., and Whisstock J.C. Phylogeny of the serpin superfamily: implications of patterns of amino acid conservation for structure and function. Genome Res. 10 (2000) 1845-1864
    • (2000) Genome Res. , vol.10 , pp. 1845-1864
    • Irving, J.A.1    Pike, R.N.2    Lesk, A.M.3    Whisstock, J.C.4
  • 37
    • 0035823595 scopus 로고    scopus 로고
    • The serpins are an expanding superfamily of structurally similar but functionally diverse proteins. Evolution, mechanism of inhibition, novel functions, and a revised nomenclature
    • Silverman G.A., Bird P.I., Carrell R.W., Church F.C., Coughlin P.B., Gettins P.G.W., et al. The serpins are an expanding superfamily of structurally similar but functionally diverse proteins. Evolution, mechanism of inhibition, novel functions, and a revised nomenclature. J. Biol. Chem. 276 (2001) 33293-33296
    • (2001) J. Biol. Chem. , vol.276 , pp. 33293-33296
    • Silverman, G.A.1    Bird, P.I.2    Carrell, R.W.3    Church, F.C.4    Coughlin, P.B.5    Gettins, P.G.W.6
  • 38
    • 0027182969 scopus 로고
    • Effects of mutations in the hinge region of serpins
    • Hopkins P.C., Carrell R.W., and Stone S.R. Effects of mutations in the hinge region of serpins. Biochemistry 32 (1993) 7650-7657
    • (1993) Biochemistry , vol.32 , pp. 7650-7657
    • Hopkins, P.C.1    Carrell, R.W.2    Stone, S.R.3
  • 39
    • 0027398809 scopus 로고
    • A gene coding for a new plant serpin
    • Rasmussen S.K. A gene coding for a new plant serpin. Biochim. Biophys. Acta 1172 (1993) 151-154
    • (1993) Biochim. Biophys. Acta , vol.1172 , pp. 151-154
    • Rasmussen, S.K.1
  • 40
    • 0030591752 scopus 로고    scopus 로고
    • Primary structure of the plant serpin BSZ7 having the capacity of chymotrypsin inhibition
    • Rasmussen S.K., Klausen J., Hejgaard J., Svensson B., and Svendsen I. Primary structure of the plant serpin BSZ7 having the capacity of chymotrypsin inhibition. Biochim. Biophys. Acta 1297 (1996) 127-130
    • (1996) Biochim. Biophys. Acta , vol.1297 , pp. 127-130
    • Rasmussen, S.K.1    Klausen, J.2    Hejgaard, J.3    Svensson, B.4    Svendsen, I.5
  • 41
    • 0034721763 scopus 로고    scopus 로고
    • Inhibitory serpins from wheat grain with reactive centers resembling glutamine-rich repeats of prolamin storage proteins. Cloning and characterization of five major molecular forms
    • Østergaard H., Rasmussen S.K., Roberts T.H., and Hejgaard J. Inhibitory serpins from wheat grain with reactive centers resembling glutamine-rich repeats of prolamin storage proteins. Cloning and characterization of five major molecular forms. J. Biol. Chem. 275 (2000) 33272-33279
    • (2000) J. Biol. Chem. , vol.275 , pp. 33272-33279
    • Østergaard, H.1    Rasmussen, S.K.2    Roberts, T.H.3    Hejgaard, J.4
  • 43
    • 0034634617 scopus 로고    scopus 로고
    • Characterization of Cucurbita maxima phloem serpin-1 (CmPS-1). A developmentally regulated elastase inhibitor
    • Yoo B.-C., Aoki K., Xiang Y., Campbell L.R., Hull R.J., Xoconostle-Cázares B., et al. Characterization of Cucurbita maxima phloem serpin-1 (CmPS-1). A developmentally regulated elastase inhibitor. J. Biol. Chem. 275 (2000) 35122-35128
    • (2000) J. Biol. Chem. , vol.275 , pp. 35122-35128
    • Yoo, B.-C.1    Aoki, K.2    Xiang, Y.3    Campbell, L.R.4    Hull, R.J.5    Xoconostle-Cázares, B.6
  • 44
    • 0033555707 scopus 로고    scopus 로고
    • Inhibition of apoptosis and clonogenic survival of cells expressing crmA variants: optimal caspase substrates are not necessarily optimal inhibitors
    • Ekert P.G., Silke J., and Vaux D.L. Inhibition of apoptosis and clonogenic survival of cells expressing crmA variants: optimal caspase substrates are not necessarily optimal inhibitors. EMBO J. 18 (1999) 330-338
    • (1999) EMBO J. , vol.18 , pp. 330-338
    • Ekert, P.G.1    Silke, J.2    Vaux, D.L.3
  • 46
    • 4644303690 scopus 로고    scopus 로고
    • Death proteases come alive
    • Woltering E.J. Death proteases come alive. Trends Plant Sci. 9 (2004) 469-472
    • (2004) Trends Plant Sci. , vol.9 , pp. 469-472
    • Woltering, E.J.1
  • 47
    • 0032970657 scopus 로고    scopus 로고
    • Vacuolar processing enzyme is self-catalytically activated by sequential removal of the C-terminal and N-terminal propeptides
    • Hiraiwa N., Nishimura M., and Hara-Nishimura I. Vacuolar processing enzyme is self-catalytically activated by sequential removal of the C-terminal and N-terminal propeptides. FEBS Letters 447 (1999) 213-216
    • (1999) FEBS Letters , vol.447 , pp. 213-216
    • Hiraiwa, N.1    Nishimura, M.2    Hara-Nishimura, I.3
  • 48
    • 0141755165 scopus 로고    scopus 로고
    • Multistep autoactivation of asparaginyl endopeptidase in vitro and in vivo
    • Li D.N., Matthews S.P., Antoniou A.N., Mazzeo D., and Watts C. Multistep autoactivation of asparaginyl endopeptidase in vitro and in vivo. J. Biol. Chem. 278 (2003) 38980-38990
    • (2003) J. Biol. Chem. , vol.278 , pp. 38980-38990
    • Li, D.N.1    Matthews, S.P.2    Antoniou, A.N.3    Mazzeo, D.4    Watts, C.5
  • 50
    • 1842712632 scopus 로고    scopus 로고
    • Purification and characterization of serine proteases that exhibit caspase-like activity and are associated with programmed cell death in Avena sativa
    • Coffeen W.C., and Wolpert T.J. Purification and characterization of serine proteases that exhibit caspase-like activity and are associated with programmed cell death in Avena sativa. Plant Cell 16 (2004) 857-873
    • (2004) Plant Cell , vol.16 , pp. 857-873
    • Coffeen, W.C.1    Wolpert, T.J.2
  • 52
    • 84986958895 scopus 로고
    • Purification and properties of protein Z - a major albumin of barley endosperm
    • Hejgaard J. Purification and properties of protein Z - a major albumin of barley endosperm. Physiol. Plant. 54 (1982) 174-182
    • (1982) Physiol. Plant. , vol.54 , pp. 174-182
    • Hejgaard, J.1
  • 53
    • 0024797319 scopus 로고
    • A 39 kD barley seed protein of the serpin superfamily inhibits alpha-chymotrypsin
    • Lundgard R., and Svensson B. A 39 kD barley seed protein of the serpin superfamily inhibits alpha-chymotrypsin. Carlsberg Res. Commun. 54 (1989) 173-180
    • (1989) Carlsberg Res. Commun. , vol.54 , pp. 173-180
    • Lundgard, R.1    Svensson, B.2
  • 56
    • 0029815085 scopus 로고    scopus 로고
    • Heterologous expression of three plant serpins with distinct inhibitory specificities
    • Dahl S., Rasmussen S.K., and Hejgaard J. Heterologous expression of three plant serpins with distinct inhibitory specificities. J. Biol. Chem. 271 (1996) 25083-25088
    • (1996) J. Biol. Chem. , vol.271 , pp. 25083-25088
    • Dahl, S.1    Rasmussen, S.K.2    Hejgaard, J.3
  • 57
    • 0035910448 scopus 로고    scopus 로고
    • 2 residues in the reactive center
    • 2 residues in the reactive center. FEBS Letters 488 (2001) 149-153
    • (2001) FEBS Letters , vol.488 , pp. 149-153
    • Hejgaard, J.1
  • 58
    • 0036787709 scopus 로고    scopus 로고
    • Serpins of oat (Avena sativa) grain with distinct reactive centres and inhibitory specificity
    • Hejgaard J., and Hauge S. Serpins of oat (Avena sativa) grain with distinct reactive centres and inhibitory specificity. Physiol. Plant. 116 (2002) 155-163
    • (2002) Physiol. Plant. , vol.116 , pp. 155-163
    • Hejgaard, J.1    Hauge, S.2
  • 59
    • 0141907260 scopus 로고    scopus 로고
    • Differential gene expression for suicide-substrate serine proteinase inhibitors (serpins) in vegetative and grain tissues of barley
    • Roberts T.H., Marttila S., Rasmussen S.K., and Hejgaard J. Differential gene expression for suicide-substrate serine proteinase inhibitors (serpins) in vegetative and grain tissues of barley. J. Exp. Bot. 54 (2003) 2251-2263
    • (2003) J. Exp. Bot. , vol.54 , pp. 2251-2263
    • Roberts, T.H.1    Marttila, S.2    Rasmussen, S.K.3    Hejgaard, J.4
  • 60
    • 0036581417 scopus 로고    scopus 로고
    • GATEWAY™ vectors for Agrobacterium-mediated plant transformation
    • Karimi M., Inzé D., and Depicker A. GATEWAY™ vectors for Agrobacterium-mediated plant transformation. Trends Plant Sci. 7 (2002) 193-195
    • (2002) Trends Plant Sci. , vol.7 , pp. 193-195
    • Karimi, M.1    Inzé, D.2    Depicker, A.3
  • 61
    • 0032447801 scopus 로고    scopus 로고
    • Floral dip: a simplified method for Agrobacterium-mediated transformation of Arabidopsis thaliana
    • Clough S.J., and Bent A.F. Floral dip: a simplified method for Agrobacterium-mediated transformation of Arabidopsis thaliana. Plant J. 16 (1998) 735-743
    • (1998) Plant J. , vol.16 , pp. 735-743
    • Clough, S.J.1    Bent, A.F.2
  • 62
    • 0030455820 scopus 로고    scopus 로고
    • Genomic libraries and a host strain designed for highly efficient two-hybrid selection in yeast
    • James P., Halladay J., and Craig E.A. Genomic libraries and a host strain designed for highly efficient two-hybrid selection in yeast. Genetics 144 (1996) 1425-1436
    • (1996) Genetics , vol.144 , pp. 1425-1436
    • James, P.1    Halladay, J.2    Craig, E.A.3
  • 63
    • 0027291015 scopus 로고
    • Prediction of protein secondary structure at better than 70% accuracy
    • Rost B., and Sander C. Prediction of protein secondary structure at better than 70% accuracy. J. Mol. Biol. 232 (1993) 584-599
    • (1993) J. Mol. Biol. , vol.232 , pp. 584-599
    • Rost, B.1    Sander, C.2
  • 65
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson J.D., Gibson T.J., Plewniak F., Jeanmougin F., and Higgins D.G. The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res. 25 (1997) 4876-4882
    • (1997) Nucleic Acids Res. , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5


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