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Volumn 45, Issue 2, 1996, Pages 113-126

Mitochondria and diabetes: Genetic, biochemical, and clinical implications of the cellular energy circuit

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; GLUCOSE 6 PHOSPHATE; HEXOKINASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE;

EID: 0030046495     PISSN: 00121797     EISSN: None     Source Type: Journal    
DOI: 10.2337/diab.45.2.113     Document Type: Article
Times cited : (286)

References (151)
  • 2
    • 0026463740 scopus 로고
    • Does the mitochondrial DNA play a role in the development of diabetes?
    • Gerbitz KD: Does the mitochondrial DNA play a role in the development of diabetes? Diabetalogia 35:1181-1186, 1992
    • (1992) Diabetalogia , vol.35 , pp. 1181-1186
    • Gerbitz, K.D.1
  • 3
    • 0024391654 scopus 로고
    • Localization of pancreatic beta cell glucose transporter to specific plasma membrane domains
    • Orci L, Thorens B, Ravazzola M, Lodish HF: Localization of pancreatic beta cell glucose transporter to specific plasma membrane domains. Science 245:295-297, 1989
    • (1989) Science , vol.245 , pp. 295-297
    • Orci, L.1    Thorens, B.2    Ravazzola, M.3    Lodish, H.F.4
  • 4
    • 0025193356 scopus 로고
    • m glucose transporter of islets of Langerhans is functionally similar to the low affinity transporter of liver and has an identical primary sequence
    • m glucose transporter of islets of Langerhans is functionally similar to the low affinity transporter of liver and has an identical primary sequence. J Biol Chem 265:6548-6551, 1990
    • (1990) J Biol Chem , vol.265 , pp. 6548-6551
    • Johnson, J.H.1    Newgard, C.B.2    Milburn, J.L.3    Lodish, H.F.4    Thorens, B.5
  • 5
    • 0021247064 scopus 로고
    • New perspectives on pancreatic islet glucokinase
    • Meglasson MD, Matschinsky FM: New perspectives on pancreatic islet glucokinase Am J Physiol 246:E1-E13, 1984
    • (1984) Am J Physiol , vol.246
    • Meglasson, M.D.1    Matschinsky, F.M.2
  • 7
    • 0027074887 scopus 로고
    • Expression of yeast hexokinase in pancreatic β-cells of transgenic mice reduces blood glucose, enhances insulin secretion and decreases diabetes
    • Epstein P, Boschero A, Atwater I, Cai X, Overbeek P: Expression of yeast hexokinase in pancreatic β-cells of transgenic mice reduces blood glucose, enhances insulin secretion and decreases diabetes. Proc Natl Acad Sci USA 89:12038-12042, 1993
    • (1993) Proc Natl Acad Sci USA , vol.89 , pp. 12038-12042
    • Epstein, P.1    Boschero, A.2    Atwater, I.3    Cai, X.4    Overbeek, P.5
  • 9
    • 0027176448 scopus 로고
    • Substrate-dependent changes in mitochondrial function, intracellular free calcium concentration and membrane channels in pancreatic β-cells
    • Duchen MR, Smith PA, Ashcroft FM: Substrate-dependent changes in mitochondrial function, intracellular free calcium concentration and membrane channels in pancreatic β-cells Biochem J 294:35-42, 1993
    • (1993) Biochem J , vol.294 , pp. 35-42
    • Duchen, M.R.1    Smith, P.A.2    Ashcroft, F.M.3
  • 10
    • 0025794049 scopus 로고
    • Inhibition of electrical activity in mouse pancreatic β-cells by the ATP/ADP translocator inhibitor, bongkrekic acid
    • Kiranadi B, Bangham JA, Smith PA: Inhibition of electrical activity in mouse pancreatic β-cells by the ATP/ADP translocator inhibitor, bongkrekic acid. FEBS Lett 283:93-90, 1991
    • (1991) FEBS Lett , vol.283 , pp. 93-190
    • Kiranadi, B.1    Bangham, J.A.2    Smith, P.A.3
  • 11
    • 0023911193 scopus 로고
    • Adenosine 5′-triphosphate-sensitive potassium channels
    • Ashcroft FM: Adenosine 5′-triphosphate-sensitive potassium channels. Annu Rev Neurosci 11 97-118, 1988
    • (1988) Annu Rev Neurosci , vol.11 , pp. 97-118
    • Ashcroft, F.M.1
  • 12
    • 0026333684 scopus 로고
    • The role of ATP and free ADP in metabolic coupling during fuel-stimulated insulin release from islet b-cells in the isolated perfused rat pancreas
    • Ghosh A, Ronner P, Cheong E, Khalid P, Matschinsky FM: The role of ATP and free ADP in metabolic coupling during fuel-stimulated insulin release from islet b-cells in the isolated perfused rat pancreas. J Biol Chem 266:22887-22892, 1991
    • (1991) J Biol Chem , vol.266 , pp. 22887-22892
    • Ghosh, A.1    Ronner, P.2    Cheong, E.3    Khalid, P.4    Matschinsky, F.M.5
  • 15
    • 0024433571 scopus 로고
    • Control of mitochondrial respiration in the heart in vivo
    • Balaban RS, Heinemann FW: Control of mitochondrial respiration in the heart in vivo. Mol Cell Biochem 89:191-197, 1989
    • (1989) Mol Cell Biochem , vol.89 , pp. 191-197
    • Balaban, R.S.1    Heinemann, F.W.2
  • 16
    • 0014010968 scopus 로고
    • Multiple hexokinases of rat tissues: Purification and comparison of soluble forms
    • Grossbrand L, Schimke RT: Multiple hexokinases of rat tissues: purification and comparison of soluble forms. J Biol Chem 241:3546-3560, 1966
    • (1966) J Biol Chem , vol.241 , pp. 3546-3560
    • Grossbrand, L.1    Schimke, R.T.2
  • 17
    • 0020016147 scopus 로고
    • The comparative isozymology of vertebrate hexokinases
    • Ureta T: The comparative isozymology of vertebrate hexokinases. Comp Biochem Physiol 71B:549-562, 1982
    • (1982) Comp Biochem Physiol , vol.71 B , pp. 549-562
    • Ureta, T.1
  • 18
    • 85132263639 scopus 로고
    • Regulation of mammalian hexokinase activity
    • Beitner R, Ed. Boca Raton, FL, CRC Press
    • Wilson JE: Regulation of mammalian hexokinase activity. In Regulation of Carbohydrate Metabolism Vol 1. Beitner R, Ed. Boca Raton, FL, CRC Press, 1985, p. 45-85
    • (1985) Regulation of Carbohydrate Metabolism , vol.1 , pp. 45-85
    • Wilson, J.E.1
  • 19
    • 0023955155 scopus 로고
    • Hexokinase metabolism in pancreatic islets: Regulation of mitochondrial binding
    • Malaisse-Langae F, Malaisse W: Hexokinase metabolism in pancreatic islets: regulation of mitochondrial binding. Biochem. Med Metab Biol 39:80-89, 1988
    • (1988) Biochem. Med Metab Biol , vol.39 , pp. 80-89
    • Malaisse-Langae, F.1    Malaisse, W.2
  • 20
    • 0028285584 scopus 로고
    • Porin proteins in mitochondria from rat pancreatic islet cells and white adipocytes: Identification and regulation of hexokinase binding by sulfonylurea Glimepiride
    • Müller G, Korndörfer A, Kornak U, Malaisse WJ: Porin proteins in mitochondria from rat pancreatic islet cells and white adipocytes: identification and regulation of hexokinase binding by sulfonylurea Glimepiride. Arch Biochem Biophys 308:8-23, 1994
    • (1994) Arch Biochem Biophys , vol.308 , pp. 8-23
    • Müller, G.1    Korndörfer, A.2    Kornak, U.3    Malaisse, W.J.4
  • 21
    • 0026636552 scopus 로고
    • Human islet glucokinase gene: Isolation and sequence analysis of full-length cDNA
    • Koranyi LI, Tanizawa Y, Welling CM, Rabin DU, Permutt MA: Human islet glucokinase gene: isolation and sequence analysis of full-length cDNA. Diabetes 41:807-811, 1992
    • (1992) Diabetes , vol.41 , pp. 807-811
    • Koranyi, L.I.1    Tanizawa, Y.2    Welling, C.M.3    Rabin, D.U.4    Permutt, M.A.5
  • 22
    • 0021740556 scopus 로고
    • An intact hydrophobic N-terminal sequence is critical for binding of rat brain hexokinase to mitochondria
    • Polakis PG, Wilson JE: An intact hydrophobic N-terminal sequence is critical for binding of rat brain hexokinase to mitochondria. Arch Biochem Biophys 234:341-352, 1984
    • (1984) Arch Biochem Biophys , vol.234 , pp. 341-352
    • Polakis, P.G.1    Wilson, J.E.2
  • 23
    • 0020482168 scopus 로고
    • Evidence for identity between the hexokinase-binding protein and the mitochondrial porin in the outer membrane of rat liver mitochondria
    • Fiek CH, 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. Biochem Biophys Acta 688:429-440, 1982
    • (1982) Biochem Biophys Acta , vol.688 , pp. 429-440
    • Fiek, C.H.1    Benz, R.2    Roos, N.3    Brdiczka, D.4
  • 24
    • 0020485742 scopus 로고
    • Pore protein and the hexokinase-binding protein from the outer membrane of rat liver mitochondria are identical
    • Lindén M, Gellerfors P, Nelson BD: Pore protein and the hexokinase-binding protein from the outer membrane of rat liver mitochondria are identical. FEBS Lett 141:189-192, 1982
    • (1982) FEBS Lett , vol.141 , pp. 189-192
    • Lindén, M.1    Gellerfors, P.2    Nelson, B.D.3
  • 25
    • 0014470116 scopus 로고
    • The effect of insulin and glucose on mitochondrial bound hexokinase activity of rat epididymal adipose tissue
    • Borrebaek B, Spydevold O. The effect of insulin and glucose on mitochondrial bound hexokinase activity of rat epididymal adipose tissue. Diabetologia 5:42-43, 1969
    • (1969) Diabetologia , vol.5 , pp. 42-43
    • Borrebaek, B.1    Spydevold, O.2
  • 26
    • 0026151278 scopus 로고
    • Influence of insulin on the catalytic activity of hexokinase isozyme II of rat skeletal muscles
    • Goncharova NY, Zelenia EV: Influence of insulin on the catalytic activity of hexokinase isozyme II of rat skeletal muscles. Biokhimiya 56.913-922, 1991
    • (1991) Biokhimiya , vol.56 , pp. 913-922
    • Goncharova, N.Y.1    Zelenia, E.V.2
  • 27
    • 0026476247 scopus 로고
    • Compartmentation of hexokinase in rat heart: A critical factor for tracer kinetic analysis of myocardial metabolism
    • Russell RR III, Mrus JM, Mommessin JI, Taegtmeyer H: Compartmentation of hexokinase in rat heart: a critical factor for tracer kinetic analysis of myocardial metabolism. Clin Invest 90.1972-1977, 1992
    • (1992) Clin Invest , vol.90 , pp. 1972-1977
    • Russell III, R.R.1    Mrus, J.M.2    Mommessin, J.I.3    Taegtmeyer, H.4
  • 28
    • 0021997991 scopus 로고
    • The regulation of mitochondrial-bound hexokinases in the liver
    • Weiler U, Riesinger I, Knoll G, Brdiczka D. The regulation of mitochondrial-bound hexokinases in the liver. Biochem. Med 33:223-236, 1985
    • (1985) Biochem. Med , vol.33 , pp. 223-236
    • Weiler, U.1    Riesinger, I.2    Knoll, G.3    Brdiczka, D.4
  • 29
    • 0024283959 scopus 로고
    • Activation of low Km hexokinases in purified hepatocytes by binding to mitochondria
    • Adams V, Bosch W, Hämmerle TH, Brdiczka D: Activation of low Km hexokinases in purified hepatocytes by binding to mitochondria. Biochim Biophys Acta 932:195-205, 1988
    • (1988) Biochim Biophys Acta , vol.932 , pp. 195-205
    • Adams, V.1    Bosch, W.2    Hämmerle, T.H.3    Brdiczka, D.4
  • 30
    • 0014025895 scopus 로고
    • m form of hexokinase from various rat tissues
    • m form of hexokinase from various rat tissues. Biochem Biophys Res Commun 24:531-536, 1965
    • (1965) Biochem Biophys Res Commun , vol.24 , pp. 531-536
    • Katzen, H.M.1
  • 33
    • 0022550296 scopus 로고
    • Enrichment and biochemical characterization of boundary membrane contact sites in rat-liver mitochondria
    • Ohlendieck K, Riesinger I, Adams V, Krause J, Brdiczka D: Enrichment and biochemical characterization of boundary membrane contact sites in rat-liver mitochondria. Biochim Biophys Acta 860:672-689, 1980
    • (1980) Biochim Biophys Acta , vol.860 , pp. 672-689
    • Ohlendieck, K.1    Riesinger, I.2    Adams, V.3    Krause, J.4    Brdiczka, D.5
  • 34
    • 0002457624 scopus 로고
    • Mitochondrial boundary membrane contact sites in brain: Points of hexokinase and creatine kinase location and of control of Ca2+ transport
    • Kottke M, Adams 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 of control of Ca2+ transport. Biochim Biophys Acta 395:807-832, 1988
    • (1988) Biochim Biophys Acta , vol.395 , pp. 807-832
    • Kottke, M.1    Adams, V.2    Riesinger, I.3    Bremm, G.4    Bosch, W.5    Brdiczka, D.6    Sandri, G.7    Panfili, E.8
  • 35
    • 0025534163 scopus 로고
    • Further characterization of mitochondrial contact sites: Effects of short-chain alcohols on membrane fluidity and activity
    • Ardail D, Lermé F, Louisot P: Further characterization of mitochondrial contact sites: effects of short-chain alcohols on membrane fluidity and activity. Biochem Biophys Res Commun 173:878-885, 1990
    • (1990) Biochem Biophys Res Commun , vol.173 , pp. 878-885
    • Ardail, D.1    Lermé, F.2    Louisot, P.3
  • 36
    • 0027230203 scopus 로고
    • Effect of macromolecules on the structure of the mitochondrial inter-membrane space and the regulation of hexokinase
    • Wicker U, Bücheler K, Gellerich FN, Wagner M, Kapischke M, Brdiczka D: Effect of macromolecules on the structure of the mitochondrial inter-membrane space and the regulation of hexokinase. Biochim Biophys Acta 1142:228-239, 1993
    • (1993) Biochim Biophys Acta , vol.1142 , pp. 228-239
    • Wicker, U.1    Bücheler, K.2    Gellerich, F.N.3    Wagner, M.4    Kapischke, M.5    Brdiczka, D.6
  • 37
    • 0025103254 scopus 로고
    • Tetrameric structure of mitochondrially bound rat brain hexokinase: A crosslinklng study
    • Xie G, Wilson JE: Tetrameric structure of mitochondrially bound rat brain hexokinase: a crosslinklng study. Arch Biochem Biophys 276:285-293, 1990
    • (1990) Arch Biochem Biophys , vol.276 , pp. 285-293
    • Xie, G.1    Wilson, J.E.2
  • 38
    • 0012009922 scopus 로고
    • The function of the outer membrane pore in the regulation of peripheral kinases and energy metabolism
    • NATO ASI Series Forte M, Colombini M, Eds. Springer Verlag, Berlin Heidelberg
    • Brdiczka D, Wicker U, Gellerich F: The function of the outer membrane pore in the regulation of peripheral kinases and energy metabolism. In Molecular Biology of Mitochondrial Transport Systems. NATO ASI Series Vol. H83. Forte M, Colombini M, Eds. Springer Verlag, Berlin Heidelberg, 1994 p. 297-311
    • (1994) Molecular Biology of Mitochondrial Transport Systems , vol.H83 , pp. 297-311
    • Brdiczka, D.1    Wicker, U.2    Gellerich, F.3
  • 39
    • 0027933027 scopus 로고
    • Function of the outer mitochondrial compartment in regulation of energy metabolism
    • Brdiczka D: Function of the outer mitochondrial compartment in regulation of energy metabolism. Biochim. Biophys Acta 1187:264-269, 1994
    • (1994) Biochim. Biophys Acta , vol.1187 , pp. 264-269
    • Brdiczka, D.1
  • 40
    • 0021111174 scopus 로고
    • Changes in freeze-fracture mitochondrial membranes correlated to their energetic state
    • Knoll G, Brdiczka D: Changes in freeze-fracture mitochondrial membranes correlated to their energetic state. Biochim Biophys Acta 733:102-110, 1983
    • (1983) Biochim Biophys Acta , vol.733 , pp. 102-110
    • Knoll, G.1    Brdiczka, D.2
  • 41
    • 0000935827 scopus 로고
    • 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
    • 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 1061:215-225, 1991
    • (1991) Biochim Biophys Acta , vol.1061 , pp. 215-225
    • Bücheler, K.1    Adams, V.2    Brdiczka, D.3
  • 42
    • 0015494364 scopus 로고
    • Kinetic enhancement of bound hexokinase activity by mitochondrial respiration
    • Gots RE, Gorin FA, Bessman SP: Kinetic enhancement of bound hexokinase activity by mitochondrial respiration. Biochem Biophys Res Commun 49:1249-1255, 1972
    • (1972) Biochem Biophys Res Commun , vol.49 , pp. 1249-1255
    • Gots, R.E.1    Gorin, F.A.2    Bessman, S.P.3
  • 44
    • 0026061129 scopus 로고
    • Hexokinase bound to rat brain mitochondria uses externally added ATP more efficiently than internally generated ATP
    • Kabir F, Nelson BD: Hexokinase bound to rat brain mitochondria uses externally added ATP more efficiently than internally generated ATP. Biochim Biophys Acta 1057:147-150, 1991
    • (1991) Biochim Biophys Acta , vol.1057 , pp. 147-150
    • Kabir, F.1    Nelson, B.D.2
  • 45
    • 0012001184 scopus 로고
    • Macromolecules increase the channeling of ADP from mitochondrially associated hexokinase to the mitochondrial matrix
    • Gnaiger E, Gellerich FN, Wyss M, Eds. New York, Plenum
    • Laterveer FD, Gellerich F, Gnaiger E, Nicolay K: Macromolecules increase the channeling of ADP from mitochondrially associated hexokinase to the mitochondrial matrix. In Modern Trends in Biothermokinetics 3. Gnaiger E, Gellerich FN, Wyss M, Eds. New York, Plenum, 1994, p. 186-190
    • (1994) Modern Trends in Biothermokinetics 3 , pp. 186-190
    • Laterveer, F.D.1    Gellerich, F.2    Gnaiger, E.3    Nicolay, K.4
  • 48
    • 0028307841 scopus 로고
    • Microcompartmentation of energy metabolism at the outer mitochondrial membrane: Role in diabetes mellitus and other diseases
    • McCabe ERB: Microcompartmentation of energy metabolism at the outer mitochondrial membrane: role in diabetes mellitus and other diseases. J Bioenerg Biomembr 26:317-325, 1994
    • (1994) J Bioenerg Biomembr , vol.26 , pp. 317-325
    • McCabe, E.R.B.1
  • 49
    • 0027166976 scopus 로고
    • Effect of macromolecules on the regulation of the mitochondrial outer membrane pore and the activity of adenylate kinase in the inter-membrane space
    • Gellerich FN, Wagner M, Kapischke M, Wicker U, Brdiczka D: Effect of macromolecules on the regulation of the mitochondrial outer membrane pore and the activity of adenylate kinase in the inter-membrane space. Biochim Biophys Acta 1142:217-227, 1993
    • (1993) Biochim Biophys Acta , vol.1142 , pp. 217-227
    • Gellerich, F.N.1    Wagner, M.2    Kapischke, M.3    Wicker, U.4    Brdiczka, D.5
  • 50
    • 0027934365 scopus 로고
    • The importance of the outer mitochondrial compartment in regulation of energy metabolism
    • Brdiczka D, Wallimann T: The importance of the outer mitochondrial compartment in regulation of energy metabolism. Mol Cell Biochem 133/134:69-83, 1994
    • (1994) Mol Cell Biochem , vol.133-134 , pp. 69-83
    • Brdiczka, D.1    Wallimann, T.2
  • 51
    • 0026585611 scopus 로고
    • Intracellular compartmentation, structure and function of creatine kinase isoenzymes in tissues with high and fluctuating energy demands: The "phosphocreatine circuit" for cellular energy homeostasis
    • Wallimann TH, Wyss M, Brdiczka D, Nicolay K: 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 281:21-40, 1992
    • (1992) Biochem J , vol.281 , pp. 21-40
    • Wallimann, T.H.1    Wyss, M.2    Brdiczka, D.3    Nicolay, K.4
  • 54
    • 0017324568 scopus 로고
    • The localization of the MM isozyme of creatine phosphokinase on the surface membrane of myocardial cells and its functional coupling to ouabain-inhibited (N,K)-ATPase
    • Saks V, Lipina NV, Sharov VG, Smirnov VN, Chazov EI, Grosse R: The localization of the MM isozyme of creatine phosphokinase on the surface membrane of myocardial cells and its functional coupling to ouabain-inhibited (N,K)-ATPase. Biochim Biophys Acta 465:350-358, 1977
    • (1977) Biochim Biophys Acta , vol.465 , pp. 350-358
    • Saks, V.1    Lipina, N.V.2    Sharov, V.G.3    Smirnov, V.N.4    Chazov, E.I.5    Grosse, R.6
  • 55
    • 0021351106 scopus 로고
    • Function of M-line bound creatine kinase as intramyofibrillar ATP regenerator at the receiving end of the phosphocreatine shuttle in muscle
    • Wallimann T, Schlösser T, Eppenberger HM: Function of M-line bound creatine kinase as intramyofibrillar ATP regenerator at the receiving end of the phosphocreatine shuttle in muscle J Biol Chem 259:5238-5246, 1984
    • (1984) J Biol Chem , vol.259 , pp. 5238-5246
    • Wallimann, T.1    Schlösser, T.2    Eppenberger, H.M.3
  • 56
    • 0014829598 scopus 로고
    • Binding of aldolase and triosephosphatdehydrogenase to F-actin and modification of catalytic properties of aldolase
    • Arnold H, Pette D: Binding of aldolase and triosephosphatdehydrogenase to F-actin and modification of catalytic properties of aldolase. Eur J Biochem 15:360-366, 1970
    • (1970) Eur J Biochem , vol.15 , pp. 360-366
    • Arnold, H.1    Pette, D.2
  • 57
    • 0025373570 scopus 로고
    • The theory of diazymes and functional coupling of pyruvate kinase and creatine kinase
    • Dillon PF, Clark JF: The theory of diazymes and functional coupling of pyruvate kinase and creatine kinase. J Theor Biol 143:275-284, 1990
    • (1990) J Theor Biol , vol.143 , pp. 275-284
    • Dillon, P.F.1    Clark, J.F.2
  • 58
    • 0026438277 scopus 로고
    • The principle islet of the Coho Salmon (Oncohyncus kisutch) contains BB isoenzyme of creatine kinase
    • White KC, Babbitt PC, Buechter DD, Kenyon GL: The principle islet of the Coho Salmon (Oncohyncus kisutch) contains BB isoenzyme of creatine kinase. J Protein Chem 11:489-494, 1992
    • (1992) J Protein Chem , vol.11 , pp. 489-494
    • White, K.C.1    Babbitt, P.C.2    Buechter, D.D.3    Kenyon, G.L.4
  • 59
    • 0028017704 scopus 로고
    • Creatine kinase in non-muscle tissues and cells
    • Wallimann T, Hemmer W: Creatine kinase in non-muscle tissues and cells. Mol Cell Biochem 133/134:193-220, 1994
    • (1994) Mol Cell Biochem , vol.133-134 , pp. 193-220
    • Wallimann, T.1    Hemmer, W.2
  • 61
    • 0023811053 scopus 로고
    • Normal oxidative damage to mitochondrial and nuclear DNA is extensive
    • Richter C, Park JW, Ames BN: Normal oxidative damage to mitochondrial and nuclear DNA is extensive. Proc Natl Acad Sci USA 85:6465-6467, 1988
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 6465-6467
    • Richter, C.1    Park, J.W.2    Ames, B.N.3
  • 62
    • 0026624980 scopus 로고
    • Diseases of the mitochondrial DNA
    • Wallace DC: Diseases of the mitochondrial DNA. Annu Rev Biochem 61:1175-1212, 1992
    • (1992) Annu Rev Biochem , vol.61 , pp. 1175-1212
    • Wallace, D.C.1
  • 63
    • 0028574053 scopus 로고
    • Mitochondrial DNA sequence variation in human evolution and disease
    • Wallace DC: Mitochondrial DNA sequence variation in human evolution and disease. Proc Natl Acad Sci USA 91:8739-8746, 1994
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 8739-8746
    • Wallace, D.C.1
  • 64
    • 0027145131 scopus 로고
    • Two novel pathogenic mitochondrial DNA mutations affecting organelle number and protein synthesis: Is the transferRNALeu(UUR) gene an etiologic hot spot?
    • Moraes CT, Ciacci F, Bonilla E, Jansen C, Hirano M, Rao N, Lovelace RE, Rowland LP, Schon EA, DiMauro S: Two novel pathogenic mitochondrial DNA mutations affecting organelle number and protein synthesis: is the transferRNALeu(UUR) gene an etiologic hot spot? J Clin Invest 92:2909-2915, 1993
    • (1993) J Clin Invest , vol.92 , pp. 2909-2915
    • Moraes, C.T.1    Ciacci, F.2    Bonilla, E.3    Jansen, C.4    Hirano, M.5    Rao, N.6    Lovelace, R.E.7    Rowland, L.P.8    Schon, E.A.9    DiMauro, S.10
  • 67
    • 0026688649 scopus 로고
    • A new mtDNA mutation in the tRNA lys gene associated with myoclonic epilepsy and ragged red fibers
    • Silvestri G, Moraes CT, Shanske S, Oh SJ, DiMauro S: A new mtDNA mutation in the tRNA lys gene associated with myoclonic epilepsy and ragged red fibers. Am J Hum Genet 51:1213-1217, 1992
    • (1992) Am J Hum Genet , vol.51 , pp. 1213-1217
    • Silvestri, G.1    Moraes, C.T.2    Shanske, S.3    Oh, S.J.4    DiMauro, S.5
  • 74
    • 0027369567 scopus 로고
    • Prevalence of mitochondrial gene mutations in families with diabetes mellitus
    • Vionnet N, Passa P, Froguel P: Prevalence of mitochondrial gene mutations in families with diabetes mellitus. Lancet 342:1429-1430, 1993
    • (1993) Lancet , vol.342 , pp. 1429-1430
    • Vionnet, N.1    Passa, P.2    Froguel, P.3
  • 80
    • 0029039460 scopus 로고
    • Mitochondrial diabetes mellitus: Glucose-induced signaling defects and beta-cell loss
    • Oka Y, Katagiri H, Tshihara H, Asano T, Kikuchi M, Kobayashi T: Mitochondrial diabetes mellitus: glucose-induced signaling defects and beta-cell loss. Muscle and Nerve (Suppl. 3):S131-S136, 1995
    • (1995) Muscle and Nerve , Issue.3 SUPPL.
    • Oka, Y.1    Katagiri, H.2    Tshihara, H.3    Asano, T.4    Kikuchi, M.5    Kobayashi, T.6
  • 81
    • 0028365102 scopus 로고
    • Maternally inherited diabetes and deafness is a distinct subtype of diabetes and associates with a single point mutation in the mitochondrial tRNALeu(UUR) gene
    • van den Ouweland JMW, Lemkes HPJ, Trembath RC, Ross R, Velho G, Cohen D, Froguel P, Maassen JA: Maternally inherited diabetes and deafness is a distinct subtype of diabetes and associates with a single point mutation in the mitochondrial tRNALeu(UUR) gene. Diabetes 43:746-751, 1994
    • (1994) Diabetes , vol.43 , pp. 746-751
    • Van Den Ouweland, J.M.W.1    Lemkes, H.P.J.2    Trembath, R.C.3    Ross, R.4    Velho, G.5    Cohen, D.6    Froguel, P.7    Maassen, J.A.8
  • 82
    • 0027447027 scopus 로고
    • Mitochondrial myopathy, encephalopathy, lactic acidosis and stroke-like episodes (MELAS) and diabetes, a molecular genetic analysis and family study
    • Orushi H, Inoe K, Osaka H, Kimura S, Nagatomo H, Hanihara T. Mitochondrial myopathy, encephalopathy, lactic acidosis and stroke-like episodes (MELAS) and diabetes, a molecular genetic analysis and family study. J Neurol Sci 114:205-208, 1993
    • (1993) J Neurol Sci , vol.114 , pp. 205-208
    • Orushi, H.1    Inoe, K.2    Osaka, H.3    Kimura, S.4    Nagatomo, H.5    Hanihara, T.6
  • 84
    • 0029072327 scopus 로고
    • Clinical features of MELAS and mitochondrial DNA mutations
    • Goto Y: Clinical features of MELAS and mitochondrial DNA mutations. Muscle and Nervre (Suppl. 3):S107-S112, 1995
    • (1995) Muscle and Nervre , Issue.3 SUPPL.
    • Goto, Y.1
  • 91
    • 0028927272 scopus 로고
    • Segregation patterns of a novel mutation in the mitochondrial tRNA glutamic acid gene associated with myopathy and diabetes
    • Hao H, Bonilla E, Manfredi G, DiMauro S, Moraes CT: Segregation patterns of a novel mutation in the mitochondrial tRNA glutamic acid gene associated with myopathy and diabetes. Am J Hum Genet 56.117-125, 1995
    • (1995) Am J Hum Genet , vol.56 , pp. 117-125
    • Hao, H.1    Bonilla, E.2    Manfredi, G.3    DiMauro, S.4    Moraes, C.T.5
  • 92
    • 0028917662 scopus 로고
    • Congenital encephalomyopathy and adult-onset myopathy and diabetes mellitus: Different phenotypic associations of a new heteroplasmic mtDNA tRNA glutamic acid mutation
    • Hanna MG, Nelson I, Sweeney MG, Cooper JM, Watkins PJ, Morgan-Hughes JA, Harding AE: Congenital encephalomyopathy and adult-onset myopathy and diabetes mellitus: different phenotypic associations of a new heteroplasmic mtDNA tRNA glutamic acid mutation. Am J Hum Genet 56:1026-1033, 1995
    • (1995) Am J Hum Genet , vol.56 , pp. 1026-1033
    • Hanna, M.G.1    Nelson, I.2    Sweeney, M.G.3    Cooper, J.M.4    Watkins, P.J.5    Morgan-Hughes, J.A.6    Harding, A.E.7
  • 93
    • 0023883150 scopus 로고
    • Deletion of the muscle mitochondrial DNA in patient with mitochondrial myopathies
    • Holt IJ, Harding AE, Morgan-Hughes JA: Deletion of the muscle mitochondrial DNA in patient with mitochondrial myopathies. Nature 331: 717-719, 1988
    • (1988) Nature , vol.331 , pp. 717-719
    • Holt, I.J.1    Harding, A.E.2    Morgan-Hughes, J.A.3
  • 94
    • 0023877476 scopus 로고
    • Kearns-Sayre syndrome with muscle mitochondrial DNA deletion
    • Lestienne P, Ponsot G: Kearns-Sayre syndrome with muscle mitochondrial DNA deletion (Letter). Lancet i:885, 1988
    • (1988) Lancet , vol.1 , pp. 885
    • Lestienne, P.1    Ponsot, G.2
  • 100
    • 0026773036 scopus 로고
    • Endocrine dysfunction in Kearns-Sayre syndrome
    • Harvey JN, Barnett D: Endocrine dysfunction in Kearns-Sayre syndrome. Clin Endocrinol 37:97-104, 1992
    • (1992) Clin Endocrinol , vol.37 , pp. 97-104
    • Harvey, J.N.1    Barnett, D.2
  • 101
    • 0026585685 scopus 로고
    • Endocrine abnormalities in mitochondrial myopathy with external ophthalmoplegia
    • Quade A, Zierz S, Klingmüller D: Endocrine abnormalities in mitochondrial myopathy with external ophthalmoplegia. Clin Invest 70:396-402, 1992
    • (1992) Clin Invest , vol.70 , pp. 396-402
    • Quade, A.1    Zierz, S.2    Klingmüller, D.3
  • 102
    • 0027403570 scopus 로고
    • Families of mitochondrial re-arrangements can be detected in patients with mtDNA deletions: Duplications may be a transient intermediate form
    • Poulton J, Deadman ME, Bindoff L, Morton K, Land J, Brown G: Families of mitochondrial re-arrangements can be detected in patients with mtDNA deletions: duplications may be a transient intermediate form. Hum Mol Genet 2:23-30, 1993
    • (1993) Hum Mol Genet , vol.2 , pp. 23-30
    • Poulton, J.1    Deadman, M.E.2    Bindoff, L.3    Morton, K.4    Land, J.5    Brown, G.6
  • 103
    • 0027381483 scopus 로고
    • Maternally transmitted partial direct tandem duplication of mitochondrial DNA associated with diabetes mellitus
    • Dunbar DR, Moonie PA, Swingler RJ, Davidson D, Roberts R, Holt IJ: Maternally transmitted partial direct tandem duplication of mitochondrial DNA associated with diabetes mellitus. Hum Mat Genet 2:1619-1624, 1993
    • (1993) Hum Mat Genet , vol.2 , pp. 1619-1624
    • Dunbar, D.R.1    Moonie, P.A.2    Swingler, R.J.3    Davidson, D.4    Roberts, R.5    Holt, I.J.6
  • 104
    • 0028286575 scopus 로고
    • Are duplications of mitochondrial DNA characteristic of Kearns-Sayre syndrome?
    • Poulton J, Morten KJ, Weber K, Brown GK, Bindoff L: Are duplications of mitochondrial DNA characteristic of Kearns-Sayre syndrome? Hum Mol Genet 3:947-951, 1994
    • (1994) Hum Mol Genet , vol.3 , pp. 947-951
    • Poulton, J.1    Morten, K.J.2    Weber, K.3    Brown, G.K.4    Bindoff, L.5
  • 105
    • 0028004453 scopus 로고
    • Mitochondrial DND. does more lead to less?
    • Poulton P, Holt U: Mitochondrial DND. does more lead to less? Nature Genet 8:313-315, 1994
    • (1994) Nature Genet , vol.8 , pp. 313-315
    • Poulton, P.1    Holt, U.2
  • 106
    • 0026569283 scopus 로고
    • Maternally inherited duplication of the mitochondrial genome in a syndrome of proximal tubulopathy, diabetes mellitus and cerebellar ataxia
    • Rotig A, Bessis JL, Romero N, Cormier V, Saudubray JM, Narcy P, Lenoir Rustin P, Munnich A: Maternally inherited duplication of the mitochondrial genome in a syndrome of proximal tubulopathy, diabetes mellitus and cerebellar ataxia. Am J Hum Genet 50:368-371, 1992
    • (1992) Am J Hum Genet , vol.50 , pp. 368-371
    • Rotig, A.1    Bessis, J.L.2    Romero, N.3    Cormier, V.4    Saudubray, J.M.5    Narcy, P.6    Lenoir Rustin, P.7    Munnich, A.8
  • 107
    • 0026041854 scopus 로고
    • Congenital hypoplastic anemia, diabetes and severe renal tubular dysfunction associated with a mitochondrial DNA deletion
    • Majander A, Suomaleinen A, Vettenranta K, Sarioly H, Perkkio M, Holmberg C, Pihko H: Congenital hypoplastic anemia, diabetes and severe renal tubular dysfunction associated with a mitochondrial DNA deletion. Pediatr Res 30:327-330, 1991
    • (1991) Pediatr Res , vol.30 , pp. 327-330
    • Majander, A.1    Suomaleinen, A.2    Vettenranta, K.3    Sarioly, H.4    Perkkio, M.5    Holmberg, C.6    Pihko, H.7
  • 108
    • 0027310104 scopus 로고
    • Pearsons bone marrow pancreas syndrome with insulin-dependent diabetes mellitus, progressive renal tubulopathy, organic aciduria, and elevated fetal hemoglobin caused by deletion and duplication of the mitochondrial DNA
    • Superti-Furga A, Schoenle E, Tuchschmid P, Caduff R, Sabato V, DeMattia D, Gitzelmann R, Steinmann B: Pearsons bone marrow pancreas syndrome with insulin-dependent diabetes mellitus, progressive renal tubulopathy, organic aciduria, and elevated fetal hemoglobin caused by deletion and duplication of the mitochondrial DNA. Eur J Pediatr 152:44-50, 1993
    • (1993) Eur J Pediatr , vol.152 , pp. 44-50
    • Superti-Furga, A.1    Schoenle, E.2    Tuchschmid, P.3    Caduff, R.4    Sabato, V.5    Demattia, D.6    Gitzelmann, R.7    Steinmann, B.8
  • 111
    • 0027230737 scopus 로고
    • A tandem duplication in the D-loop of human mitochondrial DNA is associated with deletions in mitochondrial myopathies
    • Brockington M, Sweeney MG, Hammans SR, Morgan-Hughes JA, Harding AE: A tandem duplication in the D-loop of human mitochondrial DNA is associated with deletions in mitochondrial myopathies. Nature Genet 4:67-71, 1993
    • (1993) Nature Genet , vol.4 , pp. 67-71
    • Brockington, M.1    Sweeney, M.G.2    Hammans, S.R.3    Morgan-Hughes, J.A.4    Harding, A.E.5
  • 112
    • 0028095263 scopus 로고
    • mtDNA and the origin of Caucasians: Identification of ancient Caucasian-specific haplogroups, one of which is prone to a recurrent somatic duplication in the D-loop region
    • Torroni A, Lott MT, Cabell MF, Chen YS, Lavergne L, Wallace DC: mtDNA and the origin of Caucasians: identification of ancient Caucasian-specific haplogroups, one of which is prone to a recurrent somatic duplication in the D-loop region. Am J Hum Genet 55:760-776, 1994
    • (1994) Am J Hum Genet , vol.55 , pp. 760-776
    • Torroni, A.1    Lott, M.T.2    Cabell, M.F.3    Chen, Y.S.4    Lavergne, L.5    Wallace, D.C.6
  • 114
  • 115
    • 85035157485 scopus 로고    scopus 로고
    • A novel ND1 mutation (T>C at nt pos 3398) of the mtDNA in a familiy with MELAS, cardiomyopathy and diabetes mellitus
    • In press
    • Jaksch M, Hofmann S, Kaufhold P, Obermaier-Kusser B, Zierz S, Gerbitz KD: A novel ND1 mutation (T>C at nt pos 3398) of the mtDNA in a familiy with MELAS, cardiomyopathy and diabetes mellitus. Hum Mut. In press
    • Hum Mut.
    • Jaksch, M.1    Hofmann, S.2    Kaufhold, P.3    Obermaier-Kusser, B.4    Zierz, S.5    Gerbitz, K.D.6
  • 118
    • 0029040769 scopus 로고
    • Mitochondrial DNA, diabetes and pancreatic pathology in Kearns-Sayre syndrome
    • Poulton J, O'Rahilly S, Morton KJ, Clark A. Mitochondrial DNA, diabetes and pancreatic pathology in Kearns-Sayre syndrome. Diabetologia 38:869-871, 1995
    • (1995) Diabetologia , vol.38 , pp. 869-871
    • Poulton, J.1    O'Rahilly, S.2    Morton, K.J.3    Clark, A.4
  • 119
    • 0027268052 scopus 로고
    • Mitochondrial gene mutation in islet-cell-antibody positive who were initially non-insulin dependent diabetes
    • Oka Y, Katagiri H, Yazaki Y, Murase T, Kobayaski T: Mitochondrial gene mutation in islet-cell-antibody positive who were initially non-insulin dependent diabetes. Lancet 342:527-528, 1993
    • (1993) Lancet , vol.342 , pp. 527-528
    • Oka, Y.1    Katagiri, H.2    Yazaki, Y.3    Murase, T.4    Kobayaski, T.5
  • 121
    • 0028276808 scopus 로고
    • Mitochondrial creatine kinase: A major constituent of pathological inclusions seen in mitochondrial myopathies
    • Stadhouders AM, Jap PH, Winkler HP, Eppenberger HM, Wallimann T: Mitochondrial creatine kinase: a major constituent of pathological inclusions seen in mitochondrial myopathies. Proc Natl Acad Sci USA 91:5089-5093, 1994
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 5089-5093
    • Stadhouders, A.M.1    Jap, P.H.2    Winkler, H.P.3    Eppenberger, H.M.4    Wallimann, T.5
  • 122
    • 0025802101 scopus 로고
    • Adult rat cardiomyocytes in creatine-deficient medium display large mitochondria with paracrystalline inculsions, enriched for creatine kinase
    • Eppenberger-Eberhardt M, Riesinger I, Messerli M, Schwarb P, Müller M, Eppenberger HM, Wallimann T: Adult rat cardiomyocytes in creatine-deficient medium display large mitochondria with paracrystalline inculsions, enriched for creatine kinase. J Cell Biol 113:289-302, 1991
    • (1991) J Cell Biol , vol.113 , pp. 289-302
    • Eppenberger-Eberhardt, M.1    Riesinger, I.2    Messerli, M.3    Schwarb, P.4    Müller, M.5    Eppenberger, H.M.6    Wallimann, T.7
  • 123
    • 0024448458 scopus 로고
    • Human cells lacking mtDNA: Repopulation with exogenous mitochondria by complementation
    • King MP, Attardi G. Human cells lacking mtDNA: repopulation with exogenous mitochondria by complementation. Science 246:500-503, 1989
    • (1989) Science , vol.246 , pp. 500-503
    • King, M.P.1    Attardi, G.2
  • 124
    • 0025836655 scopus 로고
    • Introduction of disease-related mitochondrial DNA deletions into HeLa cells lacking mitochondrial DNA results in mitochondrial dysfunction
    • Hayashi JI, Ohta S, Kikuchi A, Takemitsu M, Goto Y, Nonake I: Introduction of disease-related mitochondrial DNA deletions into HeLa cells lacking mitochondrial DNA results in mitochondrial dysfunction. Proc Natl Acad Sci USA 88:10614-10618, 1991
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 10614-10618
    • Hayashi, J.I.1    Ohta, S.2    Kikuchi, A.3    Takemitsu, M.4    Goto, Y.5    Nonake, I.6
  • 126
    • 0028984692 scopus 로고
    • Co-localization of L-type Ca2+ channels and insulin-containing secretory granules and its significance for the initiation of exocytosis in mouse pancreatic B-cells
    • Bokvist K, Eliasson L, Rorsman P: Co-localization of L-type Ca2+ channels and insulin-containing secretory granules and its significance for the initiation of exocytosis in mouse pancreatic B-cells. EMBO J 14:50-57, 1995
    • (1995) EMBO J , vol.14 , pp. 50-57
    • Bokvist, K.1    Eliasson, L.2    Rorsman, P.3
  • 130
    • 0027275218 scopus 로고
    • Wolfram syndrome: A mitochondrial mediated disorder
    • Bu X, Rotter JI: Wolfram syndrome: a mitochondrial mediated disorder. Lancet 342:598-600, 1993
    • (1993) Lancet , vol.342 , pp. 598-600
    • Bu, X.1    Rotter, J.I.2
  • 132
    • 0029029471 scopus 로고
    • Modeling the effects of age-related mtDNA mutation accumulation: Complex I deficiency, superoide and cell death
    • Cortopassi G, Wang E: Modeling the effects of age-related mtDNA mutation accumulation: complex I deficiency, superoide and cell death. Biochim Biophys Acta 1271:171-176, 1995
    • (1995) Biochim Biophys Acta , vol.1271 , pp. 171-176
    • Cortopassi, G.1    Wang, E.2
  • 136
    • 0028967724 scopus 로고
    • Increased expression of mitochondrial-encoded genes in skeletal muscle of humans with diabetes mellitus
    • Antonetti DA, Reynet C, Kahn CR: Increased expression of mitochondrial-encoded genes in skeletal muscle of humans with diabetes mellitus. J Clin Invest 95:1383-1388, 1995
    • (1995) J Clin Invest , vol.95 , pp. 1383-1388
    • Antonetti, D.A.1    Reynet, C.2    Kahn, C.R.3
  • 137
    • 0028914027 scopus 로고
    • Amino acid substitutions in hexokinase II among patients with NIDDM
    • Laakso M, Malkki M, Deeb SS: Amino acid substitutions in hexokinase II among patients with NIDDM. Diabetes 44:330-334, 1995
    • (1995) Diabetes , vol.44 , pp. 330-334
    • Laakso, M.1    Malkki, M.2    Deeb, S.S.3
  • 139
    • 0028962835 scopus 로고
    • Identification of four amino acid substitutions in hexokinase II and studies of the relationships to NIDDM, glucose effectiveness, and insulin sensitivity
    • Echwald SM, Bjorbaek C, Hansen T, Clansen JO, Vestergaard H, Zierath JR, Printz RL, Granner DK, Pedersen O Identification of four amino acid substitutions in hexokinase II and studies of the relationships to NIDDM, glucose effectiveness, and insulin sensitivity. Diabetes, 44.347-353, 1995
    • (1995) Diabetes , vol.44 , pp. 347-353
    • Echwald, S.M.1    Bjorbaek, C.2    Hansen, T.3    Clansen, J.O.4    Vestergaard, H.5    Zierath, J.R.6    Printz, R.L.7    Granner, D.K.8    Pedersen, O.9
  • 140
    • 0028809238 scopus 로고
    • Decreased muscle glucose transport/phosphorylation is an early defect in the pathogenesis of non-insulin-dependent diabetes mellitus
    • Rothman DL, Magnusson I, Cline G, Gerard D, Kahn CR, Shulman RG, Shulman GI: Decreased muscle glucose transport/phosphorylation is an early defect in the pathogenesis of non-insulin-dependent diabetes mellitus. Proc Natl Acad Sci USA 92:983-987, 1995
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 983-987
    • Rothman, D.L.1    Magnusson, I.2    Cline, G.3    Gerard, D.4    Kahn, C.R.5    Shulman, R.G.6    Shulman, G.I.7
  • 141
    • 0027930089 scopus 로고
    • Lack of voltage-dependent anion channel in human mitochondrial myopathies
    • Huizing M, Ruitenbeek W, Thinnes FP, DePinto V: Lack of voltage-dependent anion channel in human mitochondrial myopathies (Letter). Lancet 344:762, 1994
    • (1994) Lancet , vol.344 , pp. 762
    • Huizing, M.1    Ruitenbeek, W.2    Thinnes, F.P.3    DePinto, V.4
  • 142
    • 0029069530 scopus 로고
    • Non-insulin dependent diabetes mellitus and islet B-cell mitochondrial glycerophosphate dehydrogenase deficiency
    • Malaisse WJ: Non-insulin dependent diabetes mellitus and islet B-cell mitochondrial glycerophosphate dehydrogenase deficiency. Diabetic Med 12:479-481, 1995
    • (1995) Diabetic Med , vol.12 , pp. 479-481
    • Malaisse, W.J.1
  • 144
    • 0028236988 scopus 로고
    • More direct evidence for a malonyl-CoA-carnitine palmitoyltransferase I interaction as a key event in pancreatic β-cell signaling
    • Chen S, Ogawa A, Ohneda M, Unger RH, Foster DW, McGarry JD: More direct evidence for a malonyl-CoA-carnitine palmitoyltransferase I interaction as a key event in pancreatic β-cell signaling. Diabetes 43:878-883, 1994
    • (1994) Diabetes , vol.43 , pp. 878-883
    • Chen, S.1    Ogawa, A.2    Ohneda, M.3    Unger, R.H.4    Foster, D.W.5    McGarry, J.D.6
  • 146
    • 0345454166 scopus 로고
    • Metabolite carriers in mitochondria
    • Ernster L, Ed. New York, Elsevier
    • Kramer R, Palmieri F: Metabolite carriers in mitochondria. In Molecular Mechanism in Bioenergetics. Ernster L, Ed. New York, Elsevier, 1992, p. 359-385
    • (1992) Molecular Mechanism in Bioenergetics , pp. 359-385
    • Kramer, R.1    Palmieri, F.2
  • 147
    • 0024600466 scopus 로고
    • Molecular aspects of the adenine nucleotide carrier from mitochondria
    • Klingenberg M: Molecular aspects of the adenine nucleotide carrier from mitochondria. Arch Biochem Biophys 270:1-14, 1989
    • (1989) Arch Biochem Biophys , vol.270 , pp. 1-14
    • Klingenberg, M.1
  • 148
    • 0017054558 scopus 로고
    • Reconstitution in planar bilayers of a voltage dependent anion-selective channel obtained from parametium mitochondria
    • Schein SJ, Colombini M, Finkelstein A: Reconstitution in planar bilayers of a voltage dependent anion-selective channel obtained from parametium mitochondria. J Membr Biol 30:99-120, 1976
    • (1976) J Membr Biol , vol.30 , pp. 99-120
    • Schein, S.J.1    Colombini, M.2    Finkelstein, A.3
  • 149
    • 0026574501 scopus 로고
    • The cation-selective substrate of the mitochondrial outer membrane pore: Single-channel conductance and influence on intermembrane and peripheral kinases
    • Benz R, Brdiczka D: The cation-selective substrate of the mitochondrial outer membrane pore: single-channel conductance and influence on intermembrane and peripheral kinases. J Bioenerg Biomembr 24:313-39, 1992
    • (1992) J Bioenerg Biomembr , vol.24 , pp. 313-339
    • Benz, R.1    Brdiczka, D.2
  • 151
    • 0023147598 scopus 로고
    • Only one of the two interconvertable forms of the mitochondrial creatine kinase binds to heart mitoplasts
    • Marcillat O, Goldschmidt D, Eichenberger D, Vial C: Only one of the two interconvertable forms of the mitochondrial creatine kinase binds to heart mitoplasts. Biochim Biophys Acta 890:233-241, 1987
    • (1987) Biochim Biophys Acta , vol.890 , pp. 233-241
    • Marcillat, O.1    Goldschmidt, D.2    Eichenberger, D.3    Vial, C.4


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