메뉴 건너뛰기




Volumn 16, Issue 4, 2003, Pages 531-535

Dityrosine cross-linked Aβ peptides: Fibrillar β-structure in Aβ(1-40) is conducive to formation of dityrosine cross-links but a dityrosine cross-link in Aβ(8-14) does not induce β-structure

Author keywords

[No Author keywords available]

Indexed keywords

COPPER; DITYROSINE; HORSERADISH PEROXIDASE; HYDROGEN PEROXIDE; PEPTIDE DERIVATIVE; TYROSINE; UNCLASSIFIED DRUG;

EID: 0242417426     PISSN: 0893228X     EISSN: None     Source Type: Journal    
DOI: 10.1021/tx025666g     Document Type: Article
Times cited : (37)

References (23)
  • 1
    • 0014271005 scopus 로고
    • The cross-linkage theory of aging
    • Bjorksten, J. (1968) The cross-linkage theory of aging. J. Am. Geriatr. Soc. 16, 408-427.
    • (1968) J. Am. Geriatr. Soc. , vol.16 , pp. 408-427
    • Bjorksten, J.1
  • 2
    • 0025220737 scopus 로고
    • The cross-linking theory of aging-added evidence
    • Bjorksten, J., and Tenhu, H. (1990) The cross-linking theory of aging-added evidence. Exp. Gerontol. 25, 91-95.
    • (1990) Exp. Gerontol. , vol.25 , pp. 91-95
    • Bjorksten, J.1    Tenhu, H.2
  • 3
    • 0015135926 scopus 로고
    • Occurrence of dityrosine in Tussah silk fibroin and keratin
    • Raven, D. J., Earland, C., and Little, M. (1971) Occurrence of dityrosine in Tussah silk fibroin and keratin. Biochim. Biophys. Acta 251, 96-99.
    • (1971) Biochim. Biophys. Acta , vol.251 , pp. 96-99
    • Raven, D.J.1    Earland, C.2    Little, M.3
  • 6
    • 0034674652 scopus 로고    scopus 로고
    • Dityrosine cross-linking promotes formation of stable alpha-synuclein polymers. Implication of nitrative and oxidative stress in the pathogenesis of neurodegenerative synucleinopathies
    • Souza, J. M., Giasson, B. I., Chen, Q., Lee, V. M., and Ischiropoulos, H. (2000) Dityrosine cross-linking promotes formation of stable alpha-synuclein polymers. Implication of nitrative and oxidative stress in the pathogenesis of neurodegenerative synucleinopathies. J. Biol. Chem. 275, 18344-18349.
    • (2000) J. Biol. Chem. , vol.275 , pp. 18344-18349
    • Souza, J.M.1    Giasson, B.I.2    Chen, Q.3    Lee, V.M.4    Ischiropoulos, H.5
  • 7
    • 0028073149 scopus 로고
    • Dityrosine formation in calmodulin: Conditions for intermolecular cross-linking
    • Malencik, D. A., and Anderson, S. R. (1994) Dityrosine formation in calmodulin: conditions for intermolecular cross-linking. Biochemistry 33, 13363-13372.
    • (1994) Biochemistry , vol.33 , pp. 13363-13372
    • Malencik, D.A.1    Anderson, S.R.2
  • 8
    • 0033045848 scopus 로고    scopus 로고
    • In vitro peroxidase oxidation induces stable dimers of β-amyloid (1-42) through dityrosine bridge formation
    • Galeazzi, L., Ronchi, P., Franceschi, C., and Giunta, S. (1999) In vitro peroxidase oxidation induces stable dimers of β-amyloid (1-42) through dityrosine bridge formation. Amyloid 6, 7-13.
    • (1999) Amyloid , vol.6 , pp. 7-13
    • Galeazzi, L.1    Ronchi, P.2    Franceschi, C.3    Giunta, S.4
  • 10
    • 0032806289 scopus 로고    scopus 로고
    • Hydroxyl radical generation during exercise increases mitochondrial protein oxidation and levels of urinary dityrosine
    • Leeuwenburgh, C., Hansen, P. A., Holloszy, J. O., and Heinecke, J. W. (1999) Hydroxyl radical generation during exercise increases mitochondrial protein oxidation and levels of urinary dityrosine. Free Radical Biol. Med. 27, 186-192.
    • (1999) Free Radical Biol. Med. , vol.27 , pp. 186-192
    • Leeuwenburgh, C.1    Hansen, P.A.2    Holloszy, J.O.3    Heinecke, J.W.4
  • 11
    • 0032891777 scopus 로고    scopus 로고
    • Oxidized amino acids in the urine of aging rats: Potential markers for assessing oxidative stress in vivo
    • Leeuwenburgh, C., Hansen, P. A., Holloszy, J. O., and Heinecke, J. W. (1999) Oxidized amino acids in the urine of aging rats: potential markers for assessing oxidative stress in vivo. Am. J. Physiol. 276, R128-R135.
    • (1999) Am. J. Physiol. , vol.276
    • Leeuwenburgh, C.1    Hansen, P.A.2    Holloszy, J.O.3    Heinecke, J.W.4
  • 12
    • 0032531735 scopus 로고    scopus 로고
    • Electrochemical analysis of protein nitrotyrosine and dityrosine in the Alzheimer brain indicates region-specific accumulation
    • Hensley, K., Maidt, M. L., Yu, Z., Sang, H., Markesbery, W. R., and Floyd, R. A. (1998) Electrochemical analysis of protein nitrotyrosine and dityrosine in the Alzheimer brain indicates region-specific accumulation. J. Neurosci. 18, 8126-8132.
    • (1998) J. Neurosci. , vol.18 , pp. 8126-8132
    • Hensley, K.1    Maidt, M.L.2    Yu, Z.3    Sang, H.4    Markesbery, W.R.5    Floyd, R.A.6
  • 13
    • 0037072542 scopus 로고    scopus 로고
    • β-amyloid deposition and neurofibrillary tangle association with caspase activation in Down syndrome
    • Head, E., Lott, I., Cribbs, D., Cotman, C., and Rohn, T. (2002) β-Amyloid deposition and neurofibrillary tangle association with caspase activation in Down syndrome. Neurosci. Lett. 330, 99.
    • (2002) Neurosci. Lett. , vol.330 , pp. 99
    • Head, E.1    Lott, I.2    Cribbs, D.3    Cotman, C.4    Rohn, T.5
  • 15
    • 0032998139 scopus 로고    scopus 로고
    • Structure and stability of the dityrosine-linked dimer of gammaB-Crystallin
    • Kanwar, R., and Balasubramanian, D. (1999) Structure and stability of the dityrosine-linked dimer of gammaB-Crystallin. Exp. Eye Res. 68, 773-784.
    • (1999) Exp. Eye Res. , vol.68 , pp. 773-784
    • Kanwar, R.1    Balasubramanian, D.2
  • 16
    • 0032148270 scopus 로고    scopus 로고
    • Stabilization of a C7 equatorial gamma turn in DMSO-d6 by a ditryptophan cross-link
    • Stachel, S. J., Hu, H., Van, Q. N., Shaka, A. J., and Van Vranken, D. L. (1998) Stabilization of a C7 equatorial gamma turn in DMSO-d6 by a ditryptophan cross-link. Bioorg. Med. Chem. 6, 1439-1446.
    • (1998) Bioorg. Med. Chem. , vol.6 , pp. 1439-1446
    • Stachel, S.J.1    Hu, H.2    Van, Q.N.3    Shaka, A.J.4    Van Vranken, D.L.5
  • 17
    • 0034697120 scopus 로고    scopus 로고
    • Formation and characterization of a single Trp-Trp cross-link in indolicidin that confers protease stability without altering antimicrobial activity
    • Osapay, K., Tran, D., Ladokhin, A. S., White, S. H., Henschen, A. H., and Selsted, M. E. (2000) Formation and characterization of a single Trp-Trp cross-link in indolicidin that confers protease stability without altering antimicrobial activity. J. Biol. Chem. 275, 12017-12022.
    • (2000) J. Biol. Chem. , vol.275 , pp. 12017-12022
    • Osapay, K.1    Tran, D.2    Ladokhin, A.S.3    White, S.H.4    Henschen, A.H.5    Selsted, M.E.6
  • 18
    • 0035202459 scopus 로고    scopus 로고
    • Intramolecular ditryptophan crosslinks enforce two types of antiparallel β-structures
    • Matthews, J. H., Dinh, T. D., Tivitmahaisoon, P., Ziller, J. W., and Van Vranken, D. L. (2001) Intramolecular ditryptophan crosslinks enforce two types of antiparallel β-structures. Chem. Biol. 8, 1071-1079.
    • (2001) Chem. Biol. , vol.8 , pp. 1071-1079
    • Matthews, J.H.1    Dinh, T.D.2    Tivitmahaisoon, P.3    Ziller, J.W.4    Van Vranken, D.L.5
  • 19
    • 0029556962 scopus 로고
    • Correlation among secondary structure, amyloid precursor protein accumulation, and neurotoxicity of amyloid β(25-35) peptide as analyzed by single alanine substitution
    • Sato, K., Wakamiya, A., Maeda, T., Noguchi, K., Takashima, A., and Imahori, K. (1995) Correlation among secondary structure, amyloid precursor protein accumulation, and neurotoxicity of amyloid β(25-35) peptide as analyzed by single alanine substitution. J. Biochem. (Tokyo) 118, 1108-1111.
    • (1995) J. Biochem. (Tokyo) , vol.118 , pp. 1108-1111
    • Sato, K.1    Wakamiya, A.2    Maeda, T.3    Noguchi, K.4    Takashima, A.5    Imahori, K.6
  • 20
    • 0034682979 scopus 로고    scopus 로고
    • Immunochemical detection of protein dityrosine in atherosclerotic lesion of apo-E-deficient mice using a novel monoclonal antibody
    • Kato, Y., Wu, X., Naito, M., Nomura, H., Kitamoto, N., and Osawa, T. (2000) Immunochemical detection of protein dityrosine in atherosclerotic lesion of apo-E-deficient mice using a novel monoclonal antibody. Biochem. Biophys. Res. Commun. 275, 11-15.
    • (2000) Biochem. Biophys. Res. Commun. , vol.275 , pp. 11-15
    • Kato, Y.1    Wu, X.2    Naito, M.3    Nomura, H.4    Kitamoto, N.5    Osawa, T.6
  • 22
    • 0034600777 scopus 로고    scopus 로고
    • A designed β-hairpin containing a natural hydrophobic cluster
    • Espinosa, J. F., and Gellman, S. H. (2000) A Designed β-Hairpin Containing a Natural Hydrophobic Cluster. Angew. Chem., Int. Ed. 39, 2330-2333.
    • (2000) Angew. Chem., Int. Ed. , vol.39 , pp. 2330-2333
    • Espinosa, J.F.1    Gellman, S.H.2
  • 23
    • 0036113724 scopus 로고    scopus 로고
    • Analysis of the factors that stabilize a designed two-stranded antiparallel β-sheet
    • Espinosa, J. F., Syud, F. A., and Gellman, S. H. (2002) Analysis of the factors that stabilize a designed two-stranded antiparallel β-sheet. Protein Sci. 11, 1492-1505.
    • (2002) Protein Sci. , vol.11 , pp. 1492-1505
    • Espinosa, J.F.1    Syud, F.A.2    Gellman, S.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.