메뉴 건너뛰기




Volumn 6, Issue 5, 2011, Pages

The thermal structural transition of α-crystallin inhibits the heat induced self-aggregation

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA CRYSTALLIN; CALCIUM;

EID: 79955823896     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0018906     Document Type: Article
Times cited : (14)

References (45)
  • 1
    • 0033968166 scopus 로고    scopus 로고
    • Small heat-shock proteins and their potential role in human disease
    • Clark J, Muchowski P, (2000) Small heat-shock proteins and their potential role in human disease. CurrOpinStructBiol 10: 52-59.
    • (2000) CurrOpinStructBiol , vol.10 , pp. 52-59
    • Clark, J.1    Muchowski, P.2
  • 2
    • 0020678719 scopus 로고
    • Short-range order of crystallin proteins accounts for eye lens transparency
    • Delaye M, Tardieu A, (1983) Short-range order of crystallin proteins accounts for eye lens transparency. Nature 302: 415-417.
    • (1983) Nature , vol.302 , pp. 415-417
    • Delaye, M.1    Tardieu, A.2
  • 3
    • 0028196887 scopus 로고
    • Light scattering by bovine alpha-crystalline proteins in solution: hydrodynamic structure and interparticle interaction
    • Xia J, Aerts T, Donceel K, Clauwaert J, (1994) Light scattering by bovine alpha-crystalline proteins in solution: hydrodynamic structure and interparticle interaction. Biophys Journ 66: 861-872.
    • (1994) Biophys Journ , vol.66 , pp. 861-872
    • Xia, J.1    Aerts, T.2    Donceel, K.3    Clauwaert, J.4
  • 4
    • 0037325497 scopus 로고    scopus 로고
    • Alpha-crystallin
    • Horwitz J, (2003) Alpha-crystallin. Exp eye res 76: 145-153.
    • (2003) Exp Eye Res , vol.76 , pp. 145-153
    • Horwitz, J.1
  • 5
    • 0029986488 scopus 로고    scopus 로고
    • The nucleus of the human lens: demonstration of a highly characteristic protein pattern by two-dimensional electrophoresis and introduction of a new method of lens dissection
    • Garland D, Duglas-Tabor Y, Jimenez-Asensio J, Datiles M, Magno B, (1996) The nucleus of the human lens: demonstration of a highly characteristic protein pattern by two-dimensional electrophoresis and introduction of a new method of lens dissection. ExpEye Res 62: 285-291.
    • (1996) ExpEye Res , vol.62 , pp. 285-291
    • Garland, D.1    Duglas-Tabor, Y.2    Jimenez-Asensio, J.3    Datiles, M.4    Magno, B.5
  • 6
    • 0026787279 scopus 로고
    • Conformational stability of bovine alpha-crystallin. evidence for destabilizing effect of ascorbate
    • Santini S, Mordente A, Meucci E, Miggiano G, Martorana G, (1992) Conformational stability of bovine alpha-crystallin. evidence for destabilizing effect of ascorbate. BiochemJ 287: 107-112.
    • (1992) BiochemJ , vol.287 , pp. 107-112
    • Santini, S.1    Mordente, A.2    Meucci, E.3    Miggiano, G.4    Martorana, G.5
  • 7
    • 0027317391 scopus 로고
    • Nonenzymatic glycation alters protein structure and stability. a study of two eye lens crystallins
    • Luthra M, Balasubramanian D, (1993) Nonenzymatic glycation alters protein structure and stability. a study of two eye lens crystallins. JBiolChem 268: 18119-18127.
    • (1993) JBiolChem , vol.268 , pp. 18119-18127
    • Luthra, M.1    Balasubramanian, D.2
  • 8
    • 0028216737 scopus 로고
    • Post-translational modifications of water-soluble human lens crystallins from young adults
    • Miesbauer LR, Zhou X, Yang Z, Yang Z, Sun Y, et al. (1994) Post-translational modifications of water-soluble human lens crystallins from young adults. JBiolChem 269: 12494-12502.
    • (1994) JBiolChem , vol.269 , pp. 12494-12502
    • Miesbauer, L.R.1    Zhou, X.2    Yang, Z.3    Yang, Z.4    Sun, Y.5
  • 10
    • 0026749942 scopus 로고
    • Hydroxyl radical damage to proteins, with special reference to the crystallins
    • Guptasarma P, Balasubramanian D, Matsugo S, Saito I, (1992) Hydroxyl radical damage to proteins, with special reference to the crystallins. Biochemistry 31: 4296-4303.
    • (1992) Biochemistry , vol.31 , pp. 4296-4303
    • Guptasarma, P.1    Balasubramanian, D.2    Matsugo, S.3    Saito, I.4
  • 11
    • 0032407709 scopus 로고    scopus 로고
    • Studies of the denaturation pattern of bovine alpha-crystallin using an ionic denaturant, guanidine hydrocloride and a non-ionic denaturant, urea
    • Doss-Pepe E, Carew E, Koretz J, (1998) Studies of the denaturation pattern of bovine alpha-crystallin using an ionic denaturant, guanidine hydrocloride and a non-ionic denaturant, urea. Exp Eye Res 67: 657-679.
    • (1998) Exp Eye Res , vol.67 , pp. 657-679
    • Doss-Pepe, E.1    Carew, E.2    Koretz, J.3
  • 12
    • 0038529737 scopus 로고    scopus 로고
    • Subunit exchange demonstrates a differential chaperone activity of calf-alpha crystallin towards beta-low- and individual gamma crystallins
    • Putilina T, Skouri-Panet F, Prat K, Lubsen N, Tardieu A, (2003) Subunit exchange demonstrates a differential chaperone activity of calf-alpha crystallin towards beta-low- and individual gamma crystallins. JBC 278: 13747-13756.
    • (2003) JBC , vol.278 , pp. 13747-13756
    • Putilina, T.1    Skouri-Panet, F.2    Prat, K.3    Lubsen, N.4    Tardieu, A.5
  • 14
    • 0025787736 scopus 로고
    • Micellar subunit assembly in a three-layer model of oligomeric alpha-crystallin
    • Walsh M, Sen A, Chakrabarti B, (1991) Micellar subunit assembly in a three-layer model of oligomeric alpha-crystallin. Journ Biol Chem 266: 20079-20084.
    • (1991) Journ Biol Chem , vol.266 , pp. 20079-20084
    • Walsh, M.1    Sen, A.2    Chakrabarti, B.3
  • 15
    • 0030798628 scopus 로고    scopus 로고
    • Chaperone-like activity and temperature-induced structural changes of alpha-crystallin
    • Raman B, Rao C, (1997) Chaperone-like activity and temperature-induced structural changes of alpha-crystallin. JBC 272: 23559-23564.
    • (1997) JBC , vol.272 , pp. 23559-23564
    • Raman, B.1    Rao, C.2
  • 16
    • 0029034730 scopus 로고
    • Temperature dependent chaperone-like activity of alpha-crystallin
    • Raman B, Ramakrishna T, Rao C, (1995) Temperature dependent chaperone-like activity of alpha-crystallin. FEBS lett pp. 133-136.
    • (1995) FEBS lett , pp. 133-136
    • Raman, B.1    Ramakrishna, T.2    Rao, C.3
  • 17
    • 0027973129 scopus 로고
    • Chaperone-like activity and quaternary structure of alpha-crystalline
    • Raman B, Rao C, (1994) Chaperone-like activity and quaternary structure of alpha-crystalline. JBC 269: 27264-27268.
    • (1994) JBC , vol.269 , pp. 27264-27268
    • Raman, B.1    Rao, C.2
  • 18
    • 11844274723 scopus 로고    scopus 로고
    • The native oligomeric organization of alpha-crystallin, is it necessary for its chaperone function?
    • Horwitz J, Huang Q, Ding L, (2004) The native oligomeric organization of alpha-crystallin, is it necessary for its chaperone function? Exp Eye Res pp. 817-821.
    • (2004) Exp Eye Res , pp. 817-821
    • Horwitz, J.1    Huang, Q.2    Ding, L.3
  • 20
    • 0016439759 scopus 로고
    • On the quatemary structure of high-molecular-weight proteins from the bovine eye lens
    • Kramps HA, Stols ALH, Hoenders HJ, De Groot K, (1975) On the quatemary structure of high-molecular-weight proteins from the bovine eye lens. Eur J Biochem 50: 503-509.
    • (1975) Eur J Biochem , vol.50 , pp. 503-509
    • Kramps, H.A.1    Stols, A.L.H.2    Hoenders, H.J.3    De Groot, K.4
  • 21
    • 0019986765 scopus 로고
    • Identification of the scattering elements responsible for lens opacification in cold cataracts
    • Delaye M, Clark J, Benedek G, (1982) Identification of the scattering elements responsible for lens opacification in cold cataracts. Biophys J 37: 647-656.
    • (1982) Biophys J , vol.37 , pp. 647-656
    • Delaye, M.1    Clark, J.2    Benedek, G.3
  • 22
    • 0003851111 scopus 로고
    • Dynamic light scattering
    • Robert E. Krieger
    • Berne B, Pecora R, (1976) Dynamic light scattering. Robert E. Krieger.
    • (1976)
    • Berne, B.1    Pecora, R.2
  • 23
    • 36849103950 scopus 로고
    • Analysis of macromolecular polydispersity in intensity correlation spectroscopy: the method of cumulants
    • Koppel DE, (1972) Analysis of macromolecular polydispersity in intensity correlation spectroscopy: the method of cumulants. J Chem Phys pp. 4814-4820.
    • (1972) J Chem Phys , pp. 4814-4820
    • Koppel, D.E.1
  • 24
    • 17844382971 scopus 로고    scopus 로고
    • Particle size distribution in dmpc vesicles solutions undergoing different sonication times
    • Maulucci G, De Spirito M, Arcovito G, Boffi F, Congiu Castellano A, et al. (2005) Particle size distribution in dmpc vesicles solutions undergoing different sonication times. BiophysJ 88: 3545-3550.
    • (2005) BiophysJ , vol.88 , pp. 3545-3550
    • Maulucci, G.1    De Spirito, M.2    Arcovito, G.3    Boffi, F.4    Congiu Castellano, A.5
  • 25
    • 0020176708 scopus 로고
    • Contin: a general purpose constrained regularization program for inverting noisy linear algebric and integral equations
    • Provencher S, (1982) Contin: a general purpose constrained regularization program for inverting noisy linear algebric and integral equations. Comp Phys Comm 27: 229-242.
    • (1982) Comp Phys Comm , vol.27 , pp. 229-242
    • Provencher, S.1
  • 26
    • 0003583124 scopus 로고
    • Theory of the stability of lyophobic colloid
    • Amsterdam, Elsevier
    • Verwey E, Overbeek J, (1948) Theory of the stability of lyophobic colloid. Amsterdam Elsevier.
    • (1948)
    • Verwey, E.1    Overbeek, J.2
  • 27
    • 26744434924 scopus 로고
    • Diffusion-limited aggregation
    • Witten T, Sander L, (1983) Diffusion-limited aggregation. PhysRevB 27: 5686-5697.
    • (1983) PhysRevB , vol.27 , pp. 5686-5697
    • Witten, T.1    Sander, L.2
  • 28
    • 4243632346 scopus 로고
    • Diffusion-limited aggregation, a kinetic critical phenomenon
    • Witten T, Sander L, (1981) Diffusion-limited aggregation, a kinetic critical phenomenon. PRL 47: 1400-1403.
    • (1981) PRL , vol.47 , pp. 1400-1403
    • Witten, T.1    Sander, L.2
  • 29
    • 0000223289 scopus 로고
    • Topological properties of diffusion limited aggregation and cluster-cluster aggregation
    • Meakin P, Majid I, Havlin S, Stanley H, (1984) Topological properties of diffusion limited aggregation and cluster-cluster aggregation. JPhysA pp. L975-L981.
    • (1984) JPhysA , pp. 975-981
    • Meakin, P.1    Majid, I.2    Havlin, S.3    Stanley, H.4
  • 30
    • 9644267285 scopus 로고
    • Universal reaction-limited colloid aggregation
    • Lin M, Lindsay H, Weitz D, Ball R, Klein R, et al. (1990) Universal reaction-limited colloid aggregation. PhysRev A 41: 2005-2020.
    • (1990) PhysRev A , vol.41 , pp. 2005-2020
    • Lin, M.1    Lindsay, H.2    Weitz, D.3    Ball, R.4    Klein, R.5
  • 31
    • 0001665043 scopus 로고
    • Limits of the fractal dimension for irreversible kinetic aggregation of gold colloids
    • Weitz D, Huang J, Lin M, Sung J, (1985) Limits of the fractal dimension for irreversible kinetic aggregation of gold colloids. PRL 54: 1416-1419.
    • (1985) PRL , vol.54 , pp. 1416-1419
    • Weitz, D.1    Huang, J.2    Lin, M.3    Sung, J.4
  • 32
    • 0000627391 scopus 로고
    • Reversible-growth model: cluster-cluster aggregation with finite binding energies
    • Shih W, Aksay I, Kikuchi R, (1987) Reversible-growth model: cluster-cluster aggregation with finite binding energies. PhysRevA 36: 5015-5019.
    • (1987) PhysRevA , vol.36 , pp. 5015-5019
    • Shih, W.1    Aksay, I.2    Kikuchi, R.3
  • 33
    • 46749140860 scopus 로고    scopus 로고
    • Low density lipoprotein misfolding and amyloidogenesis
    • Parasassi T, De Spirito M, Mei G, Brunelli R, Greco G, et al. (2008) Low density lipoprotein misfolding and amyloidogenesis. FASEB J 22: 2350-2356.
    • (2008) FASEB J , vol.22 , pp. 2350-2356
    • Parasassi, T.1    De Spirito, M.2    Mei, G.3    Brunelli, R.4    Greco, G.5
  • 34
    • 0001585605 scopus 로고
    • Universal kinetics in reaction-limited aggregation
    • Ball R, Weitz D, Witten T, Leyvraz F, (1987) Universal kinetics in reaction-limited aggregation. PRL 58: 274-277.
    • (1987) PRL , vol.58 , pp. 274-277
    • Ball, R.1    Weitz, D.2    Witten, T.3    Leyvraz, F.4
  • 35
    • 0021096626 scopus 로고
    • A jump in an arrhenius plot can be the consequence of a phase transition
    • Biosca J, Travers F, Barman T, (1983) A jump in an arrhenius plot can be the consequence of a phase transition. FEBS lett 153: 217-220.
    • (1983) FEBS Lett , vol.153 , pp. 217-220
    • Biosca, J.1    Travers, F.2    Barman, T.3
  • 37
    • 85044700615 scopus 로고    scopus 로고
    • Comparative study of the crystallin supramolecular structure in the carp, frog, and rat lenses by small-angle roentgen ray scattering
    • Krivandin A, Muranov K, (1999) Comparative study of the crystallin supramolecular structure in the carp, frog, and rat lenses by small-angle roentgen ray scattering. Phys Med Biol 44: 1088-1093.
    • (1999) Phys Med Biol , vol.44 , pp. 1088-1093
    • Krivandin, A.1    Muranov, K.2
  • 38
    • 0018364640 scopus 로고
    • The interrelationship between monomeric, oligomeric and polymeric a-crystallin in the calf lens nucleus
    • Siezen RJ, Bindels JG, Hoenders HJ, (1979) The interrelationship between monomeric, oligomeric and polymeric a-crystallin in the calf lens nucleus. Exp Eye Res 28: 551-567.
    • (1979) Exp Eye Res , vol.28 , pp. 551-567
    • Siezen, R.J.1    Bindels, J.G.2    Hoenders, H.J.3
  • 39
    • 34249669706 scopus 로고    scopus 로고
    • Computational modelling of temperature rises in the eye in the near field of radiofrequency sources at 380, 900 and 1800 mhz
    • Wainwright PR, (2007) Computational modelling of temperature rises in the eye in the near field of radiofrequency sources at 380, 900 and 1800 mhz. Phys Med Biol 52: 3335-3350.
    • (2007) Phys Med Biol , vol.52 , pp. 3335-3350
    • Wainwright, P.R.1
  • 40
    • 0036597985 scopus 로고    scopus 로고
    • Viewing molecular mechanisms of ageing through a lens
    • Harding J, (2002) Viewing molecular mechanisms of ageing through a lens. Ageing ResRev 1: 465-479.
    • (2002) Ageing ResRev , vol.1 , pp. 465-479
    • Harding, J.1
  • 42
    • 0018873668 scopus 로고
    • Microwave cataractogenesis
    • Cleary S, (1980) Microwave cataractogenesis. Proceedings of the IEEE 68: 49-55.
    • (1980) Proceedings of the IEEE , vol.68 , pp. 49-55
    • Cleary, S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.