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Volumn 305, Issue 2, 2010, Pages 170-176

The fine structure of the Acanthamoeba polyphaga cyst wall

Author keywords

Acanthamoeba; Cyst; Cyst wall; Quick freeze deep etching

Indexed keywords

ACANTHAMOEBA; ACANTHAMOEBA POLYPHAGA; ARTICLE; FREEZE FRACTURE; NONHUMAN; PRIORITY JOURNAL; THREE DIMENSIONAL IMAGING; TRANSMISSION ELECTRON MICROSCOPY; CELL WALL; CRYOELECTRON MICROSCOPY; PROTOZOAN SPORE; ULTRASTRUCTURE;

EID: 77949622286     PISSN: 03781097     EISSN: 15746968     Source Type: Journal    
DOI: 10.1111/j.1574-6968.2010.01925.x     Document Type: Article
Times cited : (15)

References (32)
  • 1
    • 0036288168 scopus 로고    scopus 로고
    • Resistance of Acanthamoeba castellanii cysts to physical, chemical, and radiological conditions
    • Aksozek A, McClellan K, Howard K, Niederkorn JY Alizadeh H (2002) Resistance of Acanthamoeba castellanii cysts to physical, chemical, and radiological conditions. J Parasitol 88 : 621 623.
    • (2002) J Parasitol , vol.88 , pp. 621-623
    • Aksozek, A.1    McClellan, K.2    Howard, K.3    Niederkorn, J.Y.4    Alizadeh, H.5
  • 2
    • 0034030737 scopus 로고    scopus 로고
    • Proteinase activities in total extracts and in medium conditioned by Acanthamoeba polyphaga trophozoites
    • Alfieri SC, Correia CEB, Motegi SA Pral EMB (2000) Proteinase activities in total extracts and in medium conditioned by Acanthamoeba polyphaga trophozoites. J Parasitol 86 : 220 227.
    • (2000) J Parasitol , vol.86 , pp. 220-227
    • Alfieri, S.C.1    Correia, C.E.B.2    Motegi, S.A.3    Pral, E.M.B.4
  • 3
    • 67949091013 scopus 로고    scopus 로고
    • Acanthamoeba castellanii: Proteins involved in actin dynamics, glycolysis, and proteolysis are regulated during encystation
    • Bouyer S, Rodier MH, Guillot A Héchard Y (2009) Acanthamoeba castellanii: proteins involved in actin dynamics, glycolysis, and proteolysis are regulated during encystation. Exp Parasitol 123 : 90 94.
    • (2009) Exp Parasitol , vol.123 , pp. 90-94
    • Bouyer, S.1    Rodier, M.H.2    Guillot, A.3    Héchard, Y.4
  • 4
    • 0014340588 scopus 로고
    • The fine structure of Acanthamoeba castellanii. I. the trophozoite
    • Bowers B Korn ED (1968) The fine structure of Acanthamoeba castellanii. I. The trophozoite. J Cell Biol 39 : 95 111.
    • (1968) J Cell Biol , vol.39 , pp. 95-111
    • Bowers, B.1    Korn, E.D.2
  • 5
    • 0014532519 scopus 로고
    • The fine structure of Acanthamoeba castellanii (Neff strain). II. Encystment
    • Bowers B Korn ED (1969) The fine structure of Acanthamoeba castellanii (Neff strain). II. Encystment. J Cell Biol 41 : 786 805.
    • (1969) J Cell Biol , vol.41 , pp. 786-805
    • Bowers, B.1    Korn, E.D.2
  • 8
    • 0035687966 scopus 로고    scopus 로고
    • Acanthamoeba castellanii: Ultrastructure of trophozoites using fast freeze-fixation followed by freeze-substitution
    • Gonzalez-Robles A, Flores-Langarica A, Omana-Molina M Shibayama M (2001) Acanthamoeba castellanii: ultrastructure of trophozoites using fast freeze-fixation followed by freeze-substitution. J Electron Microsc 50 : 423 427.
    • (2001) J Electron Microsc , vol.50 , pp. 423-427
    • Gonzalez-Robles, A.1    Flores-Langarica, A.2    Omana-Molina, M.3    Shibayama, M.4
  • 9
    • 49149135185 scopus 로고
    • The quick-freeze deep-etch method of preparing samples for high resolution, 3-D electron microscopy
    • Heuser JE (1981) The quick-freeze deep-etch method of preparing samples for high resolution, 3-D electron microscopy. Trends Biochem Sci 6 : 64 68.
    • (1981) Trends Biochem Sci , vol.6 , pp. 64-68
    • Heuser, J.E.1
  • 10
    • 0027414416 scopus 로고
    • Impact of freeze substitution on biological electron microscopy
    • Hippe-Sanwald S (1993) Impact of freeze substitution on biological electron microscopy. Microsc Res Techniq 24 : 400 422.
    • (1993) Microsc Res Techniq , vol.24 , pp. 400-422
    • Hippe-Sanwald, S.1
  • 13
    • 0031939378 scopus 로고    scopus 로고
    • Biguanide-induced changes in Acanthamoeba castellanii: An electron microscopic study
    • Khunkiti W, Hann AC, Lloyd D, Furr JR Russell AD (1998) Biguanide-induced changes in Acanthamoeba castellanii: an electron microscopic study. J Appl Microbiol 84 : 53 62.
    • (1998) J Appl Microbiol , vol.84 , pp. 53-62
    • Khunkiti, W.1    Hann, A.C.2    Lloyd, D.3    Furr, J.R.4    Russell, A.D.5
  • 14
    • 0032524974 scopus 로고    scopus 로고
    • Three-dimensional ultrastructure of apoptotic nuclei in rat prostatic epithelial cells revealed by a quick-freezing and deep-etching method
    • Kubo M, Uchiyama H, Ueno A, Terada N, Fujii Y, Baba T Ohno S (1998) Three-dimensional ultrastructure of apoptotic nuclei in rat prostatic epithelial cells revealed by a quick-freezing and deep-etching method. Prostate 35 : 193 202.
    • (1998) Prostate , vol.35 , pp. 193-202
    • Kubo, M.1    Uchiyama, H.2    Ueno, A.3    Terada, N.4    Fujii, Y.5    Baba, T.6    Ohno, S.7
  • 15
    • 0037102950 scopus 로고    scopus 로고
    • Recent advances in the treatment of Acanthamoeba keratitis
    • Kumar R Lloyd D (2002) Recent advances in the treatment of Acanthamoeba keratitis. Clin Infect Dis 35 : 434 441.
    • (2002) Clin Infect Dis , vol.35 , pp. 434-441
    • Kumar, R.1    Lloyd, D.2
  • 16
    • 0036249534 scopus 로고    scopus 로고
    • Use of recombinant cellulose-binding domains of Trichoderma reesei cellulase as a selective immunocytochemical marker for cellulose in protozoa
    • Linder M, Winiecka-Krusnell J Linder E (2002) Use of recombinant cellulose-binding domains of Trichoderma reesei cellulase as a selective immunocytochemical marker for cellulose in protozoa. Appl Environ Microb 68 : 2503 2508.
    • (2002) Appl Environ Microb , vol.68 , pp. 2503-2508
    • Linder, M.1    Winiecka-Krusnell, J.2    Linder, E.3
  • 18
    • 77949608949 scopus 로고    scopus 로고
    • Cryotechniques for electron microscopy: A minireview
    • Evangelista, V. ed, Springer-Verlag, Dordrecht. the Netherlands
    • Lupetti P (2005) Cryotechniques for electron microscopy: a minireview. From Cells to Proteins: Imaging Nature Across Dimensions (Evangelista V, ed), pp. 53 70. Springer-Verlag, Dordrecht, the Netherlands.
    • (2005) From Cells to Proteins: Imaging Nature Across Dimensions , pp. 53-70
    • Lupetti, P.1
  • 19
    • 0037398448 scopus 로고    scopus 로고
    • Acanthamoeba spp. as agents of disease in humans
    • Marciano-Cabral F Cabral G (2003) Acanthamoeba spp. as agents of disease in humans. Clin Microbiol Rev 16 : 273 307.
    • (2003) Clin Microbiol Rev , vol.16 , pp. 273-307
    • Marciano-Cabral, F.1    Cabral, G.2
  • 20
    • 0025336499 scopus 로고
    • Direct visualization of cross-links in the primary plant cell wall
    • McCann MC, Wells B Roberts K (1990) Direct visualization of cross-links in the primary plant cell wall. J Cell Sci 96 : 323 334.
    • (1990) J Cell Sci , vol.96 , pp. 323-334
    • McCann, M.C.1    Wells, B.2    Roberts, K.3
  • 21
    • 51649122536 scopus 로고    scopus 로고
    • Characterization of a serine proteinase mediating encystation of Acanthamoeba
    • Moon EK, Chung DI, Hong YC Kong HH (2008) Characterization of a serine proteinase mediating encystation of Acanthamoeba. Eukaryot Cell 7 : 1513 1517.
    • (2008) Eukaryot Cell , vol.7 , pp. 1513-1517
    • Moon, E.K.1    Chung, D.I.2    Hong, Y.C.3    Kong, H.H.4
  • 22
    • 68749116180 scopus 로고    scopus 로고
    • Autophagy protein 8 mediating autophagosome in encysting Acanthamoeba
    • Moon EK, Chung DI, Hong YC Kong HH (2009) Autophagy protein 8 mediating autophagosome in encysting Acanthamoeba. Mol Biochem Parasit 168 : 743 748.
    • (2009) Mol Biochem Parasit , vol.168 , pp. 743-748
    • Moon, E.K.1    Chung, D.I.2    Hong, Y.C.3    Kong, H.H.4
  • 23
    • 67449144008 scopus 로고
    • Localization of cellulose in the cysts of Acanthamoeba sp
    • Neff RJ Benton WF (1962) Localization of cellulose in the cysts of Acanthamoeba sp. J Protozool 9 (suppl) : 11.
    • (1962) J Protozool , vol.9 , Issue.SUPPL. , pp. 11
    • Neff, R.J.1    Benton, W.F.2
  • 24
    • 0014623150 scopus 로고
    • The biochemistry of amoebic encystment
    • Neff RJ Neff RH (1969) The biochemistry of amoebic encystment. Sym Soc Exp Biol 23 : 51 81.
    • (1969) Sym Soc Exp Biol , vol.23 , pp. 51-81
    • Neff, R.J.1    Neff, R.H.2
  • 25
    • 77956803013 scopus 로고
    • Induction of synchronous encystment (differentiation) in Acanthamoeba sp
    • Prescott, D.M. ed, Academic. New York
    • Neff RJ, Ray SA, Benton WF Wilborn M (1964) Induction of synchronous encystment (differentiation) in Acanthamoeba sp. Methods in Cell Physiology (Prescott DM, ed) 55 83. Academic, New York.
    • (1964) Methods in Cell Physiology , pp. 55-83
    • Neff, R.J.1    Ray, S.A.2    Benton, W.F.3    Wilborn, M.4
  • 26
    • 0025739282 scopus 로고
    • Advantages of fast-freeze fixation followed by freeze-substitution for the preservation of cell integrity
    • Nicolas G (1991) Advantages of fast-freeze fixation followed by freeze-substitution for the preservation of cell integrity. Electron Microsc Tech 18 : 395 405.
    • (1991) Electron Microsc Tech , vol.18 , pp. 395-405
    • Nicolas, G.1
  • 27
    • 0019307757 scopus 로고
    • Quick freezing vs chemical fixation: Capture and identification of membrane fusion intermediates
    • Pinto da Silva P Kachar B (1980) Quick freezing vs chemical fixation: capture and identification of membrane fusion intermediates. Cell Biol Int Rep 4 : 625 639.
    • (1980) Cell Biol Int Rep , vol.4 , pp. 625-639
    • Pinto Da Silva, P.1    Kachar, B.2
  • 28
    • 0001671044 scopus 로고
    • Morphologies de la paroi kystique et taxonomie du genre Acanthamoeba (Protozoa, Amoebida)
    • Pussard M Pons R (1977) Morphologies de la paroi kystique et taxonomie du genre Acanthamoeba (Protozoa, Amoebida). Protistologica 13 : 557 610.
    • (1977) Protistologica , vol.13 , pp. 557-610
    • Pussard, M.1    Pons, R.2
  • 29
    • 35348923840 scopus 로고    scopus 로고
    • Biological characterization of a clinical and an environmental isolate of Acanthamoeba polyphaga: Analysis of relevant parameters to decode pathogenicity
    • Rocha-Azevedo B Silva-Filho FC (2007) Biological characterization of a clinical and an environmental isolate of Acanthamoeba polyphaga: analysis of relevant parameters to decode pathogenicity. Arch Microbiol 188 : 441 449.
    • (2007) Arch Microbiol , vol.188 , pp. 441-449
    • Rocha-Azevedo, B.1    Silva-Filho, F.C.2
  • 30
  • 31
    • 34347256383 scopus 로고    scopus 로고
    • Freeze-fracture electron microscopy
    • Severs NJ (2007) Freeze-fracture electron microscopy. Nat Protoc 2 : 547 576.
    • (2007) Nat Protoc , vol.2 , pp. 547-576
    • Severs, N.J.1
  • 32
    • 34248569659 scopus 로고    scopus 로고
    • Pathogenic and opportunistic free-living amoebae: Acanthamoeba spp., Balamuthia mandrillaris, Naegleria fowleri, and Sappinia diploidea
    • Visvesvara GS, Moura H Schuster FL (2007) Pathogenic and opportunistic free-living amoebae: Acanthamoeba spp., Balamuthia mandrillaris, Naegleria fowleri, and Sappinia diploidea. FEMS Immunol Med Mic 50 : 1 26.
    • (2007) FEMS Immunol Med Mic , vol.50 , pp. 1-26
    • Visvesvara, G.S.1    Moura, H.2    Schuster, F.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.