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Volumn 7, Issue 2, 2012, Pages

A MAP6-Related protein is present in protozoa and is involved in flagellum motility

Author keywords

[No Author keywords available]

Indexed keywords

MICROTUBULE ASSOCIATED PROTEIN; MICROTUBULE ASSOCIATED PROTEIN 6; SAXO PROTEIN; UNCLASSIFIED DRUG; PROTOZOAL PROTEIN;

EID: 84857080137     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0031344     Document Type: Article
Times cited : (47)

References (108)
  • 3
    • 0016587169 scopus 로고
    • Cold-labile and cold-stable microtubules in the mitotic spindle of mammalian cells
    • Brinkley BR, Cartwright J Jr, (1975) Cold-labile and cold-stable microtubules in the mitotic spindle of mammalian cells. Ann N Y Acad Sci 253: 428-439.
    • (1975) Ann N Y Acad Sci , vol.253 , pp. 428-439
    • Brinkley, B.R.1    Cartwright Jr., J.2
  • 4
    • 33748780075 scopus 로고    scopus 로고
    • STOP-like protein 21 is a novel member of the STOP family, revealing a Golgi localization of STOP proteins
    • Gory-Faure S, Windscheid V, Bosc C, Peris L, Proietto D, et al. (2006) STOP-like protein 21 is a novel member of the STOP family, revealing a Golgi localization of STOP proteins. J Biol Chem 281: 28387-28396.
    • (2006) J Biol Chem , vol.281 , pp. 28387-28396
    • Gory-Faure, S.1    Windscheid, V.2    Bosc, C.3    Peris, L.4    Proietto, D.5
  • 5
    • 0022497883 scopus 로고
    • Purification and assay of a 145-kDa protein (STOP145) with microtubule-stabilizing and motility behavior
    • Margolis RL, Rauch CT, Job D, (1986) Purification and assay of a 145-kDa protein (STOP145) with microtubule-stabilizing and motility behavior. Proc Natl Acad Sci U S A 83: 639-643.
    • (1986) Proc Natl Acad Sci U S A , vol.83 , pp. 639-643
    • Margolis, R.L.1    Rauch, C.T.2    Job, D.3
  • 6
    • 0035903126 scopus 로고    scopus 로고
    • Identification of novel bifunctional calmodulin-binding and microtubule-stabilizing motifs in STOP proteins
    • Bosc C, Frank R, Denarier E, Ronjat M, Schweitzer A, et al. (2001) Identification of novel bifunctional calmodulin-binding and microtubule-stabilizing motifs in STOP proteins. J Biol Chem 276: 30904-30913.
    • (2001) J Biol Chem , vol.276 , pp. 30904-30913
    • Bosc, C.1    Frank, R.2    Denarier, E.3    Ronjat, M.4    Schweitzer, A.5
  • 7
    • 77949654407 scopus 로고    scopus 로고
    • Study of possible interactions of tubulin, microtubular network, and STOP protein with mitochondria in muscle cells
    • Guerrero K, Monge C, Bruckner A, Puurand U, Kadaja L, et al. (2010) Study of possible interactions of tubulin, microtubular network, and STOP protein with mitochondria in muscle cells. Mol Cell Biochem 337: 239-249.
    • (2010) Mol Cell Biochem , vol.337 , pp. 239-249
    • Guerrero, K.1    Monge, C.2    Bruckner, A.3    Puurand, U.4    Kadaja, L.5
  • 8
    • 0032514256 scopus 로고    scopus 로고
    • STOP proteins are responsible for the high degree of microtubule stabilization observed in neuronal cells
    • Guillaud L, Bosc C, Fourest-Lieuvin A, Denarier E, Pirollet F, et al. (1998) STOP proteins are responsible for the high degree of microtubule stabilization observed in neuronal cells. J Cell Biol 142: 167-179.
    • (1998) J Cell Biol , vol.142 , pp. 167-179
    • Guillaud, L.1    Bosc, C.2    Fourest-Lieuvin, A.3    Denarier, E.4    Pirollet, F.5
  • 9
    • 0024557655 scopus 로고
    • Monoclonal antibody to microtubule-associated STOP protein: affinity purification of neuronal STOP activity and comparison of antigen with activity in neuronal and nonneuronal cell extracts
    • Pirollet F, Rauch CT, Job D, Margolis RL, (1989) Monoclonal antibody to microtubule-associated STOP protein: affinity purification of neuronal STOP activity and comparison of antigen with activity in neuronal and nonneuronal cell extracts. Biochemistry 28: 835-842.
    • (1989) Biochemistry , vol.28 , pp. 835-842
    • Pirollet, F.1    Rauch, C.T.2    Job, D.3    Margolis, R.L.4
  • 10
    • 33745829016 scopus 로고    scopus 로고
    • Phosphorylation of microtubule-associated protein STOP by calmodulin kinase II
    • Baratier J, Peris L, Brocard J, Gory-Faure S, Dufour F, et al. (2006) Phosphorylation of microtubule-associated protein STOP by calmodulin kinase II. J Biol Chem 281: 19561-19569.
    • (2006) J Biol Chem , vol.281 , pp. 19561-19569
    • Baratier, J.1    Peris, L.2    Brocard, J.3    Gory-Faure, S.4    Dufour, F.5
  • 11
    • 0142182060 scopus 로고    scopus 로고
    • The role of microtubule-associated protein 2c in the reorganization of microtubules and lamellipodia during neurite initiation
    • Dehmelt L, Smart FM, Ozer RS, Halpain S, (2003) The role of microtubule-associated protein 2c in the reorganization of microtubules and lamellipodia during neurite initiation. J Neurosci 23: 9479-9490.
    • (2003) J Neurosci , vol.23 , pp. 9479-9490
    • Dehmelt, L.1    Smart, F.M.2    Ozer, R.S.3    Halpain, S.4
  • 12
    • 1842432582 scopus 로고    scopus 로고
    • MAP2c, but not tau, binds and bundles F-actin via its microtubule binding domain
    • Roger B, Al-Bassam J, Dehmelt L, Milligan RA, Halpain S, (2004) MAP2c, but not tau, binds and bundles F-actin via its microtubule binding domain. Curr Biol 14: 363-371.
    • (2004) Curr Biol , vol.14 , pp. 363-371
    • Roger, B.1    Al-Bassam, J.2    Dehmelt, L.3    Milligan, R.A.4    Halpain, S.5
  • 13
    • 0037106228 scopus 로고    scopus 로고
    • The suppression of brain cold-stable microtubules in mice induces synaptic defects associated with neuroleptic-sensitive behavioral disorders
    • Andrieux A, Salin PA, Vernet M, Kujala P, Baratier J, et al. (2002) The suppression of brain cold-stable microtubules in mice induces synaptic defects associated with neuroleptic-sensitive behavioral disorders. Genes Dev 16: 2350-2364.
    • (2002) Genes Dev , vol.16 , pp. 2350-2364
    • Andrieux, A.1    Salin, P.A.2    Vernet, M.3    Kujala, P.4    Baratier, J.5
  • 14
    • 41849094126 scopus 로고    scopus 로고
    • Kinetoplastids: related protozoan pathogens, different diseases
    • Stuart K, Brun R, Croft S, Fairlamb A, Gurtler RE, et al. (2008) Kinetoplastids: related protozoan pathogens, different diseases. J Clin Invest 118: 1301-1310.
    • (2008) J Clin Invest , vol.118 , pp. 1301-1310
    • Stuart, K.1    Brun, R.2    Croft, S.3    Fairlamb, A.4    Gurtler, R.E.5
  • 16
    • 0032724638 scopus 로고    scopus 로고
    • The cytoskeleton of trypanosomatid parasites
    • Gull K, (1999) The cytoskeleton of trypanosomatid parasites. Annu Rev Microbiol 53: 629-655.
    • (1999) Annu Rev Microbiol , vol.53 , pp. 629-655
    • Gull, K.1
  • 18
    • 77955423689 scopus 로고    scopus 로고
    • Parasites in motion: flagellum-driven cell motility in African trypanosomes
    • Hill KL, (2010) Parasites in motion: flagellum-driven cell motility in African trypanosomes. Curr Opin Microbiol 13: 459-465.
    • (2010) Curr Opin Microbiol , vol.13 , pp. 459-465
    • Hill, K.L.1
  • 19
    • 77955423894 scopus 로고    scopus 로고
    • Composition and sensory function of the trypanosome flagellar membrane
    • Maric D, Epting CL, Engman DM, (2010) Composition and sensory function of the trypanosome flagellar membrane. Curr Opin Microbiol 13: 466-472.
    • (2010) Curr Opin Microbiol , vol.13 , pp. 466-472
    • Maric, D.1    Epting, C.L.2    Engman, D.M.3
  • 20
    • 33644858832 scopus 로고    scopus 로고
    • Flagellar motility is required for the viability of the bloodstream trypanosome
    • Broadhead R, Dawe HR, Farr H, Griffiths S, Hart SR, et al. (2006) Flagellar motility is required for the viability of the bloodstream trypanosome. Nature 440: 224-227.
    • (2006) Nature , vol.440 , pp. 224-227
    • Broadhead, R.1    Dawe, H.R.2    Farr, H.3    Griffiths, S.4    Hart, S.R.5
  • 21
    • 73749085879 scopus 로고    scopus 로고
    • The paraflagellar rod of kinetoplastid parasites: from structure to components and function
    • Portman N, Gull K, (2010) The paraflagellar rod of kinetoplastid parasites: from structure to components and function. Int J Parasitol 40: 135-148.
    • (2010) Int J Parasitol , vol.40 , pp. 135-148
    • Portman, N.1    Gull, K.2
  • 22
    • 0033785520 scopus 로고    scopus 로고
    • Flagellum ontogeny in trypanosomes studied via an inherited and regulated RNA interference system
    • Bastin P, Ellis K, Kohl L, Gull K, (2000) Flagellum ontogeny in trypanosomes studied via an inherited and regulated RNA interference system. J Cell Sci 113 (Pt 18): 3321-3328.
    • (2000) J Cell Sci , vol.113 , Issue.PART 18 , pp. 3321-3328
    • Bastin, P.1    Ellis, K.2    Kohl, L.3    Gull, K.4
  • 23
    • 0032693564 scopus 로고    scopus 로고
    • Protein transport and flagellum assembly dynamics revealed by analysis of the paralysed trypanosome mutant snl-1
    • Bastin P, Pullen TJ, Sherwin T, Gull K, (1999) Protein transport and flagellum assembly dynamics revealed by analysis of the paralysed trypanosome mutant snl-1. J Cell Sci 112 (Pt 21): 3769-3777.
    • (1999) J Cell Sci , vol.112 , Issue.PART 21 , pp. 3769-3777
    • Bastin, P.1    Pullen, T.J.2    Sherwin, T.3    Gull, K.4
  • 24
    • 0032484944 scopus 로고    scopus 로고
    • Paraflagellar rod is vital for trypanosome motility
    • Bastin P, Sherwin T, Gull K, (1998) Paraflagellar rod is vital for trypanosome motility. Nature 391: 548.
    • (1998) Nature , vol.391 , pp. 548
    • Bastin, P.1    Sherwin, T.2    Gull, K.3
  • 25
    • 0032844652 scopus 로고    scopus 로고
    • Genetic dissection of the Leishmania paraflagellar rod, a unique flagellar cytoskeleton structure
    • Maga JA, Sherwin T, Francis S, Gull K, LeBowitz JH, (1999) Genetic dissection of the Leishmania paraflagellar rod, a unique flagellar cytoskeleton structure. J Cell Sci 112 (Pt 16): 2753-2763.
    • (1999) J Cell Sci , vol.112 , Issue.PART 16 , pp. 2753-2763
    • Maga, J.A.1    Sherwin, T.2    Francis, S.3    Gull, K.4    LeBowitz, J.H.5
  • 26
    • 0031441357 scopus 로고    scopus 로고
    • A motility function for the paraflagellar rod of Leishmania parasites revealed by PFR-2 gene knockouts
    • Santrich C, Moore L, Sherwin T, Bastin P, Brokaw C, et al. (1997) A motility function for the paraflagellar rod of Leishmania parasites revealed by PFR-2 gene knockouts. Mol Biochem Parasitol 90: 95-109.
    • (1997) Mol Biochem Parasitol , vol.90 , pp. 95-109
    • Santrich, C.1    Moore, L.2    Sherwin, T.3    Bastin, P.4    Brokaw, C.5
  • 27
    • 0025773091 scopus 로고
    • Basal body movements as a mechanism for mitochondrial genome segregation in the trypanosome cell cycle
    • Robinson DR, Gull K, (1991) Basal body movements as a mechanism for mitochondrial genome segregation in the trypanosome cell cycle. Nature 352: 731-733.
    • (1991) Nature , vol.352 , pp. 731-733
    • Robinson, D.R.1    Gull, K.2
  • 28
    • 0028935746 scopus 로고
    • Microtubule polarity and dynamics in the control of organelle positioning, segregation, and cytokinesis in the trypanosome cell cycle
    • Robinson DR, Sherwin T, Ploubidou A, Byard EH, Gull K, (1995) Microtubule polarity and dynamics in the control of organelle positioning, segregation, and cytokinesis in the trypanosome cell cycle. J Cell Biol 128: 1163-1172.
    • (1995) J Cell Biol , vol.128 , pp. 1163-1172
    • Robinson, D.R.1    Sherwin, T.2    Ploubidou, A.3    Byard, E.H.4    Gull, K.5
  • 29
    • 0025128705 scopus 로고
    • Purification and assembly in vitro of tubulin from Trypanosoma brucei brucei
    • MacRae TH, Gull K, (1990) Purification and assembly in vitro of tubulin from Trypanosoma brucei brucei. Biochem J 265: 87-93.
    • (1990) Biochem J , vol.265 , pp. 87-93
    • MacRae, T.H.1    Gull, K.2
  • 30
    • 0021052732 scopus 로고
    • Trypanocidal action of neuroleptic phenothiazines in Trypanosoma brucei
    • Seebeck T, Gehr P, (1983) Trypanocidal action of neuroleptic phenothiazines in Trypanosoma brucei. Mol Biochem Parasitol 9: 197-208.
    • (1983) Mol Biochem Parasitol , vol.9 , pp. 197-208
    • Seebeck, T.1    Gehr, P.2
  • 31
    • 0024367425 scopus 로고
    • Isolation of a subpellicular microtubule protein from Trypanosoma brucei that mediates crosslinking of microtubules
    • Balaban N, Waithaka HK, Njogu AR, Goldman R, (1989) Isolation of a subpellicular microtubule protein from Trypanosoma brucei that mediates crosslinking of microtubules. Cell Motil Cytoskeleton 14: 393-400.
    • (1989) Cell Motil Cytoskeleton , vol.14 , pp. 393-400
    • Balaban, N.1    Waithaka, H.K.2    Njogu, A.R.3    Goldman, R.4
  • 32
    • 0030895509 scopus 로고    scopus 로고
    • The Trypanosoma brucei autoantigen I/6 is an internally repetitive cytoskeletal protein
    • Detmer E, Hemphill A, Muller N, Seebeck T, (1997) The Trypanosoma brucei autoantigen I/6 is an internally repetitive cytoskeletal protein. Eur J Cell Biol 72: 378-384.
    • (1997) Eur J Cell Biol , vol.72 , pp. 378-384
    • Detmer, E.1    Hemphill, A.2    Muller, N.3    Seebeck, T.4
  • 33
    • 0028905831 scopus 로고
    • Repetitive proteins from the flagellar cytoskeleton of African trypanosomes are diagnostically useful antigens
    • Imboden M, Muller N, Hemphill A, Mattioli R, Seebeck T, (1995) Repetitive proteins from the flagellar cytoskeleton of African trypanosomes are diagnostically useful antigens. Parasitology 110 (Pt 3): 249-258.
    • (1995) Parasitology , vol.110 , Issue.PART 3 , pp. 249-258
    • Imboden, M.1    Muller, N.2    Hemphill, A.3    Mattioli, R.4    Seebeck, T.5
  • 34
    • 0026541472 scopus 로고
    • Identification and characterization of two repetitive non-variable antigens from African trypanosomes which are recognized early during infection
    • Muller N, Hemphill A, Imboden M, Duvallet G, Dwinger RH, et al. (1992) Identification and characterization of two repetitive non-variable antigens from African trypanosomes which are recognized early during infection. Parasitology 104 Pt 1: 111-120.
    • (1992) Parasitology , vol.104 , Issue.PART 1 , pp. 111-120
    • Muller, N.1    Hemphill, A.2    Imboden, M.3    Duvallet, G.4    Dwinger, R.H.5
  • 35
    • 0024294566 scopus 로고
    • Large microtubule-associated protein of T. brucei has tandemly repeated, near-identical sequences
    • Schneider A, Hemphill A, Wyler T, Seebeck T, (1988) Large microtubule-associated protein of T. brucei has tandemly repeated, near-identical sequences. Science 241: 459-462.
    • (1988) Science , vol.241 , pp. 459-462
    • Schneider, A.1    Hemphill, A.2    Wyler, T.3    Seebeck, T.4
  • 36
    • 0036193639 scopus 로고    scopus 로고
    • Two related subpellicular cytoskeleton-associated proteins in Trypanosoma brucei stabilize microtubules
    • Vedrenne C, Giroud C, Robinson DR, Besteiro S, Bosc C, et al. (2002) Two related subpellicular cytoskeleton-associated proteins in Trypanosoma brucei stabilize microtubules. Mol Biol Cell 13: 1058-1070.
    • (2002) Mol Biol Cell , vol.13 , pp. 1058-1070
    • Vedrenne, C.1    Giroud, C.2    Robinson, D.R.3    Besteiro, S.4    Bosc, C.5
  • 37
    • 0026521519 scopus 로고
    • A novel microtubule-binding motif identified in a high molecular weight microtubule-associated protein from Trypanosoma brucei
    • Hemphill A, Affolter M, Seebeck T, (1992) A novel microtubule-binding motif identified in a high molecular weight microtubule-associated protein from Trypanosoma brucei. J Cell Biol 117: 95-103.
    • (1992) J Cell Biol , vol.117 , pp. 95-103
    • Hemphill, A.1    Affolter, M.2    Seebeck, T.3
  • 38
    • 0014099286 scopus 로고
    • Evidence for four classes of microtubules in individual cells
    • Behnke O, Forer A, (1967) Evidence for four classes of microtubules in individual cells. J Cell Sci 2: 169-192.
    • (1967) J Cell Sci , vol.2 , pp. 169-192
    • Behnke, O.1    Forer, A.2
  • 39
    • 0036468420 scopus 로고    scopus 로고
    • Centrosome composition and microtubule anchoring mechanisms
    • Bornens M, (2002) Centrosome composition and microtubule anchoring mechanisms. Curr Opin Cell Biol 14: 25-34.
    • (2002) Curr Opin Cell Biol , vol.14 , pp. 25-34
    • Bornens, M.1
  • 40
    • 0021745772 scopus 로고
    • Cold-stable microtubules and microtubule-organizing centres in astrocytes in primary culture
    • Hesketh JE, Ciesielski-Treska J, Aunis D, (1984) Cold-stable microtubules and microtubule-organizing centres in astrocytes in primary culture. Neurosci Lett 51: 155-160.
    • (1984) Neurosci Lett , vol.51 , pp. 155-160
    • Hesketh, J.E.1    Ciesielski-Treska, J.2    Aunis, D.3
  • 41
    • 0024563722 scopus 로고
    • Effects of Cold and Nocodazole Treatments on the Microtubular Systems of Paramecium in Interphase
    • Torres A, Delgado P, (1989) Effects of Cold and Nocodazole Treatments on the Microtubular Systems of Paramecium in Interphase. Journal of Eukaryotic Microbiology 36: 113-119.
    • (1989) Journal of Eukaryotic Microbiology , vol.36 , pp. 113-119
    • Torres, A.1    Delgado, P.2
  • 42
    • 0028948469 scopus 로고
    • Cold-stable and cold-adapted microtubules
    • Wallin M, Stromberg E, (1995) Cold-stable and cold-adapted microtubules. Int Rev Cytol 157: 1-31.
    • (1995) Int Rev Cytol , vol.157 , pp. 1-31
    • Wallin, M.1    Stromberg, E.2
  • 43
    • 58149349810 scopus 로고    scopus 로고
    • Ciliary tubulin and its post-translational modifications
    • Gaertig J, Wloga D, (2008) Ciliary tubulin and its post-translational modifications. Curr Top Dev Biol 85: 83-113.
    • (2008) Curr Top Dev Biol , vol.85 , pp. 83-113
    • Gaertig, J.1    Wloga, D.2
  • 44
    • 77953806216 scopus 로고    scopus 로고
    • Unique post-translational modifications in specialized microtubule architecture
    • Ikegami K, Setou M, (2010) Unique post-translational modifications in specialized microtubule architecture. Cell Struct Funct 35: 15-22.
    • (2010) Cell Struct Funct , vol.35 , pp. 15-22
    • Ikegami, K.1    Setou, M.2
  • 45
    • 55249093249 scopus 로고    scopus 로고
    • The tektin family of microtubule-stabilizing proteins
    • Amos LA, (2008) The tektin family of microtubule-stabilizing proteins. Genome Biol 9: 229.
    • (2008) Genome Biol , vol.9 , pp. 229
    • Amos, L.A.1
  • 46
    • 0031913583 scopus 로고    scopus 로고
    • Two proteins isolated from sea urchin sperm flagella: structural components common to the stable microtubules of axonemes and centrioles
    • Hinchcliffe EH, Linck RW, (1998) Two proteins isolated from sea urchin sperm flagella: structural components common to the stable microtubules of axonemes and centrioles. J Cell Sci 111 (Pt 5): 585-595.
    • (1998) J Cell Sci , vol.111 , Issue.PART 5 , pp. 585-595
    • Hinchcliffe, E.H.1    Linck, R.W.2
  • 47
    • 0242540472 scopus 로고    scopus 로고
    • Protofilament ribbon compartments of ciliary and flagellar microtubules
    • Linck RW, Norrander JM, (2003) Protofilament ribbon compartments of ciliary and flagellar microtubules. Protist 154: 299-311.
    • (2003) Protist , vol.154 , pp. 299-311
    • Linck, R.W.1    Norrander, J.M.2
  • 48
    • 0033984896 scopus 로고    scopus 로고
    • The Rib43a protein is associated with forming the specialized protofilament ribbons of flagellar microtubules in Chlamydomonas
    • Norrander JM, deCathelineau AM, Brown JA, Porter ME, Linck RW, (2000) The Rib43a protein is associated with forming the specialized protofilament ribbons of flagellar microtubules in Chlamydomonas. Mol Biol Cell 11: 201-215.
    • (2000) Mol Biol Cell , vol.11 , pp. 201-215
    • Norrander, J.M.1    deCathelineau, A.M.2    Brown, J.A.3    Porter, M.E.4    Linck, R.W.5
  • 49
    • 33847370317 scopus 로고    scopus 로고
    • Functional genomics in Trypanosoma brucei identifies evolutionarily conserved components of motile flagella
    • Baron DM, Ralston KS, Kabututu ZP, Hill KL, (2007) Functional genomics in Trypanosoma brucei identifies evolutionarily conserved components of motile flagella. J Cell Sci 120: 478-491.
    • (2007) J Cell Sci , vol.120 , pp. 478-491
    • Baron, D.M.1    Ralston, K.S.2    Kabututu, Z.P.3    Hill, K.L.4
  • 51
    • 59549087545 scopus 로고    scopus 로고
    • A monoclonal antibody marker for the exclusion-zone filaments of Trypanosoma brucei
    • Bonhivers M, Landrein N, Decossas M, Robinson DR, (2008) A monoclonal antibody marker for the exclusion-zone filaments of Trypanosoma brucei. Parasit Vectors 1: 21.
    • (2008) Parasit Vectors , vol.1 , pp. 21
    • Bonhivers, M.1    Landrein, N.2    Decossas, M.3    Robinson, D.R.4
  • 52
    • 45149102845 scopus 로고    scopus 로고
    • Biogenesis of the trypanosome endo-exocytotic organelle is cytoskeleton mediated
    • Bonhivers M, Nowacki S, Landrein N, Robinson DR, (2008) Biogenesis of the trypanosome endo-exocytotic organelle is cytoskeleton mediated. PLoS Biol 6: e105.
    • (2008) PLoS Biol , vol.6
    • Bonhivers, M.1    Nowacki, S.2    Landrein, N.3    Robinson, D.R.4
  • 54
    • 24044540256 scopus 로고    scopus 로고
    • Specificity and versatility of SH3 and other proline-recognition domains: structural basis and implications for cellular signal transduction
    • Li SS, (2005) Specificity and versatility of SH3 and other proline-recognition domains: structural basis and implications for cellular signal transduction. Biochem J 390: 641-653.
    • (2005) Biochem J , vol.390 , pp. 641-653
    • Li, S.S.1
  • 55
    • 0028685490 scopus 로고
    • Fitting a mixture model by expectation maximization to discover motifs in biopolymers
    • Bailey TL, Elkan C, (1994) Fitting a mixture model by expectation maximization to discover motifs in biopolymers. Proc Int Conf Intell Syst Mol Biol 2: 28-36.
    • (1994) Proc Int Conf Intell Syst Mol Biol , vol.2 , pp. 28-36
    • Bailey, T.L.1    Elkan, C.2
  • 56
    • 33747823564 scopus 로고    scopus 로고
    • MEME: discovering and analyzing DNA and protein sequence motifs
    • Bailey TL, Williams N, Misleh C, Li WW, (2006) MEME: discovering and analyzing DNA and protein sequence motifs. Nucleic Acids Res 34: W369-373.
    • (2006) Nucleic Acids Res , vol.34
    • Bailey, T.L.1    Williams, N.2    Misleh, C.3    Li, W.W.4
  • 57
    • 0034494348 scopus 로고    scopus 로고
    • Characterization and disruption of a new Trypanosoma brucei repetitive flagellum protein, using double-stranded RNA inhibition
    • Bringaud F, Robinson DR, Barradeau S, Biteau N, Baltz D, et al. (2000) Characterization and disruption of a new Trypanosoma brucei repetitive flagellum protein, using double-stranded RNA inhibition. Mol Biochem Parasitol 111: 283-297.
    • (2000) Mol Biochem Parasitol , vol.111 , pp. 283-297
    • Bringaud, F.1    Robinson, D.R.2    Barradeau, S.3    Biteau, N.4    Baltz, D.5
  • 58
    • 0033105686 scopus 로고    scopus 로고
    • Assembly of the paraflagellar rod and the flagellum attachment zone complex during the Trypanosoma brucei cell cycle
    • Kohl L, Sherwin T, Gull K, (1999) Assembly of the paraflagellar rod and the flagellum attachment zone complex during the Trypanosoma brucei cell cycle. J Eukaryot Microbiol 46: 105-109.
    • (1999) J Eukaryot Microbiol , vol.46 , pp. 105-109
    • Kohl, L.1    Sherwin, T.2    Gull, K.3
  • 59
    • 0014206483 scopus 로고
    • Two established in vitro cell lines from human mesenchymal tumours
    • Ponten J, Saksela E, (1967) Two established in vitro cell lines from human mesenchymal tumours. Int J Cancer 2: 434-447.
    • (1967) Int J Cancer , vol.2 , pp. 434-447
    • Ponten, J.1    Saksela, E.2
  • 60
    • 0030222026 scopus 로고    scopus 로고
    • The paraflagellar rod of kinetoplastida: solved and unsolved questions
    • Bastin P, Matthews KR, Gull K, (1996) The paraflagellar rod of kinetoplastida: solved and unsolved questions. Parasitol Today 12: 302-307.
    • (1996) Parasitol Today , vol.12 , pp. 302-307
    • Bastin, P.1    Matthews, K.R.2    Gull, K.3
  • 61
    • 0032410928 scopus 로고    scopus 로고
    • Double-stranded RNA induces mRNA degradation in Trypanosoma brucei
    • Ngo H, Tschudi C, Gull K, Ullu E, (1998) Double-stranded RNA induces mRNA degradation in Trypanosoma brucei. Proc Natl Acad Sci U S A 95: 14687-14692.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 14687-14692
    • Ngo, H.1    Tschudi, C.2    Gull, K.3    Ullu, E.4
  • 62
    • 0036860235 scopus 로고    scopus 로고
    • Targeting of a tetracycline-inducible expression system to the transcriptionally silent minichromosomes of Trypanosoma brucei
    • Wickstead B, Ersfeld K, Gull K, (2002) Targeting of a tetracycline-inducible expression system to the transcriptionally silent minichromosomes of Trypanosoma brucei. Mol Biochem Parasitol 125: 211-216.
    • (2002) Mol Biochem Parasitol , vol.125 , pp. 211-216
    • Wickstead, B.1    Ersfeld, K.2    Gull, K.3
  • 63
    • 33749528009 scopus 로고    scopus 로고
    • Trypanin, a component of the flagellar Dynein regulatory complex, is essential in bloodstream form African trypanosomes
    • Ralston KS, Hill KL, (2006) Trypanin, a component of the flagellar Dynein regulatory complex, is essential in bloodstream form African trypanosomes. PLoS Pathog 2: e101.
    • (2006) PLoS Pathog , vol.2
    • Ralston, K.S.1    Hill, K.L.2
  • 64
    • 0025883663 scopus 로고
    • Overexpression of tau in a nonneuronal cell induces long cellular processes
    • Knops J, Kosik KS, Lee G, Pardee JD, Cohen-Gould L, et al. (1991) Overexpression of tau in a nonneuronal cell induces long cellular processes. J Cell Biol 114: 725-733.
    • (1991) J Cell Biol , vol.114 , pp. 725-733
    • Knops, J.1    Kosik, K.S.2    Lee, G.3    Pardee, J.D.4    Cohen-Gould, L.5
  • 65
    • 0028229455 scopus 로고
    • Microtubule-associated protein function: lessons from expression in Spodoptera frugiperda cells
    • Kosik KS, McConlogue L, (1994) Microtubule-associated protein function: lessons from expression in Spodoptera frugiperda cells. Cell Motil Cytoskeleton 28: 195-198.
    • (1994) Cell Motil Cytoskeleton , vol.28 , pp. 195-198
    • Kosik, K.S.1    McConlogue, L.2
  • 66
    • 0029124172 scopus 로고
    • Analysis of MAP 4 function in living cells using green fluorescent protein (GFP) chimeras
    • Olson KR, McIntosh JR, Olmsted JB, (1995) Analysis of MAP 4 function in living cells using green fluorescent protein (GFP) chimeras. J Cell Biol 130: 639-650.
    • (1995) J Cell Biol , vol.130 , pp. 639-650
    • Olson, K.R.1    McIntosh, J.R.2    Olmsted, J.B.3
  • 67
    • 0029914696 scopus 로고    scopus 로고
    • Microinjection of intact MAP-4 and fragments induces changes of the cytoskeleton in PtK2 cells
    • Yoshida T, Imanaka-Yoshida K, Murofushi H, Tanaka J, Ito H, et al. (1996) Microinjection of intact MAP-4 and fragments induces changes of the cytoskeleton in PtK2 cells. Cell Motil Cytoskeleton 33: 252-262.
    • (1996) Cell Motil Cytoskeleton , vol.33 , pp. 252-262
    • Yoshida, T.1    Imanaka-Yoshida, K.2    Murofushi, H.3    Tanaka, J.4    Ito, H.5
  • 68
    • 33748759561 scopus 로고    scopus 로고
    • Conserved and specific functions of axoneme components in trypanosome motility
    • Branche C, Kohl L, Toutirais G, Buisson J, Cosson J, et al. (2006) Conserved and specific functions of axoneme components in trypanosome motility. J Cell Sci 119: 3443-3455.
    • (2006) J Cell Sci , vol.119 , pp. 3443-3455
    • Branche, C.1    Kohl, L.2    Toutirais, G.3    Buisson, J.4    Cosson, J.5
  • 69
    • 79960127168 scopus 로고    scopus 로고
    • Structure-function analysis of dynein light chain 1 identifies viable motility mutants in bloodstream-form Trypanosoma brucei
    • Ralston KS, Kisalu NK, Hill KL, (2011) Structure-function analysis of dynein light chain 1 identifies viable motility mutants in bloodstream-form Trypanosoma brucei. Eukaryot Cell 10: 884-894.
    • (2011) Eukaryot Cell , vol.10 , pp. 884-894
    • Ralston, K.S.1    Kisalu, N.K.2    Hill, K.L.3
  • 70
    • 0037166943 scopus 로고    scopus 로고
    • MAP2 and tau bind longitudinally along the outer ridges of microtubule protofilaments
    • Al-Bassam J, Ozer RS, Safer D, Halpain S, Milligan RA, (2002) MAP2 and tau bind longitudinally along the outer ridges of microtubule protofilaments. J Cell Biol 157: 1187-1196.
    • (2002) J Cell Biol , vol.157 , pp. 1187-1196
    • Al-Bassam, J.1    Ozer, R.S.2    Safer, D.3    Halpain, S.4    Milligan, R.A.5
  • 71
    • 0028036352 scopus 로고
    • Tau confers drug stability but not cold stability to microtubules in living cells
    • Baas PW, Pienkowski TP, Cimbalnik KA, Toyama K, Bakalis S, et al. (1994) Tau confers drug stability but not cold stability to microtubules in living cells. J Cell Sci 107 (Pt 1): 135-143.
    • (1994) J Cell Sci , vol.107 , Issue.PART 1 , pp. 135-143
    • Baas, P.W.1    Pienkowski, T.P.2    Cimbalnik, K.A.3    Toyama, K.4    Bakalis, S.5
  • 72
    • 0027511869 scopus 로고
    • Taxol-induced flexibility of microtubules and its reversal by MAP-2 and Tau
    • Dye RB, Fink SP, Williams RC Jr, (1993) Taxol-induced flexibility of microtubules and its reversal by MAP-2 and Tau. J Biol Chem 268: 6847-6850.
    • (1993) J Biol Chem , vol.268 , pp. 6847-6850
    • Dye, R.B.1    Fink, S.P.2    Williams Jr., R.C.3
  • 73
    • 0030955208 scopus 로고    scopus 로고
    • Domains of neuronal microtubule-associated proteins and flexural rigidity of microtubules
    • Felgner H, Frank R, Biernat J, Mandelkow EM, Mandelkow E, et al. (1997) Domains of neuronal microtubule-associated proteins and flexural rigidity of microtubules. J Cell Biol 138: 1067-1075.
    • (1997) J Cell Biol , vol.138 , pp. 1067-1075
    • Felgner, H.1    Frank, R.2    Biernat, J.3    Mandelkow, E.M.4    Mandelkow, E.5
  • 74
    • 0030867993 scopus 로고    scopus 로고
    • The role of central apparatus components in flagellar motility and microtubule assembly
    • Smith EF, Lefebvre PA, (1997) The role of central apparatus components in flagellar motility and microtubule assembly. Cell Motil Cytoskeleton 38: 1-8.
    • (1997) Cell Motil Cytoskeleton , vol.38 , pp. 1-8
    • Smith, E.F.1    Lefebvre, P.A.2
  • 75
    • 0027680037 scopus 로고
    • Acetylated alpha-tubulin in Trypanosoma cruzi: immunocytochemical localization
    • Souto-Padron T, Cunha e Silva NL, de Souza W, (1993) Acetylated alpha-tubulin in Trypanosoma cruzi: immunocytochemical localization. Mem Inst Oswaldo Cruz 88: 517-528.
    • (1993) Mem Inst Oswaldo Cruz , vol.88 , pp. 517-528
    • Souto-Padron, T.1    Cunha e Silva, N.L.2    de Souza, W.3
  • 76
    • 0023110716 scopus 로고
    • Subpellicular and flagellar microtubules of Trypanosoma brucei brucei contain the same alpha-tubulin isoforms
    • Schneider A, Sherwin T, Sasse R, Russell DG, Gull K, et al. (1987) Subpellicular and flagellar microtubules of Trypanosoma brucei brucei contain the same alpha-tubulin isoforms. J Cell Biol 104: 431-438.
    • (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
  • 77
    • 0024065220 scopus 로고
    • Tubulin post-translational modifications and the construction of microtubular organelles in Trypanosoma brucei
    • Sasse R, Gull K, (1988) Tubulin post-translational modifications and the construction of microtubular organelles in Trypanosoma brucei. J Cell Sci 90 (Pt 4): 577-589.
    • (1988) J Cell Sci , vol.90 , Issue.PART 4 , pp. 577-589
    • Sasse, R.1    Gull, K.2
  • 78
    • 0031049174 scopus 로고    scopus 로고
    • Subpellicular and flagellar microtubules of Trypanosoma brucei are extensively glutamylated
    • Schneider A, Plessmann U, Weber K, (1997) Subpellicular and flagellar microtubules of Trypanosoma brucei are extensively glutamylated. J Cell Sci 110 (Pt 4): 431-437.
    • (1997) J Cell Sci , vol.110 , Issue.PART 4 , pp. 431-437
    • Schneider, A.1    Plessmann, U.2    Weber, K.3
  • 79
    • 0024591582 scopus 로고
    • Visualization of detyrosination along single microtubules reveals novel mechanisms of assembly during cytoskeletal duplication in trypanosomes
    • Sherwin T, Gull K, (1989) Visualization of detyrosination along single microtubules reveals novel mechanisms of assembly during cytoskeletal duplication in trypanosomes. Cell 57: 211-221.
    • (1989) Cell , vol.57 , pp. 211-221
    • Sherwin, T.1    Gull, K.2
  • 80
    • 58149326846 scopus 로고    scopus 로고
    • Intraflagellar transport (IFT) role in ciliary assembly, resorption and signalling
    • Pedersen LB, Rosenbaum JL, (2008) Intraflagellar transport (IFT) role in ciliary assembly, resorption and signalling. Curr Top Dev Biol 85: 23-61.
    • (2008) Curr Top Dev Biol , vol.85 , pp. 23-61
    • Pedersen, L.B.1    Rosenbaum, J.L.2
  • 81
    • 70449517408 scopus 로고    scopus 로고
    • Intraflagellar transport is required for polarized recycling of the TCR/CD3 complex to the immune synapse
    • Finetti F, Paccani SR, Riparbelli MG, Giacomello E, Perinetti G, et al. (2009) Intraflagellar transport is required for polarized recycling of the TCR/CD3 complex to the immune synapse. Nat Cell Biol 11: 1332-1339.
    • (2009) Nat Cell Biol , vol.11 , pp. 1332-1339
    • Finetti, F.1    Paccani, S.R.2    Riparbelli, M.G.3    Giacomello, E.4    Perinetti, G.5
  • 82
    • 79952291357 scopus 로고    scopus 로고
    • Global Analysis of Protein Palmitoylation in African Trypanosomes
    • Emmer BT, Nakayasu ES, Souther C, Choi H, Sobreira TJ, et al. (2011) Global Analysis of Protein Palmitoylation in African Trypanosomes. Eukaryot Cell 10 (3): 455-463.
    • (2011) Eukaryot Cell , vol.10 , Issue.3 , pp. 455-463
    • Emmer, B.T.1    Nakayasu, E.S.2    Souther, C.3    Choi, H.4    Sobreira, T.J.5
  • 83
    • 0034826896 scopus 로고    scopus 로고
    • Regulation of microtubule-associated proteins
    • Cassimeris L, Spittle C, (2001) Regulation of microtubule-associated proteins. Int Rev Cytol 210: 163-226.
    • (2001) Int Rev Cytol , vol.210 , pp. 163-226
    • Cassimeris, L.1    Spittle, C.2
  • 84
    • 0030969575 scopus 로고    scopus 로고
    • MARK, a novel family of protein kinases that phosphorylate microtubule-associated proteins and trigger microtubule disruption
    • Drewes G, Ebneth A, Preuss U, Mandelkow EM, Mandelkow E, (1997) MARK, a novel family of protein kinases that phosphorylate microtubule-associated proteins and trigger microtubule disruption. Cell 89: 297-308.
    • (1997) Cell , vol.89 , pp. 297-308
    • Drewes, G.1    Ebneth, A.2    Preuss, U.3    Mandelkow, E.M.4    Mandelkow, E.5
  • 85
    • 0033786279 scopus 로고    scopus 로고
    • Phosphorylation-dependent localization of microtubule-associated protein MAP2c to the actin cytoskeleton
    • Ozer RS, Halpain S, (2000) Phosphorylation-dependent localization of microtubule-associated protein MAP2c to the actin cytoskeleton. Mol Biol Cell 11: 3573-3587.
    • (2000) Mol Biol Cell , vol.11 , pp. 3573-3587
    • Ozer, R.S.1    Halpain, S.2
  • 86
    • 70049114411 scopus 로고    scopus 로고
    • The phosphoproteome of bloodstream form Trypanosoma brucei, causative agent of African sleeping sickness
    • Nett IR, Martin DM, Miranda-Saavedra D, Lamont D, Barber JD, et al. (2009) The phosphoproteome of bloodstream form Trypanosoma brucei, causative agent of African sleeping sickness. Mol Cell Proteomics 8: 1527-1538.
    • (2009) Mol Cell Proteomics , vol.8 , pp. 1527-1538
    • Nett, I.R.1    Martin, D.M.2    Miranda-Saavedra, D.3    Lamont, D.4    Barber, J.D.5
  • 87
    • 46049094886 scopus 로고    scopus 로고
    • The rat sperm proteome characterized via IPG strip prefractionation and LC-MS/MS identification
    • Baker MA, Hetherington L, Reeves G, Muller J, Aitken RJ, (2008) The rat sperm proteome characterized via IPG strip prefractionation and LC-MS/MS identification. Proteomics 8: 2312-2321.
    • (2008) Proteomics , vol.8 , pp. 2312-2321
    • Baker, M.A.1    Hetherington, L.2    Reeves, G.3    Muller, J.4    Aitken, R.J.5
  • 88
    • 46049094886 scopus 로고    scopus 로고
    • The mouse sperm proteome characterized via IPG strip prefractionation and LC-MS/MS identification
    • Baker MA, Hetherington L, Reeves GM, Aitken RJ, (2008) The mouse sperm proteome characterized via IPG strip prefractionation and LC-MS/MS identification. Proteomics 8: 1720-1730.
    • (2008) Proteomics , vol.8 , pp. 1720-1730
    • Baker, M.A.1    Hetherington, L.2    Reeves, G.M.3    Aitken, R.J.4
  • 89
    • 33751510977 scopus 로고    scopus 로고
    • Genomic and functional evolution of the Drosophila melanogaster sperm proteome
    • Dorus S, Busby SA, Gerike U, Shabanowitz J, Hunt DF, et al. (2006) Genomic and functional evolution of the Drosophila melanogaster sperm proteome. Nat Genet 38: 1440-1445.
    • (2006) Nat Genet , vol.38 , pp. 1440-1445
    • Dorus, S.1    Busby, S.A.2    Gerike, U.3    Shabanowitz, J.4    Hunt, D.F.5
  • 92
    • 65949096636 scopus 로고    scopus 로고
    • Comparative functional analysis of the Caenorhabditis elegans and Drosophila melanogaster proteomes
    • Schrimpf SP, Weiss M, Reiter L, Ahrens CH, Jovanovic M, et al. (2009) Comparative functional analysis of the Caenorhabditis elegans and Drosophila melanogaster proteomes. PLoS Biol 7: e48.
    • (2009) PLoS Biol , vol.7
    • Schrimpf, S.P.1    Weiss, M.2    Reiter, L.3    Ahrens, C.H.4    Jovanovic, M.5
  • 93
    • 34548429735 scopus 로고    scopus 로고
    • The proteome of the mouse photoreceptor sensory cilium complex
    • Liu Q, Tan G, Levenkova N, Li T, Pugh EN Jr, et al. (2007) The proteome of the mouse photoreceptor sensory cilium complex. Mol Cell Proteomics 6: 1299-1317.
    • (2007) Mol Cell Proteomics , vol.6 , pp. 1299-1317
    • Liu, Q.1    Tan, G.2    Levenkova, N.3    Li, T.4    Pugh Jr., E.N.5
  • 95
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: a new generation of protein database search programs
    • Altschul SF, Madden TL, Schaffer AA, Zhang J, Zhang Z, et al. (1997) Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res 25: 3389-3402.
    • (1997) Nucleic Acids Res , vol.25 , pp. 3389-3402
    • Altschul, S.F.1    Madden, T.L.2    Schaffer, A.A.3    Zhang, J.4    Zhang, Z.5
  • 96
    • 27144489108 scopus 로고    scopus 로고
    • Protein database searches using compositionally adjusted substitution matrices
    • Altschul SF, Wootton JC, Gertz EM, Agarwala R, Morgulis A, et al. (2005) Protein database searches using compositionally adjusted substitution matrices. FEBS J 272: 5101-5109.
    • (2005) FEBS J , vol.272 , pp. 5101-5109
    • Altschul, S.F.1    Wootton, J.C.2    Gertz, E.M.3    Agarwala, R.4    Morgulis, A.5
  • 97
    • 10744222662 scopus 로고    scopus 로고
    • The DNA sequence of chromosome I of an African trypanosome: gene content, chromosome organisation, recombination and polymorphism
    • Hall N, Berriman M, Lennard NJ, Harris BR, Hertz-Fowler C, et al. (2003) The DNA sequence of chromosome I of an African trypanosome: gene content, chromosome organisation, recombination and polymorphism. Nucleic Acids Res 31: 4864-4873.
    • (2003) Nucleic Acids Res , vol.31 , pp. 4864-4873
    • Hall, N.1    Berriman, M.2    Lennard, N.J.3    Harris, B.R.4    Hertz-Fowler, C.5
  • 98
    • 0033525524 scopus 로고    scopus 로고
    • A tightly regulated inducible expression system for conditional gene knock-outs and dominant-negative genetics in Trypanosoma brucei
    • Wirtz E, Leal S, Ochatt C, Cross GA, (1999) A tightly regulated inducible expression system for conditional gene knock-outs and dominant-negative genetics in Trypanosoma brucei. Mol Biochem Parasitol 99: 89-101.
    • (1999) Mol Biochem Parasitol , vol.99 , pp. 89-101
    • Wirtz, E.1    Leal, S.2    Ochatt, C.3    Cross, G.A.4
  • 99
    • 33744545308 scopus 로고    scopus 로고
    • NIMA-related kinase TbNRKC is involved in basal body separation in Trypanosoma brucei
    • Pradel LC, Bonhivers M, Landrein N, Robinson DR, (2006) NIMA-related kinase TbNRKC is involved in basal body separation in Trypanosoma brucei. J Cell Sci 119: 1852-1863.
    • (2006) J Cell Sci , vol.119 , pp. 1852-1863
    • Pradel, L.C.1    Bonhivers, M.2    Landrein, N.3    Robinson, D.R.4
  • 100
    • 34250370911 scopus 로고    scopus 로고
    • An essential cell cycle-regulated nucleolar protein relocates to the mitotic spindle where it is involved in mitotic progression in Trypanosoma brucei
    • Boucher N, Dacheux D, Giroud C, Baltz T, (2007) An essential cell cycle-regulated nucleolar protein relocates to the mitotic spindle where it is involved in mitotic progression in Trypanosoma brucei. J Biol Chem 282: 13780-13790.
    • (2007) J Biol Chem , vol.282 , pp. 13780-13790
    • Boucher, N.1    Dacheux, D.2    Giroud, C.3    Baltz, T.4
  • 101
    • 0037330751 scopus 로고    scopus 로고
    • Development of RNA interference revertants in Trypanosoma brucei cell lines generated with a double stranded RNA expression construct driven by two opposing promoters
    • Chen Y, Hung CH, Burderer T, Lee GS, (2003) Development of RNA interference revertants in Trypanosoma brucei cell lines generated with a double stranded RNA expression construct driven by two opposing promoters. Mol Biochem Parasitol 126: 275-279.
    • (2003) Mol Biochem Parasitol , vol.126 , pp. 275-279
    • Chen, Y.1    Hung, C.H.2    Burderer, T.3    Lee, G.S.4
  • 102
    • 3042616190 scopus 로고    scopus 로고
    • The small chromosomes of Trypanosoma brucei involved in antigenic variation are constructed around repetitive palindromes
    • Wickstead B, Ersfeld K, Gull K, (2004) The small chromosomes of Trypanosoma brucei involved in antigenic variation are constructed around repetitive palindromes. Genome Res 14: 1014-1024.
    • (2004) Genome Res , vol.14 , pp. 1014-1024
    • Wickstead, B.1    Ersfeld, K.2    Gull, K.3
  • 103
    • 0022655932 scopus 로고
    • A human osteosarcoma cell line secretes a growth factor structurally related to a homodimer of PDGF A-chains
    • Heldin CH, Johnsson A, Wennergren S, Wernstedt C, Betsholtz C, et al. (1986) A human osteosarcoma cell line secretes a growth factor structurally related to a homodimer of PDGF A-chains. Nature 319: 511-514.
    • (1986) Nature , vol.319 , pp. 511-514
    • Heldin, C.H.1    Johnsson, A.2    Wennergren, S.3    Wernstedt, C.4    Betsholtz, C.5
  • 104
    • 0018953062 scopus 로고
    • Production of monoclonal antibodies: strategy and tactics
    • de StGroth SF, Scheidegger D, (1980) Production of monoclonal antibodies: strategy and tactics. J Immunol Methods 35: 1-21.
    • (1980) J Immunol Methods , vol.35 , pp. 1-21
    • de StGroth, S.F.1    Scheidegger, D.2
  • 105
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK, (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 106
    • 77954662426 scopus 로고    scopus 로고
    • Approaches for functional analysis of flagellar proteins in African trypanosomes
    • Oberholzer M, Lopez MA, Ralston KS, Hill KL, (2009) Approaches for functional analysis of flagellar proteins in African trypanosomes. Methods Cell Biol 93: 21-57.
    • (2009) Methods Cell Biol , vol.93 , pp. 21-57
    • Oberholzer, M.1    Lopez, M.A.2    Ralston, K.S.3    Hill, K.L.4
  • 107
    • 0024369960 scopus 로고
    • Definition of individual components within the cytoskeleton of Trypanosoma brucei by a library of monoclonal antibodies
    • Woods A, Sherwin T, Sasse R, MacRae TH, Baines AJ, et al. (1989) Definition of individual components within the cytoskeleton of Trypanosoma brucei by a library of monoclonal antibodies. J Cell Sci 93 (Pt 3): 491-500.
    • (1989) J Cell Sci , vol.93 , Issue.PART 3 , pp. 491-500
    • Woods, A.1    Sherwin, T.2    Sasse, R.3    MacRae, T.H.4    Baines, A.J.5
  • 108
    • 77951199046 scopus 로고    scopus 로고
    • MAPK scaffolding by BIT1 in the Golgi complex modulates stress resistance
    • Yi P, Nguyen DT, Higa-Nishiyama A, Auguste P, Bouchecareilh M, et al. (2010) MAPK scaffolding by BIT1 in the Golgi complex modulates stress resistance. J Cell Sci 123: 1060-1072.
    • (2010) J Cell Sci , vol.123 , pp. 1060-1072
    • Yi, P.1    Nguyen, D.T.2    Higa-Nishiyama, A.3    Auguste, P.4    Bouchecareilh, M.5


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