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Volumn 106, Issue 1, 2000, Pages 11-20

Competition and protease sensitivity assays provide evidence for the existence of a hydrogenosomal protein import machinery in Trichomonas vaginalis

Author keywords

Amitochondriate protist; Evolution; Hydrogenosome; Mitochondria

Indexed keywords

ADENOSINE TRIPHOSPHATE; HEAT SHOCK PROTEIN 60; HEAT SHOCK PROTEIN 70; HYDROGENASE; PROTEINASE; PROTOZOAL PROTEIN; TRYPSIN;

EID: 0343920067     PISSN: 01666851     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0166-6851(99)00196-6     Document Type: Article
Times cited : (6)

References (57)
  • 1
    • 0027787578 scopus 로고
    • The hydrogenosome
    • Müller M. The hydrogenosome. J. Gen. Microbiol. 139:1993;2879-2889.
    • (1993) J. Gen. Microbiol. , vol.139 , pp. 2879-2889
    • Müller, M.1
  • 2
    • 0000180552 scopus 로고
    • Psalteriomonas lanterna gen. nov., sp. nov., a free-living amoeboflagellate isolated from frehwater anaerobic sediments
    • Broers C.A.M., Stumm C.K., Vogels G.D., Brugerolle G. Psalteriomonas lanterna gen. nov., sp. nov., a free-living amoeboflagellate isolated from frehwater anaerobic sediments. Eur. J. Protistol. 25:1990;369-380.
    • (1990) Eur. J. Protistol. , vol.25 , pp. 369-380
    • Broers, C.A.M.1    Stumm, C.K.2    Vogels, G.D.3    Brugerolle, G.4
  • 3
    • 0025919193 scopus 로고
    • The biology of free-living anaerobic ciliates
    • Fenchel T., Finlay B.J. The biology of free-living anaerobic ciliates. Eur. J. Protistol. 38:1991;18-22.
    • (1991) Eur. J. Protistol. , vol.38 , pp. 18-22
    • Fenchel, T.1    Finlay, B.J.2
  • 4
    • 0000680563 scopus 로고
    • Hydrogenosomes in some anaerobic protozoa resemble mitochondria
    • Finlay B.J., Fenchel T. Hydrogenosomes in some anaerobic protozoa resemble mitochondria. FEMS Microbiol. Lett. 65:1989;311-314.
    • (1989) FEMS Microbiol. Lett. , vol.65 , pp. 311-314
    • Finlay, B.J.1    Fenchel, T.2
  • 6
    • 0025012424 scopus 로고
    • Hydrogenosomes in the rumen entodiniomorphid ciliate Polyplastron multivesiculatum
    • Paul R.G., Williams A.G., Butler R.D. Hydrogenosomes in the rumen entodiniomorphid ciliate Polyplastron multivesiculatum. J. Gen. Microbiol. 136:1990;1981-1989.
    • (1990) J. Gen. Microbiol. , vol.136 , pp. 1981-1989
    • Paul, R.G.1    Williams, A.G.2    Butler, R.D.3
  • 7
    • 0002581623 scopus 로고
    • Occurence of hydrogenosomes in the rumen ciliates Ophryoscolecidae
    • Snyers L., Hellings P., Bovy-Kesler C., Thines-Sempoux D. Occurence of hydrogenosomes in the rumen ciliates Ophryoscolecidae. FEBS Lett. 137:1982;35-39.
    • (1982) FEBS Lett. , vol.137 , pp. 35-39
    • Snyers, L.1    Hellings, P.2    Bovy-Kesler, C.3    Thines-Sempoux, D.4
  • 8
    • 0002252496 scopus 로고
    • Symbiosis of methanogenic bacteria and sapropelic protozoa
    • van Bruggen J.J.A., Stumm C.K., Vogels G.D. Symbiosis of methanogenic bacteria and sapropelic protozoa. Arch. Microbiol. 136:1983;89-95.
    • (1983) Arch. Microbiol. , vol.136 , pp. 89-95
    • Van Bruggen, J.J.A.1    Stumm, C.K.2    Vogels, G.D.3
  • 9
    • 0019882129 scopus 로고
    • Hydrogenosomes in the rumen protozoon Dasytricha ruminantium Schuberg
    • Yarlett N., Hann A.C., Lloyd D., Williams A. Hydrogenosomes in the rumen protozoon Dasytricha ruminantium Schuberg. Biochem. J. 200:1981;365-372.
    • (1981) Biochem. J. , vol.200 , pp. 365-372
    • Yarlett, N.1    Hann, A.C.2    Lloyd, D.3    Williams, A.4
  • 10
    • 0020673755 scopus 로고
    • Hydrogenosomes in a mixed isolate of Isotricha prostoma and Isotricha intestinalis from ovine rumen contents
    • Yarlett N., Hann A.C., Lloyd D., Williams A.G. Hydrogenosomes in a mixed isolate of Isotricha prostoma and Isotricha intestinalis from ovine rumen contents. Comp. Biochem. Physiol. B. 74:1983;357-364.
    • (1983) Comp. Biochem. Physiol. B , vol.74 , pp. 357-364
    • Yarlett, N.1    Hann, A.C.2    Lloyd, D.3    Williams, A.G.4
  • 12
    • 0015731174 scopus 로고
    • Hydrogenosome, a cytoplasmic organelle of the anaerobic flagellate Tritrichomonas foetus, and its role in pyruvate metabolism
    • Lindmark D.G., Müller M. Hydrogenosome, a cytoplasmic organelle of the anaerobic flagellate Tritrichomonas foetus, and its role in pyruvate metabolism. J. Biol. Chem. 248:1973;7724-7728.
    • (1973) J. Biol. Chem. , vol.248 , pp. 7724-7728
    • Lindmark, D.G.1    Müller, M.2
  • 13
    • 0020758818 scopus 로고
    • Fine structure and cytochemistry of the hydrogenosome of Tritrichomonas foetus
    • Benchimol M., De Souza W. Fine structure and cytochemistry of the hydrogenosome of Tritrichomonas foetus. J. Protozool. 30:1983;422-425.
    • (1983) J. Protozool. , vol.30 , pp. 422-425
    • Benchimol, M.1    De Souza, W.2
  • 14
    • 0008479231 scopus 로고
    • Cell biology of trichomonads: Protein targeting to the hydrogenosome
    • J.C. Boothroyd, & R. Komuniecki. New York: Wiley-Liss
    • Johnson P.J., Bradley P.J., Lahti C.J. Cell biology of trichomonads: protein targeting to the hydrogenosome. Boothroyd J.C., Komuniecki R. Molecular Approaches to Parasitology. 1995;399-411 Wiley-Liss, New York.
    • (1995) Molecular Approaches to Parasitology , pp. 399-411
    • Johnson, P.J.1    Bradley, P.J.2    Lahti, C.J.3
  • 15
    • 0020663483 scopus 로고
    • Failure to detect extrachromosomal DNA in Trichomonas vaginalis and Tritrichomonas foetus
    • Turner G., Müller M. Failure to detect extrachromosomal DNA in Trichomonas vaginalis and Tritrichomonas foetus. J. Parasitol. 69:1983;234-236.
    • (1983) J. Parasitol. , vol.69 , pp. 234-236
    • Turner, G.1    Müller, M.2
  • 16
    • 0023073536 scopus 로고
    • The simultaneous symbiotic origin of mitochondria, chloroplasts, and microbodies
    • Cavalier-Smith T. The simultaneous symbiotic origin of mitochondria, chloroplasts, and microbodies. Ann. N. Y. Acad. Sci. 503:1987;55-71.
    • (1987) Ann. N. Y. Acad. Sci. , vol.503 , pp. 55-71
    • Cavalier-Smith, T.1
  • 17
    • 0029817685 scopus 로고    scopus 로고
    • A common evolutionary origin for mitochondria and hydrogenosomes
    • Bui E.T., Bradley P.J., Johnson P.J. A common evolutionary origin for mitochondria and hydrogenosomes. Proc. Natl. Acad. Sci. USA. 18:1996;9651-9656.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.18 , pp. 9651-9656
    • Bui, E.T.1    Bradley, P.J.2    Johnson, P.J.3
  • 18
    • 0029963676 scopus 로고    scopus 로고
    • Presence of a mitochondrial-type 70-kDa heat shock protein in Trichomonas vaginalis suggests a very early mitochondrial endosymbiosis in eukaryotes
    • Germot A., Philippe H., Le Guyader H. Presence of a mitochondrial-type 70-kDa heat shock protein in Trichomonas vaginalis suggests a very early mitochondrial endosymbiosis in eukaryotes. Proc. Natl. Acad. Sci. USA. 93:1996;14614-14617.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 14614-14617
    • Germot, A.1    Philippe, H.2    Le Guyader, H.3
  • 20
    • 0029856340 scopus 로고    scopus 로고
    • A possible mitochondrial gene in the early-branching amitochondriate protist Trichomonas vaginalis
    • Roger A.J., Clark C.G., Doolittle W.F. A possible mitochondrial gene in the early-branching amitochondriate protist Trichomonas vaginalis. Proc. Natl. Acad. Sci. USA. 93:1996;14618-14628.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 14618-14628
    • Roger, A.J.1    Clark, C.G.2    Doolittle, W.F.3
  • 22
    • 0027630346 scopus 로고
    • Phylogeny of trichomonads based on partial sequences of large subunit rRNA and on cladistic analysis of morphological data
    • Viscogliosi E., Philippe H., Baroin A., Perasso R., Brugerolle G. Phylogeny of trichomonads based on partial sequences of large subunit rRNA and on cladistic analysis of morphological data. J. Eukaryot. Microbiol. 40:1993;411-421.
    • (1993) J. Eukaryot. Microbiol. , vol.40 , pp. 411-421
    • Viscogliosi, E.1    Philippe, H.2    Baroin, A.3    Perasso, R.4    Brugerolle, G.5
  • 23
    • 0027365367 scopus 로고
    • Biogenesis of the hydrogenosome in the anaerobic protist Trichomonas vaginalis
    • Johnson P.J., Lahti C.J., Bradley P.J. Biogenesis of the hydrogenosome in the anaerobic protist Trichomonas vaginalis. J. Parasitol. 79:1993;664-670.
    • (1993) J. Parasitol. , vol.79 , pp. 664-670
    • Johnson, P.J.1    Lahti, C.J.2    Bradley, P.J.3
  • 24
    • 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. USA. 92:1995;6518-6521.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 6518-6521
    • Clark, C.G.1    Roger, A.J.2
  • 25
    • 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. USA. 95:1998;229-234.
    • (1998) Proc. Natl. Acad. Sci. USA , 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
  • 26
    • 2642689666 scopus 로고    scopus 로고
    • The hydrogen hypothesis for the first eukaryote
    • Martin W., Müller M. The hydrogen hypothesis for the first eukaryote. Nature. 392:1998;37-41.
    • (1998) Nature , vol.392 , pp. 37-41
    • Martin, W.1    Müller, M.2
  • 27
    • 0025873038 scopus 로고
    • Trichomonas vaginalis hydrogenosomal proteins are synthesized on free polyribosomes and may undergo processing upon maturation
    • Lahti C.J., Johnson P.J. Trichomonas vaginalis hydrogenosomal proteins are synthesized on free polyribosomes and may undergo processing upon maturation. Mol. Biochem. Parasitol. 46:1991;307-310.
    • (1991) Mol. Biochem. Parasitol. , vol.46 , pp. 307-310
    • Lahti, C.J.1    Johnson, P.J.2
  • 28
    • 0028168012 scopus 로고
    • Molecular characterization of the alpha-subunit of Trichomonas vaginalis hydrogenosomal succinyl CoA synthetase
    • Lahti C.J., Bradley P.J., Johnson P.J. Molecular characterization of the alpha-subunit of Trichomonas vaginalis hydrogenosomal succinyl CoA synthetase. Mol. Biochem. Parasitol. 66:1994;309-318.
    • (1994) Mol. Biochem. Parasitol. , vol.66 , pp. 309-318
    • Lahti, C.J.1    Bradley, P.J.2    Johnson, P.J.3
  • 29
    • 0028132843 scopus 로고
    • Primary structure of the hydrogenosomal adenylate kinase of Trichomonas vaginalis and its phylogenetic relationships
    • Lange S., Rozario C., Müller M. Primary structure of the hydrogenosomal adenylate kinase of Trichomonas vaginalis and its phylogenetic relationships. Mol. Biochem. Parasitol. 66:1994;297-308.
    • (1994) Mol. Biochem. Parasitol. , vol.66 , pp. 297-308
    • Lange, S.1    Rozario, C.2    Müller, M.3
  • 30
    • 0026641622 scopus 로고
    • Beta-succinyl-coenzyme A synthetase from Trichomonas vaginalis is a soluble hydrogenosomal protein with an amino-terminal sequence that resembles mitochondrial presequences
    • Lahti C.J., d'Oliveira C.E., Johnson P.J. Beta-succinyl-coenzyme A synthetase from Trichomonas vaginalis is a soluble hydrogenosomal protein with an amino-terminal sequence that resembles mitochondrial presequences. J. Bacteriol. 174:1992;6822-6830.
    • (1992) J. Bacteriol. , vol.174 , pp. 6822-6830
    • Lahti, C.J.1    D'Oliveira, C.E.2    Johnson, P.J.3
  • 31
    • 0025180595 scopus 로고
    • Molecular analysis of the hydrogenosomal ferredoxin of the anaerobic protist Trichomonas vaginalis
    • Johnson P.J., d'Oliveira C.E., Gorrell T.E., Müller M. Molecular analysis of the hydrogenosomal ferredoxin of the anaerobic protist Trichomonas vaginalis. Proc. Natl. Acad. Sci. USA. 87:1990;6097-6101.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 6097-6101
    • Johnson, P.J.1    D'Oliveira, C.E.2    Gorrell, T.E.3    Müller, M.4
  • 32
    • 0029372609 scopus 로고
    • Primary structure of the hydrogenosomal malic enzyme of Trichomonas vaginalis and its relationship to homologous enzymes
    • Hrdy I., Müller M. Primary structure of the hydrogenosomal malic enzyme of Trichomonas vaginalis and its relationship to homologous enzymes. J. Eukaryot. Microbiol. 42:1995;593-603.
    • (1995) J. Eukaryot. Microbiol. , vol.42 , pp. 593-603
    • Hrdy, I.1    Müller, M.2
  • 33
    • 0028874227 scopus 로고
    • Primary structure and eubacterial relationships of the pyruvate:ferredoxin oxidoreductase of the amitochondriate eukaryote Trichomonas vaginalis
    • Hrdy I., Müller M. Primary structure and eubacterial relationships of the pyruvate:ferredoxin oxidoreductase of the amitochondriate eukaryote Trichomonas vaginalis. J. Mol. Evol. 41:1995;388-396.
    • (1995) J. Mol. Evol. , vol.41 , pp. 388-396
    • Hrdy, I.1    Müller, M.2
  • 34
    • 0031010331 scopus 로고    scopus 로고
    • Targeting and translocation of proteins into the hydrogenosome of the protist Trichomonas: Similarities with mitochondrial protein import
    • Bradley P.J., Lahti C.J., Plümper E., Johnson P.J. Targeting and translocation of proteins into the hydrogenosome of the protist Trichomonas: similarities with mitochondrial protein import. EMBO J. 16:1997;3484-3493.
    • (1997) EMBO J. , vol.16 , pp. 3484-3493
    • Bradley, P.J.1    Lahti, C.J.2    Plümper, E.3    Johnson, P.J.4
  • 35
    • 0030969942 scopus 로고    scopus 로고
    • Protein import into mitochondria
    • Neupert W. Protein import into mitochondria. Annu. Rev. Biochem. 66:1997;863-917.
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 863-917
    • Neupert, W.1
  • 36
    • 0031106617 scopus 로고    scopus 로고
    • Import of proteins into mitochondria and chloroplasts
    • Haucke V., Schatz G. Import of proteins into mitochondria and chloroplasts. Trends Cell Biol. 7:1997;103-106.
    • (1997) Trends Cell Biol. , vol.7 , pp. 103-106
    • Haucke, V.1    Schatz, G.2
  • 38
    • 77049313195 scopus 로고
    • Acetylornithinase of Escherichia coli: Partial purification and some properties
    • Vogel H.J., Bonner D.M. Acetylornithinase of Escherichia coli: partial purification and some properties. J. Biol. Chem. 218:1956;97-106.
    • (1956) J. Biol. Chem. , vol.218 , pp. 97-106
    • Vogel, H.J.1    Bonner, D.M.2
  • 39
    • 0025975314 scopus 로고
    • Analysis of mitochondrial function and assembly
    • Yaffe M.P. Analysis of mitochondrial function and assembly. Methods Enzymol. 194:1991;627-643.
    • (1991) Methods Enzymol. , vol.194 , pp. 627-643
    • Yaffe, M.P.1
  • 40
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 41
    • 0020039866 scopus 로고
    • Isolation of intracellular membranes by means of sodium carbonate treatment: Application to endoplasmic reticulum
    • Fujiki Y., Hubbard A.L., Fowler S., Lazarow P.B. Isolation of intracellular membranes by means of sodium carbonate treatment: application to endoplasmic reticulum. J. Cell Biol. 93:1982;97-102.
    • (1982) J. Cell Biol. , vol.93 , pp. 97-102
    • Fujiki, Y.1    Hubbard, A.L.2    Fowler, S.3    Lazarow, P.B.4
  • 42
    • 0025748733 scopus 로고
    • Early events in the transport of proteins into mitochondria. Import competition by a mitochondrial presequence
    • Cyr D.M., Douglas M.G. Early events in the transport of proteins into mitochondria. Import competition by a mitochondrial presequence. J. Biol. Chem. 266:1991;21700-21708.
    • (1991) J. Biol. Chem. , vol.266 , pp. 21700-21708
    • Cyr, D.M.1    Douglas, M.G.2
  • 43
    • 0025277370 scopus 로고
    • A synthetic presequence reversibly inhibits protein import into yeast mitochondria
    • Glaser S.M., Cumsky M.G. A synthetic presequence reversibly inhibits protein import into yeast mitochondria. J. Biol. Chem. 265:1990;8808-8816.
    • (1990) J. Biol. Chem. , vol.265 , pp. 8808-8816
    • Glaser, S.M.1    Cumsky, M.G.2
  • 44
    • 0022353969 scopus 로고
    • A synthetic signal peptide blocks import of precursor proteins destined for the mitochondrial inner membrane or matrix
    • Gillespie L.L., Argan C., Taneja A.T., Hodges R.S., Freeman K.B., Shore G.C. A synthetic signal peptide blocks import of precursor proteins destined for the mitochondrial inner membrane or matrix. J. Biol. Chem. 260:1985;16045-16048.
    • (1985) J. Biol. Chem. , vol.260 , pp. 16045-16048
    • Gillespie, L.L.1    Argan, C.2    Taneja, A.T.3    Hodges, R.S.4    Freeman, K.B.5    Shore, G.C.6
  • 45
    • 0026075507 scopus 로고
    • Synthetic analogues of a transit peptide inhibit binding or translocation of chloroplastic precursor proteins
    • Perry S.E., Buvinger W.E., Bennett J., Keegstra K. Synthetic analogues of a transit peptide inhibit binding or translocation of chloroplastic precursor proteins. J. Biol. Chem. 266:1991;11882-11889.
    • (1991) J. Biol. Chem. , vol.266 , pp. 11882-11889
    • Perry, S.E.1    Buvinger, W.E.2    Bennett, J.3    Keegstra, K.4
  • 46
    • 0025805676 scopus 로고
    • Signal peptide analogs derived from two chloroplast precursors interact with the signal recognition system of the chloroplast envelope
    • Schnell D.J., Blobel G., Pain D. Signal peptide analogs derived from two chloroplast precursors interact with the signal recognition system of the chloroplast envelope. J. Biol. Chem. 266:1991;3335-3342.
    • (1991) J. Biol. Chem. , vol.266 , pp. 3335-3342
    • Schnell, D.J.1    Blobel, G.2    Pain, D.3
  • 47
    • 0025732835 scopus 로고
    • Cytosolic and mitochondrial surface factor-independent import of a synthetic peptide into mitochondria
    • Furuya S., Mihara K., Aimoto S., Omura T. Cytosolic and mitochondrial surface factor-independent import of a synthetic peptide into mitochondria. EMBO J. 10:1991;1759-1766.
    • (1991) EMBO J. , vol.10 , pp. 1759-1766
    • Furuya, S.1    Mihara, K.2    Aimoto, S.3    Omura, T.4
  • 48
    • 0025150997 scopus 로고
    • Import of chemically synthesized signal peptides into rat liver mitochondria
    • Pak Y.K., Weiner H. Import of chemically synthesized signal peptides into rat liver mitochondria. J. Biol. Chem. 265:1990;14298-14307.
    • (1990) J. Biol. Chem. , vol.265 , pp. 14298-14307
    • Pak, Y.K.1    Weiner, H.2
  • 49
    • 0000262786 scopus 로고
    • Chloroplast protein import: Quantitative analysis of receptor mediated binding
    • Friedman A.L., Keegstra K. Chloroplast protein import: quantitative analysis of receptor mediated binding. Plant Physiol. 89:1989;993-999.
    • (1989) Plant Physiol. , vol.89 , pp. 993-999
    • Friedman, A.L.1    Keegstra, K.2
  • 50
    • 0020479718 scopus 로고
    • Import of proteins into mitochondria. Energy-dependent uptake of precursors by isolated mitochondria
    • Gasser S.M., Daum G., Schatz G. Import of proteins into mitochondria. Energy-dependent uptake of precursors by isolated mitochondria. J. Biol. Chem. 257:1982;13034-13041.
    • (1982) J. Biol. Chem. , vol.257 , pp. 13034-13041
    • Gasser, S.M.1    Daum, G.2    Schatz, G.3
  • 51
    • 0022431959 scopus 로고
    • Precursors to two nuclear-encoded chloroplast proteins bind to the outer envelope membrane before being imported into chloroplasts
    • Cline K., Werner-Washburne M., Lubben T.H., Keegstra K. Precursors to two nuclear-encoded chloroplast proteins bind to the outer envelope membrane before being imported into chloroplasts. J. Biol. Chem. 260:1985;3691-3696.
    • (1985) J. Biol. Chem. , vol.260 , pp. 3691-3696
    • Cline, K.1    Werner-Washburne, M.2    Lubben, T.H.3    Keegstra, K.4
  • 52
    • 0023371689 scopus 로고
    • Protein import into yeast mitochondria is inhibited by antibodies raised against 45-kDa proteins of the outer membrane
    • Ohba M., Schatz G. Protein import into yeast mitochondria is inhibited by antibodies raised against 45-kDa proteins of the outer membrane. EMBO J. 6:1987;2109-2115.
    • (1987) EMBO J. , vol.6 , pp. 2109-2115
    • Ohba, M.1    Schatz, G.2
  • 53
    • 0021275344 scopus 로고
    • Proteinaceous receptors for the import of mitochondrial precursor proteins
    • Zwizinski C., Schleyer M., Neupert W. Proteinaceous receptors for the import of mitochondrial precursor proteins. J. Biol. Chem. 259:1984;7850-7856.
    • (1984) J. Biol. Chem. , vol.259 , pp. 7850-7856
    • Zwizinski, C.1    Schleyer, M.2    Neupert, W.3
  • 54
    • 0027477738 scopus 로고
    • Insertion of MOM22 into mitochondrial outer membrane strictly depends on surface receptors
    • Keil P., Pfanner N. Insertion of MOM22 into mitochondrial outer membrane strictly depends on surface receptors. FEBS Lett. 321:1993;197-200.
    • (1993) FEBS Lett. , vol.321 , pp. 197-200
    • Keil, P.1    Pfanner, N.2
  • 55
    • 0024558880 scopus 로고
    • Mitochondrial protein import: Bypass of proteinaceous surface receptors can occur with low specificity and efficiency
    • Pfaller R., Pfanner N., Neupert W. Mitochondrial protein import: bypass of proteinaceous surface receptors can occur with low specificity and efficiency. J. Biol. Chem. 264:1989;34-39.
    • (1989) J. Biol. Chem. , vol.264 , pp. 34-39
    • Pfaller, R.1    Pfanner, N.2    Neupert, W.3
  • 56
    • 0029774146 scopus 로고    scopus 로고
    • The protein import system of mitochondria
    • Schatz G. The protein import system of mitochondria. J. Biol. Chem. 271:1996;31763-31766.
    • (1996) J. Biol. Chem. , vol.271 , pp. 31763-31766
    • Schatz, G.1


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