메뉴 건너뛰기




Volumn 928, Issue , 2001, Pages 22-38

Protein oxidation in aging and age-related diseases

Author keywords

Amino acid residues; Apoptosis; Oxidatively modified protein; Reactive oxygen species

Indexed keywords

ANTIOXIDANT; CARBONYL DERIVATIVE; GLYCOSYLATED PROTEIN; LIPID; M PROTEIN; NUCLEIC ACID; OXIDIZING AGENT; REACTIVE OXYGEN METABOLITE;

EID: 0035039021     PISSN: 00778923     EISSN: None     Source Type: Book Series    
DOI: 10.1111/j.1749-6632.2001.tb05632.x     Document Type: Conference Paper
Times cited : (555)

References (136)
  • 1
    • 77049308856 scopus 로고
    • Aging theory based on free radical and radiation chemistry
    • (1956) J. Gerontol. , vol.2 , pp. 298-300
    • Harman, D.1
  • 4
    • 0023658397 scopus 로고
    • A mechanism for accelerated degradation of intracellular proteins after limited damage by free radicals
    • (1987) FEBS Lett. , vol.220 , pp. 278-282
    • Dean, R.T.1
  • 5
    • 0027414020 scopus 로고
    • Dityrosine and tyrosine oxidation products are endogenous markers for the selective proteolysis of oxidatively modified red blood cell hemoglobin by the 19 S proteasome
    • (1993) J. Biol. Chem. , vol.268 , pp. 8752-8759
    • Giulivi, C.1    Davies, K.J.2
  • 12
    • 0000302143 scopus 로고
    • Reaction mechanisms in the radiolysis of peptides, polypeptides, and proteins
    • (1987) Chem. Rev. , vol.87 , pp. 381-398
    • Garrison, W.M.1
  • 20
    • 0028200871 scopus 로고
    • Aromatic hydroxylation of phenylalanine as an assay for hydroxyl radicals. Measurement of hydroxyl radical formation from ozone and in blood from premature babies using improved HPLC methodology
    • (1994) Anal. Biochem. , vol.220 , pp. 11-15
    • Kaur, H.1    Halliwell, B.2
  • 21
    • 0000796146 scopus 로고
    • Radiation-induced formation of dihydroxy phenylalanine from tyrosine and tyrosine-containing peptides in aqueous solution
    • (1961) Radiat. Res. , vol.15 , pp. 349-351
    • Fletcher, G.L.1    Okada, S.2
  • 40
    • 0023030789 scopus 로고
    • Sequence of a peptide susceptible to mixed-function oxidation: Probable cation binding site in glutamine synthetase
    • (1986) J. Biol. Chem. , vol.261 , pp. 4574-4578
    • Farber, J.M.1    Levine, R.L.2
  • 41
    • 0025721165 scopus 로고
    • Exposure of rat muscle phosphoglycerate kinase to a nonenzymatic MFO system generates the old form of enzyme
    • (1991) J. Gerontol. , vol.46
    • Zhou, J.Q.1    Gafni, A.2
  • 44
    • 0028132836 scopus 로고
    • Redox signaling: Nitrosylation and related target interactions of nitric oxide
    • (1994) Cell , vol.78 , pp. 931-936
    • Stamler, J.S.1
  • 45
    • 0028175539 scopus 로고
    • Mechanism of covalent modification of glyceraldehyde-3-phosphate dehydrogenase at its active site thiol by nitric oxide, peroxynitrite, and related nitrosating agents
    • (1994) FEBS Lett. , vol.348 , pp. 223-227
    • Mohr, S.1    Stamler, J.S.2    Brune, B.3
  • 55
    • 0033592423 scopus 로고    scopus 로고
    • Peroxynitrite modification of protein thiols: Oxidation, nitrosylation, and S-glutathiolation of functionally important cysteine residue(s) in the sarcoplasmic reticulum Ca-ATPase
    • (1999) Biochemistry , vol.38 , pp. 12408-12415
    • Viner, R.I.1    Williams, T.D.2    Schoneich, C.3
  • 62
    • 0004995876 scopus 로고    scopus 로고
    • Carbon dioxide stimulates nitration of tyrosine residues and inhibits oxidation of methionine residues in Escherichia coli glutamine synthetase by peroxynitrite
    • Abstract #585
    • (1996) FASEB J. , vol.10
    • Berlett, B.S.1    Stadtman, E.R.2
  • 64
    • 0028838971 scopus 로고
    • Protein kinases and phosphatases: The Ying and Yang of protein phosphorylation and signaling
    • (1995) Cell , vol.80 , pp. 225-236
    • Hunter, T.1
  • 91
    • 0029893851 scopus 로고
    • Relationship between susceptibility to protein oxidation, aging, and maximum life span potential of different species
    • (1993) Exp. Gerontol. , vol.31 , pp. 365-372
    • Agarwal, S.1    Sohal, R.S.2
  • 95
    • 0023020327 scopus 로고
    • Regulation of intracellular protein turnover: Covalent modification as a mechanism of marking proteins for degradation
    • (1986) Curr. Top. Cell. Regul. , vol.28 , pp. 291-337
    • Rivett, A.J.1
  • 98
    • 0025301715 scopus 로고
    • Covalent modification reactions are marking steps in protein turnover
    • (1990) Biochemistry , vol.29 , pp. 6323-6331
    • Stadtman, E.R.1
  • 99
    • 0022631944 scopus 로고
    • Oxidation of proteins by mixed-function oxidation systems: Implication in protein turnover, ageing and neutrophil function
    • (1986) Trends Biochem. Sci. , vol.11 , pp. 11-12
    • Stadtman, E.R.1
  • 110
    • 0024370492 scopus 로고
    • Oxidation state of tissue thiol groups and content of protein carbonyl groups in chickens with inherited muscular dystrophy
    • (1989) Biochem. J. , vol.260 , pp. 359-364
    • Murphy, M.E.1    Kherer, J.P.2
  • 125
    • 0025732948 scopus 로고
    • Perspectives in diabetes. Role of oxidative stress in development of complications in diabetes
    • (1991) Diabetes , vol.40 , pp. 405-411
    • Baynes, J.W.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.