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Volumn 75, Issue 17, 2012, Pages 5449-5462

Differential redox proteomics allows identification of proteins reversibly oxidized at cysteine residues in endothelial cells in response to acute hypoxia

Author keywords

Cell signaling; Cysteine oxidation; Post translational modifications; Redox fluorescence switch (RFS); Thiol redox proteomics; Two dimensional electrophoresis (2 DE)

Indexed keywords

CYSTEINE; HYPOXIA INDUCIBLE FACTOR; REACTIVE OXYGEN METABOLITE;

EID: 84865540710     PISSN: 18743919     EISSN: 18767737     Source Type: Journal    
DOI: 10.1016/j.jprot.2012.06.035     Document Type: Article
Times cited : (37)

References (65)
  • 1
    • 84882816411 scopus 로고    scopus 로고
    • Oxidative stress
    • Academic Press, New York, G. Fink (Ed.)
    • Sies H., Jones D. Oxidative stress. Encyclopedia of stress 2007, 45-48. Academic Press, New York. G. Fink (Ed.).
    • (2007) Encyclopedia of stress , pp. 45-48
    • Sies, H.1    Jones, D.2
  • 2
    • 34648813720 scopus 로고    scopus 로고
    • ROS as signalling molecules: mechanisms that generate specificity in ROS homeostasis
    • D'Autreaux B., Toledano M.B. ROS as signalling molecules: mechanisms that generate specificity in ROS homeostasis. Nat Rev Mol Cell Biol 2007, 8:813-824.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 813-824
    • D'Autreaux, B.1    Toledano, M.B.2
  • 3
    • 77956186783 scopus 로고    scopus 로고
    • Mitochondrial reactive oxygen species regulate cellular signaling and dictate biological outcomes
    • Hamanaka R.B., Chandel N.S. Mitochondrial reactive oxygen species regulate cellular signaling and dictate biological outcomes. Trends Biochem Sci 2010, 35:505-513.
    • (2010) Trends Biochem Sci , vol.35 , pp. 505-513
    • Hamanaka, R.B.1    Chandel, N.S.2
  • 4
    • 34548507495 scopus 로고    scopus 로고
    • Thiol oxidation in signaling and response to stress: detection and quantification of physiological and pathophysiological thiol modifications
    • Ying J., Clavreul N., Sethuraman M., Adachi T., Cohen R.A. Thiol oxidation in signaling and response to stress: detection and quantification of physiological and pathophysiological thiol modifications. Free Radic Biol Med 2007, 43:1099-1108.
    • (2007) Free Radic Biol Med , vol.43 , pp. 1099-1108
    • Ying, J.1    Clavreul, N.2    Sethuraman, M.3    Adachi, T.4    Cohen, R.A.5
  • 5
    • 34848821197 scopus 로고    scopus 로고
    • Protein sulfenation as a redox sensor: proteomics studies using a novel biotinylated dimedone analogue
    • Charles R.L., Schroder E., May G., Free P., Gaffney P.R., Wait R., et al. Protein sulfenation as a redox sensor: proteomics studies using a novel biotinylated dimedone analogue. Mol Cell Proteomics 2007, 6:1473-1484.
    • (2007) Mol Cell Proteomics , vol.6 , pp. 1473-1484
    • Charles, R.L.1    Schroder, E.2    May, G.3    Free, P.4    Gaffney, P.R.5    Wait, R.6
  • 6
    • 40849097418 scopus 로고    scopus 로고
    • Discovering mechanisms of signaling-mediated cysteine oxidation
    • Poole L.B., Nelson K.J. Discovering mechanisms of signaling-mediated cysteine oxidation. Curr Opin Chem Biol 2008, 12:18-24.
    • (2008) Curr Opin Chem Biol , vol.12 , pp. 18-24
    • Poole, L.B.1    Nelson, K.J.2
  • 7
    • 77952077940 scopus 로고    scopus 로고
    • The redox switch: dynamic regulation of protein function by cysteine modifications
    • Spadaro D., Yun B.W., Spoel S.H., Chu C., Wang Y.Q., Loake G.J. The redox switch: dynamic regulation of protein function by cysteine modifications. Physiol Plant 2010, 138:360-371.
    • (2010) Physiol Plant , vol.138 , pp. 360-371
    • Spadaro, D.1    Yun, B.W.2    Spoel, S.H.3    Chu, C.4    Wang, Y.Q.5    Loake, G.J.6
  • 8
    • 79960286223 scopus 로고    scopus 로고
    • Signal transduction by reactive oxygen species
    • Finkel T. Signal transduction by reactive oxygen species. J Cell Biol 2011, 194:7-15.
    • (2011) J Cell Biol , vol.194 , pp. 7-15
    • Finkel, T.1
  • 9
    • 1542328892 scopus 로고    scopus 로고
    • S-nitrosylation: a potential new paradigm in signal transduction
    • Martínez-Ruiz A., Lamas S. S-nitrosylation: a potential new paradigm in signal transduction. Cardiovasc Res 2004, 62:43-52.
    • (2004) Cardiovasc Res , vol.62 , pp. 43-52
    • Martínez-Ruiz, A.1    Lamas, S.2
  • 10
    • 34250738347 scopus 로고    scopus 로고
    • Signalling by NO-induced protein S-nitrosylation and S-glutathionylation: convergences and divergences
    • Martínez-Ruiz A., Lamas S. Signalling by NO-induced protein S-nitrosylation and S-glutathionylation: convergences and divergences. Cardiovasc Res 2007, 75:220-228.
    • (2007) Cardiovasc Res , vol.75 , pp. 220-228
    • Martínez-Ruiz, A.1    Lamas, S.2
  • 11
    • 79851510345 scopus 로고    scopus 로고
    • Chemical 'omics' approaches for understanding protein cysteine oxidation in biology
    • Leonard S.E., Carroll K.S. Chemical 'omics' approaches for understanding protein cysteine oxidation in biology. Curr Opin Chem Biol 2011, 15:88-102.
    • (2011) Curr Opin Chem Biol , vol.15 , pp. 88-102
    • Leonard, S.E.1    Carroll, K.S.2
  • 13
    • 79957441981 scopus 로고    scopus 로고
    • The disulfide proteome and other reactive cysteine proteomes: analysis and functional significance
    • Lindahl M., Mata-Cabana A., Kieselbach T. The disulfide proteome and other reactive cysteine proteomes: analysis and functional significance. Antioxid Redox Signal 2011, 14:2581-2642.
    • (2011) Antioxid Redox Signal , vol.14 , pp. 2581-2642
    • Lindahl, M.1    Mata-Cabana, A.2    Kieselbach, T.3
  • 14
    • 80053363811 scopus 로고    scopus 로고
    • Contemporary techniques for detecting and identifying proteins susceptible to reversible thiol oxidation
    • Burgoyne J.R., Eaton P. Contemporary techniques for detecting and identifying proteins susceptible to reversible thiol oxidation. Biochem Soc Trans 2011, 39:1260-1267.
    • (2011) Biochem Soc Trans , vol.39 , pp. 1260-1267
    • Burgoyne, J.R.1    Eaton, P.2
  • 15
    • 82355181024 scopus 로고    scopus 로고
    • Thiol redox proteomics seen with fluorescent eyes: the detection of cysteine oxidative modifications by fluorescence derivatization and 2-DE
    • Izquierdo-Álvarez A., Martínez-Ruiz A. Thiol redox proteomics seen with fluorescent eyes: the detection of cysteine oxidative modifications by fluorescence derivatization and 2-DE. J Proteomics 2011, 75:329-338.
    • (2011) J Proteomics , vol.75 , pp. 329-338
    • Izquierdo-Álvarez, A.1    Martínez-Ruiz, A.2
  • 16
    • 35248887983 scopus 로고    scopus 로고
    • Regulation of tissue perfusion in mammals by hypoxia-inducible factor 1
    • Semenza G.L. Regulation of tissue perfusion in mammals by hypoxia-inducible factor 1. Exp Physiol 2007, 92:988-991.
    • (2007) Exp Physiol , vol.92 , pp. 988-991
    • Semenza, G.L.1
  • 18
    • 35148888161 scopus 로고    scopus 로고
    • Life with oxygen
    • Semenza G.L. Life with oxygen. Science 2007, 318:62-64.
    • (2007) Science , vol.318 , pp. 62-64
    • Semenza, G.L.1
  • 19
    • 43649093915 scopus 로고    scopus 로고
    • Oxygen sensing by metazoans: the central role of the HIF hydroxylase pathway
    • Kaelin W.G., Ratcliffe P.J. Oxygen sensing by metazoans: the central role of the HIF hydroxylase pathway. Mol Cell 2008, 30:393-402.
    • (2008) Mol Cell , vol.30 , pp. 393-402
    • Kaelin, W.G.1    Ratcliffe, P.J.2
  • 20
    • 33747596652 scopus 로고    scopus 로고
    • Oxygen sensing by mitochondria at complex III: the paradox of increased reactive oxygen species during hypoxia
    • Guzy R.D., Schumacker P.T. Oxygen sensing by mitochondria at complex III: the paradox of increased reactive oxygen species during hypoxia. Exp Physiol 2006, 91:807-819.
    • (2006) Exp Physiol , vol.91 , pp. 807-819
    • Guzy, R.D.1    Schumacker, P.T.2
  • 21
    • 34548787792 scopus 로고    scopus 로고
    • Reactive oxygen species and cellular oxygen sensing
    • Cash T.P., Pan Y., Simon M.C. Reactive oxygen species and cellular oxygen sensing. Free Radic Biol Med 2007, 43:1219-1225.
    • (2007) Free Radic Biol Med , vol.43 , pp. 1219-1225
    • Cash, T.P.1    Pan, Y.2    Simon, M.C.3
  • 22
    • 70549092785 scopus 로고    scopus 로고
    • Mitochondrial reactive oxygen species regulate hypoxic signaling
    • Hamanaka R.B., Chandel N.S. Mitochondrial reactive oxygen species regulate hypoxic signaling. Curr Opin Cell Biol 2009, 21:894-899.
    • (2009) Curr Opin Cell Biol , vol.21 , pp. 894-899
    • Hamanaka, R.B.1    Chandel, N.S.2
  • 23
    • 24144493814 scopus 로고    scopus 로고
    • Mitochondrial complex III is required for hypoxia-induced ROS production and cellular oxygen sensing
    • Guzy R.D., Hoyos B., Robin E., Chen H., Liu L., Mansfield K.D., et al. Mitochondrial complex III is required for hypoxia-induced ROS production and cellular oxygen sensing. Cell Metab 2005, 1:401-408.
    • (2005) Cell Metab , vol.1 , pp. 401-408
    • Guzy, R.D.1    Hoyos, B.2    Robin, E.3    Chen, H.4    Liu, L.5    Mansfield, K.D.6
  • 24
    • 77649112162 scopus 로고    scopus 로고
    • Hypoxia triggers subcellular compartmental redox signaling in vascular smooth muscle cells
    • Waypa G.B., Marks J.D., Guzy R., Mungai P.T., Schriewer J., Dokic D., et al. Hypoxia triggers subcellular compartmental redox signaling in vascular smooth muscle cells. Circ Res 2010, 106:526-535.
    • (2010) Circ Res , vol.106 , pp. 526-535
    • Waypa, G.B.1    Marks, J.D.2    Guzy, R.3    Mungai, P.T.4    Schriewer, J.5    Dokic, D.6
  • 25
    • 76249095846 scopus 로고    scopus 로고
    • Hypoxia increases ROS signaling and cytosolic Ca(2+) in pulmonary artery smooth muscle cells of mouse lungs slices
    • Desireddi J.R., Farrow K.N., Marks J.D., Waypa G.B., Schumacker P.T. Hypoxia increases ROS signaling and cytosolic Ca(2+) in pulmonary artery smooth muscle cells of mouse lungs slices. Antioxid Redox Signal 2010, 12:595-602.
    • (2010) Antioxid Redox Signal , vol.12 , pp. 595-602
    • Desireddi, J.R.1    Farrow, K.N.2    Marks, J.D.3    Waypa, G.B.4    Schumacker, P.T.5
  • 26
    • 76249131229 scopus 로고    scopus 로고
    • Prolonged hypoxia increases ROS signaling and RhoA activation in pulmonary artery smooth muscle and endothelial cells
    • Chi A.Y., Waypa G.B., Mungai P.T., Schumacker P.T. Prolonged hypoxia increases ROS signaling and RhoA activation in pulmonary artery smooth muscle and endothelial cells. Antioxid Redox Signal 2010, 12:603-610.
    • (2010) Antioxid Redox Signal , vol.12 , pp. 603-610
    • Chi, A.Y.1    Waypa, G.B.2    Mungai, P.T.3    Schumacker, P.T.4
  • 27
    • 0030587928 scopus 로고    scopus 로고
    • Transcriptional up-regulation of intracellular adhesion molecule-1 in human endothelial cells by the antioxidant pyrrolidine dithiocarbamate involves the activation of activating protein-1
    • Muñoz C., Castellanos M.C., Alfranca A., Vara A., Esteban M.A., Redondo J.M., et al. Transcriptional up-regulation of intracellular adhesion molecule-1 in human endothelial cells by the antioxidant pyrrolidine dithiocarbamate involves the activation of activating protein-1. J Immunol 1996, 157:3587-3597.
    • (1996) J Immunol , vol.157 , pp. 3587-3597
    • Muñoz, C.1    Castellanos, M.C.2    Alfranca, A.3    Vara, A.4    Esteban, M.A.5    Redondo, J.M.6
  • 28
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels
    • Shevchenko A., Wilm M., Vorm O., Mann M. Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels. Anal Chem 1996, 68:850-858.
    • (1996) Anal Chem , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 29
    • 84874432046 scopus 로고    scopus 로고
    • A "fluorescence switch" technique increases the sensitivity of proteomic detection and identification of S-nitrosylated proteins
    • Tello D., Tarín C., Ahicart P., Bretón-Romero R., Lamas S., Martínez-Ruiz A. A "fluorescence switch" technique increases the sensitivity of proteomic detection and identification of S-nitrosylated proteins. Proteomics 2009, 53:59-70.
    • (2009) Proteomics , vol.53 , pp. 59-70
    • Tello, D.1    Tarín, C.2    Ahicart, P.3    Bretón-Romero, R.4    Lamas, S.5    Martínez-Ruiz, A.6
  • 30
    • 0036745407 scopus 로고    scopus 로고
    • Detection of oxidant sensitive thiol proteins by fluorescence labeling and two-dimensional electrophoresis
    • Baty J.W., Hampton M.B., Winterbourn C.C. Detection of oxidant sensitive thiol proteins by fluorescence labeling and two-dimensional electrophoresis. Proteomics 2002, 2:1261-1266.
    • (2002) Proteomics , vol.2 , pp. 1261-1266
    • Baty, J.W.1    Hampton, M.B.2    Winterbourn, C.C.3
  • 32
    • 26944462004 scopus 로고    scopus 로고
    • Fluorescence thiol modification assay: oxidatively modified proteins in Bacillus subtilis
    • Hochgräfe F., Mostertz J., Albrecht D., Hecker M. Fluorescence thiol modification assay: oxidatively modified proteins in Bacillus subtilis. Mol Microbiol 2005, 58:409-425.
    • (2005) Mol Microbiol , vol.58 , pp. 409-425
    • Hochgräfe, F.1    Mostertz, J.2    Albrecht, D.3    Hecker, M.4
  • 33
    • 0001637870 scopus 로고
    • Permanent cell line expressing human factor VIII-related antigen established by hybridization
    • Edgell C.J., McDonald C.C., Graham J.B. Permanent cell line expressing human factor VIII-related antigen established by hybridization. Proc Natl Acad Sci U S A 1983, 80:3734-3737.
    • (1983) Proc Natl Acad Sci U S A , vol.80 , pp. 3734-3737
    • Edgell, C.J.1    McDonald, C.C.2    Graham, J.B.3
  • 34
    • 33846630894 scopus 로고    scopus 로고
    • Multiple factors affecting cellular redox status and energy metabolism modulate hypoxia-inducible factor prolyl hydroxylase activity in vivo and in vitro
    • Pan Y., Mansfield K.D., Bertozzi C.C., Rudenko V., Chan D.A., Giaccia A.J., et al. Multiple factors affecting cellular redox status and energy metabolism modulate hypoxia-inducible factor prolyl hydroxylase activity in vivo and in vitro. Mol Cell Biol 2007, 27:912-925.
    • (2007) Mol Cell Biol , vol.27 , pp. 912-925
    • Pan, Y.1    Mansfield, K.D.2    Bertozzi, C.C.3    Rudenko, V.4    Chan, D.A.5    Giaccia, A.J.6
  • 36
    • 2942532590 scopus 로고    scopus 로고
    • Mass spectrometric characterization of the oxidation of the fluorescent lipid peroxidation reporter molecule C11-BODIPY(581/591)
    • Drummen G.P., Gadella B.M., Post J.A., Brouwers J.F. Mass spectrometric characterization of the oxidation of the fluorescent lipid peroxidation reporter molecule C11-BODIPY(581/591). Free Radic Biol Med 2004, 36:1635-1644.
    • (2004) Free Radic Biol Med , vol.36 , pp. 1635-1644
    • Drummen, G.P.1    Gadella, B.M.2    Post, J.A.3    Brouwers, J.F.4
  • 38
    • 34447333364 scopus 로고    scopus 로고
    • Nitric oxide during ischemia attenuates oxidant stress and cell death during ischemia and reperfusion in cardiomyocytes
    • Iwase H., Robin E., Guzy R.D., Mungai P.T., Vanden Hoek T.L., Chandel N.S., et al. Nitric oxide during ischemia attenuates oxidant stress and cell death during ischemia and reperfusion in cardiomyocytes. Free Radic Biol Med 2007, 43:590-599.
    • (2007) Free Radic Biol Med , vol.43 , pp. 590-599
    • Iwase, H.1    Robin, E.2    Guzy, R.D.3    Mungai, P.T.4    Vanden Hoek, T.L.5    Chandel, N.S.6
  • 39
    • 34547097807 scopus 로고    scopus 로고
    • Oxidant stress during simulated ischemia primes cardiomyocytes for cell death during reperfusion
    • Robin E., Guzy R.D., Loor G., Iwase H., Waypa G.B., Marks J.D., et al. Oxidant stress during simulated ischemia primes cardiomyocytes for cell death during reperfusion. J Biol Chem 2007, 282:19133-19143.
    • (2007) J Biol Chem , vol.282 , pp. 19133-19143
    • Robin, E.1    Guzy, R.D.2    Loor, G.3    Iwase, H.4    Waypa, G.B.5    Marks, J.D.6
  • 40
    • 0029768918 scopus 로고    scopus 로고
    • Oxidation of sulfhydryl groups of ribonuclease inhibitor in epithelial cells is sufficient for its intracellular degradation
    • Blázquez M., Fominaya J.M., Hofsteenge J. Oxidation of sulfhydryl groups of ribonuclease inhibitor in epithelial cells is sufficient for its intracellular degradation. J Biol Chem 1996, 271:18638-18642.
    • (1996) J Biol Chem , vol.271 , pp. 18638-18642
    • Blázquez, M.1    Fominaya, J.M.2    Hofsteenge, J.3
  • 42
    • 84857044092 scopus 로고    scopus 로고
    • Post-translational modifications of Hsp90 and their contributions to chaperone regulation
    • Mollapour M., Neckers L. Post-translational modifications of Hsp90 and their contributions to chaperone regulation. Biochim Biophys Acta 2012, 1823:648-655.
    • (2012) Biochim Biophys Acta , vol.1823 , pp. 648-655
    • Mollapour, M.1    Neckers, L.2
  • 43
    • 0014961369 scopus 로고
    • Mechanism of the inactivation of guinea pig liver transglutaminase by tetrathionate
    • Chung S.I., Folk J.E. Mechanism of the inactivation of guinea pig liver transglutaminase by tetrathionate. J Biol Chem 1970, 245:681-689.
    • (1970) J Biol Chem , vol.245 , pp. 681-689
    • Chung, S.I.1    Folk, J.E.2
  • 44
    • 0014690548 scopus 로고
    • Mechanism of the inactivation of guinea pig liver transglutaminase by 5,5'-dithiobis-(2-nitrobenzoic acid)
    • Connellan J.M., Folk J.E. Mechanism of the inactivation of guinea pig liver transglutaminase by 5,5'-dithiobis-(2-nitrobenzoic acid). J Biol Chem 1969, 244:3173-3181.
    • (1969) J Biol Chem , vol.244 , pp. 3173-3181
    • Connellan, J.M.1    Folk, J.E.2
  • 45
    • 0035942305 scopus 로고    scopus 로고
    • Calcium regulates S-nitrosylation, denitrosylation, and activity of tissue transglutaminase
    • Lai T.S., Hausladen A., Slaughter T.F., Eu J.P., Stamler J.S., Greenberg C.S. Calcium regulates S-nitrosylation, denitrosylation, and activity of tissue transglutaminase. Biochemistry 2001, 40:4904-4910.
    • (2001) Biochemistry , vol.40 , pp. 4904-4910
    • Lai, T.S.1    Hausladen, A.2    Slaughter, T.F.3    Eu, J.P.4    Stamler, J.S.5    Greenberg, C.S.6
  • 46
    • 51649127246 scopus 로고    scopus 로고
    • Identification of chemical inhibitors to human tissue transglutaminase by screening existing drug libraries
    • Lai T.S., Liu Y., Tucker T., Daniel K.R., Sane D.C., Toone E., et al. Identification of chemical inhibitors to human tissue transglutaminase by screening existing drug libraries. Chem Biol 2008, 15:969-978.
    • (2008) Chem Biol , vol.15 , pp. 969-978
    • Lai, T.S.1    Liu, Y.2    Tucker, T.3    Daniel, K.R.4    Sane, D.C.5    Toone, E.6
  • 47
    • 1942423136 scopus 로고    scopus 로고
    • Protein S-glutathionylation in retinal pigment epithelium converts heat shock protein 70 to an active chaperone
    • Hoppe G., Chai Y.C., Crabb J.W., Sears J. Protein S-glutathionylation in retinal pigment epithelium converts heat shock protein 70 to an active chaperone. Exp Eye Res 2004, 78:1085-1092.
    • (2004) Exp Eye Res , vol.78 , pp. 1085-1092
    • Hoppe, G.1    Chai, Y.C.2    Crabb, J.W.3    Sears, J.4
  • 48
    • 0018449645 scopus 로고
    • A detailed investigation of the properties of lactate dehydrogenase in which the 'essential' cysteine-165 is modified by thioalkylation
    • Bloxham D.P., Sharma R.P., Wilton D.C. A detailed investigation of the properties of lactate dehydrogenase in which the 'essential' cysteine-165 is modified by thioalkylation. Biochem J 1979, 177:769-780.
    • (1979) Biochem J , vol.177 , pp. 769-780
    • Bloxham, D.P.1    Sharma, R.P.2    Wilton, D.C.3
  • 49
    • 0017595429 scopus 로고
    • Modification of pig heart lactate dehydrogenase with methyl methanethiosulphonate to produce an enzyme with altered catalytic activity
    • Bloxham D.P., Wilton D.C. Modification of pig heart lactate dehydrogenase with methyl methanethiosulphonate to produce an enzyme with altered catalytic activity. Biochem J 1977, 161:643-651.
    • (1977) Biochem J , vol.161 , pp. 643-651
    • Bloxham, D.P.1    Wilton, D.C.2
  • 50
    • 0037119415 scopus 로고    scopus 로고
    • Hsp90 regulates a von Hippel-Lindau-independent hypoxia-inducible factor-1 alpha-degradative pathway
    • Isaacs J.S., Jung Y.J., Mimnaugh E.G., Martinez A., Cuttitta F., Neckers L.M. Hsp90 regulates a von Hippel-Lindau-independent hypoxia-inducible factor-1 alpha-degradative pathway. J Biol Chem 2002, 277:29936-29944.
    • (2002) J Biol Chem , vol.277 , pp. 29936-29944
    • Isaacs, J.S.1    Jung, Y.J.2    Mimnaugh, E.G.3    Martinez, A.4    Cuttitta, F.5    Neckers, L.M.6
  • 51
    • 4444260675 scopus 로고    scopus 로고
    • Interaction of the PAS B domain with HSP90 accelerates hypoxia-inducible factor-1alpha stabilization
    • Katschinski D.M., Le L., Schindler S.G., Thomas T., Voss A.K., Wenger R.H. Interaction of the PAS B domain with HSP90 accelerates hypoxia-inducible factor-1alpha stabilization. Cell Physiol Biochem 2004, 14:351-360.
    • (2004) Cell Physiol Biochem , vol.14 , pp. 351-360
    • Katschinski, D.M.1    Le, L.2    Schindler, S.G.3    Thomas, T.4    Voss, A.K.5    Wenger, R.H.6
  • 52
    • 33846254999 scopus 로고    scopus 로고
    • RACK1 competes with HSP90 for binding to HIF-1alpha and is required for O(2)-independent and HSP90 inhibitor-induced degradation of HIF-1alpha
    • Liu Y.V., Baek J.H., Zhang H., Diez R., Cole R.N., Semenza G.L. RACK1 competes with HSP90 for binding to HIF-1alpha and is required for O(2)-independent and HSP90 inhibitor-induced degradation of HIF-1alpha. Mol Cell 2007, 25:207-217.
    • (2007) Mol Cell , vol.25 , pp. 207-217
    • Liu, Y.V.1    Baek, J.H.2    Zhang, H.3    Diez, R.4    Cole, R.N.5    Semenza, G.L.6
  • 53
    • 69249206520 scopus 로고    scopus 로고
    • Hypoxia inhibits maturation and trafficking of hERG K(+) channel protein: role of Hsp90 and ROS
    • Nanduri J., Bergson P., Wang N., Ficker E., Prabhakar N.R. Hypoxia inhibits maturation and trafficking of hERG K(+) channel protein: role of Hsp90 and ROS. Biochem Biophys Res Commun 2009, 388:212-216.
    • (2009) Biochem Biophys Res Commun , vol.388 , pp. 212-216
    • Nanduri, J.1    Bergson, P.2    Wang, N.3    Ficker, E.4    Prabhakar, N.R.5
  • 54
    • 77950473770 scopus 로고    scopus 로고
    • Hsp70 and CHIP selectively mediate ubiquitination and degradation of hypoxia-inducible factor (HIF)-1alpha but not HIF-2alpha
    • Luo W., Zhong J., Chang R., Hu H., Pandey A., Semenza G.L. Hsp70 and CHIP selectively mediate ubiquitination and degradation of hypoxia-inducible factor (HIF)-1alpha but not HIF-2alpha. J Biol Chem 2010, 285:3651-3663.
    • (2010) J Biol Chem , vol.285 , pp. 3651-3663
    • Luo, W.1    Zhong, J.2    Chang, R.3    Hu, H.4    Pandey, A.5    Semenza, G.L.6
  • 55
    • 0031714410 scopus 로고    scopus 로고
    • Hypoxia-specific upregulation of calpain activity and gene expression in pulmonary artery endothelial cells
    • Zhang J., Patel J.M., Block E.R. Hypoxia-specific upregulation of calpain activity and gene expression in pulmonary artery endothelial cells. Am J Physiol 1998, 275:L461-L468.
    • (1998) Am J Physiol , vol.275
    • Zhang, J.1    Patel, J.M.2    Block, E.R.3
  • 56
    • 33745398366 scopus 로고    scopus 로고
    • Calpain mediates a von Hippel-Lindau protein-independent destruction of hypoxia-inducible factor-1alpha
    • Zhou J., Kohl R., Herr B., Frank R., Brüne B. Calpain mediates a von Hippel-Lindau protein-independent destruction of hypoxia-inducible factor-1alpha. Mol Biol Cell 2006, 17:1549-1558.
    • (2006) Mol Biol Cell , vol.17 , pp. 1549-1558
    • Zhou, J.1    Kohl, R.2    Herr, B.3    Frank, R.4    Brüne, B.5
  • 57
    • 10044276783 scopus 로고    scopus 로고
    • Regulation of mTOR function in response to hypoxia by REDD1 and the TSC1/TSC2 tumor suppressor complex
    • Brugarolas J., Lei K., Hurley R.L., Manning B.D., Reiling J.H., Hafen E., et al. Regulation of mTOR function in response to hypoxia by REDD1 and the TSC1/TSC2 tumor suppressor complex. Genes Dev 2004, 18:2893-2904.
    • (2004) Genes Dev , vol.18 , pp. 2893-2904
    • Brugarolas, J.1    Lei, K.2    Hurley, R.L.3    Manning, B.D.4    Reiling, J.H.5    Hafen, E.6
  • 58
    • 38349056675 scopus 로고    scopus 로고
    • Hypoxia regulates TSC1/2-mTOR signaling and tumor suppression through REDD1-mediated 14-3-3 shuttling
    • DeYoung M.P., Horak P., Sofer A., Sgroi D., Ellisen L.W. Hypoxia regulates TSC1/2-mTOR signaling and tumor suppression through REDD1-mediated 14-3-3 shuttling. Genes Dev 2008, 22:239-251.
    • (2008) Genes Dev , vol.22 , pp. 239-251
    • DeYoung, M.P.1    Horak, P.2    Sofer, A.3    Sgroi, D.4    Ellisen, L.W.5
  • 60
    • 66349108700 scopus 로고    scopus 로고
    • Reactive oxygen species regulate a slingshot-cofilin activation pathway
    • Kim J.S., Huang T.Y., Bokoch G.M. Reactive oxygen species regulate a slingshot-cofilin activation pathway. Mol Biol Cell 2009, 20:2650-2660.
    • (2009) Mol Biol Cell , vol.20 , pp. 2650-2660
    • Kim, J.S.1    Huang, T.Y.2    Bokoch, G.M.3
  • 61
    • 0029101515 scopus 로고
    • Hypoxic regulation of lactate dehydrogenase A. Interaction between hypoxia-inducible factor 1 and cAMP response elements
    • Firth J.D., Ebert B.L., Ratcliffe P.J. Hypoxic regulation of lactate dehydrogenase A. Interaction between hypoxia-inducible factor 1 and cAMP response elements. J Biol Chem 1995, 270:21021-21027.
    • (1995) J Biol Chem , vol.270 , pp. 21021-21027
    • Firth, J.D.1    Ebert, B.L.2    Ratcliffe, P.J.3
  • 62
    • 0030460724 scopus 로고    scopus 로고
    • Hypoxia response elements in the aldolase A, enolase 1, and lactate dehydrogenase A gene promoters contain essential binding sites for hypoxia-inducible factor 1
    • Semenza G.L., Jiang B.H., Leung S.W., Passantino R., Concordet J.-P., Maire P., et al. Hypoxia response elements in the aldolase A, enolase 1, and lactate dehydrogenase A gene promoters contain essential binding sites for hypoxia-inducible factor 1. J Biol Chem 1996, 271:32529-32537.
    • (1996) J Biol Chem , vol.271 , pp. 32529-32537
    • Semenza, G.L.1    Jiang, B.H.2    Leung, S.W.3    Passantino, R.4    Concordet, J.-P.5    Maire, P.6
  • 63
    • 0000929743 scopus 로고
    • Lactic dehydrogenases: functions of the two types. Rates of synthesis of the two major forms can be correlated with metabolic differentiation
    • Dawson D.M., Goodfriend T.L., Kaplan N.O. Lactic dehydrogenases: functions of the two types. Rates of synthesis of the two major forms can be correlated with metabolic differentiation. Science 1964, 143:929-933.
    • (1964) Science , vol.143 , pp. 929-933
    • Dawson, D.M.1    Goodfriend, T.L.2    Kaplan, N.O.3
  • 64
    • 0035342452 scopus 로고    scopus 로고
    • Structural basis for altered activity of M- and H-isozyme forms of human lactate dehydrogenase
    • Read J.A., Winter V.J., Eszes C.M., Sessions R.B., Brady R.L. Structural basis for altered activity of M- and H-isozyme forms of human lactate dehydrogenase. Proteins 2001, 43:175-185.
    • (2001) Proteins , vol.43 , pp. 175-185
    • Read, J.A.1    Winter, V.J.2    Eszes, C.M.3    Sessions, R.B.4    Brady, R.L.5
  • 65
    • 0000531487 scopus 로고
    • Approaches to the study of enzyme mechanisms lactate dehydrogenase
    • Holbrook J.J., Gutfreund H. Approaches to the study of enzyme mechanisms lactate dehydrogenase. FEBS Lett 1973, 31:157-169.
    • (1973) FEBS Lett , vol.31 , pp. 157-169
    • Holbrook, J.J.1    Gutfreund, H.2


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