Channels in Mitochondrial Membranes: Knowns, Unknowns, and Prospects for the Future

References

• Adams V., Bosch W., Schlegel J., Wallimann T., Brdiczka D. Further characterisation of contact sites from mitochondria of different tissues: topology of peripheral kinases. Biochim, Biophys. Acta 1989; 981: 213–225
   PubMed Web of Science ®Google Scholar
• Adelsberger-Mangan D. M., Colombini M. Elimination and restoration of voltage dependence in the mitochondria channel, VDAC., by graded modification with succinic anhydride. J. Membr. Biol. 1987; 98: 157–168
   PubMed Web of Science ®Google Scholar
• Albuquerque E. X., Daly J. W., Warnick J. E. Macromolecular sites for specific neurotoxins and drugs on chemiosensitive synapses and electrical excitation in biological membranes. Ion channels, T. Narahashi. Plenum Press, New York and London 1991; Vol. 1: 95–162
   Google Scholar
• Amchenkova A. A., Bakeeva L. E., Chentsov Yu S., Skulachev V. P., Zorov D. B. Coupling membranes as energy-transmitting cables. I. Filamentous mitochondria in fibroblasts and mitochondrial clusters in cardiomyocytes. J. Cell. Biol. 1988; 107: 481–495
   PubMed Web of Science ®Google Scholar
• Antonenko Y. N., Kinnally K. W., Tedeschi H. Identification of anion and cation pathways in the inner mitochondrial membrane by patch clamping of mouse liver mitoplasts. J. Membr. Biol. 1991; 124: 151–158
   PubMed Web of Science ®Google Scholar
• Antonenko Y. N., Kinnally K. W., Perini S., Tedeschi H. (Selective effect of inhibitors on inner mitochondrial membrane channels. FEBS Lett. 1991; 285: 89–93
   PubMed Web of Science ®Google Scholar
• Arizmendi J. M., Skehel J. M., Runswick M. J., Fearnley I. M., Walker J. E. Complementary DNA sequences of two 14.5 kDa subunits of NADH: ubiquinone oxidoreductase from bovine heart mitochondria. Completion of the primary structure of the complex. FEBS Lett. 1992; 313: 80–84
   PubMed Web of Science ®Google Scholar
• Arora K. K., Pedersen P. L. Functional significance of mitochondrial bound hexokinase in tumor cell metabolism. Evidence for preferential phosphorylation of glucose by intramitochondrially generated ATP. J. Biol. Chem. 1988; 263: 17422–17428
   PubMed Web of Science ®Google Scholar
• Arora K. K., Parry D. M., Pedersen P. L. Hexokinase receptors: preferential enzyme binding in normal cells to nonmitochondrial sites and in transformed cells to mitochondrial sites. J. Bioenerg. Biomembr. 1992; 24: 47–53
   PubMed Web of Science ®Google Scholar
• Ashcroft F. M., Harrison D. E., Ashcroft S. J. H. Glucose induces closures of single potassium channels in isolated rat pancreatic beta-cells. Nature 1984; 312: 446–448
   PubMed Web of Science ®Google Scholar
• Baker K. P., Schatz G. Mitochondrial proteins essential for viability mediate protein import into yeast mitochondria. Nature 1991; 349: 205–208
   PubMed Web of Science ®Google Scholar
• Baker K. P., Schaniel A., Vestweber D., Schatz G. A yeast mitochondrial outer membrane protein essential for protein import and cell viability. Nature 1990; 348: 605–609
   PubMed Web of Science ®Google Scholar
• Ballarin C., Sorgato M. C., Moran O. A minimal kinetic model of the activity of the 107 pS channel of the inner membrane of mitochondria. Molecular Biology of Mitochondrial Transport Systems, M. Forte, M. Colombini. Springer-Verlag, Heidelberg 1993, in press
   Google Scholar
• Bean B. P., Friel D. D. ATP-activated channels in excitables cells. Ion Channels, T. Narahashi. Plenum Press, New York and London 1990; Vol. 2: 169–203
   Google Scholar
• Beavis A. D. On the inhibition of the mitochondrial inner membrane anion uniporter by cationic amphiphiles and other drugs. J. Biol. Chem. 1989; 264: 1508–1515
   PubMed Web of Science ®Google Scholar
• Beavis A. D. Properties of the inner membrane anion channel in intact mitochondria. J. Bioenerg. Biomembr. 1992; 24: 77–90
   PubMed Web of Science ®Google Scholar
• Benz R. Porin from bacterial and mitochondrial outer membranes. CRC Crit. Rev. Biochem. 1985; 19: 145–190
   PubMed Web of Science ®Google Scholar
• Benz R. Biophysical properties of porin pores from mitochondrial outer membrane of eukaryotic cells. Experientia 1990; 46: 131–137
   PubMedGoogle Scholar
• Benz R., Brdiczka D. The cation-selective substate of the mitochondrial outer membrane pore: single-channel conductance and influence on intermembrane and peripheral kinases. J. Bioenerg. Biomembr. 1992; 24: 33–39
   PubMed Web of Science ®Google Scholar
• Benz R., Kottke M., Brdiczka D. The cationically selective state of the mitochondrial outer membrane pore: a study with intact mitochondria and reconstituted mitochondrial porin. Biochim. Biophys. Acta 1990; 1022: 311–318
   PubMed Web of Science ®Google Scholar
• Benz R., Janko K., Boos W., Läuger P. Formation of large, ion-permeable membrane channels by the matrix protein (porin) of Escherichia coli. Biochim. Biophys. Acta 1978; 511: 305–319
   PubMed Web of Science ®Google Scholar
• Benz R., Wojtczak L., Bosh W., Brdiczka D. Inhibition of adenine nucleotide transport through the mitochondrial porin by a synthetic poly anion. FEBS Lett. 1988; 231: 75–80
   PubMed Web of Science ®Google Scholar
• Bernardi P., Vassanelli S., Veronese P., Colonna R., Szabo' I., Zoratti M. Modulation of the mitochondrial permeability transition pore. Effect of protons and divalent cations. J. Biol. Chem. 1992; 267: 2934–2939
   PubMed Web of Science ®Google Scholar
• Bessman S. P., Carpenter C. L. The creatine-creatine phosphate energy shuttle. Annu. Rev. Biochem. 1985; 54: 831–862
   PubMed Web of Science ®Google Scholar
• Blachly-Dyson E., Peng S. Z., Colombini M., Forte M. Probing the structure of the mitochondrial channel, VDAC., by site-directed mutagenesis: a progress report. J. Bioenerg. Biomembr. 1989; 21: 471–483
   PubMed Web of Science ®Google Scholar
• Blachly-Dyson E., Peng S. Z., Colombini M., Forte M. Selectivity changes in site-directed mutants of the VDAC ion channel: structural implications. Science 1990; 247: 1233–1236
   PubMed Web of Science ®Google Scholar
• Blobel G. Intracellular protein topogenesis. Proc. Natl. Acad. Sci. U.S.A. 1980; 77: 1496–1500
   PubMed Web of Science ®Google Scholar
• Blobel G., Dobberstein B. Transfer of proteins across membranes. J. Cell. Biol. 1975; 67: 835–851
   PubMed Web of Science ®Google Scholar
• Bowen K. A., Tam K., Colombini M. Evidence for titrable gating charges controlling the voltage dependence of the outer mitochondrial membrane channel, VDAC. J. Membr. Biol. 1985; 86: 51–59
   PubMed Web of Science ®Google Scholar
• Bücheler K., Adams V., Brdiczka D. Localization of the ATP/ADP translocator in the inner membrane and regulation of contact sites between mitochondrial envelope membranes by ADP. A study on freeze-fractured isolated liver mitochondria. Biochim. Biophys. Acta 1991; 1056: 233–242
   PubMed Web of Science ®Google Scholar
• Bureau M. H., Khrestchatisky M., Heeren M. A., Zambrowicz E. B., Kim H., Grisar T. M., Colombini M., Tobin A. J., Olsen R. W. Isolation and cloning of a voltage-dependent anion channel-like M 36,000 polypeptide from mammalian brain. J. Biol. Chem. 1992; 267: 8679–8684
   PubMed Web of Science ®Google Scholar
• Campo M. L., Kinnally K. W., Tedeschi H. The effect of antimycin A on mouse liver inner mitochondrial membrane channel activity. J. Biol. Chem. 1992; 267: 8123–8127
   PubMed Web of Science ®Google Scholar
• Chich J F., Goldschmidt D., Thieffry M., Henry J P. A peptide-sensitive channel of large conductance is localized on mitochondrial outer membrane. Eur. J. Biochem. 1991; 196: 29–35
   PubMedGoogle Scholar
• Colombini M. A candidate for the permeability pathway of the outer mitochondrial membrane. Nature 1979; 279: 643–645
   PubMed Web of Science ®Google Scholar
• Colombini M. Pore size and properties of channels from mitochondria isolated from Neurospora crassa. J. Membr. Biol. 1980; 53: 79–84
   Web of Science ®Google Scholar
• Colombini M. Purification of VDAC (voltage-dependent anion-selective channel) from rat liver mitochondria. J. Membr. Biol. 1983; 74: 115–121
   PubMed Web of Science ®Google Scholar
• Colombini M. Voltage gating in VDAC. Ion Channel Reconstitution, C. Miller. Plenum Press, New York 1986; 533–552
   Google Scholar
• Colombini M. Voltage gating in the mitochondrial channel, VDAC. J. Membr. Biol. 1989; 11: 103–111
   Google Scholar
• Colombini M., Yeung C. L., Tung J., König T. The mitochondrial outer membrane channel, VDAC., is regulated by a synthetic polyanion. Biochim. Biophys. Acta 1987; 905: 279–286
   PubMed Web of Science ®Google Scholar
• Costa G., Kinnaliy K. W., Diwan J. J. Patch clamp analysis of a partially purified ion channel from rat liver mitochondria. Biochem. Biophys. Res. Comm. 1991; 175: 305–310
   PubMed Web of Science ®Google Scholar
• Craven P. A., Goldblatt P. J., Basford R. E. Brain hexokinase. The preparation of inner and outer mitochondrial membranes. Biochemistry 1969; 8: 3525–3532
   PubMed Web of Science ®Google Scholar
• Criado M., Keller B. U. A membrane fusion strategy for single-channel recordings of membranes usually non-accessible to patch-clamp pipette electrodes. FEBS Lett. 1987; 224: 172–176
   PubMed Web of Science ®Google Scholar
• Crompton M., Costi A. Kinetic evidence for a heart mitochondrial pore activated by Ca2+, inorganic phosphate and oxidative stress. A potential mechanism for mitochondrial dysfunction during cellular Ca2+ overload. Eur. J. Biochem. 1988; 178: 488–501
   Google Scholar
• Crompton M., Costi A. A heart mitochondrial Ca2+dependent pore of possible relevance to re-perfusion-induced injury. Biochem. J. 1990; 266: 33–39
   PubMed Web of Science ®Google Scholar
• De Pinto V., Palmieri F. Transmembrane arrangement of mitochondrial porin or voltage-dependent anion channel (VDAC). J. Bioenerg. Biomembr. 1992; 24: 21–26
   PubMed Web of Science ®Google Scholar
• De Pinto V., Prezioso G., Palmieri F. A simple and rapid method for the purification of the mitochondrial porin from mammalian tissues. Biochim. Biophys. Acta 1987; 905: 499–502
   PubMed Web of Science ®Google Scholar
• De Pinto V., Benz R., Palmieri F. Interaction of non-classical detergents with the mitochondrial pore. A new purification procedure and characterization of the pore-forming unit. Eur. J. Biochem. 1989; 183: 179–187
   PubMedGoogle Scholar
• De Pinto V., Tommasino M., Benz R., Palmieri F. The 35-kDa DCCD-binding protein from pig heart mitochondria is the mitochondrial porin. Biochim. Biophys. Acta 1985; 813: 230–242
   PubMed Web of Science ®Google Scholar
• De Pinto V., Benz R., Caggese C., Palmieri F. Characterization of the mitochondrial porin from Drosophila melanogaster. Biochim. Biophys. Acta 1989; 987: 1–7
   PubMed Web of Science ®Google Scholar
• De Pinto V., Al Jamal J. A., Benz R., Palmieri F. Positive residues involved in the voltage-gating of the mitochondrial porin-channel are localised in the external moiety of the pore. FEBS Lett. 1990; 274: 122–126
   PubMed Web of Science ®Google Scholar
• De Pinto V., Ludwig O., Krause J., Benz R., Palmieri F. Porin pores of mitochondrial outer membranes from high and low eukaryotic cells: biochemical and biophysical characterization. Biochim. Biophys. Acta 1987; 894: 109–119
   PubMed Web of Science ®Google Scholar
• De Pinto V., Zara V., Benz R., Gnoni V., Palmieri F. Characterization of pore-forming activity in liver mitochondria from Anguilla anguilla. Biochim. Biophys. Acta 1991a; 1061: 279–286
   PubMed Web of Science ®Google Scholar
• De Pinto V., Prezioso G., Thinnes F., Link T. A., Palmieri F. Peptide-specific antibodies and proteases as probes of the transmembrane topology of the bovine heart mitochondrial porin. Biochemistry 1991b; 30: 10191–10200
   PubMed Web of Science ®Google Scholar
• Dihanich M., Schmid A., Oppliger W., Benz R. Identification of a new pore in the mitochondrial outer membrane of a porin-deficient yeast mutant. Eur. J. Biochem. 1989; 181: 703–708
   PubMedGoogle Scholar
• Dill E. T., Holden M. J., Colombini M. Voltage gating in VDAC is markedly inhibited by micromolar quantities of aluminium. J. Membr. Biol. 1987; 99: 187–196
   PubMed Web of Science ®Google Scholar
• Dorbani L., Jancsik V., Lindén M., Leterrier J. F., Nelson B. D., Rendon A. Subfractionation of the outer membrane of rat brain mitochondria: evidence for the existence of a domain containing the porin-hexokinase complex. Arch. Biochem. Biophys. 1987; 252: 188–196
   PubMed Web of Science ®Google Scholar
• Doring C., Colombini M. On the nature of the molecular mechanism underlying the voltage dependence of the channel-forming protein, voltage-dependent anion-selective channel (VDAC). Biophys. J. 1984; 45: 44–46
   PubMed Web of Science ®Google Scholar
• Doring C., Colombini M. Voltage dependence and ion selectivity of the mitochondrial channel, VDAC., are modified by succinic anhydride. J. Membr. Biol. 1985a; 83: 81–86
   PubMed Web of Science ®Google Scholar
• Doring C., Colombini M. The mitochondrial voltagedependent channel, VDAC., is modified asymmetrically by succinic anhydride. J. Membr. Biol. 1985b; 83: 87–94
   PubMed Web of Science ®Google Scholar
• Ehrenstein G., Lecar H., Nossal R. The nature of the negative resistance in bimolecular lipid membranes containing excitability-inducing material. J. Gen. Physiol. 1970; 55: 119–133
   PubMed Web of Science ®Google Scholar
• Eilers M., Hwang S., Schatz G. Unfolding and refolding of a purified precursor protein during import into isolated mitochondria. EMBO J. 1988; 7: 1139–1145
   PubMed Web of Science ®Google Scholar
• Ermishkin L. N., Mirzabekov T. A. Redistribution of the electric field within the pore contributes to the voltage-dependence of mitochondrial porin channel. Biochim. Biophys. Acta 1990; 1021: 161–168
   PubMed Web of Science ®Google Scholar
• Fagian M. M., Pereira-da-Silva L., Martins I. S., Vercesi A. E. Membrane protein thiol cross-linking associates with the permeabilization of the inner mitochondrial membrane by Ca2+ plus prooxidants. J. Biol. Chem. 1990; 265: 19955–19960
   PubMed Web of Science ®Google Scholar
• Fasman G. D. Prediction of Protein Structure and the Principles of Protein Conformation. Plenum Press, New York 1990
   Google Scholar
• Feigner P. L., Messer J. L., Wilson J. E. Purification of a hexokinase-binding protein from the outer mitochondrial membrane. J. Biol. Chem. 1979; 254: 4946–4949
   PubMed Web of Science ®Google Scholar
• Fèvre F., Chich J R, Lauquin G. J. M., Henry J P, Thieffry M. Comparison of mitochondrial cationic channels in wild-type and porin-deficient mutant yeast. FEBS Lett. 1990; 262: 201–204
   PubMed Web of Science ®Google Scholar
• Fiek C., Benz R., Roos N., Brdiczka D. Evidence for identity between the hexokinase-binding protein and the mitochondrial porin in the outer membrane of rat liver mitochondria. Biochim. Biophys. Acta 1982; 688: 429–440
   PubMed Web of Science ®Google Scholar
• Forte M., Adelsberger-Mangan D., Colombini M. Purification and characterisation of the voltage-dependent anion channel from the outer mitochondrial membrane of yeast. J. Membr. Biol. 1987; 99: 65–72
   PubMed Web of Science ®Google Scholar
• Forte M., Guy H. R., Mannella C. A. Molecular genetics of the VDAC ion channel: structural model and sequence analysis. J. Bioenerg. Biomembr. 1987; 19: 341–350
   PubMed Web of Science ®Google Scholar
• Freitag H., Neupert W., Benz R. Purification and characterization of a pore protein of the outer mitochondrial membrane from Neurospora crassa. Eur. J. Biochem. 1982; 123: 629–636
   PubMedGoogle Scholar
• Garlid K. D., Beavis A. D. Evidence for the existence of an inner-membrane anion channel in mitochondria. Biochim. Biophys. Acta 1986; 853: 187–204
   PubMed Web of Science ®Google Scholar
• Gillespie L. L. Identification of an outer mitochondrial membrane protein that interacts with a synthetic signal peptide. J. Biol. Chem. 1987; 262: 7939–7942
   PubMed Web of Science ®Google Scholar
• Guo X. W. Cryo-electron microscopy and correlation averaging of frozen-hydrated, polymorphic 2D crystals of the mitochondrial outer membrane channel. Proceedings of the XIIth Congress for Electron Microscopy, L. D. Peachey, D. B. Williams. San Francisco Press, San Francisco 1990; 100–101
   Google Scholar
• Guo X W., Mannella C. A. Classification of projection images of crystalline arrays of the mitochondrial channel, VDAC., embedded in aurothioglucose. Biophys. J. 1992; 63: 418–427
   PubMed Web of Science ®Google Scholar
• Guo X W., Smith P. R., Radermacher M., Mannella C. A. Structure of crystalline VDAC., the voltage-gated channel in the mitochondrial outer membrane. Proceedings of the 50th Annual Meeting of the Electron Microscopy Society of America, G. W. Bailey, J. Bentley, J. A. Small. San Francisco Press, San Francisco 1992; 440–441
   Google Scholar
• Gunter T. E., Pfeiffer D. R. Mechanisms by which mitochondria transport calcium. Am. J. Physiol. 1990; 258: C755–C786
   PubMed Web of Science ®Google Scholar
• Hackenbrock C. R. Chemical and physical fixation of isolated mitochondria in low-energy and high-energy states. Proc. Natl. Acad. Sci. U.S.A. 1968; 61: 598–605
   PubMed Web of Science ®Google Scholar
• Halestrap A. P., Davidson A. M. Inhibition of Ca2+induced large-amplitude swelling of liver and heart mitochondria by cyclosporin is probably caused by the inhibitor binding to mitochondrial-matrix peptidyl-prolyl cis-trans isomerase and preventing it interacting with the adenine nucleotide translocase. Biochem. J. 1990; 268: 153–160
   PubMed Web of Science ®Google Scholar
• Hamill O. P., Marty A., Neher E., Sakmann B., Sigworth F. J. Improved patch-clamp techniques for high resolution current recording from cells and cell-free patches. Pflügers Arch. 1981; 391: 85–100
   PubMed Web of Science ®Google Scholar
• Hartl F U., Neupert W. Protein sorting to mitochondria: evolutionary conservations of folding and assembly. Science 1990; 247: 930–938
   PubMed Web of Science ®Google Scholar
• Haworth R. A., Hunter D. R. The Ca2+-induced membrane transition in mitochondria. Arch. Biochem. Biophys. 1979; 195: 460–467
   PubMed Web of Science ®Google Scholar
• Henry J. P., Chich J. F., Goldshmidt D., Thieffry M. Blockage of a mitochondrial cationic channel by an addressing peptide: an electrophysiological study. J. Membr. Biol. 1989; 112: 139–147
   PubMed Web of Science ®Google Scholar
• Hille B. Ionic Channels of Excitable Membranes. Sinauer Associates In., Sunderland, MA 1984
   Google Scholar
• Hines V., Brandt A., Griffiths G., Horstmann H., Brütsch H., Schatz G. Protein import into yeast mitochondria is accelerated by the outer membrane protein MAS70. EMBO J. 1990; 9: 3191–3200
   PubMed Web of Science ®Google Scholar
• Holden M. J., Colombini M. The mitochondrial membrane channel, VDAC, is modulated by a soluble protein. FEBS Lett. 1988; 241: 105–109
   PubMed Web of Science ®Google Scholar
• Hwang S. T., Wachter C., Schatz G. Protein import into the yeast mitochondrial matrix. J. Biol. Chem. 1991; 266: 21083–21089
   PubMed Web of Science ®Google Scholar
• Inoue I., Nagase H., Kishi K., Higuti T. ATP-sensitive K+ channel in the inner mitochondrial membrane. Nature 1991; 352: 244–247
   PubMed Web of Science ®Google Scholar
• Jacobus W. E. Respiratory control and the integration of heart high-energy phosphate metabolism by mitochondrial creatine kinase. Annu. Rev. Physiol. 1985; 47: 707–725
   PubMed Web of Science ®Google Scholar
• Jacobus W. E., Moreadith R. W., Vandegaer K. M. Control of heart oxidative phosphorylation by creatine kinase in mitochondrial membranes. Ann. N.Y. Acad. Sci. U.S.A. 1983; 414: 73–89
   PubMed Web of Science ®Google Scholar
• Jürgens L., Ilsemann P., Kratzin H. D., Hesse D., Eckart K., Thinnes F. P., Hilschmann N. Studies on human porin IV. The primary structures of “Porin 31HM” purified from human skeletal muscle membranes and of “Porin 31HL” derived from human B lymphocyte membranes are identical. Biol. Chem. Hoppe-Seyler 1991; 372: 455–463
   PubMed Web of Science ®Google Scholar
• Kabir F., Nelson B. D. Hexokinase bound to rat brain mitochondria uses externally added ATP more efficiently than internally generated ATP. Biochim. Biophys. Acta 1991; 1057: 147–150
   PubMed Web of Science ®Google Scholar
• Kayser H., Kratzin H. D., Thinnes F. P., Götz H., Schmidt W. E., Eckart K., Hilschmann N. Zur Kenntnis der Porine des Menschen II. Charakterisierung und Primärstruktur eines 31-kDa-Porins aus menschlichen B-Lymphozyten (Porin 31HL). Biol. Chem. Hoppe-Seyler 1989; 370: 1265–1268
   PubMedGoogle Scholar
• Kinnally K., Tedeschi H., Mannella C. A. Evidence for a novel voltage-activated channel in the outer mitochondrial membrane. FEBS Lett. 1987; 226: 83–87
   PubMed Web of Science ®Google Scholar
• Kinnally K. W., Campo M. L., Tedeschi H. Mitochondrial channel activity studied by patch-clamping mitoplasts. J. Bioenerg, Biomembr. 1989; 21: 497–506
   PubMed Web of Science ®Google Scholar
• Kinnally K. W., Antonenko Y. N., Zorov D. B. Modulation of the inner mitochondrial channel activity. J. Bioenerg. Biomembr. 1992; 24: 99–110
   PubMed Web of Science ®Google Scholar
• Kinnally K. W., Tedeschi H., Mannella C. A., Frisch H. L. Kinetics of voltage-induced conductance increases in the outer mitochondrial membrane. Biophys. J. 1989; 55: 1205–1213
   PubMed Web of Science ®Google Scholar
• Kinnally K. W., Zorov D., Antonenko Y., Perini S. Calcium modulation of mitochondrial inner membrane channel activity. Biochem. Biophys. Res. Comm. 1991; 176: 1183–1188
   PubMed Web of Science ®Google Scholar
• Kleene R., Pfanner N., Pfaller R., Link T. A., Sebald W., Neupert W., Tropschug M. Mitochondrial porin of Neurospora crassa: cDNA cloning, in vitro expression and import into mitochondria. EMBO J. 1987; 6: 2627–2633
   PubMed Web of Science ®Google Scholar
• Klitsch T., Siemen D. Inner mitochondrial membrane anion channel is present in brown adipocytes but is not identical to the uncoupling protein. J. Membr. Biol. 1991; 122: 69–75
   PubMed Web of Science ®Google Scholar
• Knoll G., Brdiczka D. Changes in freeze-fractured mitochondrial membranes correlated to their energetic state. Dynamic interactions of the boundary membranes. Biochim. Biophys. Acta 1983; 733: 102–110
   PubMed Web of Science ®Google Scholar
• Kolhardt M., Fichtner H. Block of single cardiac Na+ channels by antiarrhythmic drugs: the effect of amiodarone, propafenone and diprafenone. J. Membr. Biol. 1988; 102: 105–119
   PubMed Web of Science ®Google Scholar
• König T., Stipani I., Horvath I., Palmieri F. Inhibition of mitochondrial substrate anion translocators by a synthetic amphipathic polyanion. J. Bioenerg. Biomembr. 1982; 14: 297–305
   PubMed Web of Science ®Google Scholar
• König T., Kocsis B., Meszaros L., Nahm K., Zoltan S., Horvath I. Interaction of a synthetic polyanion with rat liver mitochondria. Biochim. Biophys. Acta 1977; 462: 380–389
   PubMed Web of Science ®Google Scholar
• König U., Götz H., Walter G., Babel D., Hohmeier H E., Thinnes F. P., Hilschmann N. Zur Kenntnis der Porine des Menschen V. Die Plasmalemmständigkeit von “Porin 31HL” ist keine Folge einer Zell-Transformation. Biol. Chem. Hoppe-Seyler 1991; 372: 565–572
   PubMedGoogle Scholar
• Kottke M., Adam V., Wallimann T., Nalam V. K., Brdiczka D. Location and regulation of octameric mitochondrial creatine kinase in contact sites. Biochim. Biophys. Acta 1991; 1061: 215–225
   PubMed Web of Science ®Google Scholar
• Kottke M., Adam V., Riesinger I., Bremm G., Bosch W., Brdiczka D., Sandri G., Panfili E. Mitochondrial boundary membrane contact sites in brain: points of hexokinase and creatine kinase location, and control of Ca2+ transport. Biochim. Biophys. Acta 1988; 935: 87–102
   PubMed Web of Science ®Google Scholar
• Lemmens M., Verheyden K., Van Veldhoven P., Vereecke J., Mannaerts G. P., Carmeliet E. Singlechannel analysis of a large conductance channel in peroxisomes from rat liver. Biochim. Biophys. Acta 1989; 984: 351–359
   PubMed Web of Science ®Google Scholar
• Lin A., Krockmalnic G., Penman S. Imaging cytoskeleton-mitochondrial membrane attachments by embedment-free electron microscopy of saponin-extracted cells. Proc. Natl. Acad. Sci. U.S.A. 1990; 87: 8565–8569
   PubMed Web of Science ®Google Scholar
• Lindén M., Gellerfors P. Hydrodynamic properties of porin isolated from outer membrane of rat liver mitochondria. Biochim. Biophys. Acta 1983; 736: 125–129
   PubMed Web of Science ®Google Scholar
• Lindén M., Gellerfors P., Nelson B. D. Purification of a protein having pore forming activity from the rat liver mitochondrial outer membrane. Biochem. J. 1982a; 208: 77–82
   PubMed Web of Science ®Google Scholar
• Lindén M., Gellerfors P., Nelson B. D. Pore protein and the hexokinase-binding protein from the outer membrane of rat liver mitochondria are identical. FEES Lett. 1982b; 141: 189–192
   PubMed Web of Science ®Google Scholar
• Lindén M., Andersson G., Gellerfors P., Nelson B. D. Subcellular distribution of rat liver porin. Biochim. Biophys. Acta 1984; 770: 93–96
   PubMed Web of Science ®Google Scholar
• Lindén M., Nelson B. D., Loncar D., Leterrier J. F. Studies on the interaction between mitochondria and the cytoskeleton. J. Bioenerg. Biomembr. 1989; 21: 507–518
   PubMed Web of Science ®Google Scholar
• Liu M. Y., Colombini M. Voltage gating of the mitochondrial outer membrane channel VDAC is regulated by a very conserved protein. Am. J. Physiol. 1991; 260: C371–C374
   PubMed Web of Science ®Google Scholar
• Liu M. Y., Colombini M. A soluble mitochondrial protein increases the voltage dependence of the mitochondrial channel, VDAC. J. Bioenerg. Biomembr. 1992a; 24: 41–46
   PubMed Web of Science ®Google Scholar
• Liu M. Y., Colombini M. Regulation of mitochondrial respiration by controlling the permeability of the outer membrane through the mitochondrial channel, VDAC. Biochim. Biophys. Acta 1992b; 1098: 255–260
   PubMed Web of Science ®Google Scholar
• Ludwig O., Benz R., Schultz J. E. Porin of Paramecium mitochondria isolation, characterization and ion selectivity of the closed state. Biochim. Biophys. Acta 1989; 978: 319–327
   PubMed Web of Science ®Google Scholar
• Ludwig O., De Pinto V., Palmieri F., Benz R. Pore formation by the mitochondrial porin of rat brain in lipid bilayer membranes. Biochim. Biophys. Acta 1986; 860: 268–276
   PubMed Web of Science ®Google Scholar
• Ludwig O., Krause J., Hay R., Benz R. Purification and characterization of the pore forming protein of yeast mitochondrial outer membrane. Eur. Biophys. J. 1988; 15: 269–276
   PubMed Web of Science ®Google Scholar
• Mangan P. S., Colombini M. Ultrasteep voltage dependence in a membrane channel. Proc. Natl. Acad. Sci. U.S.A. 1987; 84: 4896–4900
   PubMed Web of Science ®Google Scholar
• Mannella C. A. Structure of the outer mitochondrial membrane: analysis of X-ray diffraction from the plant membrane. Biochim. Biophys. Acta 1981; 645: 33–40
   PubMed Web of Science ®Google Scholar
• Mannella C. A. Structure of the outer mitochondrial membrane: ordered arrays of porelike subunits in outer-membrane fractions from Neurospora crassa mitochondria. J. Cell. Biol. 1982; 94: 680–687
   PubMed Web of Science ®Google Scholar
• Mannella C. A. Phospholipase-induced crystallization of channels in mitochondrial outer membranes. Science 1984; 224: 165–166
   PubMed Web of Science ®Google Scholar
• Mannella C. A. Mitochondrial outer membrane channel (VDAC., porin). Two-dimensional crystals from Neurospora. Meth. Enzymol. 1986; 125: 595–610
   PubMed Web of Science ®Google Scholar
• Mannella C. A. Electron microscopy and image analysis of the mitochondrial outer membrane channel, VDAC. J. Bioenerg. Biomembr. 1987; 19: 329–340
   PubMed Web of Science ®Google Scholar
• Mannella C. A. Lateral segregation of sterol and channel proteins in the mitochondrial outer membrane induced by phospholipase A2: evidence from negative-stain electron microscopy using filipin. J. Ultrastruct. Mol. Struct. Res. 1988; 98: 212–216
   PubMedGoogle Scholar
• Mannella C. A. Structure of the mitochondrial outer membrane channel derived from electron microscopy of 2D crystals. J. Bioenerg. Biomembr. 1989; 21: 427–437
   PubMed Web of Science ®Google Scholar
• Mannella C. A. Structural analysis of the mitochondrial pores. Experientia 1990; 46: 137–145
   PubMedGoogle Scholar
• Mannela C. A., Bonner W. D., Jr. X-ray diffraction from oriented outer mitochondrial membranes. Biochim. Biophys. Acta 1975a; 413: 226–233
   PubMed Web of Science ®Google Scholar
• Mannella C. A., Bonner W. D., Jr. Biochemical characteristics of the outer membranes of plant mitochondria. Biochim. Biophys. Acta 1975b; 413: 213–225
   PubMed Web of Science ®Google Scholar
• Mannella C. A., Frank J. Effects of divalent metal ions and chelators on the structure of outer mitochondrial membranes from Neurospora crassa. Biophys. J. 1982; 37: 3–4
   PubMed Web of Science ®Google Scholar
• Mannella C. A., Colombini M. Evidence that the crystalline arrays in the outer membrane of Neurospora mitochondria are composed of the voltage-dependent channel protein. Biochim. Biophys. Acta 1984; 774: 206–214
   PubMed Web of Science ®Google Scholar
• Mannella C. A., Frank J. Negative staining characteristics of arrays of mitochondrial pore protein: use of correspondence analysis to classify different staining patterns. Ultramicroscopy 1984; 13: 93–102
   PubMed Web of Science ®Google Scholar
• Mannella C. A., Guo X. W. Interaction between the VDAC channel and a polyanionic effector. An electron microscopic study. Biophys. J. 1990; 57: 23–31
   PubMed Web of Science ®Google Scholar
• Mannella C. A., Colombini M., Frank J. Structural and functional evidence for multiple channel complexes in the outer membrane of Neurospora crassa mitochondria. Proc. Natl. Acad. Sci. U.S.A. 1983; 80: 2243–2247
   PubMed Web of Science ®Google Scholar
• Mannella C. A., Radermacher M., Frank J. Three-dimensional structure of mitochondrial outer-membrane channels from fungus and liver. Proceedings of the 42nd Annual Meeting of the Electron Microscopy Society of America, G. W. Bailey. San Francisco Press, San Francisco 1984; 644–645
   Google Scholar
• Mannella C. A., Ribeiro A., Frank J. Structure of the channels in the outer mitochondrial membrane. Electron microscopic studies of the periodic arrays induced by phospholipase A2 treatment of the Neurospora membrane. Biophys. J. 1986; 49: 307–318
   PubMed Web of Science ®Google Scholar
• Mannella C. A., Ribeiro A., Frank J. Cytochrome c binds to lipid domains in arrays of mitochondrial outer membrane channels. Biophys. J. 1987; 51: 221–226
   PubMed Web of Science ®Google Scholar
• Mannella C. A., Guo X. W., Cognon B. Diameter of the mitochondrial outer membrane channel: evidence from electron microscopy of frozen-hydrated membrane crystals. FEBS Lett. 1989; 253: 231–234
   Web of Science ®Google Scholar
• Mannella C. A., Forte M., Colombini M. Toward the molecular structure of the mitochondrial channel, VDAC. J. Bioenerg. Biomembr. 1992; 24: 7–19
   PubMed Web of Science ®Google Scholar
• Mannella C. A., Guo X. W., Dias J. Binding of a synthetic targeting peptide to a mitochondrial channel protein. J. Bioenerg. Biomembr. 1992; 24: 55–61
   PubMed Web of Science ®Google Scholar
• Mannella C. A., Ribeiro A., Cognon B., D' Arcan-gelis D. Structure of paracrystalline arrays on the outer membranes of rat-liver and rat-heart mitochondria. J. Struct. Biol. 1992; 108: 227–237
   PubMed Web of Science ®Google Scholar
• Mazzanti M., DeFelice L. J., Cohen J., Malter H. Ion channels in the nuclear envelope. Nature 1990; 343: 764–767
   PubMed Web of Science ®Google Scholar
• McEnery M. W. The mitochondrial benzodiazepine receptor: evidence for association with the voltage-dependent anion channel (VDAC). J. Bioenerg. Biomembr. 1992; 24: 63–69
   PubMed Web of Science ®Google Scholar
• McEnery M. W., Snowman A. M., Trifiletti R. R., Snyder S. H. Isolation of the mitochondrial benzodiazepine receptor: association with the voltage-dependent anion channel and the adenine nucleotide carrier. Proc. Natl. Acad. Sci. U.S.A. 1992; 89: 3170–3174
   PubMed Web of Science ®Google Scholar
• Meves H., Pichon Y. The effect of internal and external 4-aminopyridine on the potassium currents in intracellularly perfused squid giant axons. J. Physiol. Lond. 1977; 268: 511–532
   Google Scholar
• Mihara K., Sato R. Molecular cloning and sequencing of cDNA for yeast porin, an outer mitochondrial membrane porin: a search for targeting signal in the primary structure. EMBO J. 1985; 4: 769–774
   PubMed Web of Science ®Google Scholar
• Mironova G. D., Fedotcheva N. I., Makarov P. R., Pronevich L. A., Mironov G. P. A protein of the bovine heart mitochondria inducing channel potassium conductivity in bilayer lipid membranes. Biofizika 1981; 26: 451–457
   PubMed Web of Science ®Google Scholar
• Mirzabekov T. A., Ermishkin L. N. The gate of mitochondrial porin channel is controlled by a number of negative and positive charges. FEBS Lett. 1989; 249: 375–378
   PubMed Web of Science ®Google Scholar
• Mirzabekov T. A., Ballarin C., Nicolini M., Zatta P., Sorgato M. C. Reconstitution of the native mitochondrial outer membrane in planar bilayers. Comparison with the outer membrane in a patch pipette and effect of aluminium compounds. J. Membr. Biol. 1993, in press
   PubMed Web of Science ®Google Scholar
• Mitchell P. Chemiosmotic coupling in oxidative and photosynthetic phosphorylation. Biol. Rev. 1966; 41: 445–502
   PubMed Web of Science ®Google Scholar
• Montal M., Mueller P. Formation of bimolecular membranes from lipid monolayers and a study of their electrical properties. Proc. Natl. Acad. Sci. U.S.A. 1972; 69: 3561–3566
   PubMed Web of Science ®Google Scholar
• Moran O., Sorgato M. C. High-conductance pathways in mitochondrial membranes. J. Bioenerg. Biomembr. 1992; 24: 91–98
   PubMed Web of Science ®Google Scholar
• Moran O., Sandri G., Panfili E., Stühmer W., Sorgato M. C. Electrophysiological characterization of contact sites in brain mitochondria. J. Biol. Chem. 1990; 265: 908–913
   PubMed Web of Science ®Google Scholar
• Moran O., Sciancalepore M., Sandri G., Panfili E., Bassi R., Ballarin C., Sorgato M. C. Ionic permeability of the mitochondrial outer membrane. Eur. Biophys. J. 1992; 20: 311–319
   PubMed Web of Science ®Google Scholar
• Mueller P., Rudin D. O., Tien H. T., Wescott W. C. Methods for the formation of single bimolecular lipid membranes in aqueous solution. J. Phys. Chem. 1963; 67: 534–535
   Web of Science ®Google Scholar
• Nakashima R. A. Hexokinase-binding properties of the mitochondrial channel, VDAC: inhibition by DCCD and location of putative DCCD-binding sites. J. Bioenerg. Biomembr. 1989; 21: 461–470
   PubMed Web of Science ®Google Scholar
• Nakashima R. A., Mangan P. S., Colombini M., Pedersen P. L. Hexokinase receptor complex in hepatoma mitochondria: evidence from DCCD-labeling studies for the involvement of the pore-forming protein VDAC. Biochemistry 1986; 25: 1015–1021
   PubMed Web of Science ®Google Scholar
• Nicholls D. G., Cunningham S. A., Rial E. The bioenergetic mechanism of brown adipose tissue ther-mogenesis. Brown Adipose Tissue, P. Trayhurn, D. G. Nicholls. Edwart Arnolds, London 1986; 52–85
   Google Scholar
• Nishimura M., Follmer C. H., Singer D. H. Amiodarone blocks calcium current in single guinea pig ventricular myocytes. J. Pharmacol. Exp. Ther. 1989; 251: 650–659
   PubMed Web of Science ®Google Scholar
• O'Brien R. L., Brierley G. Compartmentation of heart mitochondria. I. Permeability characteristics of beef heart mitochondria. J. Biol. Chem. 1965; 240: 4527–4531
   PubMed Web of Science ®Google Scholar
• Ohlendieck K., Riesinger I., Adams V., Krause J., Brdiczka D. Enrichment and biochemical characterization of boundary membrane contact sites from rat-liver mitochondria. Biochim. Biophys. Acta 1986; 860: 672–689
   PubMed Web of Science ®Google Scholar
• Paliwal R., Costa G., Diwan J. J. Purification and patch clamp analysis of a 40 pS channel from rat liver mitochondria. Biochemistry 1992; 31: 2223–2229
   PubMed Web of Science ®Google Scholar
• Palmieri F., De Pinto V. Purification and properties of the voltage-dependent anion channel of the outer mitochondrial membrane. J. Bioenerg. Biomembr. 1989; 21: 417–425
   PubMed Web of Science ®Google Scholar
• Parry D. M., Pedersen P. L. Intracellular localization of rat kidney hexokinase. Evidence for an association with low density mitochondria. J. Biol. Chem. 1984; 259: 8917–8923
   PubMed Web of Science ®Google Scholar
• Parry D. M., Pedersen P. L. Glucose catabolism in brain. Intracellular localization of hexokinase. J. Biol. Chem. 1990; 265: 1059–1066
   PubMed Web of Science ®Google Scholar
• Parson D. F., Bonner W. D., Verboon J. G. Electron microscopy of isolated plant mitochondria and plastids using both thin-section and negative staining techniques. Can. J. Bot. 1965; 43: 647–655
   Google Scholar
• Parson D. F., Williams G. R., Chance B. Characteristics of isolated and purified preparations of the outer and inner membranes of mitochondria. Ann. N. Y. Acad. Sci. 1966; 137: 643–666
   PubMed Web of Science ®Google Scholar
• Peng S., Blachly-Dyson E., Colombini M., Forte M. Inferring the structural changes in VDAC., associated with the channel's gating process, through site-directed mutagenesis. Biophys. J. 1991; 59: 215a
   Google Scholar
• Peng S., Blachly-Dyson E., Forte M., Colombini M. Large scale rearrangement of protein domains is associated with voltage gating of the VDAC channel. Biophys. J. 1992a; 62: 1–9
   Google Scholar
• Peng S., Blachly-Dyson E., Colombini M., Forte M. Determination of the number of polypeptide subunits in a functional VDAC channel from Saccharomyces cerevisiae. J. Bioenerg. Biomembr. 1992b; 24: 27–32
   PubMed Web of Science ®Google Scholar
• Petronilli V., Szabo' I., Zoratti M. The inner mitochondrial membrane contains ion-conducting channels similar to those found in bacteria. FEBS Lett. 1989; 259: 137–143
   PubMed Web of Science ®Google Scholar
• Pfaff E., Klingenberg M., Ritt E., Vogell W. Korrelation des unspezifisch permeablen mitochondrialen Raumes mit dem “Intermembrane-Raum”. Eur. J. Biochem. 1968; 5: 222–232
   PubMedGoogle Scholar
• Pfaller R., Freitag H., Harmey M. A., Benz R., Neupert W. A water-soluble form of porin from the mitochondrial outer membrane of Neurospora crassa. J. Biol. Chem. 1985; 260: 8188–8193
   PubMed Web of Science ®Google Scholar
• Pfanner N., Neupert W. The mitochondrial protein import apparatus. Annu. Rev. Biochem. 1990; 59: 331–353
   PubMed Web of Science ®Google Scholar
• Pfanner N., Haiti F U., Guiard B., Neupert W. Mitochondrial precursor proteins are imported through a hydrophilic membrane environment. Eur. J. Biochem. 1987; 169: 289–293
   PubMedGoogle Scholar
• Pfanner N., Rassow J., van der Klei I. J., Neupert W. A dynamic model of the mitochondrial protein import machinery. Cell 1992; 68: 999–1002
   PubMed Web of Science ®Google Scholar
• Rahamimoff R., DeRiemer S. A., Sakmann B., Stadler H., Yakir N. Ion channels in synaptic vesicles from Torpedo electric organ. Proc. Natl. Acad. Sci. U.S.A. 1988; 85: 5310–5314
   PubMed Web of Science ®Google Scholar
• Rassow J., Guiard B., Wienhues U., Herzog V., Hartl F U., Neupert W. Translocation arrest by reversible folding of a precursor protein imported into mitochondria. A means to quantitate translocation contact sites. J. Cell. Biol. 1989; 109: 1421–1428
   PubMed Web of Science ®Google Scholar
• Reizman H., Hay R., Gasser S., Daum G., Schneider G., Witte C., Schatz G. The outer membrane of yeast mitochondria: isolation of outside-out sealed vesicles. EMBO J. 1983; 2: 1105–1111
   PubMed Web of Science ®Google Scholar
• Roos N., Benz R., Brdiczka D. Identification and characterization of the pore-forming protein in the outer membrane of rat liver mitochondria. Biochim. Biophys. Acta 1982; 686: 204–214
   PubMed Web of Science ®Google Scholar
• Sandri G., Siagri M., Panfili E. Influence of Ca2+ on the isolation from rat brain mitochondria of a fraction enriched of boundary membrane contact sites. Cell Calcium 1988; 9: 908–913
   Google Scholar
• Schein S. J., Colombini M., Finkelstein A. Reconstitution in planar lipid bilayers of a voltage-dependent anion-selective channel obtained from Paramecium mitochondria. J. Membr. Biol. 1976; 30: 99–120
   PubMed Web of Science ®Google Scholar
• Seeman P. The membrane actions of anesthetics and tranquillizers. Pharmacol. Res. 1972; 24: 583–655
   Google Scholar
• Simon S. M., Blobel G. A protein-conducting channel in the endoplasmic reticulum. Cell 1991; 65: 371–380
   PubMed Web of Science ®Google Scholar
• Singer S. J., Maher P. A., Yaffe M. P. On the translocation of proteins across membranes. Proc. Natl. Acad. Sci. U.S.A. 1987; 84: 1015–1019
   PubMed Web of Science ®Google Scholar
• Skulachev V. P. Power transmission along biological membranes. J. Membr. Biol. 1990; 114: 97–112
   PubMed Web of Science ®Google Scholar
• Slater E. C. The mechanism of action of the respiratory inhibitor, antimycin. Biochim. Biophys. Acta 1973; 301: 129–154
   PubMed Web of Science ®Google Scholar
• Smack D., Colombini M. Voltage-dependent channels found in the membrane fraction of corn mitochondria. Plant Physiol. 1985; 79: 1094–1097
   PubMed Web of Science ®Google Scholar
• Snyder S. H., McEnery M. W., Verma A. Molecular mechanisms of peripheral benzodiazepine receptors. Neurochem. Res. 1990; 15: 119–123
   PubMed Web of Science ®Google Scholar
• Söllner T., Griffiths G., Pfaller R., Pfanner N., Neupert W. MOM 19, an import receptor for mitochondrial precursor proteins. Cell 1989; 59: 1061–1070
   PubMed Web of Science ®Google Scholar
• Söllner T., Pfaller R., Griffiths G., Pfanner N., Neupert W. A mitochondrial import receptor for the ADP/ATP carrier. Cell 1990; 62: 107–115
   PubMed Web of Science ®Google Scholar
• Söllner T., Rassow J., Wiedmann M., Schloßmann J., Keil P., Neupert W., Pfanner N. Mapping of the protein import machinery in the mitochondrial outer membrane by crosslinking of translocation intermediates. Nature 1991; 355: 84–87
   Web of Science ®Google Scholar
• Sorgato M. C., Keller B. U., Stühmer W. Patchclamping of the inner mitochondrial membrane reveals a voltage-dependent ion channel. Nature 1987; 330: 498–500
   PubMed Web of Science ®Google Scholar
• Sorgato M. C., Moran O., De Pinto V., Keller B. U., Stühmer W. Further investigation on the high-conductance ion channel of the inner membrane of mitochondria. J. Bioenerg. Biomembr. 1989; 21: 485–496
   PubMed Web of Science ®Google Scholar
• Stanfield P. R. The differential effects of the tetraethy-lammonium anel zinc ions on the resting conductance of frog skeletal muscle. J. Physiol. Lond. 1970; 209: 231–256
   Google Scholar
• Steger H. F., Söllner T., Kiebler M., Dietmeier K. A., Pfaller R., Trülzsch K. S., Tropschug M., Neupert W., Pfanner N. Import of ADP/ATP carrier into mitochondria: two receptors act in parallel. J. Cell. Biol. 1990; 111: 2353–2363
   PubMed Web of Science ®Google Scholar
• Stuart R. A., Nicholson D. W., Neupert W. Early steps in mitochondrial protein import: receptor functions can be substituted by the membrane insertion activity of apocytochrome C. Cell 1990; 60: 31–43
   PubMed Web of Science ®Google Scholar
• Stühmer W., Keller B., Lippe G., Sorgato M. C. The outer and inner membranes of mice liver giant mitochondria can be patch clamped: high conductance ion channels are present in both membranes. Hormones and Cell Regulation, J. Nuez, J. E. Drumont, E. Carafoli. INSERM/John Libbey Eurotext Ltd., London 1988; 165: 89–99
   Google Scholar
• Sturgess N. C., Ashford M. L. J., Cook D. L., Hales C. N. The sulphonylurea receptor may be an ATP-sensitive potassium channel. Lancet 1985; 8453: 474–475
   Google Scholar
• Suzuki K. Giant hepatic mitochondria: production in mice fed with cuprizone. Science 1969; 163: 81–82
   PubMed Web of Science ®Google Scholar
• Szabo' I., Zoratti M. The giant channel of the inner mitochondrial membrane is inhibited by cyclosporin A. J. Biol. Chem. 1991; 266: 3376–3379
   PubMed Web of Science ®Google Scholar
• Szabo' I., Zoratti M. The mitochondrial megachannel is the permeability transition pore. J. Bioenerg. Biomembr. 1992; 24: 111–117
   PubMed Web of Science ®Google Scholar
• Szabo' I., Bernardi P., Zoratti M. Modulation of the mitochondrial megachannel by divalent cations and protons. J. Biol. Chem. 1992; 267: 2940–2946
   PubMed Web of Science ®Google Scholar
• Tandler B., Hoppel C. L. Division of giant mitochondria during recovery from cuprizone intoxication. J. Cell. Biol. 1973; 56: 266–272
   PubMed Web of Science ®Google Scholar
• Tedeschi H., Mannella C. A., Bowman C. L. Patch clamping of the outer mitochondrial membrane. J. Membr. Biol. 1987; 97: 21–29
   PubMed Web of Science ®Google Scholar
• Tedeschi H., Kinnally K. W., Mannella C. A. Properties of channels in the mitochondrial outer membrane. J. Bioenerg. Biomembr. 1989; 21: 451–459
   PubMed Web of Science ®Google Scholar
• Thieffry M., Chich J R, Goldshmidt D., Henry J P. Incorporation in lipid bilayers of a large conductance cationic channel from mitochondrial membranes. EMBO J. 1988; 7: 1449–1454
   PubMed Web of Science ®Google Scholar
• Thieffry M., Neyton J., Pelleschi M., Fevre F., Henry J P. Properties of the mitochondrial peptidesensitive cationic channel studied in planar bilayers and patches of giant liposomes. Biophys. J. 1992; 63: 333–339
   PubMed Web of Science ®Google Scholar
• Thinnes F. P. Evidence for extra-mitochondrial localization of the VDAC/porin channel in eukaryotic cells. J. Bioenerg. Biomembr. 1992; 24: 71–75
   PubMed Web of Science ®Google Scholar
• Thinnes F. P., Schmid A., Benz R., Hilschmann N. Studies on human porin. III. Does the voltage-dependent anion channel “Porin 31HL” form part of the chloride channel complex, which is observed in different cells and thought to be affected in cystic fibrosis. Biol. Chem. Hoppe-Seyler 1990; 371: 1047–1050
   PubMed Web of Science ®Google Scholar
• Thinnes F. P., Götz H., Kayser H., Benz R., Schmidt W. E., Kratzin H. D., Hilschmann N. ZurKenntnis der Porine des Menschen I. Reinigung eines Porins aus menschlichen B-Lymphozyten (Porin 31HL) und sein topochemischer Nachweis auf dem Plasmalemm der Herkunftszelle. Biol. Chem. Hoppe-Seyler 1989; 370: 1253–1264
   PubMed Web of Science ®Google Scholar
• Thomas L., Kocsis E., Colombini M., Erbe E., Trus B. L., Steven A. C. Surface topography and molecular stoichiometry of the mitochondrial channel, VDAC., in crystalline arrays. J. Struct. Biol. 1991; 106: 161–171
   PubMed Web of Science ®Google Scholar
• Thomas L., Hartung K., Langosch D., Rehm H., Bamberg E., Franke W. W., Betz H. Identification of synaptophysin as a hexameric channel protein of the synaptic vesicle membrane. Science 1988; 242: 1050–1053
   PubMed Web of Science ®Google Scholar
• Towbin J. A., Minter M., Brdiczka D., Adams V., De Pinto V., Palmieri F., McCabe E. R. B. Demonstration and characterization of human cardiac porin: a voltage-dependent channel involved in adenine nucleotide movement across the outer mitochondrial membrane. Biochem. Med. Metab. Biol. 1989; 42: 161–169
   PubMedGoogle Scholar
• van Keulen M. A., Berden J. A. Antimycin binds to a small subunit of the ubiquinol: cytochrome c oxido-reductase. Biochim. Biophys. Acta 1985; 808: 33–38
   Google Scholar
• Van Venetië R., Verkleij A. J. Possible role of nonbilayer lipids in the structure of mitochondria. A freezefracture electron microscopic study. Biochim. Biophys. Acta 1982; 692: 397–405
   PubMedGoogle Scholar
• Verdoorn T. A., Draguhn A., Ymer S., Seeburg P. H., Sakmann B. Functional properties of recombinant rat GABAA receptors depend upon subunit composition. Neuron 1990; 4: 919–928
   PubMed Web of Science ®Google Scholar
• Vestweber D., Schatz G. DNA-protein conjugates can enter mitochondria via the protein import pathway. Nature 1989; 338: 170–172
   PubMed Web of Science ®Google Scholar
• Vestweber D., Brunner J., Baker A., Schatz G. A 42-K outer-membrane protein is a component of the yeast mitochondrial protein import site. Nature 1989; 341: 205–209
   PubMed Web of Science ®Google Scholar
• Wallimann T., Wyss M., Brdiczka D., Nicolay K., Eppenberger H. M. Intracellular compartmentation, structure and function of creatine kinase isoenzymes in tissues with high and fluctuating energy demands: the “phosphocreatine circuit” for cellular energy homeostasis. Biochem. J. 1992; 281: 21–40
   PubMed Web of Science ®Google Scholar
• Walker J. E., Arizmendi J. M., Dupuis A., Fearnley I. M., Finel M., Medd S. M., Pilkington S. J., Run-swick M. J., Skehel J. M. Sequences of twenty subunits of NADH:ubiquinone oxidoreductase from bovine heart mitochondria. Application of a novel strategy for sequencing proteins using the polymerase chain reaction. J. Molec. Biol. 1992; 226: 1051–1072
   PubMed Web of Science ®Google Scholar
• Weiler U., Riesinger I., Knoll G., Brdiczka D. The regulation of mitochondrial-bound hexokinases in the liver. Biochem. Med. 1985; 33: 223–235
   PubMedGoogle Scholar
• Weiss M. S., Kreusch A., Schiltz E., Nestel U., Welte W., Weckesser J., Schulz G. E. The structure of porin from Rhodobacler capsulatus at 1.8 Å resolution. FEBS Lett. 1991; 280: 379–382
   PubMed Web of Science ®Google Scholar
• Werkheiser W. C., Bartley W. The study of steady state concentrations of internal solutes of mitochondria by rapid centrifugal transfer to a fixation medium. Biochem. J. 1957; 66: 79–91
   PubMed Web of Science ®Google Scholar
• Wojtczak L., Zaluska H. On the permeability of the outer mitochondrial membrane to cytochrome c. I. Studies on whole mitochondria. Biochim. Biophys. Acta 1969; 193: 64–72
   PubMed Web of Science ®Google Scholar
• Wunder U. R., Colombini M. Patch clamping VDAC in liposomes containing whole mitochondrial membranes. J. Membr. Biol. 1991; 123: 83–91
   PubMed Web of Science ®Google Scholar
• Yang X C., Sachs F. Block of stretch-activated ion channels in Xenopus oocytes by gadolinium and calcium ions. Science 1989; 243: 1068–1071
   PubMed Web of Science ®Google Scholar
• Zalman L. S., Nikaido H., Kagawa Y. Mitochondrial outer membrane contains a protein producing nonspecific diffusion channels. J. Biol. Chem. 1980; 255: 1771–1774
   PubMed Web of Science ®Google Scholar
• Zhang D W., Colombini M. Inhibition by aluminium hydroxide of the voltage-dependent closure of the mitochondrial channel, VDAC. Biochim. Biophys. Acta 1989; 991: 68–78
   PubMed Web of Science ®Google Scholar
• Zhang D W., Colombini M. Group IIIA-metal hydroxides indirectly neutralize the voltage sensor of the voltage-dependent mitochondrial channel, VDAC., by interacting with a dynamic binding site. Biochim. Biophys. Acta 1990; 1025: 127–134
   PubMed Web of Science ®Google Scholar
• Zimmerberg J., Parsegian V. A. Polymer inaccessible volume changes during opening and closing of a voltage-dependent ionic channel. Nature 1986; 323: 36–39
   PubMed Web of Science ®Google Scholar
• Zorov D. B., Kinnally K. W., Tedeschi H. Voltage activation of the heart inner mitochondrial membrane channel. J. Bioenerg. Biomembr. 1992; 24: 119–124
   PubMed Web of Science ®Google Scholar
• Zorov D. B., Kinnally K. W., Perini S., Tedeschi H. Multiple conductance levels in rat heart inner mitochondrial membranes studied by patch clamp. Biochim. Biophys. Acta 1992; 1105: 263–270
   PubMed Web of Science ®Google Scholar