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Volumn 86, Issue 8, 2010, Pages 657-668

Oxidative stress induces mainly human centrin 2 polymerisation

Author keywords

bityrosine; human centrin 2; oxidative stress; protein oxidation; radiolysis; Xeroderma pigmentosum C

Indexed keywords

AZIDE; CENTRIN; DIMER; HYDROXYL RADICAL; MONOMER; OXYGEN; PROTEIN HSCEN 2; TETRAMER; TYROSINE; UNCLASSIFIED DRUG; XERODERMA PIGMENTOSUM GROUP C PROTEIN;

EID: 77955140230     PISSN: 09553002     EISSN: 13623095     Source Type: Journal    
DOI: 10.3109/09553001003734584     Document Type: Article
Times cited : (13)

References (55)
  • 2
    • 0035374836 scopus 로고    scopus 로고
    • Centrosome protein centrin 2/caltractin 1 is part of the Xeroderma pigmentosum group C complex that initiates global genome nucleotide excision repair
    • Araki M, Masutani C, Takemura M, Uchida A, Sugasawa K, Kondoh J, Ohkuma Y, Hanaoka F. 2001. Centrosome protein centrin 2/caltractin 1 is part of the Xeroderma pigmentosum group C complex that initiates global genome nucleotide excision repair. Journal of Biological Chemistry 276:18665-18672.
    • (2001) Journal of Biological Chemistry , vol.276 , pp. 18665-18672
    • Araki, M.1    Masutani, C.2    Takemura, M.3    Uchida, A.4    Sugasawa, K.5    Kondoh, J.6    Ohkuma, Y.7    Hanaoka, F.8
  • 4
    • 0034616963 scopus 로고    scopus 로고
    • Stable binding of human XPC complex to irradiated DNA confers strong discrimination for damaged sites
    • Batty D, Rapic-Otrin V, Levine AS, Wood RD. 2000. Stable binding of human XPC complex to irradiated DNA confers strong discrimination for damaged sites. Journal of Molecular Biology 300:275-290.
    • (2000) Journal of Molecular Biology , vol.300 , pp. 275-290
    • Batty, D.1    Rapic-Otrin, V.2    Levine, A.S.3    Wood, R.D.4
  • 6
    • 0030971178 scopus 로고    scopus 로고
    • Pulse radiolysis studies of intramolecular electron transfer in model peptides and proteins. 7. Trp-4TyrOradical transformation in hen egg-white lysozyme. Effects of pH, temperature, Trp62 oxidation and inhibitor binding
    • Bobrowski K, Holcman J, Poznanski J,Wierzchowski KL. 1997. Pulse radiolysis studies of intramolecular electron transfer in model peptides and proteins. 7. Trp-4TyrOradical transformation in hen egg-white lysozyme. Effects of pH, temperature, Trp62 oxidation and inhibitor binding. Biophysical Chemistry 63:153-166.
    • (1997) Biophysical Chemistry , vol.63 , pp. 153-166
    • Bobrowski, K.1    Holcman, J.2    Poznanski, J.3    Wierzchowski, K.L.4
  • 7
    • 27744541402 scopus 로고    scopus 로고
    • Centrosome amplification and multinuclear phenotypes are induced by hydrogen peroxide
    • Chae S, Yun C, Um H, Lee JH, Cho H. 2005. Centrosome amplification and multinuclear phenotypes are induced by hydrogen peroxide. Experimental and Molecular Medicine 37:482-487.
    • (2005) Experimental and Molecular Medicine , vol.37 , pp. 482-487
    • Chae, S.1    Yun, C.2    Um, H.3    Lee, J.H.4    Cho, H.5
  • 10
    • 0023655369 scopus 로고
    • Protein damage and degradation by oxygen radicals. I. General aspects
    • Davies KJ. 1987. Protein damage and degradation by oxygen radicals. I. General aspects. Journal of Biological Chemistry 262:9895-9901.
    • (1987) Journal of Biological Chemistry , vol.262 , pp. 9895-9901
    • Davies, K.J.1
  • 11
    • 0033429334 scopus 로고    scopus 로고
    • Stable markers of oxidant damage to proteins and their application in the study of human disease
    • Davies MJ, Fu S, Wang H, Dean RT. 1999. Stable markers of oxidant damage to proteins and their application in the study of human disease. Free Radical Biology and Medicine 27:1151-1163.
    • (1999) Free Radical Biology and Medicine , vol.27 , pp. 1151-1163
    • Davies, M.J.1    Fu, S.2    Wang, H.3    Dean, R.T.4
  • 12
    • 33845967456 scopus 로고    scopus 로고
    • Current analytical methods for the detection of dityrosine; A biomarker of oxidative stress, in biological samples
    • DiMarco T, Giulivi C. 2007. Current analytical methods for the detection of dityrosine; a biomarker of oxidative stress, in biological samples. Mass Spectrometry Reviews 26:108-120.
    • (2007) Mass Spectrometry Reviews , vol.26 , pp. 108-120
    • Dimarco, T.1    Giulivi, C.2
  • 13
    • 0036928538 scopus 로고    scopus 로고
    • DNA degradation and protein peroxidation in cells exposed to hydroxyl free radicals
    • Du J, Gebicki JM. 2002. DNA degradation and protein peroxidation in cells exposed to hydroxyl free radicals. Redox Report 7:329-331.
    • (2002) Redox Report , vol.7 , pp. 329-331
    • Du, J.1    Gebicki, J.M.2
  • 14
    • 0001873721 scopus 로고    scopus 로고
    • Nitric oxide, altered DNA and mammalian disease
    • Aruoma O, Halliwell B, editors St Lucia: OICA International (London: Academic Press
    • Felley-Bosco E, Buzard GS, Billiar TR, Keefer LK. 1998. Nitric oxide, altered DNA and mammalian disease. In: Aruoma O, Halliwell B, editors. Molecular biology of free radicals in human diseases. St Lucia: OICA International (London: Academic Press). pp 287-366.
    • (1998) Molecular Biology of Free Radicals in Human Diseases , pp. 287-366
    • Felley-Bosco, E.1    Buzard, G.S.2    Billiar, T.R.3    Keefer, L.K.4
  • 15
    • 0009634188 scopus 로고    scopus 로고
    • Molecular aspect of free radical damage to proteins
    • Aruoma O, Halliwell B, editors St Lucia: OICA International (London: Academic Press
    • Fu S, Davies MJ, Dean RT. 1998a. Molecular aspect of free radical damage to proteins. In: Aruoma O, Halliwell B, editors. Molecular biology of free radicals in human diseases. St Lucia: OICA International (London: Academic Press). pp 29-56.
    • (1998) Molecular Biology of Free Radicals in Human Diseases , pp. 29-56
    • Fu, S.1    Davies, M.J.2    Dean, R.T.3
  • 16
    • 0032143406 scopus 로고    scopus 로고
    • Evidence for roles of radicals in protein oxidation in advanced human atherosclerotic plaque
    • Fu S, Davies MJ, Stocker R, Dean RT. 1998b. Evidence for roles of radicals in protein oxidation in advanced human atherosclerotic plaque. Biochemical Journal 333(Pt 3):519-525.
    • (1998) Biochemical Journal , vol.333 , Issue.PART 3 , pp. 519-525
    • Fu, S.1    Davies, M.J.2    Stocker, R.3    Dean, R.T.4
  • 18
    • 0028283298 scopus 로고
    • Dityrosine: A marker for oxidatively modified proteins and selective proteolysis
    • Giulivi C, Davies KJ. 1994. Dityrosine: A marker for oxidatively modified proteins and selective proteolysis. Methods in Enzymology 233:363-371.
    • (1994) Methods in Enzymology , vol.233 , pp. 363-371
    • Giulivi, C.1    Davies, K.J.2
  • 19
    • 0002152698 scopus 로고    scopus 로고
    • Molecular aspects of free radical damage in inflammatory autoimmune pathology
    • Aruoma O, Halliwell B, editors St Lucia: OICA International. (London: Academic Press
    • Griffiths HR, Lunec J. 1998. Molecular aspects of free radical damage in inflammatory autoimmune pathology. In: Aruoma O, Halliwell B, editors. Molecular biology of free radicals in human diseases. St Lucia: OICA International. (London: Academic Press). pp 327-366.
    • (1998) Molecular Biology of Free Radicals in Human Diseases , pp. 327-366
    • Griffiths, H.R.1    Lunec, J.2
  • 20
    • 33745013111 scopus 로고    scopus 로고
    • Oxidative stress and neurodegeneration: Where are we now?
    • Halliwell B. 2006. Oxidative stress and neurodegeneration: Where are we now? Journal of Neurochemistry 97:1634-1658
    • (2006) Journal of Neurochemistry , vol.97 , pp. 1634-1658
    • Halliwell, B.1
  • 21
    • 0035795180 scopus 로고    scopus 로고
    • Generation and propagation of radical reactions on proteins
    • Hawkins CL, Davies MJ. 2001. Generation and propagation of radical reactions on proteins. Biochimica Biophysica Acta 1504:196-219.
    • (2001) Biochimica Biophysica Acta , vol.1504 , pp. 196-219
    • Hawkins, C.L.1    Davies, M.J.2
  • 22
    • 1842685103 scopus 로고    scopus 로고
    • Markers of protein oxidation: Different oxidants give rise to variable yields of bound and released carbonyl products
    • Headlam HA, Davies MJ. 2004. Markers of protein oxidation: Different oxidants give rise to variable yields of bound and released carbonyl products. Free Radical Biology and Medicine 36:1175-1184.
    • (2004) Free Radical Biology and Medicine , vol.36 , pp. 1175-1184
    • Headlam, H.A.1    Davies, M.J.2
  • 25
    • 0029808085 scopus 로고    scopus 로고
    • Human phagocytes employ the myeloperoxidase-hydrogen peroxide system to synthesize dityrosine, trityrosine, pulcherosine, and isodityrosine by a tyrosyl radical-dependent pathway
    • Jacob JS, Cistola DP, Hsu FF, Muzaffar S, Mueller DM, Hazen SL, Heinecke JW. 1996. Human phagocytes employ the myeloperoxidase-hydrogen peroxide system to synthesize dityrosine, trityrosine, pulcherosine, and isodityrosine by a tyrosyl radical-dependent pathway. Journal of Biological Chemistry 271:19950-19956.
    • (1996) Journal of Biological Chemistry , vol.271 , pp. 19950-19956
    • Jacob, J.S.1    Cistola, D.P.2    Hsu, F.F.3    Muzaffar, S.4    Mueller, D.M.5    Hazen, S.L.6    Heinecke, J.W.7
  • 27
    • 0014064318 scopus 로고
    • Ultraviolet irradiation effects in poly-L-tyrosine and model compounds. Identification of bityrosine as a photoproduct
    • Lehrer SS, Fasman GD. 1967. Ultraviolet irradiation effects in poly-L-tyrosine and model compounds. Identification of bityrosine as a photoproduct. Biochemistry 6:757-767.
    • (1967) Biochemistry , vol.6 , pp. 757-767
    • Lehrer, S.S.1    Fasman, G.D.2
  • 28
    • 0017878139 scopus 로고
    • Anomalous migration of leghaemoglobin on sodium dodecyl sulphate/polyacrylamide-gel electrophoresis
    • Lehtovaara P. 1978. Anomalous migration of leghaemoglobin on sodium dodecyl sulphate/polyacrylamide-gel electrophoresis. Biochemical Journal 169:251-253.
    • (1978) Biochemical Journal , vol.169 , pp. 251-253
    • Lehtovaara, P.1
  • 29
    • 47549106882 scopus 로고    scopus 로고
    • Applications of isothermal titration calorimetry in protein science
    • Liang Y. 2008. Applications of isothermal titration calorimetry in protein science. Acta Biochimica and Biophysica Sinica (Shanghai) 40:565-576.
    • (2008) Acta Biochimica and Biophysica Sinica (Shanghai) , vol.40 , pp. 565-576
    • Liang, Y.1
  • 31
    • 0035827607 scopus 로고    scopus 로고
    • Phosphorylation of centrin during the cell cycle and its role in centriole separation preceding centrosome duplication
    • Lutz W, Lingle WL, McCormick D, Greenwood TM, Salisbury JL. 2001. Phosphorylation of centrin during the cell cycle and its role in centriole separation preceding centrosome duplication. Journal of Biological Chemistry 276:20774-20780.
    • (2001) Journal of Biological Chemistry , vol.276 , pp. 20774-20780
    • Lutz, W.1    Lingle, W.L.2    McCormick, D.3    Greenwood, T.M.4    Salisbury, J.L.5
  • 32
    • 0023149376 scopus 로고
    • Dityrosine formation in calmodulin
    • Malencik DA, Anderson SR. 1987. Dityrosine formation in calmodulin. Biochemistry 26:695-704.
    • (1987) Biochemistry , vol.26 , pp. 695-704
    • Malencik, D.A.1    Anderson, S.R.2
  • 33
    • 0029919963 scopus 로고    scopus 로고
    • Dityrosine formation in calmodulin: Cross-linking and polymerization catalyzed by Arthromyces peroxidase
    • Malencik DA, Anderson SR. 1996. Dityrosine formation in calmodulin: Cross-linking and polymerization catalyzed by Arthromyces peroxidase. Biochemistry 35:4375-4386.
    • (1996) Biochemistry , vol.35 , pp. 4375-4386
    • Malencik, D.A.1    Anderson, S.R.2
  • 35
    • 35448957157 scopus 로고    scopus 로고
    • Circular dichroism and its application to the study of biomolecules
    • Martin SR, Schilstra MJ. 2008. Circular dichroism and its application to the study of biomolecules. Methods in Cellular Biology 84:263-293.
    • (2008) Methods in Cellular Biology , vol.84 , pp. 263-293
    • Martin, S.R.1    Schilstra, M.J.2
  • 36
    • 38849204912 scopus 로고    scopus 로고
    • The carboxy-terminal domain of Xeroderma pigmentosum complementation group C protein, involved in TFIIH and centrin binding, is highly disordered
    • Miron S, Duchambon P, Blouquit Y, Durand D, Craescu CT. 2008. The carboxy-terminal domain of Xeroderma pigmentosum complementation group C protein, involved in TFIIH and centrin binding, is highly disordered. Biochemistry 47:1403-1413.
    • (2008) Biochemistry , vol.47 , pp. 1403-1413
    • Miron, S.1    Duchambon, P.2    Blouquit, Y.3    Durand, D.4    Craescu, C.T.5
  • 38
    • 33847262424 scopus 로고    scopus 로고
    • Effects of gamma radiation on b-lactoglobulin: Oligomerization and aggregation
    • Oliveira CLP, de la Hoz L, Silva JC, Torriani IL, Netto FM. 2006. Effects of gamma radiation on b-lactoglobulin: Oligomerization and aggregation. Biopolymers 85:284-294.
    • (2006) Biopolymers , vol.85 , pp. 284-294
    • Clp, O.1    De La Hoz, L.2    Silva, J.C.3    Torriani, I.L.4    Netto, F.M.5
  • 39
    • 0030447537 scopus 로고    scopus 로고
    • Most of centrin in animal cells is not centrosomeassociated and centrosomal centrin is confined to the distal lumen of centrioles
    • Paoletti A, Moudjou M, Paintrand M, Salisbury JL, Bornens M. 1996. Most of centrin in animal cells is not centrosomeassociated and centrosomal centrin is confined to the distal lumen of centrioles. Journal of Cell Science 109:3089-3102.
    • (1996) Journal of Cell Science , vol.109 , pp. 3089-3102
    • Paoletti, A.1    Moudjou, M.2    Paintrand, M.3    Salisbury, J.L.4    Bornens, M.5
  • 43
    • 0346100521 scopus 로고    scopus 로고
    • Recent advances in the analysis of oxidized proteins
    • Requena JR, Levine RL, Stadtman ER. 2003. Recent advances in the analysis of oxidized proteins. Amino Acids 25:221-226.
    • (2003) Amino Acids , vol.25 , pp. 221-226
    • Requena, J.R.1    Levine, R.L.2    Stadtman, E.R.3
  • 44
    • 34848873761 scopus 로고    scopus 로고
    • A mechanistic view on the evolutionary origin for centrin-based control of centriole duplication
    • Salisbury JL. 2007. A mechanistic view on the evolutionary origin for centrin-based control of centriole duplication. Journal of Cellular Physiology 213:420-428.
    • (2007) Journal of Cellular Physiology , vol.213 , pp. 420-428
    • Salisbury, J.L.1
  • 45
    • 0034653382 scopus 로고    scopus 로고
    • Radiationinduced centrosome overduplication and multiple mitotic spindles in human tumor cells
    • Sato N, Mizumoto K, Nakamura M, Tanaka M. 2000. Radiationinduced centrosome overduplication and multiple mitotic spindles in human tumor cells. Experimental Cellular Research 255:321-326.
    • (2000) Experimental Cellular Research , vol.255 , pp. 321-326
    • Sato, N.1    Mizumoto, K.2    Nakamura, M.3    Tanaka, M.4
  • 46
    • 33749522859 scopus 로고    scopus 로고
    • Mass spectrometry of protein modifications by reactive oxygen and nitrogen species
    • Schoneich C, Sharov VS. 2006. Mass spectrometry of protein modifications by reactive oxygen and nitrogen species. Free Radical Biology and Medicine 41:1507-1520.
    • (2006) Free Radical Biology and Medicine , vol.41 , pp. 1507-1520
    • Schoneich, C.1    Sharov, V.S.2
  • 50
    • 0344549149 scopus 로고    scopus 로고
    • Microscale purification of proteins exhibiting anomalous electrophoretic migration: Application to the analysis of GAP-43 phosphorylation
    • Tejero-Diez P, Rodriguez-Sanchez P, Diez-Guerra FJ. 1999. Microscale purification of proteins exhibiting anomalous electrophoretic migration: Application to the analysis of GAP-43 phosphorylation. Analytical Biochemistry 274:278-282.
    • (1999) Analytical Biochemistry , vol.274 , pp. 278-282
    • Tejero-Diez, P.1    Rodriguez-Sanchez, P.2    Diez-Guerra, F.J.3
  • 52
  • 53
    • 0037310209 scopus 로고    scopus 로고
    • Applications of calorimetric methods to drug discovery and the study of protein interactions
    • Weber PC, Salemme FR. 2003. Applications of calorimetric methods to drug discovery and the study of protein interactions. Current Opinion in Structural Biology 13:11-121.
    • (2003) Current Opinion in Structural Biology , vol.13 , pp. 11-121
    • Weber, P.C.1    Salemme, F.R.2
  • 54
    • 33645233083 scopus 로고    scopus 로고
    • Flexibility and plasticity of human centrin 2 binding to the Xeroderma pigmentosum group C protein (XPC) from Nuclear Excision Repair
    • Yang A, Miron S, Mouawad L, Duchambon P, Blouquit Y, Craescu CT. 2006. Flexibility and plasticity of human centrin 2 binding to the Xeroderma pigmentosum group C protein (XPC) from Nuclear Excision Repair. Biochemistry 45:3653-3663.
    • (2006) Biochemistry , vol.45 , pp. 3653-3663
    • Craescu, C.T.1    Yang, A.2    Miron, S.3    Mouawad, L.4    Duchambon, P.5    Blouquit, Y.6
  • 55
    • 67649654451 scopus 로고    scopus 로고
    • Centrosome function in cancer: Guilty or innocent?
    • Zyss D, Gergely F. 2009. Centrosome function in cancer: Guilty or innocent? Trends in Cellular Biology 19:334-346.
    • (2009) Trends in Cellular Biology , vol.19 , pp. 334-346
    • Zyss, D.1    Gergely, F.2


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