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Volumn 7, Issue , 2001, Pages 228-233

Heat-induced quaternary transitions in hetero- and homo-polymers of α-crystallin

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA CRYSTALLIN; CHAPERONE; POLYMER;

EID: 0346527362     PISSN: 10900535     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (24)

References (30)
  • 1
    • 0002985024 scopus 로고
    • Evolution of lens and crystallins
    • Bloemendal H, editor. New York: Wiley
    • de Jong WW. Evolution of lens and crystallins. In: Bloemendal H, editor. Molecular and cellular biology of the eye lens. New York: Wiley; 1981. p. 221-78.
    • (1981) Molecular and Cellular Biology of the Eye Lens , pp. 221-278
    • de Jong, W.W.1
  • 3
    • 0024578954 scopus 로고
    • Alpha B subunit of lens-specific protein alpha-crystallin is present in other ocular and non-ocular tissues
    • Bhat SP, Nagineni CN. alpha B subunit of lens-specific protein alpha-crystallin is present in other ocular and non-ocular tissues. Biochem Biophys Res Commun 1989; 158:319-25.
    • (1989) Biochem. Biophys. Res. Commun. , vol.158 , pp. 319-325
    • Bhat, S.P.1    Nagineni, C.N.2
  • 4
    • 0026040828 scopus 로고
    • Immunoreactive alpha A crystallin in rat non-lenticular tissues detected with a sensitive immunoassay method
    • 1080
    • Kato K, Shinohara H, Kurobe N, Goto S, Inaguma Y, Ohshima K. Immunoreactive alpha A crystallin in rat non-lenticular tissues detected with a sensitive immunoassay method. Biochim Biophys Acta 1991; 1080:173-80.
    • (1991) Biochim. Biophys. Acta , pp. 173-180
    • Kato, K.1    Shinohara, H.2    Kurobe, N.3    Goto, S.4    Inaguma, Y.5    Ohshima, K.6
  • 5
    • 0020063988 scopus 로고
    • Four small Drosophila heat shock proteins are related to each other and to mammalian alpha-crystallin
    • Ingolia TD, Craig EA. Four small Drosophila heat shock proteins are related to each other and to mammalian alpha-crystallin. Proc Natl Acad Sci U S A 1982; 79:2360-4.
    • (1982) Proc. Natl. Acad. Sci. U S A , vol.79 , pp. 2360-2364
    • Ingolia, T.D.1    Craig, E.A.2
  • 6
    • 0028045077 scopus 로고
    • Alpha-Crystallin: Chaperoning and aggregation
    • Crabbe MJ, Goode D. alpha-Crystallin: chaperoning and aggregation. Biochem J 1994; 297:653-4.
    • (1994) Biochem. J. , vol.297 , pp. 653-654
    • Crabbe, M.J.1    Goode, D.2
  • 7
    • 0025117557 scopus 로고
    • Evolution of a protein superfamily: Relationships between vertebrate lens crystallins and microorganism dormancy proteins
    • Wistow G. Evolution of a protein superfamily: relationships between vertebrate lens crystallins and microorganism dormancy proteins. J Mol Evol 1990; 30:140-5.
    • (1990) J. Mol. Evol. , vol.30 , pp. 140-145
    • Wistow, G.1
  • 8
    • 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 U S A 1992; 89:10449-53.
    • (1992) Proc. Natl. Acad. Sci. U S A , vol.89 , pp. 10449-10453
    • Horwitz, J.1
  • 9
    • 0028293240 scopus 로고
    • Characterization of the alpha-gamma and alpha-beta complex: Evidence for an in vivo functional role of alpha-crystallin as a molecular chaperone
    • Boyle D, Takemoto L. Characterization of the alpha-gamma and alpha-beta complex: evidence for an in vivo functional role of alpha-crystallin as a molecular chaperone. Exp Eye Res 1994; 58:9-15.
    • (1994) Exp. Eye Res. , vol.58 , pp. 9-15
    • Boyle, D.1    Takemoto, L.2
  • 10
    • 0028973109 scopus 로고
    • Evidence that alpha-crystallin prevents non-specific protein aggregation in the intact eye lens
    • 1245
    • Rao PV, Huang QL, Horwitz J, Zigler JS Jr. Evidence that alpha-crystallin prevents non-specific protein aggregation in the intact eye lens. Biochim Biophys Acta 1995; 1245:439-47.
    • (1995) Biochim. Biophys. Acta , pp. 439-447
    • Rao, P.V.1    Huang, Q.L.2    Horwitz, J.3    Zigler J.S., Jr.4
  • 11
    • 0032407709 scopus 로고    scopus 로고
    • Studies of the denaturation patterns of bovine alpha-crystallin using an ionic denaturant, guanidine hydrochloride and a non-ionic denaturant, urea
    • Doss-Pepe EW, Carew EL, Koretz JF. Studies of the denaturation patterns of bovine alpha-crystallin using an ionic denaturant, guanidine hydrochloride and a non-ionic denaturant, urea. Exp Eye Res 1998; 67:657-79.
    • (1998) Exp. Eye Res. , vol.67 , pp. 657-679
    • Doss-Pepe, E.W.1    Carew, E.L.2    Koretz, J.F.3
  • 12
    • 0030891712 scopus 로고    scopus 로고
    • Heat-induced conformational change and increased chaperone activity of lens alpha-crystallin
    • Das BK, Liang JJ, Chakrabarti B. Heat-induced conformational change and increased chaperone activity of lens alpha-crystallin. Curr Eye Res 1997; 16:303-9.
    • (1997) Curr. Eye Res. , vol.16 , pp. 303-309
    • Das, B.K.1    Liang, J.J.2    Chakrabarti, B.3
  • 13
    • 0342960792 scopus 로고    scopus 로고
    • Relationship between molecular weight and hydrodynamic radius during heat-induced aggregation of recombinant human αA and αB crystallin
    • Thurston GM, Sun TX, Liang JN. Relationship between molecular weight and hydrodynamic radius during heat-induced aggregation of recombinant human αA and αB crystallin. Invest Ophthalmol Vis Sci 1998; 39:S870.
    • (1998) Invest. Ophthalmol. Vis. Sci. , vol.39
    • Thurston, G.M.1    Sun, T.X.2    Liang, J.N.3
  • 14
    • 0346633845 scopus 로고    scopus 로고
    • Quaternary structural changes in native bovine alpha-crystallin aggregates with temperature
    • Koretz JF. Quaternary structural changes in native bovine alpha-crystallin aggregates with temperature. Invest Ophthalmol Vis Sci 1999; 40:S2.
    • (1999) Invest. Ophthalmol. Vis. Sci. , vol.40
    • Koretz, J.F.1
  • 15
    • 0034673329 scopus 로고    scopus 로고
    • Correlation between the chaperone-like activity and aggregate size of alpha-crystallin with increasing temperature
    • Burgio MR, Kim CJ, Dow CC, Koretz JF. Correlation between the chaperone-like activity and aggregate size of alpha-crystallin with increasing temperature. Biochem Biophys Res Commun 2000; 268:426-32.
    • (2000) Biochem. Biophys. Res. Commun. , vol.268 , pp. 426-432
    • Burgio, M.R.1    Kim, C.J.2    Dow, C.C.3    Koretz, J.F.4
  • 16
    • 26144451500 scopus 로고    scopus 로고
    • Characterization of the heat-induced quaternary transition of α-crystallin aggregates
    • Burgio MR, Kim CJ, Koretz JF. Characterization of the heat-induced quaternary transition of α-crystallin aggregates. Invest Ophthalmol Vis Sci 2000; 41:S581.
    • (2000) Invest. Ophthalmol. Vis. Sci. , vol.41
    • Burgio, M.R.1    Kim, C.J.2    Koretz, J.F.3
  • 17
    • 0031577451 scopus 로고    scopus 로고
    • Effect of heat-induced structural perturbation of secondary and tertiary structures on the chaperone activity of alpha-crystallin
    • Lee JS, Satoh T, Shinoda H, Samejima T, Wu SH, Chiou SH. Effect of heat-induced structural perturbation of secondary and tertiary structures on the chaperone activity of alpha-crystallin. Biochem Biophys Res Commun 1997; 237:277-82.
    • (1997) Biochem. Biophys. Res. Commun. , vol.237 , pp. 277-282
    • Lee, J.S.1    Satoh, T.2    Shinoda, H.3    Samejima, T.4    Wu, S.H.5    Chiou, S.H.6
  • 18
    • 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; 275:4565-70.
    • (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
  • 19
    • 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; 369:321-5.
    • (1995) FEBS Lett. , vol.369 , pp. 321-325
    • Das, K.P.1    Surewicz, W.K.2
  • 20
    • 0021046687 scopus 로고
    • Alpha m-Crystallin: The native form of the protein?
    • Thomson JA, Augusteyn RC. alpha m-Crystallin: the native form of the protein? Exp Eye Res 1983; 37:367-77.
    • (1983) Exp. Eye Res. , vol.37 , pp. 367-377
    • Thomson, J.A.1    Augusteyn, R.C.2
  • 21
    • 0023178690 scopus 로고
    • Isolation of alpha-crystallin subunits by gel filtration
    • Stevens A, Augusteyn RC. Isolation of alpha-crystallin subunits by gel filtration. Curr Eye Res 1987; 6:739-40.
    • (1987) Curr. Eye Res. , vol.6 , pp. 739-740
    • Stevens, A.1    Augusteyn, R.C.2
  • 22
    • 0018790359 scopus 로고
    • Lipoprotein electrophoresis on acrylamide-agarose plates, with discontinuous acrylamide gradient
    • Moulin S, Fruchart JC, Dewailly P, Sezille G. [Lipoprotein electrophoresis on acrylamide-agarose plates, with discontinuous acrylamide gradient]. Clin Chim Acta 1979; 91:159-63.
    • (1979) Clin. Chim. Acta , vol.91 , pp. 159-163
    • Moulin, S.1    Fruchart, J.C.2    Dewailly, P.3    Sezille, G.4
  • 23
    • 0032502739 scopus 로고    scopus 로고
    • Interaction of 1,1′-bi(4-anilino) naphthalene-5,5′-disulfonic acid with alpha-crystallin
    • Sharma KK, Kaur H, Kumar GS, Kester K. Interaction of 1,1′-bi(4-anilino) naphthalene-5,5′-disulfonic acid with alpha-crystallin. J Biol Chem 1998; 273:8965-70.
    • (1998) J. Biol. Chem. , vol.273 , pp. 8965-8970
    • Sharma, K.K.1    Kaur, H.2    Kumar, G.S.3    Kester, K.4
  • 25
    • 0034594704 scopus 로고    scopus 로고
    • Heat-induced conformational change of human lens recombinant alphaA- and alphaB-crystallins
    • Liang JJ, Sun TX, Akhtar NJ. Heat-induced conformational change of human lens recombinant alphaA- and alphaB-crystallins. Mol Vis 2000; 6:10-4 .
    • (2000) Mol. Vis. , vol.6 , pp. 10-14
    • Liang, J.J.1    Sun, T.X.2    Akhtar, N.J.3
  • 26
    • 1342292267 scopus 로고    scopus 로고
    • Crystal structure of a small heat-shock protein
    • Kim KK, Kim R, Kim SH. Crystal structure of a small heat-shock protein. Nature 1998; 394:595-9.
    • (1998) Nature , vol.394 , pp. 595-599
    • Kim, K.K.1    Kim, R.2    Kim, S.H.3
  • 27
    • 0029956553 scopus 로고    scopus 로고
    • Effects of site-directed mutations on the chaperone-like activity of alphaB-crystallin
    • Plater ML, Goode D, Crabbe MJ. Effects of site-directed mutations on the chaperone-like activity of alphaB-crystallin. J Biol Chem 1996; 271:28558-66.
    • (1996) J. Biol. Chem. , vol.271 , pp. 28558-28566
    • Plater, M.L.1    Goode, D.2    Crabbe, M.J.3
  • 29
    • 0031566236 scopus 로고    scopus 로고
    • Analysis of the factors involved in the loss and restoration of the chaperone-like function of alpha-crystallin
    • Koretz JF, Doss EW, Reid GH. Analysis of the factors involved in the loss and restoration of the chaperone-like function of alpha-crystallin. Biochem Biophys Res Commun 1997; 231:270-6.
    • (1997) Biochem. Biophys. Res. Commun. , vol.231 , pp. 270-276
    • Koretz, J.F.1    Doss, E.W.2    Reid, G.H.3
  • 30
    • 0033521012 scopus 로고    scopus 로고
    • Differential temperature-dependent chaperone-like activity of alphaA- and alphaB-crystallin homoaggregates
    • Datta SA, Rao CM. Differential temperature-dependent chaperone-like activity of alphaA- and alphaB-crystallin homoaggregates. J Biol Chem 1999; 274:34773-8.
    • (1999) J. Biol. Chem. , vol.274 , pp. 34773-34778
    • Datta, S.A.1    Rao, C.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.