메뉴 건너뛰기




Volumn 84, Issue , 2011, Pages 63-111

Lysozyme: A model protein for amyloid research

Author keywords

Amyloidogenesis; Fibril, L arginine; Inclusion body; Lysozyme self association; Systemic nonneuropathic amyloidosis

Indexed keywords


EID: 80051903352     PISSN: 18761623     EISSN: None     Source Type: Book Series    
DOI: 10.1016/B978-0-12-386483-3.00003-3     Document Type: Chapter
Times cited : (249)

References (165)
  • 1
    • 33847217198 scopus 로고    scopus 로고
    • Suppression of protein interactions by arginine: A proposed mechanism of the arginine effects
    • T. Arakawa, D. Ejima, K. Tsumoto, N. Obeyama, Y. Tanaka, and Y. Kita Suppression of protein interactions by arginine: a proposed mechanism of the arginine effects Biophys. Chem. 127 2007 1 8
    • (2007) Biophys. Chem. , vol.127 , pp. 1-8
    • Arakawa, T.1    Ejima, D.2    Tsumoto, K.3    Obeyama, N.4    Tanaka, Y.5    Kita, Y.6
  • 2
    • 0037466513 scopus 로고    scopus 로고
    • The effects of arginine on refolding of aggregated proteins: Not facilitate refolding, but suppress aggregation
    • DOI 10.1016/S0006-291X(03)00578-3
    • T. Arakawa, and K. Tsumoto The effects of arginine on refolding of aggregated proteins: not facilitate refolding, but suppress aggregation Biochem. Biophys. Res. Commun. 304 2003 148 152 (Pubitemid 36434209)
    • (2003) Biochemical and Biophysical Research Communications , vol.304 , Issue.1 , pp. 148-152
    • Arakawa, T.1    Tsumoto, K.2
  • 3
    • 11944257160 scopus 로고
    • Hen egg white lysozyme expressed in, and secreted from, Aspergillus niger is correctly processed and folded
    • D.B. Archer, D.J. Jeenes, D.A. MacKenzie, G. Brightwell, N. Lambert, and G. Lowe Hen egg white lysozyme expressed in, and secreted from, Aspergillus niger is correctly processed and folded Biotechnology (N.Y.) 8 1990 741 745
    • (1990) Biotechnology (N.Y.) , vol.8 , pp. 741-745
    • Archer, D.B.1    Jeenes, D.J.2    MacKenzie, D.A.3    Brightwell, G.4    Lambert, N.5    Lowe, G.6
  • 4
    • 0030579519 scopus 로고    scopus 로고
    • Method for increasing the yield of properly folded recombinant human gamma interferon from inclusion bodies
    • DOI 10.1016/S0168-1656(96)01636-7, PII S0168165696016367
    • D. Arora, and N. Khanna Method for increasing the yield of properly folded recombinant human gamma interferon from inclusion bodies J. Biotechnol. 52 1996 127 133 (Pubitemid 27141634)
    • (1996) Journal of Biotechnology , vol.52 , Issue.2 , pp. 127-133
    • Arora, D.1    Khanna, N.2
  • 5
    • 11244340520 scopus 로고    scopus 로고
    • Thermally induced fibrillar aggregation of hen egg white lysozyme
    • DOI 10.1529/biophysj.104.048819
    • L.N. Arnaudov, and R. de Vries Thermally induced fibrillar aggregation of Hen egg white Lysozyme Biophys. J. 88 2005 515 526 (Pubitemid 40070697)
    • (2005) Biophysical Journal , vol.88 , Issue.1 , pp. 515-526
    • Arnaudov, L.N.1    De Vries, R.2
  • 6
    • 34347383011 scopus 로고    scopus 로고
    • Systematic analysis of aggregates from 38 kinds of non disease-related proteins: Identifying the intrinsic propensity of polypeptides to form amyloid fibrils
    • DOI 10.1271/bbb.60718
    • Y. Aso, Shiraki K., and M. Takagi Systematic analysis of aggregates from 38 kinds of non disease-related proteins: identifying the intrinsic propensity of polypeptides to form amyloid fibrils Biosci. Biotechnol. Biochem. 71 2007 1313 1321 (Pubitemid 47164241)
    • (2007) Bioscience, Biotechnology and Biochemistry , vol.71 , Issue.5 , pp. 1313-1321
    • Aso, Y.1    Shiraki, K.2    Takagi, M.3
  • 7
    • 0030570086 scopus 로고    scopus 로고
    • Protein refolding at high concentration using size-exclusion chromatography
    • DOI 10.1002/(SICI)1097-0290(19960405)50:1<16::AID-BIT3>3.0.CO;2-4
    • B. Batas, and J.B. Chaudhuri Protein refolding at high concentration using size-exclusion chromatography Biotechnol. Bioeng. 50 1996 16 23 (Pubitemid 26086779)
    • (1996) Biotechnology and Bioengineering , vol.50 , Issue.1 , pp. 16-23
    • Batas, B.1    Chaudhuri, J.B.2
  • 8
    • 0033023784 scopus 로고    scopus 로고
    • Inclusion body purification and protein refolding using microfiltration and size exclusion chromatography
    • DOI 10.1016/S0168-1656(98)00197-7, PII S0168165698001977
    • B. Batas, C. Schiraldi, and J.B. Chaudhuri Inclusion body purification and protein refolding using microfiltration and size exclusion chromatography J. Biotechnol. 68 1999 149 158 (Pubitemid 29090357)
    • (1999) Journal of Biotechnology , vol.68 , Issue.2-3 , pp. 149-158
    • Batas, B.1    Schiraldi, C.2    Chaudhuri, J.B.3
  • 9
    • 15444374846 scopus 로고    scopus 로고
    • Role of arginine in the stabilization of proteins against aggregation
    • DOI 10.1021/bi047528r
    • B.M. Baynes, D.I.C. Wang, and B.L. Trout Role of arginine in stabilisation of proteins against aggregation Biochemistry 44 2005 4919 4925 (Pubitemid 40396770)
    • (2005) Biochemistry , vol.44 , Issue.12 , pp. 4919-4925
    • Baynes, B.M.1    Wang, D.I.C.2    Trout, B.L.3
  • 11
    • 0032667078 scopus 로고    scopus 로고
    • Effect of surfactants on the prevention of protein aggregation during unfolding and refolding processes - Comparison with molecular chaperone α-Crystallin
    • J. Bhattacharyya, and K.P. Das Effect of surfactants on the prevention of protein aggregation during unfolding and refolding processes - comparison with molecular chaperone α-Crystallin J. Dispers. Sci. Technol. 20 1999 1163 1178
    • (1999) J. Dispers. Sci. Technol. , vol.20 , pp. 1163-1178
    • Bhattacharyya, J.1    Das, K.P.2
  • 14
    • 0013852463 scopus 로고
    • Structure of hen egg-white lysozyme: A three-dimensional Fourier synthesis at 2 resolution
    • C.C.F. Blake, D.F. Koenig, G.A. Mair, A.C.T. North, D.C. Phillips, and V.R. Sarma Structure of hen egg-white lysozyme: a three-dimensional Fourier synthesis at 2 resolution Nature 206 1965 757 761
    • (1965) Nature , vol.206 , pp. 757-761
    • Blake, C.C.F.1    Koenig, D.F.2    Mair, G.A.3    North, A.C.T.4    Phillips, D.C.5    Sarma, V.R.6
  • 16
    • 0034241777 scopus 로고    scopus 로고
    • A novel variant of human lysozyme (T70N) is common in the normal population
    • D.R. Booth, M.B. Pepys, and P.N. Hawkins A novel variant of human lysozyme (T70N) is common in the normal population Hum. Mutat. 16 2000 180
    • (2000) Hum. Mutat. , vol.16 , pp. 180
    • Booth, D.R.1    Pepys, M.B.2    Hawkins, P.N.3
  • 19
    • 61849106912 scopus 로고    scopus 로고
    • Formation and dissolution of hen egg white lysozyme amyloid fibrils in protic ionic liquids
    • N. Byrne, and C.A. Angell Formation and dissolution of hen egg white lysozyme amyloid fibrils in protic ionic liquids Chem. Commun. 2009 1046 1048
    • (2009) Chem. Commun. , pp. 1046-1048
    • Byrne, N.1    Angell, C.A.2
  • 20
    • 0000385093 scopus 로고
    • The amino acid sequence of egg white lysozyme
    • R.E. Canfield The amino acid sequence of egg white lysozyme J. Biol. Chem. 238 1963 2698 2707
    • (1963) J. Biol. Chem. , vol.238 , pp. 2698-2707
    • Canfield, R.E.1
  • 21
    • 1642452936 scopus 로고    scopus 로고
    • Formation of amyloid fibrils from fully reduced hen egg white lysozyme
    • DOI 10.1110/ps.03183404
    • A. Cao, D. Hu, and L. Lai Formation of amyloid fibrils from fully reduced hen egg white lysozyme Protein Sci. 13 2004 319 324 (Pubitemid 38124952)
    • (2004) Protein Science , vol.13 , Issue.2 , pp. 319-324
    • Cao, A.1    Hu, D.2    Lai, L.3
  • 22
    • 0037071906 scopus 로고    scopus 로고
    • Construction and deconstruction of bacterial inclusion bodies
    • DOI 10.1016/S0168-1656(02)00032-9, PII S0168165602000329
    • M.M. Carrio, and A. Villaverde Construction and destruction of bacterial inclusion bodies J. Biotechnol. 96 2002 3 12 (Pubitemid 34876295)
    • (2002) Journal of Biotechnology , vol.96 , Issue.1 , pp. 3-12
    • Carrio, M.M.1    Villaverde, A.2
  • 24
    • 0014558453 scopus 로고
    • Mechanism of lysozyme action
    • D.M. Chipman, and N. Sharon Mechanism of lysozyme action Science 165 1969 454 465
    • (1969) Science , vol.165 , pp. 454-465
    • Chipman, D.M.1    Sharon, N.2
  • 25
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • DOI 10.1146/annurev.biochem.75.101304.123901
    • F. Chiti, and C.M. Dobson Protein misfolding, functional amyloid, and human disease Annu. Rev. Biochem. 75 2006 333 366 (Pubitemid 44118036)
    • (2006) Annual Review of Biochemistry , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 26
    • 0035313135 scopus 로고    scopus 로고
    • Protein refolding for industrial processes
    • D.B.E. Clark Protein refolding for industrial processes Curr. Opin. Biotechnol. 12 2001 202 207
    • (2001) Curr. Opin. Biotechnol. , vol.12 , pp. 202-207
    • Clark, D.B.E.1
  • 27
    • 33845213536 scopus 로고    scopus 로고
    • The formation of nematic liquid crystal phases by hen lysozyme amyloid fibrils
    • DOI 10.1021/ja064455l
    • A.M. Corrigan, C. Muller, and M.R. Krebs The formation of nematic liquid crystal phases by hen lysozyme amyloid fibrils J. Am. Chem. Soc. 128 2006 14740 14741 (Pubitemid 44851578)
    • (2006) Journal of the American Chemical Society , vol.128 , Issue.46 , pp. 14740-14741
    • Corrigan, A.M.1    Muller, C.2    Krebs, M.R.H.3
  • 28
    • 0014687514 scopus 로고
    • The dependence of lysozyme activity on pH and ionic strength
    • R.C. Davies, A. Neuberger, and B.M. Wilson The dependence of lysozyme activity on pH and ionic strength Biochim. Biophys. Acta 178 1969 294 305
    • (1969) Biochim. Biophys. Acta , vol.178 , pp. 294-305
    • Davies, R.C.1    Neuberger, A.2    Wilson, B.M.3
  • 29
    • 9444299029 scopus 로고    scopus 로고
    • Formation of amyloid aggregates from human lysozyme and its disease-associated variants using hydrostatic pressure
    • DOI 10.1096/fj.03-1072fje
    • F.G. De Felice, M.N.N. Vieira, M.L. Meirelles, L.A. Morozova-Roche, C.M. Dobson, and S.T. Ferreira Formation of amyloid aggregates from human lysozyme and its disease-associated variants using hydrostatic pressure FASEB J. 18 2004 1099 1101 (Pubitemid 39561536)
    • (2004) FASEB Journal , vol.18 , Issue.10 , pp. 1099-1101
    • De Felice, F.G.1    Vieira, M.N.N.2    Meirelles, M.N.L.3    Morozova-Roche, L.A.4    Dobson, C.M.5    Ferreira, S.T.6
  • 30
    • 0028053187 scopus 로고
    • Understanding how proteins fold: The lysozyme story so far
    • DOI 10.1016/0968-0004(94)90171-6
    • C.M. Dobson, P.A. Evans, and S.E. Radford Understanding how protein fold: the lysozyme story so far Trends Biochem. Sci. 19 1994 31 37 (Pubitemid 24028729)
    • (1994) Trends in Biochemical Sciences , vol.19 , Issue.1 , pp. 31-37
    • Dobson, C.M.1    Evans, P.A.2    Radford, S.E.3
  • 32
    • 33749831531 scopus 로고    scopus 로고
    • Normal and aberrant biological self-assembly: Insights from studies of human lysozyme and its amyloidogenic variants
    • M. Dumoulin, J.R. Kumita, and C.M. Dobson Normal and aberrant biological self-assembly: insights from studies of human lysozyme and its amyloidogenic variants Acc. Chem. Res. 39 2006 603 610
    • (2006) Acc. Chem. Res. , vol.39 , pp. 603-610
    • Dumoulin, M.1    Kumita, J.R.2    Dobson, C.M.3
  • 34
    • 33646349196 scopus 로고    scopus 로고
    • Methods for enhancing the accuracy and reproducibility of Congo red and thioflavin T assays
    • DOI 10.1016/j.ab.2006.03.015, PII S0003269706001801
    • R. Eisert, L. Felau, and L.R. Brown Methods for enhancing the accuracy and reproducibility of congo red and thioflavin T assays Anal. Biochem. 353 2006 144 146 (Pubitemid 43668937)
    • (2006) Analytical Biochemistry , vol.353 , Issue.1 , pp. 144-146
    • Eisert, R.1    Felau, L.2    Brown, L.R.3
  • 36
    • 0026658365 scopus 로고
    • A novel sequential procedure to enhance the renaturation of recombinant protein from Escherichia coli inclusion bodies
    • B. Fischer, B. Perry, I. Sumner, and P. Goodenough A novel sequential procedure to enhance the renaturation of recombinant protein from Escherichia coli inclusion bodies Protein Eng. 5 1992 593 596
    • (1992) Protein Eng. , vol.5 , pp. 593-596
    • Fischer, B.1    Perry, B.2    Sumner, I.3    Goodenough, P.4
  • 37
    • 0000646464 scopus 로고
    • On a remarkable bacteriolytic element found in tissues and secretions
    • A. Fleming On a remarkable bacteriolytic element found in tissues and secretions Proc. R. Soc. Lond. B 93 1922 306 317
    • (1922) Proc. R. Soc. Lond. B , vol.93 , pp. 306-317
    • Fleming, A.1
  • 38
  • 41
    • 0038161262 scopus 로고    scopus 로고
    • Effects of salt concentration on association of the amyloid protofilaments of Hen egg white lysozyme studied by time-resolved neutron scattering
    • DOI 10.1016/S0022-2836(03)00722-8
    • S. Fujiwara, F. Matsumoto, and Y. Yonezawa Effects of salt concentration on association of the amyloid protofilaments of hen egg white lysozyme studied by time-resolved neutron scattering J. Mol. Biol. 331 2003 21 28 (Pubitemid 36870773)
    • (2003) Journal of Molecular Biology , vol.331 , Issue.1 , pp. 21-28
    • Fujiwara, S.1    Matsumoto, F.2    Yonezawa, Y.3
  • 42
    • 0030474922 scopus 로고    scopus 로고
    • The structure, stability, and folding process of amyloidogenic mutant human lysozyme
    • J. Funahashi, K. Takano, K. Ogasahara, Y. Yamagata, and K. Yutani The structure, stability, and folding process of amyloidogenic mutant human lysozyme J. Biochem. (Tokyo) 120 1996 1216 1223 (Pubitemid 27029165)
    • (1996) Journal of Biochemistry , vol.120 , Issue.6 , pp. 1216-1223
    • Funahashi, J.1    Takano, K.2    Ogasahara, K.3    Yamagata, Y.4    Yutani, K.5
  • 43
    • 33646486372 scopus 로고    scopus 로고
    • Disulfide cross-linking protein represents a significant fraction of ALS-associated Cu, Zn-superoxide dismutase aggregation in spinal cords of model mice
    • Y. Furukawa, R. Fu, H.X. Deng, T. Siddique, and T.V. O'Halloran Disulfide cross-linking protein represents a significant fraction of ALS-associated Cu, Zn-superoxide dismutase aggregation in spinal cords of model mice Proc. Natl. Acad. Sci. USA 103 2006 7148 7153
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 7148-7153
    • Furukawa, Y.1    Fu, R.2    Deng, H.X.3    Siddique, T.4    O'Halloran, T.V.5
  • 44
    • 23044533315 scopus 로고    scopus 로고
    • Refolding of lysozyme at high concentration in batch and fed-batch operation
    • Y.G. Gao, Yi-Xin Guan, S.J. Yao, and M.G. Cho Refolding of lysozyme at high concentration in batch and fed-batch operation Korean J. Chem. Eng. 19 2002 871 875
    • (2002) Korean J. Chem. Eng. , vol.19 , pp. 871-875
    • Gao, Y.G.1    Guan, Y.-X.2    Yao, S.J.3    Cho, M.G.4
  • 47
    • 0021256895 scopus 로고
    • Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein
    • G.G. Glenner, and C.W. Wong Alzheimer's disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein Biochem. Biophys. Res. Commun. 120 1984 885 890 (Pubitemid 14104991)
    • (1984) Biochemical and Biophysical Research Communications , vol.120 , Issue.3 , pp. 885-890
    • Glenner, G.G.1    Wong, C.W.2
  • 50
    • 0035947463 scopus 로고    scopus 로고
    • Urea gradient size-exclusion chromatography enhanced the yield of lysozyme refolding
    • DOI 10.1016/S0021-9673(01)00766-X, PII S002196730100766X
    • Z. Gu, Z. Sua, and J.C. Janson Urea gradient size-exclusion chromatography enhanced the yield of lysozyme refolding J. Chromatogr. A 918 2001 311 318 (Pubitemid 32432935)
    • (2001) Journal of Chromatography A , vol.918 , Issue.2 , pp. 311-318
    • Gu, Z.1    Su, Z.2    Janson, J.-C.3
  • 51
    • 33847662852 scopus 로고    scopus 로고
    • Soluble protein oligomers in neurodegeneration: Lessons from the Alzheimer's amyloid β-peptide
    • DOI 10.1038/nrm2101, PII NRM2101
    • C. Haass, and D.J. Selkoe Soluble oligomers in neurodegeneration: lessons from the Alzheimer's amyloid beta-peptide Nat. Rev. Mol. Cell Biol. 8 2007 101 112 (Pubitemid 46432529)
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.2 , pp. 101-112
    • Haass, C.1    Selkoe, D.J.2
  • 53
    • 38449094348 scopus 로고    scopus 로고
    • Different molten globule-like folding intermediates of hen egg white lysozyme induced by high pH and tertiary butanol
    • DOI 10.1093/jb/mvm057
    • M. Hameed, B. Ahmad, K.M. Fazili, K. Andrabi, and R.H. Khan Different molten globule-like folding intermediates of hen egg white lysozyme induced by high pH and tertiary butanol J. Biochem. (Tokyo) 141 2007 573 583 (Pubitemid 351455304)
    • (2007) Journal of Biochemistry , vol.141 , Issue.4 , pp. 573-583
    • Hameed, M.1    Ahmad, B.2    Fazili, K.M.3    Andrabi, K.4    Khan, R.H.5
  • 54
    • 61549119795 scopus 로고    scopus 로고
    • Tertiary butanol induced amyloidogenesis of hen egg white lysozyme is facilitated by aggregation-prone alkali-induced molten globule like conformation state
    • M. Hameed, B. Ahmad, R.H. Khan, K.I. Andrabi, and K.M. Fazili Tertiary butanol induced amyloidogenesis of hen egg white lysozyme is facilitated by aggregation-prone alkali-induced molten globule like conformation state Protein Pept. Lett. 16 2009 56 60
    • (2009) Protein Pept. Lett. , vol.16 , pp. 56-60
    • Hameed, M.1    Ahmad, B.2    Khan, R.H.3    Andrabi, K.I.4    Fazili, K.M.5
  • 55
    • 0037473750 scopus 로고    scopus 로고
    • Prevention of transthyretin arnyloid disease by changing protein misfolding energetics
    • DOI 10.1126/science.1079589
    • P. Hammarstrom, R.L. Wiseman, E.T. Powers, and J.W. Kelly Prevention of transthyretin amyloid disease by changing protein misfolding energetics Science 299 2003 713 716 (Pubitemid 36159487)
    • (2003) Science , vol.299 , Issue.5607 , pp. 713-716
    • Hammarstrom, P.1    Wiseman, R.L.2    Powers, E.T.3    Kelly, J.W.4
  • 57
    • 0027507714 scopus 로고
    • Role of Arg115 in the catalytic action of human lysozyme. X-ray structure of His115 and Glu115 mutants
    • DOI 10.1006/jmbi.1993.1529
    • K. Harata, M. Muraki, and Y. Jigami Role of Arg115 in the catalytic action of human lysozyme. X ray structure of His115 and Glu115 mutants J. Mol. Biol. 233 1993 524 535 (Pubitemid 23299179)
    • (1993) Journal of Molecular Biology , vol.233 , Issue.3 , pp. 524-535
    • Harata, K.1    Muraki, M.2    Jigami, Y.3
  • 58
    • 46749117136 scopus 로고    scopus 로고
    • Molecular and cellular aspects of protein misfolding and disease
    • DOI 10.1096/fj.07-099671
    • E. Herczenik, and M.F.B.G. Gebbink Molecular and cellular aspects of protein misfolding and disease FASEB J. 22 2008 2115 2133 (Pubitemid 351948631)
    • (2008) FASEB Journal , vol.22 , Issue.7 , pp. 2115-2133
    • Herczenik, E.1    Gebbink, M.F.B.G.2
  • 59
    • 0026091723 scopus 로고
    • Effects of proline mutations on the unfolding and refolding of human lysozyme: The slow refolding kinetic phase does not result from proline cis-trans isomerisation
    • T. Herning, K. Yutani, Y. Taniyama, and M. Kikuchi Effects of proline mutations on the unfolding and refolding of human lysozyme: the slow refolding kinetic phase does not result from proline cis-trans isomerisation Biochemistry 30 1991 9882 9891
    • (1991) Biochemistry , vol.30 , pp. 9882-9891
    • Herning, T.1    Yutani, K.2    Taniyama, Y.3    Kikuchi, M.4
  • 60
    • 1842410676 scopus 로고    scopus 로고
    • Oxidative renaturation of lysozyme at high concentrations
    • DOI 10.1002/(SICI)1097-0290(19970505)54:3<221::AID-BIT3>3.0.CO;2-H
    • D.L. Hevehan, and D.B.E. Clark Oxidative renaturation of lysozyme at high concentrations Biotechnol. Bioeng. 54 1997 221 230 (Pubitemid 27176594)
    • (1997) Biotechnology and Bioengineering , vol.54 , Issue.3 , pp. 221-230
    • Hevehan, D.L.1    De Bernardez Clark, E.2
  • 61
    • 67650403403 scopus 로고    scopus 로고
    • Amyloid protofibrils of lysozyme nucleate and grow via oligomer fusion
    • S.E. Hill, J. Robinson, G. Matthews, and M. Muschol Amyloid protofibrils of lysozyme nucleate and grow via oligomer fusion Biophys. J. 96 2009 3781 3790
    • (2009) Biophys. J. , vol.96 , pp. 3781-3790
    • Hill, S.E.1    Robinson, J.2    Matthews, G.3    Muschol, M.4
  • 62
    • 45849109925 scopus 로고    scopus 로고
    • Characterization of amyloidogenesis of hen egg lysozyme in concentrated ethanol solution
    • M. Holley, C. Eginton, D. David Schaefer, and L.R. Brown Characterization of amyloidogenesis of hen egg lysozyme in concentrated ethanol solution Biochem. Biophys. Res. Commun. 373 2008 164 168
    • (2008) Biochem. Biophys. Res. Commun. , vol.373 , pp. 164-168
    • Holley, M.1    Eginton, C.2    David Schaefer, D.3    Brown, L.R.4
  • 63
    • 33645211553 scopus 로고    scopus 로고
    • Slow aggregation of lysozyme in alkaline pH monitored in real time employing the fluorescence anisotropy of covalently labeled dansyl probe
    • L. Homchaudhuri, S. Kumar, and R. Swaminathan Slow aggregation of lysozyme in alkaline pH monitored in real time employing the fluorescence anisotropy of covalently labeled dansyl probe FEBS Lett. 580 2006 2097 2101
    • (2006) FEBS Lett. , vol.580 , pp. 2097-2101
    • Homchaudhuri, L.1    Kumar, S.2    Swaminathan, R.3
  • 64
    • 67649616343 scopus 로고    scopus 로고
    • Cellular membrane disruption by amyloid fibrils involved intermolecular disulfide cross-linking
    • B. Huang, J. He, J. Ren, X.Y. Yan, and C.M. Zeng Cellular membrane disruption by amyloid fibrils involved intermolecular disulfide cross-linking Biochemistry 48 2009 5794 5800
    • (2009) Biochemistry , vol.48 , pp. 5794-5800
    • Huang, B.1    He, J.2    Ren, J.3    Yan, X.Y.4    Zeng, C.M.5
  • 65
    • 77956012715 scopus 로고    scopus 로고
    • Investigating the effects of sodium dodecyl sulfate on the aggregative behavior of hen egg-white lysozyme at acidic pH
    • Y-Tz Hung, M.-S. Lin, W.-Y. Chen, and S.S.-S. Wang Investigating the effects of sodium dodecyl sulfate on the aggregative behavior of hen egg-white lysozyme at acidic pH Colloids Surf. B Biointerfaces 81 2010 141 151
    • (2010) Colloids Surf. B Biointerfaces , vol.81 , pp. 141-151
    • Hung, Y.-T.1    Lin, M.-S.2    Chen, W.-Y.3    Wang, S.S.-S.4
  • 66
    • 80053097656 scopus 로고    scopus 로고
    • Kinetics of surfactant-induced aggregation of lysozyme studied by fluorescence spectroscopy
    • 10.1007/s10895-010-0749-3 21, 615-625
    • N. Jain, M. Bhattacharya, and S. Mukhopadhyay Kinetics of surfactant-induced aggregation of lysozyme studied by fluorescence spectroscopy J. Fluoresc. 2011 10.1007/s10895-010-0749-3 21, 615-625
    • (2011) J. Fluoresc.
    • Jain, N.1    Bhattacharya, M.2    Mukhopadhyay, S.3
  • 67
    • 0035839046 scopus 로고    scopus 로고
    • Structural diversity of ex vivo amyloid fibrils studied by cryo-electron microscopy
    • DOI 10.1006/jmbi.2001.4863
    • J.L. Jimenez, G.A. Tennent, M.B. Pepys, and H.R. Saibil Structural diversity of ex vivo amyloid fibrils studied by cryo-electron microscopy J. Mol. Biol. 311 2001 241 247 (Pubitemid 32744538)
    • (2001) Journal of Molecular Biology , vol.311 , Issue.2 , pp. 241-247
    • Jimenez, J.L.1    Tennent, G.2    Pepys, M.3    Saibil, H.R.4
  • 68
    • 0013852450 scopus 로고
    • Structure of some crystalline lysozyme-inhibitor complexes determined by X-ray analysis at 6 resolution
    • L.N. Johnson, and D.C. Phillips Structure of some crystalline lysozyme-inhibitor complexes determined by X-ray analysis at 6 resolution Nature 206 1965 761 763
    • (1965) Nature , vol.206 , pp. 761-763
    • Johnson, L.N.1    Phillips, D.C.2
  • 69
    • 84884027604 scopus 로고
    • Lysozyme
    • P. Boyer, D. Lardy, K. Myrback, Academic Press New York
    • P. Jolles Lysozyme P. Boyer, D. Lardy, K. Myrback, The "Enzymes", vol. 4 1960 Academic Press New York 421
    • (1960) The "Enzymes" , vol.4 VOL. , pp. 421
    • Jolles, P.1
  • 70
    • 1842384903 scopus 로고
    • Recent developments in the study of lysozymes
    • P. Jolles Recent developments in the study of lysozymes Angew. Chem. Int. Ed. Engl. 3 1964 28 36
    • (1964) Angew. Chem. Int. Ed. Engl. , vol.3 , pp. 28-36
    • Jolles, P.1
  • 71
    • 0000676684 scopus 로고
    • The chemical structure of hen's egg-white lysozyme: Detailed study
    • J. Jolles, J. Jauregui-Adell, and P. Jolles The chemical structure of hen's egg-white lysozyme: detailed study Biochim. Biophys. Acta 78 1963 668 689
    • (1963) Biochim. Biophys. Acta , vol.78 , pp. 668-689
    • Jolles, J.1    Jauregui-Adell, J.2    Jolles, P.3
  • 72
    • 0021490172 scopus 로고
    • What's new in lysozyme research?
    • P. Jolles, and J. Jolles What's new in lysozyme research? Mol. Cell. Biochem. 63 1984 165 189
    • (1984) Mol. Cell. Biochem. , vol.63 , pp. 165-189
    • Jolles, P.1    Jolles, J.2
  • 73
    • 0242668337 scopus 로고    scopus 로고
    • Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
    • DOI 10.1126/science.1079469
    • R. Kayed, E. Head, J.L. Thompson, T.M. Mclntire, S.C. Milton, and C.W. Cotman Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis Science 300 2003 486 489 (Pubitemid 36444329)
    • (2003) Science , vol.300 , Issue.5618 , pp. 486-489
    • Kayed, R.1    Head, E.2    Thompson, J.L.3    McIntire, T.M.4    Milton, S.C.5    Cotman, C.W.6    Glabel, C.G.7
  • 74
  • 77
    • 0034647438 scopus 로고    scopus 로고
    • Formation and seeding of amyloid fibrils from wild-type hen lysozyme and a peptide fragment from the β-Domain
    • M.R.H. Krebs, D.K. Wilkins, E.W. Chung, M.C. Pitkeathly, A.K. Chamberlain, and J. Zurdo Formation and seeding of amyloid fibrils from wild-type hen lysozyme and a peptide fragment from the β-Domain J. Mol. Biol. 300 2000 541 549
    • (2000) J. Mol. Biol. , vol.300 , pp. 541-549
    • Krebs, M.R.H.1    Wilkins, D.K.2    Chung, E.W.3    Pitkeathly, M.C.4    Chamberlain, A.K.5    Zurdo, J.6
  • 78
    • 33845637320 scopus 로고    scopus 로고
    • From the Polymorphism of Amyloid Fibrils to their Assembly Mechanism and Cytotoxicity
    • DOI 10.1016/S0065-3233(06)73007-8, PII S0065323306730078, Fibrous Proteins: Amyloids, Prions and Beta Proteins
    • L. Kreplak, and U. Aebi From the polymorphism of amyloid fibrils to their assembly mechanism and cytotoxicity Adv. Protein Chem. 73 2006 217 233 (Pubitemid 44960405)
    • (2006) Advances in Protein Chemistry , vol.73 , pp. 217-233
    • Kreplak, L.1    Aebi, U.2
  • 79
    • 54049088134 scopus 로고    scopus 로고
    • How do surfactants and DTT affect the size, dynamics, activity and growth of soluble lysozyme aggregates?
    • S. Kumar, V.K. Ravi, and R. Swaminathan How do surfactants and DTT affect the size, dynamics, activity and growth of soluble lysozyme aggregates? Biochem. J. 415 2008 275 288
    • (2008) Biochem. J. , vol.415 , pp. 275-288
    • Kumar, S.1    Ravi, V.K.2    Swaminathan, R.3
  • 80
    • 67349219351 scopus 로고    scopus 로고
    • Suppression of lysozyme aggregation at alkaline pH by tri-N-acetylchitotriose
    • S. Kumar, V.K. Ravi, and R. Swaminathan Suppression of lysozyme aggregation at alkaline pH by tri-N-acetylchitotriose Biochim. Biophys. Acta 1794 2009 913 920
    • (2009) Biochim. Biophys. Acta , vol.1794 , pp. 913-920
    • Kumar, S.1    Ravi, V.K.2    Swaminathan, R.3
  • 82
    • 0026666598 scopus 로고
    • Enthalpic destabilisation of a mutant human lysozyme lacking a disulfide bridge between cysteine-77 and cysteine-95
    • R. Kuroki, K. Inaka, Y. Taniyama, S. Kidokoro, M. Matsushima, and M. Kikuchi Enthalpic destabilisation of a mutant human lysozyme lacking a disulfide bridge between cysteine-77 and cysteine-95 Biochemistry 31 1992 8323 8328
    • (1992) Biochemistry , vol.31 , pp. 8323-8328
    • Kuroki, R.1    Inaka, K.2    Taniyama, Y.3    Kidokoro, S.4    Matsushima, M.5    Kikuchi, M.6
  • 83
    • 0036068851 scopus 로고    scopus 로고
    • Refolding human lysozyme produced as an inclusion body by urea concentration and pH gradient ion exchange chromatography
    • M. Li, and Z. Su Refolding human lysozyme produced as an inclusion body by urea concentration and pH gradient ion-exchange chromatography Chromatographia 56 2002 33 38 (Pubitemid 34765489)
    • (2002) Chromatographia , vol.56 , Issue.1-2 , pp. 33-38
    • Li, M.1    Su, Z.2
  • 84
    • 34250373347 scopus 로고    scopus 로고
    • Inhibition of amyloid fibrillization of hen egg-white lysozymes by rifampicin and p-benzoquinone
    • DOI 10.1021/bp060353n
    • V.H. Lieu, J.W. Wu, S.S.S. Wang, and C.H. Wu Inhibition of amyloid fibrillization of hen egg-white lysozymes by rifampicin and p-benzoquinone Biotechnol. Prog. 23 2007 698 706 (Pubitemid 46911197)
    • (2007) Biotechnology Progress , vol.23 , Issue.3 , pp. 698-706
    • Lieu, V.H.1    Wu, J.W.2    Wang, S.S.-S.3    Wu, C.-H.4
  • 85
    • 0028917544 scopus 로고
    • Effective renaturation of reduced lysozyme by gentle removal of urea
    • Y. Maeda, H. Koga, H. Yamada, T. Ueda, and T. Imoto Effective renaturation of reduced lysozyme by gentle removal of urea Protein Eng. 8 1995 201 205
    • (1995) Protein Eng. , vol.8 , pp. 201-205
    • Maeda, Y.1    Koga, H.2    Yamada, H.3    Ueda, T.4    Imoto, T.5
  • 86
    • 33845649258 scopus 로고    scopus 로고
    • Developments in biotechnological production of sweet proteins
    • DOI 10.1263/jbb.102.375, PII S1389172306706806
    • T. Masuda, and N. Kitabatake Developments in biotechnological production of sweet proteins J. Biosci. Bioeng. 102 2006 375 389 (Pubitemid 44960139)
    • (2006) Journal of Bioscience and Bioengineering , vol.102 , Issue.5 , pp. 375-389
    • Masuda, T.1    Kitabatake, N.2
  • 87
    • 10644257662 scopus 로고    scopus 로고
    • High yield secretion of the sweet-tasting protein lysozyme from the yeast Pichia pastoris
    • DOI 10.1016/j.pep.2004.09.009, PII S1046592804003171
    • T. Masuda, Y. Ueno, and N. Kitabatake High yield secretion of the sweet-tasting protein lysozyme from the yeast Pichia pastoris Protein Expr. Purif. 39 2005 35 42 (Pubitemid 39645381)
    • (2005) Protein Expression and Purification , vol.39 , Issue.1 , pp. 35-42
    • Masuda, T.1    Ueno, Y.2    Kitabatake, N.3
  • 91
    • 0042709605 scopus 로고    scopus 로고
    • Molecular mechanisms of amyloidosis
    • DOI 10.1056/NEJMra023144
    • G. Merlini, and V. Bellotti Molecular mechanisms of amyloidosis N. Engl. J. Med. 349 2003 583 596 (Pubitemid 36951371)
    • (2003) New England Journal of Medicine , vol.349 , Issue.6 , pp. 583-596
    • Merlini, G.1    Bellotti, V.2
  • 92
    • 0023398206 scopus 로고
    • Construction of a plasmid vector for the regulatable high level expression of eukaryotic genes in Escherichia coli: An application to overproduction of chicken lysozyme
    • T. Miki, T. Yasukochi, H. Nagatani, M. Furuno, T. Orita, and H. Yamada Construction of a plasmid vector for the regulatable high level expression of eukaryotic genes in Escherichia coli: an application to overproduction of chicken lysozyme Protein Eng. 1 1987 327 332
    • (1987) Protein Eng. , vol.1 , pp. 327-332
    • Miki, T.1    Yasukochi, T.2    Nagatani, H.3    Furuno, M.4    Orita, T.5    Yamada, H.6
  • 93
    • 33749321215 scopus 로고    scopus 로고
    • Amyloid formation in denatured single-mutant lysozymes where residual structures are modulated
    • DOI 10.1110/ps.062258206
    • T. Mishima, T. Ohkuri, A. Monji, T. Imoto, and T. Ueda Amyloid formation in denatured single-mutant lysozymes where residual structures are modulated Protein Sci. 15 2006 2448 2452 (Pubitemid 44496399)
    • (2006) Protein Science , vol.15 , Issue.10 , pp. 2448-2452
    • Mishima, T.1    Ohkuri, T.2    Monji, A.3    Imoto, T.4    Ueda, T.5
  • 94
    • 0026013162 scopus 로고
    • Demonstration by NMR of folding domains in lysozyme
    • A. Miranker, S.E. Radford, M. Karplus, and C.M. Dobson Demonstration by NMR of folding domains in lysozyme Nature 349 1991 633 636 (Pubitemid 21912122)
    • (1991) Nature , vol.349 , Issue.6310 , pp. 633-636
    • Miranker, A.1    Radford, S.E.2    Karplus, M.3    Dobson, C.M.4
  • 95
    • 33846562360 scopus 로고    scopus 로고
    • Lysozyme Amyloidogenesis Is Accelerated by Specific Nicking and Fragmentation but Decelerated by Intact Protein Binding and Conversion
    • DOI 10.1016/j.jmb.2006.11.084, PII S0022283606016433
    • R. Mishra, K. Sorgjerd, S. Nystrom, A. Yen-Chi Yu, and P. Hammarstrom Lysozyme amyloidogenesis is accelerated by specific nicking and fragmentation but decelerated by intact protein binding and conversion J. Mol. Biol. 366 2007 1029 1044 (Pubitemid 46175878)
    • (2007) Journal of Molecular Biology , vol.366 , Issue.3 , pp. 1029-1044
    • Mishra, R.1    Sorgjerd, K.2    Nystrom, S.3    Nordigarden, A.4    Yu, Y.-C.5    Hammarstrom, P.6
  • 96
    • 78650081316 scopus 로고    scopus 로고
    • Protein aggregation: From inclusion bodies to amyloid and biomaterials
    • A. Mitraki Protein aggregation: from inclusion bodies to amyloid and biomaterials Adv. Protein Chem. Struct. Biol. 79 2010 89 125
    • (2010) Adv. Protein Chem. Struct. Biol. , vol.79 , pp. 89-125
    • Mitraki, A.1
  • 98
    • 0033849915 scopus 로고    scopus 로고
    • Amyloid fibril formation and seeding by wild-type human lysozyme and its disease-related mutational variants
    • L.A. Morozova-Roche, J. Zurdo, A. Spencer, W. Noppe, V. Receveur, and D.B. Archer Amyloid fibril formation and seeding by wild-type human lysozyme and its disease-related mutational variants J. Struct. Biol. 130 2000 339 351
    • (2000) J. Struct. Biol. , vol.130 , pp. 339-351
    • Morozova-Roche, L.A.1    Zurdo, J.2    Spencer, A.3    Noppe, W.4    Receveur, V.5    Archer, D.B.6
  • 99
    • 76849089849 scopus 로고    scopus 로고
    • Chemical modification of lysine residues in lysozyme may dramatically influence its amyloid fibrillation
    • D. Morshedi, A. Ebrahim-Habibi, A.A. Moosavi-Movahedi, and M. Nemat-Gorgani Chemical modification of lysine residues in lysozyme may dramatically influence its amyloid fibrillation Biochim. Biophys. Acta 1804 2010 714 722
    • (2010) Biochim. Biophys. Acta , vol.1804 , pp. 714-722
    • Morshedi, D.1    Ebrahim-Habibi, A.2    Moosavi-Movahedi, A.A.3    Nemat-Gorgani, M.4
  • 100
    • 36749011905 scopus 로고    scopus 로고
    • Inhibition of amyloid fibrillation of lysozyme by indole derivatives - Possible mechanism of action
    • DOI 10.1111/j.1742-4658.2007.06158.x
    • D. Morshedi, N. Rezaei-Ghaleh, A. Ebrahim-Habibi, S. Ahmadian, and M. Nemat-Gorgani Inhibition of amyloid fibrillation of lysozyme by indole derivatives - possible mechanism of action FEBS J. 274 2007 6415 6425 (Pubitemid 350215930)
    • (2007) FEBS Journal , vol.274 , Issue.24 , pp. 6415-6425
    • Morshedi, D.1    Rezaei-Ghaleh, N.2    Ebrahim-Habibi, A.3    Ahmadian, S.4    Nemat-Gorgani, M.5
  • 103
    • 33845652277 scopus 로고    scopus 로고
    • Structural Models of Amyloid-Like Fibrils
    • DOI 10.1016/S0065-3233(06)73008-X, PII S006532330673008X, Fibrous Proteins: Amyloids, Prions and Beta Proteins
    • R. Nelson, and D. Eisenberg Structural models of amyloid-like fibrils Adv. Protein Chem. 73 2006 235 282 (Pubitemid 44960406)
    • (2006) Advances in Protein Chemistry , vol.73 , pp. 235-282
    • Nelson, R.1    Eisenberg, D.2
  • 105
    • 0022312788 scopus 로고
    • Expression of chicken egg white lysozyme by Saccharomyces cerevisiae
    • DOI 10.1016/0378-1119(85)90024-1
    • J. Oberto, and J. Davison Expression of chicken egg white lysozyme by Saccharomyces cerevisiae Gene 40 1985 57 65 (Pubitemid 16132026)
    • (1985) Gene , vol.40 , Issue.1 , pp. 57-65
    • Oberto, J.1    Davison, J.2
  • 106
    • 0013967156 scopus 로고
    • Serum and urinary lysozyme (muramidase) in monocytic and monomyelocytic leukemia
    • E.F. Osserman, and D.P. Lawlor Serum and urinary lysozyme (muramidase) in monocytic and monomyelocytic leukemia J. Exp. Med. 124 1966 921 952
    • (1966) J. Exp. Med. , vol.124 , pp. 921-952
    • Osserman, E.F.1    Lawlor, D.P.2
  • 107
    • 32944457929 scopus 로고    scopus 로고
    • Amyloidosis
    • DOI 10.1146/annurev.med.57.121304.131243
    • M.B. Pepys Amyloidosis Annu. Rev. Med. 57 2006 223 241 (Pubitemid 43261989)
    • (2006) Annual Review of Medicine , vol.57 , pp. 223-241
    • Pepys, M.B.1
  • 110
    • 0013971370 scopus 로고
    • The three-dimensional structure of an enzyme molecule
    • D.C. Phillips The three-dimensional structure of an enzyme molecule Sci. Am. 215 1966 78 90
    • (1966) Sci. Am. , vol.215 , pp. 78-90
    • Phillips, D.C.1
  • 111
    • 0000916620 scopus 로고
    • The hen egg-white lysozyme molecule
    • D.C. Phillips The hen egg-white lysozyme molecule Proc. Natl. Acad. Sci. USA 57 1967 484 495
    • (1967) Proc. Natl. Acad. Sci. USA , vol.57 , pp. 484-495
    • Phillips, D.C.1
  • 112
    • 84907133587 scopus 로고
    • Methods for staining amyloid in tissues: A review
    • H. Puchtler, and F. Sweat Methods for staining amyloid in tissues: a review Stain Technol. 63 1988 201 212
    • (1988) Stain Technol. , vol.63 , pp. 201-212
    • Puchtler, H.1    Sweat, F.2
  • 113
    • 0026751786 scopus 로고
    • The folding of hen lysozyme involves partially structured intermediates and multiple pathways
    • S.E. Radford, C.M. Dobson, and P.A. Evans The folding of hen lysozyme involves partially structured intermediates and multiple pathways Nature 358 1992 302 307
    • (1992) Nature , vol.358 , pp. 302-307
    • Radford, S.E.1    Dobson, C.M.2    Evans, P.A.3
  • 114
    • 15244343628 scopus 로고    scopus 로고
    • L-Arginine increases the solubility of unfolded species of hen egg white lysozyme
    • DOI 10.1110/ps.041085005
    • R.C.K. Reddy, H. Lilie, R. Rudolph, and C. Lange L-Arginine increases the solubility of unfolded species of hen egg white lysozyme Protein Sci. 14 2005 929 935 (Pubitemid 40389362)
    • (2005) Protein Science , vol.14 , Issue.4 , pp. 929-935
    • Reddy, K.R.C.1    Lilie, H.2    Rudolph, R.3    Lange, C.4
  • 115
    • 0025194489 scopus 로고
    • 1 H NMR studies of human lysozyme: Spectral assignment and comparison with hen lysozyme
    • DOI 10.1021/bi00483a007
    • 1 H NMR studies of human lysozyme: spectral assignment and comparison with hen lysozyme Biochemistry 29 1990 7201 7214 (Pubitemid 20230047)
    • (1990) Biochemistry , vol.29 , Issue.31 , pp. 7201-7214
    • Redfield, C.1    Dobson, C.M.2
  • 116
  • 117
    • 34547126694 scopus 로고    scopus 로고
    • Novel therapeutic strategies for the treatment of protein-misfolding diseases
    • J.C. Rochet Novel therapeutic strategies for the treatment of protein-misfolding diseases Expert Rev. Mol. Med. 9 2007 1 34
    • (2007) Expert Rev. Mol. Med. , vol.9 , pp. 1-34
    • Rochet, J.C.1
  • 118
    • 34548058571 scopus 로고    scopus 로고
    • Alys amyloidosis caused by compound heterozygosity in Exon 2 (Thr70Asn) and Exon 4 (Trp112Arg) of the lysozyme gene
    • C. Rocken, K. Becker, M. Fandrich, V. Schroeckh, B. Stix, and T. Rath Alys amyloidosis caused by compound heterozygosity in Exon 2 (Thr70Asn) and Exon 4 (Trp112Arg) of the lysozyme gene Hum. Mutat. 27 2006 119 120
    • (2006) Hum. Mutat. , vol.27 , pp. 119-120
    • Rocken, C.1    Becker, K.2    Fandrich, M.3    Schroeckh, V.4    Stix, B.5    Rath, T.6
  • 119
    • 3142514201 scopus 로고    scopus 로고
    • Protein aggregation and neurodegenerative disease
    • C.A. Ross, and M.A. Poirier Protein aggregation and neurodegenerative disease Nat. Med. 10 2004 S10 S17
    • (2004) Nat. Med. , vol.10
    • Ross, C.A.1    Poirier, M.A.2
  • 120
    • 0029774156 scopus 로고    scopus 로고
    • Artificial chaperone-assisted refolding of denatured-reduced lysozyme: Modulation of the competition between renaturation and aggregation
    • DOI 10.1021/bi961638j
    • D. Rozema, and S.H. Gellman Artificial chaperone-assisted refolding of denatured-reduced lysozyme: modulation of the competition between renaturation and aggregation Biochemistry 35 1996 15760 15771 (Pubitemid 26422313)
    • (1996) Biochemistry , vol.35 , Issue.49 , pp. 15760-15771
    • Rozema, D.1    Gellman, S.H.2
  • 121
    • 0030046574 scopus 로고    scopus 로고
    • In vitro folding of inclusion body proteins
    • R. Rudolph, and H. Lilie In vitro folding of inclusion body proteins FASEB J. 10 1996 49 56 (Pubitemid 26035506)
    • (1996) FASEB Journal , vol.10 , Issue.1 , pp. 49-56
    • Rudolph, R.1    Lilie, H.2
  • 122
    • 0036527699 scopus 로고    scopus 로고
    • Therapeutic strategies for human amyloid diseases
    • J.C. Sacchettini, and J.W. Kelly Therapeutic strategies for human amyloid diseases Nat. Rev. Drug Discov. 1 2002 267 275 (Pubitemid 37361443)
    • (2002) Nature Reviews Drug Discovery , vol.1 , Issue.4 , pp. 267-275
    • Sacchettini, J.C.1    Kelly, J.W.2
  • 123
    • 34548389339 scopus 로고    scopus 로고
    • 2 -Microglobulin and Hen Egg-white Lysozyme into Amyloid Fibrils
    • DOI 10.1016/j.jmb.2007.06.088, PII S0022283607008960
    • 2 -microglobulin and hen egg-white lysozyme into amyloid fibrils J. Mol. Biol. 372 2007 981 991 (Pubitemid 47368345)
    • (2007) Journal of Molecular Biology , vol.372 , Issue.4 , pp. 981-991
    • Sasahara, K.1    Yagi, H.2    Naiki, H.3    Goto, Y.4
  • 124
    • 0036780877 scopus 로고    scopus 로고
    • Amyloid-β immunotherapy for Alzheimer's disease: The end of the beginning
    • DOI 10.1038/nrn938
    • D. Schenk Amyloid-beta immunotherapy for Alzheimer's disease: the end of the beginning Nat. Rev. Neurosci. 3 2002 824 828 (Pubitemid 135706694)
    • (2002) Nature Reviews Neuroscience , vol.3 , Issue.10 , pp. 824-828
    • Schenk, D.1
  • 126
    • 19644389665 scopus 로고    scopus 로고
    • Solubihzation and refolding of bacterial inclusion body proteins
    • DOI 10.1263/jbb.99.303
    • S.M. Singh, and A.K. Panda Solubilization and refolding of bacterial inclusion body proteins J. Biosci. Bioeng. 99 2005 303 310 (Pubitemid 40740579)
    • (2005) Journal of Bioscience and Bioengineering , vol.99 , Issue.4 , pp. 303-310
    • Singh, S.M.1    Panda, A.K.2
  • 127
    • 0014690594 scopus 로고
    • Association sites of lysozyme in solution: The active site
    • A.J. Sophianopoulos Association sites of lysozyme in solution: the active site J. Biol. Chem. 244 1969 3188 3193
    • (1969) J. Biol. Chem. , vol.244 , pp. 3188-3193
    • Sophianopoulos, A.J.1
  • 128
    • 0343003602 scopus 로고
    • Evidence for dimerization of lysozyme in alkaline solution
    • A.J. Sophianopoulos, and K.E. Van Holde Evidence for dimerization of lysozyme in alkaline solution J. Biol. Chem. 236 1961 PC82 PC83
    • (1961) J. Biol. Chem. , vol.236
    • Sophianopoulos, A.J.1    Van Holde, K.E.2
  • 129
    • 78651158388 scopus 로고
    • Physical studies of muramidase (lysozyme) II: PH dependent dimerization
    • A.J. Sophianopoulos, and K.E. Van Holde Physical studies of muramidase (lysozyme) II: pH dependent dimerization J. Biol. Chem. 239 1964 2516 2524
    • (1964) J. Biol. Chem. , vol.239 , pp. 2516-2524
    • Sophianopoulos, A.J.1    Van Holde, K.E.2
  • 130
    • 0033152954 scopus 로고    scopus 로고
    • Expression, purification, and characterization of the recombinant calcium-binding equine lysozyme secreted by the filamentous fungus Aspergillus niger: Comparisons with the production of hen and human lysozymes
    • DOI 10.1006/prep.1999.1036
    • A. Spencer, L.A. Morozova-Roche, W. Noppe, D.A. MacKenzie, D.J. Jeenes, and M. Joniau Expression, purification, and characterization of the recombinant calcium-binding equine lysozyme secreted by the filamentous fungus Aspergillus niger: comparisons with the production of hen and human lysozymes Protein Expr. Purif. 16 1999 171 180 (Pubitemid 29321739)
    • (1999) Protein Expression and Purification , vol.16 , Issue.1 , pp. 171-180
    • Spencer, A.1    Morozov-Roche, L.A.2    Noppe, W.3    MacKenzie, D.A.4    Jeenes, D.J.5    Joniau, M.6    Dobson, C.M.7    Archer, D.B.8
  • 131
    • 0030801746 scopus 로고    scopus 로고
    • The structure of amyloid fibrils by electron microscopy and x-ray diffraction
    • M. Sunde, and C. Blake The structure of amyloid fibrils by electron microscopy and X-ray diffraction Adv. Protein Chem. 50 1997 123 159 (Pubitemid 27449487)
    • (1997) Advances in Protein Chemistry , vol.50 , pp. 123-159
    • Sunde, M.1    Blake, C.2
  • 133
    • 0010700420 scopus 로고
    • Lysozyme and its relation to the antibacterial properties of various tissues and secretions
    • R. Thompson Lysozyme and its relation to the antibacterial properties of various tissues and secretions Arch. Pathol. 30 1940 1096 1134
    • (1940) Arch. Pathol. , vol.30 , pp. 1096-1134
    • Thompson, R.1
  • 134
    • 39349102682 scopus 로고    scopus 로고
    • The formation of amyloid fibrils from proteins in the lysozyme family
    • DOI 10.2174/138920307783018659
    • A.J. Trexler, and M.R. Nilsson The formation of amyloid fibrils from proteins in the lysozyme family Curr. Protein Pept. Sci. 6 2007 537 557 (Pubitemid 351266988)
    • (2007) Current Protein and Peptide Science , vol.8 , Issue.6 , pp. 537-557
    • Trexler, A.J.1    Nilsson, M.R.2
  • 140
    • 0001351894 scopus 로고
    • Rapid attainment of sedimentation equilibrium
    • K.E. Van Holde, and R.L. Baldwin Rapid attainment of sedimentation equilibrium J. Phys. Chem. 62 1958 734 743
    • (1958) J. Phys. Chem. , vol.62 , pp. 734-743
    • Van Holde, K.E.1    Baldwin, R.L.2
  • 141
    • 4143148674 scopus 로고    scopus 로고
    • Guanidine hydrochloride can induce amyloid fibril formation from hen egg-white lysozyme
    • DOI 10.1021/bm0498979
    • B.A. Vernaglia, J. Huang, and E.D. Clark Guanidine hydrochloride can induce amyloid fibril formation from hen egg-white lysozyme Biomacromolecules 5 2004 1362 1370 (Pubitemid 39089737)
    • (2004) Biomacromolecules , vol.5 , Issue.4 , pp. 1362-1370
    • Vernaglia, B.A.1    Huang, J.2    Clark, E.D.3
  • 145
    • 25144471718 scopus 로고    scopus 로고
    • Inhibition of amyloid fibril formation of β-amyloid peptides via the amphiphilic surfactants
    • S.S.S. Wang, Y.T. Chen, and S.W. Chou Inhibition of amyloid fibril formation of β-amyloid peptides via the amphiphilic surfactants Biochim. Biophys. Acta 1741 2005 307 313
    • (2005) Biochim. Biophys. Acta , vol.1741 , pp. 307-313
    • Wang, S.S.S.1    Chen, Y.T.2    Chou, S.W.3
  • 146
    • 33750616210 scopus 로고    scopus 로고
    • Effects of p-benzoquinone and melatonin on amyloid fibrillogenesis of hen egg-white lysozyme
    • S.S.S. Wang, P.H. Chen, and Y.Tz. Hung Effects of p-benzoquinone and melatonin on amyloid fibrillogenesis of hen egg-white lysozyme J. Mol. Catal. B Enzym. 43 2006 49 57
    • (2006) J. Mol. Catal. B Enzym. , vol.43 , pp. 49-57
    • Wang, S.S.S.1    Chen, P.H.2    Hung, Y.Tz.3
  • 147
    • 36849074751 scopus 로고    scopus 로고
    • The formation of amyloid fibril-like hen egg-white lysozyme species induced by temperature and urea concentration dependent denaturation
    • S. Wang, Y.T. Hung, P. Wang, and J.W. Wu The formation of amyloid fibril-like hen egg-white lysozyme species induced by temperature and urea concentration dependent denaturation Korean J. Chem. Engg. 24 2007 787 795
    • (2007) Korean J. Chem. Engg. , vol.24 , pp. 787-795
    • Wang, S.1    Hung, Y.T.2    Wang, P.3    Wu, J.W.4
  • 148
    • 62649114448 scopus 로고    scopus 로고
    • Amyloid fibrillation of hen egg-white lysozyme is inhibited by TCEP
    • S.S.S. Wang, K.N. Liu, and Y.C. Lu Amyloid fibrillation of hen egg-white lysozyme is inhibited by TCEP Biochem. Biophys. Res. Commun. 381 2009 639 642
    • (2009) Biochem. Biophys. Res. Commun. , vol.381 , pp. 639-642
    • Wang, S.S.S.1    Liu, K.N.2    Lu, Y.C.3
  • 149
    • 77955665370 scopus 로고    scopus 로고
    • Effects of dithiothreitol on the amyloid fibrillogenesis of hen egg-white lysozyme
    • 10.1007/s00249-010-0576-0
    • S.S.S. Wang, K.N. Liu, and B.W. Wang Effects of dithiothreitol on the amyloid fibrillogenesis of hen egg-white lysozyme Eur. Biophys. J. 39 2010 1229 1242 10.1007/s00249-010-0576-0
    • (2010) Eur. Biophys. J. , vol.39 , pp. 1229-1242
    • Wang, S.S.S.1    Liu, K.N.2    Wang, B.W.3
  • 150
    • 70249114002 scopus 로고    scopus 로고
    • Investigating the influences of redox buffer compositions on the amyloid fibrillogenesis of hen egg-white lysozyme
    • S.S. Wang, K. Liu, C. Wu, and J. Lai Investigating the influences of redox buffer compositions on the amyloid fibrillogenesis of hen egg-white lysozyme Biochim. Biophys. Acta 1794 2009 1663 1672
    • (2009) Biochim. Biophys. Acta , vol.1794 , pp. 1663-1672
    • Wang, S.S.1    Liu, K.2    Wu, C.3    Lai, J.4
  • 151
    • 78149457673 scopus 로고    scopus 로고
    • A primary study on partial purification of lysozyme from chicken egg white using foam separation method
    • W. Wang, H. Yue, and Q. Yuan A primary study on partial purification of lysozyme from chicken egg white using foam separation method Biotechnol. Biotechnol. Equip. 23 2009 1237 1241
    • (2009) Biotechnol. Biotechnol. Equip. , vol.23 , pp. 1237-1241
    • Wang, W.1    Yue, H.2    Yuan, Q.3
  • 152
    • 18744405982 scopus 로고
    • Immunological studies on egg white proteins IV. Immunochemical and physical studies of lysozyme
    • L.R. Wetter, and H.F. Deutsch Immunological studies on egg white proteins IV. Immunochemical and physical studies of lysozyme J. Biol. Chem. 192 1951 237 242
    • (1951) J. Biol. Chem. , vol.192 , pp. 237-242
    • Wetter, L.R.1    Deutsch, H.F.2
  • 156
    • 58149311483 scopus 로고    scopus 로고
    • Secreted expression of human lysozyme in the yeast Pichia pastoris under the direction of the signal peptide from human serum albumin
    • R. Xiong, J. Chen, and J. Chen Secreted expression of human lysozyme in the yeast Pichia pastoris under the direction of the signal peptide from human serum albumin Biotechnol. Appl. Biochem. 51 2008 129 134
    • (2008) Biotechnol. Appl. Biochem. , vol.51 , pp. 129-134
    • Xiong, R.1    Chen, J.2    Chen, J.3
  • 157
    • 42049114013 scopus 로고    scopus 로고
    • Successful control of aggregation and folding rates during refolding of denatured lysozyme by adding N-methylimidazolium cations with various N′-substituents
    • DOI 10.1021/bp070207x
    • S. Yamaguchi, E. Yamamoto, S. Tsukiji, and T. Nagamune Successful control of aggregation and folding rates during refolding of denatured lysozyme by adding N-methylimidazolium cations with various N′-substituents Biotechnol. Prog. 24 2008 402 408 (Pubitemid 351520355)
    • (2008) Biotechnology Progress , vol.24 , Issue.2 , pp. 402-408
    • Yamaguchi, S.1    Yamamoto, E.2    Tsukiji, S.3    Nagamune, T.4
  • 158
    • 38049187118 scopus 로고    scopus 로고
    • Thiol compounds inhibit the formation of amyloid fibrils by β2-microglobulin at neutral pH
    • K. Yamamoto, H. Yagi, D. Ozawa, K. Sasahara, H. Naiki, and Y. Goto Thiol compounds inhibit the formation of amyloid fibrils by β2-microglobulin at neutral pH J. Mol. Biol. 376 2008 258 268
    • (2008) J. Mol. Biol. , vol.376 , pp. 258-268
    • Yamamoto, K.1    Yagi, H.2    Ozawa, D.3    Sasahara, K.4    Naiki, H.5    Goto, Y.6
  • 159
    • 0242500842 scopus 로고    scopus 로고
    • A novel lysozyme mutation Phe57Ile associated with hereditary renal amyloidosis
    • DOI 10.1046/j.1523-1755.2003.00904.x
    • M. Yazaki, S.A. Farrell, and M.D. Benson A novel lysozyme mutation Phe57Ile associated with hereditary renal amyloidosis Kidney Int. 63 2003 1652 1657 (Pubitemid 36513310)
    • (2003) Kidney International , vol.63 , Issue.5 , pp. 1652-1657
    • Yazaki, M.1    Farrell, S.A.2    Benson, M.D.3
  • 160
    • 33745180199 scopus 로고    scopus 로고
    • Transgenic zebrafish expressing chicken lysozyme show resistance against bacterial diseases
    • DOI 10.1007/s11248-006-0009-0
    • R. Yazawa, I. Hirono, and T. Aoki Transgenic zebrafish expressing chicken lysozyme show resistance against bacterial diseases Transgenic Res. 15 2006 385 391 (Pubitemid 43901496)
    • (2006) Transgenic Research , vol.15 , Issue.3 , pp. 385-391
    • Yazawa, R.1    Hirono, I.2    Aoki, T.3
  • 161
    • 0036404245 scopus 로고    scopus 로고
    • An insight into the pathway of the amyloid fibril formation of hen egg white lysozyme obtained from a small-angle X-ray and neutron scattering study
    • DOI 10.1016/S0022-2836(02)00941-5
    • Y. Yonezawa, S. Tanaka, T. Kubota, K. Wakabayashi, K. Yutani, and S. Fujiwara An insight into the pathway of the amyloid fibril formation of hen egg white lysozyme obtained from a small-angle X-ray and neutron scattering study J. Mol. Biol. 323 2002 237 251 (Pubitemid 35283689)
    • (2002) Journal of Molecular Biology , vol.323 , Issue.2 , pp. 237-251
    • Yonezawa, Y.1    Tanaka, S.2    Kubota, T.3    Wakabayashi, K.4    Yutani, K.5    Fujiwara, S.6
  • 162
    • 0033006157 scopus 로고    scopus 로고
    • Oxidative refolding of denatured/reduced lysozyme utilizing the chaperone-like function of liposomes and immobilized liposome chromatography
    • DOI 10.1021/bp990050b
    • M. Yoshimoto, and R. Kuboi Oxidative refolding of denatured/reduced lysozyme utilizing the chaperone-like function of liposomes and immobilized liposome chromatography Biotechnol. Prog. 15 1999 480 487 (Pubitemid 29270693)
    • (1999) Biotechnology Progress , vol.15 , Issue.3 , pp. 480-487
    • Yoshimoto, M.1    Kuboi, R.2
  • 163
    • 0023818378 scopus 로고
    • Human lysozome: Sequencing of a cDNA, and expression and secretion by Saccharomyces cerevisiae
    • K. Yoshimura, A. Toibana, and K. Nakahama Human lysozyme: sequencing of a cDNA, and expression and secretion by Saccharomyces cerevisiae Biochem. Biophys. Res. Commun. 150 1988 794 801 (Pubitemid 18039290)
    • (1988) Biochemical and Biophysical Research Communications , vol.150 , Issue.2 , pp. 794-801
    • Yoshimura, K.1    Toibana, A.2    Nakahama, K.3
  • 164
    • 63649114518 scopus 로고    scopus 로고
    • Gold nanoparticles can induce the formation of protein-based aggregates at physiological pH
    • D. Zhang, O. Neumann, H. Wang, V.M. Yuwono, A. Barhoumi, and M. Perham Gold nanoparticles can induce the formation of protein-based aggregates at physiological pH Nano Lett. 9 2009 666 671
    • (2009) Nano Lett. , vol.9 , pp. 666-671
    • Zhang, D.1    Neumann, O.2    Wang, H.3    Yuwono, V.M.4    Barhoumi, A.5    Perham, M.6
  • 165
    • 43049096368 scopus 로고    scopus 로고
    • Mixed macromolecular crowding inhibits amyloid formation of hen egg white lysozyme
    • B.R. Zhou, Z. Zhou, Q.L. Hu, J. Chen, and Y. Liang Mixed macromolecular crowding inhibits amyloid formation of hen egg white lysozyme Biochim. Biophys. Acta 1784 2008 472 480
    • (2008) Biochim. Biophys. Acta , vol.1784 , pp. 472-480
    • Zhou, B.R.1    Zhou, Z.2    Hu, Q.L.3    Chen, J.4    Liang, Y.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.