메뉴 건너뛰기




Volumn 16, Issue 3, 2009, Pages 277-284

Trypsin-chymotrypsin inhibitors from Vigna mungo seeds

Author keywords

[No Author keywords available]

Indexed keywords

CHYMOTRYPSIN; REVERSE TRANSCRIPTASE, HUMAN IMMUNODEFICIENCY VIRUS 1; RNA DIRECTED DNA POLYMERASE; TRYPSIN; TRYPSIN INHIBITOR; VEGETABLE PROTEIN;

EID: 63449097272     PISSN: 09298665     EISSN: None     Source Type: Journal    
DOI: 10.2174/092986609787601714     Document Type: Article
Times cited : (22)

References (70)
  • 1
    • 0034737556 scopus 로고    scopus 로고
    • Prediction of the tertiary structure of a caspase-9/inhibitor complex
    • Chou, K, C.; Tomasselli, A, G,; Heinrikson, R. L. Prediction of the tertiary structure of a caspase-9/inhibitor complex, FEBS Lett., 2000, 470, 249-256,
    • (2000) FEBS Lett , vol.470 , pp. 249-256
    • Chou, K.C.1    Tomasselli, A.G.2    Heinrikson, R.L.3
  • 2
    • 0031449933 scopus 로고    scopus 로고
    • Prediction of the tertiary structure and substrate binding site of caspase-8
    • Chou, K. C.; Jones, D.; Heinrikson, R. L. Prediction of the tertiary structure and substrate binding site of caspase-8. FEBS Lett., 1997, 419, 49-54.
    • (1997) FEBS Lett , vol.419 , pp. 49-54
    • Chou, K.C.1    Jones, D.2    Heinrikson, R.L.3
  • 3
    • 3242792729 scopus 로고    scopus 로고
    • Review: Structural bioinformatics and its impact to biomedical science
    • Chou, K. C. Review: Structural bioinformatics and its impact to biomedical science. Curr. Med. Chem., 2004, 11, 2105-2134,
    • (2004) Curr. Med. Chem , vol.11 , pp. 2105-2134
    • Chou, K.C.1
  • 4
    • 0036079733 scopus 로고    scopus 로고
    • Prediction of the tertiary structure of the beta-secretase zymogen
    • Chou, K. C.; Howe, W. J, Prediction of the tertiary structure of the beta-secretase zymogen, Biochem. Biophys. Res. Commun., 2002, 292, 702-708.
    • (2002) Biochem. Biophys. Res. Commun , vol.292 , pp. 702-708
    • Chou, K.C.1    Howe, W.J.2
  • 5
    • 0034613320 scopus 로고    scopus 로고
    • Structure of the protease domain of memapsin 2 -secretase) complexed with inhibitor
    • Hong, L.; Koelsch, G.; Lin, X.; Wu, S.; Terzyan, S.; Ghosh, A. K.; Zhang, X. C.; Tang, J. Structure of the protease domain of memapsin 2 -secretase) complexed with inhibitor. Science, 2000, 290, 150-153.
    • (2000) Science , vol.290 , pp. 150-153
    • Hong, L.1    Koelsch, G.2    Lin, X.3    Wu, S.4    Terzyan, S.5    Ghosh, A.K.6    Zhang, X.C.7    Tang, J.8
  • 6
    • 7044241339 scopus 로고    scopus 로고
    • Insights from modelling the tertiary structure of BACE2
    • Chou, K. C. Insights from modelling the tertiary structure of BACE2. J. Proteome Res., 2004, 3, 1069-1072.
    • (2004) J. Proteome Res , vol.3 , pp. 1069-1072
    • Chou, K.C.1
  • 7
    • 17444427671 scopus 로고    scopus 로고
    • Modeling the tertiary structure of human cathepsin-E
    • Chou, K. C. Modeling the tertiary structure of human cathepsin-E. Biochem. Biophys. Res. Commun, 2005, 331, 56-60,
    • (2005) Biochem. Biophys. Res. Commun , vol.331 , pp. 56-60
    • Chou, K.C.1
  • 8
    • 0027219970 scopus 로고
    • A vectorized sequence-coupling model for predicting HIV protease cleavage sites in proteins
    • Chou, K. C. A vectorized sequence-coupling model for predicting HIV protease cleavage sites in proteins. J. Biol. Chem., 1993, 268, 16938-16948.
    • (1993) J. Biol. Chem , vol.268 , pp. 16938-16948
    • Chou, K.C.1
  • 9
    • 26844437646 scopus 로고    scopus 로고
    • Sirois, S.: Sing, T.; Chou, K. C. Review: HIV-1 gp120 V3 loop for structure-based drag design. Curr. Protein Pept. Sci., 2005, 6, 413-422.
    • Sirois, S.: Sing, T.; Chou, K. C. Review: HIV-1 gp120 V3 loop for structure-based drag design. Curr. Protein Pept. Sci., 2005, 6, 413-422.
  • 10
    • 0030049315 scopus 로고    scopus 로고
    • Chou, K, C. Review: Prediction of HIV protease cleavage sites in proteins. Anal. BioChem., 1996, 233, 1-14.
    • Chou, K, C. Review: Prediction of HIV protease cleavage sites in proteins. Anal. BioChem., 1996, 233, 1-14.
  • 11
    • 34248380543 scopus 로고    scopus 로고
    • Liang, G. Z. : Li, S. Z. A new sequence representation (FASGAI) as applied in better specificity elucidation for human immunodeficiency virus type 1 protease. Biopolymers, 2007, 88(3), 401-12.
    • Liang, G. Z. : Li, S. Z. A new sequence representation (FASGAI) as applied in better specificity elucidation for human immunodeficiency virus type 1 protease. Biopolymers, 2007, 88(3), 401-12.
  • 12
    • 33746116743 scopus 로고    scopus 로고
    • Selection of molecular descriptors with artificial intelligence for the understanding of HIV-1 protease peptidomimetic inhibitors-activity
    • Sirois, S.; Tsoukas, C. M.; Chou, K. C.; Wei.; Boucher, C.; Hatza-kis, G. E. Selection of molecular descriptors with artificial intelligence for the understanding of HIV-1 protease peptidomimetic inhibitors-activity. Med. Chem.,2005, 1, 173-184.
    • (2005) Med. Chem , vol.1 , pp. 173-184
    • Sirois, S.1    Tsoukas, C.M.2    Chou, K.C.3    Wei4    Boucher, C.5    Hatza-kis, G.E.6
  • 13
    • 0041848237 scopus 로고    scopus 로고
    • Binding mechanism of Coronavirus main proteinase with ligands and its implication to drug design against SARS
    • Chou, K. C.; Wei, D. Q.; Zhong, W. Z. Binding mechanism of Coronavirus main proteinase with ligands and its implication to drug design against SARS. Biochem. Biophys. Res. Comm., 2003, 308, 148-151.
    • (2003) Biochem. Biophys. Res. Comm , vol.308 , pp. 148-151
    • Chou, K.C.1    Wei, D.Q.2    Zhong, W.Z.3
  • 14
    • 33750554701 scopus 로고    scopus 로고
    • Review: Progress in computational approach to drug development against SARS
    • Chou, K. C.; Wei, D. Q.; Du, Q. S.; Sirois, S.; Zhong, W. Z. Review: Progress in computational approach to drug development against SARS, Curr. Med. Chem., 2006, 13, 3263-3270.
    • (2006) Curr. Med. Chem , vol.13 , pp. 3263-3270
    • Chou, K.C.1    Wei, D.Q.2    Du, Q.S.3    Sirois, S.4    Zhong, W.Z.5
  • 16
    • 0038120984 scopus 로고    scopus 로고
    • Coronavirus main proteinase (3CLpro) structure: Basis for design of anti-SARS drugs
    • Anand, K.; Ziebuhr, J.; Wadhwani, P.; Mesters, J. R,; Hilgenfeld, R. Coronavirus main proteinase (3CLpro) structure: basis for design of anti-SARS drugs. Science, 2003, 300, 1763-1767.
    • (2003) Science , vol.300 , pp. 1763-1767
    • Anand, K.1    Ziebuhr, J.2    Wadhwani, P.3    Mesters, J.R.4    Hilgenfeld, R.5
  • 17
    • 33846052414 scopus 로고    scopus 로고
    • Inhibitor design for SARS Coronavirus main protease based on "distorted key theory
    • Du, Q. S.: Sun, H.; Chou, K. C. Inhibitor design for SARS Coronavirus main protease based on "distorted key theory". Med. Chem., 2007, 3, 1-6.
    • (2007) Med. Chem , vol.3 , pp. 1-6
    • Du, Q.S.1    Sun, H.2    Chou, K.C.3
  • 19
    • 33746172585 scopus 로고    scopus 로고
    • Molecular modeling studies of peptide drug candidates against SARS
    • Zhang, R.; Wei, D. Q.; Du, Q. S.; Chou, K. C. Molecular modeling studies of peptide drug candidates against SARS. Med. Chem., 2006, 2, 309-314.
    • (2006) Med. Chem , vol.2 , pp. 309-314
    • Zhang, R.1    Wei, D.Q.2    Du, Q.S.3    Chou, K.C.4
  • 20
    • 6344236941 scopus 로고    scopus 로고
    • Polyprotein cleavage mechanism of SARS CoV Mpro and chemical modification of octapeptide
    • Du, Q. S.; Wang, S. Q.; Wei, D. Q.; Zhu, Y.; Guo, H.; Sirois, S.; Chou, K. C. Polyprotein cleavage mechanism of SARS CoV Mpro and chemical modification of octapeptide. Peptides, 2004, 25, 1857-1864.
    • (2004) Peptides , vol.25 , pp. 1857-1864
    • Du, Q.S.1    Wang, S.Q.2    Wei, D.Q.3    Zhu, Y.4    Guo, H.5    Sirois, S.6    Chou, K.C.7
  • 21
    • 2942750460 scopus 로고    scopus 로고
    • Virtual screening for SARS-CoV protease based on KZ7088 pharmacophore points
    • Sirois, S.; Wei, D. Q.; Du, Q. S.; Chou, K. C. Virtual screening for SARS-CoV protease based on KZ7088 pharmacophore points. J. Chem. Inf. Comput. Sci., 2004, 44, 1111-1122.
    • (2004) J. Chem. Inf. Comput. Sci , vol.44 , pp. 1111-1122
    • Sirois, S.1    Wei, D.Q.2    Du, Q.S.3    Chou, K.C.4
  • 22
    • 13244290092 scopus 로고    scopus 로고
    • Molecular modelling and chemical modification for finding peptide inhibitor against SARS CoV Mpro
    • Du, Q. S.; Wang, S.; Wei, D. Q.; Sirois, S.; Chou, K. C. Molecular modelling and chemical modification for finding peptide inhibitor against SARS CoV Mpro. Anal. BioChem., 2005, 337, 262-270.
    • (2005) Anal. BioChem , vol.337 , pp. 262-270
    • Du, Q.S.1    Wang, S.2    Wei, D.Q.3    Sirois, S.4    Chou, K.C.5
  • 23
    • 26844549522 scopus 로고    scopus 로고
    • Application of bioinformatics in search for cleavable peptides of SARS-CoV Mpro and chemical modification of octapeptides
    • Du, Q. S.; Wang, S. Q.; Jiang, Z. Q.; Gao, W. N.; Li, Y. D.; Wei, D. Q.; Chou, K. C. Application of bioinformatics in search for cleavable peptides of SARS-CoV Mpro and chemical modification of octapeptides. Med. Chem., 2005, 1, 09-213.
    • (2005) Med. Chem , vol.1 , pp. 09-213
    • Du, Q.S.1    Wang, S.Q.2    Jiang, Z.Q.3    Gao, W.N.4    Li, Y.D.5    Wei, D.Q.6    Chou, K.C.7
  • 24
    • 0022017412 scopus 로고
    • The Bowman-Birk inhibitor, trypsin- and chymotrypsininhibitor from soybeans
    • Birk, Y. The Bowman-Birk inhibitor, trypsin- and chymotrypsininhibitor from soybeans, J. Pept. Protein Res. 1985, 25, 113-131.
    • (1985) J. Pept. Protein Res , vol.25 , pp. 113-131
    • Birk, Y.1
  • 25
    • 0019880158 scopus 로고
    • Soybean trypsin inhibitor (Kunitz) is doubleheaded. Kinetics of the interaction of alpha-chymotrypsin with each side
    • Bosterling, B.; Quast, U. Soybean trypsin inhibitor (Kunitz) is doubleheaded. Kinetics of the interaction of alpha-chymotrypsin with each side. Biochim. Biophys. Acta, 1981, 657, 58-72.
    • (1981) Biochim. Biophys. Acta , vol.657 , pp. 58-72
    • Bosterling, B.1    Quast, U.2
  • 26
    • 0024489831 scopus 로고
    • Amino acid sequences and disulfide bridges of serine proteinase inhibitors from bitter gourd (Momordica charantia LINN.) seeds
    • Hara, S.; Makino, J.; Ikenaka, T. Amino acid sequences and disulfide bridges of serine proteinase inhibitors from bitter gourd (Momordica charantia LINN.) seeds. J. Biochem. (Tokyo), 1989, 105, 88-91.
    • (1989) J. Biochem. (Tokyo) , vol.105 , pp. 88-91
    • Hara, S.1    Makino, J.2    Ikenaka, T.3
  • 28
    • 0029123662 scopus 로고
    • Amino acid sequences of trypsin inhibitors from the melon Cucumis melo
    • Lee, CF.; Lin, J.Y. Amino acid sequences of trypsin inhibitors from the melon Cucumis melo. J. Biochem. (Tokyo), 1995, 118, 18-22.
    • (1995) J. Biochem. (Tokyo) , vol.118 , pp. 18-22
    • Lee, C.F.1    Lin, J.Y.2
  • 30
    • 0038057913 scopus 로고    scopus 로고
    • Spo-ramin-mediated resistance to beet cyst nematodes (Heterodera schachtii Schm.) is dependent on trypsin inhibitory activity in sugar beet (Beta vulgaris L.) hairy roots
    • Cai, D.; Thurau, T.; Tian, Y.; Lange, T.; Yeh, K.W.; Jung, C. Spo-ramin-mediated resistance to beet cyst nematodes (Heterodera schachtii Schm.) is dependent on trypsin inhibitory activity in sugar beet (Beta vulgaris L.) hairy roots. Plant Mol. Biol., 2003, 51, 839-849.
    • (2003) Plant Mol. Biol , vol.51 , pp. 839-849
    • Cai, D.1    Thurau, T.2    Tian, Y.3    Lange, T.4    Yeh, K.W.5    Jung, C.6
  • 31
    • 2342519504 scopus 로고    scopus 로고
    • A Kunitztype inhibitor of coleopteran proteases, isolated from Adenanthera pavonina L. seeds and its effect on Callosobruchus maculates
    • Macedo, M.L.; de Sa, CM.; Freire, M.D.; Parra, J.R. A Kunitztype inhibitor of coleopteran proteases, isolated from Adenanthera pavonina L. seeds and its effect on Callosobruchus maculates. J. Agric. Food Chem., 2004, 52, 2533-2540.
    • (2004) J. Agric. Food Chem , vol.52 , pp. 2533-2540
    • Macedo, M.L.1    de Sa, C.M.2    Freire, M.D.3    Parra, J.R.4
  • 32
    • 0037298753 scopus 로고    scopus 로고
    • A homodimeric sporamin-type trypsin inhibitor with antiproliferative, HIV reverse transcriptase-inhibitory and antifungal activities from wampee (Clausena lan-sium) seeds
    • Ng, T.B.; Lam, S.K.; Fong, W.P. A homodimeric sporamin-type trypsin inhibitor with antiproliferative, HIV reverse transcriptase-inhibitory and antifungal activities from wampee (Clausena lan-sium) seeds. Biol. Chem., 2003, 384, 289-293.
    • (2003) Biol. Chem , vol.384 , pp. 289-293
    • Ng, T.B.1    Lam, S.K.2    Fong, W.P.3
  • 33
    • 0028809235 scopus 로고
    • The evidence for soybean products as cancer preventive agents
    • Kennedy, A.R. The evidence for soybean products as cancer preventive agents. J. Nutr., 1995, 125, 733S-7743S.
    • (1995) J. Nutr , vol.125
    • Kennedy, A.R.1
  • 34
    • 0027318686 scopus 로고
    • Effects of various preparations of dietary protease inhibitors on oral carcinogenesis in hamsters induced by DMBA
    • Kennedy, A.R.; Billings, P.C.; Maki, P.A.: Newberne, P. Effects of various preparations of dietary protease inhibitors on oral carcinogenesis in hamsters induced by DMBA. Nutr. Cancer, 1993, 19, 191-200.
    • (1993) Nutr. Cancer , vol.19 , pp. 191-200
    • Kennedy, A.R.1    Billings, P.C.2    Maki, P.A.3    Newberne, P.4
  • 35
    • 0028598821 scopus 로고
    • Field bean protease inhibitor preparations, unlike methotrexate, can completely suppress Yoshida sarcoma tumor in rats
    • Banerji, A.P. ; Fernandes, A.O. Field bean protease inhibitor preparations, unlike methotrexate, can completely suppress Yoshida sarcoma tumor in rats. Cell Biol. Int., 1994, 18, 1025-1034.
    • (1994) Cell Biol. Int , vol.18 , pp. 1025-1034
    • Banerji, A.P.1    Fernandes, A.O.2
  • 36
    • 0032516679 scopus 로고    scopus 로고
    • Treatment with field bean protease inhibitor can effectively repress ethylnitrosourea (ENU)-induced neoplasms of the nervous system in Sprague-Dawley rats
    • Banerji, A.; Fernandes, A.; Bane, S. Treatment with field bean protease inhibitor can effectively repress ethylnitrosourea (ENU)-induced neoplasms of the nervous system in Sprague-Dawley rats. Cancer Lett., 1998, 130, 161-167.
    • (1998) Cancer Lett , vol.130 , pp. 161-167
    • Banerji, A.1    Fernandes, A.2    Bane, S.3
  • 37
    • 0032479554 scopus 로고    scopus 로고
    • The field bean protease inhibitor has the potential to suppress B16F10 melanoma cell lung metastasis in mice
    • Banerji, A.; Fernandes, A.; Bane, S.; Ahire, S. The field bean protease inhibitor has the potential to suppress B16F10 melanoma cell lung metastasis in mice. Cancer Lett., 1998, 129, 15-20.
    • (1998) Cancer Lett , vol.129 , pp. 15-20
    • Banerji, A.1    Fernandes, A.2    Bane, S.3    Ahire, S.4
  • 38
    • 0037370213 scopus 로고    scopus 로고
    • A novel trypsin inhibitor from Peltophorum dubium seeds, with lectin-like properties, triggers rat lymphoma cell apoptosis
    • Troncoso, M.; Cerda Zolezzi, P.; Hellman, U.C. A novel trypsin inhibitor from Peltophorum dubium seeds, with lectin-like properties, triggers rat lymphoma cell apoptosis. Arch. Biochem. Biophys., 2003, 411, 93-104.
    • (2003) Arch. Biochem. Biophys , vol.411 , pp. 93-104
    • Troncoso, M.1    Cerda Zolezzi, P.2    Hellman, U.C.3
  • 39
    • 0029117555 scopus 로고
    • Inhibition of benzopyrene-induced forestomach tumors by field bean protease inhibitor(s)
    • Fernandes, A.O.; Banerji, A.P. Inhibition of benzopyrene-induced forestomach tumors by field bean protease inhibitor(s). Carcinogenesis, 1995, 16, 1843-1846.
    • (1995) Carcinogenesis , vol.16 , pp. 1843-1846
    • Fernandes, A.O.1    Banerji, A.P.2
  • 40
    • 0029999182 scopus 로고    scopus 로고
    • The field bean protease inhibitor can effectively suppress 7, 12-dimethylbenz[a]anthracene-induced skin tumorigenesis in mice
    • Fernandes, A.O.; Banerji, A.P. The field bean protease inhibitor can effectively suppress 7, 12-dimethylbenz[a]anthracene-induced skin tumorigenesis in mice. Cancer Lett., 1996, 104, 219-224.
    • (1996) Cancer Lett , vol.104 , pp. 219-224
    • Fernandes, A.O.1    Banerji, A.P.2
  • 41
    • 2942708160 scopus 로고    scopus 로고
    • A soybean Kunitz trypsin inhibitor suppresses ovarian cancer cell invasion by blocking urokinase upregulation
    • Kobayashi, H.; Suzuki, M.; Kanayama, N.; Terao, T. A soybean Kunitz trypsin inhibitor suppresses ovarian cancer cell invasion by blocking urokinase upregulation. Clin. Exp. Metast., 2004, 21, 159-166.
    • (2004) Clin. Exp. Metast , vol.21 , pp. 159-166
    • Kobayashi, H.1    Suzuki, M.2    Kanayama, N.3    Terao, T.4
  • 42
    • 0025945685 scopus 로고
    • Inhibition of N-nitrosomethylbenzylamine-induced esophageal neoplasms by the Bowman-Birk protease inhibitor
    • von Hofe, E.; Newberne, P.M.; Kennedy, A.R. Inhibition of N-nitrosomethylbenzylamine-induced esophageal neoplasms by the Bowman-Birk protease inhibitor. Carcinogenesis. 1991, 12, 2147-2150.
    • (1991) Carcinogenesis , vol.12 , pp. 2147-2150
    • von Hofe, E.1    Newberne, P.M.2    Kennedy, A.R.3
  • 43
    • 0035138276 scopus 로고    scopus 로고
    • Effect of dietary cowpea trypsin inhibitor (CpTI) on the growth and development of the tomato moth Lacanobia oleracea (Lepidoptera: Noctuidae) and on the success of the gregarious ectoparasitoid Eulophus pennicornis (Hymenoptera: Eulophidae)
    • Bell, H.A.; Fitches, E.C.; Down, R.E.; Ford, L.; Marris, G.C.; Edwards, J.P.; Gatehouse, I.A.; Gatehouse, A.M. Effect of dietary cowpea trypsin inhibitor (CpTI) on the growth and development of the tomato moth Lacanobia oleracea (Lepidoptera: Noctuidae) and on the success of the gregarious ectoparasitoid Eulophus pennicornis (Hymenoptera: Eulophidae). Pest Manage. Sci., 2001, 57, 57-65.
    • (2001) Pest Manage. Sci , vol.57 , pp. 57-65
    • Bell, H.A.1    Fitches, E.C.2    Down, R.E.3    Ford, L.4    Marris, G.C.5    Edwards, J.P.6    Gatehouse, I.A.7    Gatehouse, A.M.8
  • 45
    • 1442350538 scopus 로고    scopus 로고
    • Effects of the Medicago scutellata trypsin inhibitor (MsTI) on cisplatin-induced cytotoxicity in human breast and cervical cancer cells
    • Lanza, A.; Tava, A.; Catalano, M.; Ragona, L.; Singuaroli, I.; della Cuna, R.; della Cuna, G.R. Effects of the Medicago scutellata trypsin inhibitor (MsTI) on cisplatin-induced cytotoxicity in human breast and cervical cancer cells. Anticancer Res., 2004, 24, 227-233.
    • (2004) Anticancer Res , vol.24 , pp. 227-233
    • Lanza, A.1    Tava, A.2    Catalano, M.3    Ragona, L.4    Singuaroli, I.5    della Cuna, R.6    della Cuna, G.R.7
  • 46
    • 0029780852 scopus 로고    scopus 로고
    • Purification and characterization of ostrich pancreatic secretory trypsin inhibitor
    • Zhao, M.; Naude, R.I.; Muramoto, K.; Oelofsen, W. Purification and characterization of ostrich pancreatic secretory trypsin inhibitor. Int. J. Pept. Protein Res., 1996, 48, 174-181.
    • (1996) Int. J. Pept. Protein Res , vol.48 , pp. 174-181
    • Zhao, M.1    Naude, R.I.2    Muramoto, K.3    Oelofsen, W.4
  • 47
    • 34648831038 scopus 로고    scopus 로고
    • Screening for new agonists against Alzheimer's disease
    • Zheng, H.; Wei, D. Q.; Zhang, R.; Wang, C.; Wei, H.; Chou, K. C. Screening for new agonists against Alzheimer's disease. Med. Chem., 2007, 3(5), 488-93.
    • (2007) Med. Chem , vol.3 , Issue.5 , pp. 488-493
    • Zheng, H.1    Wei, D.Q.2    Zhang, R.3    Wang, C.4    Wei, H.5    Chou, K.C.6
  • 48
    • 33846449105 scopus 로고    scopus 로고
    • Molecular insights of SAH enzyme catalysis and their implication for inhibitor design
    • Wei, H.; Zhang, R.; Wang, C.; Zheng, H.; Chou, K. C.; Wei, D. Q. Molecular insights of SAH enzyme catalysis and their implication for inhibitor design. J. Theor. Biol., 2007, 244, 692-702.
    • (2007) J. Theor. Biol , vol.244 , pp. 692-702
    • Wei, H.1    Zhang, R.2    Wang, C.3    Zheng, H.4    Chou, K.C.5    Wei, D.Q.6
  • 49
    • 34248679618 scopus 로고    scopus 로고
    • Agaritine and its derivatives are potential inhibitors against HIV proteases
    • Gao, W. N.; Wei, D. Q.; Li, Y., Gao, H.; Xu, W. R.; Li, A. X.; Chou, K. C. Agaritine and its derivatives are potential inhibitors against HIV proteases. Med. Chem., 2007, 3, 221-226.
    • (2007) Med. Chem , vol.3 , pp. 221-226
    • Gao, W.N.1    Wei, D.Q.2    Li, Y.3    Gao, H.4    Xu, W.R.5    Li, A.X.6    Chou, K.C.7
  • 50
    • 34547107293 scopus 로고    scopus 로고
    • Virtual screening for finding natural inhibitor against cathepsin-L for SARS therapy
    • Zhao, K.; Li, A. X.; Wei, D. Q.; Chou, K. C. Virtual screening for finding natural inhibitor against cathepsin-L for SARS therapy. Amino Acids, 2007, 33,129-135.
    • (2007) Amino Acids , vol.33 , pp. 129-135
    • Zhao, K.1    Li, A.X.2    Wei, D.Q.3    Chou, K.C.4
  • 51
    • 0026232395 scopus 로고
    • A monomeric protein with hemagglutinating activity from seeds of Vigna mungo (Phaseolus mungo)
    • Singh, S.S.; Rao, S.L. A monomeric protein with hemagglutinating activity from seeds of Vigna mungo (Phaseolus mungo). Indian J. Biochem. Biophys., 1991, 28, 439-443.
    • (1991) Indian J. Biochem. Biophys , vol.28 , pp. 439-443
    • Singh, S.S.1    Rao, S.L.2
  • 52
    • 0035808328 scopus 로고    scopus 로고
    • Identification of a membrane-associated cysteine protease with possible dual roles in the endoplasmic reticulum and protein storage vacuole
    • Okamoto, T.; Toyooka, K.; Minamikawa, T. Identification of a membrane-associated cysteine protease with possible dual roles in the endoplasmic reticulum and protein storage vacuole, J. Biol. Chem., 2001, 276, 742-751.
    • (2001) J. Biol. Chem , vol.276 , pp. 742-751
    • Okamoto, T.1    Toyooka, K.2    Minamikawa, T.3
  • 53
    • 1942516818 scopus 로고    scopus 로고
    • Multiple trypsin inhibitors from Momordica cochinchinensis seeds
    • Wong, R.C.; Fong, W.P.; Ng, T.B. Multiple trypsin inhibitors from Momordica cochinchinensis seeds. Chinese Drug Mubiezhi, Pept., 2004, 25, 163-169.
    • (2004) Chinese Drug Mubiezhi, Pept , vol.25 , pp. 163-169
    • Wong, R.C.1    Fong, W.P.2    Ng, T.B.3
  • 54
    • 33748753164 scopus 로고    scopus 로고
    • Immunomodulatory activity of a chymotrypsin inhibitor from Momordica cochinchinensis seeds
    • Tsoi, A.Y.; Ng, T.B.; Fong, W.P. Immunomodulatory activity of a chymotrypsin inhibitor from Momordica cochinchinensis seeds. J. Pept. Sci., 2006, 12, 605-611.
    • (2006) J. Pept. Sci , vol.12 , pp. 605-611
    • Tsoi, A.Y.1    Ng, T.B.2    Fong, W.P.3
  • 55
  • 56
    • 0017911968 scopus 로고
    • Measurements of molecular weights by gel electrophoresis
    • Nielsen, T.B.; Reynolds, I.A. Measurements of molecular weights by gel electrophoresis. Methods Enzymol, 1978, 48, 3-10.
    • (1978) Methods Enzymol , vol.48 , pp. 3-10
    • Nielsen, T.B.1    Reynolds, I.A.2
  • 57
    • 20444406094 scopus 로고    scopus 로고
    • Wong, I.H.; Ng, T.B. Sesquin, a potent defensin-like antifungal peotide from beans with inhibitory activities toward tumor cells and HIV-1 reverse transcriptase. Peptides, 2005, 26, 1120-1126.
    • Wong, I.H.; Ng, T.B. Sesquin, a potent defensin-like antifungal peotide from beans with inhibitory activities toward tumor cells and HIV-1 reverse transcriptase. Peptides, 2005, 26, 1120-1126.
  • 58
    • 1842856051 scopus 로고    scopus 로고
    • Purification and characterization of proteinase inhibitors from wild soja (Glycine soja) seeds
    • Deshimaru, M.; Hanamoto, R.; Kusano, C.; Yoshimi, S.; Terada, S. Purification and characterization of proteinase inhibitors from wild soja (Glycine soja) seeds. Biosci. Biotechnol. Biochem., 2002, 66, 1897-1903.
    • (2002) Biosci. Biotechnol. Biochem , vol.66 , pp. 1897-1903
    • Deshimaru, M.1    Hanamoto, R.2    Kusano, C.3    Yoshimi, S.4    Terada, S.5
  • 59
    • 0035941043 scopus 로고    scopus 로고
    • A Bowman-Birk-type trypsin-chymotrypsin inhibitor from broad beans
    • Ye, X.Y.; Ng, T.B.; Rao, P.F. A Bowman-Birk-type trypsin-chymotrypsin inhibitor from broad beans. Biochem. Biophys. Res. Commun., 2001, 289, 91-96.
    • (2001) Biochem. Biophys. Res. Commun , vol.289 , pp. 91-96
    • Ye, X.Y.1    Ng, T.B.2    Rao, P.F.3
  • 65
    • 0029981307 scopus 로고    scopus 로고
    • Althaus, I. W.; Chou, K. C.; Franks, K. M.; Diebel, M. R.; Kezdy, F. I.; Romero, D. L.; Thomas, R. C.; Aristoff, P. A.; Tarpley, W. G.; Reusser, F. (). The benzylthio-pyrididine U-31, 355 is a potent inhibitor of HIV-1 reverse transcriptase. Biochem. Pharmacol., 1996, 51, 743-750.
    • Althaus, I. W.; Chou, K. C.; Franks, K. M.; Diebel, M. R.; Kezdy, F. I.; Romero, D. L.; Thomas, R. C.; Aristoff, P. A.; Tarpley, W. G.; Reusser, F. (). The benzylthio-pyrididine U-31, 355 is a potent inhibitor of HIV-1 reverse transcriptase. Biochem. Pharmacol., 1996, 51, 743-750.
  • 66
    • 0028071544 scopus 로고
    • Review: Steady-state inhibition kinetics of processive nucleic acid polymerases and nucleases
    • Chou, K. C.; Kezdy, F. I.; Reusser, F. Review: Steady-state inhibition kinetics of processive nucleic acid polymerases and nucleases. Anal BioChem., 1994, 221, 217-230.
    • (1994) Anal BioChem , vol.221 , pp. 217-230
    • Chou, K.C.1    Kezdy, F.I.2    Reusser, F.3
  • 67
    • 0026579208 scopus 로고
    • The HIV-1 protease as a therapeutic target for AIDS
    • Debouck, C. The HIV-1 protease as a therapeutic target for AIDS. AIDS Res. Hum. Retroviruses, 1992, 8, 153-164.
    • (1992) AIDS Res. Hum. Retroviruses , vol.8 , pp. 153-164
    • Debouck, C.1
  • 68
    • 0027325504 scopus 로고
    • Predicting cleavability of peptide sequences by HIV protease via correlation-angle approach
    • Chou, I. I. Predicting cleavability of peptide sequences by HIV protease via correlation-angle approach. J. Protein Chem., 1993, 72, 291-302.
    • (1993) J. Protein Chem , vol.72 , pp. 291-302
    • Chou, I.I.1
  • 69
    • 0027170793 scopus 로고
    • A formulation for correlating properties of peptides and its application to predicting human immunodeficiency virus prote-ase-cleavable sites in proteins
    • Chou, J. J. A formulation for correlating properties of peptides and its application to predicting human immunodeficiency virus prote-ase-cleavable sites in proteins Biopolymers, 1993, 33, 1405-1414.
    • (1993) Biopolymers , vol.33 , pp. 1405-1414
    • Chou, J.J.1
  • 70
    • 0038120984 scopus 로고    scopus 로고
    • Coronavirus main proteinase (3CLpro) structure: Basis for design of anti-SARS drugs
    • Anand, K.; Ziebuhr, I.; Wadhwani, P.; Mesters, I. R.; Hilgenfeld, R. Coronavirus main proteinase (3CLpro) structure: basis for design of anti-SARS drugs. Science, 2003, 300, 1763-1767.
    • (2003) Science , vol.300 , pp. 1763-1767
    • Anand, K.1    Ziebuhr, I.2    Wadhwani, P.3    Mesters, I.R.4    Hilgenfeld, R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.