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Volumn 156, Issue 2, 2005, Pages 203-214

Gene discovery in the Acanthamoeba castellanii genome

Author keywords

Acanthamoeba; Free living amoeba; Genome sequence; Metabolism

Indexed keywords

ACANTHAMOEBA; ACANTHAMOEBA CASTELLANII; DICTYOSTELIUM DISCOIDEUM; ENTAMOEBA HISTOLYTICA; PROTISTA;

EID: 22744458161     PISSN: 14344610     EISSN: 16180941     Source Type: Journal    
DOI: 10.1016/j.protis.2005.04.001     Document Type: Article
Times cited : (56)

References (69)
  • 2
    • 0025226099 scopus 로고
    • Occurrence, metabolism, metabolic role, and industrial uses of bacterial polyhydroxyalkanoates
    • A.J. Anderson, and E.A. Dawes Occurrence, metabolism, metabolic role, and industrial uses of bacterial polyhydroxyalkanoates Microbiol Rev 54 1990 450 472
    • (1990) Microbiol Rev , vol.54 , pp. 450-472
    • Anderson, A.J.1    Dawes, E.A.2
  • 3
    • 4344560867 scopus 로고    scopus 로고
    • Novel non-coding RNAs in Dictyostelium discoideum and their expression during development
    • A. Aspegren, A. Hinas, P. Larsson, A. Larsson, and F. Söderbom Novel non-coding RNAs in Dictyostelium discoideum and their expression during development Nucleic Acids Res 32 2004 4646 4656
    • (2004) Nucleic Acids Res , vol.32 , pp. 4646-4656
    • Aspegren, A.1    Hinas, A.2    Larsson, P.3    Larsson, A.4    Söderbom, F.5
  • 4
    • 0034602344 scopus 로고    scopus 로고
    • A kingdom-level phylogeny of eukaryotes based on combined protein data
    • S.L. Baldauf, A.J. Roger, I. Wenk-Siefert, and W.F. Doolittle A kingdom-level phylogeny of eukaryotes based on combined protein data Science 290 2000 972 977
    • (2000) Science , vol.290 , pp. 972-977
    • Baldauf, S.L.1    Roger, A.J.2    Wenk-Siefert, I.3    Doolittle, W.F.4
  • 6
    • 0034808356 scopus 로고    scopus 로고
    • Biofilms augment the number of free-living amoebae in dental unit waterlines
    • J. Barbeau, and T. Buhler Biofilms augment the number of free-living amoebae in dental unit waterlines Res Microbiol 152 2001 753 760
    • (2001) Res Microbiol , vol.152 , pp. 753-760
    • Barbeau, J.1    Buhler, T.2
  • 9
    • 0028340887 scopus 로고
    • Role of alginate lyase in cell detachment of Pseudomonas aeruginosa
    • A. Boyd, and A.M. Chakrabarty Role of alginate lyase in cell detachment of Pseudomonas aeruginosa Appl Environ Microbiol 60 1994 2355 2359
    • (1994) Appl Environ Microbiol , vol.60 , pp. 2355-2359
    • Boyd, A.1    Chakrabarty, A.M.2
  • 11
    • 0022560056 scopus 로고
    • Molecular biology of DNA in Acanthamoeba, Amoeba, Entamoeba, and Naegleria
    • T.J. Byers Molecular biology of DNA in Acanthamoeba, Amoeba, Entamoeba, and Naegleria Int Rev Cytol 99 1986 311 341
    • (1986) Int Rev Cytol , vol.99 , pp. 311-341
    • Byers, T.J.1
  • 12
    • 15444352324 scopus 로고    scopus 로고
    • Role of carbohydrate-mediated adherence in cytopathogenic mechanisms of Acanthamoeba
    • Z. Cao, D.M. Jefferson, and N. Panjwani Role of carbohydrate-mediated adherence in cytopathogenic mechanisms of Acanthamoeba J Biol Chem 273 1998 15838 15845
    • (1998) J Biol Chem , vol.273 , pp. 15838-15845
    • Cao, Z.1    Jefferson, D.M.2    Panjwani, N.3
  • 13
    • 2542584659 scopus 로고    scopus 로고
    • In vivo interactions of the Acanthamoeba TBP gene promoter
    • L. Chen, Z. Peng, and E. Bateman In vivo interactions of the Acanthamoeba TBP gene promoter Nucleic Acids Res 32 2004 1251 1260
    • (2004) Nucleic Acids Res , vol.32 , pp. 1251-1260
    • Chen, L.1    Peng, Z.2    Bateman, E.3
  • 14
    • 0030884257 scopus 로고    scopus 로고
    • Interaction of Mycobacterium avium with environmental amoebae enhances virulence
    • J.D. Cirillo, S. Falkow, L.S. Tompkins, and L.E. Bermudez Interaction of Mycobacterium avium with environmental amoebae enhances virulence Infect Immun 65 1997 3759 3767
    • (1997) Infect Immun , vol.65 , pp. 3759-3767
    • Cirillo, J.D.1    Falkow, S.2    Tompkins, L.S.3    Bermudez, L.E.4
  • 15
    • 0032794165 scopus 로고    scopus 로고
    • Intracellular growth in Acanthamoeba castellanii affects monocyte entry mechanisms and enhances virulence of Legionella pneumophila
    • J.D. Cirillo, S.L.G. Cirillo, L. Yan, L.E. Bermudez, S. Falkow, and L.S. Tompkins Intracellular growth in Acanthamoeba castellanii affects monocyte entry mechanisms and enhances virulence of Legionella pneumophila Infect Immun 67 1999 4427 4434
    • (1999) Infect Immun , vol.67 , pp. 4427-4434
    • Cirillo, J.D.1    Cirillo, S.L.G.2    Yan, L.3    Bermudez, L.E.4    Falkow, S.5    Tompkins, L.S.6
  • 16
    • 0036427585 scopus 로고    scopus 로고
    • Bacteria and protozoa as integral components of the forest ecosystem - Their role in creating a naturally varied soil fertility
    • M. Clarholm Bacteria and protozoa as integral components of the forest ecosystem - their role in creating a naturally varied soil fertility Antonie Van Leeuwenhoek 81 2002 309 318
    • (2002) Antonie Van Leeuwenhoek , vol.81 , pp. 309-318
    • Clarholm, M.1
  • 21
    • 0000122573 scopus 로고
    • PHYLIP - Phylogeny inference package (version 3.2)
    • J. Felsenstein PHYLIP - phylogeny inference package (version 3.2) Cladistics 5 1989 164 166
    • (1989) Cladistics , vol.5 , pp. 164-166
    • Felsenstein, J.1
  • 22
    • 0031801558 scopus 로고    scopus 로고
    • Bacterial alginate biosynthesis - Recent progress and future prospects
    • P. Gacesa Bacterial alginate biosynthesis - recent progress and future prospects Microbiology 144 1998 1133 1143
    • (1998) Microbiology , vol.144 , pp. 1133-1143
    • Gacesa, P.1
  • 23
    • 3142724950 scopus 로고    scopus 로고
    • Cloning and characterization of a novel mannose-binding protein of Acanthamoeba
    • M. Garate, Z. Cao, E. Bateman, and N. Panjwani Cloning and characterization of a novel mannose-binding protein of Acanthamoeba J Biol Chem 279 2004 29849 29856
    • (2004) J Biol Chem , vol.279 , pp. 29849-29856
    • Garate, M.1    Cao, Z.2    Bateman, E.3    Panjwani, N.4
  • 25
    • 0348077471 scopus 로고    scopus 로고
    • Interactions between Salmonella typhimurium and Acanthamoeba polyphaga, and observation of a new mode of intracellular growth within contractile vacuoles
    • W.H. Gaze, N. Burroughs, M.P. Gallagher, and E.M.H. Wellington Interactions between Salmonella typhimurium and Acanthamoeba polyphaga, and observation of a new mode of intracellular growth within contractile vacuoles Microbial Ecol 46 2003 358 369
    • (2003) Microbial Ecol , vol.46 , pp. 358-369
    • Gaze, W.H.1    Burroughs, N.2    Gallagher, M.P.3    Wellington, E.M.H.4
  • 27
    • 0038051534 scopus 로고    scopus 로고
    • Parachlamydia acanthamoeba is endosymbiotic or lytic for Acanthamoeba polyphaga depending on the incubation temperature
    • G. Greub, B. La Scola, and D. Raoult Parachlamydia acanthamoeba is endosymbiotic or lytic for Acanthamoeba polyphaga depending on the incubation temperature Ann N Y Acad Sci 990 2003 628 634
    • (2003) Ann N Y Acad Sci , vol.990 , pp. 628-634
    • Greub, G.1    La Scola, B.2    Raoult, D.3
  • 29
    • 0042844806 scopus 로고    scopus 로고
    • Effects of mannose on Acanthamoeba castellanii proliferation and cytolytic ability to corneal epithelial cells
    • M. Hurt, J. Niederkorn, and H. Alizadeh Effects of mannose on Acanthamoeba castellanii proliferation and cytolytic ability to corneal epithelial cells Invest Ophthlmol Vis Sci 44 2003 3424 3431
    • (2003) Invest Ophthlmol Vis Sci , vol.44 , pp. 3424-3431
    • Hurt, M.1    Niederkorn, J.2    Alizadeh, H.3
  • 31
    • 0033975687 scopus 로고    scopus 로고
    • Interaction between Burkholderia pseudomallei and Acanthamoeba species results in coiling phagocytosis, endamebic bacterial survival, and escape
    • T.J.J. Inglis, P. Rigby, T.A. Robertson, N.S. Dutton, M. Henderson, and B.J. Chang Interaction between Burkholderia pseudomallei and Acanthamoeba species results in coiling phagocytosis, endamebic bacterial survival, and escape Infect Immun 68 2000 1681 1686
    • (2000) Infect Immun , vol.68 , pp. 1681-1686
    • Inglis, T.J.J.1    Rigby, P.2    Robertson, T.A.3    Dutton, N.S.4    Henderson, M.5    Chang, B.J.6
  • 32
    • 0029132967 scopus 로고
    • Purification and molecular cloning of a major antibacterial protein of the protozoan parasite Entamoeba histolytica with lysozyme-like properties
    • T. Jacobs, and M. Leippe Purification and molecular cloning of a major antibacterial protein of the protozoan parasite Entamoeba histolytica with lysozyme-like properties Eur J Biochem 231 1995 831 838
    • (1995) Eur J Biochem , vol.231 , pp. 831-838
    • Jacobs, T.1    Leippe, M.2
  • 33
    • 0037962406 scopus 로고    scopus 로고
    • Evolution of key cell signaling and adhesion protein families predates animal origins
    • N. King, C.T. Hittinger, and S.B. Carroll Evolution of key cell signaling and adhesion protein families predates animal origins Science 301 2003 361 363
    • (2003) Science , vol.301 , pp. 361-363
    • King, N.1    Hittinger, C.T.2    Carroll, S.B.3
  • 34
    • 0035262140 scopus 로고    scopus 로고
    • Survival of Coxiella burnetii within free-living amoeba Acanthamoeba castellanii
    • B. La Scola, and D. Raoult Survival of Coxiella burnetii within free-living amoeba Acanthamoeba castellanii Clin Microbiol Infect 7 2001 75 79
    • (2001) Clin Microbiol Infect , vol.7 , pp. 75-79
    • La Scola, B.1    Raoult, D.2
  • 36
    • 0028073698 scopus 로고
    • Amoebapores, a family of membranolytic peptides from cytoplasmic granules of Entamoeba histolytica: Isolation, primary structure, and pore formation in bacterial cytoplasmic membranes
    • M. Leippe, J. Andra, R. Nickel, E. Tannich, and H.J. Muller-Eberhard Amoebapores, a family of membranolytic peptides from cytoplasmic granules of Entamoeba histolytica: isolation, primary structure, and pore formation in bacterial cytoplasmic membranes Mol Microbiol 14 1994 895 904
    • (1994) Mol Microbiol , vol.14 , pp. 895-904
    • Leippe, M.1    Andra, J.2    Nickel, R.3    Tannich, E.4    Muller-Eberhard, H.J.5
  • 38
    • 0030854739 scopus 로고    scopus 로고
    • TRNAscan-SE: A program for improved detection of transfer RNA genes in genomic sequence
    • T.M. Lowe, and S.R. Eddy tRNAscan-SE: a program for improved detection of transfer RNA genes in genomic sequence Nucleic Acids Res 25 1997 955 964
    • (1997) Nucleic Acids Res , vol.25 , pp. 955-964
    • Lowe, T.M.1    Eddy, S.R.2
  • 39
    • 0033582628 scopus 로고    scopus 로고
    • A computational screen for methylation guide snoRNAs in yeast
    • T.M. Lowe, and S.R. Eddy A computational screen for methylation guide snoRNAs in yeast Science 283 1999 1168 1171
    • (1999) Science , vol.283 , pp. 1168-1171
    • Lowe, T.M.1    Eddy, S.R.2
  • 40
    • 0019887388 scopus 로고
    • Nucleotide sequences of Acanthamoeba castellanii 5S and 5.8S ribosomal ribonucleic acids: Phylogenetic and comparative structural analyses
    • R.M. MacKay, and W.F. Doolittle Nucleotide sequences of Acanthamoeba castellanii 5S and 5.8S ribosomal ribonucleic acids: phylogenetic and comparative structural analyses Nucleic Acids Res 9 1981 3321 3334
    • (1981) Nucleic Acids Res , vol.9 , pp. 3321-3334
    • MacKay, R.M.1    Doolittle, W.F.2
  • 41
    • 8844252293 scopus 로고    scopus 로고
    • TigrScan and GlimmerHMM: Two open-source ab initio eukaryotic gene-finders
    • W.H. Majoros, M. Pertea, and S.L. Salzberg TigrScan and GlimmerHMM: two open-source ab initio eukaryotic gene-finders Bioinformatics 20 2004 2878 2879
    • (2004) Bioinformatics , vol.20 , pp. 2878-2879
    • Majoros, W.H.1    Pertea, M.2    Salzberg, S.L.3
  • 42
    • 0027312126 scopus 로고
    • Cloning, sequence analysis, and expression in Escherichia coli of a gene encoding an alginate lyase from Pseudomonas sp. OS-ALG-9
    • H. Maki, A. Mori, K. Fujiyama, S. Kinoshita, and T. Yoshida Cloning, sequence analysis, and expression in Escherichia coli of a gene encoding an alginate lyase from Pseudomonas sp. OS-ALG-9 J Gen Microbiol 139 1993 987 993
    • (1993) J Gen Microbiol , vol.139 , pp. 987-993
    • Maki, H.1    Mori, A.2    Fujiyama, K.3    Kinoshita, S.4    Yoshida, T.5
  • 43
    • 0037398448 scopus 로고    scopus 로고
    • Acanthamoeba spp. as agents of disease in humans
    • F. Marciano-Cabral, and G. Cabral Acanthamoeba spp. as agents of disease in humans Clin Microbiol Rev 16 2003 273 307
    • (2003) Clin Microbiol Rev , vol.16 , pp. 273-307
    • Marciano-Cabral, F.1    Cabral, G.2
  • 45
    • 0032559349 scopus 로고    scopus 로고
    • Unconventional myosins in cell movement, membrane traffic, and signal transduction
    • V. Mermall, P.L. Post, and M.S. Mooseker Unconventional myosins in cell movement, membrane traffic, and signal transduction Science 279 1998 527 533
    • (1998) Science , vol.279 , pp. 527-533
    • Mermall, V.1    Post, P.L.2    Mooseker, M.S.3
  • 46
    • 0035089378 scopus 로고    scopus 로고
    • Enlarged Chlamydia-like organisms as spontaneous infection of Acanthamoeba castellanii
    • R. Michel, K.-D. Müller, and R. Hoffmann Enlarged Chlamydia-like organisms as spontaneous infection of Acanthamoeba castellanii Parasitol Res 87 2001 248 251
    • (2001) Parasitol Res , vol.87 , pp. 248-251
    • Michel, R.1    Müller, K.-D.2    Hoffmann, R.3
  • 47
    • 0033936494 scopus 로고    scopus 로고
    • Mycobacterium avium grown in Acanthamoeba castellanii is protected from the effects of antimicrobials
    • E.C. Miltner, and L.E. Bermudez Mycobacterium avium grown in Acanthamoeba castellanii is protected from the effects of antimicrobials Antimicrob Agents Chemother 44 2000 1990 1994
    • (2000) Antimicrob Agents Chemother , vol.44 , pp. 1990-1994
    • Miltner, E.C.1    Bermudez, L.E.2
  • 48
    • 0037305905 scopus 로고    scopus 로고
    • Entamoeba histolytica cysteine proteinases disrupt the polymeric structure of colonic mucin and alter its protective function
    • D. Moncada, K. Keller, and K. Chadee Entamoeba histolytica cysteine proteinases disrupt the polymeric structure of colonic mucin and alter its protective function Infect Immun 71 2003 838 844
    • (2003) Infect Immun , vol.71 , pp. 838-844
    • Moncada, D.1    Keller, K.2    Chadee, K.3
  • 49
    • 77956803013 scopus 로고
    • Induction of Synchronous Encystment (Differentiation) in Acanthamoeba sp
    • D.M. Prescott Academic Press New York
    • R.J. Neff, S.A. Ray, W.F. Benton, and M. Wilborn Induction of Synchronous Encystment (Differentiation) in Acanthamoeba sp D.M. Prescott Methods in Cell Physiology Vol. 1 1964 Academic Press New York 55 83
    • (1964) Methods in Cell Physiology , vol.1 , pp. 55-83
    • Neff, R.J.1    Ray, S.A.2    Benton, W.F.3    Wilborn, M.4
  • 50
    • 0034041714 scopus 로고    scopus 로고
    • Cysteine proteinases and the pathogenesis of amebiasis
    • X. Que, and S.L. Reed Cysteine proteinases and the pathogenesis of amebiasis Clin Microbiol Rev 13 2000 196 206
    • (2000) Clin Microbiol Rev , vol.13 , pp. 196-206
    • Que, X.1    Reed, S.L.2
  • 52
    • 0014010937 scopus 로고
    • Trehalose synthesis in the cellular slime mold Dictyostelium discoideum
    • R. Roth, and M. Sussman Trehalose synthesis in the cellular slime mold Dictyostelium discoideum Biochim Biophys Acta 122 1966 225 231
    • (1966) Biochim Biophys Acta , vol.122 , pp. 225-231
    • Roth, R.1    Sussman, M.2
  • 53
    • 0036205377 scopus 로고    scopus 로고
    • TREE-PUZZLE: Maximum likelihood phylogenetic analysis using quartets and parallel computing
    • H.A. Schmidt,, K. Strimmer,, M. Vingron,, and A. von Haeseler, TREE-PUZZLE: maximum likelihood phylogenetic analysis using quartets and parallel computing Bioinformatics 18 2002 502 504
    • (2002) Bioinformatics , vol.18 , pp. 502-504
    • Schmidt, A.H.1    Strimmer, K.2    Vingron, M.3    Von Haeseler, A.4
  • 54
    • 0036315180 scopus 로고    scopus 로고
    • Cultivation of pathogenic and opportunistic free-living amebas
    • F.L. Schuster, Cultivation of pathogenic and opportunistic free-living amebas Clin Microbiol Rev 15 2002 342 354
    • (2002) Clin Microbiol Rev , vol.15 , pp. 342-354
    • Schuster, F.L.1
  • 55
    • 0032932436 scopus 로고    scopus 로고
    • Legionella pneumophila utilizes the same genes to multiply within Acanthamoeba castellanii and human macrophages
    • G. Segal, and H.A. Shuman Legionella pneumophila utilizes the same genes to multiply within Acanthamoeba castellanii and human macrophages Infect Immun 67 1999 2117 2124
    • (1999) Infect Immun , vol.67 , pp. 2117-2124
    • Segal, G.1    Shuman, H.A.2
  • 56
    • 0015887907 scopus 로고
    • The regulation of poly beta-hydroxybutyrate metabolism in Azotobacter beijerinckii
    • P.J. Senior, and E.A. Dawes The regulation of poly beta-hydroxybutyrate metabolism in Azotobacter beijerinckii Biochem J 134 1973 225 238
    • (1973) Biochem J , vol.134 , pp. 225-238
    • Senior, P.J.1    Dawes, E.A.2
  • 57
    • 0032421366 scopus 로고    scopus 로고
    • The role of Pseudomonas aeruginosa biofilm in the attachment of Acanthamoeba to four types of hydrogel contact lens materials
    • P.A. Simmons, A. Tomlinson, and D.V. Seal The role of Pseudomonas aeruginosa biofilm in the attachment of Acanthamoeba to four types of hydrogel contact lens materials Optom Vis Sci 75 1998 860 866
    • (1998) Optom Vis Sci , vol.75 , pp. 860-866
    • Simmons, P.A.1    Tomlinson, A.2    Seal, D.V.3
  • 58
    • 0037116604 scopus 로고    scopus 로고
    • Uncoupling proteins outside the animal and plant kingdoms: Functional and evolutionary aspects
    • F.E. Sluse, and W. Jarmuszkiewicz Uncoupling proteins outside the animal and plant kingdoms: functional and evolutionary aspects FEBS Lett 510 2002 117 120
    • (2002) FEBS Lett , vol.510 , pp. 117-120
    • Sluse, F.E.1    Jarmuszkiewicz, W.2
  • 59
    • 0035909926 scopus 로고    scopus 로고
    • Cryptococcus neoformans interactions with amoebae suggest an explanation for its virulence and intracellular pathogenic strategy in macrophages
    • J.N. Steenbergen, H.A. Shuman, and A. Casadevall Cryptococcus neoformans interactions with amoebae suggest an explanation for its virulence and intracellular pathogenic strategy in macrophages Proc Natl Acad Sci USA 98 2001 15245 15250
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 15245-15250
    • Steenbergen, J.N.1    Shuman, H.A.2    Casadevall, A.3
  • 60
    • 0032990441 scopus 로고    scopus 로고
    • PAS domains: Internal sensors of oxygen, redox potential, and light
    • B.L. Taylor, and I.B. Zhulin PAS domains: internal sensors of oxygen, redox potential, and light Microbiol Mol Biol Rev 63 1999 479 506
    • (1999) Microbiol Mol Biol Rev , vol.63 , pp. 479-506
    • Taylor, B.L.1    Zhulin, I.B.2
  • 61
    • 0033788637 scopus 로고    scopus 로고
    • Eukaryotic signal transduction via histidine-aspartate phosphorelay
    • P. Thomason, and R. Kay Eukaryotic signal transduction via histidine-aspartate phosphorelay J Cell Sci 113 2000 3141 3150
    • (2000) J Cell Sci , vol.113 , pp. 3141-3150
    • Thomason, P.1    Kay, R.2
  • 63
    • 0036710445 scopus 로고    scopus 로고
    • The superoxide-generating NADPH oxidase: Structural aspects and activation mechanism
    • P.V. Vignais The superoxide-generating NADPH oxidase: structural aspects and activation mechanism Cell Mol Life Sci 59 2002 1428 1459
    • (2002) Cell Mol Life Sci , vol.59 , pp. 1428-1459
    • Vignais, P.V.1
  • 64
    • 0017222314 scopus 로고
    • Differentiation in Acanthamoeba castellanii
    • R.A. Weisman Differentiation in Acanthamoeba castellanii Annu Rev Microbiol 30 1976 189 219
    • (1976) Annu Rev Microbiol , vol.30 , pp. 189-219
    • Weisman, R.A.1
  • 66
    • 0026758739 scopus 로고
    • Isolation of genomic DNA encoding transcription factor TFIID from Acanthamoeba castellanii: Characterization of the promoter
    • J.M. Wong, F. Liu, and E. Bateman Isolation of genomic DNA encoding transcription factor TFIID from Acanthamoeba castellanii: characterization of the promoter Nucleic Acids Res 20 1992 4817 4824
    • (1992) Nucleic Acids Res , vol.20 , pp. 4817-4824
    • Wong, J.M.1    Liu, F.2    Bateman, E.3
  • 67
    • 0033759340 scopus 로고    scopus 로고
    • Alginate lyase: Review of major sources and enzyme characteristics, structure-function analysis, biological roles, and applications
    • T.Y. Wong, L.A. Preston, and N.L. Schiller Alginate lyase: review of major sources and enzyme characteristics, structure-function analysis, biological roles, and applications Annu Rev Microbiol 54 2000 289 340
    • (2000) Annu Rev Microbiol , vol.54 , pp. 289-340
    • Wong, T.Y.1    Preston, L.A.2    Schiller, N.L.3
  • 68
    • 0034243942 scopus 로고    scopus 로고
    • Entamoeba histolytica cysteine proteinases with interleukin-1 beta converting enzyme (ICE) activity cause intestinal inflammation and tissue damage in amoebiasis
    • Z. Zhang, L. Yan, L. Wang, K.B. Seydel, E. Li, S. Ankri, D. Mirelman, and S.L. Stanley Jr Entamoeba histolytica cysteine proteinases with interleukin-1 beta converting enzyme (ICE) activity cause intestinal inflammation and tissue damage in amoebiasis Mol Microbiol 37 2000 542 548
    • (2000) Mol Microbiol , vol.37 , pp. 542-548
    • Zhang, Z.1    Yan, L.2    Wang, L.3    Seydel, K.B.4    Li, E.5    Ankri, S.6    Mirelman, D.7    Stanley Jr., S.L.8
  • 69
    • 0025907449 scopus 로고
    • Sequence and organization of 5S RNA genes from the eukaryotic protist Acanthamoeba castellanii
    • M.G. Zwick, M. Wiggs, and M.R. Paule Sequence and organization of 5S RNA genes from the eukaryotic protist Acanthamoeba castellanii Gene 15 1991 153 157
    • (1991) Gene , vol.15 , pp. 153-157
    • Zwick, M.G.1    Wiggs, M.2    Paule, M.R.3


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