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Volumn 1833, Issue 2, 2013, Pages 295-303

Back to basics: A revealing secondary reduction of the mitochondrial protein import pathway in diverse intracellular parasites

Author keywords

Microsporidia; Mitosome; Parasite; Protein import; Reductive evolution

Indexed keywords

CARRIER PROTEIN; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; OUTER MEMBRANE PROTEIN; PAM18 PROTEIN; TIM17 PROTEIN; TIM22 PROTEIN; TIM23 PROTEIN; TIM50 PROTEIN; TOM40 PROTEIN; TOM70 PROTEIN; TRANSLOCASE OF OUTER MITOCHONDRIAL MEMBRANE 20; UNCLASSIFIED DRUG;

EID: 84872596030     PISSN: 01674889     EISSN: 18792596     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2012.02.006     Document Type: Review
Times cited : (26)

References (93)
  • 3
    • 0023665552 scopus 로고
    • Eukaryotes with no mitochondria
    • Cavalier-Smith T. Eukaryotes with no mitochondria. Nature 1987, 326:332-333.
    • (1987) Nature , vol.326 , pp. 332-333
    • Cavalier-Smith, T.1
  • 4
    • 33645456207 scopus 로고    scopus 로고
    • Eukaryotic evolution, changes and challenges
    • Embley T.M., Martin W. Eukaryotic evolution, changes and challenges. Nature 2006, 440:623-630.
    • (2006) Nature , vol.440 , pp. 623-630
    • Embley, T.M.1    Martin, W.2
  • 6
  • 8
    • 0032988857 scopus 로고    scopus 로고
    • The mitosome, a novel organelle related to mitochondria in the amitochondrial parasite Entamoeba histolytica
    • Tovar J., Fischer A., Clark C.G. The mitosome, a novel organelle related to mitochondria in the amitochondrial parasite Entamoeba histolytica. Mol. Microbiol. 1999, 32:1013-1021.
    • (1999) Mol. Microbiol. , vol.32 , pp. 1013-1021
    • Tovar, J.1    Fischer, A.2    Clark, C.G.3
  • 9
    • 0032499785 scopus 로고    scopus 로고
    • Secondary absence of mitochondria in Giardia lamblia and Trichomonas vaginalis revealed by valyl-tRNA synthetase phylogeny
    • Hashimoto T., Sanchez L.B., Shirakura T., Muller M., Hasegawa M. Secondary absence of mitochondria in Giardia lamblia and Trichomonas vaginalis revealed by valyl-tRNA synthetase phylogeny. Proc. Natl. Acad. Sci. U. S. A. 1998, 95:6860-6865.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 6860-6865
    • Hashimoto, T.1    Sanchez, L.B.2    Shirakura, T.3    Muller, M.4    Hasegawa, M.5
  • 10
    • 0031892089 scopus 로고    scopus 로고
    • A mitochondrial-like chaperonin 60 gene in Giardia lamblia: evidence that diplomonads once harbored an endosymbiont related to the progenitor of mitochondria
    • Roger A.J., Svard S.G., Tovar J., Clark C.G., Smith M.W., Gillin F.D., Sogin M.L. A mitochondrial-like chaperonin 60 gene in Giardia lamblia: evidence that diplomonads once harbored an endosymbiont related to the progenitor of mitochondria. Proc. Natl. Acad. Sci. U. S. A. 1998, 95:229-234.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 229-234
    • Roger, A.J.1    Svard, S.G.2    Tovar, J.3    Clark, C.G.4    Smith, M.W.5    Gillin, F.D.6    Sogin, M.L.7
  • 11
    • 0029068423 scopus 로고
    • Direct evidence for secondary loss of mitochondria in Entamoeba histolytica
    • Clark C.G., Roger A.J. Direct evidence for secondary loss of mitochondria in Entamoeba histolytica. Proc. Natl. Acad. Sci. U. S. A. 1995, 92:6518-6521.
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 6518-6521
    • Clark, C.G.1    Roger, A.J.2
  • 12
    • 0037158721 scopus 로고    scopus 로고
    • A mitochondrial remnant in the microsporidian Trachipleistophora hominis
    • Williams B.A., Hirt R.P., Lucocq J.M., Embley T.M. A mitochondrial remnant in the microsporidian Trachipleistophora hominis. Nature 2002, 418:865-869.
    • (2002) Nature , vol.418 , pp. 865-869
    • Williams, B.A.1    Hirt, R.P.2    Lucocq, J.M.3    Embley, T.M.4
  • 13
    • 0033020661 scopus 로고    scopus 로고
    • Hsp60 is targeted to a cryptic mitochondrion-derived organelle ("crypton") in the microaerophilic protozoan parasite Entamoeba histolytica
    • Mai Z., Ghosh S., Frisardi M., Rosenthal B., Rogers R., Samuelson J. Hsp60 is targeted to a cryptic mitochondrion-derived organelle ("crypton") in the microaerophilic protozoan parasite Entamoeba histolytica. Mol. Cell. Biol. 1999, 19:2198-2205.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 2198-2205
    • Mai, Z.1    Ghosh, S.2    Frisardi, M.3    Rosenthal, B.4    Rogers, R.5    Samuelson, J.6
  • 15
    • 0033932808 scopus 로고    scopus 로고
    • The Entamoeba histolytica mitochondrion-derived organelle (crypton) contains double-stranded DNA and appears to be bound by a double membrane
    • Ghosh S., Field J., Rogers R., Hickman M., Samuelson J. The Entamoeba histolytica mitochondrion-derived organelle (crypton) contains double-stranded DNA and appears to be bound by a double membrane. Infect. Immun. 2000, 68:4319-4322.
    • (2000) Infect. Immun. , vol.68 , pp. 4319-4322
    • Ghosh, S.1    Field, J.2    Rogers, R.3    Hickman, M.4    Samuelson, J.5
  • 17
    • 2342622026 scopus 로고    scopus 로고
    • Cryptosporidium parvum mitochondrial-type HSP70 targets homologous and heterologous mitochondria
    • Slapeta J., Keithly J.S. Cryptosporidium parvum mitochondrial-type HSP70 targets homologous and heterologous mitochondria. Eukaryot. Cell 2004, 3:483-494.
    • (2004) Eukaryot. Cell , vol.3 , pp. 483-494
    • Slapeta, J.1    Keithly, J.S.2
  • 18
    • 0024151128 scopus 로고
    • Energy metabolism of protozoa without mitochondria
    • Muller M. Energy metabolism of protozoa without mitochondria. Annu. Rev. Microbiol. 1988, 42:465-488.
    • (1988) Annu. Rev. Microbiol. , vol.42 , pp. 465-488
    • Muller, M.1
  • 20
    • 47249094614 scopus 로고    scopus 로고
    • Maturation of iron-sulfur proteins in eukaryotes: mechanisms, connected processes, and diseases
    • Lill R., Muhlenhoff U. Maturation of iron-sulfur proteins in eukaryotes: mechanisms, connected processes, and diseases. Annu. Rev. Biochem. 2008, 77:669-700.
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 669-700
    • Lill, R.1    Muhlenhoff, U.2
  • 22
    • 27444447414 scopus 로고    scopus 로고
    • Causes and effects of nuclear genome reduction
    • Keeling P.J., Slamovits C.H. Causes and effects of nuclear genome reduction. Curr. Opin. Genet. Dev. 2005, 15:601-608.
    • (2005) Curr. Opin. Genet. Dev. , vol.15 , pp. 601-608
    • Keeling, P.J.1    Slamovits, C.H.2
  • 23
    • 80054784355 scopus 로고    scopus 로고
    • The intriguing nature of microsporidian genomes
    • Corradi N., Slamovits C.H. The intriguing nature of microsporidian genomes. Brief. Funct. Genomics 2011, 10:115-124.
    • (2011) Brief. Funct. Genomics , vol.10 , pp. 115-124
    • Corradi, N.1    Slamovits, C.H.2
  • 24
    • 20444481760 scopus 로고    scopus 로고
    • Review of the sequential development of Loma salmonae (Microsporidia) based on experimental infections of rainbow trout (Oncorhynchus mykiss) and Chinook salmon (O. tshawytscha)
    • Kent M.L., Speare D.J. Review of the sequential development of Loma salmonae (Microsporidia) based on experimental infections of rainbow trout (Oncorhynchus mykiss) and Chinook salmon (O. tshawytscha). Folia Parasitol (Praha) 2005, 52:63-68.
    • (2005) Folia Parasitol (Praha) , vol.52 , pp. 63-68
    • Kent, M.L.1    Speare, D.J.2
  • 25
    • 77449139075 scopus 로고    scopus 로고
    • The ecology and evolution of microsporidian parasites
    • Smith J.E. The ecology and evolution of microsporidian parasites. Parasitology 2009, 136:1901-1914.
    • (2009) Parasitology , vol.136 , pp. 1901-1914
    • Smith, J.E.1
  • 27
    • 80052511877 scopus 로고    scopus 로고
    • Microsporidiosis: not just in AIDS patients
    • Didier E.S., Weiss L.M. Microsporidiosis: not just in AIDS patients. Curr. Opin. Infect. Dis. 2011, 24:490-495.
    • (2011) Curr. Opin. Infect. Dis. , vol.24 , pp. 490-495
    • Didier, E.S.1    Weiss, L.M.2
  • 31
    • 77949318583 scopus 로고    scopus 로고
    • Encephalitozoonosis in rabbits
    • Kunzel F., Joachim A. Encephalitozoonosis in rabbits. Parasitol. Res. 2010, 106:299-309.
    • (2010) Parasitol. Res. , vol.106 , pp. 299-309
    • Kunzel, F.1    Joachim, A.2
  • 32
    • 84856489199 scopus 로고    scopus 로고
    • The complete sequence of the smallest known nuclear genome from the microsporidian Encephalitozoon intestinalis
    • Corradi N., Pombert J.F., Farinelli L., Didier E.S., Keeling P.J. The complete sequence of the smallest known nuclear genome from the microsporidian Encephalitozoon intestinalis. Nat. Commun. 2010, 1:77.
    • (2010) Nat. Commun. , vol.1 , pp. 77
    • Corradi, N.1    Pombert, J.F.2    Farinelli, L.3    Didier, E.S.4    Keeling, P.J.5
  • 33
    • 72749101415 scopus 로고    scopus 로고
    • Unique physiology of host-parasite interactions in microsporidia infections
    • Williams B.A. Unique physiology of host-parasite interactions in microsporidia infections. Cell. Microbiol. 2009, 11:1551-1560.
    • (2009) Cell. Microbiol. , vol.11 , pp. 1551-1560
    • Williams, B.A.1
  • 35
    • 41049090836 scopus 로고    scopus 로고
    • Patterns of genome evolution among the microsporidian parasites Encephalitozoon cuniculi, Antonospora locustae and Enterocytozoon bieneusi
    • Corradi N., Akiyoshi D.E., Morrison H.G., Feng X., Weiss L.M., Tzipori S., Keeling P.J. Patterns of genome evolution among the microsporidian parasites Encephalitozoon cuniculi, Antonospora locustae and Enterocytozoon bieneusi. PLoS One 2007, 2:e1277.
    • (2007) PLoS One , vol.2
    • Corradi, N.1    Akiyoshi, D.E.2    Morrison, H.G.3    Feng, X.4    Weiss, L.M.5    Tzipori, S.6    Keeling, P.J.7
  • 38
    • 75349085888 scopus 로고    scopus 로고
    • Draft genome sequence of the Daphnia pathogen Octosporea bayeri: insights into the gene content of a large microsporidian genome and a model for host-parasite interactions
    • Corradi N., Haag K.L., Pombert J.F., Ebert D., Keeling P.J. Draft genome sequence of the Daphnia pathogen Octosporea bayeri: insights into the gene content of a large microsporidian genome and a model for host-parasite interactions. Genome Biol. 2009, 10:R106.
    • (2009) Genome Biol. , vol.10
    • Corradi, N.1    Haag, K.L.2    Pombert, J.F.3    Ebert, D.4    Keeling, P.J.5
  • 39
    • 79955453718 scopus 로고    scopus 로고
    • Immunolocalization of an alternative respiratory chain in Antonospora (Paranosema) locustae spores: mitosomes retain their role in microsporidial energy metabolism
    • Dolgikh V.V., Senderskiy I.V., Pavlova O.A., Naumov A.M., Beznoussenko G.V. Immunolocalization of an alternative respiratory chain in Antonospora (Paranosema) locustae spores: mitosomes retain their role in microsporidial energy metabolism. Eukaryot. Cell 2011, 10:588-593.
    • (2011) Eukaryot. Cell , vol.10 , pp. 588-593
    • Dolgikh, V.V.1    Senderskiy, I.V.2    Pavlova, O.A.3    Naumov, A.M.4    Beznoussenko, G.V.5
  • 41
    • 44349083493 scopus 로고    scopus 로고
    • A novel route for ATP acquisition by the remnant mitochondria of Encephalitozoon cuniculi
    • Tsaousis A.D., Kunji E.R., Goldberg A.V., Lucocq J.M., Hirt R.P., Embley T.M. A novel route for ATP acquisition by the remnant mitochondria of Encephalitozoon cuniculi. Nature 2008, 453:553-556.
    • (2008) Nature , vol.453 , pp. 553-556
    • Tsaousis, A.D.1    Kunji, E.R.2    Goldberg, A.V.3    Lucocq, J.M.4    Hirt, R.P.5    Embley, T.M.6
  • 44
    • 0027363793 scopus 로고
    • Cloning and disruption of the gene encoding yeast mitochondrial chaperonin 10, the homolog of E. coli groES
    • Rospert S., Junne T., Glick B.S., Schatz G. Cloning and disruption of the gene encoding yeast mitochondrial chaperonin 10, the homolog of E. coli groES. FEBS Lett. 1993, 335:358-360.
    • (1993) FEBS Lett. , vol.335 , pp. 358-360
    • Rospert, S.1    Junne, T.2    Glick, B.S.3    Schatz, G.4
  • 45
    • 0028855710 scopus 로고
    • Solution structure of the acetylated and noncleavable mitochondrial targeting signal of rat chaperonin 10
    • Jarvis J.A., Ryan M.T., Hoogenraad N.J., Craik D.J., Hoj P.B. Solution structure of the acetylated and noncleavable mitochondrial targeting signal of rat chaperonin 10. J. Biol. Chem. 1995, 270:1323-1331.
    • (1995) J. Biol. Chem. , vol.270 , pp. 1323-1331
    • Jarvis, J.A.1    Ryan, M.T.2    Hoogenraad, N.J.3    Craik, D.J.4    Hoj, P.B.5
  • 47
    • 58149327046 scopus 로고    scopus 로고
    • Evidence of a reduced and modified mitochondrial protein import apparatus in microsporidian mitosomes
    • Waller R.F., Jabbour C., Chan N.C., Celik N., Likic V.A., Mulhern T.D., Lithgow T. Evidence of a reduced and modified mitochondrial protein import apparatus in microsporidian mitosomes. Eukaryot. Cell 2009, 8:19-26.
    • (2009) Eukaryot. Cell , vol.8 , pp. 19-26
    • Waller, R.F.1    Jabbour, C.2    Chan, N.C.3    Celik, N.4    Likic, V.A.5    Mulhern, T.D.6    Lithgow, T.7
  • 48
    • 34249873947 scopus 로고    scopus 로고
    • Translocation of proteins into mitochondria
    • Neupert W., Herrmann J.M. Translocation of proteins into mitochondria. Annu. Rev. Biochem. 2007, 76:723-749.
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 723-749
    • Neupert, W.1    Herrmann, J.M.2
  • 49
    • 79851512985 scopus 로고    scopus 로고
    • Structural insight into the mitochondrial protein import system
    • Endo T., Yamano K., Kawano S. Structural insight into the mitochondrial protein import system. Biochim. Biophys. Acta 2011, 1808:955-970.
    • (2011) Biochim. Biophys. Acta , vol.1808 , pp. 955-970
    • Endo, T.1    Yamano, K.2    Kawano, S.3
  • 50
    • 0029087855 scopus 로고
    • MitoProt, a Macintosh application for studying mitochondrial proteins
    • Claros M.G. MitoProt, a Macintosh application for studying mitochondrial proteins. Comput. Appl. Biosci. 1995, 11:441-447.
    • (1995) Comput. Appl. Biosci. , vol.11 , pp. 441-447
    • Claros, M.G.1
  • 51
    • 0029915525 scopus 로고    scopus 로고
    • Computational method to predict mitochondrially imported proteins and their targeting sequences
    • Claros M.G., Vincens P. Computational method to predict mitochondrially imported proteins and their targeting sequences. Eur. J. Biochem. 1996, 241:779-786.
    • (1996) Eur. J. Biochem. , vol.241 , pp. 779-786
    • Claros, M.G.1    Vincens, P.2
  • 52
    • 33646089667 scopus 로고    scopus 로고
    • The C-terminal TPR domain of Tom70 defines a family of mitochondrial protein import receptors found only in animals and fungi
    • Chan N.C., Likic V.A., Waller R.F., Mulhern T.D., Lithgow T. The C-terminal TPR domain of Tom70 defines a family of mitochondrial protein import receptors found only in animals and fungi. J. Mol. Biol. 2006, 358:1010-1022.
    • (2006) J. Mol. Biol. , vol.358 , pp. 1010-1022
    • Chan, N.C.1    Likic, V.A.2    Waller, R.F.3    Mulhern, T.D.4    Lithgow, T.5
  • 53
    • 0037428164 scopus 로고    scopus 로고
    • Molecular chaperones Hsp90 and Hsp70 deliver preproteins to the mitochondrial import receptor Tom70
    • Young J.C., Hoogenraad N.J., Hartl F.U. Molecular chaperones Hsp90 and Hsp70 deliver preproteins to the mitochondrial import receptor Tom70. Cell 2003, 112:41-50.
    • (2003) Cell , vol.112 , pp. 41-50
    • Young, J.C.1    Hoogenraad, N.J.2    Hartl, F.U.3
  • 54
    • 0030769419 scopus 로고    scopus 로고
    • Differential recognition of preproteins by the purified cytosolic domains of the mitochondrial import receptors Tom20, Tom22, and Tom70
    • Brix J., Dietmeier K., Pfanner N. Differential recognition of preproteins by the purified cytosolic domains of the mitochondrial import receptors Tom20, Tom22, and Tom70. J. Biol. Chem. 1997, 272:20730-20735.
    • (1997) J. Biol. Chem. , vol.272 , pp. 20730-20735
    • Brix, J.1    Dietmeier, K.2    Pfanner, N.3
  • 57
    • 0345861754 scopus 로고    scopus 로고
    • The Omp85 family of proteins is essential for outer membrane biogenesis in mitochondria and bacteria
    • Gentle I., Gabriel K., Beech P., Waller R., Lithgow T. The Omp85 family of proteins is essential for outer membrane biogenesis in mitochondria and bacteria. J. Cell Biol. 2004, 164:19-24.
    • (2004) J. Cell Biol. , vol.164 , pp. 19-24
    • Gentle, I.1    Gabriel, K.2    Beech, P.3    Waller, R.4    Lithgow, T.5
  • 58
    • 0642377467 scopus 로고    scopus 로고
    • POTRA: a conserved domain in the FtsQ family and a class of beta-barrel outer membrane proteins
    • Sanchez-Pulido L., Devos D., Genevrois S., Vicente M., Valencia A. POTRA: a conserved domain in the FtsQ family and a class of beta-barrel outer membrane proteins. Trends Biochem. Sci. 2003, 28:523-526.
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 523-526
    • Sanchez-Pulido, L.1    Devos, D.2    Genevrois, S.3    Vicente, M.4    Valencia, A.5
  • 63
    • 0036674105 scopus 로고    scopus 로고
    • Cryptosporidiosis: biology, pathogenesis and disease
    • Tzipori S., Ward H. Cryptosporidiosis: biology, pathogenesis and disease. Microbes Infect. 2002, 4:1047-1058.
    • (2002) Microbes Infect. , vol.4 , pp. 1047-1058
    • Tzipori, S.1    Ward, H.2
  • 67
    • 33746575844 scopus 로고    scopus 로고
    • Evolution of the molecular machines for protein import into mitochondria
    • Dolezal P., Likic V., Tachezy J., Lithgow T. Evolution of the molecular machines for protein import into mitochondria. Science 2006, 313:314-318.
    • (2006) Science , vol.313 , pp. 314-318
    • Dolezal, P.1    Likic, V.2    Tachezy, J.3    Lithgow, T.4
  • 68
    • 0347513216 scopus 로고    scopus 로고
    • Mitochondrial-type iron-sulfur cluster biosynthesis genes (IscS and IscU) in the apicomplexan Cryptosporidium parvum
    • LaGier M.J., Tachezy J., Stejskal F., Kutisova K., Keithly J.S. Mitochondrial-type iron-sulfur cluster biosynthesis genes (IscS and IscU) in the apicomplexan Cryptosporidium parvum. Microbiology 2003, 149:3519-3530.
    • (2003) Microbiology , vol.149 , pp. 3519-3530
    • LaGier, M.J.1    Tachezy, J.2    Stejskal, F.3    Kutisova, K.4    Keithly, J.S.5
  • 69
    • 36549035976 scopus 로고    scopus 로고
    • Iron-sulfur proteins and iron-sulfur cluster assembly in organisms with hydrogenosomes and mitosomes
    • Springer Verlag, Berlin, Heidelberg (Germany), W.F. Martin, M. Müller (Eds.)
    • Tachezy J., Dolezal P. Iron-sulfur proteins and iron-sulfur cluster assembly in organisms with hydrogenosomes and mitosomes. Origin of Mitochondria and Hydrogenosomes 2007, 105-133. Springer Verlag, Berlin, Heidelberg (Germany). W.F. Martin, M. Müller (Eds.).
    • (2007) Origin of Mitochondria and Hydrogenosomes , pp. 105-133
    • Tachezy, J.1    Dolezal, P.2
  • 70
    • 51449110235 scopus 로고    scopus 로고
    • The mitochondrion-related organelle of Cryptosporidium parvum
    • Springer-Verlag, Berlin Heidelberg, J. Tachezy (Ed.)
    • Keithly J.S. The mitochondrion-related organelle of Cryptosporidium parvum. Hydrogenosomes and Mitosomes: Mitochondria of Anaerobic Eukaryotes 2007, 231-253. Springer-Verlag, Berlin Heidelberg. J. Tachezy (Ed.).
    • (2007) Hydrogenosomes and Mitosomes: Mitochondria of Anaerobic Eukaryotes , pp. 231-253
    • Keithly, J.S.1
  • 75
    • 37549063441 scopus 로고    scopus 로고
    • An ADP/ATP-specific mitochondrial carrier protein in the microsporidian Antonospora locustae
    • Williams B.A., Haferkamp I., Keeling P.J. An ADP/ATP-specific mitochondrial carrier protein in the microsporidian Antonospora locustae. J. Mol. Biol. 2008, 375:1249-1257.
    • (2008) J. Mol. Biol. , vol.375 , pp. 1249-1257
    • Williams, B.A.1    Haferkamp, I.2    Keeling, P.J.3
  • 77
    • 76249124305 scopus 로고    scopus 로고
    • Evolution. Tinkering inside the organelle
    • Alcock F., Clements A., Webb C., Lithgow T. Evolution. Tinkering inside the organelle. Science 2010, 327:649-650.
    • (2010) Science , vol.327 , pp. 649-650
    • Alcock, F.1    Clements, A.2    Webb, C.3    Lithgow, T.4
  • 81
    • 0034933985 scopus 로고    scopus 로고
    • Biology of Giardia lamblia
    • Adam R.D. Biology of Giardia lamblia. Clin. Microbiol. Rev. 2001, 14:447-475.
    • (2001) Clin. Microbiol. Rev. , vol.14 , pp. 447-475
    • Adam, R.D.1
  • 82
    • 0034804608 scopus 로고    scopus 로고
    • Mitochondrial type iron-sulfur cluster assembly in the amitochondriate eukaryotes Trichomonas vaginalis and Giardia intestinalis, as indicated by the phylogeny of IscS
    • Tachezy J., Sanchez L.B., Muller M. Mitochondrial type iron-sulfur cluster assembly in the amitochondriate eukaryotes Trichomonas vaginalis and Giardia intestinalis, as indicated by the phylogeny of IscS. Mol. Biol. Evol. 2001, 18:1919-1928.
    • (2001) Mol. Biol. Evol. , vol.18 , pp. 1919-1928
    • Tachezy, J.1    Sanchez, L.B.2    Muller, M.3
  • 84
    • 37849035275 scopus 로고    scopus 로고
    • The direct route: a simplified pathway for protein import into the mitochondrion of trypanosomes
    • Schneider A., Bursac D., Lithgow T. The direct route: a simplified pathway for protein import into the mitochondrion of trypanosomes. Trends Cell Biol. 2008, 18:12-18.
    • (2008) Trends Cell Biol. , vol.18 , pp. 12-18
    • Schneider, A.1    Bursac, D.2    Lithgow, T.3
  • 88
    • 0035874485 scopus 로고    scopus 로고
    • Self-association and precursor protein binding of Saccharomyces cerevisiae Tom40p, the core component of the protein translocation channel of the mitochondrial outer membrane
    • Gordon D.M., Wang J., Amutha B., Pain D. Self-association and precursor protein binding of Saccharomyces cerevisiae Tom40p, the core component of the protein translocation channel of the mitochondrial outer membrane. Biochem. J. 2001, 356:207-215.
    • (2001) Biochem. J. , vol.356 , pp. 207-215
    • Gordon, D.M.1    Wang, J.2    Amutha, B.3    Pain, D.4
  • 89
    • 21844467270 scopus 로고    scopus 로고
    • Electron tomographic and ultrastructural analysis of the Cryptosporidium parvum relict mitochondrion, its associated membranes, and organelles
    • Keithly J.S., Langreth S.G., Buttle K.F., Mannella C.A. Electron tomographic and ultrastructural analysis of the Cryptosporidium parvum relict mitochondrion, its associated membranes, and organelles. J. Eukaryot. Microbiol. 2005, 52:132-140.
    • (2005) J. Eukaryot. Microbiol. , vol.52 , pp. 132-140
    • Keithly, J.S.1    Langreth, S.G.2    Buttle, K.F.3    Mannella, C.A.4
  • 90
    • 80052394798 scopus 로고    scopus 로고
    • Sulfate activation in mitosomes plays an important role in the proliferation of Entamoeba histolytica
    • Mi-ichi F., Makiuchi T., Furukawa A., Sato D., Nozaki T. Sulfate activation in mitosomes plays an important role in the proliferation of Entamoeba histolytica. PLoS Negl. Trop. Dis. 2011, 5:e1263.
    • (2011) PLoS Negl. Trop. Dis. , vol.5
    • Mi-ichi, F.1    Makiuchi, T.2    Furukawa, A.3    Sato, D.4    Nozaki, T.5
  • 91
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE: multiple sequence alignment with high accuracy and high throughput
    • Edgar R.C. MUSCLE: multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res. 2004, 32:1792-1797.
    • (2004) Nucleic Acids Res. , vol.32 , pp. 1792-1797
    • Edgar, R.C.1
  • 92


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.