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Volumn 8, Issue 4, 2011, Pages

The role of macromolecular crowding in the evolution of lens crystallins with high molecular refractive index

Author keywords

[No Author keywords available]

Indexed keywords

CEPHALOPODA; VERTEBRATA;

EID: 79960925383     PISSN: 14783967     EISSN: 14783975     Source Type: Journal    
DOI: 10.1088/1478-3975/8/4/046004     Document Type: Article
Times cited : (28)

References (89)
  • 1
    • 0023917935 scopus 로고
    • Lens crystallins: The evolution and expression of proteins for a highly specialized tissue
    • Wistow G J and Piatigorsky J 1988 Lens crystallins: the evolution and expression of proteins for a highly specialized tissue Annu. Rev. Biochem. 57 479-504
    • (1988) Annu. Rev. Biochem. , vol.57 , Issue.1 , pp. 479-504
    • Wistow, G.J.1    Piatigorsky, J.2
  • 2
    • 0028978534 scopus 로고
    • 13C-NMR off-resonance rotating frame spin-lattice relaxation studies of bovine lens gamma-crystallin self association: Effect of 'macromolecular crowding'
    • Stevens A, Wang S X, Caines G H and Schleich T 1995 13C-NMR off-resonance rotating frame spin-lattice relaxation studies of bovine lens gamma-crystallin self association: effect of 'macromolecular crowding' Biochim. Biophys. Acta 1246 82-90
    • (1995) Biochim. Biophys. Acta , vol.1246 , Issue.1 , pp. 82-90
    • Stevens, A.1    Wang, S.X.2    Caines, G.H.3    Schleich, T.4
  • 3
    • 0024365241 scopus 로고
    • The protein concentration gradient within eye lens might originate from constant osmotic pressure coupled to differential interactive properties of crystallins
    • Veretout F and Tardieu A 1989 The protein concentration gradient within eye lens might originate from constant osmotic pressure coupled to differential interactive properties of crystallins Eur. Biophys. J. 17 61-8 (Pubitemid 19152918)
    • (1989) European Biophysics Journal , vol.17 , Issue.2 , pp. 61-68
    • Veretout, F.1    Tardieu, A.2
  • 4
    • 0023942003 scopus 로고
    • Rat lens gamma-crystallins. Characterization of the six gene products and their spatial and temporal distribution resulting from differential synthesis
    • Siezen R J, Wu E, Kaplan E D, Thomson J A and Benedek G B 1988 Rat lens gamma-crystallins. Characterization of the six gene products and their spatial and temporal distribution resulting from differential synthesis J. Mol. Biol. 199 475-90
    • (1988) J. Mol. Biol. , vol.199 , Issue.3 , pp. 475-490
    • Siezen, R.J.1    Wu, E.2    Kaplan, E.D.3    Thomson, J.A.4    Benedek, G.B.5
  • 7
    • 38849146266 scopus 로고    scopus 로고
    • Distribution of bovine and rabbit lens α-crystallin products by MALDI imaging mass spectrometry
    • Grey A C and Schey K L 2008 Distribution of bovine and rabbit lens alpha-crystallin products by MALDI imaging mass spectrometry Mol. Vis. 14 171-9 (Pubitemid 351194000)
    • (2008) Molecular Vision , vol.14 , pp. 171-179
    • Grey, A.C.1    Schey, K.L.2
  • 8
    • 47249146855 scopus 로고    scopus 로고
    • Patterns of crystallin distribution in porcine eye lenses
    • Keenan J, Orr D F and Pierscionek B K 2008 Patterns of crystallin distribution in porcine eye lenses Mol. Vis. 14 1245-53 (Pubitemid 351984372)
    • (2008) Molecular Vision , vol.14 , pp. 1245-1253
    • Keenan, J.1    Orr, D.F.2    Pierscionek, B.K.3
  • 10
    • 12144251370 scopus 로고    scopus 로고
    • Transparency and non-refractive functions of crystallins - A proposal
    • DOI 10.1016/j.exer.2004.08.020, PII S0014483504002489, Dr. Abraham Spector International Symposium
    • Bhat S P 2004 Transparency and non-refractive functions of crystallins-a proposal Exp. Eye Res. 79 809-16 (Pubitemid 40103508)
    • (2004) Experimental Eye Research , vol.79 , Issue.6 , pp. 809-816
    • Bhat, S.P.1
  • 12
    • 0021925299 scopus 로고
    • Structural variation in lens crystallins
    • DOI 10.1016/0968-0004(85)90088-X
    • Slingsby C 1985 Structural variation in lens crystallins Trends Biochem. Sci. 10 281-4 (Pubitemid 15237497)
    • (1985) Trends in Biochemical Sciences , vol.10 , Issue.7 , pp. 281-284
    • Slingsby, C.1
  • 13
    • 0024309379 scopus 로고
    • Packing interactions in the eye-lens. Structural analysis, internal symmetry and lattice interactions of bovine γIVa-crystallin
    • DOI 10.1016/0022-2836(89)90452-X
    • White H E, Driessen H P, Slingsby C, Moss D S and Lindley P F 1989 Packing interactions in the eye-lens. Structural analysis, internal symmetry and lattice interactions of bovine gamma IVa-crystallin J. Mol. Biol. 207 217-35 (Pubitemid 19141253)
    • (1989) Journal of Molecular Biology , vol.207 , Issue.1 , pp. 217-235
    • White, H.E.1    Driessen, H.P.C.2    Slingsby, C.3    Moss, D.S.4    Lindley, P.F.5
  • 14
    • 0029644477 scopus 로고
    • The avian eye lens protein delta-crystallin shows a novel packing arrangement of tetramers in a supramolecular helix
    • Simpson A, Moss D and Slingsby C 1995 The avian eye lens protein delta-crystallin shows a novel packing arrangement of tetramers in a supramolecular helix Structure 3 403-12
    • (1995) Structure , vol.3 , Issue.4 , pp. 403-412
    • Simpson, A.1    Moss, D.2    Slingsby, C.3
  • 16
    • 1542646982 scopus 로고    scopus 로고
    • Gene sharing, lens crystallins and speculations on an eye/ear evolutionary relationship
    • Piatigorsky J 2003 Gene sharing, lens crystallins and speculations on an eye/ear evolutionary relationship Integr. Comp. Biol. 43 492-9 (Pubitemid 38335311)
    • (2003) Integrative and Comparative Biology , vol.43 , Issue.4 , pp. 492-499
    • Piatigorsky, J.1
  • 18
    • 0015022316 scopus 로고
    • Theory of transparency of the eye
    • Benedek G B 1971 Theory of transparency of the eye Appl. Opt. 10 459-73
    • (1971) Appl. Opt. , vol.10 , Issue.3 , pp. 459-473
    • Benedek, G.B.1
  • 19
    • 0020678719 scopus 로고
    • Short-range order of crystallin proteins account for eye lens transparency
    • DOI 10.1038/302415a0
    • Delaye M and Tardieu A 1983 Short-range order of crystallin proteins accounts for eye lens transparency Nature 302 415-7 (Pubitemid 13164324)
    • (1983) Nature , vol.302 , Issue.5907 , pp. 415-417
    • Delaye, M.1    Tardieu, A.2
  • 20
    • 77952242657 scopus 로고    scopus 로고
    • Small-angle x-ray scattering studies of the intact eye lens: Effect of crystallin composition and concentration on microstructure
    • Mirarefi A Y et al 2010 Small-angle x-ray scattering studies of the intact eye lens: effect of crystallin composition and concentration on microstructure Biochim. Biophys. Acta 1800 556-64
    • (2010) Biochim. Biophys. Acta , vol.1800 , pp. 556-564
    • Mirarefi, A.Y.1
  • 21
    • 0030954844 scopus 로고    scopus 로고
    • Cataract as a protein condensation disease: The Proctor lecture
    • Benedek G B 1997 Cataract as a protein condensation disease: the Proctor Lecture Invest. Ophthalmol. Vis. Sci. 38 1911-21 (Pubitemid 27407509)
    • (1997) Investigative Ophthalmology and Visual Science , vol.38 , Issue.10 , pp. 1911-1921
    • Benedek, G.B.1
  • 22
    • 61849122908 scopus 로고    scopus 로고
    • Genetics of crystallins: Cataract and beyond
    • Graw J 2009 Genetics of crystallins: cataract and beyond Exp. Eye Res. 88 173-89
    • (2009) Exp. Eye Res. , vol.88 , Issue.2 , pp. 173-189
    • Graw, J.1
  • 25
    • 0026483279 scopus 로고
    • Alpha-crystallin can function as a molecular chaperone
    • Horwitz J 1992 Alpha-crystallin can function as a molecular chaperone Proc. Natl Acad. Sci. USA 89 10449-53
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , Issue.21 , pp. 10449-10453
    • Horwitz, J.1
  • 28
    • 0024218965 scopus 로고
    • The evolution of lenticular proteins: The beta- and gamma-crystallin super gene family
    • Lubsen N H, Aarts H J and Schoenmakers J G 1988 The evolution of lenticular proteins: the beta- and gamma-crystallin super gene family Prog. Biophys. Mol. Biol. 51 47-76
    • (1988) Prog. Biophys. Mol. Biol. , vol.51 , Issue.1 , pp. 47-76
    • Lubsen, N.H.1    Aarts, H.J.2    Schoenmakers, J.G.3
  • 30
    • 17744391285 scopus 로고    scopus 로고
    • Unfolding crystallins: The destabilizing role of a beta-hairpin cysteine in betaB2-crystallin by simulation and experiment
    • MacDonald J T et al 2005 Unfolding crystallins: the destabilizing role of a beta-hairpin cysteine in betaB2-crystallin by simulation and experiment Protein Sci. 14 1282-92
    • (2005) Protein Sci. , vol.14 , Issue.5 , pp. 1282-1292
    • MacDonald, J.T.1
  • 31
    • 35648997078 scopus 로고    scopus 로고
    • Folding and stability of the isolated Greek key domains of the long-lived human lens proteins γD-crystallin and γS-crystallin
    • DOI 10.1110/ps.072970207
    • Mills I A, Flaugh S L, Kosinski-Collins M S and King J A 2007 Folding and stability of the isolated Greek key domains of the long-lived human lens proteins gammaD-crystallin and gammaS-crystallin Protein Sci. 16 2427-44 (Pubitemid 350036749)
    • (2007) Protein Science , vol.16 , Issue.11 , pp. 2427-2444
    • Mills, I.A.1    Flaugh, S.L.2    Kosinski-Collins, M.S.3    King, J.A.4
  • 32
    • 0026554096 scopus 로고
    • Protein interactions in the calf eye lens: Interactions between beta-crystallins are repulsive whereas in gamma-crystallins they are attractive
    • Tardieu A, Veretout F, Krop B and Slingsby C 1992 Protein interactions in the calf eye lens: interactions between beta-crystallins are repulsive whereas in gamma-crystallins they are attractive Eur. Biophys. J. 21 1-12
    • (1992) Eur. Biophys. J. , vol.21 , Issue.1 , pp. 1-12
    • Tardieu, A.1    Veretout, F.2    Krop, B.3    Slingsby, C.4
  • 33
    • 36048973994 scopus 로고    scopus 로고
    • New insight into cataract formation: Enhanced stability through mutual attraction
    • Stradner A, Foffi G, Dorsaz N, Thurston G and Schurtenberger P 2007 New insight into cataract formation: enhanced stability through mutual attraction Phys. Rev. Lett. 99 198103
    • (2007) Phys. Rev. Lett. , vol.99 , Issue.19 , pp. 198103
    • Stradner, A.1    Foffi, G.2    Dorsaz, N.3    Thurston, G.4    Schurtenberger, P.5
  • 34
    • 0023271853 scopus 로고
    • The refractive increments of bovine α-, β- and γ-crystallins
    • DOI 10.1016/0042-6989(87)90162-3
    • Pierscionek B, Smith G and Augusteyn R C 1987 The refractive increments of bovine alpha-, beta-, and gamma-crystallins Vis. Res. 27 1539-41 (Pubitemid 17145830)
    • (1987) Vision Research , vol.27 , Issue.9 , pp. 1539-1541
    • Pierscionek, B.1    Smith, G.2    Augusteyn, R.C.3
  • 35
    • 77957604070 scopus 로고    scopus 로고
    • Explosive expansion of betagamma-crystallin genes in the ancestral vertebrate
    • Kappe G, Purkiss A G, van Genesen S T, Slingsby C and Lubsen N H 2010 Explosive expansion of betagamma-crystallin genes in the ancestral vertebrate J. Mol. Evol. 71 219-30
    • (2010) J. Mol. Evol. , vol.71 , Issue.3 , pp. 219-230
    • Kappe, G.1    Purkiss, A.G.2    Van Genesen, S.T.3    Slingsby, C.4    Lubsen, N.H.5
  • 36
    • 79959699676 scopus 로고    scopus 로고
    • On the distribution of protein refractive index increments
    • Zhao H, Brown P H and Schuck P 2011 On the distribution of protein refractive index increments Biophys. J. 100 2309-17
    • (2011) Biophys. J. , vol.100 , Issue.9 , pp. 2309-2317
    • Zhao, H.1    Brown, P.H.2    Schuck, P.3
  • 38
    • 0028168127 scopus 로고
    • Characterization of gamma-crystallins from a hybrid teleosten fish: Multiplicity of isoforms as revealed by cDNA sequence analysis
    • DOI 10.1006/bbrc.1994.1960
    • Pan F M, Chang W C, Chao Y K and Chiou S H 1994 Characterization of gamma-crystallins from a hybrid teleostean fish: multiplicity of isoforms as revealed by cDNA sequence analysis Biochem. Biophys. Res. Commun. 202 527-34 (Pubitemid 2105413)
    • (1994) Biochemical and Biophysical Research Communications , vol.202 , Issue.1 , pp. 527-534
    • Pan, F.M.1    Chang, W.C.2    Chao, Y.K.3    Chiou, S.H.4
  • 40
    • 0026669302 scopus 로고
    • Characterization of squid crystallin genes. Comparison with mammalian glutathione S-transferase genes
    • Tomarev S I, Zinovieva R D and Piatigorsky J 1992 Characterization of squid crystallin genes. Comparison with mammalian glutathione S-transferase genes J. Biol. Chem. 267 8604-12
    • (1992) J. Biol. Chem. , vol.267 , pp. 8604-8612
    • Tomarev, S.I.1    Zinovieva, R.D.2    Piatigorsky, J.3
  • 41
    • 0035815743 scopus 로고    scopus 로고
    • The influence of macromolecular crowding and macromolecular confinement on biochemical reactions in physiological media
    • DOI 10.1074/jbc.R100005200
    • Minton A P 2001 The influence of macromolecular crowding and macromolecular confinement on biochemical reactions in physiological media J. Biol. Chem. 276 10577-80 (Pubitemid 38089223)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.14 , pp. 10577-10580
    • Minton, A.P.1
  • 42
    • 0035478585 scopus 로고    scopus 로고
    • Macromolecular crowding: Obvious but underappreciated
    • DOI 10.1016/S0968-0004(01)01938-7, PII S0968000401019387
    • Ellis R J 2001 Macromolecular crowding: obvious but underappreciated Trends Biochem. Sci. 26 597-604 (Pubitemid 32925190)
    • (2001) Trends in Biochemical Sciences , vol.26 , Issue.10 , pp. 597-604
    • Ellis R.John1
  • 43
    • 0041822089 scopus 로고    scopus 로고
    • Cell biology: Join the crowd
    • Ellis R J and Minton A P 2003 Cell biology: join the crowd Nature 425 27-8
    • (2003) Nature , vol.425 , Issue.6953 , pp. 27-28
    • Ellis, R.J.1    Minton, A.P.2
  • 44
    • 33746099650 scopus 로고    scopus 로고
    • Protein aggregation in crowded environments
    • DOI 10.1515/BC.2006.064, PII BCHM3875485
    • Ellis R J and Minton A P 2006 Protein aggregation in crowded environments Biol. Chem. 387 485-97 (Pubitemid 44071450)
    • (2006) Biological Chemistry , vol.387 , Issue.5 , pp. 485-497
    • Ellis, R.J.1    Minton, A.P.2
  • 45
    • 0035853141 scopus 로고    scopus 로고
    • Direct observation of the enhancement of noncooperative protein self-assembly by macromolecular crowding: Indefinite linear self-association of bacterial cell division protein FtsZ
    • DOI 10.1073/pnas.051634398
    • Rivas G, Fernandez J A and Minton A P 2001 Direct observation of the enhancement of noncooperative protein self-assembly by macromolecular crowding: indefinite linear self-association of bacterial cell division protein FtsZ Proc. Natl Acad. Sci. USA 98 3150-5 (Pubitemid 32220814)
    • (2001) Proceedings of the National Academy of Sciences of the United States of America , vol.98 , Issue.6 , pp. 3150-3155
    • Rivas, G.1    Fernandez, J.A.2    Minton, A.P.3
  • 46
    • 0242584670 scopus 로고    scopus 로고
    • Essential cell division protein FtsZ assembles into one monomer-thick ribbons under conditions resembling the crowded intracellular environment
    • DOI 10.1074/jbc.M305230200
    • Gonzalez J M et al 2003 Essential cell division protein FtsZ assembles into one monomer-thick ribbons under conditions resembling the crowded intracellular environment J. Biol. Chem. 278 37664-71 (Pubitemid 37175290)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.39 , pp. 37664-37671
    • Gonzalez, J.M.1    Jimenez, M.2    Velez, M.3    Mingorance, J.4    Andreu, J.M.5    Vicente, M.6    Rivas, G.7
  • 47
    • 67249144043 scopus 로고    scopus 로고
    • FtsZ condensates: An in vitro electron microscopy study
    • Popp D, Iwasa M, Narita A, Erickson H P and Maeda Y 2009 FtsZ condensates: an in vitro electron microscopy study Biopolymers 91 340-50
    • (2009) Biopolymers , vol.91 , Issue.5 , pp. 340-350
    • Popp, D.1    Iwasa, M.2    Narita, A.3    Erickson, H.P.4    Maeda, Y.5
  • 48
    • 0030981013 scopus 로고    scopus 로고
    • Macromolecular crowding: Effects on actin polymerisation
    • DOI 10.1016/S0301-4622(97)00011-2, PII S0301462297000112
    • Lindner R A and Ralston G B 1997 Macromolecular crowding: effects on actin polymerisation Biophys. Chem. 66 57-66 (Pubitemid 27264944)
    • (1997) Biophysical Chemistry , vol.66 , Issue.1 , pp. 57-66
    • Lindner, R.A.1    Ralston, G.B.2
  • 49
    • 0018114175 scopus 로고
    • Microtubule formation by pure brain tubulin in vitro. The influence of dextran and poly(ethylene glycol)
    • Herzog W and Weber K 1978 Microtubule formation by pure brain tubulin in vitro. The influence of dextran and poly(ethylene glycol) Eur. J. Biochem. 91 249-54 (Pubitemid 9072796)
    • (1978) European Journal of Biochemistry , vol.91 , Issue.1 , pp. 249-254
    • Herzog, W.1    Weber, K.2
  • 50
    • 0037177250 scopus 로고    scopus 로고
    • Molecular crowding accelerates fibrillization of α-synuclein: Could an increase in the cytoplasmic protein concentration induce Parkinson's disease?
    • DOI 10.1021/bi0120906
    • Shtilerman M D, Ding T T and Lansbury P T Jr 2002 Molecular crowding accelerates fibrillization of alpha-synuclein: could an increase in the cytoplasmic protein concentration induce Parkinson's disease? Biochemistry 41 3855-60 (Pubitemid 34251023)
    • (2002) Biochemistry , vol.41 , Issue.12 , pp. 3855-3860
    • Shtilerman, M.D.1    Ding, T.T.2    Lansbury Jr., P.T.3
  • 51
    • 0037040878 scopus 로고    scopus 로고
    • Macromolecular crowding accelerates amyloid formation by human apolipoprotein C-II
    • DOI 10.1074/jbc.M110429200
    • Hatters D M, Minton A P and Howlett G J 2002 Macromolecular crowding accelerates amyloid formation by human apolipoprotein C-II J. Biol. Chem. 277 7824-30 (Pubitemid 34968230)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.10 , pp. 7824-7830
    • Hatters, D.M.1    Minton, A.P.2    Howlett, G.J.3
  • 52
    • 67149087384 scopus 로고    scopus 로고
    • Accelerated fibrillation of alpha-synuclein induced by the combined action of macromolecular crowding and factors inducing partial folding
    • Munishkina L A, Fink A L and Uversky V N 2009 Accelerated fibrillation of alpha-synuclein induced by the combined action of macromolecular crowding and factors inducing partial folding Curr. Alzheimer Res. 6 252-60
    • (2009) Curr. Alzheimer Res. , vol.6 , Issue.3 , pp. 252-260
    • Munishkina, L.A.1    Fink, A.L.2    Uversky, V.N.3
  • 53
    • 29544433937 scopus 로고    scopus 로고
    • Macromolecular crowding in the Escherichia coli periplasm maintains α-synuclein disorder
    • DOI 10.1016/j.jmb.2005.11.033, PII S0022283605014208
    • McNulty B C, Young G B and Pielak G J 2006 Macromolecular crowding in the Escherichia coli periplasm maintains alpha-synuclein disorder J. Mol. Biol. 355 893-7 (Pubitemid 43012748)
    • (2006) Journal of Molecular Biology , vol.355 , Issue.5 , pp. 893-897
    • McNulty, B.C.1    Young, G.B.2    Pielak, G.J.3
  • 56
    • 0017615721 scopus 로고
    • Non-ideality and the thermodynamics of sickle-cell hemoglobin gelation
    • Minton A P 1977 Non-ideality and the thermodynamics of sickle-cell hemoglobin gelation J. Mol. Biol. 110 89-103
    • (1977) J. Mol. Biol. , vol.110 , Issue.1 , pp. 89-103
    • Minton, A.P.1
  • 57
    • 0017667829 scopus 로고
    • Thermodynamics of gelation of sickle cell deoxyhemoglobin
    • DOI 10.1016/0022-2836(77)90093-6
    • Ross P D, Hofrichter J and Eaton W A 1977 Thermodynamics of gelation of sickle cell deoxyhemoglobin J. Mol. Biol. 115 111-34 (Pubitemid 8198713)
    • (1977) Journal of Molecular Biology , vol.115 , Issue.2 , pp. 111-134
    • Ross, P.D.1    Hofrichter, J.2    Eaton, W.A.3
  • 58
    • 4544329005 scopus 로고    scopus 로고
    • Crowding and the polymerization of sickle hemoglobin
    • DOI 10.1002/jmr.698, EMBO Workshop on Biological Implications of Macromolecular Crowding
    • Ferrone F A and Rotter M A 2004 Crowding and the polymerization of sickle hemoglobin J. Mol. Recognit. 17 497-504 (Pubitemid 39218994)
    • (2004) Journal of Molecular Recognition , vol.17 , Issue.5 , pp. 497-504
    • Ferrone, F.A.1    Rotter, M.A.2
  • 59
    • 43649102320 scopus 로고    scopus 로고
    • Free energy of sickle hemoglobin polymerization: A scaled-particle treatment for use with dextran as a crowding agent
    • Liu Z, Weng W, Bookchin R M, Lew V L and Ferrone F A 2008 Free energy of sickle hemoglobin polymerization: a scaled-particle treatment for use with dextran as a crowding agent Biophys. J. 94 3629-34
    • (2008) Biophys. J. , vol.94 , Issue.9 , pp. 3629-3634
    • Liu, Z.1    Weng, W.2    Bookchin, R.M.3    Lew, V.L.4    Ferrone, F.A.5
  • 60
    • 84946636147 scopus 로고
    • Equations of state of hard body fluids
    • Boublik T 1986 Equations of state of hard body fluids Mol. Phys. 59 371-80
    • (1986) Mol. Phys. , vol.59 , Issue.2 , pp. 371-380
    • Boublik, T.1
  • 61
    • 0032311227 scopus 로고    scopus 로고
    • Molecular crowding: Analysis of effects of high concentrations of inert cosolutes on biochemical equilibria and rates in terms of volume exclusion
    • DOI 10.1016/S0076-6879(98)95038-8
    • Minton A P 1998 Molecular crowding: analysis of effects of high concentrations of inert cosolutes on biochemical equilibria and rates in terms of volume exclusion Methods Enzymol. 295 127-49 (Pubitemid 29349912)
    • (1998) Methods in Enzymology , vol.295 , pp. 127-149
    • Minton, A.P.1
  • 62
    • 36849110805 scopus 로고
    • Seventh virial coefficients for hard spheres and hard disks
    • Ree F and Hoover W 1967 Seventh virial coefficients for hard spheres and hard disks J. Chem. Phys. 46 4181-97
    • (1967) J. Chem. Phys. , vol.46 , Issue.11 , pp. 4181-4197
    • Ree, F.1    Hoover, W.2
  • 63
    • 0003628866 scopus 로고
    • Statistical mechanics of rigid spheres
    • Reiss H and Frisch H L 1959 Statistical mechanics of rigid spheres J. Chem. Phys. 31 369-80
    • (1959) J. Chem. Phys. , vol.31 , Issue.2 , pp. 369-380
    • Reiss, H.1    Frisch, H.L.2
  • 64
    • 11444250496 scopus 로고    scopus 로고
    • Scaled particle theory revisited: New conditions and improved predictions of the properties of the hard sphere fluid
    • DOI 10.1021/jp040398b
    • Heying M and Corti D S 2004 Scaled particle theory revisited: new conditions and improved predictions of the properties of the hard sphere fluid J. Phys. Chem. B 108 19756-68 (Pubitemid 40079474)
    • (2004) Journal of Physical Chemistry B , vol.108 , Issue.51 , pp. 19756-19768
    • Heying, M.1    Corti, D.S.2
  • 65
    • 0025608495 scopus 로고
    • The influence of macromolecular crowding on thermodynamic activity: Solubility and dimerization constants for spherical and dumbbell-shaped molecules in a hard-sphere mixture
    • Berg O G 1990 The influence of macromolecular crowding on thermodynamic activity: solubility and dimerization constants for spherical and dumbbell-shaped molecules in a hard-sphere mixture Biopolymers 30 1027-37
    • (1990) Biopolymers , vol.30 , Issue.11-12 , pp. 1027-1037
    • Berg, O.G.1
  • 66
    • 0017381152 scopus 로고
    • Analysis of non ideal behavior in concentrated hemoglobin solutions
    • Ross P D and Minton A P 1977 Analysis of non-ideal behavior in concentrated hemoglobin solutions J. Mol. Biol. 112 437-52 (Pubitemid 8109207)
    • (1977) Journal of Molecular Biology , vol.112 , Issue.3 , pp. 437-452
    • Ross, P.D.1    Minton, A.P.2
  • 68
    • 2942560499 scopus 로고    scopus 로고
    • A precise boundary element method for macromolecular transport properties
    • Aragon S 2004 A precise boundary element method for macromolecular transport properties J. Comput. Chem. 25 1191-205
    • (2004) J. Comput. Chem. , vol.25 , Issue.9 , pp. 1191-1205
    • Aragon, S.1
  • 69
    • 84985721961 scopus 로고
    • Light scattering of bovine serum albumin solutions: Extension of the hard particle model to allow for electrostatic repulsion
    • Minton A P and Edelhoch H 1982 Light scattering of bovine serum albumin solutions: extension of the hard particle model to allow for electrostatic repulsion Biopolymers 21 451-8
    • (1982) Biopolymers , vol.21 , Issue.2 , pp. 451-458
    • Minton, A.P.1    Edelhoch, H.2
  • 70
    • 0033746785 scopus 로고    scopus 로고
    • Excluded volume in solvation: Sensitivity of scaled-particle theory to solvent size and density
    • Tang K E and Bloomfield V A 2000 Excluded volume in solvation: sensitivity of scaled-particle theory to solvent size and density Biophys. J. 79 2222-34
    • (2000) Biophys. J. , vol.79 , Issue.5 , pp. 2222-2234
    • Tang, K.E.1    Bloomfield, V.A.2
  • 71
    • 0020617086 scopus 로고
    • X-ray analysis of the eye lens protein γ-II crystallin at 1.9 Å resolution
    • Wistow G et al 1983 X-ray analysis of the eye lens protein gamma-II crystallin at 1.9 A resolution J. Mol. Biol. 170 175-202 (Pubitemid 13013747)
    • (1983) Journal of Molecular Biology , vol.170 , Issue.1 , pp. 175-202
    • Wistow, G.1    Turnell, B.2    Summers, L.3
  • 74
    • 0030040281 scopus 로고    scopus 로고
    • Phase separation in aqueous solutions of lens gamma-crystallins: Special role of gamma s
    • Liu C et al 1996 Phase separation in aqueous solutions of lens gamma-crystallins: special role of gamma s Proc. Natl Acad. Sci. USA 93 377-82
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , Issue.1 , pp. 377-382
    • Liu, C.1
  • 77
    • 0026448778 scopus 로고
    • Model for the role of macromolecular crowding in regulation of cellular volume
    • Minton A P, Colclasure G C and Parker J C 1992 Model for the role of macromolecular crowding in regulation of cellular volume Proc. Natl Acad. Sci. USA 89 10504-6
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , Issue.21 , pp. 10504-10506
    • Minton, A.P.1    Colclasure, G.C.2    Parker, J.C.3
  • 78
    • 0026726181 scopus 로고
    • Macromolecular crowding and volume perception in dog red cells
    • Parker J C and Colclasure G C 1992 Macromolecular crowding and volume perception in dog red cells Mol. Cell Biochem. 114 9-11
    • (1992) Mol. Cell Biochem. , vol.114 , Issue.1-2 , pp. 9-11
    • Parker, J.C.1    Colclasure, G.C.2
  • 79
    • 38149048416 scopus 로고    scopus 로고
    • The effective hard particle model provides a simple, robust, and broadly applicable description of nonideal behavior in concentrated solutions of bovine serum albumin and other nonassociating proteins
    • Minton A P 2007 The effective hard particle model provides a simple, robust, and broadly applicable description of nonideal behavior in concentrated solutions of bovine serum albumin and other nonassociating proteins J. Pharm. Sci. 96 3466-9
    • (2007) J. Pharm. Sci. , vol.96 , Issue.12 , pp. 3466-3469
    • Minton, A.P.1
  • 80
    • 0028959686 scopus 로고
    • Analyses of thermodynamic data for concentrated hemoglobin solutions using scaled particle theory: Implications for a simple two-state model of water in thermodynamic analyses of crowding in vitro and in vivo
    • Guttman H J, Anderson C F and Record M T Jr 1995 Analyses of thermodynamic data for concentrated hemoglobin solutions using scaled particle theory: implications for a simple two-state model of water in thermodynamic analyses of crowding in vitro and in vivo Biophys. J. 68 835-46
    • (1995) Biophys. J. , vol.68 , Issue.3 , pp. 835-846
    • Guttman, H.J.1    Anderson, C.F.2    Record, M.T.3
  • 81
    • 33747874110 scopus 로고
    • Distribution of sodium and potassium within cattle lens
    • Amoore J E, Bartley W and Van Heyningen R 1959 Distribution of sodium and potassium within cattle lens Biochem. J. 72 126-33
    • (1959) Biochem. J. , vol.72 , pp. 126-133
    • Amoore, J.E.1    Bartley, W.2    Van Heyningen, R.3
  • 82
    • 0024599510 scopus 로고
    • Local variation in absolute water content of human and rabbit eye lenses measured by Raman microspectroscopy
    • DOI 10.1016/0014-4835(89)90032-8
    • Huizinga A, Bot A C C, De Mul F F M, Vrensen G F and Greve J 1989 Local variation in absolute water content of human and rabbit eye lenses measured by Raman microspectroscopy Exp. Eye Res. 48 487-96 (Pubitemid 19123500)
    • (1989) Experimental Eye Research , vol.48 , Issue.4 , pp. 487-496
    • Huizinga, A.1    Bot, A.C.C.2    De Mul, F.F.M.3    Vrensen, G.F.J.M.4    Greve, J.5
  • 83
    • 84954358401 scopus 로고    scopus 로고
    • Refractive index measurement of the isolated crystalline lens using optical coherence tomography
    • Uhlhorn S R, Borja D, Manns F and Parel J M 2008 Refractive index measurement of the isolated crystalline lens using optical coherence tomography Vis. Res. 48 2732-8
    • (2008) Vis. Res. , vol.48 , Issue.27 , pp. 2732-2738
    • Uhlhorn, S.R.1    Borja, D.2    Manns, F.3    Parel, J.M.4
  • 84
    • 0021039895 scopus 로고
    • Interactions of lens proteins. Self-association and mixed-association studies of bovine α-crystallin and γ-crystallin
    • DOI 10.1016/0301-4622(83)80030-1
    • Siezen R J and Owen E A 1983 Interactions of lens proteins. Self-association and mixed-association studies of bovine alpha-crystallin and gamma-crystallin Biophys. Chem. 18 181-94 (Pubitemid 14236712)
    • (1983) Biophysical Chemistry , vol.18 , Issue.3 , pp. 181-194
    • Siezen, R.J.1    Owen, E.A.2
  • 85
    • 0026570857 scopus 로고
    • Solid-liquid phase boundaries of lens protein solutions
    • Berland C R et al 1992 Solid-liquid phase boundaries of lens protein solutions Proc. Natl Acad. Sci. USA 89 1214-8
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , Issue.4 , pp. 1214-1218
    • Berland, C.R.1
  • 86
    • 0021265902 scopus 로고
    • Measurement of refractive index in an intact crystalline lens
    • DOI 10.1016/0042-6989(84)90039-7
    • Campbell M C 1984 Measurement of refractive index in an intact crystalline lens Vis. Res. 24 409-15 (Pubitemid 14105999)
    • (1984) Vision Research , vol.24 , Issue.5 , pp. 409-415
    • Campbell, M.C.W.1
  • 87
    • 0343525158 scopus 로고
    • Optical properties of a cephalopod eye
    • Sivak J G 1982 Optical properties of a cephalopod eye J. Comp. Physiol. 147 323-7
    • (1982) J. Comp. Physiol. , vol.147 , Issue.3 , pp. 323-327
    • Sivak, J.G.1
  • 88
    • 0030247336 scopus 로고    scopus 로고
    • A wide-angle gradient index optical model of the crystalline lens and eye of the rainbow trout
    • DOI 10.1016/0042-6989(95)00328-2
    • Jagger W S and Sands P J 1996 A wide-angle gradient index optical model of the crystalline lens and eye of the rainbow trout Vis. Res. 36 2623-39 (Pubitemid 26270892)
    • (1996) Vision Research , vol.36 , Issue.17 , pp. 2623-2639
    • Jagger, W.S.1    Sands, P.J.2


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