메뉴 건너뛰기




Volumn 411, Issue 1-2, 2016, Pages 261-270

Effects of mild hyperhomocysteinemia on electron transport chain complexes, oxidative stress, and protein expression in rat cardiac mitochondria

Author keywords

Electron transport chain; Heart; Homocysteine; Mitochondria; Oxidative stress; Protein expression

Indexed keywords

MITOCHONDRIAL PROTEIN; MULTIENZYME COMPLEX;

EID: 84957439132     PISSN: 03008177     EISSN: 15734919     Source Type: Journal    
DOI: 10.1007/s11010-015-2588-7     Document Type: Article
Times cited : (29)

References (51)
  • 1
    • 19144371112 scopus 로고    scopus 로고
    • Is homocysteine important as risk factor for coronary heart disease?
    • PID: 15871863
    • Cesari M, Rossi GP, Sticchi D, Pessina AC (2005) Is homocysteine important as risk factor for coronary heart disease? Nutr Metab Cardiovasc Dis 15:140–147. doi:10.1016/j.numecd.2004.04.002
    • (2005) Nutr Metab Cardiovasc Dis , vol.15 , pp. 140-147
    • Cesari, M.1    Rossi, G.P.2    Sticchi, D.3    Pessina, A.C.4
  • 3
    • 54249099902 scopus 로고    scopus 로고
    • Effect of anti-oxidant treatment on hyperhomocysteinemia induced myocardial fibrosis and diastolic dysfunction
    • PID: 18971097
    • Joseph J, Joseph L, Devi S, Kennedy RH (2008) Effect of anti-oxidant treatment on hyperhomocysteinemia induced myocardial fibrosis and diastolic dysfunction. J Heart Lung Transplant 27:1237–1241. doi:10.1016/j.healun.2008.07.024
    • (2008) J Heart Lung Transplant , vol.27 , pp. 1237-1241
    • Joseph, J.1    Joseph, L.2    Devi, S.3    Kennedy, R.H.4
  • 5
    • 84867334140 scopus 로고    scopus 로고
    • The effects of homocysteine-related compounds on cardiac contractility, coronary flow, and oxidative stress markers in isolated rat heart
    • COI: 1:CAS:528:DC%2BC38XhsVCjsrzK, PID: 22821198
    • Zivkovic V, Jakovljevic V, Djordjevic D, Vuletic M, Barudzic N, Djuric D (2012) The effects of homocysteine-related compounds on cardiac contractility, coronary flow, and oxidative stress markers in isolated rat heart. Mol Cell Biochem 370:59–67. doi:10.1007/s11010-012-1398-4
    • (2012) Mol Cell Biochem , vol.370 , pp. 59-67
    • Zivkovic, V.1    Jakovljevic, V.2    Djordjevic, D.3    Vuletic, M.4    Barudzic, N.5    Djuric, D.6
  • 6
    • 33846250329 scopus 로고    scopus 로고
    • Hyperhomocysteinemia alters cardiac substrate metabolism by impairing nitric oxide bioavailability through oxidative stress
    • COI: 1:CAS:528:DC%2BD2sXisV2iuw%3D%3D, PID: 17200441
    • Suematsu N, Ojaimi C, Kinugawa S, Wang Z, Xu X, Koller A, Recchia FA, Hintze TH (2007) Hyperhomocysteinemia alters cardiac substrate metabolism by impairing nitric oxide bioavailability through oxidative stress. Circulation 115:255–262
    • (2007) Circulation , vol.115 , pp. 255-262
    • Suematsu, N.1    Ojaimi, C.2    Kinugawa, S.3    Wang, Z.4    Xu, X.5    Koller, A.6    Recchia, F.A.7    Hintze, T.H.8
  • 7
    • 84862809910 scopus 로고    scopus 로고
    • Homocysteine induces cardiomyocyte dysfunction and apoptosis through p38 MAPK-mediated increase in oxidant stress
    • COI: 1:CAS:528:DC%2BC38XjtlSms7c%3D, PID: 22227328
    • Wang X, Cui L, Joseph J, Jiang B, Pimental D, Handy DE, Liao R, Loscalyo J (2012) Homocysteine induces cardiomyocyte dysfunction and apoptosis through p38 MAPK-mediated increase in oxidant stress. J Mol Cell Cardiol 52:753–760
    • (2012) J Mol Cell Cardiol , vol.52 , pp. 753-760
    • Wang, X.1    Cui, L.2    Joseph, J.3    Jiang, B.4    Pimental, D.5    Handy, D.E.6    Liao, R.7    Loscalyo, J.8
  • 8
    • 67650753876 scopus 로고    scopus 로고
    • The treatment of hyperhomocysteinemia
    • COI: 1:CAS:528:DC%2BD1MXitlyntrc%3D, PID: 18729731
    • Maron BA, Loscalzo J (2009) The treatment of hyperhomocysteinemia. Annu Rev Med 60:39–54. doi:10.1146/annurev.med.60.041807.123308
    • (2009) Annu Rev Med , vol.60 , pp. 39-54
    • Maron, B.A.1    Loscalzo, J.2
  • 9
    • 79959521169 scopus 로고    scopus 로고
    • Homocysteine enriched diet leads to prolonged QT interval and reduced left ventricular performance in telemetric monitored mice
    • COI: 1:CAS:528:DC%2BC3MXotVyqsL8%3D, PID: 20227264
    • Rosenberger D, Gargoum R, Tyagi N, Metreveli N, Sen U, Maldonado C, Tyagi S (2011) Homocysteine enriched diet leads to prolonged QT interval and reduced left ventricular performance in telemetric monitored mice. Nutr Metab Cardiovasc Dis 21:492–498. doi:10.1016/j.numecd.2009.11.014
    • (2011) Nutr Metab Cardiovasc Dis , vol.21 , pp. 492-498
    • Rosenberger, D.1    Gargoum, R.2    Tyagi, N.3    Metreveli, N.4    Sen, U.5    Maldonado, C.6    Tyagi, S.7
  • 10
    • 34250180943 scopus 로고    scopus 로고
    • Homocysteine induces cell death in H9C2 cardiomyocytes through the generation of peroxynitrite
    • COI: 1:CAS:528:DC%2BD2sXmsFyltbo%3D, PID: 17544363
    • Levrand S, Pacher P, Pesse B, Rolli J, Feihl F, Waeber B, Liaudet L (2007) Homocysteine induces cell death in H9C2 cardiomyocytes through the generation of peroxynitrite. Biochem Biophys Res Commun 359:445–450
    • (2007) Biochem Biophys Res Commun , vol.359 , pp. 445-450
    • Levrand, S.1    Pacher, P.2    Pesse, B.3    Rolli, J.4    Feihl, F.5    Waeber, B.6    Liaudet, L.7
  • 11
    • 79952771094 scopus 로고    scopus 로고
    • Homocysteine induces oxidative-nitrative stress in heart of rats: prevention by folic acid
    • COI: 1:CAS:528:DC%2BC3MXhs1CqtLc%3D, PID: 21076891
    • Kolling J, Scherer EB, da Cunha AA, da Cunha MJ, Wyse ATS (2011) Homocysteine induces oxidative-nitrative stress in heart of rats: prevention by folic acid. Cardiovasc Toxicol 11:67–73. doi:10.1007/s12012-010-9094-7
    • (2011) Cardiovasc Toxicol , vol.11 , pp. 67-73
    • Kolling, J.1    Scherer, E.B.2    da Cunha, A.A.3    da Cunha, M.J.4    Wyse, A.T.S.5
  • 12
    • 80054757193 scopus 로고    scopus 로고
    • Methionine and homocysteine modulate the rate of ROS generation of isolated mitochondria in vitro
    • COI: 1:CAS:528:DC%2BC3MXpvFOqu74%3D, PID: 21748404
    • Gomez J, Sanchez-Roman I, Gomez A, Sanchez C, Suarez H, Lopez-Torres M, Barja G (2011) Methionine and homocysteine modulate the rate of ROS generation of isolated mitochondria in vitro. J Bioenerg Biomembr 43:377–386. doi:10.1007/s10863-011-9368-1
    • (2011) J Bioenerg Biomembr , vol.43 , pp. 377-386
    • Gomez, J.1    Sanchez-Roman, I.2    Gomez, A.3    Sanchez, C.4    Suarez, H.5    Lopez-Torres, M.6    Barja, G.7
  • 13
    • 0034624197 scopus 로고    scopus 로고
    • Homocysteine-induced changes in mRNA levels of genes coding for cytoplasmic- and endoplasmic reticulum-resident stress proteins in neuronal cell cultures
    • COI: 1:CAS:528:DC%2BD3cXoslCqurg%3D, PID: 11113529
    • Althausen S, Paschen W (2000) Homocysteine-induced changes in mRNA levels of genes coding for cytoplasmic- and endoplasmic reticulum-resident stress proteins in neuronal cell cultures. Mol Brain Res 84:32–40
    • (2000) Mol Brain Res , vol.84 , pp. 32-40
    • Althausen, S.1    Paschen, W.2
  • 14
    • 0036890065 scopus 로고    scopus 로고
    • Homocysteine determinants and the evidence to what extent homocysteine determines the risk of coronary heart disease
    • PID: 12429870
    • De Bree A, Verschuren WMM, Kromhout D, Kluijtmans LAJ, Blom HJ (2002) Homocysteine determinants and the evidence to what extent homocysteine determines the risk of coronary heart disease. Pharmacol Rev 54:599–618
    • (2002) Pharmacol Rev , vol.54 , pp. 599-618
    • De Bree, A.1    Verschuren, W.M.M.2    Kromhout, D.3    Kluijtmans, L.A.J.4    Blom, H.J.5
  • 15
    • 0037339694 scopus 로고    scopus 로고
    • Increased superoxide production in coronary arteries in hyperhomocysteinemia. Role of tumor necrosis factor-α, NAD(P)H oxidase, and inducible nitric oxide synthase
    • COI: 1:CAS:528:DC%2BD3sXhslWhsbY%3D, PID: 12615666
    • Ungvari Z, Csiszar A, Edwards JG, Kaminski PM, Wolin MS, Kaley G, Koller A (2003) Increased superoxide production in coronary arteries in hyperhomocysteinemia. Role of tumor necrosis factor-α, NAD(P)H oxidase, and inducible nitric oxide synthase. Arterioscler Thromb Vasc Biol 23:418–424
    • (2003) Arterioscler Thromb Vasc Biol , vol.23 , pp. 418-424
    • Ungvari, Z.1    Csiszar, A.2    Edwards, J.G.3    Kaminski, P.M.4    Wolin, M.S.5    Kaley, G.6    Koller, A.7
  • 16
    • 27744601111 scopus 로고    scopus 로고
    • Reactive oxygen species mediates homocysteine-induced mitchondrial biogenesis in human endothelial cells modulation by antioxidants
    • COI: 1:CAS:528:DC%2BD2MXht1WjurvN
    • Perez-de-Arce K, Foncea R, Leighton F (2005) Reactive oxygen species mediates homocysteine-induced mitchondrial biogenesis in human endothelial cells modulation by antioxidants. Biochim Biophys Res Commun 338:1103–1109
    • (2005) Biochim Biophys Res Commun , vol.338 , pp. 1103-1109
    • Perez-de-Arce, K.1    Foncea, R.2    Leighton, F.3
  • 17
    • 42549135938 scopus 로고    scopus 로고
    • Homocysteine inhibits arterial endothelial cell growth through transcriptional downregulation of fibroblast growth factor-2 involving G protein and DNA methylation
    • COI: 1:CAS:528:DC%2BD1cXkvVenu7s%3D, PID: 18309099
    • Chang P-Y, Lu S-C, Lee C-M, Chen Y-J, Dugan TA, Huang W-H, Chang S-F, Liao WSL, Chen C-H, Lee Y-T (2008) Homocysteine inhibits arterial endothelial cell growth through transcriptional downregulation of fibroblast growth factor-2 involving G protein and DNA methylation. Circ Res 102:933–941. doi:10.1161/CIRCRESAHA.108.171082
    • (2008) Circ Res , vol.102 , pp. 933-941
    • Chang, P.-Y.1    Lu, S.-C.2    Lee, C.-M.3    Chen, Y.-J.4    Dugan, T.A.5    Huang, W.-H.6    Chang, S.-F.7    Liao, W.S.L.8    Chen, C.-H.9    Lee, Y.-T.10
  • 19
    • 84901916385 scopus 로고    scopus 로고
    • Hyperhomocysteinemia and bleomycin hydrolase modulate the expression of mouse brain proteins involved in neurodegeneration
    • PID: 24496069
    • Suszyńska-Zajczyk J, Łuczak M, Marczak Ł, Jakubowski H (2014) Hyperhomocysteinemia and bleomycin hydrolase modulate the expression of mouse brain proteins involved in neurodegeneration. J Alzheimers Dis 40:713–726. doi:10.3233/JAD-132033
    • (2014) J Alzheimers Dis , vol.40 , pp. 713-726
    • Suszyńska-Zajczyk, J.1    Łuczak, M.2    Marczak, Ł.3    Jakubowski, H.4
  • 20
    • 84907494813 scopus 로고    scopus 로고
    • Hyperhomocysteinemia-induced oxidative stress differentially alters proteasome composition and activities in heart and aorta
    • COI: 1:CAS:528:DC%2BC2cXhsFWltrzN, PID: 25194809
    • Derouiche F, Bôle-Feysot C, Naïmi D, Coëffier M (2014) Hyperhomocysteinemia-induced oxidative stress differentially alters proteasome composition and activities in heart and aorta. Biochem Biophys Res Commun 452:740–745. doi:10.1016/j.bbrc.2014.08.141
    • (2014) Biochem Biophys Res Commun , vol.452 , pp. 740-745
    • Derouiche, F.1    Bôle-Feysot, C.2    Naïmi, D.3    Coëffier, M.4
  • 21
    • 84919678388 scopus 로고    scopus 로고
    • Methyl donor deficiency in H9c2 cardiomyoblasts induces ER stress as an important part of the proteome response
    • COI: 1:CAS:528:DC%2BC2cXitV2mtrzJ, PID: 25486180
    • Martinez E, Deval C, Jousse C, Mazur A, Brachet P, Comte B (2015) Methyl donor deficiency in H9c2 cardiomyoblasts induces ER stress as an important part of the proteome response. Int J Biochem Cell Biol 59:62–72. doi:10.1016/j.biocel.2014.11.013
    • (2015) Int J Biochem Cell Biol , vol.59 , pp. 62-72
    • Martinez, E.1    Deval, C.2    Jousse, C.3    Mazur, A.4    Brachet, P.5    Comte, B.6
  • 23
    • 79961210608 scopus 로고    scopus 로고
    • The role of mitochondrial membrane potential in ischemic heart failure
    • COI: 1:CAS:528:DC%2BC3MXhtVWrsr7L, PID: 21703366
    • Kadenbach B, Ramzan R, Moosdorf R, Vogt S (2011) The role of mitochondrial membrane potential in ischemic heart failure. Mitochondrion 11:700–706. doi:10.1016/j.mito.2011.06.001
    • (2011) Mitochondrion , vol.11 , pp. 700-706
    • Kadenbach, B.1    Ramzan, R.2    Moosdorf, R.3    Vogt, S.4
  • 24
    • 80255129364 scopus 로고    scopus 로고
    • Mitochondrial respiratory control and early defects of oxidative phosphorylation in the failing human heart
    • COI: 1:CAS:528:DC%2BC3MXhtl2gsrjI, PID: 21871578
    • Lemieux H, Semsroth S, Antretter H, Höfer D, Gnaiger E (2011) Mitochondrial respiratory control and early defects of oxidative phosphorylation in the failing human heart. Int J Biochem Cell Biol 43:1729–1738. doi:10.1016/j.biocel.2011.08.008
    • (2011) Int J Biochem Cell Biol , vol.43 , pp. 1729-1738
    • Lemieux, H.1    Semsroth, S.2    Antretter, H.3    Höfer, D.4    Gnaiger, E.5
  • 25
    • 84859884412 scopus 로고    scopus 로고
    • Mitochondria and cardiovascular aging
    • COI: 1:CAS:528:DC%2BC38XlsVaktLk%3D, PID: 22499901
    • Dai DF, Rabinovitch PS, Ungvari Z (2012) Mitochondria and cardiovascular aging. Circ Res 110:1109–1124. doi:10.1161/CIRCRESAHA.111.246140
    • (2012) Circ Res , vol.110 , pp. 1109-1124
    • Dai, D.F.1    Rabinovitch, P.S.2    Ungvari, Z.3
  • 26
    • 43349084839 scopus 로고    scopus 로고
    • Hydrogen sulfide inhibits myocardial injury induced by homocysteine in rats
    • COI: 1:CAS:528:DC%2BD1cXlsVOgsLg%3D, PID: 18071843
    • Chang L, Geng B, Yu F, Zhao J, Jiang H, Du J, Tang C (2008) Hydrogen sulfide inhibits myocardial injury induced by homocysteine in rats. Amino Acids 34:573–585
    • (2008) Amino Acids , vol.34 , pp. 573-585
    • Chang, L.1    Geng, B.2    Yu, F.3    Zhao, J.4    Jiang, H.5    Du, J.6    Tang, C.7
  • 28
    • 34247596471 scopus 로고    scopus 로고
    • MTHFR Gene polymorphisms, B-vitamins and hyperhomocystinemia in young and middle-aged acute myocardial infarction patients
    • COI: 1:CAS:528:DC%2BD2sXlt1Citbw%3D, PID: 17412321
    • Angeline T, Jeyaraj N, Tsongalis GJ (2007) MTHFR Gene polymorphisms, B-vitamins and hyperhomocystinemia in young and middle-aged acute myocardial infarction patients. Exp Mol Pathol 82:227–233. doi:10.1016/j.yexmp.2007.02.005
    • (2007) Exp Mol Pathol , vol.82 , pp. 227-233
    • Angeline, T.1    Jeyaraj, N.2    Tsongalis, G.J.3
  • 30
    • 8444229293 scopus 로고    scopus 로고
    • Oxidative modification of rat cardiac mitochondrial membranes and myofibrils by hydroxyl radicals
    • COI: 1:CAS:528:DC%2BD2MXhtlWjtg%3D%3D, PID: 15638120
    • Babusikova E, Kaplan P, Lehotsky J, Jesenak M, Dobrota D (2004) Oxidative modification of rat cardiac mitochondrial membranes and myofibrils by hydroxyl radicals. Gen Physiol Biophys 23:327–335
    • (2004) Gen Physiol Biophys , vol.23 , pp. 327-335
    • Babusikova, E.1    Kaplan, P.2    Lehotsky, J.3    Jesenak, M.4    Dobrota, D.5
  • 31
    • 0035968183 scopus 로고    scopus 로고
    • Modulation of mitochondrial function by hydrogen peroxide
    • Nulton-Persson AC, Szweda LI (2011) Modulation of mitochondrial function by hydrogen peroxide. J Biol Chem 276:23357–23361
    • (2011) J Biol Chem , vol.276 , pp. 23357-23361
    • Nulton-Persson, A.C.1    Szweda, L.I.2
  • 32
    • 0037974679 scopus 로고    scopus 로고
    • Mitochondrial complex I, aconitase, and succinate dehydrogenase during hypoxia-reoxygenation: modulation of enzyme activities by MnSOD
    • COI: 1:CAS:528:DC%2BD3sXls1Wmtrc%3D, PID: 12665464
    • Powell CS, Jackson RM (2003) Mitochondrial complex I, aconitase, and succinate dehydrogenase during hypoxia-reoxygenation: modulation of enzyme activities by MnSOD. Am J Physiol Lung Cell Mol Physiol 285:L189–L198
    • (2003) Am J Physiol Lung Cell Mol Physiol , vol.285 , pp. L189-L198
    • Powell, C.S.1    Jackson, R.M.2
  • 33
    • 35948941541 scopus 로고    scopus 로고
    • Oxidative modifications of cardiac mitochondria and inhibition of cytochrome c oxidase activity by 4-hydroxynonenal
    • Kaplan P, Tatarkova Z, Racay P, Lehotsky J, Pavlikova M, Dobrota D (2007) Oxidative modifications of cardiac mitochondria and inhibition of cytochrome c oxidase activity by 4-hydroxynonenal. Redox Rep 12:212–218
    • (2007) Redox Rep , vol.12 , pp. 212-218
    • Kaplan, P.1    Tatarkova, Z.2    Racay, P.3    Lehotsky, J.4    Pavlikova, M.5    Dobrota, D.6
  • 37
    • 4444245523 scopus 로고    scopus 로고
    • Taurine protected myocardial mitochondria injury induced by hyperhomocysteinemia in rats
    • COI: 1:CAS:528:DC%2BD2cXmsVKktLc%3D, PID: 15309570
    • Chang L, Xu J, Yu F, Zhao J, Tang X, Tang C (2004) Taurine protected myocardial mitochondria injury induced by hyperhomocysteinemia in rats. Amino Acids 27:37–48
    • (2004) Amino Acids , vol.27 , pp. 37-48
    • Chang, L.1    Xu, J.2    Yu, F.3    Zhao, J.4    Tang, X.5    Tang, C.6
  • 38
    • 0036774355 scopus 로고    scopus 로고
    • Generation of nitrotyrosine precedes activation of metalloproteinase in myocardium of hyperhomocysteinemic rats
    • COI: 1:CAS:528:DC%2BD3sXhtVamu7c%3D, PID: 12470508
    • Sood HS, Cox MJ, Tyagi SC (2002) Generation of nitrotyrosine precedes activation of metalloproteinase in myocardium of hyperhomocysteinemic rats. Antioxid Redox Signal 4:799–804
    • (2002) Antioxid Redox Signal , vol.4 , pp. 799-804
    • Sood, H.S.1    Cox, M.J.2    Tyagi, S.C.3
  • 39
    • 57249095767 scopus 로고    scopus 로고
    • Lipid peroxidation of membrane phospholipids generates hydroxyl-alkenals and oxidized phospholipids active in physiological and/or pathological conditions
    • PID: 18977338
    • Catalá A (2009) Lipid peroxidation of membrane phospholipids generates hydroxyl-alkenals and oxidized phospholipids active in physiological and/or pathological conditions. Chem Phys Lipids 157:1–11. doi:10.1016/j.chemphyslip.2008.09.004
    • (2009) Chem Phys Lipids , vol.157 , pp. 1-11
    • Catalá, A.1
  • 40
    • 0031035742 scopus 로고    scopus 로고
    • Metabolism of homocysteine thiolactone in human cell cultures. Possible mechanism for pathological consequences of elevated homocysteine levels
    • COI: 1:CAS:528:DyaK2sXls12qug%3D%3D, PID: 8999883
    • Jakubowski H (1997) Metabolism of homocysteine thiolactone in human cell cultures. Possible mechanism for pathological consequences of elevated homocysteine levels. J Biol Chem 272:1935–1942
    • (1997) J Biol Chem , vol.272 , pp. 1935-1942
    • Jakubowski, H.1
  • 41
    • 0032778517 scopus 로고    scopus 로고
    • Protein homocysteinylation: possible mechanism underlying pathological consequences of elevated homocysteine levels
    • COI: 1:CAS:528:DyaK1MXotVKitbs%3D, PID: 10593875
    • Jakubowski H (1999) Protein homocysteinylation: possible mechanism underlying pathological consequences of elevated homocysteine levels. FASEB J 13:2277–2283
    • (1999) FASEB J , vol.13 , pp. 2277-2283
    • Jakubowski, H.1
  • 42
    • 84895909640 scopus 로고    scopus 로고
    • Identification of N-homocysteinylation sites in plasma proteins
    • COI: 1:CAS:528:DC%2BC3sXhvVKisL%2FP, PID: 24292153
    • Sikora M, Marczak Ł, Kubalska J, Graban A, Jakubowski H (2014) Identification of N-homocysteinylation sites in plasma proteins. Amino Acids 46:235–244. doi:10.1007/s00726-013-1617-7
    • (2014) Amino Acids , vol.46 , pp. 235-244
    • Sikora, M.1    Marczak, Ł.2    Kubalska, J.3    Graban, A.4    Jakubowski, H.5
  • 43
    • 68949107623 scopus 로고    scopus 로고
    • Structural and functional organization of the mitochondrial respiratory chain: dynamic super-assembly
    • COI: 1:CAS:528:DC%2BD1MXhtVentbrL, PID: 19711505
    • Lenaz G, Genova ML (2009) Structural and functional organization of the mitochondrial respiratory chain: dynamic super-assembly. Int J Biochem Cell Biol 41:1750–1772
    • (2009) Int J Biochem Cell Biol , vol.41 , pp. 1750-1772
    • Lenaz, G.1    Genova, M.L.2
  • 44
    • 0035799352 scopus 로고    scopus 로고
    • Combined and individual mitochondrial HSP60 and HSP10 expression in cardiac myocytes protects mitochondrial function and prevents apoptotic cell deaths induced by simulated ischemia-reoxygenation
    • COI: 1:CAS:528:DC%2BD3MXjsFKisLs%3D, PID: 11282911
    • Lin KM, Lin B, Lian IY, Mestril R, Scheffler IE, Dillmann WH (2001) Combined and individual mitochondrial HSP60 and HSP10 expression in cardiac myocytes protects mitochondrial function and prevents apoptotic cell deaths induced by simulated ischemia-reoxygenation. Circulation 103:1787–1792
    • (2001) Circulation , vol.103 , pp. 1787-1792
    • Lin, K.M.1    Lin, B.2    Lian, I.Y.3    Mestril, R.4    Scheffler, I.E.5    Dillmann, W.H.6
  • 46
    • 84867401800 scopus 로고    scopus 로고
    • Native rates of superoxide production from multiple sites in isolated mitochondria measured using endogenous reportetrs
    • COI: 1:CAS:528:DC%2BC38Xhtl2rsr%2FJ, PID: 22940066
    • Quinlan CL, Treberg JR, Perevoshchikova IV, Orr AL, Brand MD (2012) Native rates of superoxide production from multiple sites in isolated mitochondria measured using endogenous reportetrs. Free Radic Biol Med 53:1807–1817. doi:10.1016/j.freeradbiomed.2012.08.015
    • (2012) Free Radic Biol Med , vol.53 , pp. 1807-1817
    • Quinlan, C.L.1    Treberg, J.R.2    Perevoshchikova, I.V.3    Orr, A.L.4    Brand, M.D.5
  • 48
    • 84863474422 scopus 로고    scopus 로고
    • Mitochondrial ATP synthase: architecture, function and pathology
    • COI: 1:CAS:528:DC%2BC38XisFShtr4%3D, PID: 21874297
    • Jonckheere AI, Smeitink JAM, Rodenburg RJT (2012) Mitochondrial ATP synthase: architecture, function and pathology. J Inherit Metab Dis 35:211–225. doi:10.1007/s10545-011-9382-9
    • (2012) J Inherit Metab Dis , vol.35 , pp. 211-225
    • Jonckheere, A.I.1    Smeitink, J.A.M.2    Rodenburg, R.J.T.3
  • 49
    • 84856510610 scopus 로고    scopus 로고
    • VDAC, a multi-functional mitochondrial protein as a pharmacological target
    • COI: 1:CAS:528:DC%2BC38XhvVOltrw%3D, PID: 21530686
    • Shoshan-Barmatz V, Ben-Hail D (2012) VDAC, a multi-functional mitochondrial protein as a pharmacological target. Mitochondrion 12:24–34
    • (2012) Mitochondrion , vol.12 , pp. 24-34
    • Shoshan-Barmatz, V.1    Ben-Hail, D.2
  • 50
    • 0037458619 scopus 로고    scopus 로고
    • Voltage-dependent anion channels control the release of the superoxide anion from mitochondria to cytosol
    • COI: 1:CAS:528:DC%2BD3sXht1aqs78%3D, PID: 12482755
    • Han D, Antunes F, Canali R, Rettori D, Cadenas E (2003) Voltage-dependent anion channels control the release of the superoxide anion from mitochondria to cytosol. J Biol Chem 278:5557–5563
    • (2003) J Biol Chem , vol.278 , pp. 5557-5563
    • Han, D.1    Antunes, F.2    Canali, R.3    Rettori, D.4    Cadenas, E.5
  • 51
    • 84859777452 scopus 로고    scopus 로고
    • The role of VDAC in cell death: friend or foe?
    • COI: 1:CAS:528:DC%2BC38Xls1emu70%3D, PID: 22062421
    • McCommis KS, Baines CP (2012) The role of VDAC in cell death: friend or foe? Biochim Biophys Acta 1818:1444–1450. doi:10.1016/j.bbamem.2011.10.025
    • (2012) Biochim Biophys Acta , vol.1818 , pp. 1444-1450
    • McCommis, K.S.1    Baines, C.P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.