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Volumn 4, Issue 1, 2010, Pages

Expression of Concern: Characterization of a Subunit of the Outer Dynein Arm Docking Complex Necessary for Correct Flagellar Assembly in Leishmania donovani (PLoS Negl Trop Dis 4(1): e586. https://doi.org/10.1371/journal.pntd.0000586 PMID: 20126266);Characterization of a subunit of the outer dynein arm docking complex necessary for correct flagellar assembly in Leishmania donovani

Author keywords

[No Author keywords available]

Indexed keywords

DYNEIN ADENOSINE TRIPHOSPHATASE; PROTEIN LDDC2; PROTOZOAL PROTEIN; UNCLASSIFIED DRUG; PROTEIN SUBUNIT; PROTOZOAL DNA; RECOMBINANT PROTEIN;

EID: 76249117548     PISSN: 19352727     EISSN: 19352735     Source Type: Journal    
DOI: 10.1371/journal.pntd.0010981     Document Type: Erratum
Times cited : (15)

References (48)
  • 2
    • 34247892142 scopus 로고    scopus 로고
    • Leishmania and the leishmaniases: A parasite genetic update and advances in taxonomy, epidemiology and pathogenicity in humans
    • Banuls AL, Hide M, Prugnolle F (2007) Leishmania and the leishmaniases: a parasite genetic update and advances in taxonomy, epidemiology and pathogenicity in humans. Adv Parasitol 64: 1-109.
    • (2007) Adv Parasitol , vol.64 , pp. 1-109
    • Banuls, A.L.1    Hide, M.2    Prugnolle, F.3
  • 3
    • 0028061958 scopus 로고
    • The role of pH and temperature in the development of Leishmania parasites
    • Zilberstein D, Shapira M (1994) The role of pH and temperature in the development of Leishmania parasites. Annu Rev Microbiol 48: 449-470.
    • (1994) Annu Rev Microbiol , vol.48 , pp. 449-470
    • Zilberstein, D.1    Shapira, M.2
  • 4
    • 43949146897 scopus 로고    scopus 로고
    • The flagellum of Trypanosoma brucei: New tricks from an old dog
    • Ralston KS, Hill KL (2008) The flagellum of Trypanosoma brucei: new tricks from an old dog. Int J Parasitol 38: 869-884.
    • (2008) Int J Parasitol , vol.38 , pp. 869-884
    • Ralston, K.S.1    Hill, K.L.2
  • 5
    • 48749108690 scopus 로고    scopus 로고
    • Leishmania sand fly interaction: Progress and challenges
    • Bates PA (2008) Leishmania sand fly interaction: progress and challenges. Curr Opin Microbiol 11: 340-344.
    • (2008) Curr Opin Microbiol , vol.11 , pp. 340-344
    • Bates, P.A.1
  • 6
    • 23944437111 scopus 로고    scopus 로고
    • The two cytoplasmic dynein-2 isoforms in Leishmania mexicana perform separate functions
    • Adhiambo C, Forney JD, Asai DJ, LeBowitz JH (2005) The two cytoplasmic dynein-2 isoforms in Leishmania mexicana perform separate functions. Mol Biochem Parasitol 143: 216-225.
    • (2005) Mol Biochem Parasitol , vol.143 , pp. 216-225
    • Adhiambo, C.1    Forney, J.D.2    Asai, D.J.3    LeBowitz, J.H.4
  • 8
    • 0028205103 scopus 로고
    • Molecular analysis of the gamma heavy chain of Chlamydomonas flagellar outer-arm dynein
    • Wilkerson CG, King SM, Witman GB (1994) Molecular analysis of the gamma heavy chain of Chlamydomonas flagellar outer-arm dynein. J Cell Sci 107(Pt 3): 497-506.
    • (1994) J Cell Sci , vol.107 , Issue.PART 3 , pp. 497-506
    • Wilkerson, C.G.1    King, S.M.2    Witman, G.B.3
  • 9
    • 0028242278 scopus 로고
    • Control of flagellar bending: A new agenda based on dynein diversity
    • Brokaw CJ (1994) Control of flagellar bending: a new agenda based on dynein diversity. Cell Motil Cytoskeleton 28: 199-204.
    • (1994) Cell Motil Cytoskeleton , vol.28 , pp. 199-204
    • Brokaw, C.J.1
  • 10
    • 0025203679 scopus 로고
    • Localization of an intermediate chain of outer arm dynein by immunoelectron microscopy
    • King SM, Witman GB (1990) Localization of an intermediate chain of outer arm dynein by immunoelectron microscopy. J Biol Chem 265: 19807-19811.
    • (1990) J Biol Chem , vol.265 , pp. 19807-19811
    • King, S.M.1    Witman, G.B.2
  • 11
    • 0027953834 scopus 로고
    • Functional reconstitution of Chlamydomonas outer dynein arms from alpha-beta and gamma subunits: Requirement of a third factor
    • Takada S, Kamiya R (1994) Functional reconstitution of Chlamydomonas outer dynein arms from alpha-beta and gamma subunits: requirement of a third factor. J Cell Biol 126: 737-745.
    • (1994) J Cell Biol , vol.126 , pp. 737-745
    • Takada, S.1    Kamiya, R.2
  • 12
    • 0142211197 scopus 로고    scopus 로고
    • DC3, the smallest subunit of the Chlamydomonas flagellar outer dynein arm-docking complex, is a redoxsensitive calcium-binding protein
    • Casey DM, Yagi T, Kamiya R, Witman GB (2003) DC3, the smallest subunit of the Chlamydomonas flagellar outer dynein arm-docking complex, is a redoxsensitive calcium-binding protein. J Biol Chem 278: 42652-42659.
    • (2003) J Biol Chem , vol.278 , pp. 42652-42659
    • Casey, D.M.1    Yagi, T.2    Kamiya, R.3    Witman, G.B.4
  • 13
    • 0030953996 scopus 로고    scopus 로고
    • The Chlamydomonas reinhardtii ODA3 gene encodes a protein of the outer dynein arm docking complex
    • Koutoulis A, Pazour GJ, Wilkerson CG, Inaba K, Sheng H, et al. (1997) The Chlamydomonas reinhardtii ODA3 gene encodes a protein of the outer dynein arm docking complex. J Cell Biol 137: 1069-1080.
    • (1997) J Cell Biol , vol.137 , pp. 1069-1080
    • Koutoulis, A.1    Pazour, G.J.2    Wilkerson, C.G.3    Inaba, K.4    Sheng, H.5
  • 14
    • 0036199035 scopus 로고    scopus 로고
    • The outer dynein arm-docking complex: Composition and characterization of a subunit (oda1) necessary for outer arm assembly
    • Takada S, Wilkerson CG, Wakabayashi K, Kamiya R, Witman GB (2002) The outer dynein arm-docking complex: composition and characterization of a subunit (oda1) necessary for outer arm assembly. Mol Biol Cell 13: 1015-1029.
    • (2002) Mol Biol Cell , vol.13 , pp. 1015-1029
    • Takada, S.1    Wilkerson, C.G.2    Wakabayashi, K.3    Kamiya, R.4    Witman, G.B.5
  • 15
    • 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
  • 16
    • 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
  • 17
    • 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
  • 18
    • 0141520538 scopus 로고    scopus 로고
    • Developmentally induced changes of the proteome in the protozoan parasite Leishmania donovani
    • Bente M, Harder S, Wiesgigl M, Heukeshoven J, Gelhaus C, et al. (2003) Developmentally induced changes of the proteome in the protozoan parasite Leishmania donovani. Proteomics 3: 1811-1829.
    • (2003) Proteomics , vol.3 , pp. 1811-1829
    • Bente, M.1    Harder, S.2    Wiesgigl, M.3    Heukeshoven, J.4    Gelhaus, C.5
  • 19
    • 0032513205 scopus 로고    scopus 로고
    • Leishmania donovani heat shock protein 100. Characterization and function in amastigote stage differentiation
    • Krobitsch S, Brandau S, Hoyer C, Schmetz C, Hubel A, et al. (1998) Leishmania donovani heat shock protein 100. Characterization and function in amastigote stage differentiation. J Biol Chem 273: 6488-6494.
    • (1998) J Biol Chem , vol.273 , pp. 6488-6494
    • Krobitsch, S.1    Brandau, S.2    Hoyer, C.3    Schmetz, C.4    Hubel, A.5
  • 20
    • 0027995077 scopus 로고
    • pJC20 and pJC40-two high-copy-number vectors for T7 RNA polymerase-dependent expression of recombinant genes in Escherichia coli
    • Clos J, Brandau S (1994) pJC20 and pJC40-two high-copy-number vectors for T7 RNA polymerase-dependent expression of recombinant genes in Escherichia coli. Protein Expr Purif 5: 133-137.
    • (1994) Protein Expr Purif , vol.5 , pp. 133-137
    • Clos, J.1    Brandau, S.2
  • 21
  • 22
    • 0033500153 scopus 로고    scopus 로고
    • Flagellar morphogenesis: Protein targeting and assembly in the paraflagellar rod of trypanosomes
    • Bastin P, MacRae TH, Francis SB, Matthews KR, Gull K (1999) Flagellar morphogenesis: protein targeting and assembly in the paraflagellar rod of trypanosomes. Mol Cell Biol 19: 8191-8200.
    • (1999) Mol Cell Biol , vol.19 , pp. 8191-8200
    • Bastin, P.1    MacRae, T.H.2    Francis, S.B.3    Matthews, K.R.4    Gull, K.5
  • 23
    • 0034523028 scopus 로고    scopus 로고
    • Protein targeting to flagella of trypanosomatid protozoa
    • Bloodgood RA (2000) Protein targeting to flagella of trypanosomatid protozoa. Cell Biol Int 24: 857-862.
    • (2000) Cell Biol Int , vol.24 , pp. 857-862
    • Bloodgood, R.A.1
  • 24
    • 0032878255 scopus 로고    scopus 로고
    • Characterization of a targeting motif for a flagellar membrane protein in Leishmania enriettii
    • Snapp EL, Landfear SM (1999) Characterization of a targeting motif for a flagellar membrane protein in Leishmania enriettii. J Biol Chem 274: 29543-29548.
    • (1999) J Biol Chem , vol.274 , pp. 29543-29548
    • Snapp, E.L.1    Landfear, S.M.2
  • 26
    • 0030841734 scopus 로고    scopus 로고
    • Loss of virulence in Leishmania donovani deficient in an amastigote-specific protein, A2
    • Zhang WW, Matlashewski G (1997) Loss of virulence in Leishmania donovani deficient in an amastigote-specific protein, A2. Proc Natl Acad Sci U S A 94: 8807-8811.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 8807-8811
    • Zhang, W.W.1    Matlashewski, G.2
  • 28
    • 0030271515 scopus 로고    scopus 로고
    • Coiled coils: New structures and new functions
    • Lupas A (1996) Coiled coils: new structures and new functions. Trends Biochem Sci 21: 375-382.
    • (1996) Trends Biochem Sci , vol.21 , pp. 375-382
    • Lupas, A.1
  • 29
    • 85047681474 scopus 로고    scopus 로고
    • Assembly and motility of eukaryotic cilia and flagella. Lessons from Chlamydomonas reinhardtii
    • Silflow CD, Lefebvre PA (2001) Assembly and motility of eukaryotic cilia and flagella. Lessons from Chlamydomonas reinhardtii. Plant Physiol 127: 1500-1507.
    • (2001) Plant Physiol , vol.127 , pp. 1500-1507
    • Silflow, C.D.1    Lefebvre, P.A.2
  • 30
    • 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
  • 31
    • 0028099525 scopus 로고
    • 22S axonemal dynein is preassembled and functional prior to being transported to and attached on the axonemes
    • Fok AK, Wang H, Katayama A, Aihara MS, Allen RD (1994) 22S axonemal dynein is preassembled and functional prior to being transported to and attached on the axonemes. Cell Motil Cytoskeleton 29: 215-224.
    • (1994) Cell Motil Cytoskeleton , vol.29 , pp. 215-224
    • Fok, A.K.1    Wang, H.2    Katayama, A.3    Aihara, M.S.4    Allen, R.D.5
  • 32
    • 0024242221 scopus 로고
    • Mutations at twelve independent loci result in absence of outer dynein arms in Chylamydomonas reinhardtii
    • Kamiya R (1988) Mutations at twelve independent loci result in absence of outer dynein arms in Chylamydomonas reinhardtii. J Cell Biol 107: 2253-2258.
    • (1988) J Cell Biol , vol.107 , pp. 2253-2258
    • Kamiya, R.1
  • 33
    • 0031021267 scopus 로고    scopus 로고
    • Beat frequency difference between the two flagella of Chlamydomonas depends on the attachment site of outer dynein arms on the outer-doublet microtubules
    • Takada S, Kamiya R (1997) Beat frequency difference between the two flagella of Chlamydomonas depends on the attachment site of outer dynein arms on the outer-doublet microtubules. Cell Motil Cytoskeleton 36: 68-75.
    • (1997) Cell Motil Cytoskeleton , vol.36 , pp. 68-75
    • Takada, S.1    Kamiya, R.2
  • 34
    • 0345255945 scopus 로고    scopus 로고
    • Intraflagellar transport
    • Scholey JM (2003) Intraflagellar transport. Annu Rev Cell Dev Biol 19: 423-443.
    • (2003) Annu Rev Cell Dev Biol , vol.19 , pp. 423-443
    • Scholey, J.M.1
  • 35
    • 0142105416 scopus 로고    scopus 로고
    • Novel roles for the flagellum in cell morphogenesis and cytokinesis of trypanosomes
    • Kohl L, Robinson D, Bastin P (2003) Novel roles for the flagellum in cell morphogenesis and cytokinesis of trypanosomes. Embo J 22: 5336-5346.
    • (2003) Embo J , vol.22 , pp. 5336-5346
    • Kohl, L.1    Robinson, D.2    Bastin, P.3
  • 36
    • 54249123694 scopus 로고    scopus 로고
    • Actin-depolymerizing factor, ADF/cofilin, is essentially required in assembly of Leishmania flagellum
    • Tammana TV, Sahasrabuddhe AA, Mitra K, Bajpai VK, Gupta CM (2008) Actin-depolymerizing factor, ADF/cofilin, is essentially required in assembly of Leishmania flagellum. Mol Microbiol 70: 837-852.
    • (2008) Mol Microbiol , vol.70 , pp. 837-852
    • Tammana, T.V.1    Sahasrabuddhe, A.A.2    Mitra, K.3    Bajpai, V.K.4    Gupta, C.M.5
  • 37
    • 33745262164 scopus 로고    scopus 로고
    • Interacting protein kinases involved in the regulation of flagellar length
    • Erdmann M, Scholz A, Melzer IM, Schmetz C, Wiese M (2006) Interacting protein kinases involved in the regulation of flagellar length. Mol Biol Cell 17: 2035-2045.
    • (2006) Mol Biol Cell , vol.17 , pp. 2035-2045
    • Erdmann, M.1    Scholz, A.2    Melzer, I.M.3    Schmetz, C.4    Wiese, M.5
  • 38
    • 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
  • 39
    • 0242720365 scopus 로고    scopus 로고
    • Identification of mitogen-activated protein kinase homologues from Leishmania mexicana
    • Wiese M, Wang Q, Gorcke I (2003) Identification of mitogen-activated protein kinase homologues from Leishmania mexicana. Int J Parasitol 33: 1577-1587.
    • (2003) Int J Parasitol , vol.33 , pp. 1577-1587
    • Wiese, M.1    Wang, Q.2    Gorcke, I.3
  • 41
    • 33645068852 scopus 로고    scopus 로고
    • Analysis of the phosphoproteome of Chlamydomonas reinhardtii provides new insights into various cellular pathways
    • Wagner V, Gessner G, Heiland I, Kaminski M, Hawat S, et al. (2006) Analysis of the phosphoproteome of Chlamydomonas reinhardtii provides new insights into various cellular pathways. Eukaryot Cell 5: 457-468.
    • (2006) Eukaryot Cell , vol.5 , pp. 457-468
    • Wagner, V.1    Gessner, G.2    Heiland, I.3    Kaminski, M.4    Hawat, S.5
  • 42
    • 76249097649 scopus 로고    scopus 로고
    • The heat shock response in Leishmania spp. In Heat shock proteins in biology and disease
    • GMulthoff, eds. Kerala, India: Research Signpost. pp
    • Clos J (1997) The heat shock response in Leishmania spp. In Heat shock proteins in biology and disease. In Heat shock proteins in biology and disease JRadons, GMulthoff, eds. Kerala, India: Research Signpost. pp 421-448.
    • (1997) Heat shock proteins in biology and disease JRadons , pp. 421-448
    • Clos, J.1
  • 43
    • 0026533657 scopus 로고
    • The interaction of Leishmania species with macrophages
    • Alexander J, Russell DG (1992) The interaction of Leishmania species with macrophages. Adv Parasitol 31: 175-254.
    • (1992) Adv Parasitol , vol.31 , pp. 175-254
    • Alexander, J.1    Russell, D.G.2
  • 44
    • 0036698235 scopus 로고    scopus 로고
    • Interaction of Leishmania with the host macrophage
    • Handman E, Bullen DV (2002) Interaction of Leishmania with the host macrophage. Trends Parasitol 18: 332-334.
    • (2002) Trends Parasitol , vol.18 , pp. 332-334
    • Handman, E.1    Bullen, D.V.2
  • 45
    • 0036178528 scopus 로고    scopus 로고
    • Targeted gene deletion in Leishmania major identifies leishmanolysin (GP63) as a virulence factor
    • Joshi PB, Kelly BL, Kamhawi S, Sacks DL, McMaster WR (2002) Targeted gene deletion in Leishmania major identifies leishmanolysin (GP63) as a virulence factor. Mol Biochem Parasitol 120: 33-40.
    • (2002) Mol Biochem Parasitol , vol.120 , pp. 33-40
    • Joshi, P.B.1    Kelly, B.L.2    Kamhawi, S.3    Sacks, D.L.4    McMaster, W.R.5
  • 46
    • 0031939025 scopus 로고    scopus 로고
    • Lipophosphoglycan (LPG) and the identification of virulence genes in the protozoan parasite Leishmania
    • Beverley SM, Turco SJ (1998) Lipophosphoglycan (LPG) and the identification of virulence genes in the protozoan parasite Leishmania. Trends Microbiol 6: 35-40.
    • (1998) Trends Microbiol , vol.6 , pp. 35-40
    • Beverley, S.M.1    Turco, S.J.2
  • 47
    • 0027487851 scopus 로고
    • Reversion to virulence in Leishmania major correlates with expression of surface lipophosphoglycan
    • Shankar A, Mitchen TK, Hall LR, Turco SJ, Titus RG (1993) Reversion to virulence in Leishmania major correlates with expression of surface lipophosphoglycan. Mol Biochem Parasitol 61: 207-216.
    • (1993) Mol Biochem Parasitol , vol.61 , pp. 207-216
    • Shankar, A.1    Mitchen, T.K.2    Hall, L.R.3    Turco, S.J.4    Titus, R.G.5
  • 48
    • 0041315545 scopus 로고    scopus 로고
    • Comparison of the A2 gene locus in Leishmania donovani and Leishmania major and its control over cutaneous infection
    • Zhang WW, Mendez S, Ghosh A, Myler P, Ivens A, et al. (2003) Comparison of the A2 gene locus in Leishmania donovani and Leishmania major and its control over cutaneous infection. J Biol Chem 278: 35508-35515.
    • (2003) J Biol Chem , vol.278 , pp. 35508-35515
    • Zhang, W.W.1    Mendez, S.2    Ghosh, A.3    Myler, P.4    Ivens, A.5


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