메뉴 건너뛰기




Volumn 1837, Issue 2, 2014, Pages 232-245

Role of mitochondria-cytoskeleton interactions in respiration regulation and mitochondrial organization in striated muscles

Author keywords

Energy flux; Intracellular energy unit; Metabolic control analysis; Respiration; Skeletal muscle

Indexed keywords

ADENINE NUCLEOTIDE TRANSLOCASE; CYTOSKELETON PROTEIN; PHOSPHOENOLPYRUVATE; PYRUVATE KINASE; TUBULIN BETA II; UNCLASSIFIED DRUG;

EID: 84890282138     PISSN: 00052728     EISSN: 18792650     Source Type: Journal    
DOI: 10.1016/j.bbabio.2013.10.011     Document Type: Article
Times cited : (40)

References (73)
  • 4
    • 68749106797 scopus 로고    scopus 로고
    • Direct measurement of energy fluxes from mitochondria into cytoplasm in permeabilized cardiac cells in situ: Some evidence for mitochondrial interactosome
    • N. Timohhina, R. Guzun, K. Tepp, C. Monge, M. Varikmaa, H. Vija, P. Sikk, T. Kaambre, D. Sackett, and V. Saks Direct measurement of energy fluxes from mitochondria into cytoplasm in permeabilized cardiac cells in situ: some evidence for mitochondrial interactosome J. Bioenerg. Biomembr. 41 2009 259 275
    • (2009) J. Bioenerg. Biomembr. , vol.41 , pp. 259-275
    • Timohhina, N.1    Guzun, R.2    Tepp, K.3    Monge, C.4    Varikmaa, M.5    Vija, H.6    Sikk, P.7    Kaambre, T.8    Sackett, D.9    Saks, V.10
  • 6
    • 38349121902 scopus 로고    scopus 로고
    • Transport ATPases into the year 2008: A brief overview related to types, structures, functions and roles in health and disease
    • P. Pedersen Transport ATPases into the year 2008: a brief overview related to types, structures, functions and roles in health and disease J. Bioenerg. Biomembr. 39 2007 349 355
    • (2007) J. Bioenerg. Biomembr. , vol.39 , pp. 349-355
    • Pedersen, P.1
  • 7
    • 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
    • T. Wallimann, M. Wyss, D. Brdiczka, K. Nicolay, and H.M. Eppenberger 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 1992 21 40
    • (1992) Biochem. J. , vol.281 , pp. 21-40
    • Wallimann, T.1    Wyss, M.2    Brdiczka, D.3    Nicolay, K.4    Eppenberger, H.M.5
  • 8
    • 0034629141 scopus 로고    scopus 로고
    • Direct evidence for the control of mitochondrial respiration by mitochondrial creatine kinase in oxidative muscle cells in situ
    • DOI 10.1074/jbc.275.10.6937
    • L. Kay, K. Nicolay, B. Wieringa, V. Saks, and T. Wallimann Direct evidence for the control of mitochondrial respiration by mitochondrial creatine kinase in oxidative muscle cells in situ J. Biol. Chem. 275 2000 6937 6944 (Pubitemid 30146236)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.10 , pp. 6937-6944
    • Kay, L.1    Nicolay, K.2    Wieringa, B.3    Saks, V.4    Wallimann, T.5
  • 10
    • 0029896830 scopus 로고    scopus 로고
    • Molecular diversity of myofibrillar proteins: Gene regulation and functional significance
    • S. Schiaffino, and C. Reggiani Molecular diversity of myofibrillar proteins: gene regulation and functional significance Physiol. Rev. 76 1996 371 423 (Pubitemid 26163713)
    • (1996) Physiological Reviews , vol.76 , Issue.2 , pp. 371-423
    • Schiaffino, S.1    Reggiani, C.2
  • 11
    • 0030024488 scopus 로고    scopus 로고
    • Composition and size of type I, IIA, IID/X, and IIB fibers and citrate synthase activity of rat muscle
    • M.D. Delp, and C. Duan Composition and size of type I, IIA, IID/X, and IIB fibers and citrate synthase activity of rat muscle J. Appl. Physiol. 80 1996 261 270 (Pubitemid 26034871)
    • (1996) Journal of Applied Physiology , vol.80 , Issue.1 , pp. 261-270
    • Delp, M.D.1    Duan, C.2
  • 13
    • 0026712942 scopus 로고
    • Ultrastructural quantitation of mitochondria and myofilaments in cardiac muscle from 10 different animal species including man
    • E. Barth, G. Stämmler, B. Speiser, and J. Schaper Ultrastructural quantitation of mitochondria and myofilaments in cardiac muscle from 10 different animal species including man J. Mol. Cell. Cardiol. 24 1992 669 681
    • (1992) J. Mol. Cell. Cardiol. , vol.24 , pp. 669-681
    • Barth, E.1    Stämmler, G.2    Speiser, B.3    Schaper, J.4
  • 14
    • 0030958862 scopus 로고    scopus 로고
    • Ultra-high-resolution scanning electron microscopy of mitochondria and sarcoplasmic reticulum arrangement in human red, white, and intermediate muscle fibers
    • DOI 10.1002/(SICI)1097-0185(199706)248:2<214::AID-AR8>3.0.CO;2-S
    • T. Ogata, and Y. Yamasaki Ultra-high-resolution scanning electron microscopy of mitochondria and sarcoplasmic reticulum arrangement in human red, white, and intermediate muscle fibers Anat. Rec. 248 1997 214 223 (Pubitemid 27246816)
    • (1997) Anatomical Record , vol.248 , Issue.2 , pp. 214-223
    • Ogata, T.1    Yamasaki, Y.2
  • 15
    • 84856579589 scopus 로고    scopus 로고
    • Mitochondrial functional specialization in glycolytic and oxidative muscle fibers: Tailoring the organelle for optimal function
    • M. Picard, R.T. Hepple, and Y. Burelle Mitochondrial functional specialization in glycolytic and oxidative muscle fibers: tailoring the organelle for optimal function Am. J. Physiol. Cell Physiol. 302 2012 C629 C641
    • (2012) Am. J. Physiol. Cell Physiol. , vol.302
    • Picard, M.1    Hepple, R.T.2    Burelle, Y.3
  • 16
    • 0021678625 scopus 로고
    • Muscle fiber type composition of the rat hindlimb
    • DOI 10.1002/aja.1001710303
    • R.B. Armstrong, and R.O. Phelps Muscle fiber type composition of the rat hindlimb Am. J. Anat. 171 1984 259 272 (Pubitemid 15189959)
    • (1984) American Journal of Anatomy , vol.171 , Issue.3 , pp. 259-272
    • Armstrong, R.B.1    Phelps, R.O.2
  • 17
    • 79957656816 scopus 로고    scopus 로고
    • Protein composition and function of red and white skeletal muscle mitochondria
    • B. Glancy, and R.S. Balaban Protein composition and function of red and white skeletal muscle mitochondria Am. J. Physiol. Cell Physiol. 300 2011 C1280 C1290
    • (2011) Am. J. Physiol. Cell Physiol. , vol.300
    • Glancy, B.1    Balaban, R.S.2
  • 19
    • 0028946589 scopus 로고
    • Control of cellular respiration in vivo bymitochondrial outer membrane and by creatine kinase. A new speculative hypothesis: Possible involvement of mitochondrial-cytoskeleton interactions
    • V.A. Saks, A.V. Kuznetsov, Z.A. Khuchua, E.V. Vasilyeva, J.O. Belikova, T. Kesvatera, and T. Tiivel Control of cellular respiration in vivo bymitochondrial outer membrane and by creatine kinase. A new speculative hypothesis: possible involvement of mitochondrial-cytoskeleton interactions J. Mol. Cell. Cardiol. 27 1995 625 645
    • (1995) J. Mol. Cell. Cardiol. , vol.27 , pp. 625-645
    • Saks, V.A.1    Kuznetsov, A.V.2    Khuchua, Z.A.3    Vasilyeva, E.V.4    Belikova, J.O.5    Kesvatera, T.6    Tiivel, T.7
  • 22
    • 54949088596 scopus 로고    scopus 로고
    • Regulation of respiration in brain mitochondria and synaptosomes: Restrictions of ADP diffusion in situ, roles of tubulin, and mitochondrial creatine kinase
    • C. Monge, N. Beraud, A.V. Kuznetsov, T. Rostovtseva, D. Sackett, U. Schlattner, M. Vendelin, and V.A. Saks Regulation of respiration in brain mitochondria and synaptosomes: restrictions of ADP diffusion in situ, roles of tubulin, and mitochondrial creatine kinase Mol. Cell. Biochem. 318 2008 147 165
    • (2008) Mol. Cell. Biochem. , vol.318 , pp. 147-165
    • Monge, C.1    Beraud, N.2    Kuznetsov, A.V.3    Rostovtseva, T.4    Sackett, D.5    Schlattner, U.6    Vendelin, M.7    Saks, V.A.8
  • 23
    • 52449104836 scopus 로고    scopus 로고
    • VDAC regulation: Role of cytosolic proteins and mitochondrial lipids
    • T.K. Rostovtseva, and S.M. Bezrukov VDAC regulation: role of cytosolic proteins and mitochondrial lipids J. Bioenerg. Biomembr. 40 2008 163 170
    • (2008) J. Bioenerg. Biomembr. , vol.40 , pp. 163-170
    • Rostovtseva, T.K.1    Bezrukov, S.M.2
  • 24
    • 84859763173 scopus 로고    scopus 로고
    • Control of mitochondrial outer membrane permeability: VDAC regulation by dimeric tubulin and cytosolic proteins
    • O.L. Svensson, Nova Biomedical Books New York
    • T.K. Rostovtseva Control of mitochondrial outer membrane permeability: VDAC regulation by dimeric tubulin and cytosolic proteins O.L. Svensson, Mitochondria: Structure, Functions and Dysfunctions 2010 Nova Biomedical Books New York 607 634
    • (2010) Mitochondria: Structure, Functions and Dysfunctions , pp. 607-634
    • Rostovtseva, T.K.1
  • 25
    • 84859742434 scopus 로고    scopus 로고
    • VDAC inhibition by tubulin and its physiological implications
    • T.K. Rostovtseva, and S.M. Bezrukov VDAC inhibition by tubulin and its physiological implications Biochim. Biophys. Acta 1818 2012 1526 1535
    • (2012) Biochim. Biophys. Acta , vol.1818 , pp. 1526-1535
    • Rostovtseva, T.K.1    Bezrukov, S.M.2
  • 28
    • 44949185670 scopus 로고    scopus 로고
    • Analysis of mitochondrial function in situ in permeabilized muscle fibers, tissues and cells
    • DOI 10.1038/nprot.2008.61, PII NPROT.2008.61
    • A.V. Kuznetsov, V. Veksler, F.N. Gellerich, V. Saks, R. Margreiter, and W.S. Kunz Analysis of mitochondrial function in situ in permeabilized muscle fibers, tissues and cells Nat. Protoc. 3 2008 965 976 (Pubitemid 351818685)
    • (2008) Nature Protocols , vol.3 , Issue.6 , pp. 965-976
    • Kuznetsov, A.V.1    Veksler, V.2    Gellerich, F.N.3    Saks, V.4    Margreiter, R.5    Kunz, W.S.6
  • 30
    • 67649588894 scopus 로고    scopus 로고
    • Regulation of respiration controlled by mitochondrial creatine kinase in permeabilized cardiac cells in situ. Importance of system level properties
    • R. Guzun, N. Timohhina, K. Tepp, C. Monge, T. Kaambre, P. Sikk, A.V. Kuznetsov, C. Pison, and V. Saks Regulation of respiration controlled by mitochondrial creatine kinase in permeabilized cardiac cells in situ. Importance of system level properties Biochim. Biophys. Acta 1787 2009 1089 1105
    • (2009) Biochim. Biophys. Acta , vol.1787 , pp. 1089-1105
    • Guzun, R.1    Timohhina, N.2    Tepp, K.3    Monge, C.4    Kaambre, T.5    Sikk, P.6    Kuznetsov, A.V.7    Pison, C.8    Saks, V.9
  • 31
  • 32
    • 0034639985 scopus 로고    scopus 로고
    • Rapid spectrophotometric method for quantitation of cytochrome c release from isolated mitochondria or permeabilized cells revisited
    • DOI 10.1016/S0005-2728(00)00098-0, PII S0005272800000980
    • F. Appaix, M. Minatchy, C. Riva-Lavieille, J. Olivares, B. Antonsson, and V.A. Saks Rapid spectrophotometric method for quantitation of cytochrome c release from isolated mitochondria or permeabilized cells revisited Biochim. Biophys. Acta 1457 2000 175 181 (Pubitemid 30201481)
    • (2000) Biochimica et Biophysica Acta - Bioenergetics , vol.1457 , Issue.3 , pp. 175-181
    • Appaix, F.1    Minatchy, M.-N.2    Riva-Lavieille, C.3    Olivares, J.4    Antonsson, B.5    Saks, V.A.6
  • 34
    • 0020490497 scopus 로고
    • Quantification of the contribution of various steps to the control of mitochondrial respiration
    • A.K. Groen, R.J. Wanders, H.V. Westerhoff, R. van der Meer, and J.M. Tager Quantification of the contribution of various steps to the control of mitochondrial respiration J. Biol. Chem. 257 1982 2754 2757
    • (1982) J. Biol. Chem. , vol.257 , pp. 2754-2757
    • Groen, A.K.1    Wanders, R.J.2    Westerhoff, H.V.3    Van Der Meer, R.4    Tager, J.M.5
  • 35
    • 0026802334 scopus 로고
    • Metabolic control analysis: A survey of its theoretical and experimental development
    • D.A. Fell Metabolic control analysis: a survey of its theoretical and experimental development Biochem. J. 286 1992 313 330
    • (1992) Biochem. J. , vol.286 , pp. 313-330
    • Fell, D.A.1
  • 37
    • 0029039749 scopus 로고
    • Distribution of flux control among the enzymes of mitochondrial oxidative phosphorylation in calcium-activated saponin-skinned rat musculus soleus fibers
    • E. Wisniewski, F.N. Gellerich, and W.S. Kunz Distribution of flux control among the enzymes of mitochondrial oxidative phosphorylation in calcium-activated saponin-skinned rat musculus soleus fibers Eur. J. Biochem. 230 1995 549 554
    • (1995) Eur. J. Biochem. , vol.230 , pp. 549-554
    • Wisniewski, E.1    Gellerich, F.N.2    Kunz, W.S.3
  • 38
    • 0030891949 scopus 로고    scopus 로고
    • Application of inhibitor titrations for the detection of oxidative phosphorylation defects in saponin-skinned muscle fibers of patients with mitochondrial diseases
    • DOI 10.1016/S0925-4439(96)00072-5, PII S0925443996000725
    • A.V. Kuznetsov, K. Winkler, E. Kirches, H. Lins, H. Feistner, and W.S. Kunz Application of inhibitor titrations for the detection of oxidative phosphorylation defects in saponin-skinned muscle fibers of patients with mitochondrial diseases Biochim. Biophys. Acta 1360 1997 142 150 (Pubitemid 27171146)
    • (1997) Biochimica et Biophysica Acta - Molecular Basis of Disease , vol.1360 , Issue.2 , pp. 142-150
    • Kuznetsov, A.V.1    Winkler, K.2    Kirches, E.3    Lins, H.4    Feistner, H.5    Kunz, W.S.6
  • 40
    • 35348932862 scopus 로고    scopus 로고
    • Flux control analysis of mitochondrial oxidative phosphorylation in rat skeletal muscle: Pyruvate and palmitoyl-carnitine as substrates give different control patterns
    • DOI 10.1007/s00421-007-0544-2
    • A.J. Fritzen, N. Grunnet, and B. Quistorff Flux control analysis of mitochondrial oxidative phosphorylation in rat skeletal muscle: pyruvate and palmitoyl-carnitine as substrates give different control patterns Eur. J. Appl. Physiol. 101 2007 679 689 (Pubitemid 47604005)
    • (2007) European Journal of Applied Physiology , vol.101 , Issue.6 , pp. 679-689
    • Fritzen, A.J.1    Grunnet, N.2    Quistorff, B.3
  • 41
    • 0024504975 scopus 로고
    • Stable and dynamic forms of cytoskeletal proteins in slow axonal transport
    • T. Tashiro, and J. Komiya Stable and dynamic forms of cytoskeletal proteins in slow axonal transport J. Neurosci. 9 1989 760 768 (Pubitemid 19085862)
    • (1989) Journal of Neuroscience , vol.9 , Issue.3 , pp. 760-768
    • Tashiro, T.1    Komiya, Y.2
  • 42
    • 0023829224 scopus 로고
    • A monoclonal antibody against the type II isotype of β-tubulin. Preparation of isotypically altered tubulin
    • A. Banerjee, M.C. Roach, K.A. Wall, M.A. Lopata, D.W. Cleveland, and R.F. Ludueña A monoclonal antibody against the type II isotype of beta-tubulin. Preparation of isotypically altered tubulin J. Biol. Chem. 263 1988 3029 3034 (Pubitemid 18062960)
    • (1988) Journal of Biological Chemistry , vol.263 , Issue.6 , pp. 3029-3034
    • Banerjee, A.1    Roach, M.C.2    Wall, K.A.3    Lopata, M.A.4    Cleveland, D.W.5    Luduena, R.F.6
  • 44
    • 0021050976 scopus 로고
    • Creatine kinase of heart mitochondria: No changes in its kinetic properties after inhibition of the adenine nucleotide translocator
    • F.N. Gellerich, M. Schlame, and V.A. Saks Creatine kinase of heart mitochondria: no changes in its kinetic properties after inhibition of the adenine nucleotide translocator Biomed. Biochim. Acta 42 1983 1335 1337 (Pubitemid 14160904)
    • (1983) Biomedica Biochimica Acta , vol.42 , Issue.10 , pp. 1335-1337
    • Gellerich, F.N.1    Schlame, M.2    Saks, V.A.3
  • 45
    • 0025029198 scopus 로고
    • Imaging cytoskeleton-mitochondrial membrane attachments by embedment-free electron microscopy of saponin-extracted cells
    • A. Lin, G. Krockmalnic, and S. Penman Imaging cytoskeleton-mitochondrial membrane attachments by embedment-free electron microscopy of saponin-extracted cells Proc. Natl. Acad. Sci. U. S. A. 87 1990 8565 8569
    • (1990) Proc. Natl. Acad. Sci. U. S. A. , vol.87 , pp. 8565-8569
    • Lin, A.1    Krockmalnic, G.2    Penman, S.3
  • 46
    • 0032806261 scopus 로고    scopus 로고
    • Oxidative myocytes of heart and skeletal muscle express abundant sarcomeric mitochondrial creatine kinase
    • DOI 10.1023/A:1003748108062
    • W.N. Qin, Z. Khuchua, J. Boero, R.M. Payne, and A.W. Strauss Oxidative myocytes of heart and skeletal muscle express abundant sarcomeric mitochondrial creatine kinase Histochem. J. 31 1999 357 365 (Pubitemid 29362820)
    • (1999) Histochemical Journal , vol.31 , Issue.6 , pp. 357-365
    • Qin, W.1    Khuchua, Z.2    Boero, J.3    Payne, R.M.4    Strauss, A.W.5
  • 47
    • 79551585807 scopus 로고    scopus 로고
    • Metabolic control analysis of integrated energy metabolism in permeabilized cardiomyocytes - Experimental study
    • K. Tepp, N. Timohhina, V. Chekulayev, I. Shevchuk, T. Kaambre, and V. Saks Metabolic control analysis of integrated energy metabolism in permeabilized cardiomyocytes - experimental study Acta Biochim. Pol. 57 2010 421 430
    • (2010) Acta Biochim. Pol. , vol.57 , pp. 421-430
    • Tepp, K.1    Timohhina, N.2    Chekulayev, V.3    Shevchuk, I.4    Kaambre, T.5    Saks, V.6
  • 48
    • 77949634569 scopus 로고    scopus 로고
    • Structure and organization of mitochondrial respiratory complexes: A new understanding of an old subject
    • G. Lenaz, and M.L. Genova Structure and organization of mitochondrial respiratory complexes: a new understanding of an old subject Antioxid. Redox Signal. 12 2010 961 1008
    • (2010) Antioxid. Redox Signal. , vol.12 , pp. 961-1008
    • Lenaz, G.1    Genova, M.L.2
  • 50
    • 56349087328 scopus 로고    scopus 로고
    • Supramolecular organization of protein complexes in the mitochondrial inner membrane
    • J. Vonck, and E. Schäfer Supramolecular organization of protein complexes in the mitochondrial inner membrane Biochim. Biophys. Acta 1793 2009 117 124
    • (2009) Biochim. Biophys. Acta , vol.1793 , pp. 117-124
    • Vonck, J.1    Schäfer, E.2
  • 52
    • 0035851099 scopus 로고    scopus 로고
    • The ratio of oxidative phosphorylation complexes I-V in bovine heart mitochondria and the composition of respiratory chain supercomplexes
    • H. Schägger, and K. Pfeiffer The ratio of oxidative phosphorylation complexes I-V in bovine heart mitochondria and the composition of respiratory chain supercomplexes J. Biol. Chem. 276 2001 37861 37867
    • (2001) J. Biol. Chem. , vol.276 , pp. 37861-37867
    • Schägger, H.1    Pfeiffer, K.2
  • 53
    • 4344630010 scopus 로고    scopus 로고
    • Significance of respirasomes for the assembly/stability of human respiratory chain complex I
    • DOI 10.1074/jbc.M404033200
    • H. Schägger, R. de Coo, M.F. Bauer, S. Hofmann, C. Godinot, and U. Brandt Significance of respirasomes for the assembly/stability of human respiratory chain complex I J. Biol. Chem. 279 2004 36349 36353 (Pubitemid 39128972)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.35 , pp. 36349-36353
    • Schagger, H.1    De Coo, R.2    Bauer, M.F.3    Hofmann, S.4    Godino, C.5    Brandt, U.6
  • 55
    • 0022790702 scopus 로고
    • The random collision model and a critical assessment of diffusion and collision in mitochondrial electron transport
    • C.R. Hackenbrock, B. Chazotte, and S.S. Gupte The random collision model and a critical assessment of diffusion and collision in mitochondrial electron transport J. Bioenerg. Biomembr. 18 1986 331 368
    • (1986) J. Bioenerg. Biomembr. , vol.18 , pp. 331-368
    • Hackenbrock, C.R.1    Chazotte, B.2    Gupte, S.S.3
  • 57
    • 0037072776 scopus 로고    scopus 로고
    • Tubulin is an inherent component of mitochondrial membranes that interacts with the voltage-dependent anion channel
    • M. Carre, N. Andre, G. Carles, H. Borghi, L. Brichese, C. Briand, and D. Braguer Tubulin is an inherent component of mitochondrial membranes that interacts with the voltage-dependent anion channel J. Biol. Chem. 277 2002 33664 33669
    • (2002) J. Biol. Chem. , vol.277 , pp. 33664-33669
    • Carre, M.1    Andre, N.2    Carles, G.3    Borghi, H.4    Brichese, L.5    Briand, C.6    Braguer, D.7
  • 58
    • 78650332649 scopus 로고    scopus 로고
    • Free tubulin modulates mitochondrial membrane potential in cancer cells
    • E.N. Maldonado, J. Patnaik, M.R. Mullins, and J.J. Lemasters Free tubulin modulates mitochondrial membrane potential in cancer cells Cancer Res. 70 2010 10192 10201
    • (2010) Cancer Res. , vol.70 , pp. 10192-10201
    • Maldonado, E.N.1    Patnaik, J.2    Mullins, M.R.3    Lemasters, J.J.4
  • 63
    • 75149115122 scopus 로고    scopus 로고
    • Control of mitochondrial transport and localization in neurons
    • A.F. MacAskill, and J.T. Kittler Control of mitochondrial transport and localization in neurons Trends Cell Biol. 20 2010 102 112
    • (2010) Trends Cell Biol. , vol.20 , pp. 102-112
    • Macaskill, A.F.1    Kittler, J.T.2
  • 66
    • 84865472739 scopus 로고    scopus 로고
    • Membrane lipid composition regulates tubulin interaction with mitochondrial voltage-dependent anion channel
    • T.K. Rostovtseva, P.A. Gurnev, M.Y. Chen, and S.M. Bezrukov Membrane lipid composition regulates tubulin interaction with mitochondrial voltage-dependent anion channel J. Biol. Chem. 287 2012 29589 29598
    • (2012) J. Biol. Chem. , vol.287 , pp. 29589-29598
    • Rostovtseva, T.K.1    Gurnev, P.A.2    Chen, M.Y.3    Bezrukov, S.M.4
  • 68
    • 0035910495 scopus 로고    scopus 로고
    • Altered mitochondrial sensitivity for ADP and maintenance of creatine-stimulated respiration in oxidative striated muscles from VDAC1-deficient mice
    • DOI 10.1074/jbc.M006587200
    • K. Anflous, D.D. Armstrong, and W.J. Craigen Altered mitochondrial sensitivity for ADP and maintenance of creatine-stimulated respiration in oxidative striated muscles from VDAC-1 deficient mice J. Biol. Chem. 276 2001 1954 1960 (Pubitemid 32109673)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.3 , pp. 1954-1960
    • Anflous, K.1    Armstrong, D.D.2    Craigen, W.J.3
  • 70
    • 33847135285 scopus 로고    scopus 로고
    • VDAC1 serves as a mitochondrial binding site for hexokinase in oxidative muscles
    • DOI 10.1016/j.bbabio.2006.11.013, PII S0005272806003604
    • K. Anflous-Pharayra, Z.J. Cai, and W.J. Craigen VDAC1 serves as a mitochondrial binding site for hexokinase in oxidative muscles Biochim. Biophys. Acta 1767 2007 136 142 (Pubitemid 46282604)
    • (2007) Biochimica et Biophysica Acta - Bioenergetics , vol.1767 , Issue.2 , pp. 136-142
    • Anflous-Pharayra, K.1    Cai, Z.-J.2    Craigen, W.J.3
  • 72
    • 84865177226 scopus 로고    scopus 로고
    • Warburg revisited: Regulation of mitochondrial metabolism by voltage-dependent anion channels in cancer cells
    • E.N. Maldonado, and J.J. Lemasters Warburg revisited: regulation of mitochondrial metabolism by voltage-dependent anion channels in cancer cells J. Pharmacol. Exp. Ther. 342 2012 637 641
    • (2012) J. Pharmacol. Exp. Ther. , vol.342 , pp. 637-641
    • Maldonado, E.N.1    Lemasters, J.J.2
  • 73
    • 46649106720 scopus 로고    scopus 로고
    • Hexokinase II detachment from mitochondria triggers apoptosis through the permeability transition pore independent of voltage-dependent anion channels
    • F. Chiara, D. Castellaro, O. Marin, V. Petronilli, W.S. Brusilow, M. Juhaszova, S.J. Solott, M. Forte, P. Bernardi, and A. Rasola Hexokinase II detachment from mitochondria triggers apoptosis through the permeability transition pore independent of voltage-dependent anion channels PLoS One 3 2008 e1852
    • (2008) PLoS One , vol.3 , pp. 1852
    • Chiara, F.1    Castellaro, D.2    Marin, O.3    Petronilli, V.4    Brusilow, W.S.5    Juhaszova, M.6    Solott, S.J.7    Forte, M.8    Bernardi, P.9    Rasola, A.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.