메뉴 건너뛰기




Volumn 45, Issue 1, 2013, Pages 90-98

Src kinases are important regulators of mitochondrial functions

Author keywords

Mitochondria; Oxidative phosphorylation; Src kinases; Tyrosine phosphorylation

Indexed keywords

BOSUTINIB; CISPLATIN; DASATINIB; DOXORUBICIN; FLUOROURACIL; IMATINIB; KX01; PHOSPHOTRANSFERASE; PHOSPHOTRANSFERASE INHIBITOR; ROTTLERIN; SARACATINIB; SRC KINASE; TYROSINE; UNCLASSIFIED DRUG;

EID: 84870695545     PISSN: 13572725     EISSN: 18785875     Source Type: Journal    
DOI: 10.1016/j.biocel.2012.08.014     Document Type: Article
Times cited : (58)

References (115)
  • 2
    • 0033520310 scopus 로고    scopus 로고
    • Nitric oxide controls src kinase activity through a sulfhydryl group modification-mediated Tyr-527-independent and Tyr-416-linked mechanism
    • A.A. Akhand, M. Pu, T. Senga, M. Kato, H. Suzuki, and T. Miyata Nitric oxide controls src kinase activity through a sulfhydryl group modification-mediated Tyr-527-independent and Tyr-416-linked mechanism Journal of Biological Chemistry 274 1999 25821 25826
    • (1999) Journal of Biological Chemistry , vol.274 , pp. 25821-25826
    • Akhand, A.A.1    Pu, M.2    Senga, T.3    Kato, M.4    Suzuki, H.5    Miyata, T.6
  • 5
    • 9144249116 scopus 로고    scopus 로고
    • Glutaredoxin 2 catalyzes the reversible oxidation and glutathionylation of mitochondrial membrane thiol proteins: Implications for mitochondrial redox regulation and antioxidant defense
    • S.M. Beer, E.R. Taylor, S.E. Brown, C.C. Dahm, N.J. Costa, and M.J. Runswick Glutaredoxin 2 catalyzes the reversible oxidation and glutathionylation of mitochondrial membrane thiol proteins: implications for mitochondrial redox regulation and antioxidant defense Journal of Biological Chemistry 279 2004 47939 47951
    • (2004) Journal of Biological Chemistry , vol.279 , pp. 47939-47951
    • Beer, S.M.1    Taylor, E.R.2    Brown, S.E.3    Dahm, C.C.4    Costa, N.J.5    Runswick, M.J.6
  • 6
    • 0033517301 scopus 로고    scopus 로고
    • The tyrosine kinase lck is required for CD95-independent caspase-8 activation and apoptosis in response to ionizing radiation
    • C. Belka, P. Marini, A. Lepple-Wienhues, W. Budach, A. Jekle, and M. Los The tyrosine kinase lck is required for CD95-independent caspase-8 activation and apoptosis in response to ionizing radiation Oncogene 18 1999 4983 4992
    • (1999) Oncogene , vol.18 , pp. 4983-4992
    • Belka, C.1    Marini, P.2    Lepple-Wienhues, A.3    Budach, W.4    Jekle, A.5    Los, M.6
  • 7
    • 3543025709 scopus 로고    scopus 로고
    • Phosphorylation of Y845 on the epidermal growth factor receptor mediates binding to the mitochondrial protein cytochrome c oxidase subunit II
    • J.L. Boerner, M.L. Demory, C. Silva, and S.J. Parsons Phosphorylation of Y845 on the epidermal growth factor receptor mediates binding to the mitochondrial protein cytochrome c oxidase subunit II Molecular and Cellular Biology 24 2004 7059 7071
    • (2004) Molecular and Cellular Biology , vol.24 , pp. 7059-7071
    • Boerner, J.L.1    Demory, M.L.2    Silva, C.3    Parsons, S.J.4
  • 8
    • 7944223078 scopus 로고    scopus 로고
    • Structure and regulation of Src family kinases
    • T.J. Boggon, and M.J. Eck Structure and regulation of Src family kinases Oncogene 23 2004 7918 7927
    • (2004) Oncogene , vol.23 , pp. 7918-7927
    • Boggon, T.J.1    Eck, M.J.2
  • 9
    • 0022519497 scopus 로고
    • Expression of the v-src or v-fps oncogene increases fructose 2,6-bisphosphate in chick-embryo fibroblasts, Novel mechanism for the stimulation of glycolysis by retroviruses
    • L. Bosca, M. Mojena, J. Ghysdael, G.G. Rousseau, and L. Hue Expression of the v-src or v-fps oncogene increases fructose 2,6-bisphosphate in chick-embryo fibroblasts, Novel mechanism for the stimulation of glycolysis by retroviruses Biochemical Journal 236 1986 595 599
    • (1986) Biochemical Journal , vol.236 , pp. 595-599
    • Bosca, L.1    Mojena, M.2    Ghysdael, J.3    Rousseau, G.G.4    Hue, L.5
  • 12
    • 2442717798 scopus 로고    scopus 로고
    • Mitochondrial AKAP121 binds and targets protein tyrosine phosphatase D1, a novel positive regulator of src signaling
    • L. Cardone, A. Carlucci, A. Affaitati, A. Livigni, T. DeCristofaro, and C. Garbi Mitochondrial AKAP121 binds and targets protein tyrosine phosphatase D1, a novel positive regulator of src signaling Molecular and Cellular Biology 24 2004 4613 4626
    • (2004) Molecular and Cellular Biology , vol.24 , pp. 4613-4626
    • Cardone, L.1    Carlucci, A.2    Affaitati, A.3    Livigni, A.4    Decristofaro, T.5    Garbi, C.6
  • 13
    • 18444375552 scopus 로고    scopus 로고
    • A-kinase anchor protein 84/121 are targeted to mitochondria and mitotic spindles by overlapping amino-terminal motifs
    • L. Cardone, T. de Cristofaro, A. Affaitati, C. Garbi, M.D. Ginsberg, and M. Saviano A-kinase anchor protein 84/121 are targeted to mitochondria and mitotic spindles by overlapping amino-terminal motifs Journal of Molecular Biology 320 2002 663 675
    • (2002) Journal of Molecular Biology , vol.320 , pp. 663-675
    • Cardone, L.1    De Cristofaro, T.2    Affaitati, A.3    Garbi, C.4    Ginsberg, M.D.5    Saviano, M.6
  • 16
    • 78650120951 scopus 로고    scopus 로고
    • Mitochondrial tyrosine phosphoproteome: New insights from an up-to-date analysis
    • L. Cesaro, and M. Salvi Mitochondrial tyrosine phosphoproteome: new insights from an up-to-date analysis Biofactors 36 2010 437 450
    • (2010) Biofactors , vol.36 , pp. 437-450
    • Cesaro, L.1    Salvi, M.2
  • 17
    • 0001433788 scopus 로고
    • A method for the localization of sites for oxidative phosphorylation
    • B. Chance, and G.R. Williams A method for the localization of sites for oxidative phosphorylation Nature 176 1955 250 254
    • (1955) Nature , vol.176 , pp. 250-254
    • Chance, B.1    Williams, G.R.2
  • 18
    • 0030972746 scopus 로고    scopus 로고
    • Organelle-specific targeting of protein kinase AII (PKAII). Molecular and in situ characterization of murine A kinase anchor proteins that recruit regulatory subunits of PKAII to the cytoplasmic surface of mitochondria
    • Q. Chen, R.Y. Lin, and C.S. Rubin Organelle-specific targeting of protein kinase AII (PKAII). Molecular and in situ characterization of murine A kinase anchor proteins that recruit regulatory subunits of PKAII to the cytoplasmic surface of mitochondria Journal of Biological Chemistry 272 1997 15247 15257
    • (1997) Journal of Biological Chemistry , vol.272 , pp. 15247-15257
    • Chen, Q.1    Lin, R.Y.2    Rubin, C.S.3
  • 19
    • 75349111140 scopus 로고    scopus 로고
    • Regulation of succinate dehydrogenase activity by SIRT3 in mammalian mitochondria
    • H. Cimen, M.J. Han, Y. Yang, Q. Tong, H. Koc, and E.C. Koc Regulation of succinate dehydrogenase activity by SIRT3 in mammalian mitochondria Biochemistry 49 2010 304 311
    • (2010) Biochemistry , vol.49 , pp. 304-311
    • Cimen, H.1    Han, M.J.2    Yang, Y.3    Tong, Q.4    Koc, H.5    Koc, E.C.6
  • 20
    • 84861491693 scopus 로고    scopus 로고
    • Src kinase inhibitors: Promising cancer therapeutics?
    • H. Creedon, and V.G. Brunton Src kinase inhibitors: promising cancer therapeutics? Critical Reviews in Oncogenesis 17 2012 145 159
    • (2012) Critical Reviews in Oncogenesis , vol.17 , pp. 145-159
    • Creedon, H.1    Brunton, V.G.2
  • 21
    • 0000203434 scopus 로고    scopus 로고
    • Phosphodiesterase 4 inhibitors, structurally unrelated to rolipram, as promising agents for the treatment of asthma and other pathologies
    • V. Dal Piaz, and M.P. Giovannoni Phosphodiesterase 4 inhibitors, structurally unrelated to rolipram, as promising agents for the treatment of asthma and other pathologies European Journal of Medical Chemistry 35 2000 463 480
    • (2000) European Journal of Medical Chemistry , vol.35 , pp. 463-480
    • Dal Piaz, V.1    Giovannoni, M.P.2
  • 23
    • 32944459966 scopus 로고    scopus 로고
    • Differential steady-state tyrosine phosphorylation of two oligomeric forms of mitochondrial F0F1ATPsynthase: A structural proteomic analysis
    • F. Di Pancrazio, E. Bisetto, V. Alverdi, I. Mavelli, G. Esposito, and G. Lippe Differential steady-state tyrosine phosphorylation of two oligomeric forms of mitochondrial F0F1ATPsynthase: a structural proteomic analysis Proteomics 6 2006 921 926
    • (2006) Proteomics , vol.6 , pp. 921-926
    • Di Pancrazio, F.1    Bisetto, E.2    Alverdi, V.3    Mavelli, I.4    Esposito, G.5    Lippe, G.6
  • 24
    • 1442310922 scopus 로고    scopus 로고
    • Control of mitochondrial integrity by Bcl-2 family members and caspase-independent cell death
    • M. Donovan, and T.G. Cotter Control of mitochondrial integrity by Bcl-2 family members and caspase-independent cell death Biochimica et Biophysica Acta 1644 2004 133 147
    • (2004) Biochimica et Biophysica Acta , vol.1644 , pp. 133-147
    • Donovan, M.1    Cotter, T.G.2
  • 27
    • 51749116257 scopus 로고    scopus 로고
    • Phosphoproteome analysis of isoflurane-protected heart mitochondria: Phosphorylation of adenine nucleotide translocator-1 on Tyr194 regulates mitochondrial function
    • J. Feng, M. Zhu, M.C. Schaub, P. Gehrig, B. Roschitzki, and E. Lucchinetti Phosphoproteome analysis of isoflurane-protected heart mitochondria: phosphorylation of adenine nucleotide translocator-1 on Tyr194 regulates mitochondrial function Cardiovascular Research 80 2008 20 29
    • (2008) Cardiovascular Research , vol.80 , pp. 20-29
    • Feng, J.1    Zhu, M.2    Schaub, M.C.3    Gehrig, P.4    Roschitzki, B.5    Lucchinetti, E.6
  • 28
    • 17344365733 scopus 로고    scopus 로고
    • Ultrastructural zonal heterogeneity of hepatocytes and mitochondria within the hepatic acinus during liver regeneration after partial hepatectomy
    • D. Ferri, L. Moro, M. Mastrodonato, F. Capuano, E. Marra, and G.E. Liquori Ultrastructural zonal heterogeneity of hepatocytes and mitochondria within the hepatic acinus during liver regeneration after partial hepatectomy Biologie Cellulaire 97 2005 277 288
    • (2005) Biologie Cellulaire , vol.97 , pp. 277-288
    • Ferri, D.1    Moro, L.2    Mastrodonato, M.3    Capuano, F.4    Marra, E.5    Liquori, G.E.6
  • 29
    • 0344629380 scopus 로고    scopus 로고
    • Bcl-2 family members as sentinels of cellular integrity and role of mitochondrial intermembrane space proteins in apoptotic cell death
    • N. Festjens, M. van Gurp, G. van Loo, X. Saelens, and P. Vandenabeele Bcl-2 family members as sentinels of cellular integrity and role of mitochondrial intermembrane space proteins in apoptotic cell death Acta Haematologica 111 2004 7 27
    • (2004) Acta Haematologica , vol.111 , pp. 7-27
    • Festjens, N.1    Van Gurp, M.2    Van Loo, G.3    Saelens, X.4    Vandenabeele, P.5
  • 30
    • 0037150728 scopus 로고    scopus 로고
    • Src in cancer: Deregulation and consequences for cell behaviour
    • M.C. Frame Src in cancer: deregulation and consequences for cell behaviour Biochimica et Biophysica Acta 1602 2002 114 130
    • (2002) Biochimica et Biophysica Acta , vol.1602 , pp. 114-130
    • Frame, M.C.1
  • 32
    • 0042665896 scopus 로고    scopus 로고
    • Identification of proteins undergoing glutathionylation in oxidatively stressed hepatocytes and hepatoma cells
    • M. Fratelli, H. Demol, M. Puype, S. Casagrande, P. Villa, and I. Eberini Identification of proteins undergoing glutathionylation in oxidatively stressed hepatocytes and hepatoma cells Proteomics 3 2003 1154 1161
    • (2003) Proteomics , vol.3 , pp. 1154-1161
    • Fratelli, M.1    Demol, H.2    Puype, M.3    Casagrande, S.4    Villa, P.5    Eberini, I.6
  • 33
    • 80053594491 scopus 로고    scopus 로고
    • Src-family tyrosine kinases as therapeutic targets in advanced cancer
    • I.H. Gelman Src-family tyrosine kinases as therapeutic targets in advanced cancer Frontiers in Bioscience 3 2011 801 807
    • (2011) Frontiers in Bioscience , vol.3 , pp. 801-807
    • Gelman, I.H.1
  • 34
    • 22544453858 scopus 로고    scopus 로고
    • Intracellular reactive oxygen species activate Src tyrosine kinase during cell adhesion and anchorage-dependent cell growth
    • E. Giannoni, F. Buricchi, G. Raugei, G. Ramponi, and P. Chiarugi Intracellular reactive oxygen species activate Src tyrosine kinase during cell adhesion and anchorage-dependent cell growth Molecular and Cellular Biology 25 2005 6391 6403
    • (2005) Molecular and Cellular Biology , vol.25 , pp. 6391-6403
    • Giannoni, E.1    Buricchi, F.2    Raugei, G.3    Ramponi, G.4    Chiarugi, P.5
  • 36
    • 73849131902 scopus 로고    scopus 로고
    • Lyn-mediated mitochondrial tyrosine phosphorylation is required to preserve mitochondrial integrity in early liver regeneration
    • E. Gringeri, A. Carraro, E. Tibaldi, F.E. D'Amico, M. Mancon, and A. Toninello Lyn-mediated mitochondrial tyrosine phosphorylation is required to preserve mitochondrial integrity in early liver regeneration Biochemical Journal 425 2010 401 412
    • (2010) Biochemical Journal , vol.425 , pp. 401-412
    • Gringeri, E.1    Carraro, A.2    Tibaldi, E.3    D'Amico, F.E.4    Mancon, M.5    Toninello, A.6
  • 37
    • 79551584971 scopus 로고    scopus 로고
    • Regulation of intermediary metabolism by protein acetylation
    • K.L. Guan, and Y. Xiong Regulation of intermediary metabolism by protein acetylation Trends in Biochemical Sciences 36 2011 108 116
    • (2011) Trends in Biochemical Sciences , vol.36 , pp. 108-116
    • Guan, K.L.1    Xiong, Y.2
  • 40
    • 70149085247 scopus 로고    scopus 로고
    • Dys-regulated activation of a Src tyroine kinase Hck at the Golgi disturbs N-glycosylation of a cytokine receptor Fms
    • R. Hassan, S. Suzu, M. Hiyoshi, N. Takahashi-Makise, T. Ueno, and T. Agatsuma Dys-regulated activation of a Src tyroine kinase Hck at the Golgi disturbs N-glycosylation of a cytokine receptor Fms Journal of Cellular Physiology 221 2009 458 468
    • (2009) Journal of Cellular Physiology , vol.221 , pp. 458-468
    • Hassan, R.1    Suzu, S.2    Hiyoshi, M.3    Takahashi-Makise, N.4    Ueno, T.5    Agatsuma, T.6
  • 44
    • 77950806433 scopus 로고    scopus 로고
    • SIRT3 regulates mitochondrial fatty-acid oxidation by reversible enzyme deacetylation
    • M.D. Hirschey, T. Shimazu, E. Goetzman, E. Jing, B. Schwer, and D.B. Lombard SIRT3 regulates mitochondrial fatty-acid oxidation by reversible enzyme deacetylation Nature 464 2010 121 125
    • (2010) Nature , vol.464 , pp. 121-125
    • Hirschey, M.D.1    Shimazu, T.2    Goetzman, E.3    Jing, E.4    Schwer, B.5    Lombard, D.B.6
  • 45
    • 10344242925 scopus 로고    scopus 로고
    • Kinase signaling cascades in the mitochondrion: A matter of life or death
    • C. Horbinski, and C.T. Chu Kinase signaling cascades in the mitochondrion: a matter of life or death Free Radical Biology and Medicine 38 2005 2 11
    • (2005) Free Radical Biology and Medicine , vol.38 , pp. 2-11
    • Horbinski, C.1    Chu, C.T.2
  • 46
    • 0030903895 scopus 로고    scopus 로고
    • Identification of a novel protein kinase A anchoring protein that binds both type i and type II regulatory subunits
    • L.J. Huang, K. Durick, J.A. Weiner, J. Chun, and S.S. Taylor Identification of a novel protein kinase A anchoring protein that binds both type I and type II regulatory subunits Journal of Biological Chemistry 272 1997 8057 8064
    • (1997) Journal of Biological Chemistry , vol.272 , pp. 8057-8064
    • Huang, L.J.1    Durick, K.2    Weiner, J.A.3    Chun, J.4    Taylor, S.S.5
  • 47
    • 0346734197 scopus 로고    scopus 로고
    • Rosmarinic acid induces p56lck-dependent apoptosis in Jurkat and peripheral T cells via mitochondrial pathway independent from Fas/Fas ligand interaction
    • Y.G. Hur, Y. Yun, and J. Won Rosmarinic acid induces p56lck-dependent apoptosis in Jurkat and peripheral T cells via mitochondrial pathway independent from Fas/Fas ligand interaction Journal of Immunology 172 2004 79 87
    • (2004) Journal of Immunology , vol.172 , pp. 79-87
    • Hur, Y.G.1    Yun, Y.2    Won, J.3
  • 48
    • 4544235743 scopus 로고    scopus 로고
    • C-Src and cooperating partners in human cancer
    • R. Ishizawar, and S.J. Parsons c-Src and cooperating partners in human cancer Cancer Cell 6 2004 209 214
    • (2004) Cancer Cell , vol.6 , pp. 209-214
    • Ishizawar, R.1    Parsons, S.J.2
  • 49
    • 0035726625 scopus 로고    scopus 로고
    • Targeting of the c-Abl tyrosine kinase to mitochondria in endoplasmic reticulum stress-induced apoptosis
    • Y. Ito, P. Pandey, N. Mishra, S. Kumar, N. Narula, and S. Kharbanda Targeting of the c-Abl tyrosine kinase to mitochondria in endoplasmic reticulum stress-induced apoptosis Molecular and Cellular Biology 21 2001 6233 6242
    • (2001) Molecular and Cellular Biology , vol.21 , pp. 6233-6242
    • Ito, Y.1    Pandey, P.2    Mishra, N.3    Kumar, S.4    Narula, N.5    Kharbanda, S.6
  • 50
    • 22544444671 scopus 로고    scopus 로고
    • Mitochondrial Dok-4 recruits Src kinase and regulates NF-kappaB activation in endothelial cells
    • S. Itoh, S. Lemay, M. Osawa, W. Che, Y. Duan, and A. Tompkins Mitochondrial Dok-4 recruits Src kinase and regulates NF-kappaB activation in endothelial cells Journal of Biological Chemistry 280 2005 26383 26396
    • (2005) Journal of Biological Chemistry , vol.280 , pp. 26383-26396
    • Itoh, S.1    Lemay, S.2    Osawa, M.3    Che, W.4    Duan, Y.5    Tompkins, A.6
  • 52
    • 0037044578 scopus 로고    scopus 로고
    • Activated pp60c-Src leads to elevated hypoxia-inducible factor (HIF)-1alpha expression under normoxia
    • R. Karni, Y. Dor, E. Keshet, O. Meyuhas, and A. Levitzki Activated pp60c-Src leads to elevated hypoxia-inducible factor (HIF)-1alpha expression under normoxia Journal of Biological Chemistry 277 2002 42919 42925
    • (2002) Journal of Biological Chemistry , vol.277 , pp. 42919-42925
    • Karni, R.1    Dor, Y.2    Keshet, E.3    Meyuhas, O.4    Levitzki, A.5
  • 53
    • 33644614520 scopus 로고    scopus 로고
    • HIF-1-mediated expression of pyruvate dehydrogenase kinase: A metabolic switch required for cellular adaptation to hypoxia
    • J.W. Kim, I. Tchernyshyov, G.L. Semenza, and C.V. Dang HIF-1-mediated expression of pyruvate dehydrogenase kinase: a metabolic switch required for cellular adaptation to hypoxia Cell Metabolism 3 2006 177 185
    • (2006) Cell Metabolism , vol.3 , pp. 177-185
    • Kim, J.W.1    Tchernyshyov, I.2    Semenza, G.L.3    Dang, C.V.4
  • 55
    • 0036210579 scopus 로고    scopus 로고
    • Signal transduction to mitochondrial ATP synthase: Evidence that PDGF-dependent phosphorylation of the delta-subunit occurs in several cell lines, involves tyrosine, and is modulated by lysophosphatidic acid
    • Y.H. Ko, W. Pan, C. Inoue, and P.L. Pedersen Signal transduction to mitochondrial ATP synthase: evidence that PDGF-dependent phosphorylation of the delta-subunit occurs in several cell lines, involves tyrosine, and is modulated by lysophosphatidic acid Mitochondrion 1 2002 339 348
    • (2002) Mitochondrion , vol.1 , pp. 339-348
    • Ko, Y.H.1    Pan, W.2    Inoue, C.3    Pedersen, P.L.4
  • 56
    • 0035907396 scopus 로고    scopus 로고
    • Targeting of the c-Abl tyrosine kinase to mitochondria in the necrotic cell death response to oxidative stress
    • S. Kumar, A. Bharti, N.C. Mishra, D. Raina, S. Kharbanda, and S. Saxena Targeting of the c-Abl tyrosine kinase to mitochondria in the necrotic cell death response to oxidative stress Journal of Biological Chemistry 276 2001 17281 17285
    • (2001) Journal of Biological Chemistry , vol.276 , pp. 17281-17285
    • Kumar, S.1    Bharti, A.2    Mishra, N.C.3    Raina, D.4    Kharbanda, S.5    Saxena, S.6
  • 57
    • 33646480748 scopus 로고    scopus 로고
    • Protein kinase PKC delta and c-Abl are required for mitochondrial apoptosis induction by genotoxic stress in the absence of p53, p73 and Fas receptor
    • M. Lasfer, L. Davenne, N. Vadrot, C. Alexia, Z. Sadji-Ouatas, and A.F. Bringuier Protein kinase PKC delta and c-Abl are required for mitochondrial apoptosis induction by genotoxic stress in the absence of p53, p73 and Fas receptor FEBS Letters 580 2006 2547 2552
    • (2006) FEBS Letters , vol.580 , pp. 2547-2552
    • Lasfer, M.1    Davenne, L.2    Vadrot, N.3    Alexia, C.4    Sadji-Ouatas, Z.5    Bringuier, A.F.6
  • 58
    • 20644466225 scopus 로고    scopus 로고
    • Tumor necrosis factor increases mitochondrial oxidant production and induces expression of uncoupling protein-2 in the regenerating mice [correction of rat] liver
    • F.Y. Lee, Y. Li, H. Zhu, S. Yang, H.Z. Lin, and M. Trush Tumor necrosis factor increases mitochondrial oxidant production and induces expression of uncoupling protein-2 in the regenerating mice [correction of rat] liver Hepatology 29 1999 677 687
    • (1999) Hepatology , vol.29 , pp. 677-687
    • Lee, F.Y.1    Li, Y.2    Zhu, H.3    Yang, S.4    Lin, H.Z.5    Trush, M.6
  • 59
    • 2442714587 scopus 로고    scopus 로고
    • Control of mitochondrial membrane potential and ROS formation by reversible phosphorylation of cytochrome c oxidase
    • I. Lee, E. Bender, and B. Kadenbach Control of mitochondrial membrane potential and ROS formation by reversible phosphorylation of cytochrome c oxidase Molecular and Cellular Biochemistry 234-235 2002 63 70
    • (2002) Molecular and Cellular Biochemistry , vol.234-235 , pp. 63-70
    • Lee, I.1    Bender, E.2    Kadenbach, B.3
  • 61
    • 33746656190 scopus 로고    scopus 로고
    • New prospects for an old enzyme: Mammalian cytochrome c is tyrosine-phosphorylated in vivo
    • I. Lee, A.R. Salomon, K. Yu, J.W. Doan, L.I. Grossman, and M. Huttemann New prospects for an old enzyme: mammalian cytochrome c is tyrosine- phosphorylated in vivo Biochemistry 45 2006 9121 9128
    • (2006) Biochemistry , vol.45 , pp. 9121-9128
    • Lee, I.1    Salomon, A.R.2    Yu, K.3    Doan, J.W.4    Grossman, L.I.5    Huttemann, M.6
  • 62
    • 0032546955 scopus 로고    scopus 로고
    • Reversible inactivation of protein-tyrosine phosphatase 1B in A431 cells stimulated with epidermal growth factor
    • S.R. Lee, K.S. Kwon, S.R. Kim, and S.G. Rhee Reversible inactivation of protein-tyrosine phosphatase 1B in A431 cells stimulated with epidermal growth factor Journal of Biological Chemistry 273 1998 15366 15372
    • (1998) Journal of Biological Chemistry , vol.273 , pp. 15366-15372
    • Lee, S.R.1    Kwon, K.S.2    Kim, S.R.3    Rhee, S.G.4
  • 65
    • 34547616284 scopus 로고    scopus 로고
    • Dual role of mitochondrial reactive oxygen species in hypoxia signaling: Activation of nuclear factor-kappa B via c-SRC and oxidant-dependent cell death
    • J.M. Lluis, F. Buricchi, P. Chiarugi, A. Morales, and J.C. Fernandez-Checa Dual role of mitochondrial reactive oxygen species in hypoxia signaling: activation of nuclear factor-kappa B via c-SRC and oxidant-dependent cell death Cancer Research 67 2007 7368 7377
    • (2007) Cancer Research , vol.67 , pp. 7368-7377
    • Lluis, J.M.1    Buricchi, F.2    Chiarugi, P.3    Morales, A.4    Fernandez-Checa, J.C.5
  • 67
    • 0034656414 scopus 로고    scopus 로고
    • Differential requirement for p56lck in HIV-tat versus TNF-induced cellular responses: Effects on NF-kappa B, activator protein-1, c-Jun N-terminal kinase, and apoptosis
    • S.K. Manna, and B.B. Aggarwal Differential requirement for p56lck in HIV-tat versus TNF-induced cellular responses: effects on NF-kappa B, activator protein-1, c-Jun N-terminal kinase, and apoptosis Journal of Immunology 164 2000 5156 5166
    • (2000) Journal of Immunology , vol.164 , pp. 5156-5166
    • Manna, S.K.1    Aggarwal, B.B.2
  • 68
    • 0026720657 scopus 로고
    • Activation of 6-phosphofructo-2-kinase by pp60v-src is an indirect effect
    • M.J. Marchand, L. Maisin, L. Hue, and G.G. Rousseau Activation of 6-phosphofructo-2-kinase by pp60v-src is an indirect effect Biochemical Journal 285 Pt 2 1992 413 417
    • (1992) Biochemical Journal , vol.285 , Issue.PART 2 , pp. 413-417
    • Marchand, M.J.1    Maisin, L.2    Hue, L.3    Rousseau, G.G.4
  • 69
    • 36949083936 scopus 로고
    • Coupling of phosphorylation to electron and hydrogen transfer by a chemi-osmotic type of mechanism
    • P. Mitchell Coupling of phosphorylation to electron and hydrogen transfer by a chemi-osmotic type of mechanism Nature 191 1961 144 148
    • (1961) Nature , vol.191 , pp. 144-148
    • Mitchell, P.1
  • 71
    • 33645988520 scopus 로고    scopus 로고
    • The role of c-Src kinase in the regulation of osteoclast function
    • T. Miyazaki, S. Tanaka, A. Sanjay, and R. Baron The role of c-Src kinase in the regulation of osteoclast function Modern Rheumatology 16 2006 68 74
    • (2006) Modern Rheumatology , vol.16 , pp. 68-74
    • Miyazaki, T.1    Tanaka, S.2    Sanjay, A.3    Baron, R.4
  • 73
    • 79953719964 scopus 로고    scopus 로고
    • Role of Bcl-2 family proteins and caspases in the regulation of apoptosis
    • M.S. Ola, M. Nawaz, and H. Ahsan Role of Bcl-2 family proteins and caspases in the regulation of apoptosis Molecular and Cellular Biochemistry 351 2011 41 58
    • (2011) Molecular and Cellular Biochemistry , vol.351 , pp. 41-58
    • Ola, M.S.1    Nawaz, M.2    Ahsan, H.3
  • 74
    • 30944449043 scopus 로고    scopus 로고
    • Mitochondrial modulation: Reversible phosphorylation takes center stage?
    • D.J. Pagliarini, and J.E. Dixon Mitochondrial modulation: reversible phosphorylation takes center stage? Trends in Biochemical Sciences 31 2006 26 34
    • (2006) Trends in Biochemical Sciences , vol.31 , pp. 26-34
    • Pagliarini, D.J.1    Dixon, J.E.2
  • 75
    • 0030040319 scopus 로고    scopus 로고
    • The nuclear-encoded 18 kDa (IP) AQDQ subunit of bovine heart complex i is phosphorylated by the mitochondrial cAMP-dependent protein kinase
    • S. Papa, A.M. Sardanelli, T. Cocco, F. Speranza, S.C. Scacco, and Z. Technikova-Dobrova The nuclear-encoded 18 kDa (IP) AQDQ subunit of bovine heart complex I is phosphorylated by the mitochondrial cAMP-dependent protein kinase FEBS Letters 379 1996 299 301
    • (1996) FEBS Letters , vol.379 , pp. 299-301
    • Papa, S.1    Sardanelli, A.M.2    Cocco, T.3    Speranza, F.4    Scacco, S.C.5    Technikova-Dobrova, Z.6
  • 76
    • 33644622570 scopus 로고    scopus 로고
    • HIF-1 mediates adaptation to hypoxia by actively downregulating mitochondrial oxygen consumption
    • I. Papandreou, R.A. Cairns, L. Fontana, A.L. Lim, and N.C. Denko HIF-1 mediates adaptation to hypoxia by actively downregulating mitochondrial oxygen consumption Cell Metabolism 3 2006 187 197
    • (2006) Cell Metabolism , vol.3 , pp. 187-197
    • Papandreou, I.1    Cairns, R.A.2    Fontana, L.3    Lim, A.L.4    Denko, N.C.5
  • 77
    • 7944236785 scopus 로고    scopus 로고
    • Src family kinases, key regulators of signal transduction
    • S.J. Parsons, and J.T. Parsons Src family kinases, key regulators of signal transduction Oncogene 23 2004 7906 7909
    • (2004) Oncogene , vol.23 , pp. 7906-7909
    • Parsons, S.J.1    Parsons, J.T.2
  • 78
    • 77955235585 scopus 로고    scopus 로고
    • Phosphomimetic substitution of cytochrome C tyrosine 48 decreases respiration and binding to cardiolipin and abolishes ability to trigger downstream caspase activation
    • P. Pecina, G.G. Borisenko, N.A. Belikova, Y.Y. Tyurina, A. Pecinova, and I. Lee Phosphomimetic substitution of cytochrome C tyrosine 48 decreases respiration and binding to cardiolipin and abolishes ability to trigger downstream caspase activation Biochemistry 49 2010 6705 6714
    • (2010) Biochemistry , vol.49 , pp. 6705-6714
    • Pecina, P.1    Borisenko, G.G.2    Belikova, N.A.3    Tyurina, Y.Y.4    Pecinova, A.5    Lee, I.6
  • 79
    • 0015239241 scopus 로고
    • The glucagon-sensitive adenyl cyclase system in plasma membranes of rat liver. I. Properties
    • S.L. Pohl, L. Birnbaumer, and M. Rodbell The glucagon-sensitive adenyl cyclase system in plasma membranes of rat liver. I. Properties Journal of Biological Chemistry 246 1971 1849 1856
    • (1971) Journal of Biological Chemistry , vol.246 , pp. 1849-1856
    • Pohl, S.L.1    Birnbaumer, L.2    Rodbell, M.3
  • 80
    • 79956283619 scopus 로고    scopus 로고
    • Current status of SRC inhibitors in solid tumor malignancies
    • L.N. Puls, M. Eadens, and W. Messersmith Current status of SRC inhibitors in solid tumor malignancies The Oncologist 16 2011 566 578
    • (2011) The Oncologist , vol.16 , pp. 566-578
    • Puls, L.N.1    Eadens, M.2    Messersmith, W.3
  • 81
    • 42549153340 scopus 로고    scopus 로고
    • The PKCdelta-Abl complex communicates ER stress to the mitochondria - An essential step in subsequent apoptosis
    • X. Qi, and D. Mochly-Rosen The PKCdelta-Abl complex communicates ER stress to the mitochondria - an essential step in subsequent apoptosis Journal of Cell Science 121 2008 804 813
    • (2008) Journal of Cell Science , vol.121 , pp. 804-813
    • Qi, X.1    Mochly-Rosen, D.2
  • 82
    • 0030750736 scopus 로고    scopus 로고
    • Distinctive functions of Syk and Lyn in mediating osmotic stress- and ultraviolet C irradiation-induced apoptosis in chicken B cells
    • S. Qin, Y. Minami, T. Kurosaki, and H. Yamamura Distinctive functions of Syk and Lyn in mediating osmotic stress- and ultraviolet C irradiation-induced apoptosis in chicken B cells Journal of Biological Chemistry 272 1997 17994 17999
    • (1997) Journal of Biological Chemistry , vol.272 , pp. 17994-17999
    • Qin, S.1    Minami, Y.2    Kurosaki, T.3    Yamamura, H.4
  • 86
    • 18044384816 scopus 로고    scopus 로고
    • Tyrosine phosphorylation in mitochondria: A new frontier in mitochondrial signaling
    • M. Salvi, A.M. Brunati, and A. Toninello Tyrosine phosphorylation in mitochondria: a new frontier in mitochondrial signaling Free Radical Biology and Medicine 38 2005 1267 1277
    • (2005) Free Radical Biology and Medicine , vol.38 , pp. 1267-1277
    • Salvi, M.1    Brunati, A.M.2    Toninello, A.3
  • 87
    • 36549017624 scopus 로고    scopus 로고
    • Identification of the flavoprotein of succinate dehydrogenase and aconitase as in vitro mitochondrial substrates of Fgr tyrosine kinase
    • M. Salvi, N.A. Morrice, A.M. Brunati, and A. Toninello Identification of the flavoprotein of succinate dehydrogenase and aconitase as in vitro mitochondrial substrates of Fgr tyrosine kinase FEBS Letters 581 2007 5579 5585
    • (2007) FEBS Letters , vol.581 , pp. 5579-5585
    • Salvi, M.1    Morrice, N.A.2    Brunati, A.M.3    Toninello, A.4
  • 89
    • 30544443793 scopus 로고    scopus 로고
    • The tyrosine kinase Lck is a positive regulator of the mitochondrial apoptosis pathway by controlling Bak expression
    • A.K. Samraj, C. Stroh, U. Fischer, and K. Schulze-Osthoff The tyrosine kinase Lck is a positive regulator of the mitochondrial apoptosis pathway by controlling Bak expression Oncogene 25 2006 186 197
    • (2006) Oncogene , vol.25 , pp. 186-197
    • Samraj, A.K.1    Stroh, C.2    Fischer, U.3    Schulze-Osthoff, K.4
  • 90
    • 65549171192 scopus 로고    scopus 로고
    • Liar, a novel Lyn-binding nuclear/cytoplasmic shuttling protein that influences erythropoietin-induced differentiation
    • A.L. Samuels, S.P. Klinken, and E. Ingley Liar, a novel Lyn-binding nuclear/cytoplasmic shuttling protein that influences erythropoietin-induced differentiation Blood 113 2009 3845 3856
    • (2009) Blood , vol.113 , pp. 3845-3856
    • Samuels, A.L.1    Klinken, S.P.2    Ingley, E.3
  • 91
    • 33749469540 scopus 로고    scopus 로고
    • Occurrence of A-kinase anchor protein and associated cAMP-dependent protein kinase in the inner compartment of mammalian mitochondria
    • A.M. Sardanelli, A. Signorile, R. Nuzzi, D.D. Rasmo, Z. Technikova-Dobrova, and Z. Drahota Occurrence of A-kinase anchor protein and associated cAMP-dependent protein kinase in the inner compartment of mammalian mitochondria FEBS Letters 580 2006 5690 5696
    • (2006) FEBS Letters , vol.580 , pp. 5690-5696
    • Sardanelli, A.M.1    Signorile, A.2    Nuzzi, R.3    Rasmo, D.D.4    Technikova-Dobrova, Z.5    Drahota, Z.6
  • 92
    • 0029560855 scopus 로고
    • Characterization of proteins phosphorylated by the cAMP-dependent protein kinase of bovine heart mitochondria
    • A.M. Sardanelli, Z. Technikova-Dobrova, S.C. Scacco, F. Speranza, and S. Papa Characterization of proteins phosphorylated by the cAMP-dependent protein kinase of bovine heart mitochondria FEBS Letters 377 1995 470 474
    • (1995) FEBS Letters , vol.377 , pp. 470-474
    • Sardanelli, A.M.1    Technikova-Dobrova, Z.2    Scacco, S.C.3    Speranza, F.4    Papa, S.5
  • 94
    • 22744438100 scopus 로고    scopus 로고
    • Mitochondrial reactive oxygen species and c-Src play a critical role in hypoxic response in vascular smooth muscle cells
    • H. Sato, M. Sato, H. Kanai, T. Uchiyama, T. Iso, and Y. Ohyama Mitochondrial reactive oxygen species and c-Src play a critical role in hypoxic response in vascular smooth muscle cells Cardiovascular Research 67 2005 714 722
    • (2005) Cardiovascular Research , vol.67 , pp. 714-722
    • Sato, H.1    Sato, M.2    Kanai, H.3    Uchiyama, T.4    Iso, T.5    Ohyama, Y.6
  • 95
    • 0026163635 scopus 로고
    • ATP-producing and consuming processes of Ehrlich mouse ascites tumor cells in proliferating and resting phases
    • H. Schmidt, W. Siems, M. Muller, R. Dumdey, and S.M. Rapoport ATP-producing and consuming processes of Ehrlich mouse ascites tumor cells in proliferating and resting phases Experimental Cell Research 194 1991 122 127
    • (1991) Experimental Cell Research , vol.194 , pp. 122-127
    • Schmidt, H.1    Siems, W.2    Muller, M.3    Dumdey, R.4    Rapoport, S.M.5
  • 97
    • 35448961940 scopus 로고    scopus 로고
    • HIF-1 mediates the Warburg effect in clear cell renal carcinoma
    • G.L. Semenza HIF-1 mediates the Warburg effect in clear cell renal carcinoma Journal of Bioenergetics and Biomembranes 39 2007 231 234
    • (2007) Journal of Bioenergetics and Biomembranes , vol.39 , pp. 231-234
    • Semenza, G.L.1
  • 98
    • 67649274379 scopus 로고    scopus 로고
    • Modulation of mitochondrial K(+) permeability and reactive oxygen species production by the p13 protein of human T-cell leukemia virus type 1
    • M. Silic-Benussi, E. Cannizzaro, A. Venerando, I. Cavallari, V. Petronilli, and N. La Rocca Modulation of mitochondrial K(+) permeability and reactive oxygen species production by the p13 protein of human T-cell leukemia virus type 1 Biochimica et Biophysica Acta 1787 2009 947 954
    • (2009) Biochimica et Biophysica Acta , vol.1787 , pp. 947-954
    • Silic-Benussi, M.1    Cannizzaro, E.2    Venerando, A.3    Cavallari, I.4    Petronilli, V.5    La Rocca, N.6
  • 99
    • 0024803488 scopus 로고
    • The proteins associated with the soluble form of p36, the main target of the src oncogene product in chicken fibroblasts, are glycolytic enzymes
    • M. Simon, P.F. Spahr, and F. Dainous The proteins associated with the soluble form of p36, the main target of the src oncogene product in chicken fibroblasts, are glycolytic enzymes Biochemistry and Cell Biology - Biochimie et Biologie Cellulaire 67 1989 740 748
    • (1989) Biochemistry and Cell Biology - Biochimie et Biologie Cellulaire , vol.67 , pp. 740-748
    • Simon, M.1    Spahr, P.F.2    Dainous, F.3
  • 100
    • 46649090918 scopus 로고    scopus 로고
    • Protein tyrosine nitration - Functional alteration or just a biomarker?
    • J.M. Souza, G. Peluffo, and R. Radi Protein tyrosine nitration - functional alteration or just a biomarker? Free Radical Biology & Medicine 45 2008 357 366
    • (2008) Free Radical Biology & Medicine , vol.45 , pp. 357-366
    • Souza, J.M.1    Peluffo, G.2    Radi, R.3
  • 101
    • 15844365555 scopus 로고    scopus 로고
    • Modulation of the SH2 binding specificity and kinase activity of Src by tyrosine phosphorylation within its SH2 domain
    • D.R. Stover, P. Furet, and N.B. Lydon Modulation of the SH2 binding specificity and kinase activity of Src by tyrosine phosphorylation within its SH2 domain Journal of Biological Chemistry 271 1996 12481 12487
    • (1996) Journal of Biological Chemistry , vol.271 , pp. 12481-12487
    • Stover, D.R.1    Furet, P.2    Lydon, N.B.3
  • 102
  • 105
    • 80054045391 scopus 로고    scopus 로고
    • Interaction between the SH3 domain of Src family kinases and the proline-rich motif of HTLV-1 p13: A novel mechanism underlying delivery of Src family kinases to mitochondria
    • E. Tibaldi, A. Venerando, F. Zonta, C. Bidoia, E. Magrin, and O. Marin Interaction between the SH3 domain of Src family kinases and the proline-rich motif of HTLV-1 p13: a novel mechanism underlying delivery of Src family kinases to mitochondria Biochemical Journal 439 2011 505 516
    • (2011) Biochemical Journal , vol.439 , pp. 505-516
    • Tibaldi, E.1    Venerando, A.2    Zonta, F.3    Bidoia, C.4    Magrin, E.5    Marin, O.6
  • 106
    • 0029838226 scopus 로고    scopus 로고
    • BTK as a mediator of radiation-induced apoptosis in DT-40 lymphoma B cells
    • F.M. Uckun, K.G. Waddick, S. Mahajan, X. Jun, M. Takata, and J. Bolen BTK as a mediator of radiation-induced apoptosis in DT-40 lymphoma B cells Science 273 1996 1096 1100
    • (1996) Science , vol.273 , pp. 1096-1100
    • Uckun, F.M.1    Waddick, K.G.2    Mahajan, S.3    Jun, X.4    Takata, M.5    Bolen, J.6
  • 108
    • 77149120797 scopus 로고    scopus 로고
    • Acetylation of metabolic enzymes coordinates carbon source utilization and metabolic flux
    • Q. Wang, Y. Zhang, C. Yang, H. Xiong, Y. Lin, and J. Yao Acetylation of metabolic enzymes coordinates carbon source utilization and metabolic flux Science 327 2010 1004 1007
    • (2010) Science , vol.327 , pp. 1004-1007
    • Wang, Q.1    Zhang, Y.2    Yang, C.3    Xiong, H.4    Lin, Y.5    Yao, J.6
  • 109
    • 12444279265 scopus 로고
    • On the origin of cancer cells
    • O. Warburg On the origin of cancer cells Science 123 1956 309 314
    • (1956) Science , vol.123 , pp. 309-314
    • Warburg, O.1
  • 112
    • 46349095835 scopus 로고    scopus 로고
    • Mammalian liver cytochrome c is tyrosine-48 phosphorylated in vivo, inhibiting mitochondrial respiration
    • H. Yu, I. Lee, A.R. Salomon, K. Yu, and M. Huttemann Mammalian liver cytochrome c is tyrosine-48 phosphorylated in vivo, inhibiting mitochondrial respiration Biochimica et Biophysica Acta 1777 2008 1066 1071
    • (2008) Biochimica et Biophysica Acta , vol.1777 , pp. 1066-1071
    • Yu, H.1    Lee, I.2    Salomon, A.R.3    Yu, K.4    Huttemann, M.5
  • 113
    • 0028971637 scopus 로고
    • Phosphorylation of F1F0 ATPase delta-subunit is regulated by platelet-derived growth factor in mouse cortical neurons in vitro
    • F.X. Zhang, W. Pan, and J.B. Hutchins Phosphorylation of F1F0 ATPase delta-subunit is regulated by platelet-derived growth factor in mouse cortical neurons in vitro Journal of Neurochemistry 65 1995 2812 2815
    • (1995) Journal of Neurochemistry , vol.65 , pp. 2812-2815
    • Zhang, F.X.1    Pan, W.2    Hutchins, J.B.3
  • 114
    • 51449095730 scopus 로고    scopus 로고
    • Low-power laser irradiation activates Src tyrosine kinase through reactive oxygen species-mediated signaling pathway
    • J. Zhang, D. Xing, and X. Gao Low-power laser irradiation activates Src tyrosine kinase through reactive oxygen species-mediated signaling pathway Journal of Cellular Physiology 217 2008 518 528
    • (2008) Journal of Cellular Physiology , vol.217 , pp. 518-528
    • Zhang, J.1    Xing, D.2    Gao, X.3
  • 115
    • 84857916018 scopus 로고    scopus 로고
    • Targeting Src family kinases in anti-cancer therapies: Turning promise into triumph
    • S. Zhang, and D. Yu Targeting Src family kinases in anti-cancer therapies: turning promise into triumph Trends in Pharmacological Sciences 33 2012 122 128
    • (2012) Trends in Pharmacological Sciences , vol.33 , pp. 122-128
    • Zhang, S.1    Yu, D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.