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Volumn 12, Issue 6, 1998, Pages 495-502

Double-stranded DNA can be translocated across a planar membrane containing purified mitochondrial porin

Author keywords

Channels; DNA transport; Mitochondria; VDAC

Indexed keywords

ANION CHANNEL; BACTERIAL PROTEIN; DOUBLE STRANDED DNA; GRAMICIDIN A; PORIN; PROTEIN ANTIBODY;

EID: 2642694705     PISSN: 08926638     EISSN: None     Source Type: Journal    
DOI: 10.1096/fasebj.12.6.495     Document Type: Article
Times cited : (57)

References (57)
  • 1
    • 0025854858 scopus 로고
    • A protein-conducting channel in the endoplasmic reticulum
    • Simon, S. M., and Blobel, G. (1991) A protein-conducting channel in the endoplasmic reticulum. Cell 65, 371-380
    • (1991) Cell , vol.65 , pp. 371-380
    • Simon, S.M.1    Blobel, G.2
  • 2
    • 0029047327 scopus 로고
    • The ion channel behavior of the nuclear pore complex
    • Bustamante, J. O., Hanover, J. A., and Liepins, A. (1995) The ion channel behavior of the nuclear pore complex. J. Membr. Biol. 146, 239-251
    • (1995) J. Membr. Biol. , vol.146 , pp. 239-251
    • Bustamante, J.O.1    Hanover, J.A.2    Liepins, A.3
  • 3
    • 0027938423 scopus 로고
    • Translocation of DNA across bacterial membranes
    • Dreiseikelmann, B. (1994) Translocation of DNA across bacterial membranes. Microbiol. Rev. 58, 293-316
    • (1994) Microbiol. Rev. , vol.58 , pp. 293-316
    • Dreiseikelmann, B.1
  • 4
    • 0030771374 scopus 로고    scopus 로고
    • DNA translocation across planar bilayers containing Bacillus subtilision channels
    • Szabò, I., Bàthori, G., Tombola, F., Brini, M., Coppola, A., and Zoratti, M. (1997) DNA translocation across planar bilayers containing Bacillus subtilision channels. J. Biol. Chem. 272, 25275-25282
    • (1997) J. Biol. Chem. , vol.272 , pp. 25275-25282
    • Szabò, I.1    Bàthori, G.2    Tombola, F.3    Brini, M.4    Coppola, A.5    Zoratti, M.6
  • 5
    • 0029914253 scopus 로고    scopus 로고
    • FhuA, a transporter of the Escherichia coli outer membrane, is converted into a channel upon binding of bacteriophage T5
    • Bonhivers, M., Ghazi, A., Boulanger, P., and Letellier, L. (1996) FhuA, a transporter of the Escherichia coli outer membrane, is converted into a channel upon binding of bacteriophage T5. EMBO J. 15, 1850-1856
    • (1996) EMBO J , vol.15 , pp. 1850-1856
    • Bonhivers, M.1    Ghazi, A.2    Boulanger, P.3    Letellier, L.4
  • 6
    • 0025009142 scopus 로고
    • Pore formation associated with the tail-tip protein pb2 of bacteriophage T5
    • Feucht, A., Schmidt, A., Benz, R., Schwarz, H., and Heller, K. J. (1990) Pore formation associated with the tail-tip protein pb2 of bacteriophage T5. J. Biol. Chem. 265, 18561-18567
    • (1990) J. Biol. Chem. , vol.265 , pp. 18561-18567
    • Feucht, A.1    Schmidt, A.2    Benz, R.3    Schwarz, H.4    Heller, K.J.5
  • 7
    • 0026726725 scopus 로고
    • Involvement of phage T5 tail proteins and contact sites between the outer and inner membrane of Escherichia coli in phage T5 DNA injection
    • Guihard, G., Boulanger, P., and Letellier, L. (1992) Involvement of phage T5 tail proteins and contact sites between the outer and inner membrane of Escherichia coli in phage T5 DNA injection. J. Biol. Chem. 267, 3173-3178
    • (1992) J. Biol. Chem. , vol.267 , pp. 3173-3178
    • Guihard, G.1    Boulanger, P.2    Letellier, L.3
  • 8
    • 0024414757 scopus 로고
    • Poreforming properties of the adsorption protein of filamentous phage fd
    • Glaser-Wuttke, G., Keppner, J., and Rasched, I. (1989) Poreforming properties of the adsorption protein of filamentous phage fd. Biochim. Biophys. Acta 985, 239-247
    • (1989) Biochim. Biophys. Acta , vol.985 , pp. 239-247
    • Glaser-Wuttke, G.1    Keppner, J.2    Rasched, I.3
  • 9
    • 0027455152 scopus 로고
    • Transport of nucleic acids through membrane channels: Snaking through small holes
    • Citovsky, V., and Zambryski, P. (1993) Transport of nucleic acids through membrane channels: snaking through small holes. Annu. Rev. Microbiol. 47, 167-197
    • (1993) Annu. Rev. Microbiol. , vol.47 , pp. 167-197
    • Citovsky, V.1    Zambryski, P.2
  • 10
    • 0030465241 scopus 로고    scopus 로고
    • Characterization of individual polynucleotide molecules using a membrane channel
    • Kasianowicz, J. J., Brandin, F., Branton, D., and Deamer, D. W. (1996) Characterization of individual polynucleotide molecules using a membrane channel Proc. Natl. Acad. Sci. USA 93, 13770-13773
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 13770-13773
    • Kasianowicz, J.J.1    Brandin, F.2    Branton, D.3    Deamer, D.W.4
  • 11
    • 0018277518 scopus 로고
    • Origins of prokaryotes, eukaryotes, mitochondria and chloroplasts
    • Schwartz, R. M., and Dayhoff, M. O. (1978) Origins of prokaryotes, eukaryotes, mitochondria and chloroplasts. Science 199, 395-403
    • (1978) Science , vol.199 , pp. 395-403
    • Schwartz, R.M.1    Dayhoff, M.O.2
  • 13
    • 0026563681 scopus 로고
    • In vivo import of a normal or mutagenized heterologous transfer RNA into the mitochondria of transgenic plants: Towards a way of influencing mitochondrial gene expression?
    • Small, I., Maréchal-Drouard, L., Masson, J., Pelletier, G., Cosset, A., Weil, J. H., and Dietrich, A. (1992) In vivo import of a normal or mutagenized heterologous transfer RNA into the mitochondria of transgenic plants: towards a way of influencing mitochondrial gene expression? EMBO J. 11, 1291-1296
    • (1992) EMBO J , vol.11 , pp. 1291-1296
    • Small, I.1    Maréchal-Drouard, L.2    Masson, J.3    Pelletier, G.4    Cosset, A.5    Weil, J.H.6    Dietrich, A.7
  • 14
    • 0029155450 scopus 로고
    • TRNAs are imported into mitochondria of Trypanosoma bmcei independently of their genomic context and genetic origin
    • Hauser, R., and Schneider, A. (1995) tRNAs are imported into mitochondria of Trypanosoma bmcei independently of their genomic context and genetic origin. EMBO J. 14, 4212-4220
    • (1995) EMBO J , vol.14 , pp. 4212-4220
    • Hauser, R.1    Schneider, A.2
  • 15
    • 0029017974 scopus 로고
    • Mitochondrial import of cytoplasmic lysine-tRNA in yeast is mediated by cooperation of cytoplasmic and mitochondrial lysyl-tRNA synthetases
    • Tarassov, I., Entelis, N., and Martin, R. P. (1995) Mitochondrial import of cytoplasmic lysine-tRNA in yeast is mediated by cooperation of cytoplasmic and mitochondrial lysyl-tRNA synthetases. EMBOJ. 14, 3461-3471
    • (1995) EMBOJ , vol.14 , pp. 3461-3471
    • Tarassov, I.1    Entelis, N.2    Martin, R.P.3
  • 16
    • 0028929930 scopus 로고
    • An intact protein translocation machinery is required for mitochondrial import of a yeast cytoplasmic tRNA
    • Tarassov, I. A., Entelis, N. S., and Martin, R. P. (1995) An intact protein translocation machinery is required for mitochondrial import of a yeast cytoplasmic tRNA. J. Mol. Biol. 245, 315-323
    • (1995) J. Mol. Biol. , vol.245 , pp. 315-323
    • Tarassov, I.A.1    Entelis, N.S.2    Martin, R.P.3
  • 18
    • 0024536726 scopus 로고
    • DNA-protein conjugates can enter mitochondria via the protein import pathway
    • Vestweber, D., and Schatz, G. (1989) DNA-protein conjugates can enter mitochondria via the protein import pathway. Nature (London) 338, 170-172
    • (1989) Nature (London) , vol.338 , pp. 170-172
    • Vestweber, D.1    Schatz, G.2
  • 19
    • 0028804570 scopus 로고
    • Transfection of mitochondria: Strategy towards a gene therapy of mitochondrial DNA diseases
    • Seibel, P., Trappe, J., Villani, G., Klopstock, T., Papa, S., and Reichmann, H. (1995) Transfection of mitochondria: strategy towards a gene therapy of mitochondrial DNA diseases. Nucleic Acids Res. 23, 10-17
    • (1995) Nucleic Acids Res , vol.23 , pp. 10-17
    • Seibel, P.1    Trappe, J.2    Villani, G.3    Klopstock, T.4    Papa, S.5    Reichmann, H.6
  • 20
    • 0028341536 scopus 로고
    • Permeation of hydrophilic solutes through mitochondrial outer membranes: Review on mitochondrial porins
    • Benz, R. (1994) Permeation of hydrophilic solutes through mitochondrial outer membranes: review on mitochondrial porins. Biochim. Biophys. Acta 1197, 167-196
    • (1994) Biochim. Biophys. Acta , vol.1197 , pp. 167-196
    • Benz, R.1
  • 21
    • 79959414421 scopus 로고
    • Anion channels in the mitochondrial outer membrane
    • Colombini, M. (1994) Anion channels in the mitochondrial outer membrane. Curr. Top. Membr. 42, 73-101
    • (1994) Curr. Top. Membr. , vol.42 , pp. 73-101
    • Colombini, M.1
  • 22
    • 0029685882 scopus 로고    scopus 로고
    • VDAC, a channel in the outer mitochondrial membrane
    • Narahashi, T., ed, Plenum Press, New York
    • Colombini, M., Blachly-Dyson, E., and Forte, M. (1996) VDAC, a channel in the outer mitochondrial membrane. In Ion Channels (Narahashi, T., ed) Vol. 4., pp. 169-202, Plenum Press, New York
    • (1996) Ion Channels , vol.4 , pp. 169-202
    • Colombini, M.1    Blachly-Dyson, E.2    Forte, M.3
  • 23
    • 0026538575 scopus 로고
    • Toward the molecular structure of the mitochondrial channel, VDAC
    • Mannella, C. A., Forte, M., and Colombini, M. (1992) Toward the molecular structure of the mitochondrial channel, VDAC. J. Bioenerg. Biomembr. 24, 7-19
    • (1992) J. Bioenerg. Biomembr. , vol.24 , pp. 7-19
    • Mannella, C.A.1    Forte, M.2    Colombini, M.3
  • 24
    • 0026079408 scopus 로고
    • Contact sites between mitochondrial envelope membranes. Structure and function in energy- and proteintransfer
    • Brdiczka, D. (1991) Contact sites between mitochondrial envelope membranes. Structure and function in energy- and proteintransfer. Biochim. Biophys. Acta 1071, 291-312
    • (1991) Biochim. Biophys. Acta , vol.1071 , pp. 291-312
    • Brdiczka, D.1
  • 25
    • 0026591024 scopus 로고
    • Isolation of the mitochondrial benzodiazepine receptor: Association with the voltage-dependent anion channel and the adenine nucleotide carrier
    • McEnery, M. W., Snowman, A. M., Trifiletti, R. R., and Snyder, S. H. (1991) Isolation of the mitochondrial benzodiazepine receptor: association with the voltage-dependent anion channel and the adenine nucleotide carrier. Proc. Natl. Acad. Sci. USA 89, 3170-3174
    • (1991) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 3170-3174
    • McEnery, M.W.1    Snowman, A.M.2    Trifiletti, R.R.3    Snyder, S.H.4
  • 26
    • 0028091583 scopus 로고
    • Electrophysiology of the inner mitochondrial membrane
    • Zoratti, M., and Szabo, I. (1994) Electrophysiology of the inner mitochondrial membrane. J. Bioenerg. Biomembr. 26, 543-553
    • (1994) J. Bioenerg. Biomembr. , vol.26 , pp. 543-553
    • Zoratti, M.1    Szabo, I.2
  • 27
    • 0030947935 scopus 로고    scopus 로고
    • VDAC channels mediate and gate the flow of ATP: Implications for the regulation of mitochondrial function
    • Rostovtseva, T., and Colombini, M. (1997) VDAC channels mediate and gate the flow of ATP: implications for the regulation of mitochondrial function. Biophys. J. 72, 1954-1962
    • (1997) Biophys. J. , vol.72 , pp. 1954-1962
    • Rostovtseva, T.1    Colombini, M.2
  • 28
    • 0026555536 scopus 로고
    • Evidence for extramitochondrial localization of VDAC/porin channel in eukaryotic cells
    • Thinnes, F. P. (1992) Evidence for extramitochondrial localization of VDAC/porin channel in eukaryotic cells. J. Bioenerg. Biomembr. 24, 71-75
    • (1992) J. Bioenerg. Biomembr. , vol.24 , pp. 71-75
    • Thinnes, F.P.1
  • 30
    • 0028324788 scopus 로고
    • Electron micrographic studies of transport of oligodeoxynucletides across eukaryotic cell membranes
    • Zamecnik, P., Aghajanian, J., Zamecnik, M., Goodchild, J., and Witman, G. (1994) Electron micrographic studies of transport of oligodeoxynucletides across eukaryotic cell membranes. Proc. Natl. Acad. Sci. USA 91, 3156-3160
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 3156-3160
    • Zamecnik, P.1    Aghajanian, J.2    Zamecnik, M.3    Goodchild, J.4    Witman, G.5
  • 31
    • 0023651581 scopus 로고
    • A simple and rapid method for the purification of the mitochondrial porin from mammalian tissues
    • De Pinto, V., Prezioso, G., and Palmieri, F. (1987) A simple and rapid method for the purification of the mitochondrial porin from mammalian tissues. Biochim. Biophys. Acta 905, 499-502
    • (1987) Biochim. Biophys. Acta , vol.905 , pp. 499-502
    • De Pinto, V.1    Prezioso, G.2    Palmieri, F.3
  • 32
    • 0024347661 scopus 로고
    • Interaction of non-classical detergents with the mitochondrial porin. A new purification procedure and characterization of the pore-forming unit
    • De Pinto, V., Benz, R., and Palmieri, F. (1989) Interaction of non-classical detergents with the mitochondrial porin. A new purification procedure and characterization of the pore-forming unit. Eur. J. Biochem. 183, 179-187
    • (1989) Eur. J. Biochem. , vol.183 , pp. 179-187
    • De Pinto, V.1    Benz, R.2    Palmieri, F.3
  • 33
    • 0025788323 scopus 로고
    • Peptide-specific antibodies and proteases as probes of the transmembrane topography of the bovine heart mitochondrial porin
    • De Pinto, V., Thinnes, F., Link, T., and Palmieri, F. (1991) Peptide-specific antibodies and proteases as probes of the transmembrane topography of the bovine heart mitochondrial porin. Biochemistry 30, 10191-10200
    • (1991) Biochemistry , vol.30 , pp. 10191-10200
    • De Pinto, V.1    Thinnes, F.2    Link, T.3    Palmieri, F.4
  • 34
    • 2642629212 scopus 로고
    • Purification of human immunoglobulins by sequential precipitation with caprylic acid and ammonium sulphate
    • Perosa, F., Carbone, R., Ferrone, S., and Dammaco, F. (1990) Purification of human immunoglobulins by sequential precipitation with caprylic acid and ammonium sulphate. J. Immunol. Methods 74, 385-394
    • (1990) J. Immunol. Methods , vol.74 , pp. 385-394
    • Perosa, F.1    Carbone, R.2    Ferrone, S.3    Dammaco, F.4
  • 35
    • 0017083729 scopus 로고
    • Multiple steps during interaction between coliphage lambda and its receptor protein in vitro
    • Roa, M., and Scandella, D. (1976) Multiple steps during interaction between coliphage lambda and its receptor protein in vitro. Virology 72, 182-194
    • (1976) Virology , vol.72 , pp. 182-194
    • Roa, M.1    Scandella, D.2
  • 36
    • 0025912181 scopus 로고
    • Affinity Chromatographic purification of cysteine-substituted maltoporin variants: Thiol reactivity and cross-linking in an outer membrane protein of E
    • Francis, G., Brennan, L., and Ferenci, T. (1991) Affinity Chromatographic purification of cysteine-substituted maltoporin variants: thiol reactivity and cross-linking in an outer membrane protein of E. coli. Biochim. Biophys. Acta 1067, 89-96
    • (1991) Coli. Biochim. Biophys. Acta , vol.1067 , pp. 89-96
    • Francis, G.1    Brennan, L.2    Ferenci, T.3
  • 37
    • 0028877091 scopus 로고
    • Photoprotein-mediated measurement of calcium ion concentration in mitochondria of living cells
    • Rizzuto, R., Brini, M., Bastianutto, C., Marsault, R., and Pozzan, T. (1995) Photoprotein-mediated measurement of calcium ion concentration in mitochondria of living cells. Methods Enzymol. 260, 417-428
    • (1995) Methods Enzymol , vol.260 , pp. 417-428
    • Rizzuto, R.1    Brini, M.2    Bastianutto, C.3    Marsault, R.4    Pozzan, T.5
  • 39
    • 0002465964 scopus 로고
    • How to set up a bilayer system
    • Miller, C., ed, Plenum Press, New York
    • Alvarez, O. (1986) How to set up a bilayer system. In Ion Channel Reconstitution (Miller, C., ed) pp. 115-130, Plenum Press, New York
    • (1986) Ion Channel Reconstitution , pp. 115-130
    • Alvarez, O.1
  • 40
    • 0028946962 scopus 로고
    • Structural basis for sugar translocation through maltoporin channels at 3.1 Å resolution
    • Schirmer, T., Keller, T. A., Wang, Y.-F., and Rosenbusch, J. P. (1995) Structural basis for sugar translocation through maltoporin channels at 3.1 Å resolution. Science 267, 512-514
    • (1995) Science , vol.267 , pp. 512-514
    • Schirmer, T.1    Keller, T.A.2    Wang, Y.-F.3    Rosenbusch, J.P.4
  • 41
    • 0031557404 scopus 로고    scopus 로고
    • Structure of maltoporin from Salmonella typhimurium ligated with a nitrophenyl maltotrioside
    • Meyer, J. E. W., Hofnung, M., and Schulz, G. E. (1997) Structure of maltoporin from Salmonella typhimurium ligated with a nitrophenyl maltotrioside J. Mol. Biol. 266, 761-775
    • (1997) J. Mol. Biol. , vol.266 , pp. 761-775
    • Meyer, J.E.W.1    Hofnung, M.2    Schulz, G.E.3
  • 43
    • 0026872512 scopus 로고
    • Studies on human porin. VII. The channel properties of the human B-lymphocyte membrane-derived 'porin 31 HL' are similar to those of mitochondrial porin
    • Benz, R., Maier, E., Thinnes, F. P., Gotz, H., and Hilschmann, N. (1992) studies on human porin. VII. The channel properties of the human B-lymphocyte membrane-derived 'porin 31 HL' are similar to those of mitochondrial porin. Biol. Chem. Hoppe-Seyler 373, 295-303
    • (1992) Biol. Chem. Hoppe-Seyler , vol.373 , pp. 295-303
    • Benz, R.1    Maier, E.2    Thinnes, F.P.3    Gotz, H.4    Hilschmann, N.5
  • 44
    • 0030447720 scopus 로고    scopus 로고
    • Structure of staphylococcal alpha-hemolysin, a heptameric transmembrane pore
    • Song, L. Z., Hobaugh, M. R., Shustak, C., Cheley, S., Bayley, H., and Gouaux, J. E. (1996) Structure of staphylococcal alpha-hemolysin, a heptameric transmembrane pore. Science 274, 1859-1866
    • (1996) Science , vol.274 , pp. 1859-1866
    • Song, L.Z.1    Hobaugh, M.R.2    Shustak, C.3    Cheley, S.4    Bayley, H.5    Gouaux, J.E.6
  • 46
    • 0029914605 scopus 로고    scopus 로고
    • Indications of a common folding pattern for VDAC channels from all sources
    • Song, J., and Colombini, M. (1996) Indications of a common folding pattern for VDAC channels from all sources. J. Bioenerg. Biomembr. 28, 153-161
    • (1996) J. Bioenerg. Biomembr. , vol.28 , pp. 153-161
    • Song, J.1    Colombini, M.2
  • 47
    • 0028351141 scopus 로고
    • On the structure of mitochondrial porin and its homologies with bacterial porins
    • Rauch, G., and Moran, O. (1994) On the structure of mitochondrial porin and its homologies with bacterial porins. Biochem. Biophys. Res. Commun. 200, 908-915
    • (1994) Biochem. Biophys. Res. Commun. , vol.200 , pp. 908-915
    • Rauch, G.1    Moran, O.2
  • 48
    • 0027450611 scopus 로고
    • Insertion derivatives containing segments up to 16 amino acids identify surface- and periplasm-exposed regions of the FhuA outer membrane receptor of Escherichia coli K-12
    • Koebnik, R., and Braun, V. (1993) Insertion derivatives containing segments up to 16 amino acids identify surface- and periplasm-exposed regions of the FhuA outer membrane receptor of Escherichia coli K-12. J. Bacteriol. 175, 826-839
    • (1993) J. Bacteriol. , vol.175 , pp. 826-839
    • Koebnik, R.1    Braun, V.2
  • 49
    • 0028465092 scopus 로고
    • Counting polymers moving through a single ion channel
    • Bezrukov, S. M., Vodyanoy, I., and Parsegian, V. A. (1994) Counting polymers moving through a single ion channel. Nature (London) 370, 279-281
    • (1994) Nature (London) , vol.370 , pp. 279-281
    • Bezrukov, S.M.1    Vodyanoy, I.2    Parsegian, V.A.3
  • 50
    • 0028286006 scopus 로고
    • Molecular basis of mitochondrial DNA disease
    • Brown, M. D., and Wallace, D. C. (1994) Molecular basis of mitochondrial DNA disease. J. Bioenerg. Biomembr. 26, 273-289
    • (1994) J. Bioenerg. Biomembr. , vol.26 , pp. 273-289
    • Brown, M.D.1    Wallace, D.C.2
  • 52
    • 0024541837 scopus 로고
    • Mitochondrial DNA mutations as an important contributor to aging and degenerative diseases
    • Linnane, A. W., Marzuki, S., Ozawa, T., and Tanaka, M. (1989) Mitochondrial DNA mutations as an important contributor to aging and degenerative diseases. Lancet 1, 642-645 .
    • (1989) Lancet , vol.1 , pp. 642-645
    • Linnane, A.W.1    Marzuki, S.2    Ozawa, T.3    Tanaka, M.4
  • 53
    • 0029026639 scopus 로고
    • Mechanism of somatic mitochondrial DNA mutations associated with age and diseases
    • Ozawa, T. (1995) Mechanism of somatic mitochondrial DNA mutations associated with age and diseases. Biochim. Biophys. Acta 1271, 177-189
    • (1995) Biochim. Biophys. Acta , vol.1271 , pp. 177-189
    • Ozawa, T.1
  • 54
    • 0025315698 scopus 로고
    • Mitochondrial diseases: Gene mapping and gene therapy
    • Lander, E. S., and Lodish, H. (1990) Mitochondrial diseases: gene mapping and gene therapy. Cell 61, 925-926
    • (1990) Cell , vol.61 , pp. 925-926
    • Lander, E.S.1    Lodish, H.2
  • 55
    • 0026591024 scopus 로고
    • Isolation of the mitochondrial benzodiazepine receptor: Association with the voltage-dependent anion channel and the adenine nucleotide carrier
    • McEnery, M. W., Snowman, A. M., Trifiletti, R. R., and Snyder, S. H. (1991) Isolation of the mitochondrial benzodiazepine receptor: association with the voltage-dependent anion channel and the adenine nucleotide carrier. Proc. Natl. Acad. Sci. USA 89, 3170-3174
    • (1991) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 3170-3174
    • McEnery, M.W.1    Snowman, A.M.2    Trifiletti, R.R.3    Snyder, S.H.4
  • 56
    • 0028987664 scopus 로고
    • Involvement of peripheral-type benzodiazepine receptors in the intracellular transport of heme and porphyrins
    • Taketani, S., Kohno, H., Furukawa, T., and Tokunaga, R. (1995) Involvement of peripheral-type benzodiazepine receptors in the intracellular transport of heme and porphyrins. J. Biochem. Tokyo 117, 875-880
    • (1995) J. Biochem. Tokyo , vol.117 , pp. 875-880
    • Taketani, S.1    Kohno, H.2    Furukawa, T.3    Tokunaga, R.4
  • 57
    • 0029116916 scopus 로고
    • The mitochondrial permeability transition
    • Zoratti, M., and Szabò, I. (1995) The mitochondrial permeability transition. Biochim. Biophys. Acta 1241, 139-176
    • (1995) Biochim. Biophys. Acta , vol.1241 , pp. 139-176
    • Zoratti, M.1    Szabò, I.2


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