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Volumn 68, Issue 6, 1999, Pages 773-784

Structure and stability of the dityrosine-linked dimer of γB-crystallin

Author keywords

Conformational analysis; Dityrosine crosslinks; Post translational modifications in proteins; Structural stability; B crystallin

Indexed keywords

CRYSTALLIN; DIMER; TYROSINE;

EID: 0032998139     PISSN: 00144835     EISSN: None     Source Type: Journal    
DOI: 10.1006/exer.1999.0669     Document Type: Article
Times cited : (22)

References (51)
  • 1
    • 0017182516 scopus 로고
    • Formation of dityrosine cross-links in proteins by oxidation of tyrosine residues
    • Aeschbach R., Amado R., Neukom H. Formation of dityrosine cross-links in proteins by oxidation of tyrosine residues. Biochim. Biophys. Acta. 439:1976;292-301.
    • (1976) Biochim. Biophys. Acta , vol.439 , pp. 292-301
    • Aeschbach, R.1    Amado, R.2    Neukom, H.3
  • 2
    • 0021117853 scopus 로고
    • Dityrosine: Invitro production and characterization
    • Amado R., Aeshbach R., Neukom H. Dityrosine: invitro production and characterization. Methods Enzymol. 107:1984;377-388.
    • (1984) Methods Enzymol. , vol.107 , pp. 377-388
    • Amado, R.1    Aeshbach, R.2    Neukom, H.3
  • 3
    • 50549192159 scopus 로고
    • The cross-links in resilin identified as dityrosine and trityrosine
    • Anderson S. O. The cross-links in resilin identified as dityrosine and trityrosine. Biochim. Biophys. Acta. 93:1964;213-215.
    • (1964) Biochim. Biophys. Acta , vol.93 , pp. 213-215
    • Anderson, S.O.1
  • 4
    • 0025506306 scopus 로고
    • The reaction of singlet oxygen with proteins, with special reference to the crystallins
    • Balasubramanian D., Du X., Zigler, Jr J. S. The reaction of singlet oxygen with proteins, with special reference to the crystallins. Photochem. Photobiol. 52:1990;761-768.
    • (1990) Photochem. Photobiol. , vol.52 , pp. 761-768
    • Balasubramanian, D.1    Du, X.2    Zigler J.S., Jr.3
  • 5
    • 0025732948 scopus 로고
    • Role of glycation in modification of lens crystallins in diabetic and nondiabetic senile cataracts
    • Baynes J. W. Role of glycation in modification of lens crystallins in diabetic and nondiabetic senile cataracts. Diabetes. 40:1991;405-412.
    • (1991) Diabetes , vol.40 , pp. 405-412
    • Baynes, J.W.1
  • 6
    • 0027436101 scopus 로고
    • Serum form of the erythropoietin receptor identified by a sequence specific peptide antibody
    • Baynes R. D., Reddy G. K., Shih Y. J., Skikne B. S., Cook J. D. Serum form of the erythropoietin receptor identified by a sequence specific peptide antibody. Blood. 82:1993;2088-2095.
    • (1993) Blood , vol.82 , pp. 2088-2095
    • Baynes, R.D.1    Reddy, G.K.2    Shih, Y.J.3    Skikne, B.S.4    Cook, J.D.5
  • 8
    • 0021287535 scopus 로고
    • 2mediated cross-linking of lens crystallins catalyzed by the heme-undecapeptide from cytochrome c
    • 2mediated cross-linking of lens crystallins catalyzed by the heme-undecapeptide from cytochrome c. Arch. Biochem. Biophys. 231:1984;461-469.
    • (1984) Arch. Biochem. Biophys. , vol.231 , pp. 461-469
    • Bodaness, R.S.1    Leclair, M.2    Zigler J.S., Jr.3
  • 10
    • 0023655369 scopus 로고
    • Protein damage and degradation by oxygen radicals
    • Davies K. J. A. Protein damage and degradation by oxygen radicals. J. Biol. Chem. 262:1987;9895-9901.
    • (1987) J. Biol. Chem. , vol.262 , pp. 9895-9901
    • Davies, K.J.A.1
  • 11
    • 0018095222 scopus 로고
    • Photodynamic effects of protoporphyrin on human erythrocytes: Nature of the cross-linking of membrane proteins
    • Dubbelman T. M. A. R., De Goeij A. F. P. M., van Steveninck J. Photodynamic effects of protoporphyrin on human erythrocytes: nature of the cross-linking of membrane proteins. Biochim. Biophys. Acta. 511:1978;141-151.
    • (1978) Biochim. Biophys. Acta. , vol.511 , pp. 141-151
    • Dubbelman, T.M.A.R.1    De Goeij, A.F.P.M.2    Van Steveninck, J.3
  • 12
    • 0000816482 scopus 로고
    • Non-tryptophan fluorescence associated with human lens proteins: Apparent complexity and isolation of dityrosine and anthranilic acid
    • Garcia-Castineiras S., Dillon J., Spector A. Non-tryptophan fluorescence associated with human lens proteins: apparent complexity and isolation of dityrosine and anthranilic acid. Exp. Eye Res. 26:1987;464-476.
    • (1987) Exp. Eye Res. , vol.26 , pp. 464-476
    • Garcia-Castineiras, S.1    Dillon, J.2    Spector, A.3
  • 13
    • 0019519573 scopus 로고
    • Gamma-crystallin, a major cytoplasmic polypeptide disulfide linked to membrane proteins in human cataract
    • Garner W. H., Garner M. H., Spector A. Gamma-crystallin, a major cytoplasmic polypeptide disulfide linked to membrane proteins in human cataract. Biochem. Biophys. Res. Commun. 98:1981;439-447.
    • (1981) Biochem. Biophys. Res. Commun. , vol.98 , pp. 439-447
    • Garner, W.H.1    Garner, M.H.2    Spector, A.3
  • 14
    • 0005697399 scopus 로고
    • Determination of the solvent accessibility of specific aromatic residues in gamma-crystallin by photo-CIDNP NMR measurements
    • Garner W. H., Spector A., Schleiche T., Kaptein R. Determination of the solvent accessibility of specific aromatic residues in gamma-crystallin by photo-CIDNP NMR measurements. Curr. Eye Res. 25:1984;199-208.
    • (1984) Curr. Eye Res. , vol.25 , pp. 199-208
    • Garner, W.H.1    Spector, A.2    Schleiche, T.3    Kaptein, R.4
  • 15
    • 0026496731 scopus 로고
    • Dityrosine formation in the proteins of the eye lens
    • Guptasarma P., Balasubramanian D. Dityrosine formation in the proteins of the eye lens. Curr. Eye Res. 11:1992;1121-1125.
    • (1992) Curr. Eye Res. , vol.11 , pp. 1121-1125
    • Guptasarma, P.1    Balasubramanian, D.2
  • 16
    • 0026749942 scopus 로고
    • Hydroxyl radical mediated damage of proteins, with special reference to the crystallins
    • Guptasarma P., Balasubramanian D., Matsugo S., Saito I. Hydroxyl radical mediated damage of proteins, with special reference to the crystallins. Biochemistry. 31:1992;4296-4303.
    • (1992) Biochemistry , vol.31 , pp. 4296-4303
    • Guptasarma, P.1    Balasubramanian, D.2    Matsugo, S.3    Saito, I.4
  • 19
    • 0023070088 scopus 로고
    • Free radical modification of low-density lipoprotein: Mechanisms and biological consequences
    • Heinecke J. W. Free radical modification of low-density lipoprotein: mechanisms and biological consequences. Free Radical Biol. Med. 3:1987;65-73.
    • (1987) Free Radical Biol. Med. , vol.3 , pp. 65-73
    • Heinecke, J.W.1
  • 20
    • 0024312127 scopus 로고
    • A qualitative fluorescence-based assay for tyrosyl radical scavenging activity: Ovothiol A is an efficient scavenger
    • Holler T. P., Hopkins P. B. A qualitative fluorescence-based assay for tyrosyl radical scavenging activity: ovothiol A is an efficient scavenger. Anal. Biochem. 180:1989;326-330.
    • (1989) Anal. Biochem. , vol.180 , pp. 326-330
    • Holler, T.P.1    Hopkins, P.B.2
  • 21
    • 0027180882 scopus 로고
    • Formation of o-tyrosine and dityrosine in proteins during radiolytic and metal-catalyzed oxidation
    • Huggins T. G., Wells-Knecht M. C., Detorie N. A., Baynes J. W., Thorpe S. R. Formation of o-tyrosine and dityrosine in proteins during radiolytic and metal-catalyzed oxidation. J. Biol. Chem. 268:1993;12341-12347.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12341-12347
    • Huggins, T.G.1    Wells-Knecht, M.C.2    Detorie, N.A.3    Baynes, J.W.4    Thorpe, S.R.5
  • 23
    • 0025099402 scopus 로고
    • Thermodynamics of thermal and athermal denaturation of γ-crystallins: Changes in conformational stability upon glutathione reaction
    • Kono M., Sen A. C., Chakrabarti B. Thermodynamics of thermal and athermal denaturation of γ-crystallins: changes in conformational stability upon glutathione reaction. Biochemistry. 29:1990;464-470.
    • (1990) Biochemistry , vol.29 , pp. 464-470
    • Kono, M.1    Sen, A.C.2    Chakrabarti, B.3
  • 25
    • 0031021944 scopus 로고    scopus 로고
    • Mass spectrometric quantification of markers for protein oxidation by tyrosyl radical, copper, and hydroxyl radical in low density lipoprotein isolated from human atherosclerotic plaques
    • Leeuwenburgh C., Rasmussen J. E., Hsu F. F., Mueller D. M., Subramaniam P., Heinecke J. W. Mass spectrometric quantification of markers for protein oxidation by tyrosyl radical, copper, and hydroxyl radical in low density lipoprotein isolated from human atherosclerotic plaques. J. Biol. Chem. 272:1997;3520-3526.
    • (1997) J. Biol. Chem. , vol.272 , pp. 3520-3526
    • Leeuwenburgh, C.1    Rasmussen, J.E.2    Hsu, F.F.3    Mueller, D.M.4    Subramaniam, P.5    Heinecke, J.W.6
  • 26
    • 0015230409 scopus 로고
    • Solute perturbation of protein fluorescence. The quenching of the tryptophyl fluorescence of model compounds and of lysozyme by iodide ion
    • Lehrer S. S. Solute perturbation of protein fluorescence. The quenching of the tryptophyl fluorescence of model compounds and of lysozyme by iodide ion. Biochemistry. 10:1971;3254-3263.
    • (1971) Biochemistry , vol.10 , pp. 3254-3263
    • Lehrer, S.S.1
  • 27
    • 0014064318 scopus 로고
    • Ultraviolet irradiation effects in poly- l -tyrosine and model compounds. Identification of bityrosine as a photoproduct
    • Lehrer S. S., Fasman G. D. Ultraviolet irradiation effects in poly- l -tyrosine and model compounds. Identification of bityrosine as a photoproduct. Biochemistry. 6:1967;757-767.
    • (1967) Biochemistry , vol.6 , pp. 757-767
    • Lehrer, S.S.1    Fasman, G.D.2
  • 28
    • 0018875753 scopus 로고
    • 3-3"-dityrosine in the proteins of senile nuclear cataracts
    • McNamara M. K., Augusteyn R. C. 3-3"-dityrosine in the proteins of senile nuclear cataracts. Exp. Eye Res. 30:1980;319-321.
    • (1980) Exp. Eye Res. , vol.30 , pp. 319-321
    • McNamara, M.K.1    Augusteyn, R.C.2
  • 29
    • 0023149376 scopus 로고
    • Dityrosine formation in calmodulin
    • Malencik D. A., Anderson S. R. Dityrosine formation in calmodulin. Biochemistry. 26:1987;695-704.
    • (1987) Biochemistry , vol.26 , pp. 695-704
    • Malencik, D.A.1    Anderson, S.R.2
  • 30
    • 0025745082 scopus 로고
    • Fluorometric characterization of dityrosine: Complex formation with boric acid and borate ion
    • Malencik D. A., Anderson S. R. Fluorometric characterization of dityrosine: complex formation with boric acid and borate ion. Biochem. Biophys. Res. Commun. 178:1991;60-67.
    • (1991) Biochem. Biophys. Res. Commun. , vol.178 , pp. 60-67
    • Malencik, D.A.1    Anderson, S.R.2
  • 31
    • 0028073149 scopus 로고
    • Dityrosine formation in calmodulin: Conditions for intermolecular cross-linking
    • Malencik D. A., Anderson S. R. Dityrosine formation in calmodulin: conditions for intermolecular cross-linking. Biochemistry. 33:1994;13363-13376.
    • (1994) Biochemistry , vol.33 , pp. 13363-13376
    • Malencik, D.A.1    Anderson, S.R.2
  • 33
    • 0024286081 scopus 로고
    • Structure and stability of γ-crystallins: Tryptophan, tyrosine and cysteine accessibility
    • Mandal K., Chakrabarti B. Structure and stability of γ-crystallins: tryptophan, tyrosine and cysteine accessibility. Biochemistry. 27:1988;4564-4571.
    • (1988) Biochemistry , vol.27 , pp. 4564-4571
    • Mandal, K.1    Chakrabarti, B.2
  • 34
    • 84995036150 scopus 로고
    • Chemical reaction rates of amino acids with singlet oxygen
    • Matheson I. B. C., Lee J. Chemical reaction rates of amino acids with singlet oxygen. Photochem. Photobiol. 29:1979;879-881.
    • (1979) Photochem. Photobiol. , vol.29 , pp. 879-881
    • Matheson, I.B.C.1    Lee, J.2
  • 35
    • 84913806054 scopus 로고
    • Formation of dityrosine in collagen and elastin
    • Mullerova A., Michlik I., Blazej A. Formation of dityrosine in collagen and elastin. Leder. 25:1974;85-88.
    • (1974) Leder , vol.25 , pp. 85-88
    • Mullerova, A.1    Michlik, I.2    Blazej, A.3
  • 36
    • 0024993265 scopus 로고
    • Chemical modification of tryptophan residues and stability changes in proteins
    • Okajima T., Kawata Y., Hamaguchi K. Chemical modification of tryptophan residues and stability changes in proteins. Biochemistry. 29:1990;9168-9175.
    • (1990) Biochemistry , vol.29 , pp. 9168-9175
    • Okajima, T.1    Kawata, Y.2    Hamaguchi, K.3
  • 37
    • 0016505899 scopus 로고
    • The stability of globular proteins
    • Pace C. N. The stability of globular proteins. CRC Crit. Rev. Biochem. 3:1975;3-43.
    • (1975) CRC Crit. Rev. Biochem. , vol.3 , pp. 3-43
    • Pace, C.N.1
  • 40
    • 0015135926 scopus 로고
    • Occurrence of dityrosine in tussel silk fibroin and keratin
    • Raven D. J., Earland C., Little M. Occurrence of dityrosine in tussel silk fibroin and keratin. Biochim. Biophys. Acta. 251:1971;96-99.
    • (1971) Biochim. Biophys. Acta , vol.251 , pp. 96-99
    • Raven, D.J.1    Earland, C.2    Little, M.3
  • 41
    • 0020536198 scopus 로고
    • Interactions of heme proteins with hydrogen peroxide: Protein crosslinking and covalent binding of benzo[a] pyrene and 17 beta-estradiol
    • Rice R. H., Lee Y. M., Brown W. D. Interactions of heme proteins with hydrogen peroxide: protein crosslinking and covalent binding of benzo[a] pyrene and 17 beta-estradiol. Arch. Biochem. Biophys. 221:1983;417-427.
    • (1983) Arch. Biochem. Biophys. , vol.221 , pp. 417-427
    • Rice, R.H.1    Lee, Y.M.2    Brown, W.D.3
  • 44
    • 0025301715 scopus 로고
    • Covalent modification reactions are marking steps in protein turnover
    • Stadtman E. R. Covalent modification reactions are marking steps in protein turnover. Biochemistry. 29:1990;6323-6331.
    • (1990) Biochemistry , vol.29 , pp. 6323-6331
    • Stadtman, E.R.1
  • 45
    • 0025911829 scopus 로고
    • Metal-catalyzed oxidation of proteins. Physiological consequences
    • Stadtman E. R., Oliver C. N. Metal-catalyzed oxidation of proteins. Physiological consequences. J. Biol. Chem. 268:1991;2005-2008.
    • (1991) J. Biol. Chem. , vol.268 , pp. 2005-2008
    • Stadtman, E.R.1    Oliver, C.N.2
  • 46
    • 0014354873 scopus 로고
    • Fluorescence spectroscopy of proteins
    • Stryer L. Fluorescence spectroscopy of proteins. Science. 162:1968;526-533.
    • (1968) Science , vol.162 , pp. 526-533
    • Stryer, L.1
  • 47
    • 0026554096 scopus 로고
    • Protein interactions in the calf eye lens: Interactions between β-crystallins are repulsive whereas in γ-crystallins they are attractive
    • Tardieu A., Veretout F., Krop B., Slingsby C. Protein interactions in the calf eye lens: interactions between β-crystallins are repulsive whereas in γ-crystallins they are attractive. Eur. Biophys. J. 21:1992;1-12.
    • (1992) Eur. Biophys. J. , vol.21 , pp. 1-12
    • Tardieu, A.1    Veretout, F.2    Krop, B.3    Slingsby, C.4
  • 48
    • 0018651318 scopus 로고
    • Peroxidase-catalysed formation of dityrosine, a protein cross-link, in human periodontal ligament collagen
    • Tenovuo J., Paunio K. Peroxidase-catalysed formation of dityrosine, a protein cross-link, in human periodontal ligament collagen. Arch. Oral Biol. 24:1979;591-594.
    • (1979) Arch. Oral Biol. , vol.24 , pp. 591-594
    • Tenovuo, J.1    Paunio, K.2


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