메뉴 건너뛰기




Volumn 202, Issue 1-3, 2013, Pages 288-297

Detoxification of aldehydes by histidine-containing dipeptides: From chemistry to clinical implications

Author keywords

Aldehyde; Carnosine; Histidine dipeptides; Oxidative stress

Indexed keywords

ACROLEIN; ALDEHYDE; ALDEHYDE DEHYDROGENASE; CARNOSINE; DIGLYCOALDEHYDE; GLUTATHIONE; GLYOXAL; HEXOBARBITAL; HISTIDINE; HISTIDINE DIPEPTIDE; HOMOCARNOSINE; HYDROXYL GROUP; METHYLGLYOXAL; PEROXY RADICAL; REACTIVE OXYGEN METABOLITE; SCHIFF BASE; SINGLET OXYGEN; SUPEROXIDE; UNCLASSIFIED DRUG;

EID: 84875229063     PISSN: 00092797     EISSN: 18727786     Source Type: Journal    
DOI: 10.1016/j.cbi.2012.12.017     Document Type: Conference Paper
Times cited : (45)

References (139)
  • 1
    • 0025814980 scopus 로고
    • Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes
    • H. Esterbauer, R.J. Schaur, and H. Zollner Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes Free Radic. Biol. Med. 11 1991 81 128
    • (1991) Free Radic. Biol. Med. , vol.11 , pp. 81-128
    • Esterbauer, H.1    Schaur, R.J.2    Zollner, H.3
  • 2
    • 37849013375 scopus 로고    scopus 로고
    • Advanced lipid peroxidation end products in oxidative damage to proteins. Potential role in diseases and therapeutic prospects for the inhibitors
    • A. Negre-Salvayre, C. Coatrieux, C. Ingueneau, and R. Salvayre Advanced lipid peroxidation end products in oxidative damage to proteins. Potential role in diseases and therapeutic prospects for the inhibitors Br. J. Pharmacol. 153 2008 6 20
    • (2008) Br. J. Pharmacol. , vol.153 , pp. 6-20
    • Negre-Salvayre, A.1    Coatrieux, C.2    Ingueneau, C.3    Salvayre, R.4
  • 3
    • 77956234404 scopus 로고    scopus 로고
    • Reactive oxygen species and alpha, beta-unsaturated aldehydes as second messengers in signal transduction
    • H.J. Forman Reactive oxygen species and alpha, beta-unsaturated aldehydes as second messengers in signal transduction Ann. N. Y. Acad. Sci. 1203 2010 35 44
    • (2010) Ann. N. Y. Acad. Sci. , vol.1203 , pp. 35-44
    • Forman, H.J.1
  • 5
    • 84861112820 scopus 로고    scopus 로고
    • Flavour chemistry of methylglyoxal and glyoxal
    • Y. Wang, and C.T. Ho Flavour chemistry of methylglyoxal and glyoxal Chem. Soc. Rev. 41 2012 4140 4149
    • (2012) Chem. Soc. Rev. , vol.41 , pp. 4140-4149
    • Wang, Y.1    Ho, C.T.2
  • 6
    • 33646902155 scopus 로고    scopus 로고
    • Oxidized phospholipids predict the presence and progression of carotid and femoral atherosclerosis and symptomatic cardiovascular disease: Five-year prospective results from the Bruneck study
    • S. Tsimikas, S. Kiechl, J. Willeit, M. Mayr, E.R. Miller, F. Kronenberg, Q. Xu, C. Bergmark, S. Weger, F. Oberhollenzer, and J.L. Witztum Oxidized phospholipids predict the presence and progression of carotid and femoral atherosclerosis and symptomatic cardiovascular disease: five-year prospective results from the Bruneck study J. Am. Coll. Cardiol. 47 2006 2219 2228
    • (2006) J. Am. Coll. Cardiol. , vol.47 , pp. 2219-2228
    • Tsimikas, S.1    Kiechl, S.2    Willeit, J.3    Mayr, M.4    Miller, E.R.5    Kronenberg, F.6    Xu, Q.7    Bergmark, C.8    Weger, S.9    Oberhollenzer, F.10    Witztum, J.L.11
  • 7
    • 0035901607 scopus 로고    scopus 로고
    • Measuring circulating oxidized low-density lipoprotein to evaluate coronary risk
    • S. Tsimikas, and J.L. Witztum Measuring circulating oxidized low-density lipoprotein to evaluate coronary risk Circulation 103 2001 1930 1932
    • (2001) Circulation , vol.103 , pp. 1930-1932
    • Tsimikas, S.1    Witztum, J.L.2
  • 8
    • 4644310560 scopus 로고    scopus 로고
    • Role of oxidative modifications in atherosclerosis
    • R. Stocker, and J.F. Keaney Jr. Role of oxidative modifications in atherosclerosis Physiol. Rev. 84 2004 1381 1478
    • (2004) Physiol. Rev. , vol.84 , pp. 1381-1478
    • Stocker, R.1    Keaney, Jr.J.F.2
  • 9
    • 84863495004 scopus 로고    scopus 로고
    • The role of oxidized phospholipids in atherosclerosis
    • J.A. Berliner, N. Leitinger, and S. Tsimikas The role of oxidized phospholipids in atherosclerosis J. Lipid Res. 50 Suppl. 2009 S207 S212
    • (2009) J. Lipid Res. , vol.50 , Issue.SUPPL.
    • Berliner, J.A.1    Leitinger, N.2    Tsimikas, S.3
  • 12
    • 0028908348 scopus 로고
    • Advanced protein glycosylation in diabetes and aging
    • M. Brownlee Advanced protein glycosylation in diabetes and aging Annu. Rev. Med. 46 1995 223 234
    • (1995) Annu. Rev. Med. , vol.46 , pp. 223-234
    • Brownlee, M.1
  • 13
    • 84862643485 scopus 로고    scopus 로고
    • Lipid glycation and protein glycation in diabetes and atherosclerosis
    • T. Miyazawa, K. Nakagawa, S. Shimasaki, and R. Nagai Lipid glycation and protein glycation in diabetes and atherosclerosis Amino Acids 42 2012 1163 1170
    • (2012) Amino Acids , vol.42 , pp. 1163-1170
    • Miyazawa, T.1    Nakagawa, K.2    Shimasaki, S.3    Nagai, R.4
  • 14
    • 43449110447 scopus 로고    scopus 로고
    • Methylglyoxal, diabetes mellitus and diabetic complications
    • D.L. Vander Jagt Methylglyoxal, diabetes mellitus and diabetic complications Drug Metabol. Drug Interact. 23 2008 93 124
    • (2008) Drug Metabol. Drug Interact. , vol.23 , pp. 93-124
    • Vander Jagt, D.L.1
  • 15
    • 84862688640 scopus 로고    scopus 로고
    • Methylglyoxal, glyoxalase 1 and the dicarbonyl proteome
    • N. Rabbani, and P.J. Thornalley Methylglyoxal, glyoxalase 1 and the dicarbonyl proteome Amino Acids 42 2012 1133 1142
    • (2012) Amino Acids , vol.42 , pp. 1133-1142
    • Rabbani, N.1    Thornalley, P.J.2
  • 16
    • 0035991444 scopus 로고    scopus 로고
    • In situ detection of lipid peroxidation and oxidative DNA damage in non-alcoholic fatty liver diseases
    • S. Seki, T. Kitada, T. Yamada, H. Sakaguchi, K. Nakatani, and K. Wakasa In situ detection of lipid peroxidation and oxidative DNA damage in non-alcoholic fatty liver diseases J. Hepatol. 37 2002 56 62
    • (2002) J. Hepatol. , vol.37 , pp. 56-62
    • Seki, S.1    Kitada, T.2    Yamada, T.3    Sakaguchi, H.4    Nakatani, K.5    Wakasa, K.6
  • 17
    • 71549121960 scopus 로고    scopus 로고
    • High urinary excretion of lipid peroxidation-derived DNA damage in patients with cancer-prone liver diseases
    • J. Nair, P. Srivatanakul, C. Haas, A. Jedpiyawongse, T. Khuhaprema, H.K. Seitz, and H. Bartsch High urinary excretion of lipid peroxidation-derived DNA damage in patients with cancer-prone liver diseases Mutat. Res. 683 2010 23 28
    • (2010) Mutat. Res. , vol.683 , pp. 23-28
    • Nair, J.1    Srivatanakul, P.2    Haas, C.3    Jedpiyawongse, A.4    Khuhaprema, T.5    Seitz, H.K.6    Bartsch, H.7
  • 20
    • 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
    • P.A. Grimsrud, M.J. Picklo Sr., T.J. Griffin, and D.A. Bernlohr 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 2007 624 637
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 624-637
    • Grimsrud, P.A.1    Picklo, Sr.M.J.2    Griffin, T.J.3    Bernlohr, D.A.4
  • 21
    • 77957256030 scopus 로고    scopus 로고
    • Role of by-products of lipid oxidation in Alzheimer's disease brain: A focus on acrolein
    • M. Singh, T.N. Dang, M. Arseneault, and C. Ramassamy Role of by-products of lipid oxidation in Alzheimer's disease brain: a focus on acrolein J. Alzheimers Dis. 21 2010 741 756
    • (2010) J. Alzheimers Dis. , vol.21 , pp. 741-756
    • Singh, M.1    Dang, T.N.2    Arseneault, M.3    Ramassamy, C.4
  • 22
    • 70349492687 scopus 로고    scopus 로고
    • Molecular mechanisms of 4-hydroxy-2-nonenal and acrolein toxicity: Nucleophilic targets and adduct formation
    • R.M. LoPachin, T. Gavin, D.R. Petersen, and D.S. Barber Molecular mechanisms of 4-hydroxy-2-nonenal and acrolein toxicity: nucleophilic targets and adduct formation Chem. Res. Toxicol. 22 2009 1499 1508
    • (2009) Chem. Res. Toxicol. , vol.22 , pp. 1499-1508
    • Lopachin, R.M.1    Gavin, T.2    Petersen, D.R.3    Barber, D.S.4
  • 24
    • 71549144988 scopus 로고    scopus 로고
    • Lipid oxidation and peroxidation in CNS health and disease: From molecular mechanisms to therapeutic opportunities
    • R.M. Adibhatla, and J.F. Hatcher Lipid oxidation and peroxidation in CNS health and disease: from molecular mechanisms to therapeutic opportunities Antioxid. Redox Signal. 12 2010 125 169
    • (2010) Antioxid. Redox Signal. , vol.12 , pp. 125-169
    • Adibhatla, R.M.1    Hatcher, J.F.2
  • 27
    • 0035371184 scopus 로고    scopus 로고
    • Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple
    • F.Q. Schafer, and G.R. Buettner Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple Free Radic. Biol. Med. 30 2001 1191 1212
    • (2001) Free Radic. Biol. Med. , vol.30 , pp. 1191-1212
    • Schafer, F.Q.1    Buettner, G.R.2
  • 29
    • 38449115264 scopus 로고    scopus 로고
    • Endogenous alpha-oxoaldehydes and formation of protein and nucleotide advanced glycation endproducts in tissue damage
    • discussion 243-226
    • P.J. Thornalley Endogenous alpha-oxoaldehydes and formation of protein and nucleotide advanced glycation endproducts in tissue damage Novartis Found. Symp. 285 2007 229 243 discussion 243-226
    • (2007) Novartis Found. Symp. , vol.285 , pp. 229-243
    • Thornalley, P.J.1
  • 30
    • 34250704858 scopus 로고    scopus 로고
    • Methylglyoxal and advanced glycation endproducts: New therapeutic horizons?
    • K. Desai, and L. Wu Methylglyoxal and advanced glycation endproducts: new therapeutic horizons? Recent Pat. Cardiovasc. Drug Discovery 2 2007 89 99
    • (2007) Recent Pat. Cardiovasc. Drug Discovery , vol.2 , pp. 89-99
    • Desai, K.1    Wu, L.2
  • 31
    • 4243088697 scopus 로고    scopus 로고
    • Aldehyde-sequestering drugs: Tools for studying protein damage by lipid peroxidation products
    • P.C. Burcham, L.M. Kaminskas, F.R. Fontaine, D.R. Petersen, and S.M. Pyke Aldehyde-sequestering drugs: tools for studying protein damage by lipid peroxidation products Toxicology 181-182 2002 229 236
    • (2002) Toxicology , vol.181-182 , pp. 229-236
    • Burcham, P.C.1    Kaminskas, L.M.2    Fontaine, F.R.3    Petersen, D.R.4    Pyke, S.M.5
  • 32
    • 67649877903 scopus 로고    scopus 로고
    • Carnosine and its possible roles in nutrition and health
    • A.R. Hipkiss Carnosine and its possible roles in nutrition and health Adv. Food Nutr. Res. 57 2009 87 154
    • (2009) Adv. Food Nutr. Res. , vol.57 , pp. 87-154
    • Hipkiss, A.R.1
  • 33
    • 28644435734 scopus 로고    scopus 로고
    • Carnosine and related dipeptides as quenchers of reactive carbonyl species: From structural studies to therapeutic perspectives
    • G. Aldini, R.M. Facino, G. Beretta, and M. Carini Carnosine and related dipeptides as quenchers of reactive carbonyl species: from structural studies to therapeutic perspectives Biofactors 24 2005 77 87
    • (2005) Biofactors , vol.24 , pp. 77-87
    • Aldini, G.1    Facino, R.M.2    Beretta, G.3    Carini, M.4
  • 34
    • 0034222401 scopus 로고    scopus 로고
    • Problems and perspectives in studying the biological role of carnosine
    • A.A. Boldyrev Problems and perspectives in studying the biological role of carnosine Biochemistry (Mosc) 65 2000 751 756
    • (2000) Biochemistry (Mosc) , vol.65 , pp. 751-756
    • Boldyrev, A.A.1
  • 35
    • 0025081749 scopus 로고
    • The histidine-containing dipeptides, carnosine and anserine: Distribution, properties and biological significance
    • A.A. Boldyrev, and S.E. Severin The histidine-containing dipeptides, carnosine and anserine: distribution, properties and biological significance Adv. Enzyme Regul. 30 1990 175 194
    • (1990) Adv. Enzyme Regul. , vol.30 , pp. 175-194
    • Boldyrev, A.A.1    Severin, S.E.2
  • 36
    • 34548670389 scopus 로고
    • Quantitative studies of carnosine and anserine in mammalian muscle: II. The distribution of carnosine and anserine in various muscles of different species
    • J.A. Zapp, and D.W. Wilson Quantitative studies of carnosine and anserine in mammalian muscle: II. The distribution of carnosine and anserine in various muscles of different species J. Biol. Chem. 126 1938 19 27
    • (1938) J. Biol. Chem. , vol.126 , pp. 19-27
    • Zapp, J.A.1    Wilson, D.W.2
  • 37
    • 0014785883 scopus 로고
    • Carnosine and related substances in animal tissues
    • K.G. Crush Carnosine and related substances in animal tissues Comp. Biochem. Physiol. 34 1970 3 30
    • (1970) Comp. Biochem. Physiol. , vol.34 , pp. 3-30
    • Crush, K.G.1
  • 38
    • 0025836299 scopus 로고
    • Carnosine in the brain and olfactory system of amphibia and reptilia: A comparative study using immunocytochemical and biochemical methods
    • C. Artero, E. Marti, S. Biffo, B. Mulatero, C. Andreone, F.L. Margolis, and A. Fasolo Carnosine in the brain and olfactory system of amphibia and reptilia: a comparative study using immunocytochemical and biochemical methods Neurosci. Lett. 130 1991 182 186
    • (1991) Neurosci. Lett. , vol.130 , pp. 182-186
    • Artero, C.1    Marti, E.2    Biffo, S.3    Mulatero, B.4    Andreone, C.5    Margolis, F.L.6    Fasolo, A.7
  • 40
    • 79952022812 scopus 로고    scopus 로고
    • Effects of beta-alanine on muscle carnosine and exercise performance. A review of the current literature
    • J.Y. Culbertson, R.B. Kreider, M. Greenwood, and M. Cooke Effects of beta-alanine on muscle carnosine and exercise performance. A review of the current literature Nutrients 2 2010 75 98
    • (2010) Nutrients , vol.2 , pp. 75-98
    • Culbertson, J.Y.1    Kreider, R.B.2    Greenwood, M.3    Cooke, M.4
  • 41
    • 33846696040 scopus 로고    scopus 로고
    • Influence of beta-alanine supplementation on skeletal muscle carnosine concentrations and high intensity cycling capacity
    • C.A. Hill, R.C. Harris, H.J. Kim, B.D. Harris, C. Sale, L.H. Boobis, C.K. Kim, and J.A. Wise Influence of beta-alanine supplementation on skeletal muscle carnosine concentrations and high intensity cycling capacity Amino Acids 32 2007 225 233
    • (2007) Amino Acids , vol.32 , pp. 225-233
    • Hill, C.A.1    Harris, R.C.2    Kim, H.J.3    Harris, B.D.4    Sale, C.5    Boobis, L.H.6    Kim, C.K.7    Wise, J.A.8
  • 42
    • 0000519943 scopus 로고
    • The catabolism of C14-labeled uracil, dihydrouracil, and beta-ureidopropionic acid in rat liver slices
    • P. Fritzson The catabolism of C14-labeled uracil, dihydrouracil, and beta-ureidopropionic acid in rat liver slices J. Biol. Chem. 226 1957 223 228
    • (1957) J. Biol. Chem. , vol.226 , pp. 223-228
    • Fritzson, P.1
  • 43
    • 0018082943 scopus 로고
    • Purification and characterization of carnosine synthetase from mouse olfactory bulbs
    • H. Horinishi, M. Grillo, and F.L. Margolis Purification and characterization of carnosine synthetase from mouse olfactory bulbs J. Neurochem. 31 1978 909 919
    • (1978) J. Neurochem. , vol.31 , pp. 909-919
    • Horinishi, H.1    Grillo, M.2    Margolis, F.L.3
  • 44
    • 0033154861 scopus 로고    scopus 로고
    • Influence of oral beta-alanine and l-histidine supplementation on the carnosine content of the gluteus medius
    • M. Dunnett, and R.C. Harris Influence of oral beta-alanine and l-histidine supplementation on the carnosine content of the gluteus medius Equine Vet. J. Suppl. 30 1999 499 504
    • (1999) Equine Vet. J. Suppl. , vol.30 , pp. 499-504
    • Dunnett, M.1    Harris, R.C.2
  • 45
    • 0028171948 scopus 로고
    • Transport of beta-alanine and biosynthesis of carnosine by skeletal muscle cells in primary culture
    • A. Bakardjiev, and K. Bauer Transport of beta-alanine and biosynthesis of carnosine by skeletal muscle cells in primary culture Eur. J. Biochem. 225 1994 617 623
    • (1994) Eur. J. Biochem. , vol.225 , pp. 617-623
    • Bakardjiev, A.1    Bauer, K.2
  • 46
    • 17044401851 scopus 로고    scopus 로고
    • Identification and characterization of a mouse dipeptidase that hydrolyzes l-carnosine
    • H. Otani, N. Okumura, A. Hashida-Okumura, and K. Nagai Identification and characterization of a mouse dipeptidase that hydrolyzes l-carnosine J. Biochem. 137 2005 167 175
    • (2005) J. Biochem. , vol.137 , pp. 167-175
    • Otani, H.1    Okumura, N.2    Hashida-Okumura, A.3    Nagai, K.4
  • 50
    • 1942487737 scopus 로고    scopus 로고
    • Carnosine uptake in rat choroid plexus primary cell cultures and choroid plexus whole tissue from PEPT2 null mice
    • N.S. Teuscher, H. Shen, C. Shu, J. Xiang, R.F. Keep, and D.E. Smith Carnosine uptake in rat choroid plexus primary cell cultures and choroid plexus whole tissue from PEPT2 null mice J. Neurochem. 89 2004 375 382
    • (2004) J. Neurochem. , vol.89 , pp. 375-382
    • Teuscher, N.S.1    Shen, H.2    Shu, C.3    Xiang, J.4    Keep, R.F.5    Smith, D.E.6
  • 51
    • 65949111504 scopus 로고    scopus 로고
    • Influence of genetic knockout of Pept2 on the in vivo disposition of endogenous and exogenous carnosine in wild-type and Pept2 null mice
    • M.A. Kamal, H. Jiang, Y. Hu, R.F. Keep, and D.E. Smith Influence of genetic knockout of Pept2 on the in vivo disposition of endogenous and exogenous carnosine in wild-type and Pept2 null mice Am. J. Physiol. Regul. Integr. Comp. Physiol. 296 2009 R986 R991
    • (2009) Am. J. Physiol. Regul. Integr. Comp. Physiol. , vol.296
    • Kamal, M.A.1    Jiang, H.2    Hu, Y.3    Keep, R.F.4    Smith, D.E.5
  • 52
    • 41949096418 scopus 로고    scopus 로고
    • Anserine and carnosine determination in meat samples by pure micellar liquid chromatography
    • M. Gil-Agusti, J. Esteve-Romero, and S. Carda-Broch Anserine and carnosine determination in meat samples by pure micellar liquid chromatography J. Chromatogr. A 1189 2008 444 450
    • (2008) J. Chromatogr. A , vol.1189 , pp. 444-450
    • Gil-Agusti, M.1    Esteve-Romero, J.2    Carda-Broch, S.3
  • 53
    • 77955983628 scopus 로고    scopus 로고
    • Retention modeling under organic modifier gradient conditions in ion-pair reversed-phase chromatography. Application to the separation of a set of underivatized amino acids
    • A. Pappa-Louisi, P. Agrafiotou, and K. Papachristos Retention modeling under organic modifier gradient conditions in ion-pair reversed-phase chromatography. Application to the separation of a set of underivatized amino acids Anal. Bioanal. Chem. 397 2010 2151 2159
    • (2010) Anal. Bioanal. Chem. , vol.397 , pp. 2151-2159
    • Pappa-Louisi, A.1    Agrafiotou, P.2    Papachristos, K.3
  • 54
    • 0026639585 scopus 로고
    • Determination of carnosine and other biogenic imidazoles in equine plasma by isocratic reversed-phase ion-pair high-performance liquid chromatography
    • M. Dunnett, and R.C. Harris Determination of carnosine and other biogenic imidazoles in equine plasma by isocratic reversed-phase ion-pair high-performance liquid chromatography J. Chromatogr. 579 1992 45 53
    • (1992) J. Chromatogr. , vol.579 , pp. 45-53
    • Dunnett, M.1    Harris, R.C.2
  • 55
    • 1842480572 scopus 로고    scopus 로고
    • Determination of carnosine in feed and meat by high-performance anion-exchange chromatography with integrated pulsed amperometric detection
    • D. Nardiello, and T.R.I. Cataldi Determination of carnosine in feed and meat by high-performance anion-exchange chromatography with integrated pulsed amperometric detection J. Chromatogr. A 1035 2004 285 289
    • (2004) J. Chromatogr. A , vol.1035 , pp. 285-289
    • Nardiello, D.1    Cataldi, T.R.I.2
  • 56
    • 0034617374 scopus 로고    scopus 로고
    • Precise analysis of primary amino acids in urine by an automated high-performance liquid chromatography method: Comparison with ion-exchange chromatography
    • D. Fekkes, A. Voskuilen-Kooyman, R. Jankie, and J. Huijmans Precise analysis of primary amino acids in urine by an automated high-performance liquid chromatography method: comparison with ion-exchange chromatography J. Chromatogr. B. Biomed. Sci. Appl. 744 2000 183 188
    • (2000) J. Chromatogr. B. Biomed. Sci. Appl. , vol.744 , pp. 183-188
    • Fekkes, D.1    Voskuilen-Kooyman, A.2    Jankie, R.3    Huijmans, J.4
  • 57
    • 34248632238 scopus 로고    scopus 로고
    • Optimization of separation and detection of 6-aminoquinolyl derivatives of amino acids by using reversed-phase liquid chromatography with on line UV, fluorescence and electrochemical detection
    • A. Pappa-Louisi, P. Nikitas, P. Agrafiotou, and A. Papageorgiou Optimization of separation and detection of 6-aminoquinolyl derivatives of amino acids by using reversed-phase liquid chromatography with on line UV, fluorescence and electrochemical detection Anal. Chim. Acta 593 2007 92 97
    • (2007) Anal. Chim. Acta , vol.593 , pp. 92-97
    • Pappa-Louisi, A.1    Nikitas, P.2    Agrafiotou, P.3    Papageorgiou, A.4
  • 58
    • 74049151985 scopus 로고    scopus 로고
    • Sensitive determination of carnosine in urine by high-performance liquid chromatography using 4-(5,6-dimethoxy-2-phthalimidinyl)-2-methoxyphenylsulfonyl chloride as a fluorescent labeling reagent
    • Y. Tsuruta, K. Maruyama, H. Inoue, K. Kosha, Y. Date, N. Okamura, S. Eto, and E. Kojima Sensitive determination of carnosine in urine by high-performance liquid chromatography using 4-(5,6-dimethoxy-2-phthalimidinyl)-2- methoxyphenylsulfonyl chloride as a fluorescent labeling reagent J. Chromatogr. B. Anal. Technol. Biomed. Life Sci. 878 2010 327 332
    • (2010) J. Chromatogr. B. Anal. Technol. Biomed. Life Sci. , vol.878 , pp. 327-332
    • Tsuruta, Y.1    Maruyama, K.2    Inoue, H.3    Kosha, K.4    Date, Y.5    Okamura, N.6    Eto, S.7    Kojima, E.8
  • 59
    • 84875211138 scopus 로고    scopus 로고
    • Content determination of carnosine by pre-column derivatization with reversed phase-high performance liquid chromatography
    • Q. Hu, X. Chen, K. Bi, and J. Yao Content determination of carnosine by pre-column derivatization with reversed phase-high performance liquid chromatography Shenyang Yaoke Daxue Xuebao 26 2009 376 378
    • (2009) Shenyang Yaoke Daxue Xuebao , vol.26 , pp. 376-378
    • Hu, Q.1    Chen, X.2    Bi, K.3    Yao, J.4
  • 60
    • 31544434287 scopus 로고    scopus 로고
    • Method for the quantification of underivatized amino acids on dry blood spots from newborn screening by HPLC-ESI-MS/MS
    • M. Zoppa, L. Gallo, F. Zacchello, and G. Giordano Method for the quantification of underivatized amino acids on dry blood spots from newborn screening by HPLC-ESI-MS/MS J. Chromatogr. B Anal. Technol. Biomed. Life Sci. 831 2006 267 273
    • (2006) J. Chromatogr. B Anal. Technol. Biomed. Life Sci. , vol.831 , pp. 267-273
    • Zoppa, M.1    Gallo, L.2    Zacchello, F.3    Giordano, G.4
  • 61
    • 27944467126 scopus 로고    scopus 로고
    • A new reversed-phase liquid chromatographic/tandem mass spectrometric method for analysis of underivatised amino acids: Evaluation for the diagnosis and the management of inherited disorders of amino acid metabolism
    • M. Piraud, C. Vianey-Saban, C. Bourdin, C. Acquaviva-Bourdain, S. Boyer, C. Elfakir, and D. Bouchu A new reversed-phase liquid chromatographic/tandem mass spectrometric method for analysis of underivatised amino acids: evaluation for the diagnosis and the management of inherited disorders of amino acid metabolism Rapid Commun. Mass Spectrom. 19 2005 3287 3297
    • (2005) Rapid Commun. Mass Spectrom. , vol.19 , pp. 3287-3297
    • Piraud, M.1    Vianey-Saban, C.2    Bourdin, C.3    Acquaviva-Bourdain, C.4    Boyer, S.5    Elfakir, C.6    Bouchu, D.7
  • 62
    • 77954197821 scopus 로고    scopus 로고
    • High-throughput and multiplexed LC/MS/MRM method for targeted metabolomics
    • R. Wei, G. Li, and A.B. Seymour High-throughput and multiplexed LC/MS/MRM method for targeted metabolomics Anal. Chem. 82 2010 5527 5533
    • (2010) Anal. Chem. , vol.82 , pp. 5527-5533
    • Wei, R.1    Li, G.2    Seymour, A.B.3
  • 63
    • 20644444777 scopus 로고    scopus 로고
    • Ion-pairing reversed-phase liquid chromatography/electrospray ionization mass spectrometric analysis of 76 underivatized amino acids of biological interest: A new tool for the diagnosis of inherited disorders of amino acid metabolism
    • M. Piraud, C. Vianey-Saban, K. Petritis, C. Elfakir, J.P. Steghens, and D. Bouchu Ion-pairing reversed-phase liquid chromatography/electrospray ionization mass spectrometric analysis of 76 underivatized amino acids of biological interest: a new tool for the diagnosis of inherited disorders of amino acid metabolism Rapid Commun. Mass Spectrom. 19 2005 1587 1602
    • (2005) Rapid Commun. Mass Spectrom. , vol.19 , pp. 1587-1602
    • Piraud, M.1    Vianey-Saban, C.2    Petritis, K.3    Elfakir, C.4    Steghens, J.P.5    Bouchu, D.6
  • 64
    • 0037930740 scopus 로고    scopus 로고
    • ESI-MS/MS analysis of underivatised amino acids: A new tool for the diagnosis of inherited disorders of amino acid metabolism. Fragmentation study of 79 molecules of biological interest in positive and negative ionisation mode
    • M. Piraud, C. Vianey-Saban, K. Petritis, C. Elfakir, J.P. Steghens, A. Morla, and D. Bouchu ESI-MS/MS analysis of underivatised amino acids: a new tool for the diagnosis of inherited disorders of amino acid metabolism. Fragmentation study of 79 molecules of biological interest in positive and negative ionisation mode Rapid Commun. Mass Spectrom. 17 2003 1297 1311
    • (2003) Rapid Commun. Mass Spectrom. , vol.17 , pp. 1297-1311
    • Piraud, M.1    Vianey-Saban, C.2    Petritis, K.3    Elfakir, C.4    Steghens, J.P.5    Morla, A.6    Bouchu, D.7
  • 65
    • 0345827782 scopus 로고    scopus 로고
    • Recent advances in capillary electrophoresis and capillary electrochromatography of peptides
    • V. Kasicka Recent advances in capillary electrophoresis and capillary electrochromatography of peptides Electrophoresis 24 2003 4013 4046
    • (2003) Electrophoresis , vol.24 , pp. 4013-4046
    • Kasicka, V.1
  • 66
    • 84875222026 scopus 로고    scopus 로고
    • Comparison of HPLC and CE to separate and quantify carnosine and anserin in meat product
    • C. Jiang, K. Lin, and T. Tsai Comparison of HPLC and CE to separate and quantify carnosine and anserin in meat product Taiwan Nongye Huaxue Yu Shipin Kexue 41 2003 294 299
    • (2003) Taiwan Nongye Huaxue Yu Shipin Kexue , vol.41 , pp. 294-299
    • Jiang, C.1    Lin, K.2    Tsai, T.3
  • 67
    • 84855955383 scopus 로고    scopus 로고
    • Enhancing the coverage of the urinary metabolome by sheathless capillary electrophoresis-mass spectrometry
    • R. Ramautar, J.M. Busnel, A.M. Deelder, and O.A. Mayboroda Enhancing the coverage of the urinary metabolome by sheathless capillary electrophoresis-mass spectrometry Anal. Chem. 84 2012 885 892
    • (2012) Anal. Chem. , vol.84 , pp. 885-892
    • Ramautar, R.1    Busnel, J.M.2    Deelder, A.M.3    Mayboroda, O.A.4
  • 68
    • 80455150007 scopus 로고    scopus 로고
    • Analysis of therapeutic peptides in human urine by combination of capillary zone electrophoresis-electrospray mass spectrometry with preparative capillary isotachophoresis sample pretreatment
    • A. Stanova, J. Marak, M. Rezeli, C. Pager, F. Kilar, and D. Kaniansky Analysis of therapeutic peptides in human urine by combination of capillary zone electrophoresis-electrospray mass spectrometry with preparative capillary isotachophoresis sample pretreatment J. Chromatogr. A 1218 2011 8701 8707
    • (2011) J. Chromatogr. A , vol.1218 , pp. 8701-8707
    • Stanova, A.1    Marak, J.2    Rezeli, M.3    Pager, C.4    Kilar, F.5    Kaniansky, D.6
  • 69
    • 79955488796 scopus 로고    scopus 로고
    • Solid-phase extraction for metabolomic analysis of high-salinity samples by capillary electrophoresis-mass spectrometry
    • A. Oikawa, N. Fujita, R. Horie, K. Saito, and K. Tawaraya Solid-phase extraction for metabolomic analysis of high-salinity samples by capillary electrophoresis-mass spectrometry J. Sep. Sci. 34 2011 1063 1068
    • (2011) J. Sep. Sci. , vol.34 , pp. 1063-1068
    • Oikawa, A.1    Fujita, N.2    Horie, R.3    Saito, K.4    Tawaraya, K.5
  • 70
    • 78650313159 scopus 로고    scopus 로고
    • Simultaneous analysis of amino acids and carboxylic acids by capillary electrophoresis-mass spectrometry using an acidic electrolyte and uncoated fused-silica capillary
    • M. Wakayama, N. Aoki, H. Sasaki, and R. Ohsugi Simultaneous analysis of amino acids and carboxylic acids by capillary electrophoresis-mass spectrometry using an acidic electrolyte and uncoated fused-silica capillary Anal. Chem. 82 2010 9967 9976
    • (2010) Anal. Chem. , vol.82 , pp. 9967-9976
    • Wakayama, M.1    Aoki, N.2    Sasaki, H.3    Ohsugi, R.4
  • 72
    • 4344622634 scopus 로고    scopus 로고
    • Qualitative and quantitative analysis of amino acids by capillary electrophoresis-electrospray ionization-tandem mass spectrometry
    • T. Soga, Y. Kakazu, M. Robert, M. Tomita, and T. Nishioka Qualitative and quantitative analysis of amino acids by capillary electrophoresis-electrospray ionization-tandem mass spectrometry Electrophoresis 25 2004 1964 1972
    • (2004) Electrophoresis , vol.25 , pp. 1964-1972
    • Soga, T.1    Kakazu, Y.2    Robert, M.3    Tomita, M.4    Nishioka, T.5
  • 74
    • 11144341557 scopus 로고    scopus 로고
    • Noninvasive measurement of temperature and fractional dissociation of imidazole in human lower leg muscles using 1H-nuclear magnetic resonance spectroscopy
    • Y. Yoshioka, H. Oikawa, S. Ehara, T. Inoue, A. Ogawa, Y. Kanbara, and M. Kubokawa Noninvasive measurement of temperature and fractional dissociation of imidazole in human lower leg muscles using 1H-nuclear magnetic resonance spectroscopy J. Appl. Physiol. 98 2005 282 287
    • (2005) J. Appl. Physiol. , vol.98 , pp. 282-287
    • Yoshioka, Y.1    Oikawa, H.2    Ehara, S.3    Inoue, T.4    Ogawa, A.5    Kanbara, Y.6    Kubokawa, M.7
  • 76
    • 33947683803 scopus 로고    scopus 로고
    • Carnosine, taurine and enzyme activities of human skeletal muscle fibres from elderly subjects with osteoarthritis and young moderately active subjects
    • M.J. Tallon, R.C. Harris, N. Maffulli, and M.A. Tarnopolsky Carnosine, taurine and enzyme activities of human skeletal muscle fibres from elderly subjects with osteoarthritis and young moderately active subjects Biogerontology 8 2007 129 137
    • (2007) Biogerontology , vol.8 , pp. 129-137
    • Tallon, M.J.1    Harris, R.C.2    Maffulli, N.3    Tarnopolsky, M.A.4
  • 77
    • 0028399024 scopus 로고
    • 1H-NMR measurement of fractional dissociation of imidazole in intact animals
    • B.M. Hitzig, W.C. Perng, T. Burt, P. Okunieff, and D.C. Johnson 1H-NMR measurement of fractional dissociation of imidazole in intact animals Am. J. Physiol. 266 1994 R1008 R1015
    • (1994) Am. J. Physiol. , vol.266
    • Hitzig, B.M.1    Perng, W.C.2    Burt, T.3    Okunieff, P.4    Johnson, D.C.5
  • 79
    • 12244286776 scopus 로고    scopus 로고
    • The carnosine C-2 proton's chemical shift reports intracellular pH in oxidative and glycolytic muscle fibers
    • B.M. Damon, A.C. Hsu, H.J. Stark, and M.J. Dawson The carnosine C-2 proton's chemical shift reports intracellular pH in oxidative and glycolytic muscle fibers Magn. Reson. Med. 49 2003 233 240
    • (2003) Magn. Reson. Med. , vol.49 , pp. 233-240
    • Damon, B.M.1    Hsu, A.C.2    Stark, H.J.3    Dawson, M.J.4
  • 80
    • 0026089320 scopus 로고
    • Localized Proton NMR-spectroscopy using stimulated echoes-applications to human skeletal-muscle in vivo
    • H. Bruhn, J. Frahm, M.L. Gyngell, K.D. Merboldt, W. Hanicke, and R. Sauter Localized Proton NMR-spectroscopy using stimulated echoes-applications to human skeletal-muscle in vivo Magn. Reson. Med. 17 1991 82 94
    • (1991) Magn. Reson. Med. , vol.17 , pp. 82-94
    • Bruhn, H.1    Frahm, J.2    Gyngell, M.L.3    Merboldt, K.D.4    Hanicke, W.5    Sauter, R.6
  • 82
    • 78049246732 scopus 로고    scopus 로고
    • Discrimination of the geographical origin of beef by 1h NMR-based metabolomics
    • Y. Jung, J. Lee, J. Kwon, K.-S. Lee, D.H. Ryu, and G.-S. Hwang Discrimination of the geographical origin of beef by 1h NMR-based metabolomics J. Agric. Food. Chem. 58 2010 10458 10466
    • (2010) J. Agric. Food. Chem. , vol.58 , pp. 10458-10466
    • Jung, Y.1    Lee, J.2    Kwon, J.3    Lee, K.-S.4    Ryu, D.H.5    Hwang, G.-S.6
  • 85
    • 79954436653 scopus 로고    scopus 로고
    • Vegetarianism, female gender and increasing age, but not CNDP1 genotype, are associated with reduced muscle carnosine levels in humans
    • I. Everaert, A. Mooyaart, A. Baguet, A. Zutinic, H. Baelde, E. Achten, Y. Taes, E. De Heer, and W. Derave Vegetarianism, female gender and increasing age, but not CNDP1 genotype, are associated with reduced muscle carnosine levels in humans Amino Acids 40 2011 1221 1229
    • (2011) Amino Acids , vol.40 , pp. 1221-1229
    • Everaert, I.1    Mooyaart, A.2    Baguet, A.3    Zutinic, A.4    Baelde, H.5    Achten, E.6    Taes, Y.7    De Heer, E.8    Derave, W.9
  • 87
    • 35649013167 scopus 로고    scopus 로고
    • Beta-Alanine supplementation augments muscle carnosine content and attenuates fatigue during repeated isokinetic contraction bouts in trained sprinters
    • W. Derave, M.S. Ozdemir, R.C. Harris, A. Pottier, H. Reyngoudt, K. Koppo, J.A. Wise, and E. Achten Beta-Alanine supplementation augments muscle carnosine content and attenuates fatigue during repeated isokinetic contraction bouts in trained sprinters J. Appl. Physiol. 103 2007 1736 1743
    • (2007) J. Appl. Physiol. , vol.103 , pp. 1736-1743
    • Derave, W.1    Ozdemir, M.S.2    Harris, R.C.3    Pottier, A.4    Reyngoudt, H.5    Koppo, K.6    Wise, J.A.7    Achten, E.8
  • 88
    • 37049056278 scopus 로고
    • Model compounds for metal-protein interaction: The crystal structure of the copper(II) complex of β-alanyl-l-histidine (carnosine)
    • H.C. Freeman, and J.J. Szymanski Model compounds for metal-protein interaction: the crystal structure of the copper(II) complex of β-alanyl-l-histidine (carnosine) Chem. Commun. (London) 1965 598 599
    • (1965) Chem. Commun. (London) , pp. 598-599
    • Freeman, H.C.1    Szymanski, J.J.2
  • 90
    • 0017591002 scopus 로고
    • Carnosine in olfaction-proton magnetic-resonance spectral evidence for tissue-specific carnosine binding-sites
    • C.E. Brown, F.L. Margolis, T.H. Williams, R.G. Pitcher, and G. Elgar Carnosine in olfaction-proton magnetic-resonance spectral evidence for tissue-specific carnosine binding-sites Neurochem. Res. 2 1977 555 579
    • (1977) Neurochem. Res. , vol.2 , pp. 555-579
    • Brown, C.E.1    Margolis, F.L.2    Williams, T.H.3    Pitcher, R.G.4    Elgar, G.5
  • 91
    • 0006432644 scopus 로고
    • Chelation chemistry of carnosine-evidence that mixed complexes may occur in vivo
    • C.E. Brown, and W.E. Antholine Chelation chemistry of carnosine-evidence that mixed complexes may occur in vivo J. Phys. Chem. 83 1979 3314 3319
    • (1979) J. Phys. Chem. , vol.83 , pp. 3314-3319
    • Brown, C.E.1    Antholine, W.E.2
  • 92
    • 1542571791 scopus 로고    scopus 로고
    • Vibrational characterisation and biological activity of carnosine and its metal complexes
    • A. Torreggiani, A. Trinchero, M. Tamba, and G. Fini Vibrational characterisation and biological activity of carnosine and its metal complexes Ital. J. Biochem. 52 2003 87 97
    • (2003) Ital. J. Biochem. , vol.52 , pp. 87-97
    • Torreggiani, A.1    Trinchero, A.2    Tamba, M.3    Fini, G.4
  • 93
    • 0034219225 scopus 로고    scopus 로고
    • Metal complexes of carnosine
    • E.J. Baran Metal complexes of carnosine Biochemistry (Mosc.) 65 2000 789 797
    • (2000) Biochemistry (Mosc.) , vol.65 , pp. 789-797
    • Baran, E.J.1
  • 94
    • 0026076395 scopus 로고
    • The membrane-stabilizing action of zinc carnosine (Z-103) in stress-induced gastric ulceration in rats
    • C.H. Cho, C.T. Luk, and C.W. Ogle The membrane-stabilizing action of zinc carnosine (Z-103) in stress-induced gastric ulceration in rats Life Sci. 49 1991 PL189 PL194
    • (1991) Life Sci. , vol.49
    • Cho, C.H.1    Luk, C.T.2    Ogle, C.W.3
  • 95
    • 0026094240 scopus 로고
    • The antioxidant properties of a novel zinc-carnosine chelate compound, N-(3-aminopropionyl)-l-histidinato zinc
    • T. Yoshikawa, Y. Naito, T. Tanigawa, T. Yoneta, and M. Kondo The antioxidant properties of a novel zinc-carnosine chelate compound, N-(3-aminopropionyl)-l-histidinato zinc Biochim. Biophys. Acta 1115 1991 15 22
    • (1991) Biochim. Biophys. Acta , vol.1115 , pp. 15-22
    • Yoshikawa, T.1    Naito, Y.2    Tanigawa, T.3    Yoneta, T.4    Kondo, M.5
  • 97
    • 0034219226 scopus 로고    scopus 로고
    • Applicability of zinc complex of l-carnosine for medical use
    • T. Matsukura, and H. Tanaka Applicability of zinc complex of l-carnosine for medical use Biochemistry (Mosc.) 65 2000 817 823
    • (2000) Biochemistry (Mosc.) , vol.65 , pp. 817-823
    • Matsukura, T.1    Tanaka, H.2
  • 98
    • 0028172783 scopus 로고
    • L-carnosine (beta-alanyl-l-histidine) and carcinine (beta- alanylhistamine) act as natural antioxidants with hydroxyl-radical-scavenging and lipid-peroxidase activities
    • M.A. Babizhayev, M.C. Seguin, J. Gueyne, R.P. Evstigneeva, E.A. Ageyeva, and G.A. Zheltukhina l-carnosine (beta-alanyl-l-histidine) and carcinine (beta-alanylhistamine) act as natural antioxidants with hydroxyl-radical- scavenging and lipid-peroxidase activities Biochem. J. 304 1994 509 516
    • (1994) Biochem. J. , vol.304 , pp. 509-516
    • Babizhayev, M.A.1    Seguin, M.C.2    Gueyne, J.3    Evstigneeva, R.P.4    Ageyeva, E.A.5    Zheltukhina, G.A.6
  • 99
    • 0344158770 scopus 로고
    • Antioxidant activity of carnosine, homocarnosine, and anserine present in muscle and brain
    • R. Kohen, Y. Yamamoto, K.C. Cundy, and B.N. Ames Antioxidant activity of carnosine, homocarnosine, and anserine present in muscle and brain Proc. Natl. Acad. Sci. USA 85 1988 3175 3179
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 3175-3179
    • Kohen, R.1    Yamamoto, Y.2    Cundy, K.C.3    Ames, B.N.4
  • 100
    • 18744386952 scopus 로고    scopus 로고
    • Antioxidant properties of carnosine re-evaluated with oxidizing systems involving iron and copper ions
    • M. Mozdzan, J. Szemraj, J. Rysz, and D. Nowak Antioxidant properties of carnosine re-evaluated with oxidizing systems involving iron and copper ions Basic Clin. Pharmacol. Toxicol. 96 2005 352 360
    • (2005) Basic Clin. Pharmacol. Toxicol. , vol.96 , pp. 352-360
    • Mozdzan, M.1    Szemraj, J.2    Rysz, J.3    Nowak, D.4
  • 101
    • 0030934522 scopus 로고    scopus 로고
    • Quenching of singlet molecular oxygen by carnosine and related antioxidants. Monitoring 1270-nm phosphorescence in aqueous media
    • S. Egorov, E.G. Kurella, A.A. Boldyrev, and A.A. Krasnovsky Jr. Quenching of singlet molecular oxygen by carnosine and related antioxidants. Monitoring 1270-nm phosphorescence in aqueous media Biochem. Mol. Biol. Int. 41 1997 687 694
    • (1997) Biochem. Mol. Biol. Int. , vol.41 , pp. 687-694
    • Egorov, S.1    Kurella, E.G.2    Boldyrev, A.A.3    Krasnovsky, Jr.A.A.4
  • 102
    • 0025032997 scopus 로고
    • Scavenging of singlet molecular oxygen by imidazole compounds: High and sustained activities of carboxy terminal histidine dipeptides and exceptional activity of imidazole-4-acetic acid
    • P.E. Hartman, Z. Hartman, and K.T. Ault Scavenging of singlet molecular oxygen by imidazole compounds: high and sustained activities of carboxy terminal histidine dipeptides and exceptional activity of imidazole-4-acetic acid Photochem. Photobiol. 51 1990 59 66
    • (1990) Photochem. Photobiol. , vol.51 , pp. 59-66
    • Hartman, P.E.1    Hartman, Z.2    Ault, K.T.3
  • 103
    • 0032987671 scopus 로고    scopus 로고
    • Improved functional recovery of ischemic rat hearts due to singlet oxygen scavengers histidine and carnosine
    • J.W. Lee, H. Miyawaki, E.V. Bobst, J.D. Hester, M. Ashraf, and A.M. Bobst Improved functional recovery of ischemic rat hearts due to singlet oxygen scavengers histidine and carnosine J. Mol. Cell. Cardiol. 31 1999 113 121
    • (1999) J. Mol. Cell. Cardiol. , vol.31 , pp. 113-121
    • Lee, J.W.1    Miyawaki, H.2    Bobst, E.V.3    Hester, J.D.4    Ashraf, M.5    Bobst, A.M.6
  • 105
    • 0036366273 scopus 로고    scopus 로고
    • Effect of carnosine and related compounds on the inactivation of human Cu, Zn-superoxide dismutase by modification of fructose and glycolaldehyde
    • H. Ukeda, Y. Hasegawa, Y. Harada, and M. Sawamura Effect of carnosine and related compounds on the inactivation of human Cu, Zn-superoxide dismutase by modification of fructose and glycolaldehyde Biosci. Biotechnol. Biochem. 66 2002 36 43
    • (2002) Biosci. Biotechnol. Biochem. , vol.66 , pp. 36-43
    • Ukeda, H.1    Hasegawa, Y.2    Harada, Y.3    Sawamura, M.4
  • 106
    • 0031555339 scopus 로고    scopus 로고
    • Protective effects of carnosine against malondialdehyde-induced toxicity towards cultured rat brain endothelial cells
    • A.R. Hipkiss, J.E. Preston, D.T.M. Himswoth, V.C. Worthington, and N.J. Abbot Protective effects of carnosine against malondialdehyde-induced toxicity towards cultured rat brain endothelial cells Neurosci. Lett. 238 1997 135 138
    • (1997) Neurosci. Lett. , vol.238 , pp. 135-138
    • Hipkiss, A.R.1    Preston, J.E.2    Himswoth, D.T.M.3    Worthington, V.C.4    Abbot, N.J.5
  • 107
    • 0032499880 scopus 로고    scopus 로고
    • Carnosine protects proteins against methylglyoxal-mediated modifications
    • A.R. Hipkiss, and H. Chana Carnosine protects proteins against methylglyoxal-mediated modifications Biochem. Biophys. Res. Commun. 248 1998 28 32
    • (1998) Biochem. Biophys. Res. Commun. , vol.248 , pp. 28-32
    • Hipkiss, A.R.1    Chana, H.2
  • 108
    • 79956200130 scopus 로고    scopus 로고
    • Glycation of the muscle-specific enolase by reactive carbonyls: Effect of temperature and the protection role of carnosine pirydoxamine and phosphatidylserine
    • J. Pietkiewicz, A. Bronowicka-Szydelko, K. Dzierzba, R. Danielewicz, and A. Gamian Glycation of the muscle-specific enolase by reactive carbonyls: effect of temperature and the protection role of carnosine pirydoxamine and phosphatidylserine Protein J. 30 2011 149 158
    • (2011) Protein J. , vol.30 , pp. 149-158
    • Pietkiewicz, J.1    Bronowicka-Szydelko, A.2    Dzierzba, K.3    Danielewicz, R.4    Gamian, A.5
  • 109
    • 0345737136 scopus 로고    scopus 로고
    • Carnosine inhibits (E)-4-hydroxy-2-nonenal-induced protein cross-linking: Structural characterization of carnosine-HNE adducts
    • Y.H. Liu, G.Z. Xu, and L.M. Sayre Carnosine inhibits (E)-4-hydroxy-2- nonenal-induced protein cross-linking: structural characterization of carnosine-HNE adducts Chem. Res. Toxicol. 16 2003 1589 1597
    • (2003) Chem. Res. Toxicol. , vol.16 , pp. 1589-1597
    • Liu, Y.H.1    Xu, G.Z.2    Sayre, L.M.3
  • 110
    • 0034129716 scopus 로고    scopus 로고
    • The antihypertensive hydralazine is an efficient scavenger of acrolein
    • P.C. Burcham, P.G. Kerr, and F. Fontaine The antihypertensive hydralazine is an efficient scavenger of acrolein Redox Rep. 5 2000 47 49
    • (2000) Redox Rep. , vol.5 , pp. 47-49
    • Burcham, P.C.1    Kerr, P.G.2    Fontaine, F.3
  • 111
    • 67449086731 scopus 로고    scopus 로고
    • Covalent cross-linking of glutathione and carnosine to proteins by 4-oxo-2-nonenal
    • X. Zhu, M.M. Gallogly, J.J. Mieyal, V.E. Anderson, and L.M. Sayre Covalent cross-linking of glutathione and carnosine to proteins by 4-oxo-2-nonenal Chem. Res. Toxicol. 22 2009 1050 1059
    • (2009) Chem. Res. Toxicol. , vol.22 , pp. 1050-1059
    • Zhu, X.1    Gallogly, M.M.2    Mieyal, J.J.3    Anderson, V.E.4    Sayre, L.M.5
  • 112
    • 0032901632 scopus 로고    scopus 로고
    • Ability of carnosine and other skeletal muscle components to quench unsaturated aldehydic lipid oxidation products
    • S. Zhou, and E.A. Decker Ability of carnosine and other skeletal muscle components to quench unsaturated aldehydic lipid oxidation products J. Agric. Food Chem. 47 1999 51 55
    • (1999) J. Agric. Food Chem. , vol.47 , pp. 51-55
    • Zhou, S.1    Decker, E.A.2
  • 114
    • 0036931210 scopus 로고    scopus 로고
    • Detoxification of cytotoxic alpha, beta-unsaturated aldehydes by carnosine: Characterization of conjugated adducts by electrospray ionization tandem mass spectrometry and detection by liquid chromatography/mass spectrometry in rat skeletal muscle
    • G. Aldini, P. Granata, and M. Carini Detoxification of cytotoxic alpha, beta-unsaturated aldehydes by carnosine: characterization of conjugated adducts by electrospray ionization tandem mass spectrometry and detection by liquid chromatography/mass spectrometry in rat skeletal muscle J. Mass Spectrom. 37 2002 1219 1228
    • (2002) J. Mass Spectrom. , vol.37 , pp. 1219-1228
    • Aldini, G.1    Granata, P.2    Carini, M.3
  • 115
    • 0008999229 scopus 로고    scopus 로고
    • Carnosine inhibits (E)-4-hydroxy-2-nonenal-induced protein cross-linking: Structural characterization of carnosine-HNE adducts
    • Y.H. Liu, G.Z. Xu, and L.M. Sayre Carnosine inhibits (E)-4-hydroxy-2- nonenal-induced protein cross-linking: structural characterization of carnosine-HNE adducts Abstracts of Papers of the American Chemical Society 222 2001 U291
    • (2001) Abstracts of Papers of the American Chemical Society , vol.222 , pp. 291
    • Liu, Y.H.1    Xu, G.Z.2    Sayre, L.M.3
  • 116
    • 24944457313 scopus 로고    scopus 로고
    • Carnosine and carnosine-related antioxidants: A review
    • A. Guiotto, A. Calderan, P. Ruzza, and G. Borin Carnosine and carnosine-related antioxidants: a review Curr. Med. Chem. 12 2005 2293 2315
    • (2005) Curr. Med. Chem. , vol.12 , pp. 2293-2315
    • Guiotto, A.1    Calderan, A.2    Ruzza, P.3    Borin, G.4
  • 117
    • 67049097541 scopus 로고    scopus 로고
    • Design, synthesis, and evaluation of carnosine derivatives as selective and efficient sequestering agents of cytotoxic reactive carbonyl species
    • G. Vistoli, M. Orioli, A. Pedretti, L. Regazzoni, R. Canevotti, G. Negrisoli, M. Carini, and G. Aldini Design, synthesis, and evaluation of carnosine derivatives as selective and efficient sequestering agents of cytotoxic reactive carbonyl species ChemMedChem 4 2009 967 975
    • (2009) ChemMedChem , vol.4 , pp. 967-975
    • Vistoli, G.1    Orioli, M.2    Pedretti, A.3    Regazzoni, L.4    Canevotti, R.5    Negrisoli, G.6    Carini, M.7    Aldini, G.8
  • 118
    • 27644525132 scopus 로고    scopus 로고
    • LC-ESI-MS/MS determination of 4-hydroxy-trans-2-nonenal Michael adducts with cysteine and histidine-containing peptides as early markers of oxidative stress in excitable tissues
    • M. Orioli, G. Aldini, G. Beretta, R.M. Facino, and M. Carini LC-ESI-MS/MS determination of 4-hydroxy-trans-2-nonenal Michael adducts with cysteine and histidine-containing peptides as early markers of oxidative stress in excitable tissues J. Chromatogr. B Anal. Technol. Biomed. Life Sci. 827 2005 109 118
    • (2005) J. Chromatogr. B Anal. Technol. Biomed. Life Sci. , vol.827 , pp. 109-118
    • Orioli, M.1    Aldini, G.2    Beretta, G.3    Facino, R.M.4    Carini, M.5
  • 119
    • 36849089644 scopus 로고    scopus 로고
    • HNE Michael adducts to histidine and histidine-containing peptides as biomarkers of lipid-derived carbonyl stress in urines: LC-MS/MS profiling in Zucker obese rats
    • M. Orioli, G. Aldini, M.C. Benfatto, R.M. Facino, and M. Carini HNE Michael adducts to histidine and histidine-containing peptides as biomarkers of lipid-derived carbonyl stress in urines: LC-MS/MS profiling in Zucker obese rats Anal. Chem. 79 2007 9174 9184
    • (2007) Anal. Chem. , vol.79 , pp. 9174-9184
    • Orioli, M.1    Aldini, G.2    Benfatto, M.C.3    Facino, R.M.4    Carini, M.5
  • 121
    • 0141457973 scopus 로고    scopus 로고
    • Acrolein-sequestering ability of endogenous dipeptides: Characterization of carnosine and homocarnosine/acrolein adducts by electrospray ionization tandem mass spectrometry
    • M. Carini, G. Aldini, G. Beretta, E. Arlandini, and R.M. Facino Acrolein-sequestering ability of endogenous dipeptides: characterization of carnosine and homocarnosine/acrolein adducts by electrospray ionization tandem mass spectrometry J. Mass Spectrom. 38 2003 996 1006
    • (2003) J. Mass Spectrom. , vol.38 , pp. 996-1006
    • Carini, M.1    Aldini, G.2    Beretta, G.3    Arlandini, E.4    Facino, R.M.5
  • 122
    • 34548851693 scopus 로고    scopus 로고
    • Assay for quantitative determination of glutathione and glutathione disulfide levels using enzymatic recycling method
    • I. Rahman, A. Kode, and S.K. Biswas Assay for quantitative determination of glutathione and glutathione disulfide levels using enzymatic recycling method Nat. Protoc. 1 2006 3159 3165
    • (2006) Nat. Protoc. , vol.1 , pp. 3159-3165
    • Rahman, I.1    Kode, A.2    Biswas, S.K.3
  • 127
    • 0025198459 scopus 로고
    • The presence and significance of carnosine in histamine-containing tissues of several mammalian species
    • L. Flancbaum, J.C. Fitzpatrick, D.N. Brotman, A.M. Marcoux, E. Kasziba, and H. Fisher The presence and significance of carnosine in histamine-containing tissues of several mammalian species Agents Actions 31 1990 190 196
    • (1990) Agents Actions , vol.31 , pp. 190-196
    • Flancbaum, L.1    Fitzpatrick, J.C.2    Brotman, D.N.3    Marcoux, A.M.4    Kasziba, E.5    Fisher, H.6
  • 128
    • 33847050170 scopus 로고    scopus 로고
    • Neuroprotective effect of carnosine on necrotic cell death in PC12 cells
    • Y. Shen, Y. Fan, H. Dai, Q. Fu, W. Hu, and Z. Chen Neuroprotective effect of carnosine on necrotic cell death in PC12 cells Neurosci. Lett. 414 2007 145 149
    • (2007) Neurosci. Lett. , vol.414 , pp. 145-149
    • Shen, Y.1    Fan, Y.2    Dai, H.3    Fu, Q.4    Hu, W.5    Chen, Z.6
  • 129
    • 84862772594 scopus 로고    scopus 로고
    • Role of l-carnosine in the control of blood glucose, blood pressure, thermogenesis, and lipolysis by autonomic nerves in rats: Involvement of the circadian clock and histamine
    • K. Nagai, M. Tanida, A. Niijima, N. Tsuruoka, Y. Kiso, Y. Horii, J. Shen, and N. Okumura Role of l-carnosine in the control of blood glucose, blood pressure, thermogenesis, and lipolysis by autonomic nerves in rats: involvement of the circadian clock and histamine Amino Acids 43 2012 97 109
    • (2012) Amino Acids , vol.43 , pp. 97-109
    • Nagai, K.1    Tanida, M.2    Niijima, A.3    Tsuruoka, N.4    Kiso, Y.5    Horii, Y.6    Shen, J.7    Okumura, N.8
  • 131
    • 0022400478 scopus 로고
    • Effects of various compounds on histidine-decarboxylase activity-active-site mapping
    • Y. Sakamoto, T. Watanabe, H. Hayashi, Y. Taguchi, and H. Wada Effects of various compounds on histidine-decarboxylase activity-active-site mapping Agents Actions 17 1985 32 37
    • (1985) Agents Actions , vol.17 , pp. 32-37
    • Sakamoto, Y.1    Watanabe, T.2    Hayashi, H.3    Taguchi, Y.4    Wada, H.5
  • 132
    • 42949085348 scopus 로고    scopus 로고
    • Carnosine attenuates mast cell degranulation and histamine release induced by oxygen-glucose deprivation
    • Y. Shen, S.H. Zhang, L. Fu, W.W. Hu, and Z. Chen Carnosine attenuates mast cell degranulation and histamine release induced by oxygen-glucose deprivation Cell Biochem. Funct. 26 2008 334 338
    • (2008) Cell Biochem. Funct. , vol.26 , pp. 334-338
    • Shen, Y.1    Zhang, S.H.2    Fu, L.3    Hu, W.W.4    Chen, Z.5
  • 133
    • 0036879619 scopus 로고    scopus 로고
    • Double-blind, placebo-controlled study of l-carnosine supplementation in children with autistic spectrum disorders
    • M.G. Chez, C.P. Buchanan, M.C. Aimonovitch, M. Becker, K. Schaefer, C. Black, and J. Komen Double-blind, placebo-controlled study of l-carnosine supplementation in children with autistic spectrum disorders J. Child Neurol. 17 2002 833 837
    • (2002) J. Child Neurol. , vol.17 , pp. 833-837
    • Chez, M.G.1    Buchanan, C.P.2    Aimonovitch, M.C.3    Becker, M.4    Schaefer, K.5    Black, C.6    Komen, J.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.