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Volumn 55, Issue , 2011, Pages 81-103

Chemical Biology of Homocysteine Thiolactone and Related Metabolites

Author keywords

Homocysteine thiolactone; N Homocysteinylated protein; N Homocysteinyl lysine

Indexed keywords


EID: 80052665221     PISSN: 00652423     EISSN: None     Source Type: Book Series    
DOI: 10.1016/B978-0-12-387042-1.00005-8     Document Type: Chapter
Times cited : (63)

References (92)
  • 1
    • 0001517759 scopus 로고
    • The formation of homologue of cysteine by the decomposition of methionine with sulfuric acid
    • Butz L.W., du Vigneaud V. The formation of homologue of cysteine by the decomposition of methionine with sulfuric acid. J. Biol. Chem. 1932, 99:135-142.
    • (1932) J. Biol. Chem. , vol.99 , pp. 135-142
    • Butz, L.W.1    du Vigneaud, V.2
  • 2
    • 0001607609 scopus 로고
    • A modification of the method for determining methionine in proteins
    • Baernstein H.D. A modification of the method for determining methionine in proteins. J. Biol. Chem. 1934, 106:451-456.
    • (1934) J. Biol. Chem. , vol.106 , pp. 451-456
    • Baernstein, H.D.1
  • 3
    • 0033818441 scopus 로고    scopus 로고
    • Pathways and regulation of homocysteine metabolism in mammals
    • Finkelstein J.D. Pathways and regulation of homocysteine metabolism in mammals. Semin. Thromb. Hemost. 2000, 26:219-225.
    • (2000) Semin. Thromb. Hemost. , vol.26 , pp. 219-225
    • Finkelstein, J.D.1
  • 4
    • 0027534543 scopus 로고
    • Synthesis of homocysteine thiolactone by methionyl-tRNA synthetase in cultured mammalian cells
    • Jakubowski H., Goldman E. Synthesis of homocysteine thiolactone by methionyl-tRNA synthetase in cultured mammalian cells. FEBS Lett. 1993, 317:593-598.
    • (1993) FEBS Lett. , vol.317 , pp. 593-598
    • Jakubowski, H.1    Goldman, E.2
  • 5
    • 0034617073 scopus 로고    scopus 로고
    • Homocysteine thiolactone and protein homocysteinylation in human endothelial cells: implications for atherosclerosis
    • Jakubowski H., Zhang L., Bardeguez A., Aviv A. Homocysteine thiolactone and protein homocysteinylation in human endothelial cells: implications for atherosclerosis. Circ. Res. 2000, 87:45-51.
    • (2000) Circ. Res. , vol.87 , pp. 45-51
    • Jakubowski, H.1    Zhang, L.2    Bardeguez, A.3    Aviv, A.4
  • 6
    • 0031035742 scopus 로고    scopus 로고
    • Metabolism of homocysteine thiolactone in human cell cultures: possible mechanism for pathological consequences of elevated homocysteine levels
    • Jakubowski H. Metabolism of homocysteine thiolactone in human cell cultures: possible mechanism for pathological consequences of elevated homocysteine levels. J. Biol. Chem. 1997, 272:1935-1942.
    • (1997) J. Biol. Chem. , vol.272 , pp. 1935-1942
    • Jakubowski, H.1
  • 7
    • 0032778517 scopus 로고    scopus 로고
    • Protein homocysteinylation: possible mechanism underlying pathological consequences of elevated homocysteine levels
    • Jakubowski H. Protein homocysteinylation: possible mechanism underlying pathological consequences of elevated homocysteine levels. FASEB J. 1999, 13:2277-2283.
    • (1999) FASEB J. , vol.13 , pp. 2277-2283
    • Jakubowski, H.1
  • 8
    • 57349180605 scopus 로고    scopus 로고
    • Mutations in cystathionine beta-synthase or methylenetetrahydrofolate reductase gene increase N-homocysteinylated protein levels in humans
    • Jakubowski H., Boers G.H., Strauss K.A. Mutations in cystathionine beta-synthase or methylenetetrahydrofolate reductase gene increase N-homocysteinylated protein levels in humans. FASEB J. 2008, 22:4071-4076.
    • (2008) FASEB J. , vol.22 , pp. 4071-4076
    • Jakubowski, H.1    Boers, G.H.2    Strauss, K.A.3
  • 9
    • 78449301117 scopus 로고    scopus 로고
    • Identification and origin of Nε-homocysteinyllysine isopeptide in humans and mice
    • Glowacki R., Bald E., Jakubowski H. Identification and origin of Nε-homocysteinyllysine isopeptide in humans and mice. Amino Acids 2010, 39:1563-1569.
    • (2010) Amino Acids , vol.39 , pp. 1563-1569
    • Glowacki, R.1    Bald, E.2    Jakubowski, H.3
  • 10
    • 79954538856 scopus 로고    scopus 로고
    • Elevated levels of N-Hcy-Lysine isopeptide in acute myocardial infarction: links with ADMA formation
    • Za{ogonek}bczyk M., Glowacki R., Machnik A., et al. Elevated levels of N-Hcy-Lysine isopeptide in acute myocardial infarction: links with ADMA formation. Clin. Chem. Lab. Med. 2010, 49:729-735.
    • (2010) Clin. Chem. Lab. Med. , vol.49 , pp. 729-735
    • Zabczyk, M.1    Glowacki, R.2    Machnik, A.3
  • 11
    • 0035513846 scopus 로고    scopus 로고
    • Translational accuracy of aminoacyl-tRNA synthetases: implications for atherosclerosis
    • Jakubowski H. Translational accuracy of aminoacyl-tRNA synthetases: implications for atherosclerosis. J. Nutr. 2001, 131:2983S-2987S.
    • (2001) J. Nutr. , vol.131
    • Jakubowski, H.1
  • 12
    • 0034698140 scopus 로고    scopus 로고
    • Translational incorporation of S-nitroso-homocysteine into protein
    • Jakubowski H. Translational incorporation of S-nitroso-homocysteine into protein. J. Biol. Chem. 2000, 275:21813-21816.
    • (2000) J. Biol. Chem. , vol.275 , pp. 21813-21816
    • Jakubowski, H.1
  • 13
    • 0000167774 scopus 로고    scopus 로고
    • Disorders of transsulfuration
    • McGraw-Hill, New York, C. Scriver, A.L. Beaudet, W.S. Sly, D. Valle (Eds.)
    • Mudd S.H., Levy H.L., Kraus J.P. Disorders of transsulfuration. The metbolic & molecular bases of inherited disease 2001, 2007-2056. McGraw-Hill, New York, vol. II. eighth ed. C. Scriver, A.L. Beaudet, W.S. Sly, D. Valle (Eds.).
    • (2001) The metbolic & molecular bases of inherited disease , vol.2 , pp. 2007-2056
    • Mudd, S.H.1    Levy, H.L.2    Kraus, J.P.3
  • 15
    • 28344446460 scopus 로고    scopus 로고
    • Mechanisms of homocysteine-induced atherothrombosis
    • Lentz S.R. Mechanisms of homocysteine-induced atherothrombosis. J. Thromb. Haemost. 2005, 3:1646-1654.
    • (2005) J. Thromb. Haemost. , vol.3 , pp. 1646-1654
    • Lentz, S.R.1
  • 16
    • 77958567930 scopus 로고    scopus 로고
    • Homocysteine-lowering by B vitamins slows the rate of accelerated brain atrophy in mild cognitive impairment: a randomized controlled trial
    • Smith A.D., Smith S.M., de Jager C.A., et al. Homocysteine-lowering by B vitamins slows the rate of accelerated brain atrophy in mild cognitive impairment: a randomized controlled trial. PLoS ONE 2010, 5(1-10):e12244. 10.1371/journal.pone.0012244.
    • (2010) PLoS ONE , vol.5 , Issue.1-10
    • Smith, A.D.1    Smith, S.M.2    de Jager, C.A.3
  • 18
    • 3242792577 scopus 로고    scopus 로고
    • Homocysteine and folate in pregnancy
    • Ueland P.M., Vollset S.E. Homocysteine and folate in pregnancy. Clin. Chem. 2004, 50:1293-1295.
    • (2004) Clin. Chem. , vol.50 , pp. 1293-1295
    • Ueland, P.M.1    Vollset, S.E.2
  • 19
    • 20244379275 scopus 로고    scopus 로고
    • Homocysteine triggers mucosal microvascular activation in inflammatory bowel disease
    • Danese S., Sgambato A., Papa A., et al. Homocysteine triggers mucosal microvascular activation in inflammatory bowel disease. Am. J. Gastroenterol. 2005, 100:886-895.
    • (2005) Am. J. Gastroenterol. , vol.100 , pp. 886-895
    • Danese, S.1    Sgambato, A.2    Papa, A.3
  • 21
    • 3142735995 scopus 로고    scopus 로고
    • Hyperhomocysteinemia, endoplasmic reticulum stress, and alcoholic liver injury
    • Ji C., Kaplowitz N. Hyperhomocysteinemia, endoplasmic reticulum stress, and alcoholic liver injury. World J. Gastroenterol. 2004, 10:1699-1708.
    • (2004) World J. Gastroenterol. , vol.10 , pp. 1699-1708
    • Ji, C.1    Kaplowitz, N.2
  • 22
    • 1542373560 scopus 로고    scopus 로고
    • Molecular basis of homocysteine toxicity in humans
    • Jakubowski H. Molecular basis of homocysteine toxicity in humans. Cell. Mol. Life Sci. 2004, 61:470-487.
    • (2004) Cell. Mol. Life Sci. , vol.61 , pp. 470-487
    • Jakubowski, H.1
  • 23
    • 27744574426 scopus 로고    scopus 로고
    • Anti-N-homocysteinylated protein autoantibodies and cardiovascular disease
    • Jakubowski H. Anti-N-homocysteinylated protein autoantibodies and cardiovascular disease. Clin. Chem. Lab. Med. 2005, 43:1011-1014.
    • (2005) Clin. Chem. Lab. Med. , vol.43 , pp. 1011-1014
    • Jakubowski, H.1
  • 24
    • 33646788784 scopus 로고    scopus 로고
    • Pathophysiological consequences of homocysteine excess
    • Jakubowski H. Pathophysiological consequences of homocysteine excess. J. Nutr. 2006, 136:1741S-1749S.
    • (2006) J. Nutr. , vol.136
    • Jakubowski, H.1
  • 25
    • 36848998882 scopus 로고    scopus 로고
    • The molecular basis of homocysteine thiolactone-mediated vascular disease
    • Jakubowski H. The molecular basis of homocysteine thiolactone-mediated vascular disease. Clin. Chem. Lab. Med. 2007, 45:1704-1716.
    • (2007) Clin. Chem. Lab. Med. , vol.45 , pp. 1704-1716
    • Jakubowski, H.1
  • 26
    • 64049095638 scopus 로고    scopus 로고
    • The pathophysiological hypothesis of homocysteine thiolactone-mediated vascular disease
    • Jakubowski H. The pathophysiological hypothesis of homocysteine thiolactone-mediated vascular disease. J. Physiol. Pharmacol. 2008, 59:155-167.
    • (2008) J. Physiol. Pharmacol. , vol.59 , pp. 155-167
    • Jakubowski, H.1
  • 27
    • 0033981289 scopus 로고    scopus 로고
    • Homocysteine thiolactone: metabolic origin and protein homocysteinylation in humans
    • Jakubowski H. Homocysteine thiolactone: metabolic origin and protein homocysteinylation in humans. J. Nutr. 2000, 130:377S-381S.
    • (2000) J. Nutr. , vol.130
    • Jakubowski, H.1
  • 28
    • 0034802174 scopus 로고    scopus 로고
    • Protein N-homocysteinylation: implications for atherosclerosis
    • Jakubowski H. Protein N-homocysteinylation: implications for atherosclerosis. Biomed. Pharmacother. 2001, 55:443-447.
    • (2001) Biomed. Pharmacother. , vol.55 , pp. 443-447
    • Jakubowski, H.1
  • 29
    • 36849023284 scopus 로고    scopus 로고
    • TRNA synthetase editing of amino acids
    • John Wiley & Sons, Chichester
    • Jakubowski H. tRNA synthetase editing of amino acids. Encyclopedia of Life Sciences 2005, John Wiley & Sons, Chichester. 10.1038/npg.els.0003933.
    • (2005) Encyclopedia of Life Sciences
    • Jakubowski, H.1
  • 30
    • 0000954081 scopus 로고    scopus 로고
    • Biosynthesis and reactions of homocysteine thiolactone
    • Cambridge University Press, Cambridge, D.W. Jacobson, R. Carmel (Eds.)
    • Jakubowski H. Biosynthesis and reactions of homocysteine thiolactone. Homocysteine in Health and Disease 2001, 21-31. Cambridge University Press, Cambridge. D.W. Jacobson, R. Carmel (Eds.).
    • (2001) Homocysteine in Health and Disease , pp. 21-31
    • Jakubowski, H.1
  • 31
    • 80052676715 scopus 로고    scopus 로고
    • The aminoacyl-tRNA synthetases, Landes Bioscience/Eureka.com, Georgetown, TX, M. Ibba, C. Francklyn, S. Cusack (Eds.)
    • Jakubowski H. Accuracy of aminoacyl-tRNA synthetases: proofreading of amino acids 2005, 21-31. The aminoacyl-tRNA synthetases, Landes Bioscience/Eureka.com, Georgetown, TX. M. Ibba, C. Francklyn, S. Cusack (Eds.).
    • (2005) Accuracy of aminoacyl-tRNA synthetases: proofreading of amino acids , pp. 21-31
    • Jakubowski, H.1
  • 32
    • 0034635449 scopus 로고    scopus 로고
    • Calcium-dependent human serum homocysteine thiolactone hydrolase: a protective mechanism against protein-N-homocysteinylation
    • Jakubowski H. Calcium-dependent human serum homocysteine thiolactone hydrolase: a protective mechanism against protein-N-homocysteinylation. J. Biol. Chem. 2000, 275:3957-3962.
    • (2000) J. Biol. Chem. , vol.275 , pp. 3957-3962
    • Jakubowski, H.1
  • 33
    • 0035936847 scopus 로고    scopus 로고
    • Genetic determinants of homocysteine thiolactonase activity in humans: implications for atherosclerosis
    • Jakubowski H., Ambrosius W., Pratt J.H. Genetic determinants of homocysteine thiolactonase activity in humans: implications for atherosclerosis. FEBS Lett. 2001, 491:35-39.
    • (2001) FEBS Lett. , vol.491 , pp. 35-39
    • Jakubowski, H.1    Ambrosius, W.2    Pratt, J.H.3
  • 34
    • 0035800663 scopus 로고    scopus 로고
    • Yeast cytoplasmic and mitochondrial methionyl-tRNA synthetases: two structural frameworks for identical functions
    • Despons L., Senger B., Jakubowski H., Fasiolo F. Yeast cytoplasmic and mitochondrial methionyl-tRNA synthetases: two structural frameworks for identical functions. J. Mol. Biol. 2001, 311:205-216.
    • (2001) J. Mol. Biol. , vol.311 , pp. 205-216
    • Despons, L.1    Senger, B.2    Jakubowski, H.3    Fasiolo, F.4
  • 35
    • 2442641844 scopus 로고    scopus 로고
    • Cross-talk between Cys34 and lysine residues in human serum albumin revealed by N-homocysteinylation
    • Glowacki R., Jakubowski H. Cross-talk between Cys34 and lysine residues in human serum albumin revealed by N-homocysteinylation. J. Biol. Chem. 2004, 279:10864-10871.
    • (2004) J. Biol. Chem. , vol.279 , pp. 10864-10871
    • Glowacki, R.1    Jakubowski, H.2
  • 36
    • 33747355994 scopus 로고    scopus 로고
    • Protective mechanisms against homocysteine toxicity: the role of bleomycin hydrolase
    • Zimny J., Sikora M., Guranowski A., Jakubowski H. Protective mechanisms against homocysteine toxicity: the role of bleomycin hydrolase. J. Biol. Chem. 2006, 281:22485-22492.
    • (2006) J. Biol. Chem. , vol.281 , pp. 22485-22492
    • Zimny, J.1    Sikora, M.2    Guranowski, A.3    Jakubowski, H.4
  • 37
    • 34548624195 scopus 로고    scopus 로고
    • Facile syntheses of [35S] homocysteine-thiolactone, [35S] homocysteine, [35S] homocysteine, and [S-nitroso-35S] homocysteine
    • Jakubowski H. Facile syntheses of [35S] homocysteine-thiolactone, [35S] homocysteine, [35S] homocysteine, and [S-nitroso-35S] homocysteine. Anal. Biochem. 2007, 370:124-126.
    • (2007) Anal. Biochem. , vol.370 , pp. 124-126
    • Jakubowski, H.1
  • 38
    • 0000283376 scopus 로고
    • The isolation of homocysteine and its conversion to a thiolactone
    • Riegel B., du Vigneaud V. The isolation of homocysteine and its conversion to a thiolactone. J. Biol. Chem. 1935, 112:149-154.
    • (1935) J. Biol. Chem. , vol.112 , pp. 149-154
    • Riegel, B.1    du Vigneaud, V.2
  • 39
    • 0036750807 scopus 로고    scopus 로고
    • The determination of homocysteine thiolactone in biological samples
    • Jakubowski H. The determination of homocysteine thiolactone in biological samples. Anal. Biochem. 2002, 308:112-119.
    • (2002) Anal. Biochem. , vol.308 , pp. 112-119
    • Jakubowski, H.1
  • 40
    • 13244287981 scopus 로고    scopus 로고
    • The determination of homocysteine-thiolactone in human plasma
    • Chwatko G., Jakubowski H. The determination of homocysteine-thiolactone in human plasma. Anal. Biochem. 2005, 337:271-277.
    • (2005) Anal. Biochem. , vol.337 , pp. 271-277
    • Chwatko, G.1    Jakubowski, H.2
  • 41
    • 0025806820 scopus 로고
    • Homocysteine thiolactone disposal by human arterial endothelial cells and serum in vitro
    • Dudman N.P., Hicks C., Lynch J.F., Wilcken D.E., Wang J. Homocysteine thiolactone disposal by human arterial endothelial cells and serum in vitro. Arterioscler. Thromb. 1991, 11:663-670.
    • (1991) Arterioscler. Thromb. , vol.11 , pp. 663-670
    • Dudman, N.P.1    Hicks, C.2    Lynch, J.F.3    Wilcken, D.E.4    Wang, J.5
  • 42
    • 0032515953 scopus 로고    scopus 로고
    • Aminoacylation of coenzyme A and pantetheine by aminoacyl-tRNA synthetases: possible link between non-coded and coded peptide synthesis
    • Jakubowski H. Aminoacylation of coenzyme A and pantetheine by aminoacyl-tRNA synthetases: possible link between non-coded and coded peptide synthesis. Biochemistry 1998, 37:5147-5153.
    • (1998) Biochemistry , vol.37 , pp. 5147-5153
    • Jakubowski, H.1
  • 43
    • 0013040537 scopus 로고
    • Opening the ring of the thiolactone of homocysteine
    • du Vigneaud V., Patterson W.I., Hunt M. Opening the ring of the thiolactone of homocysteine. J. Biol. Chem. 1938, 126:217-231.
    • (1938) J. Biol. Chem. , vol.126 , pp. 217-231
    • du Vigneaud, V.1    Patterson, W.I.2    Hunt, M.3
  • 44
    • 0013969948 scopus 로고
    • Preparation of L-homocysteine from L-homocysteine thiolactone
    • Duerre J., Miller C.H. Preparation of L-homocysteine from L-homocysteine thiolactone. Anal. Biochem. 1966, 17:310-315.
    • (1966) Anal. Biochem. , vol.17 , pp. 310-315
    • Duerre, J.1    Miller, C.H.2
  • 45
    • 0344948718 scopus 로고
    • Metabolism of thiolesters of glutathione
    • Racker E. Metabolism of thiolesters of glutathione. Fed. Proc. 1953, 12:711-715.
    • (1953) Fed. Proc. , vol.12 , pp. 711-715
    • Racker, E.1
  • 46
    • 0027973762 scopus 로고
    • Role of carboxy terminal region in proofreading function of methionyl-tRNA synthetase in Escherichia coli
    • Gao W., Goldman E., Jakubowski H. Role of carboxy terminal region in proofreading function of methionyl-tRNA synthetase in Escherichia coli. Biochemistry 1994, 33:11528-11535.
    • (1994) Biochemistry , vol.33 , pp. 11528-11535
    • Gao, W.1    Goldman, E.2    Jakubowski, H.3
  • 47
    • 0029078593 scopus 로고
    • Proofreading in vivo: editing of homocysteine by aminoacyl-tRNA synthetases in Escherichia coli
    • Jakubowski H. Proofreading in vivo: editing of homocysteine by aminoacyl-tRNA synthetases in Escherichia coli. J. Biol. Chem. 1995, 270:17672-17673.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17672-17673
    • Jakubowski, H.1
  • 48
    • 0037470248 scopus 로고    scopus 로고
    • Metabolism of homocysteine-thiolactone in plants
    • Jakubowski H., Guranowski A. Metabolism of homocysteine-thiolactone in plants. J. Biol. Chem. 2003, 278:6765-6770.
    • (2003) J. Biol. Chem. , vol.278 , pp. 6765-6770
    • Jakubowski, H.1    Guranowski, A.2
  • 49
    • 33750550442 scopus 로고    scopus 로고
    • Mechanism of the condensation of homocysteine thiolactone with aldehydes
    • Jakubowski H. Mechanism of the condensation of homocysteine thiolactone with aldehydes. Chem. Eur. J. 2006, 12:8039-8043.
    • (2006) Chem. Eur. J. , vol.12 , pp. 8039-8043
    • Jakubowski, H.1
  • 50
    • 0025974977 scopus 로고
    • Proofreading in vivo: editing of homocysteine by methionyl-tRNA synthetase in the yeast Saccharomyces cerevisiae
    • Jakubowski H. Proofreading in vivo: editing of homocysteine by methionyl-tRNA synthetase in the yeast Saccharomyces cerevisiae. EMBO J. 1991, 10:593-598.
    • (1991) EMBO J. , vol.10 , pp. 593-598
    • Jakubowski, H.1
  • 51
    • 0025371584 scopus 로고
    • Proofreading in vivo: editing of homocysteine by methionyl-tRNA synthetase in Escherichia coli
    • Jakubowski H. Proofreading in vivo: editing of homocysteine by methionyl-tRNA synthetase in Escherichia coli. PNAS 1990, 87:4504-4508.
    • (1990) PNAS , vol.87 , pp. 4504-4508
    • Jakubowski, H.1
  • 52
    • 67650762757 scopus 로고    scopus 로고
    • Homocysteine editing and growth inhibition in Escherichia coli
    • Sikora M., Jakubowski H. Homocysteine editing and growth inhibition in Escherichia coli. Microbiology 2009, 155:1858-1865.
    • (2009) Microbiology , vol.155 , pp. 1858-1865
    • Sikora, M.1    Jakubowski, H.2
  • 53
    • 0031043135 scopus 로고    scopus 로고
    • The internal thioester and the covalent binding properties of the complement proteins C3 and C4
    • Law S.K., Dodds A.W. The internal thioester and the covalent binding properties of the complement proteins C3 and C4. Protein Sci. 1997, 6:263-274.
    • (1997) Protein Sci. , vol.6 , pp. 263-274
    • Law, S.K.1    Dodds, A.W.2
  • 54
    • 0029838842 scopus 로고    scopus 로고
    • The mechanism of protein splicing and its modulation by mutation
    • Xu M.Q., Perler F.B. The mechanism of protein splicing and its modulation by mutation. EMBO J. 1996, 15:5146-5153.
    • (1996) EMBO J. , vol.15 , pp. 5146-5153
    • Xu, M.Q.1    Perler, F.B.2
  • 55
    • 0029844192 scopus 로고    scopus 로고
    • Cholesterol modification of hedgehog signaling proteins in animal development
    • Porter J.A., Young K.E., Beachy P.A. Cholesterol modification of hedgehog signaling proteins in animal development. Science 1996, 274:255-259.
    • (1996) Science , vol.274 , pp. 255-259
    • Porter, J.A.1    Young, K.E.2    Beachy, P.A.3
  • 56
    • 0036165216 scopus 로고    scopus 로고
    • Determination of homocysteine thiolactone and homocysteine in cell cultures using high-performance liquid chromatography with fluorescence detection
    • Mukai Y., Togawa T., Suzuki T., Ohata K., Tanabe S. Determination of homocysteine thiolactone and homocysteine in cell cultures using high-performance liquid chromatography with fluorescence detection. J. Chromatogr. B 2002, 767:263-268.
    • (2002) J. Chromatogr. B , vol.767 , pp. 263-268
    • Mukai, Y.1    Togawa, T.2    Suzuki, T.3    Ohata, K.4    Tanabe, S.5
  • 57
    • 12944309749 scopus 로고    scopus 로고
    • Urinary excretion of homocysteine-thiolactone in humans
    • Chwatko G., Jakubowski H. Urinary excretion of homocysteine-thiolactone in humans. Clin. Chem. 2005, 51:408-415.
    • (2005) Clin. Chem. , vol.51 , pp. 408-415
    • Chwatko, G.1    Jakubowski, H.2
  • 58
    • 0037277037 scopus 로고    scopus 로고
    • Quantitative assay of plasma homocysteine thiolactone by gas chromatography/mass spectrometry
    • Deneshvar P., Yazdanpanah M., Cuthbert C., Cole D.E.C. Quantitative assay of plasma homocysteine thiolactone by gas chromatography/mass spectrometry. Rapid Commun. Mass Spectrom. 2003, 17:358-362.
    • (2003) Rapid Commun. Mass Spectrom. , vol.17 , pp. 358-362
    • Deneshvar, P.1    Yazdanpanah, M.2    Cuthbert, C.3    Cole, D.E.C.4
  • 59
    • 79960396482 scopus 로고    scopus 로고
    • An on-column derivatization method for the determination of homocysteine-thiolactone and protein N-linked homocysteine
    • Glowacki R., Bald E., Jakubowski H. An on-column derivatization method for the determination of homocysteine-thiolactone and protein N-linked homocysteine. Amino Acids. 2010, 41:187-194.
    • (2010) Amino Acids. , vol.41 , pp. 187-194
    • Glowacki, R.1    Bald, E.2    Jakubowski, H.3
  • 60
    • 0019877050 scopus 로고
    • Alternative pathways for editing non-cognate amino acids by aminoacyl-tRNA synthetases
    • Jakubowski H., Fersht A.R. Alternative pathways for editing non-cognate amino acids by aminoacyl-tRNA synthetases. Nucleic Acids Res. 1981, 9:3105-3117.
    • (1981) Nucleic Acids Res. , vol.9 , pp. 3105-3117
    • Jakubowski, H.1    Fersht, A.R.2
  • 61
    • 0030885191 scopus 로고    scopus 로고
    • Aminoacyl thioester chemistry of class II aminoacyl-tRNA synthetases
    • Jakubowski H. Aminoacyl thioester chemistry of class II aminoacyl-tRNA synthetases. Biochemistry 1997, 36:11077-11085.
    • (1997) Biochemistry , vol.36 , pp. 11077-11085
    • Jakubowski, H.1
  • 62
    • 34249775796 scopus 로고    scopus 로고
    • Mutations in methylenetetrahydrofolate reductase or cystathionine beta-synthase gene, or a high-methionine diet, increase homocysteine thiolactone levels in humans and mice
    • Chwatko G., Boers G.H., Strauss K.A., Shih D.M., Jakubowski H. Mutations in methylenetetrahydrofolate reductase or cystathionine beta-synthase gene, or a high-methionine diet, increase homocysteine thiolactone levels in humans and mice. FASEB J. 2007, 21:1707-1713.
    • (2007) FASEB J. , vol.21 , pp. 1707-1713
    • Chwatko, G.1    Boers, G.H.2    Strauss, K.A.3    Shih, D.M.4    Jakubowski, H.5
  • 63
    • 77952294286 scopus 로고    scopus 로고
    • Paraoxonase 1 protects against protein N-homocysteinylation in humans
    • Perła-Kajan J., Jakubowski H. Paraoxonase 1 protects against protein N-homocysteinylation in humans. FASEB J. 2010, 24:931-936.
    • (2010) FASEB J. , vol.24 , pp. 931-936
    • Perła-Kajan, J.1    Jakubowski, H.2
  • 65
    • 67649371083 scopus 로고    scopus 로고
    • Genetic or nutritional disorders in homocysteine or folate metabolism increase protein N-homocysteinylation in mice
    • Jakubowski H., Perla-Kajan J., Finnell R.H., et al. Genetic or nutritional disorders in homocysteine or folate metabolism increase protein N-homocysteinylation in mice. FASEB J. 2009, 23:1721-1727.
    • (2009) FASEB J. , vol.23 , pp. 1721-1727
    • Jakubowski, H.1    Perla-Kajan, J.2    Finnell, R.H.3
  • 66
    • 58149352709 scopus 로고    scopus 로고
    • Plasma homocysteine thiolactone associated with risk of macrovasculopathy in Chinese patients with type 2 diabetes mellitus
    • Gu W., Lu J., Yang G., et al. Plasma homocysteine thiolactone associated with risk of macrovasculopathy in Chinese patients with type 2 diabetes mellitus. Adv. Ther. 2008, 25:914-924.
    • (2008) Adv. Ther. , vol.25 , pp. 914-924
    • Gu, W.1    Lu, J.2    Yang, G.3
  • 67
    • 77955094846 scopus 로고    scopus 로고
    • Direct monitoring of albumin lysine-525 N-homocysteinylation in human serum by liquid chromatography/mass spectrometry
    • Sikora M., Marczak Ł., Twardowski T., Stobiecki M., Jakubowski H. Direct monitoring of albumin lysine-525 N-homocysteinylation in human serum by liquid chromatography/mass spectrometry. Anal. Biochem. 2010, 405:132-134.
    • (2010) Anal. Biochem. , vol.405 , pp. 132-134
    • Sikora, M.1    Marczak, Ł.2    Twardowski, T.3    Stobiecki, M.4    Jakubowski, H.5
  • 68
    • 33644553466 scopus 로고    scopus 로고
    • Modification of fibrinogen by homocysteine thiolactone increases resistance to fibrinolysis: a potential mechanism of the thrombotic tendency in hyperhomocysteinemia
    • Sauls D.L., Lockhart E., Warren M.E., Lenkowski A., Wilhelm S.E., Hoffman M. Modification of fibrinogen by homocysteine thiolactone increases resistance to fibrinolysis: a potential mechanism of the thrombotic tendency in hyperhomocysteinemia. Biochemistry 2006, 45:2480-2487.
    • (2006) Biochemistry , vol.45 , pp. 2480-2487
    • Sauls, D.L.1    Lockhart, E.2    Warren, M.E.3    Lenkowski, A.4    Wilhelm, S.E.5    Hoffman, M.6
  • 69
    • 70350645116 scopus 로고    scopus 로고
    • Chemical methods for the detection of protein N-homocysteinylation via selective reactions with aldehydes
    • Zang T., Dai S., Chen D., Lee B.W.K., Liu S., Karger B.L., et al. Chemical methods for the detection of protein N-homocysteinylation via selective reactions with aldehydes. Anal. Chem. 2009, 81:9065-9071.
    • (2009) Anal. Chem. , vol.81 , pp. 9065-9071
    • Zang, T.1    Dai, S.2    Chen, D.3    Lee, B.W.K.4    Liu, S.5    Karger, B.L.6
  • 71
  • 72
    • 74149091653 scopus 로고    scopus 로고
    • Effect of homocysteinylation on high density lipoprotein physico-chemical properties
    • Ferretti G., Bacchetti T., Masciangelob S., Bicchiega V. Effect of homocysteinylation on high density lipoprotein physico-chemical properties. Chem. Phys. Lipids 2010, 163:228-235.
    • (2010) Chem. Phys. Lipids , vol.163 , pp. 228-235
    • Ferretti, G.1    Bacchetti, T.2    Masciangelob, S.3    Bicchiega, V.4
  • 73
    • 77954357800 scopus 로고    scopus 로고
    • Protein N-homocysteinylation induces the formation of toxic amyloid-like protofibrils
    • Paoli P., Sbrana F., Tiribilli B., et al. Protein N-homocysteinylation induces the formation of toxic amyloid-like protofibrils. J. Mol. Biol. 2010, 400:889-907.
    • (2010) J. Mol. Biol. , vol.400 , pp. 889-907
    • Paoli, P.1    Sbrana, F.2    Tiribilli, B.3
  • 74
    • 0031831270 scopus 로고    scopus 로고
    • Reactive oxygen-mediated protein oxidation in aging and disease
    • Stadtman E.R., Berlett B.S. Reactive oxygen-mediated protein oxidation in aging and disease. Drug Metab. Rev. 1998, 30:225-243.
    • (1998) Drug Metab. Rev. , vol.30 , pp. 225-243
    • Stadtman, E.R.1    Berlett, B.S.2
  • 75
    • 0026795635 scopus 로고
    • Protein oxidation and aging
    • Stadtman E.R. Protein oxidation and aging. Science 1992, 257:1220-1224.
    • (1992) Science , vol.257 , pp. 1220-1224
    • Stadtman, E.R.1
  • 76
    • 0034890121 scopus 로고    scopus 로고
    • Aging and oxidation of reactive protein sulfhydryls
    • Thomas J.A., Mallis R.J. Aging and oxidation of reactive protein sulfhydryls. Exp. Gerontol. 2001, 36:1519-1526.
    • (2001) Exp. Gerontol. , vol.36 , pp. 1519-1526
    • Thomas, J.A.1    Mallis, R.J.2
  • 77
    • 0025790342 scopus 로고
    • Excess brain protein oxidation and enzyme dysfunction in normal aging and in Alzheimer disease
    • Smith C.D., Carney J.M., Starke-Reed P.E., et al. Excess brain protein oxidation and enzyme dysfunction in normal aging and in Alzheimer disease. PNAS 1991, 88:10540-10543.
    • (1991) PNAS , vol.88 , pp. 10540-10543
    • Smith, C.D.1    Carney, J.M.2    Starke-Reed, P.E.3
  • 79
    • 0028347834 scopus 로고
    • Oxidation of proteins in neonatal lungs
    • Gladstone I.M., Levine R.L. Oxidation of proteins in neonatal lungs. Pediatrics 1994, 93:764-768.
    • (1994) Pediatrics , vol.93 , pp. 764-768
    • Gladstone, I.M.1    Levine, R.L.2
  • 80
    • 0030841350 scopus 로고    scopus 로고
    • Protein oxidation in aging, disease, and oxidative stress
    • Berlett B.S., Stadtman E.R. Protein oxidation in aging, disease, and oxidative stress. J. Biol. Chem. 1997, 272:20313-20316.
    • (1997) J. Biol. Chem. , vol.272 , pp. 20313-20316
    • Berlett, B.S.1    Stadtman, E.R.2
  • 81
    • 0037163003 scopus 로고    scopus 로고
    • Homocysteine is a protein amino acid in humans: implications for homocysteine-linked disease
    • Jakubowski H. Homocysteine is a protein amino acid in humans: implications for homocysteine-linked disease. J. Biol. Chem. 2002, 277:30425-30428.
    • (2002) J. Biol. Chem. , vol.277 , pp. 30425-30428
    • Jakubowski, H.1
  • 83
    • 47749089308 scopus 로고    scopus 로고
    • New method for the determination of protein N-linked homocysteine
    • Jakubowski H. New method for the determination of protein N-linked homocysteine. Anal. Biochem. 2008, 380:257-261.
    • (2008) Anal. Biochem. , vol.380 , pp. 257-261
    • Jakubowski, H.1
  • 84
    • 67649371083 scopus 로고    scopus 로고
    • Genetic or nutritional disorders in homocysteine or folate metabolism increase protein N-homocysteinylation in mice
    • Jakubowski H., Perła-Kaján J., Finnell R.H., et al. Genetic or nutritional disorders in homocysteine or folate metabolism increase protein N-homocysteinylation in mice. FASEB J. 2009, 23:1721-1727.
    • (2009) FASEB J. , vol.23 , pp. 1721-1727
    • Jakubowski, H.1    Perła-Kaján, J.2    Finnell, R.H.3
  • 85
    • 0036270587 scopus 로고    scopus 로고
    • Protein-bound homocystamide measured in human plasma by HPLC
    • Uji Y., Motomiya Y., Hanyu N., Ukaji F., Okabe H. Protein-bound homocystamide measured in human plasma by HPLC. Clin. Chem. 2002, 48:941-944.
    • (2002) Clin. Chem. , vol.48 , pp. 941-944
    • Uji, Y.1    Motomiya, Y.2    Hanyu, N.3    Ukaji, F.4    Okabe, H.5
  • 87
    • 31044453984 scopus 로고    scopus 로고
    • Plasma homocysteine thiolactone adducts associated with risk of coronary heart disease
    • Yang X., Gao Y., Zhou J., et al. Plasma homocysteine thiolactone adducts associated with risk of coronary heart disease. Clin. Chim. Acta 2006, 364:230-234.
    • (2006) Clin. Chim. Acta , vol.364 , pp. 230-234
    • Yang, X.1    Gao, Y.2    Zhou, J.3
  • 88
    • 48249093757 scopus 로고    scopus 로고
    • Immunohistochemical detection of N-homocysteinylated proteins in humans and mice
    • Perla-Kajan J., Stanger O., Luczak M., et al. Immunohistochemical detection of N-homocysteinylated proteins in humans and mice. Biomed. Pharmacother. 2008, 62:473-479.
    • (2008) Biomed. Pharmacother. , vol.62 , pp. 473-479
    • Perla-Kajan, J.1    Stanger, O.2    Luczak, M.3
  • 89
    • 2542618547 scopus 로고    scopus 로고
    • Autoantibodies against N-homocysteinylated proteins in humans: implications for atherosclerosis
    • Undas A., Perla J., Lacinski M., Trzeciak W., Kazmierski R., Jakubowski H. Autoantibodies against N-homocysteinylated proteins in humans: implications for atherosclerosis. Stroke 2004, 35:1299-1304.
    • (2004) Stroke , vol.35 , pp. 1299-1304
    • Undas, A.1    Perla, J.2    Lacinski, M.3    Trzeciak, W.4    Kazmierski, R.5    Jakubowski, H.6
  • 90
    • 13844253976 scopus 로고    scopus 로고
    • Antibodies to N-homocysteinylated albumin as a marker for early-onset coronary artery disease in men
    • Undas A., Jankowski M., Twardowska M., Padjas A., Jakubowski H., Szczeklik A. Antibodies to N-homocysteinylated albumin as a marker for early-onset coronary artery disease in men. Thromb. Haemost. 2005, 93:346-350.
    • (2005) Thromb. Haemost. , vol.93 , pp. 346-350
    • Undas, A.1    Jankowski, M.2    Twardowska, M.3    Padjas, A.4    Jakubowski, H.5    Szczeklik, A.6
  • 91
    • 70249128338 scopus 로고    scopus 로고
    • Fully automated method for simultaneous determination of cysteine, cysteinylglycine, glutathione and homocysteine in plasma by high performance liquid chromatography
    • Glowacki R., Bald E. Fully automated method for simultaneous determination of cysteine, cysteinylglycine, glutathione and homocysteine in plasma by high performance liquid chromatography. J. Chromatogr. B 2009, 877:3400-3404.
    • (2009) J. Chromatogr. B , vol.877 , pp. 3400-3404
    • Glowacki, R.1    Bald, E.2
  • 92
    • 0034965934 scopus 로고    scopus 로고
    • 2-Chloro-1-methylquinolinium tetrafluoroborate as effective and thiol specific UV-tagging reagent for liquid chromatography
    • Bald E., Glowacki R. 2-Chloro-1-methylquinolinium tetrafluoroborate as effective and thiol specific UV-tagging reagent for liquid chromatography. J. Liq. Chromatogr. Rel. Techn. 2001, 24:1323-1339.
    • (2001) J. Liq. Chromatogr. Rel. Techn. , vol.24 , pp. 1323-1339
    • Bald, E.1    Glowacki, R.2


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