메뉴 건너뛰기




Volumn 41, Issue 1, 2018, Pages 29-38

Role of protein carbonylation in diabetes

Author keywords

Methylglyoxal; Post translational modification; Protein carbonylation; Reactive oxygen species; Redox signaling

Indexed keywords

ACROLEIN; ANTIOXIDANT; CARNITINE; GLUTATHIONE PEROXIDASE 1; GLUTATHIONE TRANSFERASE A4; MALONALDEHYDE; PEROXIREDOXIN; PEROXIREDOXIN 1; PEROXIREDOXIN 2; PEROXIREDOXIN 4; PEROXIREDOXIN 6; REACTIVE OXYGEN METABOLITE; SUPEROXIDE DISMUTASE; UBIQUITINATED PROTEIN; ANTIDIABETIC AGENT;

EID: 85033448807     PISSN: 01418955     EISSN: 15732665     Source Type: Journal    
DOI: 10.1007/s10545-017-0104-9     Document Type: Review
Times cited : (66)

References (84)
  • 1
    • 84905575037 scopus 로고    scopus 로고
    • Circulating peroxiredoxin 4 and type 2 diabetes risk: the prevention of renal and vascular endstage disease (PREVEND) study
    • COI: 1:CAS:528:DC%2BC2cXpsFelsLs%3D, PID: 24893865
    • Abbasi A, Corpeleijn E, Gansevoort RT et al (2014) Circulating peroxiredoxin 4 and type 2 diabetes risk: the prevention of renal and vascular endstage disease (PREVEND) study. Diabetologia 57:1842–1849
    • (2014) Diabetologia , vol.57 , pp. 1842-1849
    • Abbasi, A.1    Corpeleijn, E.2    Gansevoort, R.T.3
  • 2
    • 0035434379 scopus 로고    scopus 로고
    • Reactive carbonyl formation by oxidative and non-oxidative pathways
    • COI: 1:CAS:528:DC%2BD3MXnsFChsLg%3D, PID: 11487471
    • Adams S, Green P, Claxton R et al (2001) Reactive carbonyl formation by oxidative and non-oxidative pathways. Front Biosci 6:A17–A24
    • (2001) Front Biosci , vol.6 , pp. A17-A24
    • Adams, S.1    Green, P.2    Claxton, R.3
  • 3
    • 79955757695 scopus 로고    scopus 로고
    • Oxidative stress-mediated regulation of proteasome complexes
    • PID: 21543789
    • Aiken CT, Kaake RM, Wang X, Huang L (2011) Oxidative stress-mediated regulation of proteasome complexes. Mol Cell Proteomics 10:R110 006924
    • (2011) Mol Cell Proteomics , vol.10 , pp. 110
    • Aiken, C.T.1    Kaake, R.M.2    Wang, X.3    Huang, L.4
  • 4
    • 84908542711 scopus 로고    scopus 로고
    • Proteasome inhibition in skeletal muscle cells unmasks metabolic derangements in type 2 diabetes
    • Al-Khalili L, de Castro Barbosa T, Ostling J et al (2014) Proteasome inhibition in skeletal muscle cells unmasks metabolic derangements in type 2 diabetes. Am J Physiol Cell Physiol 307: C774-C787
    • (2014) Am J Physiol Cell Physiol , vol.307 , pp. C774-C787
    • Al-Khalili, L.1    de Castro Barbosa, T.2    Ostling, J.3
  • 5
    • 85014891926 scopus 로고    scopus 로고
    • Carnosine attenuates the development of both type 2 diabetes and diabetic nephropathy in BTBR ob/ob mice
    • PID: 28281693
    • Albrecht T, Schilperoort M, Zhang S et al (2017) Carnosine attenuates the development of both type 2 diabetes and diabetic nephropathy in BTBR ob/ob mice. Sci Rep 7:44492
    • (2017) Sci Rep , vol.7 , pp. 44492
    • Albrecht, T.1    Schilperoort, M.2    Zhang, S.3
  • 6
    • 84962463376 scopus 로고    scopus 로고
    • 6. Obesity management for the treatment of type 2 diabetes
    • American Diabetes Association
    • American Diabetes Association (2016) 6. Obesity management for the treatment of type 2 diabetes. Diabetes Care 39(Suppl 1):S47–S51
    • (2016) Diabetes Care , vol.39 , pp. S47-S51
  • 7
    • 84908868650 scopus 로고    scopus 로고
    • Carbonylated plasma proteins as potential biomarkers of obesity induced type 2 diabetes mellitus
    • COI: 1:CAS:528:DC%2BC2cXhtFeisbvM, PID: 25010493
    • Bollineni RC, Fedorova M, Bluher M, Hoffmann R (2014) Carbonylated plasma proteins as potential biomarkers of obesity induced type 2 diabetes mellitus. J Proteome Res 13:5081–5093
    • (2014) J Proteome Res , vol.13 , pp. 5081-5093
    • Bollineni, R.C.1    Fedorova, M.2    Bluher, M.3    Hoffmann, R.4
  • 8
    • 38949135755 scopus 로고    scopus 로고
    • Molecular mechanisms for myocardial mitochondrial dysfunction in the metabolic syndrome
    • COI: 1:CAS:528:DC%2BD1cXksVCqsQ%3D%3D
    • Bugger H, Abel ED (2008) Molecular mechanisms for myocardial mitochondrial dysfunction in the metabolic syndrome. Clin Sci (Lond) 114:195–210
    • (2008) Clin Sci (Lond) , vol.114 , pp. 195-210
    • Bugger, H.1    Abel, E.D.2
  • 9
    • 84896092380 scopus 로고    scopus 로고
    • Molecular mechanisms of diabetic cardiomyopathy
    • COI: 1:CAS:528:DC%2BC2cXhs1Gltrw%3D, PID: 24477973
    • Bugger H, Abel ED (2014) Molecular mechanisms of diabetic cardiomyopathy. Diabetologia 57:660–671
    • (2014) Diabetologia , vol.57 , pp. 660-671
    • Bugger, H.1    Abel, E.D.2
  • 10
    • 55849133043 scopus 로고    scopus 로고
    • Diabetes-related microvascular and macrovascular diseases in the physical therapy setting
    • PID: 18801863
    • Cade WT (2008) Diabetes-related microvascular and macrovascular diseases in the physical therapy setting. Phys Ther 88:1322–1335
    • (2008) Phys Ther , vol.88 , pp. 1322-1335
    • Cade, W.T.1
  • 11
    • 84880141276 scopus 로고    scopus 로고
    • Kinetics of reversible reductive carbonylation of heme in human cystathionine beta-synthase
    • COI: 1:CAS:528:DC%2BC3sXpvVGhtb0%3D, PID: 23790103
    • Carballal S, Cuevasanta E, Marmisolle I et al (2013) Kinetics of reversible reductive carbonylation of heme in human cystathionine beta-synthase. Biochemistry 52:4553–4562
    • (2013) Biochemistry , vol.52 , pp. 4553-4562
    • Carballal, S.1    Cuevasanta, E.2    Marmisolle, I.3
  • 12
    • 70349633646 scopus 로고    scopus 로고
    • TIMP3 is reduced in atherosclerotic plaques from subjects with type 2 diabetes and increased by SirT1
    • COI: 1:CAS:528:DC%2BD1MXht1yrsr%2FP, PID: 19581416
    • Cardellini M, Menghini R, Martelli E et al (2009) TIMP3 is reduced in atherosclerotic plaques from subjects with type 2 diabetes and increased by SirT1. Diabetes 58:2396–2401
    • (2009) Diabetes , vol.58 , pp. 2396-2401
    • Cardellini, M.1    Menghini, R.2    Martelli, E.3
  • 13
    • 83655167191 scopus 로고    scopus 로고
    • Overexpression of tissue inhibitor of metalloproteinase 3 in macrophages reduces atherosclerosis in low-density lipoprotein receptor knockout mice
    • COI: 1:CAS:528:DC%2BC3MXhs1Wksr%2FJ, PID: 22015660
    • Casagrande V, Menghini R, Menini S et al (2012) Overexpression of tissue inhibitor of metalloproteinase 3 in macrophages reduces atherosclerosis in low-density lipoprotein receptor knockout mice. Arterioscler Thromb Vasc Biol 32:74–81
    • (2012) Arterioscler Thromb Vasc Biol , vol.32 , pp. 74-81
    • Casagrande, V.1    Menghini, R.2    Menini, S.3
  • 14
    • 85006789333 scopus 로고    scopus 로고
    • 4-Hydroxynonenal (HNE) modified proteins in metabolic diseases
    • COI: 1:CAS:528:DC%2BC28XhvVOgsrbO, PID: 27815191
    • Castro JP, Jung T, Grune T, Siems W (2017) 4-Hydroxynonenal (HNE) modified proteins in metabolic diseases. Free Radic Biol Med 111:309–315
    • (2017) Free Radic Biol Med , vol.111 , pp. 309-315
    • Castro, J.P.1    Jung, T.2    Grune, T.3    Siems, W.4
  • 15
    • 39449134085 scopus 로고    scopus 로고
    • Protein carbonylation and decarboylation: a new twist to the complex response of vascular cells to oxidative stress
    • COI: 1:CAS:528:DC%2BD1cXlslant7g%3D, PID: 18276922
    • Cattaruzza M, Hecker M (2008) Protein carbonylation and decarboylation: a new twist to the complex response of vascular cells to oxidative stress. Circ Res 102:273–274
    • (2008) Circ Res , vol.102 , pp. 273-274
    • Cattaruzza, M.1    Hecker, M.2
  • 16
    • 66349086461 scopus 로고    scopus 로고
    • Diabetes and atherosclerosis: is there a role for hyperglycemia?
    • PID: 19029122
    • Chait A, Bornfeldt KE (2009) Diabetes and atherosclerosis: is there a role for hyperglycemia? J Lipid Res 50(Suppl):S335–S339
    • (2009) J Lipid Res , vol.50 , pp. S335-S339
    • Chait, A.1    Bornfeldt, K.E.2
  • 17
    • 84975047098 scopus 로고    scopus 로고
    • Microvasular and macrovascular complications in diabetes mellitus: distinct or continuum?
    • COI: 1:CAS:528:DC%2BC28XhsFWrtbrP, PID: 27366724
    • Chawla A, Chawla R, Jaggi S (2016) Microvasular and macrovascular complications in diabetes mellitus: distinct or continuum? Indian J Endocrinol Metab 20:546–551
    • (2016) Indian J Endocrinol Metab , vol.20 , pp. 546-551
    • Chawla, A.1    Chawla, R.2    Jaggi, S.3
  • 18
    • 84883257025 scopus 로고    scopus 로고
    • Advanced glycation end products and diabetic retinopathy
    • COI: 1:CAS:528:DC%2BC3sXht1GmurbJ, PID: 23745547
    • Chen M, Curtis TM, Stitt AW (2013) Advanced glycation end products and diabetic retinopathy. Curr Med Chem 20:3234–3240
    • (2013) Curr Med Chem , vol.20 , pp. 3234-3240
    • Chen, M.1    Curtis, T.M.2    Stitt, A.W.3
  • 19
    • 0042867413 scopus 로고    scopus 로고
    • Contribution of polyol pathway to diabetes-induced oxidative stress
    • COI: 1:CAS:528:DC%2BD3sXmslCqsL8%3D, PID: 12874437
    • Chung SS, Ho EC, Lam KS, Chung SK (2003) Contribution of polyol pathway to diabetes-induced oxidative stress. J Am Soc Nephrol 14:S233–S236
    • (2003) J Am Soc Nephrol , vol.14 , pp. S233-S236
    • Chung, S.S.1    Ho, E.C.2    Lam, K.S.3    Chung, S.K.4
  • 20
    • 77951842594 scopus 로고    scopus 로고
    • Downregulation of adipose glutathione S-transferase A4 leads to increased protein carbonylation, oxidative stress, and mitochondrial dysfunction
    • COI: 1:CAS:528:DC%2BC3cXmtFegsbw%3D, PID: 20150287
    • Curtis JM, Grimsrud PA, Wright WS et al (2010) Downregulation of adipose glutathione S-transferase A4 leads to increased protein carbonylation, oxidative stress, and mitochondrial dysfunction. Diabetes 59:1132–1142
    • (2010) Diabetes , vol.59 , pp. 1132-1142
    • Curtis, J.M.1    Grimsrud, P.A.2    Wright, W.S.3
  • 22
    • 80755168955 scopus 로고    scopus 로고
    • Nrf2 activators as attractive therapeutics for diabetic nephropathy
    • PID: 22025774
    • de Haan JB (2011) Nrf2 activators as attractive therapeutics for diabetic nephropathy. Diabetes 60:2683–2684
    • (2011) Diabetes , vol.60 , pp. 2683-2684
    • de Haan, J.B.1
  • 24
    • 84925485590 scopus 로고    scopus 로고
    • Increased oxidative stress in patients with 3-hydroxy-3-methylglutaric aciduria
    • COI: 1:CAS:528:DC%2BC2MXmtVGquw%3D%3D, PID: 25557019
    • Dos Santos Mello M, Ribas GS, Wayhs CA et al (2015) Increased oxidative stress in patients with 3-hydroxy-3-methylglutaric aciduria. Mol Cell Biochem 402:149–155
    • (2015) Mol Cell Biochem , vol.402 , pp. 149-155
    • Dos Santos Mello, M.1    Ribas, G.S.2    Wayhs, C.A.3
  • 25
    • 84930009758 scopus 로고    scopus 로고
    • Peroxiredoxin isoforms are associated with cardiovascular risk factors in type 2 diabetes mellitus
    • PID: 25742636
    • El Eter E, Al-Masri AA (2015) Peroxiredoxin isoforms are associated with cardiovascular risk factors in type 2 diabetes mellitus. Braz J Med Biol Res 48:465–469
    • (2015) Braz J Med Biol Res , vol.48 , pp. 465-469
    • El Eter, E.1    Al-Masri, A.A.2
  • 26
    • 84893775972 scopus 로고    scopus 로고
    • Protein carbonylation as a major hallmark of oxidative damage: update of analytical strategies
    • COI: 1:CAS:528:DC%2BC2cXitFWnsLc%3D, PID: 23832618
    • Fedorova M, Bollineni RC, Hoffmann R (2014) Protein carbonylation as a major hallmark of oxidative damage: update of analytical strategies. Mass Spectrom Rev 33:79–97
    • (2014) Mass Spectrom Rev , vol.33 , pp. 79-97
    • Fedorova, M.1    Bollineni, R.C.2    Hoffmann, R.3
  • 27
    • 84878512756 scopus 로고    scopus 로고
    • In vivo experimental evidence that the major metabolites accumulating in 3-hydroxy-3-methylglutaryl-CoA lyase deficiency induce oxidative stress in striatum of developing rats: a potential pathophysiological mechanism of striatal damage in this disorder
    • Fernandes CG, da Rosa MS, Seminotti B et al (2013) In vivo experimental evidence that the major metabolites accumulating in 3-hydroxy-3-methylglutaryl-CoA lyase deficiency induce oxidative stress in striatum of developing rats: a potential pathophysiological mechanism of striatal damage in this disorder. Mol Genet Metab 109: 144-153
    • (2013) Mol Genet Metab , vol.109 , pp. 144-153
    • Fernandes, C.G.1    da Rosa, M.S.2    Seminotti, B.3
  • 28
    • 65349100528 scopus 로고    scopus 로고
    • Redox signaling across cell membranes
    • COI: 1:CAS:528:DC%2BD1MXkvVGnsbg%3D, PID: 19061438
    • Fisher AB (2009) Redox signaling across cell membranes. Antioxid Redox Signal 11:1349–1356
    • (2009) Antioxid Redox Signal , vol.11 , pp. 1349-1356
    • Fisher, A.B.1
  • 29
    • 84882981103 scopus 로고    scopus 로고
    • Protein carbonylation, mitochondrial dysfunction, and insulin resistance
    • COI: 1:CAS:528:DC%2BC3sXms1KhtLw%3D, PID: 23493532
    • Frohnert BI, Bernlohr DA (2013) Protein carbonylation, mitochondrial dysfunction, and insulin resistance. Adv Nutr 4:157–163
    • (2013) Adv Nutr , vol.4 , pp. 157-163
    • Frohnert, B.I.1    Bernlohr, D.A.2
  • 30
    • 84935064641 scopus 로고    scopus 로고
    • Emerging role of post-translational modifications in chronic kidney disease and cardiovascular disease
    • COI: 1:CAS:528:DC%2BC2sXhs1KjtbnN, PID: 25862763
    • Gajjala PR, Fliser D, Speer T, Jankowski V, Jankowski J (2015) Emerging role of post-translational modifications in chronic kidney disease and cardiovascular disease. Nephrol Dial Transplant 30:1814–1824
    • (2015) Nephrol Dial Transplant , vol.30 , pp. 1814-1824
    • Gajjala, P.R.1    Fliser, D.2    Speer, T.3    Jankowski, V.4    Jankowski, J.5
  • 31
    • 78349297565 scopus 로고    scopus 로고
    • Oxidative stress and diabetic complications
    • COI: 1:CAS:528:DC%2BC3cXhtlGjsrrP, PID: 21030723
    • Giacco F, Brownlee M (2010) Oxidative stress and diabetic complications. Circ Res 107:1058–1070
    • (2010) Circ Res , vol.107 , pp. 1058-1070
    • Giacco, F.1    Brownlee, M.2
  • 32
    • 34247361278 scopus 로고    scopus 로고
    • Carbonylation of adipose proteins in obesity and insulin resistance: identification of adipocyte fatty acid-binding protein as a cellular target of 4-hydroxynonenal
    • COI: 1:CAS:528:DC%2BD2sXksVKgtbk%3D, PID: 17205980
    • Grimsrud PA, Picklo MJ Sr, Griffin TJ, Bernlohr DA (2007) Carbonylation of adipose proteins in obesity and insulin resistance: identification of adipocyte fatty acid-binding protein as a cellular target of 4-hydroxynonenal. Mol Cell Proteomics 6:624–637
    • (2007) Mol Cell Proteomics , vol.6 , pp. 624-637
    • Grimsrud, P.A.1    Picklo, M.J.2    Griffin, T.J.3    Bernlohr, D.A.4
  • 33
    • 52049088770 scopus 로고    scopus 로고
    • Oxidative stress and covalent modification of protein with bioactive aldehydes
    • COI: 1:CAS:528:DC%2BD1cXpt1arsr4%3D, PID: 18445586
    • Grimsrud PA, Xie H, Griffin TJ, Bernlohr DA (2008) Oxidative stress and covalent modification of protein with bioactive aldehydes. J Biol Chem 283:21837–21841
    • (2008) J Biol Chem , vol.283 , pp. 21837-21841
    • Grimsrud, P.A.1    Xie, H.2    Griffin, T.J.3    Bernlohr, D.A.4
  • 34
    • 0036824710 scopus 로고    scopus 로고
    • Antioxidant vitamins and their influence in diabetes mellitus
    • PID: 12643171
    • Hasanain B, Mooradian AD (2002) Antioxidant vitamins and their influence in diabetes mellitus. Curr Diab Rep 2:448–456
    • (2002) Curr Diab Rep , vol.2 , pp. 448-456
    • Hasanain, B.1    Mooradian, A.D.2
  • 35
    • 84857833776 scopus 로고    scopus 로고
    • Cell signalling by reactive lipid species: new concepts and molecular mechanisms
    • COI: 1:CAS:528:DC%2BC38XivV2itbo%3D, PID: 22364280
    • Higdon A, Diers AR, Oh JY, Landar A, Darley-Usmar VM (2012) Cell signalling by reactive lipid species: new concepts and molecular mechanisms. Biochem J 442:453–464
    • (2012) Biochem J , vol.442 , pp. 453-464
    • Higdon, A.1    Diers, A.R.2    Oh, J.Y.3    Landar, A.4    Darley-Usmar, V.M.5
  • 36
    • 85041065464 scopus 로고    scopus 로고
    • Cerebrospinal fluid protein carbonylation identifies oxidative damage in autoimmune demyelination
    • COI: 1:CAS:528:DC%2BC2sXitVSntr0%3D, PID: 28168214
    • Irani DN (2017) Cerebrospinal fluid protein carbonylation identifies oxidative damage in autoimmune demyelination. Ann Clin Transl Neurol 4:145–150
    • (2017) Ann Clin Transl Neurol , vol.4 , pp. 145-150
    • Irani, D.N.1
  • 37
    • 58149350129 scopus 로고    scopus 로고
    • The proteasome and its role in the degradation of oxidized proteins
    • COI: 1:CAS:528:DC%2BD1cXhsVKgsLnE, PID: 18636510
    • Jung T, Grune T (2008) The proteasome and its role in the degradation of oxidized proteins. IUBMB Life 60:743–752
    • (2008) IUBMB Life , vol.60 , pp. 743-752
    • Jung, T.1    Grune, T.2
  • 38
    • 84901239787 scopus 로고    scopus 로고
    • Effect of metformin on methylglyoxal metabolism in patients with type 2 diabetes
    • COI: 1:CAS:528:DC%2BC2cXhsl2nsr7E, PID: 24710646
    • Kender Z, Fleming T, Kopf S et al (2014) Effect of metformin on methylglyoxal metabolism in patients with type 2 diabetes. Exp Clin Endocrinol Diabetes 122:316–319
    • (2014) Exp Clin Endocrinol Diabetes , vol.122 , pp. 316-319
    • Kender, Z.1    Fleming, T.2    Kopf, S.3
  • 39
    • 84911937037 scopus 로고    scopus 로고
    • Increased plasma levels of the methylglyoxal in patients with newly diagnosed type 2 diabetes 2
    • COI: 1:CAS:528:DC%2BC2cXhvVWnsLjN, PID: 24720446
    • Kong X, Ma MZ, Huang K et al (2014) Increased plasma levels of the methylglyoxal in patients with newly diagnosed type 2 diabetes 2. J Diabetes 6:535–540
    • (2014) J Diabetes , vol.6 , pp. 535-540
    • Kong, X.1    Ma, M.Z.2    Huang, K.3
  • 40
    • 84866605658 scopus 로고    scopus 로고
    • Diabetes mellitus and myocardial mitochondrial dysfunction: bench to bedside
    • PID: 22999239
    • Konig A, Bode C, Bugger H (2012) Diabetes mellitus and myocardial mitochondrial dysfunction: bench to bedside. Heart Fail Clin 8:551–561
    • (2012) Heart Fail Clin , vol.8 , pp. 551-561
    • Konig, A.1    Bode, C.2    Bugger, H.3
  • 41
    • 79951870962 scopus 로고    scopus 로고
    • A gene expression signature for insulin resistance
    • COI: 1:CAS:528:DC%2BC3MXmslWjurw%3D, PID: 21081660
    • Konstantopoulos N, Foletta VC, Segal DH et al (2011) A gene expression signature for insulin resistance. Physiol Genomics 43:110–120
    • (2011) Physiol Genomics , vol.43 , pp. 110-120
    • Konstantopoulos, N.1    Foletta, V.C.2    Segal, D.H.3
  • 43
    • 71449103025 scopus 로고    scopus 로고
    • Oxidized laminin-1 induces increased monocyte attachment and expression of ICAM-1 in endothelial cells
    • COI: 1:CAS:528:DC%2BC3cXhtFOntLo%3D, PID: 19958399
    • Kostidou E, Topouridou K, Daniilidis A, Kaloyianni M, Koliakos G (2009) Oxidized laminin-1 induces increased monocyte attachment and expression of ICAM-1 in endothelial cells. Int J Exp Pathol 90:630–637
    • (2009) Int J Exp Pathol , vol.90 , pp. 630-637
    • Kostidou, E.1    Topouridou, K.2    Daniilidis, A.3    Kaloyianni, M.4    Koliakos, G.5
  • 44
    • 41949134709 scopus 로고    scopus 로고
    • Functional mechanics of the ATP-dependent Lon protease- lessons from endogenous protein and synthetic peptide substrates
    • COI: 1:CAS:528:DC%2BD1cXkvVOhtL8%3D, PID: 18359303
    • Lee I, Suzuki CK (2008) Functional mechanics of the ATP-dependent Lon protease- lessons from endogenous protein and synthetic peptide substrates. Biochim Biophys Acta 1784:727–735
    • (2008) Biochim Biophys Acta , vol.1784 , pp. 727-735
    • Lee, I.1    Suzuki, C.K.2
  • 46
    • 84901327057 scopus 로고    scopus 로고
    • Elevated protein carbonyl and HIF-1alpha levels in eyes with proliferative diabetic retinopathy
    • COI: 1:CAS:528:DC%2BC2cXosVOmtb0%3D, PID: 23718695
    • Loukovaara S, Koivunen P, Ingles M, Escobar J, Vento M, Andersson S (2014) Elevated protein carbonyl and HIF-1alpha levels in eyes with proliferative diabetic retinopathy. Acta Ophthalmol 92:323–327
    • (2014) Acta Ophthalmol , vol.92 , pp. 323-327
    • Loukovaara, S.1    Koivunen, P.2    Ingles, M.3    Escobar, J.4    Vento, M.5    Andersson, S.6
  • 47
    • 84892366219 scopus 로고    scopus 로고
    • The thioredoxin antioxidant system
    • COI: 1:CAS:528:DC%2BC3sXhtlyitLzE, PID: 23899494
    • Lu J, Holmgren A (2014) The thioredoxin antioxidant system. Free Radic Biol Med 66:75–87
    • (2014) Free Radic Biol Med , vol.66 , pp. 75-87
    • Lu, J.1    Holmgren, A.2
  • 48
    • 84929942019 scopus 로고    scopus 로고
    • The role of methylglyoxal and the glyoxalase system in diabetes and other age-related diseases
    • COI: 1:CAS:528:DC%2BC2MXlsl2rsb8%3D
    • Maessen DE, Stehouwer CD, Schalkwijk CG (2015) The role of methylglyoxal and the glyoxalase system in diabetes and other age-related diseases. Clin Sci (Lond) 128:839–861
    • (2015) Clin Sci (Lond) , vol.128 , pp. 839-861
    • Maessen, D.E.1    Stehouwer, C.D.2    Schalkwijk, C.G.3
  • 49
    • 70350025576 scopus 로고    scopus 로고
    • Rules governing selective protein carbonylation
    • PID: 19802390
    • Maisonneuve E, Ducret A, Khoueiry P et al (2009) Rules governing selective protein carbonylation. PLoS One 4:e7269
    • (2009) PLoS One , vol.4
    • Maisonneuve, E.1    Ducret, A.2    Khoueiry, P.3
  • 51
    • 67749117788 scopus 로고    scopus 로고
    • Profiling of oxidative stress in patients with inborn errors of metabolism
    • COI: 1:CAS:528:DC%2BD1MXptlWkur0%3D, PID: 19604711
    • Mc Guire PJ, Parikh A, Diaz GA (2009) Profiling of oxidative stress in patients with inborn errors of metabolism. Mol Genet Metab 98:173–180
    • (2009) Mol Genet Metab , vol.98 , pp. 173-180
    • Mc Guire, P.J.1    Parikh, A.2    Diaz, G.A.3
  • 52
    • 2942667688 scopus 로고    scopus 로고
    • Development of insulin resistance and obesity in mice overexpressing cellular glutathione peroxidase
    • COI: 1:CAS:528:DC%2BD2cXltlWru70%3D, PID: 15184668
    • McClung JP, Roneker CA, Mu W et al (2004) Development of insulin resistance and obesity in mice overexpressing cellular glutathione peroxidase. Proc Natl Acad Sci U S A 101:8852–8857
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 8852-8857
    • McClung, J.P.1    Roneker, C.A.2    Mu, W.3
  • 53
    • 84915747811 scopus 로고    scopus 로고
    • Glyoxylate, a new marker metabolite of type 2 diabetes
    • PID: 25525609
    • Nikiforova VJ, Giesbertz P, Wiemer J et al (2014) Glyoxylate, a new marker metabolite of type 2 diabetes. J Diabetes Res 2014:685204
    • (2014) J Diabetes Res , vol.2014 , pp. 685204
    • Nikiforova, V.J.1    Giesbertz, P.2    Wiemer, J.3
  • 54
    • 84878366185 scopus 로고    scopus 로고
    • Mechanism-based antioxidant therapies promise to prevent diabetic complications?
    • COI: 1:CAS:528:DC%2BC3sXnsVCmsro%3D, PID: 24843640
    • Nishikawa T, Araki E (2013) Mechanism-based antioxidant therapies promise to prevent diabetic complications? J Diabetes Investig 4:105–107
    • (2013) J Diabetes Investig , vol.4 , pp. 105-107
    • Nishikawa, T.1    Araki, E.2
  • 55
    • 17844403545 scopus 로고    scopus 로고
    • Role of oxidative carbonylation in protein quality control and senescence
    • PID: 15775985
    • Nystrom T (2005) Role of oxidative carbonylation in protein quality control and senescence. EMBO J 24:1311–1317
    • (2005) EMBO J , vol.24 , pp. 1311-1317
    • Nystrom, T.1
  • 56
    • 0033603599 scopus 로고    scopus 로고
    • Methylglyoxal modification of protein. Chemical and immunochemical characterization of methylglyoxal-arginine adducts
    • COI: 1:CAS:528:DyaK1MXkt1Siur8%3D, PID: 10373458
    • Oya T, Hattori N, Mizuno Y et al (1999) Methylglyoxal modification of protein. Chemical and immunochemical characterization of methylglyoxal-arginine adducts. J Biol Chem 274:18492–18502
    • (1999) J Biol Chem , vol.274 , pp. 18492-18502
    • Oya, T.1    Hattori, N.2    Mizuno, Y.3
  • 57
    • 84907494213 scopus 로고    scopus 로고
    • Peroxiredoxin 6, a novel player in the pathogenesis of diabetes
    • COI: 1:CAS:528:DC%2BC2cXhslWiurrM, PID: 24947358
    • Pacifici F, Arriga R, Sorice GP et al (2014) Peroxiredoxin 6, a novel player in the pathogenesis of diabetes. Diabetes 63:3210–3220
    • (2014) Diabetes , vol.63 , pp. 3210-3220
    • Pacifici, F.1    Arriga, R.2    Sorice, G.P.3
  • 58
    • 79960392126 scopus 로고    scopus 로고
    • Plasma protein carbonylation in chronic uremia
    • COI: 1:CAS:528:DC%2BC3MXhsFSktbjJ, PID: 21607919
    • Pavone B, Sirolli V, Giardinelli A et al (2011) Plasma protein carbonylation in chronic uremia. J Nephrol 24:453–464
    • (2011) J Nephrol , vol.24 , pp. 453-464
    • Pavone, B.1    Sirolli, V.2    Giardinelli, A.3
  • 59
    • 84945496049 scopus 로고    scopus 로고
    • Carnosine metabolism in diabetes is altered by reactive metabolites
    • COI: 1:CAS:528:DC%2BC2MXhtVaiu7nL, PID: 26081982
    • Peters V, Lanthaler B, Amberger A et al (2015) Carnosine metabolism in diabetes is altered by reactive metabolites. Amino Acids 47:2367–2376
    • (2015) Amino Acids , vol.47 , pp. 2367-2376
    • Peters, V.1    Lanthaler, B.2    Amberger, A.3
  • 60
    • 84890116227 scopus 로고    scopus 로고
    • Peroxiredoxins as biomarkers of oxidative stress
    • COI: 1:CAS:528:DC%2BC3sXhvFOlsbrK, PID: 23939310
    • Poynton RA, Hampton MB (2014) Peroxiredoxins as biomarkers of oxidative stress. Biochim Biophys Acta 1840:906–912
    • (2014) Biochim Biophys Acta , vol.1840 , pp. 906-912
    • Poynton, R.A.1    Hampton, M.B.2
  • 61
    • 77950362951 scopus 로고    scopus 로고
    • Hyperglycemia impairs proteasome function by methylglyoxal
    • COI: 1:CAS:528:DC%2BC3cXjslegur8%3D, PID: 20009088
    • Queisser MA, Yao D, Geisler S et al (2010) Hyperglycemia impairs proteasome function by methylglyoxal. Diabetes 59:670–678
    • (2010) Diabetes , vol.59 , pp. 670-678
    • Queisser, M.A.1    Yao, D.2    Geisler, S.3
  • 62
    • 84891816601 scopus 로고    scopus 로고
    • The critical role of methylglyoxal and glyoxalase 1 in diabetic nephropathy
    • COI: 1:CAS:528:DC%2BC2cXhsFKlsw%3D%3D, PID: 24357696
    • Rabbani N, Thornalley PJ (2014) The critical role of methylglyoxal and glyoxalase 1 in diabetic nephropathy. Diabetes 63:50–52
    • (2014) Diabetes , vol.63 , pp. 50-52
    • Rabbani, N.1    Thornalley, P.J.2
  • 63
    • 67849090570 scopus 로고    scopus 로고
    • The fate of monocytes in atherosclerosis
    • COI: 1:CAS:528:DC%2BD1MXpvV2jtbg%3D, PID: 19630762
    • Randolph GJ (2009) The fate of monocytes in atherosclerosis. J Thromb Haemost 7(Suppl 1):28–30
    • (2009) J Thromb Haemost , vol.7 , pp. 28-30
    • Randolph, G.J.1
  • 64
    • 84887615195 scopus 로고    scopus 로고
    • L-carnitine supplementation as a potential antioxidant therapy for inherited neurometabolic disorders
    • COI: 1:CAS:528:DC%2BC3sXhs12kt73O, PID: 24148561
    • Ribas GS, Vargas CR, Wajner M (2014) L-carnitine supplementation as a potential antioxidant therapy for inherited neurometabolic disorders. Gene 533:469–476
    • (2014) Gene , vol.533 , pp. 469-476
    • Ribas, G.S.1    Vargas, C.R.2    Wajner, M.3
  • 65
    • 0035990307 scopus 로고    scopus 로고
    • Oxidative stress in inborn errors of metabolism: lessons from glutathione deficiency
    • COI: 1:CAS:528:DC%2BD38XmtFShsL8%3D, PID: 12137231
    • Ristoff E, Larsson A (2002) Oxidative stress in inborn errors of metabolism: lessons from glutathione deficiency. J Inherit Metab Dis 25:223–226
    • (2002) J Inherit Metab Dis , vol.25 , pp. 223-226
    • Ristoff, E.1    Larsson, A.2
  • 66
    • 84886945867 scopus 로고    scopus 로고
    • Oxidative stress and protein carbonylation in adipose tissue—implications for insulin resistance and diabetes mellitus
    • Ruskovska T, Bernlohr DA (2013) Oxidative stress and protein carbonylation in adipose tissue—implications for insulin resistance and diabetes mellitus. J Proteome 92:323–334
    • (2013) J Proteome , vol.92 , pp. 323-334
    • Ruskovska, T.1    Bernlohr, D.A.2
  • 67
    • 84874918845 scopus 로고    scopus 로고
    • Thioredoxin-interacting protein mediates high glucose-induced reactive oxygen species generation by mitochondria and the NADPH oxidase, Nox4, in mesangial cells
    • COI: 1:CAS:528:DC%2BC3sXjslegs78%3D, PID: 23329835
    • Shah A, Xia L, Goldberg H, Lee KW, Quaggin SE, Fantus IG (2013) Thioredoxin-interacting protein mediates high glucose-induced reactive oxygen species generation by mitochondria and the NADPH oxidase, Nox4, in mesangial cells. J Biol Chem 288:6835–6848
    • (2013) J Biol Chem , vol.288 , pp. 6835-6848
    • Shah, A.1    Xia, L.2    Goldberg, H.3    Lee, K.W.4    Quaggin, S.E.5    Fantus, I.G.6
  • 68
    • 85015811994 scopus 로고    scopus 로고
    • Carbonylation modification regulates Na/K-ATPase Signaling and salt sensitivity: a review and a hypothesis
    • PID: 27445847
    • Shah PT, Martin R, Yan Y, Shapiro JI, Liu J (2016) Carbonylation modification regulates Na/K-ATPase Signaling and salt sensitivity: a review and a hypothesis. Front Physiol 7:256
    • (2016) Front Physiol , vol.7 , pp. 256
    • Shah, P.T.1    Martin, R.2    Yan, Y.3    Shapiro, J.I.4    Liu, J.5
  • 69
    • 84994876695 scopus 로고    scopus 로고
    • Association of glutathione-S-transferase with patients of type 2 diabetes mellitus with and without nephropathy
    • PID: 27377684
    • Sharma M, Gupta S, Singh K et al (2016) Association of glutathione-S-transferase with patients of type 2 diabetes mellitus with and without nephropathy. Diabetes Metab Syndr 10:194–197
    • (2016) Diabetes Metab Syndr , vol.10 , pp. 194-197
    • Sharma, M.1    Gupta, S.2    Singh, K.3
  • 70
    • 84869094223 scopus 로고    scopus 로고
    • Screening for type 2 diabetes and population mortality over 10 years (ADDITION-Cambridge): a cluster-randomised controlled trial
    • PID: 23040422
    • Simmons RK, Echouffo-Tcheugui JB, Sharp SJ et al (2012) Screening for type 2 diabetes and population mortality over 10 years (ADDITION-Cambridge): a cluster-randomised controlled trial. Lancet 380:1741–1748
    • (2012) Lancet , vol.380 , pp. 1741-1748
    • Simmons, R.K.1    Echouffo-Tcheugui, J.B.2    Sharp, S.J.3
  • 71
    • 84947798077 scopus 로고    scopus 로고
    • Antioxidant role of glutathione S-transferases: 4-Hydroxynonenal, a key molecule in stress-mediated signaling
    • COI: 1:CAS:528:DC%2BC2MXhslekt7%2FP, PID: 26476300
    • Singhal SS, Singh SP, Singhal P, Horne D, Singhal J, Awasthi S (2015) Antioxidant role of glutathione S-transferases: 4-Hydroxynonenal, a key molecule in stress-mediated signaling. Toxicol Appl Pharmacol 289:361–370
    • (2015) Toxicol Appl Pharmacol , vol.289 , pp. 361-370
    • Singhal, S.S.1    Singh, S.P.2    Singhal, P.3    Horne, D.4    Singhal, J.5    Awasthi, S.6
  • 72
    • 84859787172 scopus 로고    scopus 로고
    • Glucose-6-phosphate dehydrogenase, NADPH, and cell survival
    • COI: 1:CAS:528:DC%2BC38XktFWrtL0%3D, PID: 22431005
    • Stanton RC (2012) Glucose-6-phosphate dehydrogenase, NADPH, and cell survival. IUBMB Life 64:362–369
    • (2012) IUBMB Life , vol.64 , pp. 362-369
    • Stanton, R.C.1
  • 73
    • 84876327840 scopus 로고    scopus 로고
    • Glycation of human erythrocyte glutathione peroxidase: effect on the physical and kinetic properties
    • COI: 1:CAS:528:DC%2BC3sXnsVygsr0%3D, PID: 23524033
    • Suravajjala S, Cohenford M, Frost LR, Pampati PK, Dain JA (2013) Glycation of human erythrocyte glutathione peroxidase: effect on the physical and kinetic properties. Clin Chim Acta 421:170–176
    • (2013) Clin Chim Acta , vol.421 , pp. 170-176
    • Suravajjala, S.1    Cohenford, M.2    Frost, L.R.3    Pampati, P.K.4    Dain, J.A.5
  • 74
    • 37749024370 scopus 로고    scopus 로고
    • Keap1/Nrf2 signaling regulates oxidative stress tolerance and lifespan in drosophila
    • COI: 1:CAS:528:DC%2BD1cXhtFyjtL0%3D, PID: 18194654
    • Sykiotis GP, Bohmann D (2008) Keap1/Nrf2 signaling regulates oxidative stress tolerance and lifespan in drosophila. Dev Cell 14:76–85
    • (2008) Dev Cell , vol.14 , pp. 76-85
    • Sykiotis, G.P.1    Bohmann, D.2
  • 75
    • 84959302197 scopus 로고    scopus 로고
    • The possible role of glutathione-S-transferase activity in diabetic nephropathy
    • COI: 1:CAS:528:DC%2BC2MXhtVCqsbzL, PID: 25816416
    • Tesauro M, Nistico S, Noce A et al (2015) The possible role of glutathione-S-transferase activity in diabetic nephropathy. Int J Immunopathol Pharmacol 28:129–133
    • (2015) Int J Immunopathol Pharmacol , vol.28 , pp. 129-133
    • Tesauro, M.1    Nistico, S.2    Noce, A.3
  • 76
    • 43449094351 scopus 로고    scopus 로고
    • Protein and nucleotide damage by glyoxal and methylglyoxal in physiological systems—role in ageing and disease
    • Thornalley PJ (2008) Protein and nucleotide damage by glyoxal and methylglyoxal in physiological systems—role in ageing and disease. Drug Metabol Drug Interact 23:125–150
    • (2008) Drug Metabol Drug Interact , vol.23 , pp. 125-150
    • Thornalley, P.J.1
  • 77
    • 84878276346 scopus 로고    scopus 로고
    • Keap1-Nrf2 signaling pathway: mechanisms of regulation and role in protection of cells against toxicity caused by xenobiotics and electrophiles
    • COI: 1:CAS:528:DC%2BC3sXis1Wmu70%3D
    • Turpaev KT (2013) Keap1-Nrf2 signaling pathway: mechanisms of regulation and role in protection of cells against toxicity caused by xenobiotics and electrophiles. Biochemistry (Mosc) 78:111–126
    • (2013) Biochemistry (Mosc) , vol.78 , pp. 111-126
    • Turpaev, K.T.1
  • 79
    • 80052546167 scopus 로고    scopus 로고
    • Experimental evidence of oxidative stress in plasma of homocystinuric patients: a possible role for homocysteine
    • COI: 1:CAS:528:DC%2BC3MXhtFGlsLjE, PID: 21742526
    • Vanzin CS, Biancini GB, Sitta A et al (2011) Experimental evidence of oxidative stress in plasma of homocystinuric patients: a possible role for homocysteine. Mol Genet Metab 104:112–117
    • (2011) Mol Genet Metab , vol.104 , pp. 112-117
    • Vanzin, C.S.1    Biancini, G.B.2    Sitta, A.3
  • 80
    • 84937513354 scopus 로고    scopus 로고
    • Lipid, oxidative and inflammatory profile and alterations in the enzymes paraoxonase and butyrylcholinesterase in plasma of patients with homocystinuria due CBS deficiency: the vitamin B12 and folic acid importance
    • Vanzin CS, Mescka CP, Donida B et al (2015) Lipid, oxidative and inflammatory profile and alterations in the enzymes paraoxonase and butyrylcholinesterase in plasma of patients with homocystinuria due CBS deficiency: the vitamin B12 and folic acid importance. Cell Mol Neurobiol 35:899–911
    • (2015) Cell Mol Neurobiol , vol.35 , pp. 899-911
    • Vanzin, C.S.1    Mescka, C.P.2    Donida, B.3
  • 81
    • 84861130344 scopus 로고    scopus 로고
    • Proposed role of primary protein carbonylation in cell signaling
    • COI: 1:CAS:528:DC%2BC38XhsVKju7jL, PID: 22564352
    • Wong CM, Bansal G, Marcocci L, Suzuki YJ (2012) Proposed role of primary protein carbonylation in cell signaling. Redox Rep 17:90–94
    • (2012) Redox Rep , vol.17 , pp. 90-94
    • Wong, C.M.1    Bansal, G.2    Marcocci, L.3    Suzuki, Y.J.4
  • 82
    • 39449105514 scopus 로고    scopus 로고
    • Protein carbonylation as a novel mechanism in redox signaling
    • COI: 1:CAS:528:DC%2BD1cXhslGku7o%3D, PID: 18079412
    • Wong CM, Cheema AK, Zhang L, Suzuki YJ (2008) Protein carbonylation as a novel mechanism in redox signaling. Circ Res 102:310–318
    • (2008) Circ Res , vol.102 , pp. 310-318
    • Wong, C.M.1    Cheema, A.K.2    Zhang, L.3    Suzuki, Y.J.4
  • 83
    • 84884767245 scopus 로고    scopus 로고
    • Mechanism of protein decarbonylation
    • COI: 1:CAS:528:DC%2BC3sXhvFyksrjK, PID: 24044890
    • Wong CM, Marcocci L, Das D et al (2013) Mechanism of protein decarbonylation. Free Radic Biol Med 65:1126–1133
    • (2013) Free Radic Biol Med , vol.65 , pp. 1126-1133
    • Wong, C.M.1    Marcocci, L.2    Das, D.3
  • 84
    • 84886837226 scopus 로고    scopus 로고
    • The role of antioxidants in the pathophysiology, complications, and management of diabetes mellitus
    • PID: 23770795
    • Zatalia SR, Sanusi H (2013) The role of antioxidants in the pathophysiology, complications, and management of diabetes mellitus. Acta Med Indones 45:141–147
    • (2013) Acta Med Indones , vol.45 , pp. 141-147
    • Zatalia, S.R.1    Sanusi, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.