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Volumn 43, Issue 10, 2002, Pages 3265-3272

Enhanced C-terminal truncation of αA- and αB-crystallins in diabetic lenses

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA CRYSTALLIN; BETA CRYSTALLIN; CALPAIN;

EID: 0036784934     PISSN: 01460404     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (68)

References (61)
  • 1
    • 0016706399 scopus 로고
    • Changes in proteins of the human lens in development and aging
    • Dilley KJ, Harding JJ. Changes in proteins of the human lens in development and aging. Biochim Biophys Acta. 1975;386:391-408.
    • (1975) Biochim Biophys Acta , vol.386 , pp. 391-408
    • Dilley, K.J.1    Harding, J.J.2
  • 2
    • 0028023344 scopus 로고
    • Structure and modifications of the junior chaperone alpha-crystallin: From lens transparency to molecular pathology
    • Groenen PJ, Merck KB, de Jong WW, Bloemendal H. Structure and modifications of the junior chaperone alpha-crystallin: from lens transparency to molecular pathology. Eur J Biochem. 1994;225: 1-19.
    • (1994) Eur J Biochem , vol.225 , pp. 1-19
    • Groenen, P.J.1    Merck, K.B.2    De Jong, W.W.3    Bloemendal, H.4
  • 3
    • 0026483279 scopus 로고
    • Alpha-crystallin can function as a molecular chaperone
    • Horwitz J. Alpha-crystallin can function as a molecular chaperone. Proc Natl Acad Sci USA. 1992;89:10449-10453.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 10449-10453
    • Horwitz, J.1
  • 4
    • 0028282965 scopus 로고
    • The chaperone activity of bovine alpha-crystallin: Interaction with other lens crystallins in native and denatured states
    • Wang K, Spector A. The chaperone activity of bovine alpha-crystallin: interaction with other lens crystallins in native and denatured states. J Biol Chem. 1994;269:13601-13608.
    • (1994) J Biol Chem , vol.269 , pp. 13601-13608
    • Wang, K.1    Spector, A.2
  • 5
    • 0027973129 scopus 로고
    • Chaperone-like activity and quaternary structure of alpha-crystallin
    • Raman B, Rao CM. Chaperone-like activity and quaternary structure of alpha-crystallin. J Biol Chem. 1994;269:27264-27268.
    • (1994) J Biol Chem , vol.269 , pp. 27264-27268
    • Raman, B.1    Rao, C.M.2
  • 6
    • 0028988412 scopus 로고
    • Interaction of alpha-crystallin with spin-labeled peptides
    • Farahbakhsh ZT, Huang QL, Ding LL, et al. Interaction of alpha-crystallin with spin-labeled peptides. Biochemistry. 1995;34:509-516.
    • (1995) Biochemistry , vol.34 , pp. 509-516
    • Farahbakhsh, Z.T.1    Huang, Q.L.2    Ding, L.L.3
  • 7
    • 0029124685 scopus 로고
    • Temperature-induced exposure of hydrophobic surfaces and its effect on the chaperone activity of alpha-crystallin
    • Das KP, Surewicz WK. Temperature-induced exposure of hydrophobic surfaces and its effect on the chaperone activity of alpha-crystallin. FEBS Lett. 1995;369:321-325.
    • (1995) FEBS Lett , vol.369 , pp. 321-325
    • Das, K.P.1    Surewicz, W.K.2
  • 8
    • 0027391629 scopus 로고
    • Small heat shock proteins are molecular chaperones
    • Jakob U, Gaestel M, Engel K, Buchner J. Small heat shock proteins are molecular chaperones. J Biol Chem. 1993;268:1517-1520.
    • (1993) J Biol Chem , vol.268 , pp. 1517-1520
    • Jakob, U.1    Gaestel, M.2    Engel, K.3    Buchner, J.4
  • 9
    • 0034141214 scopus 로고    scopus 로고
    • Alpha-crystallin assists the renaturation of glyceraldehyde-3-phosphate dehydrogenase
    • Ganea E, Harding JJ. Alpha-crystallin assists the renaturation of glyceraldehyde-3-phosphate dehydrogenase. Biochem J. 2000;345: 467-472.
    • (2000) Biochem J , vol.345 , pp. 467-472
    • Ganea, E.1    Harding, J.J.2
  • 10
    • 0035504258 scopus 로고    scopus 로고
    • Unfolding and refolding of a quinone oxidoreductase: Alpha-crystallin, a molecular chaperone, assists its reactivation
    • Goenka S, Raman B, Ramakrishnan T, Rao CM. Unfolding and refolding of a quinone oxidoreductase: alpha-crystallin, a molecular chaperone, assists its reactivation. Biochem J. 2001;359:547-556.
    • (2001) Biochem J , vol.359 , pp. 547-556
    • Goenka, S.1    Raman, B.2    Ramakrishnan, T.3    Rao, C.M.4
  • 11
    • 0016778248 scopus 로고
    • The amino acid sequence of the A chain of human alpha-crystallin
    • de Jong WW, Terwindt EC, Bloemendal H. The amino acid sequence of the A chain of human alpha-crystallin. FEBS Lett. 1975; 58:310-313.
    • (1975) FEBS Lett , vol.58 , pp. 310-313
    • De Jong, W.W.1    Terwindt, E.C.2    Bloemendal, H.3
  • 12
    • 0024989296 scopus 로고
    • Human alphaB-crystallin gene and preferential promoter function in lens
    • Dubin RA, Ally AH, Chung S, Piatigorsky J. Human alphaB-crystallin gene and preferential promoter function in lens. Genomics. 1990; 7:594-601.
    • (1990) Genomics , vol.7 , pp. 594-601
    • Dubin, R.A.1    Ally, A.H.2    Chung, S.3    Piatigorsky, J.4
  • 13
    • 0017287697 scopus 로고
    • Human alpha-crystallin. I: The isolation and characterization of newly synthesized alpha-crystallin
    • Spector A, Stauffer J, Roy D, Li KK, Adams D. Human alpha-crystallin. I: the isolation and characterization of newly synthesized alpha-crystallin. Invest Ophthalmol Vis Sci. 1976;15:288-296.
    • (1976) Invest Ophthalmol Vis Sci , vol.15 , pp. 288-296
    • Spector, A.1    Stauffer, J.2    Roy, D.3    Li, K.K.4    Adams, D.5
  • 14
    • 0002985024 scopus 로고
    • Evolution of lens and crystallins
    • Bloemendal B, Bloemendal H, eds. New York: John Wiley and Sons
    • de Jong WW. Evolution of lens and crystallins. In: Bloemendal B, Bloemendal H, eds. Molecular and Cellular Biology of the Eye Lens. New York: John Wiley and Sons; 1981:221-278.
    • (1981) Molecular and Cellular Biology of the Eye Lens , pp. 221-278
    • De Jong, W.W.1
  • 15
    • 0025903667 scopus 로고
    • Reverse-phase HPLC analysis of human alpha-crystallin
    • Swamy MS, Abraham EC. Reverse-phase HPLC analysis of human alpha-crystallin. Curr Eye Res. 1991;10:213-220.
    • (1991) Curr Eye Res , vol.10 , pp. 213-220
    • Swamy, M.S.1    Abraham, E.C.2
  • 18
    • 0028216737 scopus 로고
    • Posttranslational modifications of water-soluble human lens crystallins from young adults
    • Miesbauer LR, Zhou X, Yang Z, Sun Y, Smith DL, Smith JB. Posttranslational modifications of water-soluble human lens crystallins from young adults. J Biol Chem. 1994;269:12494-12502.
    • (1994) J Biol Chem , vol.269 , pp. 12494-12502
    • Miesbauer, L.R.1    Zhou, X.2    Yang, Z.3    Sun, Y.4    Smith, D.L.5    Smith, J.B.6
  • 19
    • 0033558894 scopus 로고    scopus 로고
    • The mechanisms of simultaneous stereoinversion, racemization, and isomerization at specific aspartyl residues of aged lens proteins
    • Fujii N, Momose Y, Ishii N, Takita M, Akaboshi M, Kodama M. The mechanisms of simultaneous stereoinversion, racemization, and isomerization at specific aspartyl residues of aged lens proteins. Mech Ageing Dev. 1999;107:347-358.
    • (1999) Mech Ageing Dev , vol.107 , pp. 347-358
    • Fujii, N.1    Momose, Y.2    Ishii, N.3    Takita, M.4    Akaboshi, M.5    Kodama, M.6
  • 20
    • 0028218937 scopus 로고
    • Simultaneous racemization and isomerization at specific aspartic acid residues in alpha B-crystallin from the aged human lens
    • Fujii N, Ishibashi Y, Satoh K, Fujino M, Harada K. Simultaneous racemization and isomerization at specific aspartic acid residues in alpha B-crystallin from the aged human lens. Biochim Biophys Acta. 1994;1204:157-163.
    • (1994) Biochim Biophys Acta , vol.1204 , pp. 157-163
    • Fujii, N.1    Ishibashi, Y.2    Satoh, K.3    Fujino, M.4    Harada, K.5
  • 21
    • 0029144240 scopus 로고
    • Identification of the in vivo truncation sites at the C-terminal region of alpha-A crystallin from aged bovine and human lens
    • Takemoto LJ. Identification of the in vivo truncation sites at the C-terminal region of alpha-A crystallin from aged bovine and human lens. Curr Eye Res. 1995;14:837-841.
    • (1995) Curr Eye Res , vol.14 , pp. 837-841
    • Takemoto, L.J.1
  • 22
    • 0032699590 scopus 로고    scopus 로고
    • Increased cleavage of the C-terminal serine from alpha-A crystallin present in the high molecular weight aggregate fraction from human and bovine lenses
    • Takemoto L. Increased cleavage of the C-terminal serine from alpha-A crystallin present in the high molecular weight aggregate fraction from human and bovine lenses. Curr Eye Res. 1999;19: 450-455.
    • (1999) Curr Eye Res , vol.19 , pp. 450-455
    • Takemoto, L.1
  • 23
    • 0031566251 scopus 로고    scopus 로고
    • Cleavage of amino acid residue(s) from the N-terminal region of alpha A- and alpha B-crystallins in human crystalline lens during aging
    • Kamei A, Iwase H, Masuda K. Cleavage of amino acid residue(s) from the N-terminal region of alpha A- and alpha B-crystallins in human crystalline lens during aging. Biochem Biophys Res Commun. 1997;231:373-378.
    • (1997) Biochem Biophys Res Commun , vol.231 , pp. 373-378
    • Kamei, A.1    Iwase, H.2    Masuda, K.3
  • 24
    • 0029020964 scopus 로고
    • Glutathione adducts, not carbamylated lysines, are the major modification of lens alpha-crystallins from renal failure patients
    • Smith JB, Shun-Shin GA, Sun Y, et al. Glutathione adducts, not carbamylated lysines, are the major modification of lens alpha-crystallins from renal failure patients. J Protein Chem. 1995;14: 179-188.
    • (1995) J Protein Chem , vol.14 , pp. 179-188
    • Smith, J.B.1    Shun-Shin, G.A.2    Sun, Y.3
  • 25
    • 0028960435 scopus 로고
    • Analysis of normal human fetal eye lens crystallins by high-performance liquid chromatography/mass spectrometry
    • He S, Pan S, Wu K, Amster J, Orlando R. Analysis of normal human fetal eye lens crystallins by high-performance liquid chromatography/mass spectrometry. J Mass Spectrom. 1995;30:424-431.
    • (1995) J Mass Spectrom , vol.30 , pp. 424-431
    • He, S.1    Pan, S.2    Wu, K.3    Amster, J.4    Orlando, R.5
  • 26
    • 0029992808 scopus 로고    scopus 로고
    • Differential phosphorylation of alpha-A crystallin in human lens of different age
    • Takemoto LJ. Differential phosphorylation of 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
  • 27
    • 0026777029 scopus 로고
    • Oxidation of the N-terminal methionine of lens alpha-A crystallin
    • Takemoto L, Horwitz J, Emmons T. Oxidation of the N-terminal methionine of lens alpha-A crystallin. Curr Eye Res. 1992;11:651-655.
    • (1992) Curr Eye Res , vol.11 , pp. 651-655
    • Takemoto, L.1    Horwitz, J.2    Emmons, T.3
  • 28
    • 0030296072 scopus 로고    scopus 로고
    • Increase in the intramolecular disulfide bonding of alphaA-crystallin during aging of human lens
    • Takemoto L. Increase in the intramolecular disulfide bonding of alphaA-crystallin during aging of human lens. Exp Eye Res. 1996; 63:585-590.
    • (1996) Exp Eye Res , vol.63 , pp. 585-590
    • Takemoto, L.1
  • 29
    • 0030811288 scopus 로고    scopus 로고
    • Identification of hydrogen peroxide oxidation sites of alpha A- and alpha B-crystallins
    • Smith JB, Jiang X, Abraham EC. Identification of hydrogen peroxide oxidation sites of alpha A- and alpha B-crystallins. Free Radic Res. 1997;26:103-111.
    • (1997) Free Radic Res , vol.26 , pp. 103-111
    • Smith, J.B.1    Jiang, X.2    Abraham, E.C.3
  • 30
    • 0032878640 scopus 로고    scopus 로고
    • Intrapolypeptide disulfides in human alphaA-crystallin and their effect on chaperone-like function
    • Cherian-Shaw M, Smith JB, Jiang XY, Abraham EC. Intrapolypeptide disulfides in human alphaA-crystallin and their effect on chaperone-like function. Mol Cell Biochem. 1999;199:163-167.
    • (1999) Mol Cell Biochem , vol.199 , pp. 163-167
    • Cherian-Shaw, M.1    Smith, J.B.2    Jiang, X.Y.3    Abraham, E.C.4
  • 32
    • 0031745913 scopus 로고    scopus 로고
    • In vivo acetylation identified at lysine 70 of human lens alphaA-crystallin
    • Lin PP, Barry RC, Smith DL, Smith JB. In vivo acetylation identified at lysine 70 of human lens alphaA-crystallin. Protein Sci. 1998;7: 1451-1457.
    • (1998) Protein Sci , vol.7 , pp. 1451-1457
    • Lin, P.P.1    Barry, R.C.2    Smith, D.L.3    Smith, J.B.4
  • 33
    • 0035008831 scopus 로고    scopus 로고
    • In vivo carbamylation and acetylation of water-soluble human lens alphaB-crystallin lysine 92
    • Lapko VN, Smith DL, Smith JB. In vivo carbamylation and acetylation of water-soluble human lens alphaB-crystallin lysine 92. Protein Sci. 2001;10:1130-1136.
    • (2001) Protein Sci , vol.10 , pp. 1130-1136
    • Lapko, V.N.1    Smith, D.L.2    Smith, J.B.3
  • 34
    • 0024376778 scopus 로고
    • The Maillard reaction in aging, diabetes and nutrition
    • Monnier M. The Maillard reaction in aging, diabetes and nutrition. Prog Clin Biol Res. 1989;304:1-22.
    • (1989) Prog Clin Biol Res , vol.304 , pp. 1-22
    • Monnier, M.1
  • 35
    • 0027980444 scopus 로고
    • Site selectivity in the glycation of alpha A- and alpha B-crystallins by glucose
    • Abraham EC, Cherian M, Smith JB. Site selectivity in the glycation of alpha A- and alpha B-crystallins by glucose. Biochem Biophys Res Commun. 1994;201:1451-1456.
    • (1994) Biochem Biophys Res Commun , vol.201 , pp. 1451-1456
    • Abraham, E.C.1    Cherian, M.2    Smith, J.B.3
  • 36
    • 0030450279 scopus 로고    scopus 로고
    • Isoelectric focusing of crystallins in microsections of calf and adult bovine lens: Identification of water-insoluble crystallins complexing under nondenaturing conditions: Demonstration of chaperone activity of alpha-crystallin
    • Babizhayev MA, Bours J, Utikal KJ. Isoelectric focusing of crystallins in microsections of calf and adult bovine lens: identification of water-insoluble crystallins complexing under nondenaturing conditions: demonstration of chaperone activity of alpha-crystallin. Ophthalmic Res. 1996;28:365-374.
    • (1996) Ophthalmic Res , vol.28 , pp. 365-374
    • Babizhayev, M.A.1    Bours, J.2    Utikal, K.J.3
  • 37
    • 0023232589 scopus 로고
    • Lens protein composition, glycation and high molecular weight aggregation in aging rats
    • Swamy MS, Abraham EC. Lens protein composition, glycation and high molecular weight aggregation in aging rats. Invest Ophthalmol Vis Sci. 1987;28:1693-1701.
    • (1987) Invest Ophthalmol Vis Sci , vol.28 , pp. 1693-1701
    • Swamy, M.S.1    Abraham, E.C.2
  • 38
    • 0029085624 scopus 로고
    • Diabetes affects α-crystallin chaperone function
    • Cherian M, Abraham EC. Diabetes affects α-crystallin chaperone function. Biochem Biophys Res Commun. 1995;212:184-189.
    • (1995) Biochem Biophys Res Commun , vol.212 , pp. 184-189
    • Cherian, M.1    Abraham, E.C.2
  • 39
    • 0028899440 scopus 로고
    • Decreased molecular chaperone property of alpha-crystallins due to posttranslational modifications
    • Cherian M, Abraham EC. Decreased molecular chaperone property of alpha-crystallins due to posttranslational modifications. Biochem Biophys Res Commun. 1995;208:675-679.
    • (1995) Biochem Biophys Res Commun , vol.208 , pp. 675-679
    • Cherian, M.1    Abraham, E.C.2
  • 40
    • 0036191135 scopus 로고    scopus 로고
    • Alpha-crystallin function in diabetic rat and human lenses
    • Thampi P, Zarina S, Abraham EC. Alpha-crystallin function in diabetic rat and human lenses. Mol Cell Biochem. 2002;229:113-118.
    • (2002) Mol Cell Biochem , vol.229 , pp. 113-118
    • Thampi, P.1    Zarina, S.2    Abraham, E.C.3
  • 41
    • 0030670158 scopus 로고    scopus 로고
    • Influence of proteinglutathione mixed disulfide on the chaperone-like function of alpha-crystallin
    • Cherian M, Smith JB, Jiang XY, Abraham EC. Influence of proteinglutathione mixed disulfide on the chaperone-like function of alpha-crystallin. J Biol Chem. 1997;272:29099-29103.
    • (1997) J Biol Chem , vol.272 , pp. 29099-29103
    • Cherian, M.1    Smith, J.B.2    Jiang, X.Y.3    Abraham, E.C.4
  • 42
    • 0031889967 scopus 로고    scopus 로고
    • Quantitation of specific cleavage sites at the C-terminal region of alpha-A crystallin from human lenses of different age
    • Takemoto LJ. Quantitation of specific cleavage sites at the C-terminal region of alpha-A crystallin from human lenses of different age. Exp Eye Res. 1998;66:263-266.
    • (1998) Exp Eye Res , vol.66 , pp. 263-266
    • Takemoto, L.J.1
  • 43
    • 0023214514 scopus 로고
    • Progressive changes in lens crystallin glycation and high-molecular-weight aggregate formation leading to cataract development in streptozotocin-diabetic rats
    • Perry RE, Swamy MS, Abraham EC. Progressive changes in lens crystallin glycation and high-molecular-weight aggregate formation leading to cataract development in streptozotocin-diabetic rats. Exp Eye Res. 1987;44:269-282.
    • (1987) Exp Eye Res , vol.44 , pp. 269-282
    • Perry, R.E.1    Swamy, M.S.2    Abraham, E.C.3
  • 44
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970;227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 45
    • 0016256467 scopus 로고
    • Intracellular degradation of alpha-crystallin: Fractionation and characterization of degraded alpha A-chains
    • van Kleef FS, Nijzink-Maas MJ, Hoenders HJ. Intracellular degradation of alpha-crystallin: fractionation and characterization of degraded alpha A-chains. Eur J Biochem. 1974;48:563-570.
    • (1974) Eur J Biochem , vol.48 , pp. 563-570
    • Van Kleef, F.S.1    Nijzink-Maas, M.J.2    Hoenders, H.J.3
  • 46
    • 0017122111 scopus 로고
    • Intracellular degradation and deamidation of alpha-crystallin subunits
    • van Kleef SM, Willems-Thijssen W, Hoenders HJ. Intracellular degradation and deamidation of alpha-crystallin subunits. Eur J Biochem. 1976;66:477-483.
    • (1976) Eur J Biochem , vol.66 , pp. 477-483
    • Van Kleef, S.M.1    Willems-Thijssen, W.2    Hoenders, H.J.3
  • 47
    • 0018243862 scopus 로고
    • The quaternary structure of bovine alpha-crystallin: Surface probing by limited proteolysis in vitro
    • Siezen RJ, Hoenders HJ. The quaternary structure of bovine alpha-crystallin: surface probing by limited proteolysis in vitro. Eur J Biochem. 1979;96:431-440.
    • (1979) Eur J Biochem , vol.96 , pp. 431-440
    • Siezen, R.J.1    Hoenders, H.J.2
  • 48
    • 0010439488 scopus 로고    scopus 로고
    • Mass measurements of C-terminally truncated α-crystallins from two-dimensional gel identifies Lp82 as a major rat lens endopeptidase
    • In press
    • Ueda Y, Fukiage C, Shih M, Shearer TR, David LL. Mass measurements of C-terminally truncated α-crystallins from two-dimensional gel identifies Lp82 as a major rat lens endopeptidase. Mol Cell Prot. In press.
    • Mol Cell Prot
    • Ueda, Y.1    Fukiage, C.2    Shih, M.3    Shearer, T.R.4    David, L.L.5
  • 50
    • 0030475908 scopus 로고    scopus 로고
    • Modifications of the water-insoluble human lens alpha-crystallins
    • Lund AL, Smith JB, Smith DL. Modifications of the water-insoluble human lens alpha-crystallins. Exp Eye Res. 1996;63:661-672.
    • (1996) Exp Eye Res , vol.63 , pp. 661-672
    • Lund, A.L.1    Smith, J.B.2    Smith, D.L.3
  • 51
    • 0343289311 scopus 로고    scopus 로고
    • Identification of new lens protease(s) using peptide substrates having in vivo cleavage sites
    • Sharma KK, Kester K, Elser N. Identification of new lens protease(s) using peptide substrates having in vivo cleavage sites. Biochem Biophys Res Commun. 1996;218:365-370.
    • (1996) Biochem Biophys Res Commun , vol.218 , pp. 365-370
    • Sharma, K.K.1    Kester, K.2    Elser, N.3
  • 52
    • 0033527449 scopus 로고    scopus 로고
    • An atypical form of alphaB-crystallin is present in high concentration in some human cataractous lenses. Identification and characterization of aberrant N- and C-terminal processing
    • Jimenez-Asensio J, Colvis CM, Kowalak JA, et al. An atypical form of alphaB-crystallin is present in high concentration in some human cataractous lenses. Identification and characterization of aberrant N- and C-terminal processing. J Biol Chem. 1999;274: 32287-32294.
    • (1999) J Biol Chem , vol.274 , pp. 32287-32294
    • Jimenez-Asensio, J.1    Colvis, C.M.2    Kowalak, J.A.3
  • 53
    • 0033948884 scopus 로고    scopus 로고
    • Tracking pathology with proteomics: Identification of in vivo degradation products of alphaB-crystallin
    • Colvis CM, Duglas-Tabor Y, Werth KB, et al. Tracking pathology with proteomics: identification of in vivo degradation products of alphaB-crystallin. Electrophoresis. 2000;21:2219-2227.
    • (2000) Electrophoresis , vol.21 , pp. 2219-2227
    • Colvis, C.M.1    Duglas-Tabor, Y.2    Werth, K.B.3
  • 54
    • 0030933472 scopus 로고    scopus 로고
    • Conformational and functional differences between recombinant human lens alphaA- and alphaB-crystallin
    • Sun TX, Das BK, Liang JJ. Conformational and functional differences between recombinant human lens alphaA- and alphaB-crystallin. J Biol Chem. 1997;272:6220-6225.
    • (1997) J Biol Chem , vol.272 , pp. 6220-6225
    • Sun, T.X.1    Das, B.K.2    Liang, J.J.3
  • 55
    • 0034681446 scopus 로고    scopus 로고
    • Temperature-dependent chaperone activity and structural properties of human alphaA- and alphaB-crystallins
    • Reddy GB, Das KP, Petrash JM, Surewicz WK. Temperature-dependent chaperone activity and structural properties of human alphaA- and alphaB-crystallins. J Biol Chem. 2000;275:4565-4570.
    • (2000) J Biol Chem , vol.275 , pp. 4565-4570
    • Reddy, G.B.1    Das, K.P.2    Petrash, J.M.3    Surewicz, W.K.4
  • 56
    • 0035032876 scopus 로고    scopus 로고
    • Argpyrimidine, a blue fluorophore in human lens proteins: High levels in brunescent cataractous lenses
    • Padayatti PS, Ng AS, Uchida K, Glomb MA, Nagaraj RH. Argpyrimidine, a blue fluorophore in human lens proteins: high levels in brunescent cataractous lenses. Invest Ophthalmol Vis Sci. 2001; 42:1299-1304.
    • (2001) Invest Ophthalmol Vis Sci , vol.42 , pp. 1299-1304
    • Padayatti, P.S.1    Ng, A.S.2    Uchida, K.3    Glomb, M.A.4    Nagaraj, R.H.5
  • 57
    • 0035834748 scopus 로고    scopus 로고
    • Amides are novel protein modifications formed by physiological sugars
    • Glomb MA, Pfahler C. Amides are novel protein modifications formed by physiological sugars. J Biol Chem. 2001;276:41638-41647.
    • (2001) J Biol Chem , vol.276 , pp. 41638-41647
    • Glomb, M.A.1    Pfahler, C.2
  • 58
    • 0033829222 scopus 로고    scopus 로고
    • The major in vivo modifications of the human water-insoluble lens crystallins are disulfide bonds, deamidation, methionine oxidation and backbone cleavage
    • Hanson SR, Hasan A, Smith DL, Smith JB. The major in vivo modifications of the human water-insoluble lens crystallins are disulfide bonds, deamidation, methionine oxidation and backbone cleavage. Exp Eye Res. 2000;71:195-207.
    • (2000) Exp Eye Res , vol.71 , pp. 195-207
    • Hanson, S.R.1    Hasan, A.2    Smith, D.L.3    Smith, J.B.4
  • 59
    • 0027217891 scopus 로고
    • α-crystallin chaperone activity is reduced by calpain II in vitro and in selenite cataract
    • Kelly MJ, David LL, Iwasaki N, Wright J, Shearer TR. α-Crystallin chaperone activity is reduced by calpain II in vitro and in selenite cataract. J Biol Chem. 1993;268:18844-18849.
    • (1993) J Biol Chem , vol.268 , pp. 18844-18849
    • Kelly, M.J.1    David, L.L.2    Iwasaki, N.3    Wright, J.4    Shearer, T.R.5
  • 60
    • 0010476684 scopus 로고    scopus 로고
    • Truncation of C-terminal serine of human αA-crystallin results in decreased chaperone activity
    • Thampi P, Abraham E. Truncation of C-terminal serine of human αA-crystallin results in decreased chaperone activity. ARVO Abstract. 2002:B544.
    • (2002) ARVO Abstract
    • Thampi, P.1    Abraham, E.2
  • 61
    • 0010513829 scopus 로고    scopus 로고
    • C-terminal truncation of five amino acid residues of αB-crystallin influences its chaperone function
    • Cho W, Abraham E. C-terminal truncation of five amino acid residues of αB-crystallin influences its chaperone function. ARVO Abstract. 2002;B545.
    • (2002) ARVO Abstract
    • Cho, W.1    Abraham, E.2


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