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Volumn 93, Issue 1, 1998, Pages

Molecular architecture of the trypanosome cytoskeleton

Author keywords

Cell cycle; Cytoskeleton; Trypanosome

Indexed keywords

ALPHA TUBULIN; BETA TUBULIN; TUBULIN;

EID: 0032523906     PISSN: 01666851     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0166-6851(98)00014-0     Document Type: Article
Times cited : (85)

References (67)
  • 1
    • 0024967876 scopus 로고
    • The cell cycle division of Trypanosoma brucei brucei: Timing of event markers and cytoskeletal modulations
    • [1] Sherwin T, Gull K. The cell cycle division of Trypanosoma brucei brucei: timing of event markers and cytoskeletal modulations. Phil Trans R Soc London 1989;B323:573-88.
    • (1989) Phil Trans R Soc London , vol.B323 , pp. 573-588
    • Sherwin, T.1    Gull, K.2
  • 2
    • 0002827648 scopus 로고
    • Comparative cell biology of the kinetoplastid flagellates
    • Lumsden WHR, Evans DA, editors. London, Amsterdam: Academic Press
    • [2] Vickerman K, Preston T. Comparative cell biology of the kinetoplastid flagellates. In: Lumsden WHR, Evans DA, editors. Biology of the Kinetoplastida. London, Amsterdam: Academic Press, 1976:35-130.
    • (1976) Biology of the Kinetoplastida , pp. 35-130
    • Vickerman, K.1    Preston, T.2
  • 3
    • 0028935746 scopus 로고
    • Microtubule polarity and dynamics in the control of organelle positioning segregation, and cytokinesis in the trypanosome cell cycle
    • [3] Robinson DR, Sherwin T, Ploupidou A, Byard EH, Gull K. Microtubule polarity and dynamics in the control of organelle positioning segregation, and cytokinesis in the trypanosome cell cycle. J Cell Biol 1995;128:1163-72.
    • (1995) J Cell Biol , vol.128 , pp. 1163-1172
    • Robinson, D.R.1    Sherwin, T.2    Ploupidou, A.3    Byard, E.H.4    Gull, K.5
  • 4
    • 0022257583 scopus 로고
    • Tubulin genes of the African trypanosome Trypanosoma brucei rhodesiense: Nucleotide sequence of a 3.7 kb fragment containing genes for alpha and beta-tubulin
    • [4] Kimmel BE, Samson S, Wu J, Hirschberg R, Yarbrough IR. Tubulin genes of the African trypanosome Trypanosoma brucei rhodesiense: nucleotide sequence of a 3.7 kb fragment containing genes for alpha and beta-tubulin. Gene 1985;35:148-237.
    • (1985) Gene , vol.35 , pp. 148-237
    • Kimmel, B.E.1    Samson, S.2    Wu, J.3    Hirschberg, R.4    Yarbrough, I.R.5
  • 5
    • 0021264678 scopus 로고
    • Purification and partial characterization of microtubular protein from Trypanosoma brucei
    • [5] Stieger J, Wyler T, Seebeck T. Purification and partial characterization of microtubular protein from Trypanosoma brucei. J Biol Chem 1984;259:4596-602.
    • (1984) J Biol Chem , vol.259 , pp. 4596-4602
    • Stieger, J.1    Wyler, T.2    Seebeck, T.3
  • 7
    • 0020659292 scopus 로고
    • Tubulin genes are tandemly linked and clustered in the genome of Trypanosoma brucei
    • [7] Thomashow LS, Milhausen M, Rutter WJ, Agabian N. Tubulin genes are tandemly linked and clustered in the genome of Trypanosoma brucei. Cell 1983;32:35-43.
    • (1983) Cell , vol.32 , pp. 35-43
    • Thomashow, L.S.1    Milhausen, M.2    Rutter, W.J.3    Agabian, N.4
  • 8
    • 0024286475 scopus 로고
    • The tubulin genes of Trypanosoma cruzi
    • [8] Maingon R, Gerke R, Rodrigues M, et al. The tubulin genes of Trypanosoma cruzi. Eur J Biochem 1988;171:285-91.
    • (1988) Eur J Biochem , vol.171 , pp. 285-291
    • Maingon, R.1    Gerke, R.2    Rodrigues, M.3
  • 9
    • 0020573178 scopus 로고
    • Tandem arrangment of tubulin genes in the protozoan parasite Leishmania enriettii
    • [9] Landfear SM, McMahon-Pratt D, Wirth DF. Tandem arrangment of tubulin genes in the protozoan parasite Leishmania enriettii. Mol Cell Biol 1983;3:1070-6.
    • (1983) Mol Cell Biol , vol.3 , pp. 1070-1076
    • Landfear, S.M.1    McMahon-Pratt, D.2    Wirth, D.F.3
  • 10
    • 0025128705 scopus 로고
    • Purification and assembly in vitro of tubulin from Trypanosoma brucei
    • [10] MacRae TH, Lange BMH, Gull K. Purification and assembly in vitro of tubulin from Trypanosoma brucei. Biochem J 1990;265:87-93.
    • (1990) Biochem J , vol.265 , pp. 87-93
    • MacRae, T.H.1    Lange, B.M.H.2    Gull, K.3
  • 11
    • 0021198880 scopus 로고
    • Flagellar regeneration of the trypanosome Crithidia fasciculata involves post-translational modification of cytoplasmic alpha-tubulin
    • [11] Russell DG, Gull K. Flagellar regeneration of the trypanosome Crithidia fasciculata involves post-translational modification of cytoplasmic alpha-tubulin. Mol Cell Biol 1984;4:1182-5.
    • (1984) Mol Cell Biol , vol.4 , pp. 1182-1185
    • Russell, D.G.1    Gull, K.2
  • 12
    • 0021233954 scopus 로고
    • Tubulin heterogenicity in the trypanosome Crithidia fasciculata
    • [12] Russell DG, Miller D, Gull K. Tubulin heterogenicity in the trypanosome Crithidia fasciculata. Mol Cell Biol 1984;4:779-90.
    • (1984) Mol Cell Biol , vol.4 , pp. 779-790
    • Russell, D.G.1    Miller, D.2    Gull, K.3
  • 13
    • 0023110716 scopus 로고
    • Subpellicular and flagellar microtubules of Trypanosoma brucei brucei contain the same αβ-tubulin isoforms
    • [13] Schneider A, Sherwin T, Sasse R, Russell DG, Gull K, Seebeck T. Subpellicular and flagellar microtubules of Trypanosoma brucei brucei contain the same αβ-tubulin isoforms. J Cell Biol 1987;104:431-8.
    • (1987) J Cell Biol , vol.104 , pp. 431-438
    • Schneider, A.1    Sherwin, T.2    Sasse, R.3    Russell, D.G.4    Gull, K.5    Seebeck, T.6
  • 14
    • 0024065220 scopus 로고
    • Tubulin post-translational modifications and the construction of microtubular organelles in Trypanosoma brucei
    • [14] Sasse R, Gull K. Tubulin post-translational modifications and the construction of microtubular organelles in Trypanosoma brucei. J Cell Sci 1988;90:577-89.
    • (1988) J Cell Sci , vol.90 , pp. 577-589
    • Sasse, R.1    Gull, K.2
  • 15
    • 0023389780 scopus 로고
    • Identification of an acetylation site of Chlamydomonas alpha-tubulin
    • [15] Ledizet M, Piperno G. Identification of an acetylation site of Chlamydomonas alpha-tubulin. Proc Natl Acad Sci USA 1987;84:5720-4.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 5720-5724
    • Ledizet, M.1    Piperno, G.2
  • 16
    • 0024369960 scopus 로고
    • Definition of individual components within the cytoskeleton of Trypanosoma brucei by a library of monoclonal antibodies
    • [16] Woods A, Sherwin T, Sasse R, MacRae TH, Baines AJ, Gull K. Definition of individual components within the cytoskeleton of Trypanosoma brucei by a library of monoclonal antibodies. J Cell Sci 1989;93:491-500.
    • (1989) J Cell Sci , vol.93 , pp. 491-500
    • Woods, A.1    Sherwin, T.2    Sasse, R.3    MacRae, T.H.4    Baines, A.J.5    Gull, K.6
  • 17
    • 0031049174 scopus 로고    scopus 로고
    • Subpellicular and flagellar microtubules of Trypanosoma brucei are extensively glutamylated
    • [17] Schneider A, Plessmann U, Weber K. Subpellicular and flagellar microtubules of Trypanosoma brucei are extensively glutamylated. J Cell Sci 1997;110:431-7.
    • (1997) J Cell Sci , vol.110 , pp. 431-437
    • Schneider, A.1    Plessmann, U.2    Weber, K.3
  • 18
    • 0023094196 scopus 로고
    • Distinct localisation and cell cycle dependence of COOH terminally tyrosinolated α-tubulin in the microtubules of Trypanosoma brucei brucei
    • [18] Sherwin T, Schneider A, Sasse R, Seebeck T, Gull K. Distinct localisation and cell cycle dependence of COOH terminally tyrosinolated α-tubulin in the microtubules of Trypanosoma brucei brucei. J Cell Biol 1987;104:439-46.
    • (1987) J Cell Biol , vol.104 , pp. 439-446
    • Sherwin, T.1    Schneider, A.2    Sasse, R.3    Seebeck, T.4    Gull, K.5
  • 19
    • 0024591582 scopus 로고
    • Visualization of detyrosination along single microtubules reveals novel mechanisms of assembly during cytoskeletal duplication in trypanosomes
    • [19] Sherwin T, Gull K. Visualization of detyrosination along single microtubules reveals novel mechanisms of assembly during cytoskeletal duplication in trypanosomes. Cell 1989;57:211-21.
    • (1989) Cell , vol.57 , pp. 211-221
    • Sherwin, T.1    Gull, K.2
  • 20
    • 0031049074 scopus 로고    scopus 로고
    • γ-Tubulin in trypanosomes: Molecular characterisation and localisation to multiple and diverse microtubule organising centres
    • [20] Scott V, Sherwin T, Gull K. γ-Tubulin in trypanosomes: molecular characterisation and localisation to multiple and diverse microtubule organising centres. J Cell Sci 1997;110:157-68.
    • (1997) J Cell Sci , vol.110 , pp. 157-168
    • Scott, V.1    Sherwin, T.2    Gull, K.3
  • 21
    • 0025741699 scopus 로고
    • The fission yeast γ-tubulin is essential for mitosis and is localised at microtubule organising centers
    • [21] Horio T, Uzawa S, Jung MK, Oakley BR, Tanaka K, Yanagida M. The fission yeast γ-tubulin is essential for mitosis and is localised at microtubule organising centers. J Cell Sci 1991;99:693-700.
    • (1991) J Cell Sci , vol.99 , pp. 693-700
    • Horio, T.1    Uzawa, S.2    Jung, M.K.3    Oakley, B.R.4    Tanaka, K.5    Yanagida, M.6
  • 22
    • 0027298559 scopus 로고
    • γ-Tubulin is present in acentriolar MTOCs during early mouse development
    • [22] Gueth-Hallonet C, Antony C, Aghion J, et al. γ-Tubulin is present in acentriolar MTOCs during early mouse development. J Cell Sci 1993;105:157-66.
    • (1993) J Cell Sci , vol.105 , pp. 157-166
    • Gueth-Hallonet, C.1    Antony, C.2    Aghion, J.3
  • 23
    • 0025358911 scopus 로고
    • γ-Tubulin is a component of the spindle pole body that is essential for microtubule function in Aspergillus nidulans
    • [23] Oakley BR, Oakley CE, Yoon Y, Jung MK. γ-Tubulin is a component of the spindle pole body that is essential for microtubule function in Aspergillus nidulans. Cell 1990;61:1289-301.
    • (1990) Cell , vol.61 , pp. 1289-1301
    • Oakley, B.R.1    Oakley, C.E.2    Yoon, Y.3    Jung, M.K.4
  • 24
    • 0025735679 scopus 로고
    • Microtubules, tubulin, and microtubule-associated proteins of trypanosomes
    • [24] Robinson D, Beattie P, Sherwin T, Gull K. Microtubules, tubulin, and microtubule-associated proteins of trypanosomes. Methods Enzymol 1990;196:285-99.
    • (1990) Methods Enzymol , vol.196 , pp. 285-299
    • Robinson, D.1    Beattie, P.2    Sherwin, T.3    Gull, K.4
  • 25
    • 0027102657 scopus 로고
    • A high molecular mass phosphoprotein defined by a novel monoclonal antibody is closely associated with the intermicrotubule cross bridges in the Trypanosoma brucei cytoskeleton
    • [25] Woods A, Baines AJ, Gull K. A high molecular mass phosphoprotein defined by a novel monoclonal antibody is closely associated with the intermicrotubule cross bridges in the Trypanosoma brucei cytoskeleton. J Cell Sci 1992;103:665-75.
    • (1992) J Cell Sci , vol.103 , pp. 665-675
    • Woods, A.1    Baines, A.J.2    Gull, K.3
  • 26
    • 0026521519 scopus 로고
    • A novel microtubule-binding motif identified in a high molecular weight microtubule-associated protein from Trypanosoma brucei
    • [26] Hemphill A, Affolter M, Seebeck T. A novel microtubule-binding motif identified in a high molecular weight microtubule-associated protein from Trypanosoma brucei. J Cell Biol 1992;117:95-103.
    • (1992) J Cell Biol , vol.117 , pp. 95-103
    • Hemphill, A.1    Affolter, M.2    Seebeck, T.3
  • 27
    • 0020493159 scopus 로고
    • Actin-binding proteins-regulators of cell architecture and motility
    • [27] Weeds A. Actin-binding proteins-regulators of cell architecture and motility. Nature 1982;296:811-6.
    • (1982) Nature , vol.296 , pp. 811-816
    • Weeds, A.1
  • 28
    • 0023874813 scopus 로고
    • Structure and transcription of the actin gene of Trypanosoma brucei
    • [28] Ben Amar MF, Pays A, Tebabi P, et al. Structure and transcription of the actin gene of Trypanosoma brucei. Mol Cell Biol 1988;8:2166-76.
    • (1988) Mol Cell Biol , vol.8 , pp. 2166-2176
    • Ben Amar, M.F.1    Pays, A.2    Tebabi, P.3
  • 29
    • 0028267322 scopus 로고
    • Cloning and sequencing of the Leishmania major actin-encoding gene
    • [29] de Arruda M, Matsudaira V, Matsudaira P. Cloning and sequencing of the Leishmania major actin-encoding gene. Gene 1994;139:123-5.
    • (1994) Gene , vol.139 , pp. 123-125
    • De Arruda, M.1    Matsudaira, V.2    Matsudaira, P.3
  • 30
    • 0024565366 scopus 로고
    • Studies on trypanosomatid actin. I. Immunochemical and biochemical identification
    • [30] Mortara RA. Studies on trypanosomatid actin. I. Immunochemical and biochemical identification. J Protozool 1989;36:8-13.
    • (1989) J Protozool , vol.36 , pp. 8-13
    • Mortara, R.A.1
  • 32
    • 0014472562 scopus 로고
    • The fine stucture of the epimastigote froms of Trypanosoma lewisi in the rectum of the flea Nosopsyllus fasciatus
    • [32] Molyneux DH. The fine stucture of the epimastigote froms of Trypanosoma lewisi in the rectum of the flea Nosopsyllus fasciatus. Parasitology 1969;59:55-66.
    • (1969) Parasitology , vol.59 , pp. 55-66
    • Molyneux, D.H.1
  • 33
    • 0015885540 scopus 로고
    • The mode of attachment of Trypanosoma vivax in the proboscis of the tsetse fly Glossina fuscipes: An ultrastructural study of the epimastigote stage of the trypanosome
    • [33] Vickerman K. The mode of attachment of Trypanosoma vivax in the proboscis of the tsetse fly Glossina fuscipes: an ultrastructural study of the epimastigote stage of the trypanosome. J Protozool 1973;20:394-404.
    • (1973) J Protozool , vol.20 , pp. 394-404
    • Vickerman, K.1
  • 34
    • 0015168092 scopus 로고
    • Flagellar attachment and detachment of Crithidia fasciculata to the gut wall of Anopheles gambiae
    • [34] Brooker BE. Flagellar attachment and detachment of Crithidia fasciculata to the gut wall of Anopheles gambiae. Protoplasma 1971;73:191-202.
    • (1971) Protoplasma , vol.73 , pp. 191-202
    • Brooker, B.E.1
  • 35
    • 84985143591 scopus 로고
    • Cryptobia sp. in the snail Triadopsis multilineata (say): Fine structure of attached flagellates and their mode of attachment to the spermatheca
    • [35] Current WL. Cryptobia sp. in the snail Triadopsis multilineata (say): fine structure of attached flagellates and their mode of attachment to the spermatheca. J Protozool 1980;27:278-87.
    • (1980) J Protozool , vol.27 , pp. 278-287
    • Current, W.L.1
  • 36
    • 0030751081 scopus 로고    scopus 로고
    • Cytoskeletal architecture and components involved in the attachment of Trypanosoma congolense epimastigotes
    • [36] Beattie P, Gull K. Cytoskeletal architecture and components involved in the attachment of Trypanosoma congolense epimastigotes. Parasitology 1997;115:47-55.
    • (1997) Parasitology , vol.115 , pp. 47-55
    • Beattie, P.1    Gull, K.2
  • 37
    • 0017430981 scopus 로고
    • Vector relationships in the Trypanosomatidae
    • [37] Molyneux DH. Vector relationships in the Trypanosomatidae. Adv Parasit 1977;15:1-82.
    • (1977) Adv Parasit , vol.15 , pp. 1-82
    • Molyneux, D.H.1
  • 38
    • 0016259250 scopus 로고
    • Leishmania in phlebotomid sandflies. I. Modifications of the flagellum associated with the attachment to the mid-gut and oesophageal valve of the sandfly
    • [38] Killick-Kendrick R, Molyneux DH, Ashford RW. Leishmania in phlebotomid sandflies. I. Modifications of the flagellum associated with the attachment to the mid-gut and oesophageal valve of the sandfly. Proc R Soc London B 1974;187:409-19.
    • (1974) Proc R Soc London B , vol.187 , pp. 409-419
    • Killick-Kendrick, R.1    Molyneux, D.H.2    Ashford, R.W.3
  • 39
    • 84985164297 scopus 로고
    • Ultrastructure of the flagellar apparatus of Herpetomonas ampelophilae in the gut and malpighian tubules of Drosophila melanogaster
    • [39] Rowton ED, Lushbaugh WB, McGhee RB. Ultrastructure of the flagellar apparatus of Herpetomonas ampelophilae in the gut and malpighian tubules of Drosophila melanogaster. J Protozool 1981;28:297-301.
    • (1981) J Protozool , vol.28 , pp. 297-301
    • Rowton, E.D.1    Lushbaugh, W.B.2    McGhee, R.B.3
  • 40
    • 0030222026 scopus 로고    scopus 로고
    • The paraflagellar rod of Kinetoplastida: Solved and unsolved questions
    • [40] Bastin P, Matthews KR, Gull K. The paraflagellar rod of Kinetoplastida: solved and unsolved questions. Parasitol Today 1996;12:302-7.
    • (1996) Parasitol Today , vol.12 , pp. 302-307
    • Bastin, P.1    Matthews, K.R.2    Gull, K.3
  • 43
    • 0019630344 scopus 로고
    • Cell surface antigens of Trypanosoma cruzi: Use of monoclonal antibodies to identify and isolate an epimastigote specific glycoprotein
    • [43] Snary D, Ferguson MAJ, Scott MT, Allen AK. Cell surface antigens of Trypanosoma cruzi: use of monoclonal antibodies to identify and isolate an epimastigote specific glycoprotein. Mol Biochem Parasitol 1981;3:343-56.
    • (1981) Mol Biochem Parasitol , vol.3 , pp. 343-356
    • Snary, D.1    Ferguson, M.A.J.2    Scott, M.T.3    Allen, A.K.4
  • 44
    • 0026500956 scopus 로고
    • Trypanosoma cruzi glycoprotein 72: Immunological analysis and cellular localisation
    • [44] Harth G, Mills AA, Souto-Padron T, de Souza W. Trypanosoma cruzi glycoprotein 72: immunological analysis and cellular localisation. Mol Cell Biochem 1982;109:27-36.
    • (1982) Mol Cell Biochem , vol.109 , pp. 27-36
    • Harth, G.1    Mills, A.A.2    Souto-Padron, T.3    De Souza, W.4
  • 45
    • 0027158311 scopus 로고
    • Deletion of an immunodominant Trypanosoma cruzi surface glycoprotein disrupts flagellum-cell adhesion
    • [45] Cooper R, Ribeiro de Jesus A, Cross GAM. Deletion of an immunodominant Trypanosoma cruzi surface glycoprotein disrupts flagellum-cell adhesion. J Cell Biol 1993;122:149-56.
    • (1993) J Cell Biol , vol.122 , pp. 149-156
    • Cooper, R.1    Ribeiro De Jesus, A.2    Cross, G.A.M.3
  • 46
    • 0027751979 scopus 로고
    • Gene deletion suggests a role for Trypanosoma cruzi surface glycoprotein GP72 in the insect and mammalian stages of the life cycle
    • [46] de Jesus A, Cooper R, Espinosa M. Gene deletion suggests a role for Trypanosoma cruzi surface glycoprotein GP72 in the insect and mammalian stages of the life cycle. J Cell Sci 1993;106:1023-33.
    • (1993) J Cell Sci , vol.106 , pp. 1023-1033
    • De Jesus, A.1    Cooper, R.2    Espinosa, M.3
  • 47
    • 0030602236 scopus 로고    scopus 로고
    • Characterization of the Trypanosoma brucei homologue of a Trypanosoma cruzi flagellum-adhesion glycoprotein
    • [47] Nozaki T, Haynes PA, Cross GAM. Characterization of the Trypanosoma brucei homologue of a Trypanosoma cruzi flagellum-adhesion glycoprotein. Mol Biochem Parasitol 1996;82:245-55.
    • (1996) Mol Biochem Parasitol , vol.82 , pp. 245-255
    • Nozaki, T.1    Haynes, P.A.2    Cross, G.A.M.3
  • 48
    • 0024360558 scopus 로고
    • r 88 000 glycoprotein with a transmembrane association to a unique flagellum attachment region in Trypanosoma brucei
    • r 88 000 glycoprotein with a transmembrane association to a unique flagellum attachment region in Trypanosoma brucei. J Cell Sci 1989;93:501-8.
    • (1989) J Cell Sci , vol.93 , pp. 501-508
    • Woods, A.1    Baines, A.J.2    Gull, K.3
  • 49
    • 0014741854 scopus 로고
    • Pellicular microtubules in the family Trypanosomatidae
    • [49] Angelopoulos E. Pellicular microtubules in the family Trypanosomatidae. J Protozool 1970;17:39-51.
    • (1970) J Protozool , vol.17 , pp. 39-51
    • Angelopoulos, E.1
  • 50
    • 0030978125 scopus 로고    scopus 로고
    • Partitioning of large and minichromosomes in Trypanosoma brucei
    • [50] Ersfeld K, Gull K. Partitioning of large and minichromosomes in Trypanosoma brucei. Science 1997;276:611-4.
    • (1997) Science , vol.276 , pp. 611-614
    • Ersfeld, K.1    Gull, K.2
  • 51
    • 0025773091 scopus 로고
    • Basal body movements as a mechanism for mitochondrial genome segregation in the trypanosome cell
    • [51] Robinson DR, Gull K. Basal body movements as a mechanism for mitochondrial genome segregation in the trypanosome cell. Nature 1991;352:731-4.
    • (1991) Nature , vol.352 , pp. 731-734
    • Robinson, D.R.1    Gull, K.2
  • 52
    • 0025061165 scopus 로고
    • Timing of nuclear and kinetoplast DNA replication and early morphological events in the cell cycle of Trypanosoma brucei
    • [52] Woodward R, Gull K. Timing of nuclear and kinetoplast DNA replication and early morphological events in the cell cycle of Trypanosoma brucei. J Cell Sci 1991;95:49-57.
    • (1991) J Cell Sci , vol.95 , pp. 49-57
    • Woodward, R.1    Gull, K.2
  • 53
    • 0023924102 scopus 로고
    • A microtubule-binding protein of Trypanosoma brucei which contains covalently bound fatty acid
    • [53] Schneider A, Eichenberger W, Seebeck T. A microtubule-binding protein of Trypanosoma brucei which contains covalently bound fatty acid. J Biol Chem 1988;263:6472-5.
    • (1988) J Biol Chem , vol.263 , pp. 6472-6475
    • Schneider, A.1    Eichenberger, W.2    Seebeck, T.3
  • 54
    • 0024367425 scopus 로고
    • Isolation of a subpellicular microtubule protein from Trypanosoma brucei that mediates crosslinking of microtubules
    • [54] Balaban N, Waithaka HK, Njogu AR, Goldman R. Isolation of a subpellicular microtubule protein from Trypanosoma brucei that mediates crosslinking of microtubules. Cell Mot Cytoskeleton 1989;14:393-400.
    • (1989) Cell Mot Cytoskeleton , vol.14 , pp. 393-400
    • Balaban, N.1    Waithaka, H.K.2    Njogu, A.R.3    Goldman, R.4
  • 55
    • 0027339872 scopus 로고
    • A repetitive protein from Trypanosoma brucei which caps the microtubules at the posterior end of the cytoskeleton
    • [55] Rindisbacher L, Hemphill A, Seebeck T. A repetitive protein from Trypanosoma brucei which caps the microtubules at the posterior end of the cytoskeleton. Mol Biochem Parasitol 1993;58:83-96.
    • (1993) Mol Biochem Parasitol , vol.58 , pp. 83-96
    • Rindisbacher, L.1    Hemphill, A.2    Seebeck, T.3
  • 56
    • 0024294566 scopus 로고
    • Large microtubule-associated protein of T. brucei has tandemly repeated, near-identical sequences
    • [56] Schneider A, Hemphill A, Wyler T, Seebeck T. Large microtubule-associated protein of T. brucei has tandemly repeated, near-identical sequences. Science 1988;460:459-62.
    • (1988) Science , vol.460 , pp. 459-462
    • Schneider, A.1    Hemphill, A.2    Wyler, T.3    Seebeck, T.4
  • 57
    • 0026355354 scopus 로고
    • The Trypanosoma brucei cytoskeleton: Ultrastructure and localization of microtubule-associated and spectrin-like proteins using quick-freeze, deep-etch, immunogold electron microscopy
    • [57] Hemphill A, Seebeck T, Lawson D. The Trypanosoma brucei cytoskeleton: ultrastructure and localization of microtubule-associated and spectrin-like proteins using quick-freeze, deep-etch, immunogold electron microscopy. J Struct Biol 1991;107:211-20.
    • (1991) J Struct Biol , vol.107 , pp. 211-220
    • Hemphill, A.1    Seebeck, T.2    Lawson, D.3
  • 58
    • 0026521519 scopus 로고
    • A novel microtubule-binding motif identified in a high molecular weight microtubule-associated protein from Trypanosoma brucei
    • [58] Hemphill A, Affolter M, Seebeck T. A novel microtubule-binding motif identified in a high molecular weight microtubule-associated protein from Trypanosoma brucei. J Cell Biol 1992;117:95-103.
    • (1992) J Cell Biol , vol.117 , pp. 95-103
    • Hemphill, A.1    Affolter, M.2    Seebeck, T.3
  • 59
    • 0024451447 scopus 로고
    • The major component of the paraflagellar rod of Trypanosoma brucei is a helical protein that is encoded by two identical, tandemly linked genes
    • [59] Schlaeppi K, Deflorin J, Seebeck T. The major component of the paraflagellar rod of Trypanosoma brucei is a helical protein that is encoded by two identical, tandemly linked genes. J Cell Biol 1989;109:1695-709.
    • (1989) J Cell Biol , vol.109 , pp. 1695-1709
    • Schlaeppi, K.1    Deflorin, J.2    Seebeck, T.3
  • 60
    • 0028036696 scopus 로고
    • The major components of the paraflagellar rod of Trypanosoma brucei are two similar, but distinct proteins which are encoded by two different gene loci
    • [60] Deflorin J, Rudolf M, Seebeck T. The major components of the paraflagellar rod of Trypanosoma brucei are two similar, but distinct proteins which are encoded by two different gene loci. J Biol Chem 1984;269:27745-8751.
    • (1984) J Biol Chem , vol.269 , pp. 27745-28751
    • Deflorin, J.1    Rudolf, M.2    Seebeck, T.3
  • 61
    • 0028023630 scopus 로고
    • Molecular characterisation of a novel, repetitive protein of the paraflagellar rod in Trypanosoma brucei
    • [61] Woodward R, Carden MJ, Gull K. Molecular characterisation of a novel, repetitive protein of the paraflagellar rod in Trypanosoma brucei. Mol Biochem Parasitol 1994;67:31-9.
    • (1994) Mol Biochem Parasitol , vol.67 , pp. 31-39
    • Woodward, R.1    Carden, M.J.2    Gull, K.3
  • 62
    • 0028905831 scopus 로고
    • Repetitive proteins from the flagellar cytoskeleton of African trypanosomes are diagnostically useful antigens
    • [62] Imboden M, Müller N, Hemphill A, Mattioli R, Seebeck T. Repetitive proteins from the flagellar cytoskeleton of African trypanosomes are diagnostically useful antigens. Parasitology 1995;110:249-58.
    • (1995) Parasitology , vol.110 , pp. 249-258
    • Imboden, M.1    Müller, N.2    Hemphill, A.3    Mattioli, R.4    Seebeck, T.5
  • 63
    • 0029065327 scopus 로고
    • Immunological characterization of cytoskeletal proteins associated with the basal body, axoneme and flagellum attachment zone of Trypanosoma brucei
    • [63] Woodward R, Carden MJ, Gull K. Immunological characterization of cytoskeletal proteins associated with the basal body, axoneme and flagellum attachment zone of Trypanosoma brucei. Parasitology 1995;111:77-85.
    • (1995) Parasitology , vol.111 , pp. 77-85
    • Woodward, R.1    Carden, M.J.2    Gull, K.3
  • 64
    • 0027429214 scopus 로고
    • Cytoskeleton-associated antigens from African trypanosomes are recognized by self-reactive antibodies of unifected mice
    • [64] Müller N, Imboden M, Detmer E, Manfield JM, Seebeck T. Cytoskeleton-associated antigens from African trypanosomes are recognized by self-reactive antibodies of unifected mice. Parasitology 1993;107:411-7.
    • (1993) Parasitology , vol.107 , pp. 411-417
    • Müller, N.1    Imboden, M.2    Detmer, E.3    Manfield, J.M.4    Seebeck, T.5
  • 65
    • 0026541472 scopus 로고
    • Identification and characterization of two repetitive non-variable antigens from African trypanosomes which are recognized early during infection
    • [65] Müller N, Hemphill A, Imboden M, Duvallet G, Dwinger RH, Seebeck T. Identification and characterization of two repetitive non-variable antigens from African trypanosomes which are recognized early during infection. Parasitology 1992;104:111-20.
    • (1992) Parasitology , vol.104 , pp. 111-120
    • Müller, N.1    Hemphill, A.2    Imboden, M.3    Duvallet, G.4    Dwinger, R.H.5    Seebeck, T.6
  • 66
    • 0023942738 scopus 로고
    • Multiple Trypanosoma cruzi antigens containing tandemly amino acid sequence motif
    • [66] Ibanez CF, Affranchino JL, Macina RA, et al. Multiple Trypanosoma cruzi antigens containing tandemly amino acid sequence motif. Mol Biochem Parasitol 1988;30:27-34.
    • (1988) Mol Biochem Parasitol , vol.30 , pp. 27-34
    • Ibanez, C.F.1    Affranchino, J.L.2    Macina, R.A.3
  • 67
    • 0029019769 scopus 로고
    • Trypanosoma cruzi: Monoclonal antibody to cytoskeleton recognizes giant proteins of the flagellum attachment zone
    • [67] Ruiz-Moreno L, Bijovsky TA, Pudles J, Alves MJM, Colli W. Trypanosoma cruzi: monoclonal antibody to cytoskeleton recognizes giant proteins of the flagellum attachment zone. Exp Parasitol 1995;80:605-15.
    • (1995) Exp Parasitol , vol.80 , pp. 605-615
    • Ruiz-Moreno, L.1    Bijovsky, T.A.2    Pudles, J.3    Alves, M.J.M.4    Colli, W.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.