메뉴 건너뛰기




Volumn 100, Issue 2, 2011, Pages 498-506

Separating instability from aggregation propensity in γS-crystallin variants

Author keywords

[No Author keywords available]

Indexed keywords


EID: 78751691643     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2010.12.3691     Document Type: Article
Times cited : (64)

References (67)
  • 1
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • Chiti, F., and C. M. Dobson. 2006. Protein misfolding, functional amyloid, and human disease. Annu. Rev. Biochem. 75:333-366.
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 2
    • 0031056829 scopus 로고    scopus 로고
    • Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis
    • Booth, D. R., M. Sunde,..., M. B. Pepys. 1997. Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis. Nature. 385:787-793.
    • (1997) Nature , vol.385 , pp. 787-793
    • Booth, D.R.1    Sunde, M.2    Pepys, M.B.3
  • 3
    • 0027506498 scopus 로고
    • Human lysozyme gene mutations cause hereditary systemic amyloidosis
    • Pepys, M. B., P. N. Hawkins,..., J. J. Hsuan. 1993. Human lysozyme gene mutations cause hereditary systemic amyloidosis. Nature. 362:553-557.
    • (1993) Nature , vol.362 , pp. 553-557
    • Pepys, M.B.1    Hawkins, P.N.2    Hsuan, J.J.3
  • 4
    • 0033574161 scopus 로고    scopus 로고
    • Influence of amino acid substitutions related to inherited human prion diseases on the thermodynamic stability of the cellular prion protein
    • Liemann, S., and R. Glockshuber. 1999. Influence of amino acid substitutions related to inherited human prion diseases on the thermodynamic stability of the cellular prion protein. Biochemistry. 38:3258-3267.
    • (1999) Biochemistry , vol.38 , pp. 3258-3267
    • Liemann, S.1    Glockshuber, R.2
  • 5
    • 0037551741 scopus 로고    scopus 로고
    • Protofibrils, pores, fibrils, and neurodegeneration: Separating the responsible protein aggregates from the innocent bystanders
    • Caughey, B., and P. T. Lansbury. 2003. Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders. Annu. Rev. Neurosci. 26:267-298.
    • (2003) Annu. Rev. Neurosci. , vol.26 , pp. 267-298
    • Caughey, B.1    Lansbury, P.T.2
  • 6
    • 3142615402 scopus 로고    scopus 로고
    • The residue 129 polymorphism in human prion protein does not confer susceptibility to creutzfeldt-jakob disease by altering the structure or global stability of prpc
    • Hosszu, L. L. P., G. S. Jackson,..., J. Collinge. 2004. The residue 129 polymorphism in human prion protein does not confer susceptibility to Creutzfeldt-Jakob disease by altering the structure or global stability of PrPC. J. Biol. Chem. 279:28515-28521.
    • (2004) J. Biol. Chem. , vol.279 , pp. 28515-28521
    • Hosszu, L.L.P.1    Jackson, G.S.2    Collinge, J.3
  • 7
    • 69249123818 scopus 로고    scopus 로고
    • Prion proteins with pathogenic and protective mutations show similar structure and dynamics
    • Bae, S.-H., G. Legname,..., H. J. Dyson. 2009. Prion proteins with pathogenic and protective mutations show similar structure and dynamics. Biochemistry. 48:8120-8128.
    • (2009) Biochemistry , vol.48 , pp. 8120-8128
    • Bae, S.-H.1    Legname, G.2    Dyson, H.J.3
  • 8
    • 0035037143 scopus 로고    scopus 로고
    • A proposed structural model for amyloid fibril elongation: Domain swapping forms an interdigitating β-structure polymer
    • Sinha, N., C. Tsai, and R. Nussinov. 2001. A proposed structural model for amyloid fibril elongation: domain swapping forms an interdigitating β-structure polymer. Protein Eng. 14:93-103.
    • (2001) Protein Eng. , vol.14 , pp. 93-103
    • Sinha, N.1    Tsai, C.2    Nussinov, R.3
  • 9
    • 0035127031 scopus 로고    scopus 로고
    • A domain-swapped rnase a dimer with implications for amyloid formation
    • Liu, Y., G. Gotte,..., D. Eisenberg. 2001. A domain-swapped RNase A dimer with implications for amyloid formation. Nat. Struct. Biol. 8:211-214.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 211-214
    • Liu, Y.1    Gotte, G.2    Eisenberg, D.3
  • 10
    • 0345869697 scopus 로고    scopus 로고
    • Cystatin forms a tetramer through structural rearrangement of domain-swapped dimers prior to amyloidogenesis
    • Sanders, A., C. Jeremy Craven,..., R. A. Staniforth. 2004. Cystatin forms a tetramer through structural rearrangement of domain-swapped dimers prior to amyloidogenesis. J. Mol. Biol. 336:165-178.
    • (2004) J. Mol. Biol. , vol.336 , pp. 165-178
    • Sanders, A.1    Craven, C.J.2    Staniforth, R.A.3
  • 11
    • 9144264986 scopus 로고    scopus 로고
    • Polyglutamine expansion in ataxin-3 does not affect protein stability: Implications for misfolding and disease
    • Chow, M. K., A. M. Ellisdon,..., S. P. Bottomley. 2004. Polyglutamine expansion in ataxin-3 does not affect protein stability: implications for misfolding and disease. J. Biol. Chem. 279:47643-47651.
    • (2004) J. Biol. Chem. , vol.279 , pp. 47643-47651
    • Chow, M.K.1    Ellisdon, A.M.2    Bottomley, S.P.3
  • 12
    • 2942748436 scopus 로고    scopus 로고
    • Oligomeric assembly of native-like precursors precedes amyloid formation by β-2 microglobulin
    • Eakin, C. M., F. J. Attenello,..., A. D. Miranker. 2004. Oligomeric assembly of native-like precursors precedes amyloid formation by β-2 microglobulin. Biochemistry. 43:7808-7815.
    • (2004) Biochemistry , vol.43 , pp. 7808-7815
    • Eakin, C.M.1    Attenello, F.J.2    Miranker, A.D.3
  • 13
    • 57749098600 scopus 로고    scopus 로고
    • Amyloid formation by globular proteins under native conditions
    • Chiti, F., and C. M. Dobson. 2009. Amyloid formation by globular proteins under native conditions. Nat. Chem. Biol. 5:15-22.
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 15-22
    • Chiti, F.1    Dobson, C.M.2
  • 14
    • 61949248657 scopus 로고    scopus 로고
    • Effect of dehydration on the aggregation kinetics of two amyloid peptides
    • Mukherjee, S., P. Chowdhury, and F. Gai. 2009. Effect of dehydration on the aggregation kinetics of two amyloid peptides. J. Phys. Chem. B. 113:531-535.
    • (2009) J. Phys. Chem. B , vol.113 , pp. 531-535
    • Mukherjee, S.1    Chowdhury, P.2    Gai, F.3
  • 15
    • 70449584579 scopus 로고    scopus 로고
    • 2d ir provides evidence for mobile water molecules in β-amyloid fibrils
    • Kim, Y. S., L. Liu,..., R. M. Hochstrasser. 2009. 2D IR provides evidence for mobile water molecules in β-amyloid fibrils. Proc. Natl. Acad. Sci. USA. 106:17751-17756.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 17751-17756
    • Kim, Y.S.1    Liu, L.2    Hochstrasser, R.M.3
  • 16
    • 75649120781 scopus 로고    scopus 로고
    • Influence of the solvent on the self-assembly of a modified amyloid β Peptide fragment. Ii. Nmr and computer simulation investigation
    • Hamley, I. W., D. R. Nutt,..., F. Rodríguez-Llansola. 2010. Influence of the solvent on the self-assembly of a modified amyloid β peptide fragment. II. NMR and computer simulation investigation. J. Phys. Chem. B. 114:940-951.
    • (2010) J. Phys. Chem. B , vol.114 , pp. 940-951
    • Hamley, I.W.1    Nutt, D.R.2    Rodríguez-Llansola, F.3
  • 17
    • 0026483279 scopus 로고
    • α-crystallin can function as a Molecular chaperone
    • Horwitz, J. 1992. α-Crystallin can function as a molecular chaperone. Proc. Natl. Acad. Sci. USA. 89:10449-10453.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 10449-10453
    • Horwitz, J.1
  • 18
    • 40149109190 scopus 로고    scopus 로고
    • Amyloid fibril formation and chaperone-like activity of peptides from αa-crystallin
    • Tanaka, N., R. Tanaka,..., D. Hamada. 2008. Amyloid fibril formation and chaperone-like activity of peptides from αA-crystallin. Biochemistry. 47:2961-2967.
    • (2008) Biochemistry , vol.47 , pp. 2961-2967
    • Tanaka, N.1    Tanaka, R.2    Hamada, D.3
  • 19
    • 0034734298 scopus 로고    scopus 로고
    • γS-crystallin of bovine and human eye lens: Solution structure, stability and folding of the intact two-domain protein and its separate domains
    • Wenk, M., R. Herbst,..., R. Jaenicke. 2000. γS-crystallin of bovine and human eye lens: solution structure, stability and folding of the intact two-domain protein and its separate domains. Biophys. Chem. 86:95-108.
    • (2000) Biophys. Chem. , vol.86 , pp. 95-108
    • Wenk, M.1    Herbst, R.2    Jaenicke, R.3
  • 20
    • 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
    • Mills, I. A., S. L. Flaugh,..., J. A. King. 2007. Folding and stability of the isolated Greek key domains of the long-lived human lens proteins γD-crystallin and γS-crystallin. Protein Sci. 16:2427-2444.
    • (2007) Protein Sci. , vol.16 , pp. 2427-2444
    • Mills, I.A.1    Flaugh, S.L.2    King, J.A.3
  • 21
    • 0020678719 scopus 로고
    • Short-range order of crystallin proteins accounts for eye lens transparency
    • Delaye, M., and A. Tardieu. 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
  • 22
    • 0026554096 scopus 로고
    • Protein interactions in the calf eye lens: Interactions between β-crystallins are repulsive whereas in γ-crystallins they are attractive
    • Tardieu, A., F. Vérétout,..., C. Slingsby. 1992. Protein interactions in the calf eye lens: interactions between β-crystallins are repulsive whereas in γ-crystallins they are attractive. Eur. Biophys. J. 21:1-12.
    • (1992) Eur. Biophys. J , vol.21 , pp. 1-12
    • Tardieu, A.1    Vérétout, F.2    Slingsby, C.3
  • 23
    • 38449111855 scopus 로고    scopus 로고
    • Formation of amyloid fibrils in vitro by human γd-crystallin and its isolated domains
    • Papanikolopoulou, K., I. Mills-Henry,..., J. King. 2008. Formation of amyloid fibrils in vitro by human γD-crystallin and its isolated domains. Mol. Vis. 14:81-89.
    • (2008) Mol. Vis. , vol.14 , pp. 81-89
    • Papanikolopoulou, K.1    Mills-Henry, I.2    King, J.3
  • 24
    • 77449100085 scopus 로고    scopus 로고
    • Formation of amyloid fibrils in vitro from partially unfolded intermediates of human γc-crystallin. Invest
    • Wang, Y., S. Petty,..., J. King. 2010. Formation of amyloid fibrils in vitro from partially unfolded intermediates of human γC-crystallin. Invest. Ophthalmol. Vis. Sci. 51:672-678.
    • (2010) Ophthalmol. Vis. Sci. , vol.51 , pp. 672-678
    • Wang, Y.1    Petty, S.2    King, J.3
  • 25
    • 44449156326 scopus 로고    scopus 로고
    • Age-dependent association of γ-crystallins with aged α-crystallins from old bovine lens
    • Takemoto, L., A. Ponce, and C. M. Sorensen. 2008. Age-dependent association of γ-crystallins with aged α-crystallins from old bovine lens. Mol. Vis. 14:970-974.
    • (2008) Mol. Vis. , vol.14 , pp. 970-974
    • Takemoto, L.1    Ponce, A.2    Sorensen, C.M.3
  • 26
    • 0038690113 scopus 로고    scopus 로고
    • Cross-β Order and diversity in nanocrystals of an amyloid-forming peptide
    • Diaz-Avalos, R., C. Long,..., D. L. Caspar. 2003. Cross-β order and diversity in nanocrystals of an amyloid-forming peptide. J. Mol. Biol. 330:1165-1175.
    • (2003) J. Mol. Biol. , vol.330 , pp. 1165-1175
    • Diaz-Avalos, R.1    Long, C.2    Caspar, D.L.3
  • 27
    • 34249290108 scopus 로고    scopus 로고
    • Atomic structures of amyloid cross-β Spines reveal varied steric zippers
    • Sawaya, M. R., S. Sambashivan,..., D. Eisenberg. 2007. Atomic structures of amyloid cross-β spines reveal varied steric zippers. Nature. 447:453-457.
    • (2007) Nature , vol.447 , pp. 453-457
    • Sawaya, M.R.1    Sambashivan, S.2    Eisenberg, D.3
  • 28
    • 33750826280 scopus 로고    scopus 로고
    • General structural motifs of amyloid protofilaments
    • Ferguson, N., J. Becker,..., A. R. Fersht. 2006. General structural motifs of amyloid protofilaments. Proc. Natl. Acad. Sci. USA. 103:16248-16253.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 16248-16253
    • Ferguson, N.1    Becker, J.2    Fersht, A.R.3
  • 29
    • 30744433878 scopus 로고    scopus 로고
    • Experimental constraints on quaternary structure in alzheimer's β-amyloid fibrils
    • Petkova, A. T., W. M. Yau, and R. Tycko. 2006. Experimental constraints on quaternary structure in Alzheimer's β-amyloid fibrils. Biochemistry. 45:498-512.
    • (2006) Biochemistry , vol.45 , pp. 498-512
    • Petkova, A.T.1    Yau, W.M.2    Tycko, R.3
  • 30
    • 38849108169 scopus 로고    scopus 로고
    • Solid-state nmr spectroscopy of amyloid proteins
    • Heise, H. 2008. Solid-state NMR spectroscopy of amyloid proteins. Chem Bio Chem. 9:179-189.
    • (2008) Chem. Bio Chem. , vol.9 , pp. 179-189
    • Heise, H.1
  • 31
    • 66149140617 scopus 로고    scopus 로고
    • Seeded growth of bamyloid fibrils from alzheimer's brain-derived fibrils produces a distinct fibril structure
    • Paravastu, A. K., I. Qahwash,..., R. Tycko. 2009. Seeded growth of bamyloid fibrils from Alzheimer's brain-derived fibrils produces a distinct fibril structure. Proc. Natl. Acad. Sci. USA. 106:7443-7448.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 7443-7448
    • Paravastu, A.K.1    Qahwash, I.2    Tycko, R.3
  • 32
    • 71549122584 scopus 로고    scopus 로고
    • Strategies for extracting structural information from 2d ir spectroscopy of amyloid: Application to islet amyloid polypeptide
    • Strasfeld, D. B., Y. L. Ling,..., M. T. Zanni. 2009. Strategies for extracting structural information from 2D IR spectroscopy of amyloid: application to islet amyloid polypeptide. J. Phys. Chem. B. 113:15679-15691.
    • (2009) J. Phys. Chem. B , vol.113 , pp. 15679-15691
    • Strasfeld, D.B.1    Ling, Y.L.2    Zanni, M.T.3
  • 33
    • 77952075172 scopus 로고    scopus 로고
    • Structural variations in the cross-β Core of amyloid β Fibrils revealed by deep uv resonance raman spectroscopy
    • Popova, L. A., R. Kodali,..., I. K. Lednev. 2010. Structural variations in the cross-β core of amyloid β fibrils revealed by deep UV resonance Raman spectroscopy. J. Am. Chem. Soc. 132:6324-6328.
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 6324-6328
    • Popova, L.A.1    Kodali, R.2    Lednev, I.K.3
  • 34
    • 0037040233 scopus 로고    scopus 로고
    • The x-ray crystal structure of human γS-crystallin c-terminal domain
    • Purkiss, A. G., O. A. Bateman,..., C. Slingsby. 2002. The X-ray crystal structure of human γS-crystallin C-terminal domain. J. Biol. Chem. 277:4199-4205.
    • (2002) J. Biol. Chem. , vol.277 , pp. 4199-4205
    • Purkiss, A.G.1    Bateman, O.A.2    Slingsby, C.3
  • 35
    • 28444452862 scopus 로고    scopus 로고
    • Solution structure of (γ) S-crystallin by Molecular fragment replacement nmr
    • Wu, Z., F. Delaglio,..., A. Bax. 2005. Solution structure of (γ) S-crystallin by molecular fragment replacement NMR. Protein Sci. 14:3101-3114.
    • (2005) Protein Sci. , vol.14 , pp. 3101-3114
    • Wu, Z.1    Delaglio, F.2    Bax, A.3
  • 36
    • 0031934121 scopus 로고    scopus 로고
    • Autosomal dominant congenital cataract associated with a missense mutation in the human a crystallin gene cryaa
    • Litt, M., P. Kramer,..., R. G. Weleber. 1998. Autosomal dominant congenital cataract associated with a missense mutation in the human a crystallin gene CRYAA. Hum. Mol. Genet. 7:471-474.
    • (1998) Hum. Mol. Genet. , vol.7 , pp. 471-474
    • Litt, M.1    Kramer, P.2    Weleber, R.G.3
  • 37
    • 33645401324 scopus 로고    scopus 로고
    • A novel αb-crystallin mutation associated with autosomal dominant congenital lamellar cataract. Invest
    • Liu, Y. Z., X. Y. Zhang,..., F. Shang. 2006. A novel αB-crystallin mutation associated with autosomal dominant congenital lamellar cataract. Invest. Ophthalmol. Vis. Sci. 47:1069-1075.
    • (2006) Ophthalmol. Vis. Sci. , vol.47 , pp. 1069-1075
    • Liu, Y.Z.1    Zhang, X.Y.2    Shang, F.3
  • 38
    • 0030914095 scopus 로고    scopus 로고
    • Autosomal dominant cerulean cataract is associated with a chain termination mutation in the human β-crystallin gene crybb2
    • Litt, M., R. Carrero-Valenzuela,..., I. H. Maumenee. 1997. Autosomal dominant cerulean cataract is associated with a chain termination mutation in the human β-crystallin gene CRYBB2. Hum. Mol. Genet. 6:665-668.
    • (1997) Hum. Mol. Genet. , vol.6 , pp. 665-668
    • Litt, M.1    Carrero-Valenzuela, R.2    Maumenee, I.H.3
  • 39
    • 24944483800 scopus 로고    scopus 로고
    • γ-s crystallin gene (crygs) mutation causes dominant progressive cortical cataract in humans
    • Sun, H., Z. Ma,..., Y. Shen. 2005. γ-S crystallin gene (CRYGS) mutation causes dominant progressive cortical cataract in humans. J. Med. Genet. 42:706-710.
    • (2005) J. Med. Genet. , vol.42 , pp. 706-710
    • Sun, H.1    Ma, Z.2    Shen, Y.3
  • 40
    • 40749099375 scopus 로고    scopus 로고
    • Mutation g61c in the crygd gene causing autosomal dominant congenital coralliform cataracts
    • Li, F. F., S. Z. Wang,..., X. Ma. 2008. Mutation G61C in the CRYGD gene causing autosomal dominant congenital coralliform cataracts. Mol. Vis. 14:378-386.
    • (2008) Mol. Vis. , vol.14 , pp. 378-386
    • Li, F.F.1    Wang, S.Z.2    Ma, X.3
  • 41
    • 0037449145 scopus 로고    scopus 로고
    • High-resolution x-ray crystal structures of human γd crystallin (1.25 a) and the r58h mutant (1.15 a) associated with aculeiform cataract
    • Basak, A., O. Bateman,..., J. Pande. 2003. High-resolution X-ray crystal structures of human γD crystallin (1.25 A) and the R58H mutant (1.15 A) associated with aculeiform cataract. J. Mol. Biol. 328:1137-1147.
    • (2003) J. Mol. Biol. , vol.328 , pp. 1137-1147
    • Basak, A.1    Bateman, O.2    Pande, J.3
  • 42
    • 0035933113 scopus 로고    scopus 로고
    • Crystal cataracts: Human genetic cataract caused by protein crystallization
    • Pande, A., J. Pande,..., G. B. Benedek. 2001. Crystal cataracts: human genetic cataract caused by protein crystallization. Proc. Natl. Acad. Sci. USA. 98:6116-6120.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 6116-6120
    • Pande, A.1    Pande, J.2    Benedek, G.B.3
  • 43
    • 14044262967 scopus 로고    scopus 로고
    • Decrease in protein solubility and cataract formation caused by the pro23 to thr mutation in human γ D-crystallin
    • Pande, A., O. Annunziata,..., J. Pande. 2005. Decrease in protein solubility and cataract formation caused by the Pro23 to Thr mutation in human γ D-crystallin. Biochemistry. 44:2491-2500.
    • (2005) Biochemistry , vol.44 , pp. 2491-2500
    • Pande, A.1    Annunziata, O.2    Pande, J.3
  • 44
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte, J., and R. F. Doolittle. 1982. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157:105-132.
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 45
    • 0000192486 scopus 로고
    • Sickle cell anemia a Molecular disease
    • Pauling, L., H. A. Itano,..., I. C. Wells. 1949. Sickle cell anemia a molecular disease. Science. 110:543-548.
    • (1949) Science , vol.110 , pp. 543-548
    • Pauling, L.1    Itano, H.A.2    Wells, I.C.3
  • 46
    • 33846016196 scopus 로고    scopus 로고
    • Metastable mesoscopic clusters in solutions of sickle-cell hemoglobin
    • DOI 10.1529/biophysj.106.094854
    • Pan, W., O. Galkin,..., P. G. Vekilov. 2007. Metastable mesoscopic clusters in solutions of sickle-cell hemoglobin. Biophys. J. 92:267-277. (Pubitemid 46048434)
    • (2007) Biophysical Journal , vol.92 , Issue.1 , pp. 267-277
    • Pan, W.1    Galkin, O.2    Filobelo, L.3    Nagel, R.L.4    Vekilov, P.G.5
  • 47
    • 77953148643 scopus 로고    scopus 로고
    • Origin of anomalous mesoscopic phases in protein solutions
    • Pan, W., P. G. Vekilov, and V. Lubchenko. 2010. Origin of anomalous mesoscopic phases in protein solutions. J. Phys. Chem. B. 114:7620-7630.
    • (2010) J. Phys. Chem. B , vol.114 , pp. 7620-7630
    • Pan, W.1    Vekilov, P.G.2    Lubchenko, V.3
  • 48
    • 68049104001 scopus 로고    scopus 로고
    • The G18V crygs mutation associated with human cataracts increases 7gamma;s-crystallin sensitivity to thermal and chemical stress
    • Ma, Z., G. Piszczek,..., J. F. Hejtmancik. 2009. The G18V CRYGS mutation associated with human cataracts increases 7gamma;S-crystallin sensitivity to thermal and chemical stress. Biochemistry. 48:7334-7341.
    • (2009) Biochemistry , vol.48 , pp. 7334-7341
    • Ma, Z.1    Piszczek, G.2    Hejtmancik, J.F.3
  • 49
    • 0031473847 scopus 로고    scopus 로고
    • Swiss-model and the swiss-pdbviewer: An environment for comparative protein modeling
    • Guex, N., and M. C. Peitsch. 1997. SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis. 18:2714-2723.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 50
    • 0042415783 scopus 로고    scopus 로고
    • Namd2: Greater scalability for parallel Molecular dynamics
    • Kale, L., R. Skeel,..., K. Schulten. 1999. NAMD2: greater scalability for parallel molecular dynamics. J. Comput. Phys. 151:283-312.
    • (1999) J. Comput. Phys. , vol.151 , pp. 283-312
    • Kale, L.1    Skeel, R.2    Schulten, K.3
  • 51
    • 0041784950 scopus 로고    scopus 로고
    • All-atom empirical potential for Molecular modeling and dynamics studies of proteins
    • MacKerell, Jr., A. D., D. Bashford., M. Karplus. 1998. All-atom empirical potential for molecular modeling and dynamics studies of proteins. J. Phys. Chem. B. 102:3586-3616.
    • (1998) J. Phys. Chem. B , vol.102 , pp. 3586-3616
    • MacKerell Jr., A.D.1    Bashford, D.2    Karplus, M.3
  • 52
    • 0004016501 scopus 로고
    • Comparison of simple potential functions for simulating liquid water
    • Jorgensen, W., J. Chandrasekhar,..., M. Klein. 1983. Comparison of simple potential functions for simulating liquid water. J. Chem. Phys. 79:926.
    • (1983) J. Chem. Phys. , vol.79 , pp. 926
    • Jorgensen, W.1    Chandrasekhar, J.2    Klein, M.3
  • 53
    • 33645961739 scopus 로고
    • A smooth particle mesh ewald method
    • Essmann, U., L. Perera,..., L. G. Pedersen. 1995. A smooth particle mesh Ewald method. J. Chem. Phys. 103:8577-8593.
    • (1995) J. Chem. Phys. , vol.103 , pp. 8577-8593
    • Essmann, U.1    Perera, L.2    Pedersen, L.G.3
  • 54
    • 0035449971 scopus 로고    scopus 로고
    • Optimized particlemesh ewald/multiple-time step integration for Molecular dynamics simulations
    • Batcho, P. F., D. A. Case, and T. Schlick. 2001. Optimized particlemesh Ewald/multiple-time step integration for molecular dynamics simulations. J. Chem. Phys. 115:4003-4018.
    • (2001) J. Chem. Phys. , vol.115 , pp. 4003-4018
    • Batcho, P.F.1    Case, D.A.2    Schlick, T.3
  • 55
    • 84963146276 scopus 로고
    • Generalized verlet algorithm for efficient Molecular dynamics simulations with longrange interactions
    • Grubmuller, H., H. Heller,..., K. Schulten. 1991. Generalized Verlet algorithm for efficient molecular dynamics simulations with longrange interactions. Mol. Simul. 6:121-142.
    • (1991) Mol. Simul. , vol.6 , pp. 121-142
    • Grubmuller, H.1    Heller, H.2    Schulten, K.3
  • 56
    • 36449007836 scopus 로고
    • Constant-pressure molecular-dynamics simulation-the langevin piston method
    • Feller, S. E., Y. Zhang,..., B. R. Brooks. 1995. Constant-pressure molecular-dynamics simulation-the Langevin piston method. J. Chem. Phys. 103:4613-4621.
    • (1995) J. Chem. Phys. , vol.103 , pp. 4613-4621
    • Feller, S.E.1    Zhang, Y.2    Brooks, B.R.3
  • 57
    • 36449003554 scopus 로고
    • Constant-pressure molecular-dynamics algorithms
    • Martyna, G. J., D. J. Tobias, and M. L. Klein. 1994. Constant-pressure molecular-dynamics algorithms. J. Chem. Phys. 101:4177-4189.
    • (1994) J. Chem. Phys. , vol.101 , pp. 4177-4189
    • Martyna, G.J.1    Tobias, D.J.2    Klein, M.L.3
  • 58
  • 59
    • 4444221565 scopus 로고    scopus 로고
    • Ucsf chimera-a visualization system for exploratory research and analysis
    • Pettersen, E. F., T. D. Goddard,..., T. E. Ferrin. 2004. UCSF Chimera-a visualization system for exploratory research and analysis. J. Comput. Chem. 25:1605-1612.
    • (2004) J. Comput. Chem. , vol.25 , pp. 1605-1612
    • Pettersen, E.F.1    Goddard, T.D.2    Ferrin, T.E.3
  • 60
    • 5344244656 scopus 로고    scopus 로고
    • R Development Core Team, R Foundation for Statistical Computing, Vienna, Austria
    • R Development Core Team. 2008. R: A Language and Environment for Statistical Computing. R Foundation for Statistical Computing, Vienna, Austria. http://www.R-project.org.
    • (2008) R: A Language and Environment for Statistical Computing
  • 61
    • 33750398103 scopus 로고    scopus 로고
    • Bio3d: An r package for the comparative analysis of protein structures
    • Grant, B. J., A. P. C. Rodrigues,..., L. S. Caves. 2006. Bio3d: an R package for the comparative analysis of protein structures. Bioinformatics. 22:2695-2696.
    • (2006) Bioinformatics , vol.22 , pp. 2695-2696
    • Grant, B.J.1    Rodrigues, A.P.C.2    Caves, L.S.3
  • 62
    • 66049087099 scopus 로고    scopus 로고
    • Mechanism of the very efficient quenching of tryptophan fluorescence in human γd-and γs-crystallins: The γ-crystallin fold may have evolved to protect tryptophan residues from ultraviolet photodamage
    • Chen, J., P. R. Callis, and J. King. 2009. Mechanism of the very efficient quenching of tryptophan fluorescence in human γD-and γS-crystallins: the γ-crystallin fold may have evolved to protect tryptophan residues from ultraviolet photodamage. Biochemistry. 48:3708-3716.
    • (2009) Biochemistry , vol.48 , pp. 3708-3716
    • Chen, J.1    Callis, P.R.2    King, J.3
  • 63
    • 70450161122 scopus 로고    scopus 로고
    • Femtosecond fluorescence spectra of tryptophan in human γ-crystallin mutants: Site-dependent ultrafast quenching
    • Xu, J., J. Chen,..., J. R. Knutson. 2009. Femtosecond fluorescence spectra of tryptophan in human γ-crystallin mutants: site-dependent ultrafast quenching. J. Am. Chem. Soc. 131:16751-16757.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 16751-16757
    • Xu, J.1    Chen, J.2    Knutson, J.R.3
  • 64
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of alzheimer's disease: Progress and problems on the road to therapeutics
    • Hardy, J., and D. J. Selkoe. 2002. The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science. 297:353-356.
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 65
    • 24144467366 scopus 로고    scopus 로고
    • Light-scattering studies of protein solutions: Role of hydration in weak protein-protein interactions
    • Paliwal, A., D. Asthagiri,..., M. E. Paulaitis. 2005. Light-scattering studies of protein solutions: role of hydration in weak protein-protein interactions. Biophys. J. 89:1564-1573.
    • (2005) Biophys. J , vol.89 , pp. 1564-1573
    • Paliwal, A.1    Asthagiri, D.2    Paulaitis, M.E.3
  • 66
    • 43049122273 scopus 로고    scopus 로고
    • Water in nonpolar confinement: From nanotubes to proteins and beyond
    • Rasaiah, J. C., S. Garde, and G. Hummer. 2008. Water in nonpolar confinement: from nanotubes to proteins and beyond. Annu. Rev. Phys. Chem. 59:713-740.
    • (2008) Annu. Rev. Phys. Chem. , vol.59 , pp. 713-740
    • Rasaiah, J.C.1    Garde, S.2    Hummer, G.3
  • 67
    • 0037046151 scopus 로고    scopus 로고
    • Islet amyloid: Phase partitioning and secondary nucleation are central to the mechanism of fibrillogenesis
    • Padrick, S. B., and A. D. Miranker. 2002. Islet amyloid: phase partitioning and secondary nucleation are central to the mechanism of fibrillogenesis. Biochemistry. 41:4694-4703.
    • (2002) Biochemistry , vol.41 , pp. 4694-4703
    • Padrick, S.B.1    Miranker, A.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.