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Volumn 175, Issue 1, 2011, Pages 73-84

Crystal structures of the free and inhibited forms of plasmepsin I (PMI) from Plasmodium falciparum

Author keywords

Aspartic protease; Crystal structure; Enzyme inhibition; Malaria; Plasmepsin

Indexed keywords

ALLOPHENYLNORSTATINE DIMETHYLTHIOPROLINE; APOENZYME; ASPARTIC PROTEINASE; KNI 10006; PLASMEPSIN I; PLASMEPSIN INHIBITOR; PROLINE DERIVATIVE; UNCLASSIFIED DRUG;

EID: 79956214335     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2011.04.009     Document Type: Article
Times cited : (38)

References (65)
  • 1
    • 10044264132 scopus 로고    scopus 로고
    • Design of inhibitors against HIV, HTLV-I, and Plasmodium falciparum aspartic proteases
    • Abdel-Rahman H.M., Kimura T., Hidaka K., Kiso A., Nezami A., et al. Design of inhibitors against HIV, HTLV-I, and Plasmodium falciparum aspartic proteases. Biol. Chem. 2004, 385:1035-1039.
    • (2004) Biol. Chem. , vol.385 , pp. 1035-1039
    • Abdel-Rahman, H.M.1    Kimura, T.2    Hidaka, K.3    Kiso, A.4    Nezami, A.5
  • 2
    • 0036900890 scopus 로고    scopus 로고
    • Structures of Ser205 mutant plasmepsin II from Plasmodium falciparum at 1.8Å in complex with the inhibitors rs367 and rs370
    • Asojo O.A., Afonina E., Gulnik S.V., Yu B., Erickson J.W., et al. Structures of Ser205 mutant plasmepsin II from Plasmodium falciparum at 1.8Å in complex with the inhibitors rs367 and rs370. Acta Crystallogr. 2002, D58:2001-2008.
    • (2002) Acta Crystallogr. , vol.D58 , pp. 2001-2008
    • Asojo, O.A.1    Afonina, E.2    Gulnik, S.V.3    Yu, B.4    Erickson, J.W.5
  • 3
    • 0037436389 scopus 로고    scopus 로고
    • Novel uncomplexed and complexed structures of plasmepsin II, an aspartic protease from Plasmodium falciparum
    • Asojo O.A., Gulnik S.V., Afonina E., Yu B., Ellman J.A., Haque T.S., Silva A.M. Novel uncomplexed and complexed structures of plasmepsin II, an aspartic protease from Plasmodium falciparum. J. Mol. Biol. 2003, 327:173-181.
    • (2003) J. Mol. Biol. , vol.327 , pp. 173-181
    • Asojo, O.A.1    Gulnik, S.V.2    Afonina, E.3    Yu, B.4    Ellman, J.A.5    Haque, T.S.6    Silva, A.M.7
  • 4
    • 0026915311 scopus 로고
    • Plasmodium falciparum: differential sensitivity in vitro to E-64 (cysteine protease inhibitor) and Pepstatin A (aspartyl protease inhibitor)
    • Bailly E., Jambou R., Savel J., Jaureguiberry G. Plasmodium falciparum: differential sensitivity in vitro to E-64 (cysteine protease inhibitor) and Pepstatin A (aspartyl protease inhibitor). J. Protozool. 1992, 39:593-599.
    • (1992) J. Protozool. , vol.39 , pp. 593-599
    • Bailly, E.1    Jambou, R.2    Savel, J.3    Jaureguiberry, G.4
  • 5
    • 0037154180 scopus 로고    scopus 로고
    • Four plasmepsins are active in the Plasmodium falciparum food vacuole, including a protease with an active-site histidine
    • Banerjee R., Liu J., Beatty W., Pelosof L., Klemba M., Goldberg D.E. Four plasmepsins are active in the Plasmodium falciparum food vacuole, including a protease with an active-site histidine. Proc. Natl. Acad. Sci. USA 2002, 99:990-995.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 990-995
    • Banerjee, R.1    Liu, J.2    Beatty, W.3    Pelosof, L.4    Klemba, M.5    Goldberg, D.E.6
  • 6
    • 0032924352 scopus 로고    scopus 로고
    • Crystal structure of the novel aspartic proteinase zymogen proplasmepsin II from Plasmodium falciparum
    • Bernstein N.K., Cherney M.M., Loetscher H., Ridley R.G., James M.N. Crystal structure of the novel aspartic proteinase zymogen proplasmepsin II from Plasmodium falciparum. Nat. Struct. Biol. 1999, 6:32-37.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 32-37
    • Bernstein, N.K.1    Cherney, M.M.2    Loetscher, H.3    Ridley, R.G.4    James, M.N.5
  • 8
    • 0032971605 scopus 로고    scopus 로고
    • A distinct member of the aspartic proteinase gene family from the human malaria parasite Plasmodium falciparum
    • Berry C., Humphreys M.J., Matharu P., Granger R., Horrocks P., et al. A distinct member of the aspartic proteinase gene family from the human malaria parasite Plasmodium falciparum. FEBS Lett. 1999, 447:149-154.
    • (1999) FEBS Lett. , vol.447 , pp. 149-154
    • Berry, C.1    Humphreys, M.J.2    Matharu, P.3    Granger, R.4    Horrocks, P.5
  • 10
    • 0023643147 scopus 로고
    • The high-resolution X-ray crystal structure of the complex formed between subtilisin Carlsberg and eglin c, an elastase inhibitor from the leech Hirudo medicinalis. Structural analysis, subtilisin structure and interface geometry
    • Bode W., Papamokos E., Musil D. The high-resolution X-ray crystal structure of the complex formed between subtilisin Carlsberg and eglin c, an elastase inhibitor from the leech Hirudo medicinalis. Structural analysis, subtilisin structure and interface geometry. Eur. J. Biochem. 1987, 166:673-692.
    • (1987) Eur. J. Biochem. , vol.166 , pp. 673-692
    • Bode, W.1    Papamokos, E.2    Musil, D.3
  • 11
    • 0028103275 scopus 로고
    • CCP4, Collaborative Computational Project
    • Number 4, 1994. The CCP4 Suite: Programs for Protein Crystallography. Acta Crystallogr. D50.
    • CCP4, 1994. Collaborative Computational Project, Number 4, 1994. The CCP4 Suite: Programs for Protein Crystallography. Acta Crystallogr. D50, 760-763.
    • (1994) , pp. 760-763
  • 12
    • 33646573016 scopus 로고    scopus 로고
    • Structure of the aspartic protease plasmepsin 4 from the malarial parasite Plasmodium malariae bound to an allophenylnorstatine-based inhibitor
    • Clemente J.C., Govindasamy L., Madabushi A., Fisher S.Z., Moose R.E., et al. Structure of the aspartic protease plasmepsin 4 from the malarial parasite Plasmodium malariae bound to an allophenylnorstatine-based inhibitor. Acta Crystallogr. 2006, D62:246-252.
    • (2006) Acta Crystallogr. , vol.D62 , pp. 246-252
    • Clemente, J.C.1    Govindasamy, L.2    Madabushi, A.3    Fisher, S.Z.4    Moose, R.E.5
  • 13
    • 0001679473 scopus 로고    scopus 로고
    • ALIGN: a program to superimpose protein coordinates, accounting for insertions and deletions
    • Cohen G.E. ALIGN: a program to superimpose protein coordinates, accounting for insertions and deletions. J. Appl. Crystallogr. 1997, 30:1160-1161.
    • (1997) J. Appl. Crystallogr. , vol.30 , pp. 1160-1161
    • Cohen, G.E.1
  • 14
    • 0035521154 scopus 로고    scopus 로고
    • Aspartic proteases of Plasmodium falciparum and other parasitic protozoa as drug targets
    • Coombs G.H., Goldberg D.E., Klemba M., Berry C., Kay J., Mottram J.C. Aspartic proteases of Plasmodium falciparum and other parasitic protozoa as drug targets. Trends Parasitol. 2001, 17:532-537.
    • (2001) Trends Parasitol. , vol.17 , pp. 532-537
    • Coombs, G.H.1    Goldberg, D.E.2    Klemba, M.3    Berry, C.4    Kay, J.5    Mottram, J.C.6
  • 15
    • 0025290527 scopus 로고
    • The structure and function of the aspartic proteinases
    • Davies D.R. The structure and function of the aspartic proteinases. Annu. Rev. Biophys. Biophys. Chem. 1990, 19:189-215.
    • (1990) Annu. Rev. Biophys. Biophys. Chem. , vol.19 , pp. 189-215
    • Davies, D.R.1
  • 17
    • 0036882390 scopus 로고    scopus 로고
    • Structure and mechanism of the pepsin-like family of aspartic peptidases
    • Dunn B.M. Structure and mechanism of the pepsin-like family of aspartic peptidases. Chem. Rev. 2002, 102:4431-4458.
    • (2002) Chem. Rev. , vol.102 , pp. 4431-4458
    • Dunn, B.M.1
  • 18
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley P., Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallogr. 2004, D60:2126-2132.
    • (2004) Acta Crystallogr. , vol.D60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 19
    • 33747177314 scopus 로고    scopus 로고
    • Plasmepsins as potential targets for new antimalarial therapy
    • Ersmark K., Samuelsson B., Hallberg A. Plasmepsins as potential targets for new antimalarial therapy. Med. Res. Rev. 2006, 26:626-666.
    • (2006) Med. Res. Rev. , vol.26 , pp. 626-666
    • Ersmark, K.1    Samuelsson, B.2    Hallberg, A.3
  • 20
    • 0031004534 scopus 로고    scopus 로고
    • Biosynthesis and maturation of the malaria aspartic hemoglobinases plasmepsins I and II
    • Francis S.E., Banerjee R., Goldberg D.E. Biosynthesis and maturation of the malaria aspartic hemoglobinases plasmepsins I and II. J. Biol. Chem. 1997, 272:14961-14968.
    • (1997) J. Biol. Chem. , vol.272 , pp. 14961-14968
    • Francis, S.E.1    Banerjee, R.2    Goldberg, D.E.3
  • 21
    • 0028009428 scopus 로고
    • Molecular characterization and inhibition of a Plasmodium falciparum aspartic hemoglobinase
    • Francis S.E., Gluzman I.Y., Oksman A., Knickerbocker A., Mueller R., et al. Molecular characterization and inhibition of a Plasmodium falciparum aspartic hemoglobinase. EMBO J. 1994, 13:306-317.
    • (1994) EMBO J. , vol.13 , pp. 306-317
    • Francis, S.E.1    Gluzman, I.Y.2    Oksman, A.3    Knickerbocker, A.4    Mueller, R.5
  • 24
    • 33750087338 scopus 로고    scopus 로고
    • Computational analysis of plasmepsin IV bound to an allophenylnorstatine inhibitor
    • Gutierrez-de-Teran H., Nervall M., Dunn B.M., Clemente J.C., Aqvist J. Computational analysis of plasmepsin IV bound to an allophenylnorstatine inhibitor. FEBS Lett. 2006, 580:5910-5916.
    • (2006) FEBS Lett. , vol.580 , pp. 5910-5916
    • Gutierrez-de-Teran, H.1    Nervall, M.2    Dunn, B.M.3    Clemente, J.C.4    Aqvist, J.5
  • 25
    • 0028025371 scopus 로고
    • High level expression and characterisation of Plasmepsin II, an aspartic proteinase from Plasmodium falciparum
    • Hill J., Tyas L., Phylip L.H., Kay J., Dunn B.M., Berry C. High level expression and characterisation of Plasmepsin II, an aspartic proteinase from Plasmodium falciparum. FEBS Lett. 1994, 352:155-158.
    • (1994) FEBS Lett. , vol.352 , pp. 155-158
    • Hill, J.1    Tyas, L.2    Phylip, L.H.3    Kay, J.4    Dunn, B.M.5    Berry, C.6
  • 26
    • 34247534257 scopus 로고    scopus 로고
    • Stereochemical restraints revisited: how accurate are refinement targets and how much should protein structures be allowed to deviate from them?
    • Jaskolski M., Gilski M., Dauter Z., Wlodawer A. Stereochemical restraints revisited: how accurate are refinement targets and how much should protein structures be allowed to deviate from them?. Acta Crystallogr. 2007, D63:611-620.
    • (2007) Acta Crystallogr. , vol.D63 , pp. 611-620
    • Jaskolski, M.1    Gilski, M.2    Dauter, Z.3    Wlodawer, A.4
  • 27
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch W. Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J. Appl. Cryst. 1993, 26:795-800.
    • (1993) J. Appl. Cryst. , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 28
    • 34249289725 scopus 로고    scopus 로고
    • Chipping at large, potent human T-cell leukemia virus type 1 protease inhibitors to uncover smaller, equipotent inhibitors
    • Kimura T., Nguyen J.T., Maegawa H., Nishiyama K., Arii Y., et al. Chipping at large, potent human T-cell leukemia virus type 1 protease inhibitors to uncover smaller, equipotent inhibitors. Bioorg. Med. Chem. Lett. 2007, 17:3276-3280.
    • (2007) Bioorg. Med. Chem. Lett. , vol.17 , pp. 3276-3280
    • Kimura, T.1    Nguyen, J.T.2    Maegawa, H.3    Nishiyama, K.4    Arii, Y.5
  • 29
    • 0027401867 scopus 로고
    • Pharmacokinetic study of a tripeptide HIV-1 protease inhibitor, KNI-174, in rats after intravenous and intraduodenal administrations
    • Kiriyama A., Mimoto T., Kiso Y., Takada K. Pharmacokinetic study of a tripeptide HIV-1 protease inhibitor, KNI-174, in rats after intravenous and intraduodenal administrations. Biopharm. Drug Dispos. 1993, 14:199-207.
    • (1993) Biopharm. Drug Dispos. , vol.14 , pp. 199-207
    • Kiriyama, A.1    Mimoto, T.2    Kiso, Y.3    Takada, K.4
  • 30
    • 0029949211 scopus 로고    scopus 로고
    • The bioavailability of oral dosage forms of a new HIV-1 protease inhibitor, KNI-272, in beagle dogs
    • Kiriyama A., Sugahara M., Yoshikawa Y., Kiso Y., Takada K. The bioavailability of oral dosage forms of a new HIV-1 protease inhibitor, KNI-272, in beagle dogs. Biopharm. Drug Dispos. 1996, 17:125-134.
    • (1996) Biopharm. Drug Dispos. , vol.17 , pp. 125-134
    • Kiriyama, A.1    Sugahara, M.2    Yoshikawa, Y.3    Kiso, Y.4    Takada, K.5
  • 31
    • 8644243887 scopus 로고    scopus 로고
    • Search for substrate-based inhibitors fitting the S2' space of malarial aspartic protease plasmepsin II
    • Kiso A., Hidaka K., Kimura T., Hayashi Y., Nezami A., Freire E., Kiso Y. Search for substrate-based inhibitors fitting the S2' space of malarial aspartic protease plasmepsin II. J. Pept. Sci. 2004, 10:641-647.
    • (2004) J. Pept. Sci. , vol.10 , pp. 641-647
    • Kiso, A.1    Hidaka, K.2    Kimura, T.3    Hayashi, Y.4    Nezami, A.5    Freire, E.6    Kiso, Y.7
  • 32
    • 0027653897 scopus 로고
    • Kynostatin (KNI)-272 - a rationally designed tripeptide inhibitor of HIV protease
    • Kiso Y. Kynostatin (KNI)-272 - a rationally designed tripeptide inhibitor of HIV protease. Nippon. Rinsho. 1993, 51(Suppl.):139-145.
    • (1993) Nippon. Rinsho. , vol.51 , Issue.SUPPL. , pp. 139-145
    • Kiso, Y.1
  • 33
    • 0029027901 scopus 로고
    • Design and synthesis of HIV protease inhibitors containing allophenylnorstatine as a transition-state mimic
    • Kiso Y. Design and synthesis of HIV protease inhibitors containing allophenylnorstatine as a transition-state mimic. Adv. Exp. Med. Biol. 1995, 362:413-423.
    • (1995) Adv. Exp. Med. Biol. , vol.362 , pp. 413-423
    • Kiso, Y.1
  • 34
    • 0029943637 scopus 로고    scopus 로고
    • Design and synthesis of substrate-based peptidomimetic human immunodeficiency virus protease inhibitors containing the hydroxymethylcarbonyl isostere
    • Kiso Y. Design and synthesis of substrate-based peptidomimetic human immunodeficiency virus protease inhibitors containing the hydroxymethylcarbonyl isostere. Biopolymers 1996, 40:235-244.
    • (1996) Biopolymers , vol.40 , pp. 235-244
    • Kiso, Y.1
  • 35
    • 0033003998 scopus 로고    scopus 로고
    • Small dipeptide-based HIV protease inhibitors containing the hydroxymethylcarbonyl isostere as an ideal transition-state mimic
    • Kiso Y., Matsumoto H., Mizumoto S., Kimura T., Fujiwara Y., Akaji K. Small dipeptide-based HIV protease inhibitors containing the hydroxymethylcarbonyl isostere as an ideal transition-state mimic. Biopolymers 1999, 51:59-68.
    • (1999) Biopolymers , vol.51 , pp. 59-68
    • Kiso, Y.1    Matsumoto, H.2    Mizumoto, S.3    Kimura, T.4    Fujiwara, Y.5    Akaji, K.6
  • 36
    • 0028296812 scopus 로고
    • Multiple functions of pro-parts of aspartic proteinase zymogens
    • Koelsch G., Mares M., Metcalf P., Fusek M. Multiple functions of pro-parts of aspartic proteinase zymogens. FEBS Lett. 1994, 343:6-10.
    • (1994) FEBS Lett. , vol.343 , pp. 6-10
    • Koelsch, G.1    Mares, M.2    Metcalf, P.3    Fusek, M.4
  • 37
    • 0030873366 scopus 로고    scopus 로고
    • Generation of hemoglobin peptides in the acidic digestive vacuole of Plasmodium falciparum implicates peptide transport in amino acid production
    • Kolakovich K.A., Gluzman I.Y., Duffin K.L., Goldberg D.E. Generation of hemoglobin peptides in the acidic digestive vacuole of Plasmodium falciparum implicates peptide transport in amino acid production. Mol. Biochem. Parasitol. 1997, 87:123-135.
    • (1997) Mol. Biochem. Parasitol. , vol.87 , pp. 123-135
    • Kolakovich, K.A.1    Gluzman, I.Y.2    Duffin, K.L.3    Goldberg, D.E.4
  • 38
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
    • Krissinel E., Henrick K. Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Crystallogr. 2004, D60:2256-2268.
    • (2004) Acta Crystallogr. , vol.D60 , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2
  • 39
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 41
    • 0028825817 scopus 로고
    • Gene fusion expression systems in Escherichia coli
    • LaVallie E.R., McCoy J.M. Gene fusion expression systems in Escherichia coli. Curr. Opin. Biotechnol. 1995, 6:501-506.
    • (1995) Curr. Opin. Biotechnol. , vol.6 , pp. 501-506
    • LaVallie, E.R.1    McCoy, J.M.2
  • 42
    • 66049110565 scopus 로고    scopus 로고
    • Recombinant plasmepsin 1 from the human malaria parasite Plasmodium falciparum: enzymatic characterization, active site inhibitor design, and structural analysis
    • Liu P., Marzahn M.R., Robbins A.H., Gutierrez-de-Teran H., Rodriguez D., et al. Recombinant plasmepsin 1 from the human malaria parasite Plasmodium falciparum: enzymatic characterization, active site inhibitor design, and structural analysis. Biochemistry 2009, 48:4086-4099.
    • (2009) Biochemistry , vol.48 , pp. 4086-4099
    • Liu, P.1    Marzahn, M.R.2    Robbins, A.H.3    Gutierrez-de-Teran, H.4    Rodriguez, D.5
  • 43
    • 0030200511 scopus 로고    scopus 로고
    • Kinetic analysis of plasmepsins I and II aspartic proteases of the Plasmodium falciparum digestive vacuole
    • Luker K.E., Francis S.E., Gluzman I.Y., Goldberg D.E. Kinetic analysis of plasmepsins I and II aspartic proteases of the Plasmodium falciparum digestive vacuole. Mol. Biochem. Parasitol. 1996, 79:71-78.
    • (1996) Mol. Biochem. Parasitol. , vol.79 , pp. 71-78
    • Luker, K.E.1    Francis, S.E.2    Gluzman, I.Y.3    Goldberg, D.E.4
  • 44
    • 0035823008 scopus 로고    scopus 로고
    • Crystal structure of LexA: a conformational switch for regulation of self-cleavage
    • Luo Y., Pfuetzner R.A., Mosimann S., Paetzel M., Frey E.A., et al. Crystal structure of LexA: a conformational switch for regulation of self-cleavage. Cell 2001, 106:585-594.
    • (2001) Cell , vol.106 , pp. 585-594
    • Luo, Y.1    Pfuetzner, R.A.2    Mosimann, S.3    Paetzel, M.4    Frey, E.A.5
  • 45
    • 7044254904 scopus 로고    scopus 로고
    • Identification of peptidomimetic HTLV-I protease inhibitors containing hydroxymethylcarbonyl (HMC) isostere as the transition-state mimic
    • Maegawa H., Kimura T., Arii Y., Matsui Y., Kasai S., Hayashi Y., Kiso Y. Identification of peptidomimetic HTLV-I protease inhibitors containing hydroxymethylcarbonyl (HMC) isostere as the transition-state mimic. Bioorg. Med. Chem. Lett. 2004, 14:5925-5929.
    • (2004) Bioorg. Med. Chem. Lett. , vol.14 , pp. 5925-5929
    • Maegawa, H.1    Kimura, T.2    Arii, Y.3    Matsui, Y.4    Kasai, S.5    Hayashi, Y.6    Kiso, Y.7
  • 46
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews B.W. Solvent content of protein crystals. J. Mol. Biol. 1968, 33:491-497.
    • (1968) J. Mol. Biol. , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 47
    • 0026345730 scopus 로고
    • KNI-102, a novel tripeptide HIV protease inhibitor containing allophenylnorstatine as a transition-state mimic
    • Mimoto T., Imai J., Tanaka S., Hattori N., Kisanuki S., Akaji K., Kiso Y. KNI-102, a novel tripeptide HIV protease inhibitor containing allophenylnorstatine as a transition-state mimic. Chem. Pharm. Bull. (Tokyo) 1991, 39:3088-3090.
    • (1991) Chem. Pharm. Bull. (Tokyo) , vol.39 , pp. 3088-3090
    • Mimoto, T.1    Imai, J.2    Tanaka, S.3    Hattori, N.4    Kisanuki, S.5    Akaji, K.6    Kiso, Y.7
  • 48
    • 8044224013 scopus 로고    scopus 로고
    • Expression and characterisation of plasmepsin I from Plasmodium falciparum
    • Moon R.P., Tyas L., Certa U., Rupp K., Bur D., et al. Expression and characterisation of plasmepsin I from Plasmodium falciparum. Eur. J. Biochem. 1997, 244:552-560.
    • (1997) Eur. J. Biochem. , vol.244 , pp. 552-560
    • Moon, R.P.1    Tyas, L.2    Certa, U.3    Rupp, K.4    Bur, D.5
  • 49
    • 71249149462 scopus 로고    scopus 로고
    • Role of Plasmodium falciparum digestive vacuole plasmepsins in the specificity and antimalarial mode of action of cysteine and aspartic protease inhibitors
    • Moura P.A., Dame J.B., Fidock D.A. Role of Plasmodium falciparum digestive vacuole plasmepsins in the specificity and antimalarial mode of action of cysteine and aspartic protease inhibitors. Antimicrob. Agents Chemother. 2009, 53:4968-4978.
    • (2009) Antimicrob. Agents Chemother. , vol.53 , pp. 4968-4978
    • Moura, P.A.1    Dame, J.B.2    Fidock, D.A.3
  • 50
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov G.N., Vagin A.A., Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. 1997, D53:240-255.
    • (1997) Acta Crystallogr. , vol.D53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 51
    • 0037780064 scopus 로고    scopus 로고
    • High-affinity inhibition of a family of Plasmodium falciparum proteases by a designed adaptive inhibitor
    • Nezami A., Kimura T., Hidaka K., Kiso A., Liu J., et al. High-affinity inhibition of a family of Plasmodium falciparum proteases by a designed adaptive inhibitor. Biochemistry 2003, 42:8459-8464.
    • (2003) Biochemistry , vol.42 , pp. 8459-8464
    • Nezami, A.1    Kimura, T.2    Hidaka, K.3    Kiso, A.4    Liu, J.5
  • 52
    • 53549084594 scopus 로고    scopus 로고
    • Design of potent aspartic protease inhibitors to treat various diseases
    • Nguyen J.T., Hamada Y., Kimura T., Kiso Y. Design of potent aspartic protease inhibitors to treat various diseases. Arch. Pharm. (Weinheim) 2008, 341:523-535.
    • (2008) Arch. Pharm. (Weinheim) , vol.341 , pp. 523-535
    • Nguyen, J.T.1    Hamada, Y.2    Kimura, T.3    Kiso, Y.4
  • 53
    • 37548998994 scopus 로고    scopus 로고
    • Truncation and non-natural amino acid substitution studies on HTLV-I protease hexapeptidic inhibitors
    • Nguyen J.T., Zhang M., Kumada H.O., Itami A., Nishiyama K., et al. Truncation and non-natural amino acid substitution studies on HTLV-I protease hexapeptidic inhibitors. Bioorg. Med. Chem. Lett. 2008, 18:366-370.
    • (2008) Bioorg. Med. Chem. Lett. , vol.18 , pp. 366-370
    • Nguyen, J.T.1    Zhang, M.2    Kumada, H.O.3    Itami, A.4    Nishiyama, K.5
  • 55
    • 0035788107 scopus 로고    scopus 로고
    • Pushing the boundaries of molecular replacement with maximum likelihood
    • Read R.J. Pushing the boundaries of molecular replacement with maximum likelihood. Acta Crystallogr. 2001, D57:1373-1382.
    • (2001) Acta Crystallogr. , vol.D57 , pp. 1373-1382
    • Read, R.J.1
  • 56
    • 61349188242 scopus 로고    scopus 로고
    • Crystallographic evidence for noncoplanar catalytic aspartic acids in plasmepsin II resides in the Protein Data Bank
    • Robbins A.H., Dunn B.M., Agbandje-McKenna M., McKenna R. Crystallographic evidence for noncoplanar catalytic aspartic acids in plasmepsin II resides in the Protein Data Bank. Acta Crystallogr. 2009, D65:294-296.
    • (2009) Acta Crystallogr. , vol.D65 , pp. 294-296
    • Robbins, A.H.1    Dunn, B.M.2    Agbandje-McKenna, M.3    McKenna, R.4
  • 57
    • 0025354599 scopus 로고
    • Molecular and crystal structures of monoclinic porcine pepsin refined at 1.8Å resolution
    • Sielecki A.R., Fedorov A.A., Boodhoo A., Andreeva N.S., James M.N. Molecular and crystal structures of monoclinic porcine pepsin refined at 1.8Å resolution. J. Mol. Biol. 1990, 214:143-170.
    • (1990) J. Mol. Biol. , vol.214 , pp. 143-170
    • Sielecki, A.R.1    Fedorov, A.A.2    Boodhoo, A.3    Andreeva, N.S.4    James, M.N.5
  • 58
    • 16044374702 scopus 로고    scopus 로고
    • Structure and inhibition of plasmepsin II, a hemoglobin-degrading enzyme from Plasmodium falciparum
    • Silva A.M., Lee A.Y., Gulnik S.V., Maier P., Collins J., et al. Structure and inhibition of plasmepsin II, a hemoglobin-degrading enzyme from Plasmodium falciparum. Proc. Natl. Acad. Sci. USA 1996, 93:10034-10039.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 10034-10039
    • Silva, A.M.1    Lee, A.Y.2    Gulnik, S.V.3    Maier, P.4    Collins, J.5
  • 59
    • 0029983494 scopus 로고    scopus 로고
    • Expression of soluble cloned porcine pepsinogen A in Escherichia coli
    • Tanaka T., Yada R.Y. Expression of soluble cloned porcine pepsinogen A in Escherichia coli. Biochem. J. 1996, 315(Pt. 2):443-446.
    • (1996) Biochem. J. , vol.315 , Issue.PART. 2 , pp. 443-446
    • Tanaka, T.1    Yada, R.Y.2
  • 61
    • 37349016530 scopus 로고    scopus 로고
    • Protein crystallography for non-crystallographers or how to get the best (but not more) from the published macromolecular structures
    • Wlodawer A., Minor W., Dauter Z., Jaskolski M. Protein crystallography for non-crystallographers or how to get the best (but not more) from the published macromolecular structures. FEBS J. 2008, 275:1-21.
    • (2008) FEBS J. , vol.275 , pp. 1-21
    • Wlodawer, A.1    Minor, W.2    Dauter, Z.3    Jaskolski, M.4
  • 62
    • 33747750905 scopus 로고    scopus 로고
    • Recombinant expression and partial characterization of an active soluble histo-aspartic protease from Plasmodium falciparum
    • Xiao H., Sinkovits A.F., Bryksa B.C., Ogawa M., Yada R.Y. Recombinant expression and partial characterization of an active soluble histo-aspartic protease from Plasmodium falciparum. Protein Expr. Purif. 2006, 49:88-94.
    • (2006) Protein Expr. Purif. , vol.49 , pp. 88-94
    • Xiao, H.1    Sinkovits, A.F.2    Bryksa, B.C.3    Ogawa, M.4    Yada, R.Y.5
  • 63
    • 37849000476 scopus 로고    scopus 로고
    • Expression and enzymatic characterization of the soluble recombinant plasmepsin I from Plasmodium falciparum
    • Xiao H., Tanaka T., Ogawa M., Yada R.Y. Expression and enzymatic characterization of the soluble recombinant plasmepsin I from Plasmodium falciparum. Protein Eng. Des. Sel. 2007, 20:625-633.
    • (2007) Protein Eng. Des. Sel. , vol.20 , pp. 625-633
    • Xiao, H.1    Tanaka, T.2    Ogawa, M.3    Yada, R.Y.4
  • 65
    • 43749120718 scopus 로고    scopus 로고
    • Synthesis and activity of tetrapeptidic HTLV-I protease inhibitors possessing different P3-cap moieties
    • Zhang M., Nguyen J.T., Kumada H.O., Kimura T., Cheng M., Hayashi Y., Kiso Y. Synthesis and activity of tetrapeptidic HTLV-I protease inhibitors possessing different P3-cap moieties. Bioorg. Med. Chem. 2008, 16:5795-5802.
    • (2008) Bioorg. Med. Chem. , vol.16 , pp. 5795-5802
    • Zhang, M.1    Nguyen, J.T.2    Kumada, H.O.3    Kimura, T.4    Cheng, M.5    Hayashi, Y.6    Kiso, Y.7


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