메뉴 건너뛰기




Volumn 17, Issue , 2011, Pages 2798-2807

Understanding the α-crystallin cell membrane conjunction

Author keywords

[No Author keywords available]

Indexed keywords

ALKALI; ALPHA CRYSTALLIN; RECOMBINANT PROTEIN; UREA;

EID: 83055170897     PISSN: None     EISSN: 10900535     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (18)

References (53)
  • 1
    • 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
    • [PMID: 8690038]
    • Garland DL, Duglas-Tabor Y, Jimenez-Asensio J, Datiles MB, Magno B. 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. Exp Eye Res 1996; 62:285-91. [PMID: 8690038]
    • (1996) Exp Eye Res , vol.62 , pp. 285-291
    • Garland, D.L.1    Duglas-Tabor, Y.2    Jimenez-Asensio, J.3    Datiles, M.B.4    Magno, B.5
  • 3
    • 0026483279 scopus 로고
    • Alpha-Crystallin can function as a molecular chaperone
    • [PMID: 1438232]
    • Horwitz J. Alpha-Crystallin can function as a molecular chaperone. Proc Natl Acad Sci USA 1992; 89:10449-53. [PMID: 1438232]
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 10449-10453
    • Horwitz, J.1
  • 4
    • 0028973109 scopus 로고
    • Evidence that alpha-crystallin prevents non-specific protein aggregation in the intact eye lens
    • [PMID: 8541324]
    • 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. [PMID: 8541324]
    • (1995) Biochim Biophys Acta , vol.1245 , pp. 439-447
    • Rao, P.V.1    Huang, Q.L.2    Horwitz, J.3    Zigler Jr., J.S.4
  • 5
    • 45149103497 scopus 로고    scopus 로고
    • Radiocarbon dating of the human eye lens crystallines reveal proteins without carbon turnover throughout life
    • [PMID: 18231610]
    • Lynnerup N, Kjeldsen H, Heegaard S, Jacobsen C, Heinemeier J. Radiocarbon dating of the human eye lens crystallines reveal proteins without carbon turnover throughout life. PLoS One 2008; 3:e1529. [PMID: 18231610]
    • (2008) PLoS One , vol.3
    • Lynnerup, N.1    Kjeldsen, H.2    Heegaard, S.3    Jacobsen, C.4    Heinemeier, J.5
  • 7
    • 33750142707 scopus 로고    scopus 로고
    • Age-related changes in human crystallins determined from comparative analysis of post-translational modifications in young and aged lens: Does deamidation contribute to crystallin insolubility?
    • [PMID: 17022627]
    • Wilmarth PA, Tanner S, Dasari S, Nagalla SR, Riviere MA, Bafna V, Pevzner PA, David LL. Age-related changes in human crystallins determined from comparative analysis of post-translational modifications in young and aged lens: does deamidation contribute to crystallin insolubility? J Proteome Res 2006; 5:2554-66. [PMID: 17022627]
    • (2006) J Proteome Res , vol.5 , pp. 2554-2566
    • Wilmarth, P.A.1    Tanner, S.2    Dasari, S.3    Nagalla, S.R.4    Riviere, M.A.5    Bafna, V.6    Pevzner, P.A.7    David, L.L.8
  • 8
    • 4043127599 scopus 로고    scopus 로고
    • Crystallins in water soluble-high molecular weight protein fractions and water insoluble protein fractions in aging and cataractous human lenses
    • [PMID: 15303090]
    • Harrington V, McCall S, Huynh S, Srivastava K, Srivastava OP. Crystallins in water soluble-high molecular weight protein fractions and water insoluble protein fractions in aging and cataractous human lenses. Mol Vis 2004; 10:476-89. [PMID: 15303090]
    • (2004) Mol Vis , vol.10 , pp. 476-489
    • Harrington, V.1    McCall, S.2    Huynh, S.3    Srivastava, K.4    Srivastava, O.P.5
  • 9
    • 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
    • [PMID: 10930324]
    • 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. [PMID: 10930324]
    • (2000) Exp Eye Res , vol.71 , pp. 195-207
    • Hanson, S.R.1    Hasan, A.2    Smith, D.L.3    Smith, J.B.4
  • 10
    • 78650202678 scopus 로고    scopus 로고
    • Presbyopia and cataract: A question of heat and time
    • [PMID: 20472092]
    • Truscott RJ, Zhu X. Presbyopia and cataract: a question of heat and time. Prog Retin Eye Res 2010; 29:487-99. [PMID: 20472092]
    • (2010) Prog Retin Eye Res , vol.29 , pp. 487-499
    • Truscott, R.J.1    Zhu, X.2
  • 11
    • 0024311462 scopus 로고
    • Crystallin gene expression during rat lens development
    • [PMID: 2753045]
    • Aarts HJ, Lubsen NH, Schoenmakers JG. Crystallin gene expression during rat lens development. Eur J Biochem 1989; 183:31-6. [PMID: 2753045]
    • (1989) Eur J Biochem , vol.183 , pp. 31-36
    • Aarts, H.J.1    Lubsen, N.H.2    Schoenmakers, J.G.3
  • 12
    • 79955623990 scopus 로고    scopus 로고
    • Truncation, cross-linking and interaction of crystallins and intermediate filament proteins in the aging human lens
    • [PMID: 21447408]
    • Su S-P, McArthur JD, Truscott RJ, Aquilina JA. Truncation, cross-linking and interaction of crystallins and intermediate filament proteins in the aging human lens. Biochim Biophys Acta 2011; 1814:647-56. [PMID: 21447408]
    • (2011) Biochim Biophys Acta , vol.1814 , pp. 647-656
    • Su, S.-P.1    McArthur, J.D.2    Truscott, R.J.3    Aquilina, J.A.4
  • 13
    • 36249023238 scopus 로고    scopus 로고
    • Presbyopia and heat: Changes associated with aging of the human lens suggest a functional role for the small heat shock protein, alphacrystallin, in maintaining lens flexibility
    • [PMID: 17973972]
    • Heys KR, Friedrich MG, Truscott RJW. Presbyopia and heat: changes associated with aging of the human lens suggest a functional role for the small heat shock protein, alphacrystallin, in maintaining lens flexibility. Aging Cell 2007; 6:807-15. [PMID: 17973972]
    • (2007) Aging Cell , vol.6 , pp. 807-815
    • Heys, K.R.1    Friedrich, M.G.2    Truscott, R.J.W.3
  • 14
    • 0022336641 scopus 로고
    • Spatial and temporal mapping of the age-related changes in human lens crystallins
    • [PMID: 3830737]
    • McFall-Ngai MJ, Ding LL, Takemoto LJ, Horwitz J. Spatial and temporal mapping of the age-related changes in human lens crystallins. Exp Eye Res 1985; 41:745-58. [PMID: 3830737]
    • (1985) Exp Eye Res , vol.41 , pp. 745-758
    • McFall-Ngai, M.J.1    Ding, L.L.2    Takemoto, L.J.3    Horwitz, J.4
  • 15
    • 0013358797 scopus 로고
    • Absence of low-molecular-weight alpha crystallin in nuclear region of old human lenses
    • [PMID: 1068460]
    • Roy D, Spector A. Absence of low-molecular-weight alpha crystallin in nuclear region of old human lenses. Proc Natl Acad Sci USA 1976; 73:3484-7. [PMID: 1068460]
    • (1976) Proc Natl Acad Sci USA , vol.73 , pp. 3484-3487
    • Roy, D.1    Spector, A.2
  • 16
    • 0032128377 scopus 로고    scopus 로고
    • Age-related changes in human lens crystallins identified by two-dimensional electrophoresis and mass spectrometry
    • [PMID: 9702176]
    • Lampi KJ, Ma Z, Hanson SR, Azuma M, Shih M, Shearer TR, Smith DL, Smith JB, David LL. Age-related changes in human lens crystallins identified by two-dimensional electrophoresis and mass spectrometry. Exp Eye Res 1998; 67:31-43. [PMID: 9702176]
    • (1998) Exp Eye Res , vol.67 , pp. 31-43
    • Lampi, K.J.1    Ma, Z.2    Hanson, S.R.3    Azuma, M.4    Shih, M.5    Shearer, T.R.6    Smith, D.L.7    Smith, J.B.8    David, L.L.9
  • 17
    • 0030011325 scopus 로고    scopus 로고
    • Levels of crystallin fragments and identification of their origin in water soluble high molecular weight (HMW) proteins of human lenses
    • [PMID: 8670752]
    • Srivastava OP, Srivastava K, Silney C. Levels of crystallin fragments and identification of their origin in water soluble high molecular weight (HMW) proteins of human lenses. Curr Eye Res 1996; 15:511-20. [PMID: 8670752]
    • (1996) Curr Eye Res , vol.15 , pp. 511-520
    • Srivastava, O.P.1    Srivastava, K.2    Silney, C.3
  • 18
    • 0032128077 scopus 로고    scopus 로고
    • Age-related changes in human lens crystallins identified by HPLC and mass spectrometry
    • [PMID: 9702175]
    • Ma Z, Hanson SR, Lampi KJ, David LL, Smith DL, Smith JB. Age-related changes in human lens crystallins identified by HPLC and mass spectrometry. Exp Eye Res 1998; 67:21-30. [PMID: 9702175]
    • (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
  • 19
    • 0021259081 scopus 로고
    • Characterization of lens proteins. IV. Analysis of soluble high molecular weight protein aggregates in human lenses
    • [PMID: 6745324]
    • Fu SC, Su SW, Wagner BJ, Hart R. Characterization of lens proteins. IV. Analysis of soluble high molecular weight protein aggregates in human lenses. Exp Eye Res 1984; 38:485-95. [PMID: 6745324]
    • (1984) Exp Eye Res , vol.38 , pp. 485-495
    • Fu, S.C.1    Su, S.W.2    Wagner, B.J.3    Hart, R.4
  • 20
    • 0030015111 scopus 로고    scopus 로고
    • EM immunolocalization of alphacrystallins: Association with the plasma membrane from normal and cataractous human lenses
    • [PMID: 8670759]
    • Boyle DL, Takemoto L. EM immunolocalization of alphacrystallins: association with the plasma membrane from normal and cataractous human lenses. Curr Eye Res 1996; 15:577-82. [PMID: 8670759]
    • (1996) Curr Eye Res , vol.15 , pp. 577-582
    • Boyle, D.L.1    Takemoto, L.2
  • 21
    • 0026649322 scopus 로고
    • Selective association of crystallins with lens 'native' membrane during dynamic cataractogenesis
    • [PMID: 1424724]
    • Cenedella RJ, Fleschner CR. Selective association of crystallins with lens 'native' membrane during dynamic cataractogenesis. Curr Eye Res 1992; 11:801-15. [PMID: 1424724]
    • (1992) Curr Eye Res , vol.11 , pp. 801-815
    • Cenedella, R.J.1    Fleschner, C.R.2
  • 22
    • 77958141738 scopus 로고    scopus 로고
    • Large-scale binding of alphacrystallin to cell membranes of aged normal human lenses: A phenomenon that can be induced by mild thermal stress
    • [PMID: 20435594]
    • Friedrich MG, Truscott RJ. Large-scale binding of alphacrystallin to cell membranes of aged normal human lenses: a phenomenon that can be induced by mild thermal stress. Invest Ophthalmol Vis Sci 2010; 51:5145-52. [PMID: 20435594]
    • (2010) Invest Ophthalmol Vis Sci , vol.51 , pp. 5145-5152
    • Friedrich, M.G.1    Truscott, R.J.2
  • 23
    • 70349578965 scopus 로고    scopus 로고
    • Membrane association of proteins in the aging human lens: Profound changes take place in the fifth decade of life
    • [PMID: 19458333]
    • Friedrich MG, Truscott RJ. Membrane association of proteins in the aging human lens: profound changes take place in the fifth decade of life. Invest Ophthalmol Vis Sci 2009; 50:4786-93. [PMID: 19458333]
    • (2009) Invest Ophthalmol Vis Sci , vol.50 , pp. 4786-4793
    • Friedrich, M.G.1    Truscott, R.J.2
  • 24
    • 18044388716 scopus 로고    scopus 로고
    • Age-related nuclear cataract-oxidation is the key
    • [PMID: 15862178]
    • Truscott RJ. Age-related nuclear cataract-oxidation is the key. Exp Eye Res 2005; 80:709-25. [PMID: 15862178]
    • (2005) Exp Eye Res , vol.80 , pp. 709-725
    • Truscott, R.J.1
  • 25
    • 0029060305 scopus 로고
    • Protein associated with human lens 'native' membrane during aging and cataract formation
    • [PMID: 7641853]
    • Chandrasekher G, Cenedella RJ. Protein associated with human lens 'native' membrane during aging and cataract formation. Exp Eye Res 1995; 60:707-17. [PMID: 7641853]
    • (1995) Exp Eye Res , vol.60 , pp. 707-717
    • Chandrasekher, G.1    Cenedella, R.J.2
  • 26
    • 0037080002 scopus 로고    scopus 로고
    • alpha-Crystallin chaperone-like activity and membrane binding in age-related cataracts
    • [PMID: 11781086]
    • Cobb BA, Petrash JM. alpha-Crystallin chaperone-like activity and membrane binding in age-related cataracts. Biochemistry 2002; 41:483-90. [PMID: 11781086]
    • (2002) Biochemistry , vol.41 , pp. 483-490
    • Cobb, B.A.1    Petrash, J.M.2
  • 27
    • 23144437087 scopus 로고    scopus 로고
    • alpha-Crystallin binding in vitro to lipids from clear human lenses
    • [PMID: 15967437]
    • Grami V, Marrero Y, Huang L, Tang D, Yappert MC, Borchman D. alpha-Crystallin binding in vitro to lipids from clear human lenses. Exp Eye Res 2005; 81:138-46. [PMID: 15967437]
    • (2005) Exp Eye Res , vol.81 , pp. 138-146
    • Grami, V.1    Marrero, Y.2    Huang, L.3    Tang, D.4    Yappert, M.C.5    Borchman, D.6
  • 28
    • 0032077957 scopus 로고    scopus 로고
    • Influence of cholesterol on the interaction of alpha-crystallin with phospholipids
    • [PMID: 9628803]
    • Tang D, Borchman D, Yappert MC, Cenedella RJ. Influence of cholesterol on the interaction of alpha-crystallin with phospholipids. Exp Eye Res 1998; 66:559-67. [PMID: 9628803]
    • (1998) Exp Eye Res , vol.66 , pp. 559-567
    • Tang, D.1    Borchman, D.2    Yappert, M.C.3    Cenedella, R.J.4
  • 29
    • 0031105338 scopus 로고    scopus 로고
    • Properties of alpha-crystallin bound to lens membrane: Probing organization at the membrane surface
    • [PMID: 9196394]
    • Chandrasekher G, Cenedella RJ. Properties of alpha-crystallin bound to lens membrane: probing organization at the membrane surface. Exp Eye Res 1997; 64:423-30. [PMID: 9196394]
    • (1997) Exp Eye Res , vol.64 , pp. 423-430
    • Chandrasekher, G.1    Cenedella, R.J.2
  • 30
    • 0034009392 scopus 로고    scopus 로고
    • Characterization of alpha-crystallinplasma membrane binding
    • [PMID: 10692476]
    • Cobb BA, Petrash JM. Characterization of alpha-crystallinplasma membrane binding. J Biol Chem 2000; 275:6664-72. [PMID: 10692476]
    • (2000) J Biol Chem , vol.275 , pp. 6664-6672
    • Cobb, B.A.1    Petrash, J.M.2
  • 31
    • 0019435458 scopus 로고
    • A new method for rapid isolation of the intrinsic membrane proteins from lens
    • [PMID: 6786906]
    • Russell P, Robison WG Jr, Kinoshita JH. A new method for rapid isolation of the intrinsic membrane proteins from lens. Exp Eye Res 1981; 32:511-6. [PMID: 6786906]
    • (1981) Exp Eye Res , vol.32 , pp. 511-516
    • Russell, P.1    Robison Jr., W.G.2    Kinoshita, J.H.3
  • 33
    • 0030962474 scopus 로고    scopus 로고
    • Quantitative analysis of biological membrane lipids at the low picomole level by nano-electrospray ionization tandem mass spectrometry
    • [PMID: 9122196]
    • Brügger B, Erben G, Sandhoff R, Wieland FT, Lehmann WD. Quantitative analysis of biological membrane lipids at the low picomole level by nano-electrospray ionization tandem mass spectrometry. Proc Natl Acad Sci USA 1997; 94:2339-44. [PMID: 9122196]
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 2339-2344
    • Brügger, B.1    Erben, G.2    Sandhoff, R.3    Wieland, F.T.4    Lehmann, W.D.5
  • 34
    • 0031918807 scopus 로고    scopus 로고
    • Lens alpha-crystallin: Chaperone-like properties
    • [PMID: 9534176]
    • Horwitz J, Huang Q-L, Ding L, Bova MP. Lens alpha-crystallin: chaperone-like properties. Methods Enzymol 1998; 290:365-83. [PMID: 9534176]
    • (1998) Methods Enzymol , vol.290 , pp. 365-383
    • Horwitz, J.1    Huang, Q.-L.2    Ding, L.3    Bova, M.P.4
  • 35
    • 43749091530 scopus 로고    scopus 로고
    • Significance of interactions of low molecular weight crystallin fragments in lens aging and cataract formation
    • [PMID: 18227073]
    • Santhoshkumar P, Udupa P, Murugesan R, Sharma KK. Significance of interactions of low molecular weight crystallin fragments in lens aging and cataract formation. J Biol Chem 2008; 283:8477-85. [PMID: 18227073]
    • (2008) J Biol Chem , vol.283 , pp. 8477-8485
    • Santhoshkumar, P.1    Udupa, P.2    Murugesan, R.3    Sharma, K.K.4
  • 36
    • 77953357415 scopus 로고    scopus 로고
    • Localization of low molecular weight crystallin peptides in the aging human lens using a MALDI mass spectrometry imaging approach
    • [PMID: 20433829]
    • Su S-P, McArthur JD, Aquilina JA. Localization of low molecular weight crystallin peptides in the aging human lens using a MALDI mass spectrometry imaging approach. Exp Eye Res 2010; 91:97-103. [PMID: 20433829]
    • (2010) Exp Eye Res , vol.91 , pp. 97-103
    • Su, S.-P.1    McArthur, J.D.2    Aquilina, J.A.3
  • 37
    • 70349263467 scopus 로고    scopus 로고
    • Age-related changes in the spatial distribution of human lens alpha-crystallin products by MALDI imaging mass spectrometry
    • [PMID: 19387068]
    • Grey AC, Schey KL. Age-related changes in the spatial distribution of human lens alpha-crystallin products by MALDI imaging mass spectrometry. Invest Ophthalmol Vis Sci 2009; 50:4319-29. [PMID: 19387068]
    • (2009) Invest Ophthalmol Vis Sci , vol.50 , pp. 4319-4329
    • Grey, A.C.1    Schey, K.L.2
  • 38
    • 0032412746 scopus 로고    scopus 로고
    • An impediment to glutathione diffusion in older normal human lenses: A possible precondition for nuclear cataract
    • [PMID: 9878221]
    • Sweeney MHJ, Truscott RJW. An impediment to glutathione diffusion in older normal human lenses: a possible precondition for nuclear cataract. Exp Eye Res 1998; 67:587-95. [PMID: 9878221]
    • (1998) Exp Eye Res , vol.67 , pp. 587-595
    • Sweeney, M.H.J.1    Truscott, R.J.W.2
  • 39
    • 0033824238 scopus 로고    scopus 로고
    • Age-related nuclear cataract: A lens transport problem
    • [PMID: 10971179]
    • Truscott RJ. Age-related nuclear cataract: a lens transport problem. Ophthalmic Res 2000; 32:185-94. [PMID: 10971179]
    • (2000) Ophthalmic Res , vol.32 , pp. 185-194
    • Truscott, R.J.1
  • 40
    • 0024340465 scopus 로고
    • Differential binding of alpha-crystallins to bovine lens membrane
    • [PMID: 2759187]
    • Ifeanyi F, Takemoto L. Differential binding of alpha-crystallins to bovine lens membrane. Exp Eye Res 1989; 49:143-7. [PMID: 2759187]
    • (1989) Exp Eye Res , vol.49 , pp. 143-147
    • Ifeanyi, F.1    Takemoto, L.2
  • 42
    • 0025374422 scopus 로고
    • Specificity of alpha crystallin binding to the lens membrane
    • [PMID: 2347203]
    • Ifeanyi F, Takemoto L. Specificity of alpha crystallin binding to the lens membrane. Curr Eye Res 1990; 9:259-65. [PMID: 2347203]
    • (1990) Curr Eye Res , vol.9 , pp. 259-265
    • Ifeanyi, F.1    Takemoto, L.2
  • 44
    • 0027371857 scopus 로고
    • High capacity binding of alpha crystallins to various bovine lens membrane preparations
    • [PMID: 8306713]
    • Cenedella RJ, Chandrasekher G. High capacity binding of alpha crystallins to various bovine lens membrane preparations. Curr Eye Res 1993; 12:1025-38. [PMID: 8306713]
    • (1993) Curr Eye Res , vol.12 , pp. 1025-1038
    • Cenedella, R.J.1    Chandrasekher, G.2
  • 45
    • 0028831015 scopus 로고
    • In vitro studies on the assembly properties of the lens proteins CP49, CP115: Coassembly with alpha-crystallin but not with vimentin
    • [PMID: 7781747]
    • Carter JM, Hutcheson AM, Quinlan RA. In vitro studies on the assembly properties of the lens proteins CP49, CP115: coassembly with alpha-crystallin but not with vimentin. Exp Eye Res 1995; 60:181-92. [PMID: 7781747]
    • (1995) Exp Eye Res , vol.60 , pp. 181-192
    • Carter, J.M.1    Hutcheson, A.M.2    Quinlan, R.A.3
  • 46
    • 0030004555 scopus 로고    scopus 로고
    • The beaded filament of the eye lens: An unexpected key to intermediate filament structure and function
    • [PMID: 15157473]
    • Quinlan RA, Carter JM, Sandilands A, Prescott AR. The beaded filament of the eye lens: an unexpected key to intermediate filament structure and function. Trends Cell Biol 1996; 6:123-6. [PMID: 15157473]
    • (1996) Trends Cell Biol , vol.6 , pp. 123-126
    • Quinlan, R.A.1    Carter, J.M.2    Sandilands, A.3    Prescott, A.R.4
  • 47
    • 78149421964 scopus 로고    scopus 로고
    • Novel fatty acid acylation of lens integral membrane protein aquaporin-0
    • [PMID: 20942504]
    • Schey KL, Gutierrez DB, Wang Z, Wei J, Grey AC. Novel fatty acid acylation of lens integral membrane protein aquaporin-0. Biochemistry 2010; 49:9858-65. [PMID: 20942504]
    • (2010) Biochemistry , vol.49 , pp. 9858-9865
    • Schey, K.L.1    Gutierrez, D.B.2    Wang, Z.3    Wei, J.4    Grey, A.C.5
  • 48
    • 0034681446 scopus 로고    scopus 로고
    • Temperaturedependent chaperone activity and structural properties of human alphaA-and alphaB-crystallins
    • [PMID: 10671481]
    • Reddy GB, Das KP, Petrash JM, Surewicz WK. Temperaturedependent chaperone activity and structural properties of human alphaA-and alphaB-crystallins. J Biol Chem 2000; 275:4565-70. [PMID: 10671481]
    • (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
  • 49
    • 43749091530 scopus 로고    scopus 로고
    • Significance of interactions of low molecular weight crystallin fragments in lens aging and cataract formation
    • [PMID: 18227073]
    • Santhoshkumar P, Udupa P, Murugesan R, Sharma KK. Significance of interactions of low molecular weight crystallin fragments in lens aging and cataract formation. J Biol Chem 2008; 283:8477-85. [PMID: 18227073]
    • (2008) J Biol Chem , vol.283 , pp. 8477-8485
    • Santhoshkumar, P.1    Udupa, P.2    Murugesan, R.3    Sharma, K.K.4
  • 50
    • 0021307250 scopus 로고
    • Effect of lipid composition on hydrophobic properties of liposomes
    • [PMID: 6200761]
    • Zaslavsky, BYU; Borovskaya, AA.; Rogozhin, SV. Effect of lipid composition on hydrophobic properties of liposomes. Mol Cell Biochem 1984; 60:131-6. [PMID: 6200761]
    • (1984) Mol Cell Biochem , vol.60 , pp. 131-136
    • Zaslavsky, B.Y.U.1    Borovskaya, A.A.2    Rogozhin, S.V.3
  • 51
    • 0032986520 scopus 로고    scopus 로고
    • Alpha-crystallin as a molecular chaperone
    • [PMID: 10217480]
    • Derham BK, Harding JJ. Alpha-crystallin as a molecular chaperone. Prog Retin Eye Res 1999; 18:463-509. [PMID: 10217480]
    • (1999) Prog Retin Eye Res , vol.18 , pp. 463-509
    • Derham, B.K.1    Harding, J.J.2
  • 52
    • 33846161926 scopus 로고    scopus 로고
    • The N-terminal domain of alphaBcrystallin is protected from proteolysis by bound substrate
    • [PMID: 17207466]
    • Aquilina JA, Watt SJ. The N-terminal domain of alphaBcrystallin is protected from proteolysis by bound substrate. Biochem Biophys Res Commun 2007; 353:1115-20. [PMID: 17207466]
    • (2007) Biochem Biophys Res Commun , vol.353 , pp. 1115-1120
    • Aquilina, J.A.1    Watt, S.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.