메뉴 건너뛰기




Volumn 89, Issue 6, 2005, Pages 3950-3959

New insights into the mechanism of permeation through large channels

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; CATION; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; UNCLASSIFIED DRUG; VOLTAGE GATED CHANNEL FORMING PROTEIN; VOLTAGE GATED CHANNEL FORMING PROTEIN 2;

EID: 28444483998     PISSN: 00063495     EISSN: 00063495     Source Type: Journal    
DOI: 10.1529/biophysj.105.070037     Document Type: Article
Times cited : (42)

References (42)
  • 1
    • 0018775962 scopus 로고
    • A candidate for the permeability pathway of the outer mitochondrial membrane
    • Colombini, M. 1979. A candidate for the permeability pathway of the outer mitochondrial membrane. Nature. 279:643-645.
    • (1979) Nature , vol.279 , pp. 643-645
    • Colombini, M.1
  • 2
    • 0021770701 scopus 로고
    • Evidence that the crystalline arrays in the outer membrane of Neurospora mitochondria are composed of the voltage-dependent channel protein
    • Mannella, C. A., and M. Colombini. 1984. Evidence that the crystalline arrays in the outer membrane of Neurospora mitochondria are composed of the voltage-dependent channel protein. Biochim. Biophys. Acta. 774:206-214.
    • (1984) Biochim. Biophys. Acta , vol.774 , pp. 206-214
    • Mannella, C.A.1    Colombini, M.2
  • 3
    • 0026538575 scopus 로고
    • Toward the molecular structure of the mitochondrial channel, VDAC
    • Mannella, C. A., M. Forte, and M. Colombini. 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
  • 4
    • 15644371838 scopus 로고    scopus 로고
    • The role of yeast VDAC genes on the permeability of the mitochondrial outer membrane
    • Lee, A. C., X. Xu, E. Blachly-Dyson, M. Forte, and M. Colombini. 1998. The role of yeast VDAC genes on the permeability of the mitochondrial outer membrane. J. Membr. Biol. 161:173-181.
    • (1998) J. Membr. Biol. , vol.161 , pp. 173-181
    • Lee, A.C.1    Xu, X.2    Blachly-Dyson, E.3    Forte, M.4    Colombini, M.5
  • 5
    • 0032765963 scopus 로고    scopus 로고
    • Mouse VDAC isoforms expressed in yeast: Channel properties and their roles in mitochondrial outer membrane permeability
    • Xu, X., W. Decker, M. J. Sampson, W. J. Craigen, and M. Colombini. 1999. Mouse VDAC isoforms expressed in yeast: channel properties and their roles in mitochondrial outer membrane permeability. J. Membr. Biol. 170:89-102.
    • (1999) J. Membr. Biol. , vol.170 , pp. 89-102
    • Xu, X.1    Decker, W.2    Sampson, M.J.3    Craigen, W.J.4    Colombini, M.5
  • 6
    • 0018847077 scopus 로고
    • Structure and mode of action of a voltage dependent anion-selective channel (VDAC) located in the outer mitochondrial membrane
    • Colombini, M. 1980. Structure and mode of action of a voltage dependent anion-selective channel (VDAC) located in the outer mitochondrial membrane. Ann. N. Y. Acad. Sci. 341:552-563.
    • (1980) Ann. N. Y. Acad. Sci. , vol.341 , pp. 552-563
    • Colombini, M.1
  • 7
    • 0023392488 scopus 로고
    • Regulation of the mitochondrial outer membrane channel, VDAC
    • Colombini, M. 1987. Regulation of the mitochondrial outer membrane channel, VDAC. J. Bioenerg. Biomembr. 19:309-320.
    • (1987) J. Bioenerg. Biomembr. , vol.19 , pp. 309-320
    • Colombini, M.1
  • 8
    • 0024448106 scopus 로고
    • Structure of the mitochondrial outer membrane channel derived from electron microscopy of 2D crystals
    • Mannella, C. A. 1989. Structure of the mitochondrial outer membrane channel derived from electron microscopy of 2D crystals. J. Bioenerg. Biomembr. 21:427-437.
    • (1989) J. Bioenerg. Biomembr. , vol.21 , pp. 427-437
    • Mannella, C.A.1
  • 10
    • 0034731386 scopus 로고    scopus 로고
    • Structure and orientation of two voltage-dependent anion-selective channel isoforms. An attenuated total reflection Fourier-transform infrared spectroscopy study
    • Abrecht, H., E. Goormaghtigh, J. M. Ruysschaert, and F. Homble. 2000. Structure and orientation of two voltage-dependent anion-selective channel isoforms. An attenuated total reflection Fourier-transform infrared spectroscopy study. J. Biol. Chem. 275:40992-40999.
    • (2000) J. Biol. Chem. , vol.275 , pp. 40992-40999
    • Abrecht, H.1    Goormaghtigh, E.2    Ruysschaert, J.M.3    Homble, F.4
  • 11
    • 0024458675 scopus 로고
    • Voltage gating in the mitochondrial channel, VDAC
    • Colombini, M. 1989. Voltage gating in the mitochondrial channel, VDAC. J. Membr. Biol. 111:103-111.
    • (1989) J. Membr. Biol. , vol.111 , pp. 103-111
    • Colombini, M.1
  • 12
    • 0031806216 scopus 로고    scopus 로고
    • The sensor regions of VDAC are translocated from within the membrane to the surface during the gating processes
    • Song, J., C. Midson, E. Blachly-Dyson, M. Forte, and M. Colombini. 1998. The sensor regions of VDAC are translocated from within the membrane to the surface during the gating processes. Biophys. J. 74:2926-2944.
    • (1998) Biophys. J. , vol.74 , pp. 2926-2944
    • Song, J.1    Midson, C.2    Blachly-Dyson, E.3    Forte, M.4    Colombini, M.5
  • 13
    • 0017054558 scopus 로고
    • Reconstitution in planar lipid bilayers of a voltage-dependent anion-selective channel obtained from paramecium mitochondria
    • Schein, S. J., M. Colombini, and A. Finkelstein. 1976. Reconstitution in planar lipid bilayers of a voltage-dependent anion-selective channel obtained from paramecium mitochondria. J. Membr. Biol. 30:99-120.
    • (1976) J. Membr. Biol. , vol.30 , pp. 99-120
    • Schein, S.J.1    Colombini, M.2    Finkelstein, A.3
  • 14
    • 0030947935 scopus 로고    scopus 로고
    • VDAC channels mediate and gate the flow of ATP: Implications for the regulation of mitochondrial function
    • Rostovtseva, T., and M. Colombini. 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
  • 15
    • 0036219774 scopus 로고    scopus 로고
    • Dynamics of nucleotides in VDAC channels: Structure-specific noise generation
    • Rostovtseva, T. K., A. Komarov, S. M. Bezrukov, and M. Colombini. 2002. Dynamics of nucleotides in VDAC channels: structure-specific noise generation. Biophys. J. 82:193-205.
    • (2002) Biophys. J. , vol.82 , pp. 193-205
    • Rostovtseva, T.K.1    Komarov, A.2    Bezrukov, S.M.3    Colombini, M.4
  • 16
    • 0031967829 scopus 로고    scopus 로고
    • ATP transport through a single mitochondrial channel, VDAC, studied by current fluctuation analysis
    • Rostovtseva, T. K., and S. M. Bezrukov. 1998. ATP transport through a single mitochondrial channel, VDAC, studied by current fluctuation analysis. Biophys. J. 74:2365-2373.
    • (1998) Biophys. J. , vol.74 , pp. 2365-2373
    • Rostovtseva, T.K.1    Bezrukov, S.M.2
  • 17
    • 0037092536 scopus 로고    scopus 로고
    • VDAC channels differentiate between natural metabolites and synthetic molecules
    • Rostovtseva, T. K., A. Komarov, S. M. Bezrukov, and M. Colombini. 2002. VDAC channels differentiate between natural metabolites and synthetic molecules. J. Membr. Biol. 187:147-156.
    • (2002) J. Membr. Biol. , vol.187 , pp. 147-156
    • Rostovtseva, T.K.1    Komarov, A.2    Bezrukov, S.M.3    Colombini, M.4
  • 18
    • 0025355620 scopus 로고
    • Selectivity changes in site-directed mutants of the VDAC ion channel: Structural implications
    • Blachly-Dyson, E., S. Peng, M. Colombini, and M. Forte. 1990. Selectivity changes in site-directed mutants of the VDAC ion channel: structural implications. Science. 247:1233-1236.
    • (1990) Science , vol.247 , pp. 1233-1236
    • Blachly-Dyson, E.1    Peng, S.2    Colombini, M.3    Forte, M.4
  • 19
    • 0030856487 scopus 로고    scopus 로고
    • The murine voltage-dependent anion channel gene family. Conserved structure and function
    • Sampson, M. J., R. S. Lovell, and W. J. Craigen. 1997. The murine voltage-dependent anion channel gene family. Conserved structure and function. J. Biol. Chem. 272:18966-18973.
    • (1997) J. Biol. Chem. , vol.272 , pp. 18966-18973
    • Sampson, M.J.1    Lovell, R.S.2    Craigen, W.J.3
  • 20
    • 0020479807 scopus 로고
    • Import of proteins into mitochondria. Cytochrome b2 and cytochrome c peroxidase are located in the intermembrane space of yeast mitochondria
    • Daum, G., P. C. Bohni, and G. Schatz. 1982. Import of proteins into mitochondria. Cytochrome b2 and cytochrome c peroxidase are located in the intermembrane space of yeast mitochondria. J. Biol. Chem. 257:13028-13033.
    • (1982) J. Biol. Chem. , vol.257 , pp. 13028-13033
    • Daum, G.1    Bohni, P.C.2    Schatz, G.3
  • 21
    • 0017229768 scopus 로고
    • A major polypeptide component of rat liver mitochondria: Carbamyl phosphate synthetase
    • Clarke, S. 1976. A major polypeptide component of rat liver mitochondria: carbamyl phosphate synthetase. J. Biol. Chem. 251:950-961.
    • (1976) J. Biol. Chem. , vol.251 , pp. 950-961
    • Clarke, S.1
  • 22
    • 77957088304 scopus 로고
    • Isolation of plant mitochondria: General principles and criteria of integrity
    • Douce, R., J. Bourguignon, R. Brouquisse, and N. Neuburger. 1987. Isolation of plant mitochondria: general principles and criteria of integrity. Methods Enzymol. 148:403-412.
    • (1987) Methods Enzymol. , vol.148 , pp. 403-412
    • Douce, R.1    Bourguignon, J.2    Brouquisse, R.3    Neuburger, N.4
  • 23
    • 0014027335 scopus 로고
    • Preparation and some properties of yeast mitochondria
    • Ohnishi, T., K. Kawaguchi, and B. Hagihara. 1966. Preparation and some properties of yeast mitochondria. J. Biol. Chem. 241:1797-1806.
    • (1966) J. Biol. Chem. , vol.241 , pp. 1797-1806
    • Ohnishi, T.1    Kawaguchi, K.2    Hagihara, B.3
  • 24
    • 0000103467 scopus 로고
    • Separation and enzymatic properties of the inner and outer membranes of rat liver mitochondria
    • Sotocassa, G. L., B. Kuylenstiema, L. Ernster, and A. Begstrand. 1967. Separation and enzymatic properties of the inner and outer membranes of rat liver mitochondria. Methods Enzymol. 10:448-463.
    • (1967) Methods Enzymol. , vol.10 , pp. 448-463
    • Sotocassa, G.L.1    Kuylenstiema, B.2    Ernster, L.3    Begstrand, A.4
  • 25
    • 0014204014 scopus 로고
    • Adenylate kinase from baker's yeast (II. Substrate specificity)
    • Su, S., and P. J. Russell. 1967. Adenylate kinase from baker's yeast (II. Substrate specificity). Biochim. Biophys. Acta. 132:370-378.
    • (1967) Biochim. Biophys. Acta , vol.132 , pp. 370-378
    • Su, S.1    Russell, P.J.2
  • 26
    • 0020450839 scopus 로고
    • Structure of the outer mitochondrial membrane: Ordered arrays of porelike subunits in outer-membrane fractions from Neurospora crassa mitochondria
    • Mannella, C. A. 1982. Structure of the outer mitochondrial membrane: ordered arrays of porelike subunits in outer-membrane fractions from Neurospora crassa mitochondria. J. Cell Biol. 94:680-687.
    • (1982) J. Cell Biol. , vol.94 , pp. 680-687
    • Mannella, C.A.1
  • 27
    • 0020995433 scopus 로고
    • Isolation and properties of the porin of the outer mitochondrial membrane from Neurospora crassa
    • Freitag, H., R. Benz, and W. Neupert. 1983. Isolation and properties of the porin of the outer mitochondrial membrane from Neurospora crassa. Methods Enzymol. 97:286-294.
    • (1983) Methods Enzymol. , vol.97 , pp. 286-294
    • Freitag, H.1    Benz, R.2    Neupert, W.3
  • 28
    • 0015459562 scopus 로고
    • Formation of bimolecular membranes from lipid mortolayers and a study of their electrical properties
    • Montai, M., and P. Mueller. 1972. Formation of bimolecular membranes from lipid mortolayers and a study of their electrical properties. Proc. Natl. Acad. Sci. USA. 69:3561-3566.
    • (1972) Proc. Natl. Acad. Sci. USA , vol.69 , pp. 3561-3566
    • Montai, M.1    Mueller, P.2
  • 29
    • 0027400112 scopus 로고
    • Probing alamethicin channels with water-soluble polymers. Effect on conductance of channel states
    • Bezrukov, S. M., and I. Vodyanoy. 1993. Probing alamethicin channels with water-soluble polymers. Effect on conductance of channel states. Biophys. J. 64:16-25.
    • (1993) Biophys. J. , vol.64 , pp. 16-25
    • Bezrukov, S.M.1    Vodyanoy, I.2
  • 31
    • 0027389308 scopus 로고
    • Cloning and functional expression in yeast of two human isoforms of the outer mitochondrial membrane channel, the voltage-dependent anion channel
    • Blachly-Dyson, E., E. B. Zambronicz, W. H. Yu, V. Adams, E. R. McCabe, J. Adelman, M. Colombini, and M. Forte. 1993. Cloning and functional expression in yeast of two human isoforms of the outer mitochondrial membrane channel, the voltage-dependent anion channel. J. Biol. Chem. 268:1835-1841.
    • (1993) J. Biol. Chem. , vol.268 , pp. 1835-1841
    • Blachly-Dyson, E.1    Zambronicz, E.B.2    Yu, W.H.3    Adams, V.4    McCabe, E.R.5    Adelman, J.6    Colombini, M.7    Forte, M.8
  • 32
    • 0029854155 scopus 로고    scopus 로고
    • ATP flux is controlled by a voltage-gated channel from the mitochondrial outer membrane
    • Rostovtseva, T. K., and M. Colombini. 1996. ATP flux is controlled by a voltage-gated channel from the mitochondrial outer membrane. J. Biol. Chem. 271:28006-28008.
    • (1996) J. Biol. Chem. , vol.271 , pp. 28006-28008
    • Rostovtseva, T.K.1    Colombini, M.2
  • 33
    • 0016678144 scopus 로고
    • Maltose transport in Escherichia coli K-12: Involvement of the bacteriophage lambda receptor
    • Szmelcman, S., and M. Hofnung. 1975. Maltose transport in Escherichia coli K-12: involvement of the bacteriophage lambda receptor. J. Bacteriol. 124:112-118.
    • (1975) J. Bacteriol. , vol.124 , pp. 112-118
    • Szmelcman, S.1    Hofnung, M.2
  • 34
    • 0009551491 scopus 로고
    • Specificity of diffusion channels produced by lambda phage receptor protein of Escherichia coli
    • Luckey, M., and H. Nikaido. 1980. Specificity of diffusion channels produced by lambda phage receptor protein of Escherichia coli. Proc. Natl. Acad. Sci. USA. 77:167-171.
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 167-171
    • Luckey, M.1    Nikaido, H.2
  • 35
    • 0036154083 scopus 로고    scopus 로고
    • Transport of maltodextrins through maltoporin: A single-channel study
    • Kullman, L., M. Winterhalter, and S. M. Bezrukov. 2002. Transport of maltodextrins through maltoporin: a single-channel study. Biophys. J. 82:803-812.
    • (2002) Biophys. J. , vol.82 , pp. 803-812
    • Kullman, L.1    Winterhalter, M.2    Bezrukov, S.M.3
  • 36
    • 0037162486 scopus 로고    scopus 로고
    • Designed to penetrate: Time-resolved interaction of single antibiotic molecules with bacterial pores
    • Nestorovich, E. M., C. Danelon, M. Winterhalter, and S. M. Bezrukov. 2002. Designed to penetrate: time-resolved interaction of single antibiotic molecules with bacterial pores. Proc. Natl. Acad. Sci. USA. 99:9789-9794.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 9789-9794
    • Nestorovich, E.M.1    Danelon, C.2    Winterhalter, M.3    Bezrukov, S.M.4
  • 37
    • 18744434646 scopus 로고
    • Cause and consequences of dynamic compartmentation of adenine nucleotides in the mitochondrial intermembrane space in respect to exchange of energy-rich phosphates between cytosol and mitochondria
    • Gellerich, F. N., and W. Kunz. 1987. Cause and consequences of dynamic compartmentation of adenine nucleotides in the mitochondrial intermembrane space in respect to exchange of energy-rich phosphates between cytosol and mitochondria. Biomed. Biochim. Acta. 46:S545-S548.
    • (1987) Biomed. Biochim. Acta , vol.46
    • Gellerich, F.N.1    Kunz, W.2
  • 38
    • 0027473130 scopus 로고
    • Influence of the mitochondrial outer membrane and the binding of creatine kinase to the mitochondrial inner membrane on the compartmentation of adenine nucleotides in the intermembrane space of rat liver mitochondria
    • Gellerich, F. N., Z. A. Khuchua, and A. V. Kuznetsov. 1993. Influence of the mitochondrial outer membrane and the binding of creatine kinase to the mitochondrial inner membrane on the compartmentation of adenine nucleotides in the intermembrane space of rat liver mitochondria. Biochim. Biophys. Acta. 1140:327-334.
    • (1993) Biochim. Biophys. Acta , vol.1140 , pp. 327-334
    • Gellerich, F.N.1    Khuchua, Z.A.2    Kuznetsov, A.V.3
  • 39
    • 0030384264 scopus 로고    scopus 로고
    • Dynamics and free energy of polymers partitioning into a nano-scale pore
    • Bezrukov, S. M., I. Vodyanoy, R. A. Brutyan, and J. J. Kasianowicz. 1996. Dynamics and free energy of polymers partitioning into a nano-scale pore. Macromolecules. 29:8517-8522.
    • (1996) Macromolecules , vol.29 , pp. 8517-8522
    • Bezrukov, S.M.1    Vodyanoy, I.2    Brutyan, R.A.3    Kasianowicz, J.J.4
  • 40
    • 21244505884 scopus 로고    scopus 로고
    • Optimizing transport of metabolites through large channels: Molecular sieves with and without binding
    • Berezhkovskii, A. M., and S. M. Bezrukov. 2005. Optimizing transport of metabolites through large channels: molecular sieves with and without binding. Biophys. J. 88:L17-L19.
    • (2005) Biophys. J. , vol.88
    • Berezhkovskii, A.M.1    Bezrukov, S.M.2
  • 41
    • 0029914605 scopus 로고    scopus 로고
    • Indication of a common folding pattern for VDAC channels from all sources
    • Song, J., and M. Colombini. 1996. Indication 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
  • 42
    • 0035881510 scopus 로고    scopus 로고
    • Calcium binding and translocation by the voltage-dependent anion channel: A possible regulatory mechanism in mitochondrial function
    • Gincel, D., H. Zaid, and V. Shoshan-Barmatz. 2001. Calcium binding and translocation by the voltage-dependent anion channel: a possible regulatory mechanism in mitochondrial function. Biochem. J. 358:147-155.
    • (2001) Biochem. J. , vol.358 , pp. 147-155
    • Gincel, D.1    Zaid, H.2    Shoshan-Barmatz, V.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.