메뉴 건너뛰기




Volumn 130, Issue 1, 2003, Pages 1-12

Plasmepsin 4, the food vacuole aspartic proteinase found in all Plasmodium spp. infecting man

Author keywords

Aspartic proteinase; Food vacuole; Malaria; Multigene family; Ortholog; Paralog; Plasmepsin; Plasmodium falciparum

Indexed keywords

ASPARTIC PROTEINASE; HISTOASPARTIC PROTEASE; PLASMEPSIN 4; PLASMEPSIN I; PLASMEPSIN II; UNCLASSIFIED DRUG;

EID: 0141448822     PISSN: 01666851     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0166-6851(03)00137-3     Document Type: Article
Times cited : (72)

References (47)
  • 2
    • 0037589002 scopus 로고    scopus 로고
    • Excess hemoglobin digestion and the osmotic stability of Plasmodium falciparum - Infected cells
    • Lew V.L., Tiffert T., Ginsburg H. Excess hemoglobin digestion and the osmotic stability of Plasmodium falciparum - infected cells. Blood. 101:2003;4189-4194.
    • (2003) Blood , vol.101 , pp. 4189-4194
    • Lew, V.L.1    Tiffert, T.2    Ginsburg, H.3
  • 3
    • 0000072220 scopus 로고
    • Studies on malarial parasites. IX. Chemical and metabolic changes during growth and multiplication in vivo and in vitro
    • Ball E.G., McKee R.W., Anfinsen C.B., Cruz W.O., Geiman Q.M. Studies on malarial parasites. IX. Chemical and metabolic changes during growth and multiplication in vivo and in vitro. J. Biol. Chem. 175:1948;547-571.
    • (1948) J. Biol. Chem. , vol.175 , pp. 547-571
    • Ball, E.G.1    McKee, R.W.2    Anfinsen, C.B.3    Cruz, W.O.4    Geiman, Q.M.5
  • 4
    • 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., Bryant M.L.et al. Molecular characterization and inhibition of a Plasmodium falciparum aspartic hemoglobinase. EMBO J. 13:1994;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    Bryant, M.L.6
  • 5
    • 0025255254 scopus 로고
    • Hemoglobin degradation in the malaria parasite: An ordered process in a unique organelle
    • Goldberg D.E., Slater A.F., Cerami A., Henderson G.B. Hemoglobin degradation in the malaria parasite: an ordered process in a unique organelle. Proc. Natl. Acad. Sci. U.S.A. 87:1990;2931-2935.
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 2931-2935
    • Goldberg, D.E.1    Slater, A.F.2    Cerami, A.3    Henderson, G.B.4
  • 6
    • 0001402353 scopus 로고    scopus 로고
    • Cysteine proteinase inhibitors block early steps in hemoglobin degradation by cultured malaria parasites
    • Gamboa-de D.N., Rosenthal P.J. Cysteine proteinase inhibitors block early steps in hemoglobin degradation by cultured malaria parasites. Blood. 87:1996;4448-4454.
    • (1996) Blood , vol.87 , pp. 4448-4454
    • Gamboa-de, D.N.1    Rosenthal, P.J.2
  • 7
    • 0028948564 scopus 로고
    • Plasmodium falciparum: Effects of proteinase inhibitors on globin hydrolysis by cultured malaria parasites
    • Rosenthal P.J. Plasmodium falciparum: effects of proteinase inhibitors on globin hydrolysis by cultured malaria parasites. Exp. Parasitol. 80:1995;272-281.
    • (1995) Exp. Parasitol. , vol.80 , pp. 272-281
    • Rosenthal, P.J.1
  • 8
    • 0024334026 scopus 로고
    • Plasmodium falciparum: Inhibitors of lysosomal cysteine proteinases inhibit a trophozoite proteinase and block parasite development
    • Rosenthal P.J., McKerrow J.H., Rasnick D., Leech J.H. Plasmodium falciparum: inhibitors of lysosomal cysteine proteinases inhibit a trophozoite proteinase and block parasite development. Mol. Biochem. Parasitol. 35:1989;177-183.
    • (1989) Mol. Biochem. Parasitol. , vol.35 , pp. 177-183
    • Rosenthal, P.J.1    McKerrow, J.H.2    Rasnick, D.3    Leech, J.H.4
  • 9
    • 0024208917 scopus 로고
    • A malarial cysteine proteinase is necessary for hemoglobin degradation by Plasmodium falciparum
    • Rosenthal P.J., McKerrow J.H., Aikawa M., Nagasawa H., Leech J.H. A malarial cysteine proteinase is necessary for hemoglobin degradation by Plasmodium falciparum. J. Clin. Invest. 82:1988;1560-1566.
    • (1988) J. Clin. Invest. , vol.82 , pp. 1560-1566
    • Rosenthal, P.J.1    McKerrow, J.H.2    Aikawa, M.3    Nagasawa, H.4    Leech, J.H.5
  • 10
    • 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. 17:2001;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
  • 11
    • 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. U.S.A. 99:2002;990-995.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 990-995
    • Banerjee, R.1    Liu, J.2    Beatty, W.3    Pelosof, L.4    Klemba, M.5    Goldberg, D.E.6
  • 12
    • 0033553410 scopus 로고    scopus 로고
    • Plasmepsin II an acidic hemoglobinase from the Plasmodium falciparum food vacuole, is active at neutral pH on the host erythrocyte membrane skeleton
    • Le Bonniec S., Deregnaucourt C., Redeker V., Banerjee R., Grellier P., Goldberg D.E.et al. Plasmepsin II an acidic hemoglobinase from the Plasmodium falciparum food vacuole, is active at neutral pH on the host erythrocyte membrane skeleton. J. Biol. Chem. 274:1999;14218-14223.
    • (1999) J. Biol. Chem. , vol.274 , pp. 14218-14223
    • Le Bonniec, S.1    Deregnaucourt, C.2    Redeker, V.3    Banerjee, R.4    Grellier, P.5    Goldberg, D.E.6
  • 13
    • 0037181136 scopus 로고    scopus 로고
    • Activity and inhibition of plasmepsin IV, a new aspartic proteinase from the malaria parasite, Plasmodium falciparum
    • Wyatt D.M., Berry C. Activity and inhibition of plasmepsin IV, a new aspartic proteinase from the malaria parasite, Plasmodium falciparum. FEBS Lett. 513:2002;159-162.
    • (2002) FEBS Lett. , vol.513 , pp. 159-162
    • Wyatt, D.M.1    Berry, C.2
  • 14
    • 0028948564 scopus 로고
    • Plasmodium falciparum: Effects of proteinase inhibitors on globin hydrolysis by cultured malaria parasites
    • Rosenthal P.J. Plasmodium falciparum: effects of proteinase inhibitors on globin hydrolysis by cultured malaria parasites. Exp. Parasitol. 80:1995;272-281.
    • (1995) Exp. Parasitol. , vol.80 , pp. 272-281
    • Rosenthal, P.J.1
  • 15
    • 0037133223 scopus 로고    scopus 로고
    • Identification and characterization of allophenylnorstatine-based inhibitors of plasmepsin II an antimalarial target
    • Nezami A., Luque I., Kimura T., Kiso Y., Freire E. Identification and characterization of allophenylnorstatine-based inhibitors of plasmepsin II an antimalarial target. Biochemistry. 41:2002;2273-2280.
    • (2002) Biochemistry , vol.41 , pp. 2273-2280
    • Nezami, A.1    Luque, I.2    Kimura, T.3    Kiso, Y.4    Freire, E.5
  • 16
    • 0033594354 scopus 로고    scopus 로고
    • Potent, low-molecular-weight non-peptide inhibitors of malarial aspartyl protease plasmepsin II
    • Haque T.S., Skillman A.G., Lee C.E., Habashita H., Gluzman I.Y., Ewing T.J.A.et al. Potent, low-molecular-weight non-peptide inhibitors of malarial aspartyl protease plasmepsin II. J. Med. Chem. 42:1999;1428-1440.
    • (1999) J. Med. Chem. , vol.42 , pp. 1428-1440
    • Haque, T.S.1    Skillman, A.G.2    Lee, C.E.3    Habashita, H.4    Gluzman, I.Y.5    Ewing, T.J.A.6
  • 17
    • 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. 79:1996;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
  • 18
    • 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., Bhat T.N.et al. Structure and inhibition of plasmepsin II a hemoglobin-degrading enzyme from Plasmodium falciparum. Proc. Natl. Acad. Sci. U.S.A. 93:1996;10034-10039.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 10034-10039
    • Silva, A.M.1    Lee, A.Y.2    Gulnik, S.V.3    Maier, P.4    Collins, J.5    Bhat, T.N.6
  • 19
    • 0034864129 scopus 로고    scopus 로고
    • New class of small nonpeptidyl compounds blocks Plasmodium falciparum development in vitro by inhibiting plasmepsins
    • Jiang S.P., Prigge S.T., Wei L., Gao Y.E., Hudson T.H., Gerena L.et al. New class of small nonpeptidyl compounds blocks Plasmodium falciparum development in vitro by inhibiting plasmepsins. Antimicrob. Agents Chemother. 45:2001;2577-2584.
    • (2001) Antimicrob. Agents Chemother. , vol.45 , pp. 2577-2584
    • Jiang, S.P.1    Prigge, S.T.2    Wei, L.3    Gao, Y.E.4    Hudson, T.H.5    Gerena, L.6
  • 21
    • 0027262263 scopus 로고
    • Rapid isolation of DNA from trypanosomatid protozoa using a simple mini-prep procedure
    • Medina-Acosta E., Cross G.A.M. Rapid isolation of DNA from trypanosomatid protozoa using a simple mini-prep procedure. Mol. Biochem. Parasitol. 59:1993;327-329.
    • (1993) Mol. Biochem. Parasitol. , vol.59 , pp. 327-329
    • Medina-Acosta, E.1    Cross, G.A.M.2
  • 23
    • 0028287766 scopus 로고
    • Sequence, expression and modeled structure of an aspartic proteinase from the human malaria parasite Plasmodium falciparum
    • Dame J.B., Reddy G.R., Yowell C.A., Dunn B.M., Kay J., Berry C. Sequence, expression and modeled structure of an aspartic proteinase from the human malaria parasite Plasmodium falciparum. Mol. Biochem. Parasitol. 64:1994;177-190.
    • (1994) Mol. Biochem. Parasitol. , vol.64 , pp. 177-190
    • Dame, J.B.1    Reddy, G.R.2    Yowell, C.A.3    Dunn, B.M.4    Kay, J.5    Berry, C.6
  • 24
    • 0032998957 scopus 로고    scopus 로고
    • Karyotype and synteny among the chromosomes of all four species of human malaria parasite
    • Carlton J.M.R., Galinski M.R., Barnwell J.W., Dame J.B. Karyotype and synteny among the chromosomes of all four species of human malaria parasite. Mol. Biochem. Parasitol. 101:1999;23-32.
    • (1999) Mol. Biochem. Parasitol. , vol.101 , pp. 23-32
    • Carlton, J.M.R.1    Galinski, M.R.2    Barnwell, J.W.3    Dame, J.B.4
  • 25
    • 0023691425 scopus 로고
    • Genetic applications of an inverse polymerase chain reaction
    • Ochman H., Gerber A.S., Hartl D.L. Genetic applications of an inverse polymerase chain reaction. Genetics. 120:1988;621-623.
    • (1988) Genetics , vol.120 , pp. 621-623
    • Ochman, H.1    Gerber, A.S.2    Hartl, D.L.3
  • 26
    • 0037015614 scopus 로고    scopus 로고
    • Genome sequence of the human malaria parasite Plasmodium falciparum
    • Gardner M.J., Hall N., Fung E., White O., Berriman M., Hyman R.W.et al. Genome sequence of the human malaria parasite Plasmodium falciparum. Nature. 419:2002;498-511.
    • (2002) Nature , vol.419 , pp. 498-511
    • Gardner, M.J.1    Hall, N.2    Fung, E.3    White, O.4    Berriman, M.5    Hyman, R.W.6
  • 27
    • 0031282557 scopus 로고    scopus 로고
    • Plasmodium falciparum P. vivax and P. malariae: A comparison of the active site properties of plasmepsins cloned and expressed from three different species of the malaria parasite
    • Westling J., Yowell C.A., Majer P., Erickson J.W., Dame J.B., Dunn B.M. Plasmodium falciparum P. vivax and P. malariae: a comparison of the active site properties of plasmepsins cloned and expressed from three different species of the malaria parasite. Exp. Parasitol. 87:1997;185-193.
    • (1997) Exp. Parasitol. , vol.87 , pp. 185-193
    • Westling, J.1    Yowell, C.A.2    Majer, P.3    Erickson, J.W.4    Dame, J.B.5    Dunn, B.M.6
  • 29
    • 0027968068 scopus 로고
    • Clustal-W - Improving the sensitivity of progressive multiple sequence alignment through sequence weighting
    • Thompson J.D., Higgins D.G., Gibson T.J. Clustal-W - improving the sensitivity of progressive multiple sequence alignment through sequence weighting. Nucleic Acids Res. 22:1994;4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 30
    • 0000122573 scopus 로고
    • Phylogeny inference package (version 3.2)
    • Felsenstein J. Phylogeny inference package (version 3.2). Cladistics. 5:1989;164-166.
    • (1989) Cladistics , vol.5 , pp. 164-166
    • Felsenstein, J.1
  • 31
    • 0030807655 scopus 로고    scopus 로고
    • BIONJ: An improved version of the NJ algorithm based on a simple model of sequence data
    • Gascuel O. BIONJ: an improved version of the NJ algorithm based on a simple model of sequence data. Mol. Biol. Evol. 14:1997;685-695.
    • (1997) Mol. Biol. Evol. , vol.14 , pp. 685-695
    • Gascuel, O.1
  • 32
    • 0031713287 scopus 로고    scopus 로고
    • Role for the Plasmodium falciparum digestive vacuole in chloroquine resistance
    • Saliba K.J., Folb P.I., Smith P.J. Role for the Plasmodium falciparum digestive vacuole in chloroquine resistance. Biochemical Pharmacology. 56:1998;3.
    • (1998) Biochemical Pharmacology , vol.56 , pp. 3
    • Saliba, K.J.1    Folb, P.I.2    Smith, P.J.3
  • 33
    • 0033636607 scopus 로고    scopus 로고
    • Mutations in the P. falciparum digestive vacuole transmembrane protein PfCRT and evidence for their role in chloroquine resistance
    • Fidock D.A., Nomura T., Talley A.K., Cooper R.A., Dzekunov S.M., Ferdig M.T.et al. Mutations in the P. falciparum digestive vacuole transmembrane protein PfCRT and evidence for their role in chloroquine resistance. Mol. Cell. 6:2000;861-871.
    • (2000) Mol. Cell , vol.6 , pp. 861-871
    • Fidock, D.A.1    Nomura, T.2    Talley, A.K.3    Cooper, R.A.4    Dzekunov, S.M.5    Ferdig, M.T.6
  • 34
    • 0016711037 scopus 로고
    • High resolution two-dimensional electrophoresis of proteins
    • O'Farrell P.H. High resolution two-dimensional electrophoresis of proteins. J. Biol. Chem. 250:1975;4007-4021.
    • (1975) J. Biol. Chem. , vol.250 , pp. 4007-4021
    • O'Farrell, P.H.1
  • 35
    • 0030898043 scopus 로고    scopus 로고
    • Identification of mouse liver proteins on two-dimensional electrophoresis gels by matrix-assisted laser desorption/ionization mass spectrometry of in situ enzymatic digests
    • O'Connell K.L., Stults J.T. Identification of mouse liver proteins on two-dimensional electrophoresis gels by matrix-assisted laser desorption/ionization mass spectrometry of in situ enzymatic digests. Electrophoresis. 18:1997;349-359.
    • (1997) Electrophoresis , vol.18 , pp. 349-359
    • O'Connell, K.L.1    Stults, J.T.2
  • 36
    • 0032961627 scopus 로고    scopus 로고
    • Mass spectrometric identification of proteins from silver-stained polyacrylamide gel: A method for the removal of silver ions to enhance sensitivity
    • Gharahdaghi F., Weinberg C.R., Meagher D.A., Imai B.S., Mische S.M. Mass spectrometric identification of proteins from silver-stained polyacrylamide gel: a method for the removal of silver ions to enhance sensitivity. Electrophoresis. 20:1999;601-605.
    • (1999) Electrophoresis , vol.20 , pp. 601-605
    • Gharahdaghi, F.1    Weinberg, C.R.2    Meagher, D.A.3    Imai, B.S.4    Mische, S.M.5
  • 37
    • 0033565832 scopus 로고    scopus 로고
    • Role of accurate mass measurement (±10 ppm) in protein identification strategies employing MS or MS/MS and database searching
    • Clauser K.R., Baker P., Burlingame A.L. Role of accurate mass measurement (±10. ppm) in protein identification strategies employing MS or MS/MS and database searching Anal. Chem. 71:1999;2871-2882.
    • (1999) Anal. Chem. , vol.71 , pp. 2871-2882
    • Clauser, K.R.1    Baker, P.2    Burlingame, A.L.3
  • 38
    • 0037689718 scopus 로고    scopus 로고
    • Additional plasmepsins
    • Barrett AJ, Rawlings ND, Woessner FJ, editors. London: Academic Press
    • Dame JB. Additional plasmepsins. In: Barrett AJ, Rawlings ND, Woessner FJ, editors. Handbook of proteolytic enzymes. London: Academic Press; 1998. p. 862-4.
    • (1998) Handbook of Proteolytic Enzymes , pp. 862-864
    • Dame, J.B.1
  • 39
    • 0035662389 scopus 로고    scopus 로고
    • Profiling the malaria genome: A gene survey of three species of malaria parasite with comparison to other apicomplexan species
    • Carlton J.M.R., Muller R., Yowell C.A., Fluegge M.R., Sturrock K.A., Pritt J.R.et al. Profiling the malaria genome: a gene survey of three species of malaria parasite with comparison to other apicomplexan species. Mol. Biochem. Parasitol. 118:2001;201-210.
    • (2001) Mol. Biochem. Parasitol. , vol.118 , pp. 201-210
    • Carlton, J.M.R.1    Muller, R.2    Yowell, C.A.3    Fluegge, M.R.4    Sturrock, K.A.5    Pritt, J.R.6
  • 40
    • 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., Jacquet C.et al. Expression and characterisation of plasmepsin I from Plasmodium falciparum. Eur. J. Biochem. 244:1997;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    Jacquet, C.6
  • 41
    • 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. 272:1997;14961-14968.
    • (1997) J. Biol. Chem. , vol.272 , pp. 14961-14968
    • Francis, S.E.1    Banerjee, R.2    Goldberg, D.E.3
  • 42
    • 0031894719 scopus 로고    scopus 로고
    • Structural analysis of plasmepsin II - A comparison with human aspartic proteases
    • Silva A.M., Lee A.Y., Erickson J.W., Goldberg D.E. Structural analysis of plasmepsin II - a comparison with human aspartic proteases. Aspartic Proteinases. 436:1998;363-373.
    • (1998) Aspartic Proteinases , vol.436 , pp. 363-373
    • Silva, A.M.1    Lee, A.Y.2    Erickson, J.W.3    Goldberg, D.E.4
  • 43
    • 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., Moon R.P.et al. A distinct member of the aspartic proteinase gene family from the human malaria parasite Plasmodium falciparum. FEBS Lett. 447:1999;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    Moon, R.P.6
  • 44
    • 0033430156 scopus 로고    scopus 로고
    • The aspartic proteinase from the rodent parasite Plasmodium berghei as a potential model for plasmepsins from the human malaria parasite Plasmodium falciparum
    • Humphreys M.J., Moon R.P., Klinder A., Fowler S.D., Rupp K., Bur D.et al. The aspartic proteinase from the rodent parasite Plasmodium berghei as a potential model for plasmepsins from the human malaria parasite Plasmodium falciparum. FEBS Lett. 463:1999;43-48.
    • (1999) FEBS Lett. , vol.463 , pp. 43-48
    • Humphreys, M.J.1    Moon, R.P.2    Klinder, A.3    Fowler, S.D.4    Rupp, K.5    Bur, D.6
  • 45
    • 0037015592 scopus 로고    scopus 로고
    • Genome sequence and comparative analysis of the model rodent malaria parasite Plasmodium yoelii yoelii
    • Carlton J.M., Angiuoli S.V., Suh B.B., Kooij T.W., Pertea M., Silva J.C.et al. Genome sequence and comparative analysis of the model rodent malaria parasite Plasmodium yoelii yoelii. Nature. 419:2002;512-519.
    • (2002) Nature , vol.419 , pp. 512-519
    • Carlton, J.M.1    Angiuoli, S.V.2    Suh, B.B.3    Kooij, T.W.4    Pertea, M.5    Silva, J.C.6
  • 46
    • 0037015625 scopus 로고    scopus 로고
    • Sequence of Plasmodium falciparum chromosomes 1, 3-9 and 13
    • Hall N., Pain A., Berriman M., Churcher C., Harris B., Harris D.et al. Sequence of Plasmodium falciparum chromosomes 1, 3-9 and 13. Nature. 419:2002;527-531.
    • (2002) Nature , vol.419 , pp. 527-531
    • Hall, N.1    Pain, A.2    Berriman, M.3    Churcher, C.4    Harris, B.5    Harris, D.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.