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Volumn 53, Issue 2, 2003, Pages 162-173

Prediction of possible sites for posttranslational modifications in human gamma crystallins: Effect of glycation on the structure of human gamma-B-crystallin as analyzed by molecular modeling

Author keywords

3D structure prediction; Glycosylation; Homology or comparative modeling; Long lived proteins; Phosphorylation

Indexed keywords

ALPHA GLUCOSE; ALPHA GLUCOSE 6 PHOSPHATE; CYSTEINE DERIVATIVE; DISULFIDE; GAMMA B CRYSTALLIN; GAMMA CRYSTALLIN; GAMMA D CRYSTALLIN; GLUCOSE; GLUCOSE 6 PHOSPHATE; PROTEIN SUBUNIT; THIOL GROUP; UNCLASSIFIED DRUG;

EID: 0141480852     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.10493     Document Type: Article
Times cited : (12)

References (55)
  • 1
    • 0024559375 scopus 로고
    • Acylation of viral and eukaryotic proteins
    • Grand RJA. Acylation of viral and eukaryotic proteins. Biochem J 1989;258:625-638.
    • (1989) Biochem J , vol.258 , pp. 625-638
    • Grand, R.J.A.1
  • 2
    • 0024852380 scopus 로고
    • Structure elucidation of a senescence cross-link from human extracellular matrix
    • Sell DR, Monnier VM. Structure elucidation of a senescence cross-link from human extracellular matrix. J Biol Chem 1989;264: 21597-21602.
    • (1989) J Biol Chem , vol.264 , pp. 21597-21602
    • Sell, D.R.1    Monnier, V.M.2
  • 3
    • 0032170644 scopus 로고    scopus 로고
    • Deamidation and disulfide bonding in human lens γ-crystallins
    • Hanson SRA, Smith DL, Smith JB. Deamidation and disulfide bonding in human lens γ-crystallins Exp Eye Res 1998;67:301-312.
    • (1998) Exp Eye Res , vol.67 , pp. 301-312
    • Hanson, S.R.A.1    Smith, D.L.2    Smith, J.B.3
  • 4
    • 0032132710 scopus 로고    scopus 로고
    • The contribution of glycation to cataract formation in diabetes
    • Stevens A. The contribution of glycation to cataract formation in diabetes. Clin Sci 1998;69:519-530.
    • (1998) Clin Sci , vol.69 , pp. 519-530
    • Stevens, A.1
  • 5
    • 0141530330 scopus 로고
    • The role of alpha- and epsilon-amino groups in the glycation-mediated cross-linking of gammaB-crystallin. Study of three site-directed mutants
    • Casey EB, Zhao H.-R, Abraham EC. The role of alpha- and epsilon-amino groups in the glycation-mediated cross-linking of gammaB-crystallin. Study of three site-directed mutants. J Biol Chem 1985;270:20781-20786.
    • (1985) J Biol Chem , vol.270 , pp. 20781-20786
    • Casey, E.B.1    Zhao, H.-R.2    Abraham, E.C.3
  • 6
    • 0028959741 scopus 로고
    • The culture of rat lenses in high sugar media: Effect on mixed disulfide levels
    • Dickerson JE Jr, Lou MF, Gracy RW. The culture of rat lenses in high sugar media: effect on mixed disulfide levels. Curr Eye Res 1995;14:109-118.
    • (1995) Curr Eye Res , vol.14 , pp. 109-118
    • Dickerson J.E., Jr.1    Lou, M.F.2    Gracy, R.W.3
  • 7
    • 0019475899 scopus 로고
    • Nonenzymatic browing in vitro: Possible process for aging of long lived proteins
    • Monnier VM, Cerami A. Nonenzymatic browing in vitro: possible process for aging of long lived proteins. Science 1981;211:491-494.
    • (1981) Science , vol.211 , pp. 491-494
    • Monnier, V.M.1    Cerami, A.2
  • 8
    • 0028453652 scopus 로고
    • Lilly Lecture 1993. Glycation and diabetic complications
    • Brownlee M. Lilly Lecture 1993. Glycation and diabetic complications. Diabetes 1994;43:836-841.
    • (1994) Diabetes , vol.43 , pp. 836-841
    • Brownlee, M.1
  • 9
    • 0028469809 scopus 로고
    • Recent progress on the biologic and clinical significance of advanced glycosylation end products
    • Vlassara H. Recent progress on the biologic and clinical significance of advanced glycosylation end products. J Lab Clin Med 1994;124:19-30.
    • (1994) J Lab Clin Med , vol.124 , pp. 19-30
    • Vlassara, H.1
  • 10
    • 0026887742 scopus 로고
    • Pharmacological treatment strategies in age related cataracts
    • Harding JJ. Pharmacological treatment strategies in age related cataracts. Drugs Aging 1992;2:287-300.
    • (1992) Drugs Aging , vol.2 , pp. 287-300
    • Harding, J.J.1
  • 11
    • 0021929455 scopus 로고
    • Prevalence of cataracts in a population-based study of persons with diabetes mellitus
    • Klein BE, Klein R, Moss SE. Prevalence of cataracts in a population-based study of persons with diabetes mellitus. Ophthalmology 1985;92:1191-1196.
    • (1985) Ophthalmology , vol.92 , pp. 1191-1196
    • Klein, B.E.1    Klein, R.2    Moss, S.E.3
  • 13
    • 0030861438 scopus 로고    scopus 로고
    • The SWISS-PROT protein sequence data bank and its supplement TrEMBL
    • Bairoch A, Apweiler R. The SWISS-PROT protein sequence data bank and its supplement TrEMBL. Nucleic Acids Res 1997;25:31-36.
    • (1997) Nucleic Acids Res , vol.25 , pp. 31-36
    • Bairoch, A.1    Apweiler, R.2
  • 18
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali A, Blundell TL. Comparative protein modelling by satisfaction of spatial restraints. J Mol Biol 1993;234:779-815.
    • (1993) J Mol Biol , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 20
    • 0030047142 scopus 로고    scopus 로고
    • Verification of protein structures: Side-chain planarity
    • Hooft RWW, Vriend G, Sander C, Abola EE. Verification of protein structures: side-chain planarity. Nature 1996;381:272-272.
    • (1996) Nature , vol.381 , pp. 272-272
    • Hooft, R.W.W.1    Vriend, G.2    Sander, C.3    Abola, E.E.4
  • 21
    • 0037449865 scopus 로고    scopus 로고
    • Homology models of human gamma crystallins: Structural study of the extensive charge network in gamma crystallins
    • Salim A, Zaidi ZH. Homology models of human gamma crystallins: structural study of the extensive charge network in gamma crystallins. Biochem Biophys Res Commun 2003;300:624-630.
    • (2003) Biochem Biophys Res Commun , vol.300 , pp. 624-630
    • Salim, A.1    Zaidi, Z.H.2
  • 22
    • 0141641452 scopus 로고    scopus 로고
    • http://www.accelrys.com/viewer/.
  • 23
    • 0141641454 scopus 로고    scopus 로고
    • http://www.genome.adjp/ligand/.
  • 24
    • 0025398721 scopus 로고
    • A molecular modelling and drug design program
    • Vriend G. A molecular modelling and drug design program. J Mol Graph. 1990;8:52-56.
    • (1990) J Mol Graph , vol.8 , pp. 52-56
    • Vriend, G.1
  • 25
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG, Gibson TJ. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 1994;22:4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 26
    • 0030665259 scopus 로고    scopus 로고
    • The glycation of bovine lens betaL-, betaS-and gamma-crystallins demonstrated by isoelectric focusing and lectin staining
    • Ahrend MHJ, Bours J. The glycation of bovine lens betaL-, betaS-and gamma-crystallins demonstrated by isoelectric focusing and lectin staining. Exp Eye Res 1997;65:711-715.
    • (1997) Exp Eye Res , vol.65 , pp. 711-715
    • Ahrend, M.H.J.1    Bours, J.2
  • 28
    • 0033105819 scopus 로고    scopus 로고
    • Relationship between autofluorescence advanced glycation end products in diabetic lenses
    • Abiko T, Abiko A, Ishiko S, Takeda M, Horiuchi S, Yoshida Y. Relationship between autofluorescence advanced glycation end products in diabetic lenses. Exp Eye Res 1999;68:361-366.
    • (1999) Exp Eye Res , vol.68 , pp. 361-366
    • Abiko, T.1    Abiko, A.2    Ishiko, S.3    Takeda, M.4    Horiuchi, S.5    Yoshida, Y.6
  • 29
    • 0021703378 scopus 로고
    • Conformational changes induced in bovine lens α-crystallin by carbamylation
    • Beswick HT, Harding JJ. Conformational changes induced in bovine lens α-crystallin by carbamylation. Biochem J 1984;223: 221-227.
    • (1984) Biochem J , vol.223 , pp. 221-227
    • Beswick, H.T.1    Harding, J.J.2
  • 30
    • 0011442220 scopus 로고
    • Diabetic cataract formation: Potential role of glycosylation of lens crystallins
    • Stevens VJ, Rouzer CA, Monnier VM, Diabetic cataract formation: potential role of glycosylation of lens crystallins. Proc Natl Acad Sci USA 1978;75:2918-2922.
    • (1978) Proc Natl Acad Sci USA , vol.75 , pp. 2918-2922
    • Stevens, V.J.1    Rouzer, C.A.2    Monnier, V.M.3
  • 31
    • 0018944813 scopus 로고
    • Effect of experimental diabetes on glycolytic intermediates and regulation of phosphofructokinase in rat lens
    • Gonzalez AM, Sochor M, McLean P. Effect of experimental diabetes on glycolytic intermediates and regulation of phosphofructokinase in rat lens. Biochem Biophys Res Commun 1980;95:1173-1179.
    • (1980) Biochem Biophys Res Commun , vol.95 , pp. 1173-1179
    • Gonzalez, A.M.1    Sochor, M.2    McLean, P.3
  • 32
    • 0026575313 scopus 로고
    • Mechanistic studies of advanced glycosylation end product inhibition by aminoguanidine
    • Edelstein D, Brownlee M. Mechanistic studies of advanced glycosylation end product inhibition by aminoguanidine. Diabetes 1992;41:26-28.
    • (1992) Diabetes , vol.41 , pp. 26-28
    • Edelstein, D.1    Brownlee, M.2
  • 33
    • 0023655983 scopus 로고
    • Conformational changes induced in lens crystallins by modification with glucose-6-phosphate; implications for cataract
    • Beswick HT, Harding JJ. Conformational changes induced in lens crystallins by modification with glucose-6-phosphate; implications for cataract. Biochem J 1987;247:761-769.
    • (1987) Biochem J , vol.247 , pp. 761-769
    • Beswick, H.T.1    Harding, J.J.2
  • 34
    • 0025234587 scopus 로고
    • pH-induced denaturation of proteins: A single salt bridge contributes 3-5 kcal/mol to the free energy of folding of T4 lysozyme
    • Anderson DE, Becktel WJ, Dahlquist FW. pH-induced denaturation of proteins: a single salt bridge contributes 3-5 kcal/mol to the free energy of folding of T4 lysozyme. Biochemistry 1990;29: 2403-2408.
    • (1990) Biochemistry , vol.29 , pp. 2403-2408
    • Anderson, D.E.1    Becktel, W.J.2    Dahlquist, F.W.3
  • 35
    • 0033624640 scopus 로고    scopus 로고
    • Advanced glycation end products in human senile and diabetic cataractous lenses
    • Zarina S, Zhao H-R, Abraham EC. Advanced glycation end products in human senile and diabetic cataractous lenses. Mol Cell Biochem 2000;210:29-34.
    • (2000) Mol Cell Biochem , vol.210 , pp. 29-34
    • Zarina, S.1    Zhao, H.-R.2    Abraham, E.C.3
  • 36
    • 0020713174 scopus 로고
    • Structural requirements of N-glycosylation of proteins. Studies with proline peptides as conformational probes
    • Bause E. Structural requirements of N-glycosylation of proteins. Studies with proline peptides as conformational probes. Biochem J 1983;209:331-336.
    • (1983) Biochem J , vol.209 , pp. 331-336
    • Bause, E.1
  • 38
    • 0019880745 scopus 로고
    • Circular dichroism studies of synthetic Asn-X-Ser/Thr-containing peptides: Structure-glycosylation relationship
    • Aubert JP, Helbecque N, Loucheux-Lefebvre MH. Circular dichroism studies of synthetic Asn-X-Ser/Thr-containing peptides: structure-glycosylation relationship. Arch Biochem Biophys 1981;208: 20-29.
    • (1981) Arch Biochem Biophys , vol.208 , pp. 20-29
    • Aubert, J.P.1    Helbecque, N.2    Loucheux-Lefebvre, M.H.3
  • 39
    • 0020146990 scopus 로고
    • Conformational aspects of N-glycosylation of proteins. Studies with linear and cyclic peptides as probes
    • Bause E, Hettkamp H, Legler G. Conformational aspects of N-glycosylation of proteins. Studies with linear and cyclic peptides as probes. Biochem J 1982;203:761-768.
    • (1982) Biochem J , vol.203 , pp. 761-768
    • Bause, E.1    Hettkamp, H.2    Legler, G.3
  • 40
    • 0019579733 scopus 로고
    • The role of the hydroxy amino acid in the thetriplet sequence Asn-Xaa-Thr(Ser) for the N-glycosylation step during glycoprotein biosynthesis
    • Bause E, Legler G. The role of the hydroxy amino acid in the intriplet sequence Asn-Xaa-Thr(Ser) for the N-glycosylation step during glycoprotein biosynthesis Biochem J 1981;195:639-644.
    • (1981) Biochem J , vol.195 , pp. 639-644
    • Bause, E.1    Legler, G.2
  • 41
    • 0019321115 scopus 로고
    • Optimal spatial requirements for the location of basic residues in peptide substrates for the cyclic AMP-dependent protein kinase
    • Feramisco JR, Glass DB, Krebs EG. Optimal spatial requirements for the location of basic residues in peptide substrates for the cyclic AMP-dependent protein kinase. J Biol Chem 1980;255:4240-4245.
    • (1980) J Biol Chem , vol.255 , pp. 4240-4245
    • Feramisco, J.R.1    Glass, D.B.2    Krebs, E.G.3
  • 42
    • 0022881173 scopus 로고
    • Substrate specificity of protein kinase C. Use of synthetic peptides corresponding to physiological sites as probes for substrate recognition requirements
    • Woodgett JR, Gould KL, Hunter T. Substrate specificity of protein kinase C. Use of synthetic peptides corresponding to physiological sites as probes for substrate recognition requirements. Eur J Biochem 1986;161:177-184.
    • (1986) Eur J Biochem , vol.161 , pp. 177-184
    • Woodgett, J.R.1    Gould, K.L.2    Hunter, T.3
  • 43
    • 0025113220 scopus 로고
    • Casein kinase 2: An "eminence grise" in cellular regulation?
    • Pinna LA. Casein kinase 2: an "eminence grise" in cellular regulation? Biochim Biophys Acta 1990;1054:267-284.
    • (1990) Biochim Biophys Acta , vol.1054 , pp. 267-284
    • Pinna, L.A.1
  • 44
    • 0020478990 scopus 로고
    • Synthetic peptide substrates for a tyrosine protein kinase
    • Hunter T. Synthetic peptide substrates for a tyrosine protein kinase. J Biol Chem 1982;257:4843-4848.
    • (1982) J Biol Chem , vol.257 , pp. 4843-4848
    • Hunter, T.1
  • 45
    • 0029993727 scopus 로고    scopus 로고
    • Active and inactive protein kinases: Structural basis for regulation
    • Johnson LN, Noble MEM, Owen DJ. Active and inactive protein kinases: structural basis for regulation. Cell 1996;85:149-158.
    • (1996) Cell , vol.85 , pp. 149-158
    • Johnson, L.N.1    Noble, M.E.M.2    Owen, D.J.3
  • 46
    • 0022978498 scopus 로고
    • Synthetic peptides corresponding to the site phosphorylated in 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase as substrates of cyclic nucleotide-dependent protein kinases
    • Glass DB, el-Maghrabi MR, Pilkis SJ. Synthetic peptides corresponding to the site phosphorylated in 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase as substrates of cyclic nucleotide-dependent protein kinases. J Biol Chem 1986;261:2987-2993.
    • (1986) J Biol Chem , vol.261 , pp. 2987-2993
    • Glass, D.B.1    El-Maghrabi, M.R.2    Pilkis, S.J.3
  • 47
  • 49
    • 0024325713 scopus 로고
    • The dephosphrylation of lens α-crystallin
    • Chiesa R, Spector A. The dephosphrylation of lens α-crystallin. Biochem Biophys Res Commun 1989;162:1494-1501.
    • (1989) Biochem Biophys Res Commun , vol.162 , pp. 1494-1501
    • Chiesa, R.1    Spector, A.2
  • 50
    • 0023644471 scopus 로고
    • The phosphorylation of the primary gene products of α-crystallin
    • Chiesa R, Gawinowicz-Kolks MA, Spector A. The phosphorylation of the primary gene products of α-crystallin. J Biol Chem 1987;262: 1438-1441.
    • (1987) J Biol Chem , vol.262 , pp. 1438-1441
    • Chiesa, R.1    Gawinowicz-Kolks, M.A.2    Spector, A.3
  • 51
    • 0023888625 scopus 로고
    • Definition and comparison of the phosphorylation sites of the A and B chains of bovine α-crystallin
    • Chiesa R, Gawinowicz-Kolks MA, Kleiman NJ, Spector A. Definition and comparison of the phosphorylation sites of the A and B chains of bovine α-crystallin. Exp Eye Res 1988;46:199-208.
    • (1988) Exp Eye Res , vol.46 , pp. 199-208
    • Chiesa, R.1    Gawinowicz-Kolks, M.A.2    Kleiman, N.J.3    Spector, A.4
  • 52
    • 0029992808 scopus 로고    scopus 로고
    • Differential phosphorylation of the alpha-A crystallin in human lens of different age
    • Takemoto LJ. Differential phosphorylation of the alpha-A crystallin in human lens of different age. Exp Eye Res 1996;62: 499-504.
    • (1996) Exp Eye Res , vol.62 , pp. 499-504
    • Takemoto, L.J.1
  • 53
    • 0032077176 scopus 로고    scopus 로고
    • Phosphorylations of α-A and αB-crystallin
    • Kantorow M, Piatigorsky J. Phosphorylations of α-A and αB-crystallin. Int J Biol Macromol 1998;22:307-314.
    • (1998) Int J Biol Macromol , vol.22 , pp. 307-314
    • Kantorow, M.1    Piatigorsky, J.2
  • 54
    • 0029083170 scopus 로고
    • Conversion from oligomers to tetramers enhances autophosphrylation by lens alpha A-crystallin: Specificity between α-A and αB-crystallin
    • Kantorow M, Horwitz J, van Boekal MAM, de Jong WW, Piatigorsky J. Conversion from oligomers to tetramers enhances autophosphrylation by lens alpha A-crystallin: specificity between α-A and αB-crystallin. J Biol Chem 1995;270:17215-17220.
    • (1995) J Biol Chem , vol.270 , pp. 17215-17220
    • Kantorow, M.1    Horwitz, J.2    Van Boekal, M.A.M.3    De Jong, W.W.4    Piatigorsky, J.5
  • 55
    • 0032077168 scopus 로고    scopus 로고
    • Thermodynamic stability of bovine alpha-crystallin in its interactions with other bovine crystallins
    • Bettelheim FA, Clen A. Thermodynamic stability of bovine alpha-crystallin in its interactions with other bovine crystallins. Int J Biol Macromol 1998;22:247-252.
    • (1998) Int J Biol Macromol , vol.22 , pp. 247-252
    • Bettelheim, F.A.1    Clen, A.2


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