메뉴 건너뛰기




Volumn 92, Issue 1, 2011, Pages 76-86

Mechanism of aggregation of UV-irradiated βL-crystallin

Author keywords

crystallin; Aggregation; Denaturation; Differential scanning calorimetry; Dynamic light scattering; UV irradiation

Indexed keywords

BETA CRYSTALLIN; TRYPTOPHAN;

EID: 78650545398     PISSN: 00144835     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.exer.2010.11.005     Document Type: Article
Times cited : (34)

References (85)
  • 1
    • 0023938965 scopus 로고
    • Spectroscopic studies on the photooxidation of calf-lens gamma-crystallin
    • Andley U.P., Clark B.A. Spectroscopic studies on the photooxidation of calf-lens gamma-crystallin. Curr. Eye Res. 1988, 7:571-579.
    • (1988) Curr. Eye Res. , vol.7 , pp. 571-579
    • Andley, U.P.1    Clark, B.A.2
  • 5
    • 0032306459 scopus 로고    scopus 로고
    • Macromolecular structure of the eye lens
    • Augusteyn A., Stevens A. Macromolecular structure of the eye lens. Prog. Polymer. Sci. 1998, 23:375-413.
    • (1998) Prog. Polymer. Sci. , vol.23 , pp. 375-413
    • Augusteyn, A.1    Stevens, A.2
  • 11
    • 14044264953 scopus 로고    scopus 로고
    • Relation between aggregation kinetics and the structure of kaolinite aggregates
    • Berka M., Rice J.A. Relation between aggregation kinetics and the structure of kaolinite aggregates. Langmuir 2005, 21:1223-1229.
    • (2005) Langmuir , vol.21 , pp. 1223-1229
    • Berka, M.1    Rice, J.A.2
  • 12
    • 0019479055 scopus 로고
    • Structural aspects of bovine beta-crystallins: physical characterization including dissociation-association behavior
    • Bindels J.G., Koppers A., Hoenders H.J. Structural aspects of bovine beta-crystallins: physical characterization including dissociation-association behavior. Exp. Eye Res. 1981, 33:333-343.
    • (1981) Exp. Eye Res. , vol.33 , pp. 333-343
    • Bindels, J.G.1    Koppers, A.2    Hoenders, H.J.3
  • 14
    • 0029447845 scopus 로고
    • The molecular chaperone function of alpha-crystallin is impaired by UV photolysis
    • Borkman R.F., McLaughlin J. The molecular chaperone function of alpha-crystallin is impaired by UV photolysis. Photochem. Photobiol. 1995, 62:1046-1051.
    • (1995) Photochem. Photobiol. , vol.62 , pp. 1046-1051
    • Borkman, R.F.1    McLaughlin, J.2
  • 15
    • 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
  • 17
    • 54349106147 scopus 로고    scopus 로고
    • Association properties of betaB1- and betaA3-crystallins: ability to form heterotetramers
    • Chan M.P., Dolinska M., Sergeev Y.V., Wingfield P.T., Hejtmancik J.F. Association properties of betaB1- and betaA3-crystallins: ability to form heterotetramers. Biochemistry 2008, 47:11062-11069.
    • (2008) Biochemistry , vol.47 , pp. 11062-11069
    • Chan, M.P.1    Dolinska, M.2    Sergeev, Y.V.3    Wingfield, P.T.4    Hejtmancik, J.F.5
  • 18
    • 56149112073 scopus 로고    scopus 로고
    • Nonreciprocal XeCl laser-induced aggregation of beta-crystallins in water solution
    • Chelnokov E., Soustov L., Sapogova N., Ostrovsky M., Bityurin N. Nonreciprocal XeCl laser-induced aggregation of beta-crystallins in water solution. Opt. Express 2008, 16:18798-18803.
    • (2008) Opt. Express , vol.16 , pp. 18798-18803
    • Chelnokov, E.1    Soustov, L.2    Sapogova, N.3    Ostrovsky, M.4    Bityurin, N.5
  • 20
    • 0033991596 scopus 로고    scopus 로고
    • Lens cytoplasmic phase separation
    • Clark J.I., Clark J.M. Lens cytoplasmic phase separation. Int. Rev. Cytol. 2000, 192:171-187.
    • (2000) Int. Rev. Cytol. , vol.192 , pp. 171-187
    • Clark, J.I.1    Clark, J.M.2
  • 21
    • 0020678719 scopus 로고
    • Short-range order of crystallin proteins accounts for eye lens transparency
    • Delaye M., Tardieu A. Short-range order of crystallin proteins accounts for eye lens transparency. Nature 1983, 302:415-417.
    • (1983) Nature , vol.302 , pp. 415-417
    • Delaye, M.1    Tardieu, A.2
  • 23
    • 70350050551 scopus 로고    scopus 로고
    • N-terminal extension of beta B1-crystallin: identification of a critical region that modulates protein interaction with beta A3-crystallin
    • Dolinska M.B., Sergeev Y.V., Chan M.P., Palmer I., Wingfield P.T. N-terminal extension of beta B1-crystallin: identification of a critical region that modulates protein interaction with beta A3-crystallin. Biochemistry 2009, 48:9684-9695.
    • (2009) Biochemistry , vol.48 , pp. 9684-9695
    • Dolinska, M.B.1    Sergeev, Y.V.2    Chan, M.P.3    Palmer, I.4    Wingfield, P.T.5
  • 24
    • 60249099857 scopus 로고    scopus 로고
    • Effect of proline on thermal inactivation, denaturation and aggregation of glycogen phosphorylase b from rabbit skeletal muscle
    • Eronina T.B., Chebotareva N.A., Bazhina S.G., Makeeva V.F., Kleymenov S.Y., Kurganov B.I. Effect of proline on thermal inactivation, denaturation and aggregation of glycogen phosphorylase b from rabbit skeletal muscle. Biophys. Chem. 2009, 141:66-74.
    • (2009) Biophys. Chem. , vol.141 , pp. 66-74
    • Eronina, T.B.1    Chebotareva, N.A.2    Bazhina, S.G.3    Makeeva, V.F.4    Kleymenov, S.Y.5    Kurganov, B.I.6
  • 25
    • 0034612274 scopus 로고    scopus 로고
    • Control of protein crystal nucleation around the metastable liquid-liquid phase boundary
    • Galkin O., Vekilov P.G. Control of protein crystal nucleation around the metastable liquid-liquid phase boundary. Proc. Natl. Acad. Sci. U.S.A. 2000, 97:6277-6281.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 6277-6281
    • Galkin, O.1    Vekilov, P.G.2
  • 26
    • 84882524359 scopus 로고    scopus 로고
    • Reliability theory of aging and longevity
    • Academic Press, San Diego, CA, U.S.A. E.J. Masoro, S.N. Austad (Eds.)
    • Gavrilov L.A., Gavrilova N.S. Reliability theory of aging and longevity. Handbook of the Biology of Aging 2006, 3-42. Academic Press, San Diego, CA, U.S.A. sixth ed. E.J. Masoro, S.N. Austad (Eds.).
    • (2006) Handbook of the Biology of Aging , pp. 3-42
    • Gavrilov, L.A.1    Gavrilova, N.S.2
  • 29
    • 67349110220 scopus 로고    scopus 로고
    • Study of kinetics of thermal aggregation of mitochondrial aspartate aminotransferase by dynamic light scattering: protective effect of alpha-crystallin
    • Golub N.V., Markossian K.A., Sholukh M.V., Muranov K.O., Kurganov B.I. Study of kinetics of thermal aggregation of mitochondrial aspartate aminotransferase by dynamic light scattering: protective effect of alpha-crystallin. Eur. Biophys. J. 2009, 38:547-556.
    • (2009) Eur. Biophys. J. , vol.38 , pp. 547-556
    • Golub, N.V.1    Markossian, K.A.2    Sholukh, M.V.3    Muranov, K.O.4    Kurganov, B.I.5
  • 30
    • 0021344070 scopus 로고
    • Photochemistry of proteins: a review
    • Grossweiner L.I. Photochemistry of proteins: a review. Curr. Eye Res. 1984, 3:137-144.
    • (1984) Curr. Eye Res. , vol.3 , pp. 137-144
    • Grossweiner, L.I.1
  • 33
    • 0027950307 scopus 로고
    • Beta A3/A1-crystallin association: role of the N-terminal arm
    • Hope J.N., Chen H.C., Hejtmancik J.F. Beta A3/A1-crystallin association: role of the N-terminal arm. Protein Eng. 1994, 7:445-451.
    • (1994) Protein Eng. , vol.7 , pp. 445-451
    • Hope, J.N.1    Chen, H.C.2    Hejtmancik, J.F.3
  • 34
    • 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, 89:10449-10453.
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 10449-10453
    • Horwitz, J.1
  • 35
    • 0027551136 scopus 로고
    • Concentration dependence of transmission losses in UV-laser irradiated bovine alpha-, beta H-, beta L- and gamma-crystallin solutions
    • Hott J.L., Borkman R.F. Concentration dependence of transmission losses in UV-laser irradiated bovine alpha-, beta H-, beta L- and gamma-crystallin solutions. Photochem. Photobiol. 1993, 57:312-317.
    • (1993) Photochem. Photobiol. , vol.57 , pp. 312-317
    • Hott, J.L.1    Borkman, R.F.2
  • 36
    • 50549198780 scopus 로고
    • A micro-biuret method for estimating proteins
    • Itzhaki R.F., Gill D.M. A micro-biuret method for estimating proteins. Anal. Biochem. 1964, 9:401-410.
    • (1964) Anal. Biochem. , vol.9 , pp. 401-410
    • Itzhaki, R.F.1    Gill, D.M.2
  • 40
    • 18744396443 scopus 로고    scopus 로고
    • Temperature effect on the kinetics of the polystyrene aggregation progress by using static and dynamic light scatterings
    • Kim D.C., Kang M.H., Choi C.K., Ryu J.Y. Temperature effect on the kinetics of the polystyrene aggregation progress by using static and dynamic light scatterings. J. Korean Phys. Soc. 1997, 31:271-276.
    • (1997) J. Korean Phys. Soc. , vol.31 , pp. 271-276
    • Kim, D.C.1    Kang, M.H.2    Choi, C.K.3    Ryu, J.Y.4
  • 41
    • 0027553229 scopus 로고
    • Programs for signal recovery from noisy data using the maximum likelihood principle. 1: general description
    • Kosarev E.L., Gelfgat V.I., Podolyak E.R. Programs for signal recovery from noisy data using the maximum likelihood principle. 1: general description. Comput. Phys. Commun. 1993, 74:335-348.
    • (1993) Comput. Phys. Commun. , vol.74 , pp. 335-348
    • Kosarev, E.L.1    Gelfgat, V.I.2    Podolyak, E.R.3
  • 43
    • 0024404851 scopus 로고
    • Structural conversions of crystallins under senile cataract, dehydration and UV-irradiation studied by X-ray diffraction
    • Krivandin A.V., Lvov Yu M., Ostrovski M.A., Fedorovich I.B., Feigin L.A. Structural conversions of crystallins under senile cataract, dehydration and UV-irradiation studied by X-ray diffraction. Exp. Eye Res. 1989, 49:853-859.
    • (1989) Exp. Eye Res. , vol.49 , pp. 853-859
    • Krivandin, A.V.1    Lvov Yu, M.2    Ostrovski, M.A.3    Fedorovich, I.B.4    Feigin, L.A.5
  • 45
    • 0013821844 scopus 로고
    • Thermal after-effects of UV-irradiated lactate dehydrogenase from rabbit muscles
    • (Russian)
    • Kurganov B.I. Thermal after-effects of UV-irradiated lactate dehydrogenase from rabbit muscles. Biofizika 1965, 10:875-876. (Russian).
    • (1965) Biofizika , vol.10 , pp. 875-876
    • Kurganov, B.I.1
  • 46
    • 0032014876 scopus 로고    scopus 로고
    • Kinetics of heat aggregation of proteins
    • Kurganov B.I. Kinetics of heat aggregation of proteins. Biochemistry (Mosc) 1998, 63:364-366.
    • (1998) Biochemistry (Mosc) , vol.63 , pp. 364-366
    • Kurganov, B.I.1
  • 47
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. 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
  • 49
    • 0030614501 scopus 로고    scopus 로고
    • Sequence analysis of betaA3, betaB3, and betaA4 crystallins completes the identification of the major proteins in young human lens
    • Lampi K.J., Ma Z., Shih M., Shearer T.R., Smith J.B., Smith D.L., David L.L. Sequence analysis of betaA3, betaB3, and betaA4 crystallins completes the identification of the major proteins in young human lens. J. Biol. Chem. 1997, 272:2268-2275.
    • (1997) J. Biol. Chem. , vol.272 , pp. 2268-2275
    • Lampi, K.J.1    Ma, Z.2    Shih, M.3    Shearer, T.R.4    Smith, J.B.5    Smith, D.L.6    David, L.L.7
  • 50
    • 0026354773 scopus 로고
    • High resolution structure of an oligomeric eye lens beta-crystallin. Loops, arches, linkers and interfaces in beta B2 dimer compared to a monomeric gamma-crystallin
    • Lapatto R., Nalini V., Bax B., Driessen H., Lindley P.F., Blundell T.L., Slingsby C. High resolution structure of an oligomeric eye lens beta-crystallin. Loops, arches, linkers and interfaces in beta B2 dimer compared to a monomeric gamma-crystallin. J. Mol. Biol. 1991, 222:10671-10683.
    • (1991) J. Mol. Biol. , vol.222 , pp. 10671-10683
    • Lapatto, R.1    Nalini, V.2    Bax, B.3    Driessen, H.4    Lindley, P.F.5    Blundell, T.L.6    Slingsby, C.7
  • 51
    • 0025077090 scopus 로고
    • Photodamage to calf lenses in vitro by excimer laser radiation at 308, 337, and 350 nm
    • Li D.Y., Borkman R.F. Photodamage to calf lenses in vitro by excimer laser radiation at 308, 337, and 350 nm. Invest. Ophthalmol. Vis. Sci. 1990, 31:2180-2184.
    • (1990) Invest. Ophthalmol. Vis. Sci. , vol.31 , pp. 2180-2184
    • Li, D.Y.1    Borkman, R.F.2
  • 53
    • 33646377432 scopus 로고    scopus 로고
    • Domain interaction sites of human lens betaB2-crystallin
    • Liu B.F., Liang J.J. Domain interaction sites of human lens betaB2-crystallin. J. Biol. Chem. 2006, 281:2624-2630.
    • (2006) J. Biol. Chem. , vol.281 , pp. 2624-2630
    • Liu, B.F.1    Liang, J.J.2
  • 54
    • 0032128077 scopus 로고    scopus 로고
    • Age-related changes in human lens crystallins identified by HPLC and mass spectrometry
    • Ma Z., Hanson S.R., Lampi K.J., David L.L., Smith D.L., Smith J.B. Age-related changes in human lens crystallins identified by HPLC and mass spectrometry. Exp. Eye Res. 1998, 67:21-30.
    • (1998) Exp. Eye Res. , vol.67 , pp. 21-30
    • Ma, Z.1    Hanson, S.R.2    Lampi, K.J.3    David, L.L.4    Smith, D.L.5    Smith, J.B.6
  • 55
    • 0000478452 scopus 로고    scopus 로고
    • A model of attractive interactions to account for fluid-fluid phase separation of protein solutions
    • Malfois M., Bonnete F., Belloni L., Tardieu A. A model of attractive interactions to account for fluid-fluid phase separation of protein solutions. J. Chem. Phys. 1996, 105:3290-3300.
    • (1996) J. Chem. Phys. , vol.105 , pp. 3290-3300
    • Malfois, M.1    Bonnete, F.2    Belloni, L.3    Tardieu, A.4
  • 56
    • 75049084608 scopus 로고    scopus 로고
    • Comparative analysis of the effects of alpha-crystallin and GroEL on the kinetics of thermal aggregation of rabbit muscle glyceraldehyde-3-phosphate dehydrogenase
    • Markossian K.A., Golub N.V., Chebotareva N.A., Asryants R.A., Naletova I.N., Muronetz V.I., Muranov K.A., Kurganov B.I. Comparative analysis of the effects of alpha-crystallin and GroEL on the kinetics of thermal aggregation of rabbit muscle glyceraldehyde-3-phosphate dehydrogenase. Protein J. 2010, 29:11-25.
    • (2010) Protein J. , vol.29 , pp. 11-25
    • Markossian, K.A.1    Golub, N.V.2    Chebotareva, N.A.3    Asryants, R.A.4    Naletova, I.N.5    Muronetz, V.I.6    Muranov, K.A.7    Kurganov, B.I.8
  • 61
    • 63449134763 scopus 로고    scopus 로고
    • Mechanism of suppression of protein aggregation by alpha-crystallin
    • Markossian K.A., Yudin I.K., Kurganov B.I. Mechanism of suppression of protein aggregation by alpha-crystallin. Intern. J. Mol. Sci. 2009, 10:1314-1345.
    • (2009) Intern. J. Mol. Sci. , vol.10 , pp. 1314-1345
    • Markossian, K.A.1    Yudin, I.K.2    Kurganov, B.I.3
  • 62
    • 0036043869 scopus 로고    scopus 로고
    • A review of the epidemiologic evidence linking ultraviolet radiation and cataracts
    • McCarty C.A., Taylor H.R. A review of the epidemiologic evidence linking ultraviolet radiation and cataracts. Dev. Ophthalmol. 2002, 35:21-31.
    • (2002) Dev. Ophthalmol. , vol.35 , pp. 21-31
    • McCarty, C.A.1    Taylor, H.R.2
  • 65
    • 38949188930 scopus 로고    scopus 로고
    • Kinetics of thermal aggregation of glycogen phosphorylase b from rabbit skeletal muscle. Mechanism of protective action of alpha-crystallin
    • Meremyanin A.V., Eronina T.B., Chebotareva N.A., Kurganov B.I. Kinetics of thermal aggregation of glycogen phosphorylase b from rabbit skeletal muscle. Mechanism of protective action of alpha-crystallin. Biopolymers 2008, 89:124-134.
    • (2008) Biopolymers , vol.89 , pp. 124-134
    • Meremyanin, A.V.1    Eronina, T.B.2    Chebotareva, N.A.3    Kurganov, B.I.4
  • 66
    • 0036978853 scopus 로고    scopus 로고
    • Comparison of ultraviolet induced photo-kinetics for lens-derived and recombinant beta-crystallins
    • Ostrovsky M.A., Sergeev Y.V., Atkinson D.B., Soustov L.V., Hejtmancik J.F. Comparison of ultraviolet induced photo-kinetics for lens-derived and recombinant beta-crystallins. Mol. Vis. 2002, 8:72-78.
    • (2002) Mol. Vis. , vol.8 , pp. 72-78
    • Ostrovsky, M.A.1    Sergeev, Y.V.2    Atkinson, D.B.3    Soustov, L.V.4    Hejtmancik, J.F.5
  • 67
    • 33847191324 scopus 로고    scopus 로고
    • The study of amorphous aggregation of tobacco mosaic virus coat protein by dynamic light scattering
    • Panyukov Y., Yudin I., Drachev V., Dobrov E., Kurganov B. The study of amorphous aggregation of tobacco mosaic virus coat protein by dynamic light scattering. Biophys. Chem. 2007, 127:9-18.
    • (2007) Biophys. Chem. , vol.127 , pp. 9-18
    • Panyukov, Y.1    Yudin, I.2    Drachev, V.3    Dobrov, E.4    Kurganov, B.5
  • 68
    • 0038529737 scopus 로고    scopus 로고
    • Subunit exchange demonstrates a differential chaperone activity of calf alpha-crystallin toward beta LOW- and individual gamma-crystallins
    • Putilina T., Skouri-Panet F., Prat K., Lubsen N.H., Tardieu A. Subunit exchange demonstrates a differential chaperone activity of calf alpha-crystallin toward beta LOW- and individual gamma-crystallins. J. Biol. Chem. 2003, 278:13747-13756.
    • (2003) J. Biol. Chem. , vol.278 , pp. 13747-13756
    • Putilina, T.1    Skouri-Panet, F.2    Prat, K.3    Lubsen, N.H.4    Tardieu, A.5
  • 69
    • 0027267599 scopus 로고
    • Alpha-crystallin, a molecular chaperone, forms a stable complex with carbonic anhydrase upon heat denaturation
    • Rao P.V., Horwitz J., Zigler J.S. Alpha-crystallin, a molecular chaperone, forms a stable complex with carbonic anhydrase upon heat denaturation. Biochem. Biophys. Res. Commun. 1993, 190:786-793.
    • (1993) Biochem. Biophys. Res. Commun. , vol.190 , pp. 786-793
    • Rao, P.V.1    Horwitz, J.2    Zigler, J.S.3
  • 71
    • 33745303518 scopus 로고    scopus 로고
    • Quantitative measurement of young human eye lens crystallins by direct injection Fourier transform ion cyclotron resonance mass spectrometry
    • Robinson N.E., Lampi K.J., Speir J.P., Kruppa G., Easterling M., Robinson A.B. Quantitative measurement of young human eye lens crystallins by direct injection Fourier transform ion cyclotron resonance mass spectrometry. Mol. Vis. 2006, 12:704-711.
    • (2006) Mol. Vis. , vol.12 , pp. 704-711
    • Robinson, N.E.1    Lampi, K.J.2    Speir, J.P.3    Kruppa, G.4    Easterling, M.5    Robinson, A.B.6
  • 72
    • 0021436359 scopus 로고
    • Nondisulfide polymerization of gamma- and beta-crystallins in the human lens
    • Roy D., Dillon J., Wada E., Chaney W., Spector A. Nondisulfide polymerization of gamma- and beta-crystallins in the human lens. Proc. Natl. Acad. Sci. U.S.A. 1984, 81:2878-2881.
    • (1984) Proc. Natl. Acad. Sci. U.S.A. , vol.81 , pp. 2878-2881
    • Roy, D.1    Dillon, J.2    Wada, E.3    Chaney, W.4    Spector, A.5
  • 73
    • 77954757549 scopus 로고    scopus 로고
    • Thermodynamic study of protein phases formation and clustering in model water-protein-salt solutions
    • Rozhkov S.P., Goryunov A.S. Thermodynamic study of protein phases formation and clustering in model water-protein-salt solutions. Biophys. Chem. 2010, 151:22-28.
    • (2010) Biophys. Chem. , vol.151 , pp. 22-28
    • Rozhkov, S.P.1    Goryunov, A.S.2
  • 74
    • 78650564752 scopus 로고
    • Scientist for Experimental Data Fitting, MicroMath, Inc., Salt Lake City
    • Microsoft Windows Version 2.0 1995, Scientist for Experimental Data Fitting, MicroMath, Inc., Salt Lake City.
    • (1995) Microsoft Windows Version 2.0
  • 76
    • 49749173314 scopus 로고
    • The action of monochromatic ultraviolet light on proteins
    • Setlow R., Doyle B. The action of monochromatic ultraviolet light on proteins. Biochim. Biophys. Acta 1957, 24:27-41.
    • (1957) Biochim. Biophys. Acta , vol.24 , pp. 27-41
    • Setlow, R.1    Doyle, B.2
  • 77
    • 0022443288 scopus 로고
    • Interactions of lens proteins. Concentration dependence of beta-crystallin aggregation
    • Siezen R.J., Anello R.D., Thomson J.A. Interactions of lens proteins. Concentration dependence of beta-crystallin aggregation. Exp. Eye Res. 1986, 43:293-303.
    • (1986) Exp. Eye Res. , vol.43 , pp. 293-303
    • Siezen, R.J.1    Anello, R.D.2    Thomson, J.A.3
  • 79
    • 56349133640 scopus 로고    scopus 로고
    • Protein-protein interactions and lens transparency
    • Takemoto L., Sorensen C.M. Protein-protein interactions and lens transparency. Exp. Eye Res. 2008, 87:496-501.
    • (2008) Exp. Eye Res. , vol.87 , pp. 496-501
    • Takemoto, L.1    Sorensen, C.M.2
  • 80
    • 0026815107 scopus 로고
    • A superfamily in the mammalian eye lens: the beta/gamma-crystallins
    • van Rens G.L., de Jong W.W., Bloemendal H. A superfamily in the mammalian eye lens: the beta/gamma-crystallins. Mol. Biol. Rep. 1992, 16:1-10.
    • (1992) Mol. Biol. Rep. , vol.16 , pp. 1-10
    • van Rens, G.L.1    de Jong, W.W.2    Bloemendal, H.3
  • 81
    • 65249155468 scopus 로고    scopus 로고
    • Metastable mesoscopic phases in concentrated protein solutions
    • Vekilov P.G. Metastable mesoscopic phases in concentrated protein solutions. Ann. N.Y. Acad. Sci. 2009, 1161:377-386.
    • (2009) Ann. N.Y. Acad. Sci. , vol.1161 , pp. 377-386
    • Vekilov, P.G.1
  • 82
    • 0024520467 scopus 로고
    • Light scattering and photocrosslinking in the calf lens crystallins gamma-II, III and IV
    • Walker M.L., Borkman R.F. Light scattering and photocrosslinking in the calf lens crystallins gamma-II, III and IV. Exp. Eye Res. 1989, 48:375-383.
    • (1989) Exp. Eye Res. , vol.48 , pp. 375-383
    • Walker, M.L.1    Borkman, R.F.2
  • 83
    • 0001137442 scopus 로고
    • Dynamics of diffusion-limited kinetic aggregation
    • Weitz D.A., Huang J.S., Lin M.Y., Sung J. Dynamics of diffusion-limited kinetic aggregation. Phys. Rev. Lett. 1984, 53:1657-1660.
    • (1984) Phys. Rev. Lett. , vol.53 , pp. 1657-1660
    • Weitz, D.A.1    Huang, J.S.2    Lin, M.Y.3    Sung, J.4
  • 84
    • 0001665043 scopus 로고
    • Limits of the fractal dimension for irreversible kinetic aggregation of gold colloids
    • Weitz D.A., Huang J.S., Lin M.Y., Sung J. Limits of the fractal dimension for irreversible kinetic aggregation of gold colloids. Phys. Rev. Lett. 1985, 54:1416-1419.
    • (1985) Phys. Rev. Lett. , vol.54 , pp. 1416-1419
    • Weitz, D.A.1    Huang, J.S.2    Lin, M.Y.3    Sung, J.4
  • 85
    • 0018968340 scopus 로고
    • Human beta-crystallin. I. Comparative studies on the beta 1, beta 2 and beta 3-crystallins
    • Zigler J.S., Horwitz J., Kinoshita J.H. Human beta-crystallin. I. Comparative studies on the beta 1, beta 2 and beta 3-crystallins. Exp. Eye Res. 1980, 31:41-55.
    • (1980) Exp. Eye Res. , vol.31 , pp. 41-55
    • Zigler, J.S.1    Horwitz, J.2    Kinoshita, J.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.