메뉴 건너뛰기




Volumn 3, Issue , 2013, Pages 3331-3337

Sedolisin

Author keywords

[No Author keywords available]

Indexed keywords


EID: 84884850128     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-0-12-382219-2.00735-3     Document Type: Chapter
Times cited : (1)

References (53)
  • 1
    • 0037779903 scopus 로고    scopus 로고
    • Structural and enzymatic properties of the sedolisin family of serine-carboxyl peptidases
    • Wlodawer A., Li M., Gustchina A., Oyama H., Dunn B.M., Oda K. Structural and enzymatic properties of the sedolisin family of serine-carboxyl peptidases. Acta Biochemica Plonica 2003, 50:81-102.
    • (2003) Acta Biochemica Plonica , vol.50 , pp. 81-102
    • Wlodawer, A.1    Li, M.2    Gustchina, A.3    Oyama, H.4    Dunn, B.M.5    Oda, K.6
  • 2
    • 0002663359 scopus 로고
    • Aspartic proteinases and their inhibitors
    • Walter de Gruyter, Belin, V. Kostka (Ed.)
    • Kay J. Aspartic proteinases and their inhibitors. Aspartic Proteinases and Their Inhibitors 1985, 1-17. Walter de Gruyter, Belin. V. Kostka (Ed.).
    • (1985) Aspartic Proteinases and Their Inhibitors , pp. 1-17
    • Kay, J.1
  • 3
    • 0006097121 scopus 로고
    • Pepstatin-insensitive acid proteases
    • Walter de Gruyter, Berlin, V. Kostka (Ed.)
    • Murao S., Oda K. Pepstatin-insensitive acid proteases. Aspartic Proteinase and Their Inhibitors 1985, 379-399. Walter de Gruyter, Berlin. V. Kostka (Ed.).
    • (1985) Aspartic Proteinase and Their Inhibitors , pp. 379-399
    • Murao, S.1    Oda, K.2
  • 4
    • 0026317864 scopus 로고
    • Pestatin-insensitive carboxyl proteinases
    • Plenum Press, New York, B. Dunn (Ed.)
    • Oda K., Murao S. Pestatin-insensitive carboxyl proteinases. Structure and Function of the Aspartic Proteinases 1991, 185-201. Plenum Press, New York. B. Dunn (Ed.).
    • (1991) Structure and Function of the Aspartic Proteinases , pp. 185-201
    • Oda, K.1    Murao, S.2
  • 6
    • 0031919526 scopus 로고    scopus 로고
    • Pepstatin-insensitive carboxyl proteinases from prokaryotes Catalytic residues and substrate specificities
    • Plenum Press, New York, M.N.G. James (Ed.)
    • Oda K., Takahashi S., Ito M., Dunn B.M. Pepstatin-insensitive carboxyl proteinases from prokaryotes Catalytic residues and substrate specificities. Aspartic Proteinases 1998, 349-353. Plenum Press, New York. M.N.G. James (Ed.).
    • (1998) Aspartic Proteinases , pp. 349-353
    • Oda, K.1    Takahashi, S.2    Ito, M.3    Dunn, B.M.4
  • 7
    • 0001464924 scopus 로고
    • New pepsin inhibitors (S-PI) from Streptomyces EF-44-201. Agric
    • Murao S., Satoi S. New pepsin inhibitors (S-PI) from Streptomyces EF-44-201. Agric. Biol. Chem. 1970, 34:1265-1267.
    • (1970) Biol. Chem. , vol.34 , pp. 1265-1267
    • Murao, S.1    Satoi, S.2
  • 9
    • 0014027980 scopus 로고
    • The inactivation of pepsin by diazoacetyl-norleucine methyl ester
    • Rajagopalan T.G., Stein W.H., Moore S. The inactivation of pepsin by diazoacetyl-norleucine methyl ester. J. Biol. Chem. 1966, 241:4295-4297.
    • (1966) J. Biol. Chem. , vol.241 , pp. 4295-4297
    • Rajagopalan, T.G.1    Stein, W.H.2    Moore, S.3
  • 10
    • 0015239836 scopus 로고
    • Specific and irreversible inactivation of pepsin by substrate-like expoxides
    • Tang J. Specific and irreversible inactivation of pepsin by substrate-like expoxides. J. Biol. Chem. 1971, 246:4510-4517.
    • (1971) J. Biol. Chem. , vol.246 , pp. 4510-4517
    • Tang, J.1
  • 12
    • 84954976476 scopus 로고
    • New acid proteases from Scytalidium lignicolum M-133
    • Murao S., Oda K., Matsushita Y. New acid proteases from Scytalidium lignicolum M-133. Agric. Biol. Chem. 1972, 36:1647-1650.
    • (1972) Agric. Biol. Chem. , vol.36 , pp. 1647-1650
    • Murao, S.1    Oda, K.2    Matsushita, Y.3
  • 13
    • 84998498632 scopus 로고
    • Isolation and identification of a microorganism which produces non-Streptomyces pepsin inhibitor and N-diazoacetyl-DL-norleucine methylester sensitive acid proteases
    • Murao S., Oda K., Matsushita Y. Isolation and identification of a microorganism which produces non-Streptomyces pepsin inhibitor and N-diazoacetyl-DL-norleucine methylester sensitive acid proteases. Agric. Biol. Chem. 1973, 37:1417-1421.
    • (1973) Agric. Biol. Chem. , vol.37 , pp. 1417-1421
    • Murao, S.1    Oda, K.2    Matsushita, Y.3
  • 14
    • 0016153960 scopus 로고
    • Purification and some properties of acid protease A and B of Scytalidium lignicolum ATCC 24568
    • Oda K., Murao S. Purification and some properties of acid protease A and B of Scytalidium lignicolum ATCC 24568. Agric. Biol. Chem. 1974, 38:2435-2444.
    • (1974) Agric. Biol. Chem. , vol.38 , pp. 2435-2444
    • Oda, K.1    Murao, S.2
  • 15
    • 0000954429 scopus 로고
    • Purification and characterization of acid proteinase C of Scytalidium lignicolum ATCC 24568
    • Oda K., Torishima H., Murao S. Purification and characterization of acid proteinase C of Scytalidium lignicolum ATCC 24568. Agric. Biol. Chem. 1986, 50:651-658.
    • (1986) Agric. Biol. Chem. , vol.50 , pp. 651-658
    • Oda, K.1    Torishima, H.2    Murao, S.3
  • 16
    • 0007932957 scopus 로고
    • Some physicochemical properties and substrate specificity of acid protease B of Scytalidium lignicolum ATCC 24568. Agric
    • Oda K., Murao S., Oka T., Morihara K. Some physicochemical properties and substrate specificity of acid protease B of Scytalidium lignicolum ATCC 24568. Agric. Biol. Chem. 1975, 39:477-484.
    • (1975) Biol. Chem. , vol.39 , pp. 477-484
    • Oda, K.1    Murao, S.2    Oka, T.3    Morihara, K.4
  • 17
    • 0007924467 scopus 로고
    • Some physicochemical properties and substrate specificities of acid proteases A-1 and A-2 of Scytalidium lignicolum ATCC 24568
    • Oda K., Murao S., Oka T., Morihara K. Some physicochemical properties and substrate specificities of acid proteases A-1 and A-2 of Scytalidium lignicolum ATCC 24568. Agric. Biol. Chem 1976, 40:859-866.
    • (1976) Agric. Biol. Chem , vol.40 , pp. 859-866
    • Oda, K.1    Murao, S.2    Oka, T.3    Morihara, K.4
  • 18
    • 0018452208 scopus 로고
    • Pepstatin-insensitive acid proteases from Scytalidium lignicolum. Kinetic study with synthetic peptides
    • Morihara K., Tsuzuki H., Murao S., Oda K. Pepstatin-insensitive acid proteases from Scytalidium lignicolum. Kinetic study with synthetic peptides. J. Biochem. (Tokyo) 1979, 85:661-668.
    • (1979) J. Biochem. (Tokyo) , vol.85 , pp. 661-668
    • Morihara, K.1    Tsuzuki, H.2    Murao, S.3    Oda, K.4
  • 19
    • 0345541896 scopus 로고
    • Comparative specificity of microbial acid proteinases
    • Mladinska Knjiga-Pergamon Press, Ljubljana, Oxford, V. Turk, L.J. Vitale (Eds.)
    • Morihara K. Comparative specificity of microbial acid proteinases. Proteinases and Their inhibitors: Structure, Function, and Applied Aspects 1981, 213-222. Mladinska Knjiga-Pergamon Press, Ljubljana, Oxford. V. Turk, L.J. Vitale (Eds.).
    • (1981) Proteinases and Their inhibitors: Structure, Function, and Applied Aspects , pp. 213-222
    • Morihara, K.1
  • 20
    • 0007877133 scopus 로고
    • Action of Scytalidium lignicolum acid proteases on insulin B-chain. Agric
    • Oda K., Murao S. Action of Scytalidium lignicolum acid proteases on insulin B-chain. Agric. Biol. Chem. 1976, 40:1221-1225.
    • (1976) Biol. Chem. , vol.40 , pp. 1221-1225
    • Oda, K.1    Murao, S.2
  • 21
    • 85004455867 scopus 로고
    • Comparative study on the specificities of several fungal aspartic and acidic proteinases towards the tetradecapeptide of a rennin substrate
    • Majima E., Oda K., Murao S., Ichishima E. Comparative study on the specificities of several fungal aspartic and acidic proteinases towards the tetradecapeptide of a rennin substrate. Agric. Biol. Chem. 1988, 52:787-793.
    • (1988) Agric. Biol. Chem. , vol.52 , pp. 787-793
    • Majima, E.1    Oda, K.2    Murao, S.3    Ichishima, E.4
  • 23
    • 0017042829 scopus 로고
    • Effects of acid protease-specific inhibitors on the acid proteases from Aspergillus niger var. macrosporus
    • Chang W.J., Horiuchi S., Takahashi K., Yamasaki M., Yamada Y. Effects of acid protease-specific inhibitors on the acid proteases from Aspergillus niger var. macrosporus. J. Biochem. (Tokyo) 1976, 80:975-981.
    • (1976) J. Biochem. (Tokyo) , vol.80 , pp. 975-981
    • Chang, W.J.1    Horiuchi, S.2    Takahashi, K.3    Yamasaki, M.4    Yamada, Y.5
  • 24
    • 0007876427 scopus 로고
    • Occurrence of Streptomyces pepsin inhibitor-insensitive carboxyl proteinase in Basidiomycetes. Agric
    • Oda K., Terashita T., Kono M., Murao S. Occurrence of Streptomyces pepsin inhibitor-insensitive carboxyl proteinase in Basidiomycetes. Agric. Biol. Chem. 1981, 45:2339-2340.
    • (1981) Biol. Chem. , vol.45 , pp. 2339-2340
    • Oda, K.1    Terashita, T.2    Kono, M.3    Murao, S.4
  • 25
    • 84953967145 scopus 로고
    • Streptomyces pepsin inhibitor-insensitive carboxyl proteinase from Lentinus edodes. Agric
    • Terashita T., Oda K., Kono M., Murao S. Streptomyces pepsin inhibitor-insensitive carboxyl proteinase from Lentinus edodes. Agric. Biol. Chem. 1981, 45:1937-1943.
    • (1981) Biol. Chem. , vol.45 , pp. 1937-1943
    • Terashita, T.1    Oda, K.2    Kono, M.3    Murao, S.4
  • 26
    • 84953965833 scopus 로고
    • Streptomyces pepsin inhibitor-insensitive carboxyl proteinase from Ganoderma lucidum. Agric
    • Terashita T., Oda K., Kono M., Murao S. Streptomyces pepsin inhibitor-insensitive carboxyl proteinase from Ganoderma lucidum. Agric. Biol. Chem. 1984, 48:1029-1035.
    • (1984) Biol. Chem. , vol.48 , pp. 1029-1035
    • Terashita, T.1    Oda, K.2    Kono, M.3    Murao, S.4
  • 27
    • 0007877365 scopus 로고
    • Purification and characterization of pepstatin-insensitive carboxyl proteinase from Polyporus tulipiferae (Irpex lacteus). Agric
    • Kobayashi H., Kusakabe I., Murakami K. Purification and characterization of pepstatin-insensitive carboxyl proteinase from Polyporus tulipiferae (Irpex lacteus). Agric. Biol. Chem. 1985, 49:2393-2397.
    • (1985) Biol. Chem. , vol.49 , pp. 2393-2397
    • Kobayashi, H.1    Kusakabe, I.2    Murakami, K.3
  • 28
    • 0023154620 scopus 로고
    • Purification and properties of a pepstatin-insensitive carboxyl proteinase from a gram-negative bacterium
    • Oda K., Sugitani M., Fukuhara K., Murao S. Purification and properties of a pepstatin-insensitive carboxyl proteinase from a gram-negative bacterium. Biochim. Biophys. Acta 1987, 923:463-469.
    • (1987) Biochim. Biophys. Acta , vol.923 , pp. 463-469
    • Oda, K.1    Sugitani, M.2    Fukuhara, K.3    Murao, S.4
  • 29
    • 85010093042 scopus 로고
    • Purification and properties of an S-PI (Pepstatin Ac)-insensitive carboxyl proteinase from a Xanthomonas sp. Bacterium
    • Oda K., Nakazima T., Terashita T., Suzuki K., Murao S. Purification and properties of an S-PI (Pepstatin Ac)-insensitive carboxyl proteinase from a Xanthomonas sp. Bacterium. Agric. Biol. Chem. 1987, 51:3073-3080.
    • (1987) Agric. Biol. Chem. , vol.51 , pp. 3073-3080
    • Oda, K.1    Nakazima, T.2    Terashita, T.3    Suzuki, K.4    Murao, S.5
  • 30
    • 0000077693 scopus 로고
    • A novel thermostable, S-PI (pepstatin Ac)-insensitive acid proteinase from thermophilic Bacillus novosp. strain MN-32
    • Murao S., Ohkuni K., Nagao M., Oda K., Shin T. A novel thermostable, S-PI (pepstatin Ac)-insensitive acid proteinase from thermophilic Bacillus novosp. strain MN-32. Agric. Biol. Chem. 1988, 52:1629-1631.
    • (1988) Agric. Biol. Chem. , vol.52 , pp. 1629-1631
    • Murao, S.1    Ohkuni, K.2    Nagao, M.3    Oda, K.4    Shin, T.5
  • 31
    • 0027446449 scopus 로고
    • Purification and characterization of kumamolysin, a novel thermostable pepstatin-insensitive carboxyl proteinase from Bacillus novosp. MN-32
    • Murao S., Ohkuni K., Nagao M., Hirayama K., Fukuhara K., Oda K., Oyama H., Shin T. Purification and characterization of kumamolysin, a novel thermostable pepstatin-insensitive carboxyl proteinase from Bacillus novosp. MN-32. J. Biol. Chem. 1993, 268:349-355.
    • (1993) J. Biol. Chem. , vol.268 , pp. 349-355
    • Murao, S.1    Ohkuni, K.2    Nagao, M.3    Hirayama, K.4    Fukuhara, K.5    Oda, K.6    Oyama, H.7    Shin, T.8
  • 32
    • 0029002927 scopus 로고
    • A pepstatin-insensitive aspartic proteinases from a thermophilic Bacillus sp
    • Toogood H.S., Prescott M., Daniel R.M. A pepstatin-insensitive aspartic proteinases from a thermophilic Bacillus sp. Biochem. J. 1995, 307:783-789.
    • (1995) Biochem. J. , vol.307 , pp. 783-789
    • Toogood, H.S.1    Prescott, M.2    Daniel, R.M.3
  • 33
    • 0029146134 scopus 로고
    • Characterization of a thermostable pepstatin-insensitive acid proteinase from a Bacillus sp
    • Prescott M., Peek K., Daniel R.M. Characterization of a thermostable pepstatin-insensitive acid proteinase from a Bacillus sp. Int. J. Biochem. (Tokyo) Cell Biol. 1995, 27:729-739.
    • (1995) Int. J. Biochem. (Tokyo) Cell Biol. , vol.27 , pp. 729-739
    • Prescott, M.1    Peek, K.2    Daniel, R.M.3
  • 36
    • 0031719820 scopus 로고    scopus 로고
    • Substrate specificity of pepstatin-insensitive carboxyl proteinase from Bacillus coagulans J-4
    • Shibata M., Dunn B.M., Oda K. Substrate specificity of pepstatin-insensitive carboxyl proteinase from Bacillus coagulans J-4. J. Biochem. (Tokyo) 1998, 124:642-647.
    • (1998) J. Biochem. (Tokyo) , vol.124 , pp. 642-647
    • Shibata, M.1    Dunn, B.M.2    Oda, K.3
  • 37
    • 0030866233 scopus 로고    scopus 로고
    • Association of mutations in a lysosomal protein with classical late-infantile neuronal ceroid lipofuscinosis
    • Sleat D.E., Donnelly R.J., Lackland H., Liu C.G., Sohar I., Pullarkat R.K., Lobel P. Association of mutations in a lysosomal protein with classical late-infantile neuronal ceroid lipofuscinosis. Science 1997, 277:1802-1805.
    • (1997) Science , vol.277 , pp. 1802-1805
    • Sleat, D.E.1    Donnelly, R.J.2    Lackland, H.3    Liu, C.G.4    Sohar, I.5    Pullarkat, R.K.6    Lobel, P.7
  • 38
    • 0000367534 scopus 로고    scopus 로고
    • Pepstatin-insensitive carboxyl proteinases: A biochemical marker for late lysosomes in Amoeba proteus
    • Kwon H.K., Kim H., Ahn T.I. Pepstatin-insensitive carboxyl proteinases: A biochemical marker for late lysosomes in Amoeba proteus. Korean J. Biol. Sci. 1999, 3:221-228.
    • (1999) Korean J. Biol. Sci. , vol.3 , pp. 221-228
    • Kwon, H.K.1    Kim, H.2    Ahn, T.I.3
  • 39
    • 1542723495 scopus 로고    scopus 로고
    • The molecular structure and catalytic mechanism of a novel carboxyl peptidase from Scytalidium lignicolum
    • Fujinaga M., Chernev M.M., Oyama H., Oda K., James M.N.G. The molecular structure and catalytic mechanism of a novel carboxyl peptidase from Scytalidium lignicolum. Proc. Natl. Acad. Sci. USA 2004, 101:3364-3369.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 3364-3369
    • Fujinaga, M.1    Chernev, M.M.2    Oyama, H.3    Oda, K.4    James, M.N.G.5
  • 40
    • 20444398543 scopus 로고    scopus 로고
    • Catalytic residues and substrate specificity of scytalidoglutamic peptidase, the first member of the eqolisin in family (G1) of peptidases
    • Kataoka Y., Takada K., Oyama H., Tsunemi M., James M.N.G., Oda K. Catalytic residues and substrate specificity of scytalidoglutamic peptidase, the first member of the eqolisin in family (G1) of peptidases. FEBS Letts 2005, 579:2991-2994.
    • (2005) FEBS Letts , vol.579 , pp. 2991-2994
    • Kataoka, Y.1    Takada, K.2    Oyama, H.3    Tsunemi, M.4    James, M.N.G.5    Oda, K.6
  • 41
    • 33751506102 scopus 로고    scopus 로고
    • Crystal structure of scytalidoglutamic peptidase with its first potent inhibitor provides insights into substrate specificity and catalysis
    • Pillai B., Cherney M.M., Hiraga K., Takada K., Oda K., James M.N.G. Crystal structure of scytalidoglutamic peptidase with its first potent inhibitor provides insights into substrate specificity and catalysis. J. Mol. Biol. 2007, 365:343-361.
    • (2007) J. Mol. Biol. , vol.365 , pp. 343-361
    • Pillai, B.1    Cherney, M.M.2    Hiraga, K.3    Takada, K.4    Oda, K.5    James, M.N.G.6
  • 44
    • 0000916308 scopus 로고
    • A novel proteinase inhibitor, tyrostatin, inhibiting some pepstatin-insensitive carboxyl proteinases
    • Oda K., Fukuda Y., Murao S., Uchida K., Kainosho M. A novel proteinase inhibitor, tyrostatin, inhibiting some pepstatin-insensitive carboxyl proteinases. Agric. Biol. Chem. 1989, 53:405-415.
    • (1989) Agric. Biol. Chem. , vol.53 , pp. 405-415
    • Oda, K.1    Fukuda, Y.2    Murao, S.3    Uchida, K.4    Kainosho, M.5
  • 45
    • 0026555406 scopus 로고
    • Substrate specificity and kinetic properties of pepstatin-insensitive carboxyl proteinase from Pseudomonas sp No. 101
    • Oda K., Nakatani H., Dunn B.M. Substrate specificity and kinetic properties of pepstatin-insensitive carboxyl proteinase from Pseudomonas sp No. 101. Biochim. Biophys. Acta 1992, 1120:208-214.
    • (1992) Biochim. Biophys. Acta , vol.1120 , pp. 208-214
    • Oda, K.1    Nakatani, H.2    Dunn, B.M.3
  • 46
    • 0029809254 scopus 로고    scopus 로고
    • Substrate specificities of pepstatin-insensitive carboxyl proteinases from Gram-negative bacteria
    • Ito M., Dunn B.M., Oda K. Substrate specificities of pepstatin-insensitive carboxyl proteinases from Gram-negative bacteria. J. Biochem. (Tokyo) 1996, 120:845-850.
    • (1996) J. Biochem. (Tokyo) , vol.120 , pp. 845-850
    • Ito, M.1    Dunn, B.M.2    Oda, K.3
  • 47
    • 0033049372 scopus 로고    scopus 로고
    • Subsite preferences of pepstatin-insensitive carboxyl proteinases from bacteria
    • Narutaki S., Dunn B.M., Oda K. Subsite preferences of pepstatin-insensitive carboxyl proteinases from bacteria. J. Biochem. (Tokyo) 1999, 125:75-81.
    • (1999) J. Biochem. (Tokyo) , vol.125 , pp. 75-81
    • Narutaki, S.1    Dunn, B.M.2    Oda, K.3
  • 48
    • 0028815656 scopus 로고
    • The primary structure of pepstatin-insensitive carboxyl proteinases produced by Pseudomonas sp No. 101
    • Hayashi K., Izu H., Oda K., Fukuhara K., Matsuo M., Takano R., Hara S. The primary structure of pepstatin-insensitive carboxyl proteinases produced by Pseudomonas sp No. 101. J. Biochem. (Tokyo) 1995, 118:738-744.
    • (1995) J. Biochem. (Tokyo) , vol.118 , pp. 738-744
    • Hayashi, K.1    Izu, H.2    Oda, K.3    Fukuhara, K.4    Matsuo, M.5    Takano, R.6    Hara, S.7
  • 49
    • 0028046586 scopus 로고
    • Cloning, nucleotide sequence, and expression of an isovaleryl pepstatin-insensitive carboxyl proteinase gene from Pseudomonas sp. 101
    • Oda K., Takahashi T., Tokuda Y., Shibano Y., Takahashi S. Cloning, nucleotide sequence, and expression of an isovaleryl pepstatin-insensitive carboxyl proteinase gene from Pseudomonas sp. 101. J. Biol. Chem. 1994, 269:26518-26524.
    • (1994) J. Biol. Chem. , vol.269 , pp. 26518-26524
    • Oda, K.1    Takahashi, T.2    Tokuda, Y.3    Shibano, Y.4    Takahashi, S.5
  • 50
    • 0033051346 scopus 로고    scopus 로고
    • Identification of carboxyl residues in pepstatin-insensitive carboxyl proteinases from Pseudomonas sp. 101 that participate in catalysis and substrate binding
    • Ito M., Narutaki S., Uchida K., Oda K. Identification of carboxyl residues in pepstatin-insensitive carboxyl proteinases from Pseudomonas sp. 101 that participate in catalysis and substrate binding. J. Biochem. (Tokyo) 1999, 125:210-216.
    • (1999) J. Biochem. (Tokyo) , vol.125 , pp. 210-216
    • Ito, M.1    Narutaki, S.2    Uchida, K.3    Oda, K.4
  • 51
    • 0033600764 scopus 로고    scopus 로고
    • Identification of catalytic residues of pepstatin-insensitive carboxyl proteinases from prokaryotes by site-directed mutagenesis
    • Oyama H., Abe S., Ushiyama S., Takahashi S., Oda K. Identification of catalytic residues of pepstatin-insensitive carboxyl proteinases from prokaryotes by site-directed mutagenesis. J. Biol. Chem. 1999, 274:27815-27822.
    • (1999) J. Biol. Chem. , vol.274 , pp. 27815-27822
    • Oyama, H.1    Abe, S.2    Ushiyama, S.3    Takahashi, S.4    Oda, K.5
  • 52
    • 0347004614 scopus 로고    scopus 로고
    • Two inhibitor molecules bound in the active site of Pseudomonas sedolisin: a model for the bi-product complex following cleavage of a peptide substrate
    • Wlodawer A., Li M., Gustchina A., Oyama H., Oda K., Beyer B.B., Clemente J., Dunn B.M. Two inhibitor molecules bound in the active site of Pseudomonas sedolisin: a model for the bi-product complex following cleavage of a peptide substrate. Biochem. Biophys. Res. Comm. 2004, 314:638-645.
    • (2004) Biochem. Biophys. Res. Comm. , vol.314 , pp. 638-645
    • Wlodawer, A.1    Li, M.2    Gustchina, A.3    Oyama, H.4    Oda, K.5    Beyer, B.B.6    Clemente, J.7    Dunn, B.M.8
  • 53
    • 33746926428 scopus 로고    scopus 로고
    • The peptidases from fungi and viruses
    • James M.N.G. The peptidases from fungi and viruses. Biol. Chem. 2006, 387:1023-1029.
    • (2006) Biol. Chem. , vol.387 , pp. 1023-1029
    • James, M.N.G.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.