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Volumn 415, Issue 2, 2008, Pages 275-288

How do surfactants and DTT affect the size, dynamics, activity and growth of soluble lysozyme aggregates?

Author keywords

Atomic force microscopy (AFM); Disulfide bond; Fluorescence anisotropy; Gel filtration; Protein aggregation; Thioflavin T.

Indexed keywords

ACIDS; AGGREGATES; AMMONIUM COMPOUNDS; ANISOTROPY; ATOMIC PHYSICS; ATOMS; CHROMATOGRAPHIC ANALYSIS; COLLOIDS; DIFFUSERS (OPTICAL); DYNAMICS; ENZYMES; FLUORESCENCE; GELATION; GELS; GROWTH KINETICS; HYDROPHOBICITY; LIGHT EMISSION; LUMINESCENCE; MOLECULAR DYNAMICS; OLIGOMERS; POLYMERS; POROUS MATERIALS; QUANTUM CHEMISTRY; SURFACE ACTIVE AGENTS; SURFACE CHEMISTRY;

EID: 54049088134     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20071499     Document Type: Article
Times cited : (72)

References (57)
  • 1
    • 0037264120 scopus 로고    scopus 로고
    • Unfolding the role of protein misfolding in neurodegenerative diseases
    • Soto, C. (2003) Unfolding the role of protein misfolding in neurodegenerative diseases. Nat. Rev. Neurosci. 4. 49-60
    • (2003) Nat. Rev. Neurosci , vol.4 , pp. 49-60
    • Soto, C.1
  • 2
    • 10644225416 scopus 로고    scopus 로고
    • Protein misfolding and aggregation: New examples in medicine and biology of the dark side of the protein world
    • Stefani, M. (2004) Protein misfolding and aggregation: new examples in medicine and biology of the dark side of the protein world. Biochim. Biophys. Acta 1739, 5-25
    • (2004) Biochim. Biophys. Acta , vol.1739 , pp. 5-25
    • Stefani, M.1
  • 3
    • 0037551741 scopus 로고    scopus 로고
    • Caughey, B. and Lansbury, P. T. (2003) Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders. Annu. Rev. Neurosci. 26, 267-298
    • Caughey, B. and Lansbury, P. T. (2003) Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders. Annu. Rev. Neurosci. 26, 267-298
  • 4
    • 0037071906 scopus 로고    scopus 로고
    • Construction and destruction of bacterial inclusion bodies
    • Carrio. M. M. and Villaverce, A. (2002) Construction and destruction of bacterial inclusion bodies. J. Biotechnol. 96, 3-12
    • (2002) J. Biotechnol , vol.96 , pp. 3-12
    • Carrio, M.M.1    Villaverce, A.2
  • 5
    • 0037397705 scopus 로고    scopus 로고
    • Emerging ideas on the molecular basis of protein and peptice aggregation
    • Thirumalai, D., Klimov, D. K. and Dima, R. I. (2003) Emerging ideas on the molecular basis of protein and peptice aggregation. Curr. Opin. Struct. Biol. 13, 146-159
    • (2003) Curr. Opin. Struct. Biol , vol.13 , pp. 146-159
    • Thirumalai, D.1    Klimov, D.K.2    Dima, R.I.3
  • 6
    • 3142514201 scopus 로고    scopus 로고
    • Protein aggregation and neurodegenerative disease
    • Ross, C. A. and Poirier, M. A. (2004) Protein aggregation and neurodegenerative disease. Nat. Med. 10. S10-S17
    • (2004) Nat. Med , vol.10
    • Ross, C.A.1    Poirier, M.A.2
  • 7
    • 33644868088 scopus 로고    scopus 로고
    • Developing therapeutics for diseases of protein misfolding
    • May, B. C. H., Govaerts, C. and Cohen, F E. (2006) Developing therapeutics for diseases of protein misfolding. Neurology 66, (Suppl. 1), S118-S122
    • (2006) Neurology , vol.66 , Issue.SUPPL. 1
    • May, B.C.H.1    Govaerts, C.2    Cohen, F.E.3
  • 8
    • 33746237577 scopus 로고    scopus 로고
    • To be or not to be toxic: Aggregation in Huntington and Alzheimer disease
    • Slow, E. J., Graham, R. K, and Hayden, M. R. (2006) To be or not to be toxic: aggregation in Huntington and Alzheimer disease. Trends Genet. 22, 408-411
    • (2006) Trends Genet , vol.22 , pp. 408-411
    • Slow, E.J.1    Graham, R.K.2    Hayden, M.R.3
  • 10
    • 11544279355 scopus 로고    scopus 로고
    • 1-42 are potent central nervous system neurotoxins. Proc. Natl. Acad. Sci. U.S.A, 95, 6448-6453
    • 1-42 are potent central nervous system neurotoxins. Proc. Natl. Acad. Sci. U.S.A, 95, 6448-6453
  • 11
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long term potentiation in vivo
    • Walsh, D. M., Klyubin, I., Fadeeva, J. V., Cullen. W. K., Anwyl, R,, Wolfe, M. S., Rowan, M. J. and Selkoe, D. J. (2002) Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long term potentiation in vivo. Nature 416. 535-539
    • (2002) Nature , vol.416 , pp. 535-539
    • Walsh, D.M.1    Klyubin, I.2    Fadeeva, J.V.3    Cullen, W.K.4    Anwyl, R.5    Wolfe, M.S.6    Rowan, M.J.7    Selkoe, D.J.8
  • 12
    • 0343003602 scopus 로고
    • Evidence for dinnerization of lysozyme in alkaline solution
    • Sophianopoulos, A. J. and Van Holde, K. E. (1961) Evidence for dinnerization of lysozyme in alkaline solution. J. Biol. Chem. 236, PC82-PC83
    • (1961) J. Biol. Chem , vol.236
    • Sophianopoulos, A.J.1    Van Holde, K.E.2
  • 13
    • 78651158388 scopus 로고
    • Physical studies of muramidase (lysozyme)
    • Sophianopoulos, A. J. and Van Holde, K. E. (1964) Physical studies of muramidase (lysozyme). J. Biol. Chem. 239, 2516-2524
    • (1964) J. Biol. Chem , vol.239 , pp. 2516-2524
    • Sophianopoulos, A.J.1    Van Holde, K.E.2
  • 15
    • 0014690594 scopus 로고
    • Association sites of lysozyme in solution
    • Sophianopoulos, A. J. (1969) Association sites of lysozyme in solution. J. Biol. Chem. 244, 3188-3193
    • (1969) J. Biol. Chem , vol.244 , pp. 3188-3193
    • Sophianopoulos, A.J.1
  • 17
    • 0034005357 scopus 로고    scopus 로고
    • Annyloid protofilament formation of hen egg lysozyme in highly concentrated ethanol solution
    • Goda, S., Takano, K., Yamagata, Y., Nagata, R., Akutsu, H.. Maki, S., Namba, K. and Yutani, K. (2000) Annyloid protofilament formation of hen egg lysozyme in highly concentrated ethanol solution, Protein Sci. 9, 369-375
    • (2000) Protein Sci , vol.9 , pp. 369-375
    • Goda, S.1    Takano, K.2    Yamagata, Y.3    Nagata, R.4    Akutsu, H.5    Maki, S.6    Namba, K.7    Yutani, K.8
  • 19
    • 1642452936 scopus 로고    scopus 로고
    • Formation of amyloid fibril from fully reduced hen egg white lysozyme
    • Cao, A., Hu, D. and Lai, L. (2004) Formation of amyloid fibril from fully reduced hen egg white lysozyme. Protein Sci. 13, 319-324
    • (2004) Protein Sci , vol.13 , pp. 319-324
    • Cao, A.1    Hu, D.2    Lai, L.3
  • 20
    • 0344198173 scopus 로고    scopus 로고
    • Temperature-induced dissociation of protein aggregates: Accessing the denatured state
    • Meersman, F. and Heremans, F (2003) Temperature-induced dissociation of protein aggregates: accessing the denatured state. Biochemistry 42, 14234-14241
    • (2003) Biochemistry , vol.42 , pp. 14234-14241
    • Meersman, F.1    Heremans, F.2
  • 22
    • 0042467574 scopus 로고    scopus 로고
    • Dumoulin, M., Last, A. M., Desmyter, A., Decanniere, K., Canet, D., Larsson, G., Spencer, A.. Archer, D. B.. Sasse, J., Muyldermans, S. et al. (2003) A camelid antibody fragment inhibits the formation of amyloid fibrils by human lysozyme. Nature 424, 783-788
    • Dumoulin, M., Last, A. M., Desmyter, A., Decanniere, K., Canet, D., Larsson, G., Spencer, A.. Archer, D. B.. Sasse, J., Muyldermans, S. et al. (2003) A camelid antibody fragment inhibits the formation of amyloid fibrils by human lysozyme. Nature 424, 783-788
  • 23
    • 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
    • Homchaudhuri, L., Kumar, S. and Swaminathan. R. (2006) Slow aggregation of lysozyme in alkaline pH monitored in real time employing the fluorescence anisotropy of covalently labeled dansyl probe. FEBS Lett, 580, 2097-2101
    • (2006) FEBS Lett , vol.580 , pp. 2097-2101
    • Homchaudhuri, L.1    Kumar, S.2    Swaminathan, R.3
  • 24
    • 0001440492 scopus 로고
    • Molten globule-like conformation of barstar: A study by fluorescence dynamics
    • Swaminathan, R., Periasamy, N., Udgaonkar, J. B. and Krishnamoorthy, G. (1994) Molten globule-like conformation of barstar: A study by fluorescence dynamics. J. Phys. Chem. 98, 9270-9278
    • (1994) J. Phys. Chem , vol.98 , pp. 9270-9278
    • Swaminathan, R.1    Periasamy, N.2    Udgaonkar, J.B.3    Krishnamoorthy, G.4
  • 26
    • 12244255727 scopus 로고    scopus 로고
    • Constrained analysis of fluorescence anisotropy decay: Application to experimental protein dynamics
    • Feinstein, E., Deikus, G., Rusinova, E., Rachofsky, E. L., Ross, J. B. A. and Laws, W. R. (2003) Constrained analysis of fluorescence anisotropy decay: application to experimental protein dynamics. Biophys. J. 84, 599-611
    • (2003) Biophys. J , vol.84 , pp. 599-611
    • Feinstein, E.1    Deikus, G.2    Rusinova, E.3    Rachofsky, E.L.4    Ross, J.B.A.5    Laws, W.R.6
  • 27
    • 0032830122 scopus 로고    scopus 로고
    • In vitro immunoglobulin light chain fibrillogenesis
    • Wall, J., Murphy, C. L. and Solomon, A. (1999) In vitro immunoglobulin light chain fibrillogenesis. Methods Enzymol. 309, 204-217
    • (1999) Methods Enzymol , vol.309 , pp. 204-217
    • Wall, J.1    Murphy, C.L.2    Solomon, A.3
  • 28
    • 0015292329 scopus 로고
    • Determining simple sulfhydryl compounds (low molecular weight) and their contents in biological samples by using 2,2′-dithiobis-(5-nitropyridine)
    • Swatditat, A. and Tsen, C. C. (1972) Determining simple sulfhydryl compounds (low molecular weight) and their contents in biological samples by using 2,2′-dithiobis-(5-nitropyridine). Anal. Biochem. 45, 349-356
    • (1972) Anal. Biochem , vol.45 , pp. 349-356
    • Swatditat, A.1    Tsen, C.C.2
  • 29
    • 0036318194 scopus 로고    scopus 로고
    • Quick measurement of protein sulfhydryls with Ellman's reagent and with 4,4′-dithiodipyridine
    • Riener, C. K., Kada, G. and Gruber, H. J. (2002) Quick measurement of protein sulfhydryls with Ellman's reagent and with 4,4′-dithiodipyridine. Anal. Bioanal. Chem. 373, 266-276
    • (2002) Anal. Bioanal. Chem , vol.373 , pp. 266-276
    • Riener, C.K.1    Kada, G.2    Gruber, H.J.3
  • 30
    • 0014687514 scopus 로고
    • The dependence of lysozyme activity on pH and ionic strength
    • Davies, R. C., Neuberger, A, and Wilson, B. M. (1969) The dependence of lysozyme activity on pH and ionic strength. Biochim. Biophys. Acta 178, 294-305
    • (1969) Biochim. Biophys. Acta , vol.178 , pp. 294-305
    • Davies, R.C.1    Neuberger, A.2    Wilson, B.M.3
  • 32
    • 33745039756 scopus 로고    scopus 로고
    • Characterization of the formation of amyloid protofibrils from barstar by mapping residue-specific fluorescence dynamics
    • Mukhopadhyay, S., Nayak, P. K., Udgaonkar, J, B. and Krishnamoorthy, G. (2006) Characterization of the formation of amyloid protofibrils from barstar by mapping residue-specific fluorescence dynamics. J. Mol. Biol. 358, 935-942
    • (2006) J. Mol. Biol , vol.358 , pp. 935-942
    • Mukhopadhyay, S.1    Nayak, P.K.2    Udgaonkar, J.B.3    Krishnamoorthy, G.4
  • 33
    • 33847137710 scopus 로고    scopus 로고
    • Early aggregation in prion pepticle nanostructures investigated by nonlinear and ultrafast time-resolved fluorescence spectroscopy
    • Wang, Y. and Goodson, III, T. (2007) Early aggregation in prion pepticle nanostructures investigated by nonlinear and ultrafast time-resolved fluorescence spectroscopy, J. Phys. Chem. B 111, 327-330
    • (2007) J. Phys. Chem. B , vol.111 , pp. 327-330
    • Wang, Y.1    Goodson III, T.2
  • 34
    • 54049109005 scopus 로고    scopus 로고
    • Steiner, R. F. (1991) Fluorescence anisotropy: theory and applications. Topics in Fluorescence Spectroscopy, 2, (Lakowicz, J.R. ed.), pp. 1-52, Plenum Press, New York 1-52
    • Steiner, R. F. (1991) Fluorescence anisotropy: theory and applications. Topics in Fluorescence Spectroscopy, Vol. 2, (Lakowicz, J.R. ed.), pp. 1-52, Plenum Press, New York 1-52
  • 35
    • 0037008404 scopus 로고    scopus 로고
    • Studies on surfactant-biopolymer interaction. I. Microcalorimetric investigation on the interaction of cetyltrimethylammonium bromide (CTAB) and sodium dodecylsulfate (SDS) with gelatin (Gn), lysozyme (Lz) and deoxyribonucleic acid (DNA)
    • Chatterjee, A., Moulik, S. P., Majhi, P. R. and Sanyal, S. K. (2002) Studies on surfactant-biopolymer interaction. I. Microcalorimetric investigation on the interaction of cetyltrimethylammonium bromide (CTAB) and sodium dodecylsulfate (SDS) with gelatin (Gn), lysozyme (Lz) and deoxyribonucleic acid (DNA). Biophys. Chem. 98, 313-327
    • (2002) Biophys. Chem , vol.98 , pp. 313-327
    • Chatterjee, A.1    Moulik, S.P.2    Majhi, P.R.3    Sanyal, S.K.4
  • 36
    • 0023221204 scopus 로고
    • Application of a reference convolution to tryptophan fluorescence in proteins. A refined description of rotational dynamics
    • Vos, K., van Hoek, A. and Visser, A. J. (1987) Application of a reference convolution to tryptophan fluorescence in proteins. A refined description of rotational dynamics. Eur. J. Biochem. 165, 55-63
    • (1987) Eur. J. Biochem , vol.165 , pp. 55-63
    • Vos, K.1    van Hoek, A.2    Visser, A.J.3
  • 37
    • 33845982898 scopus 로고    scopus 로고
    • pH dependent self-assembly of polyalanine peptices
    • Giri, K., Bhattacharyya, N. P. and Basak, S. (2007) pH dependent self-assembly of polyalanine peptices. Biophys. J. 92, 293-302
    • (2007) Biophys. J , vol.92 , pp. 293-302
    • Giri, K.1    Bhattacharyya, N.P.2    Basak, S.3
  • 38
    • 0030982184 scopus 로고    scopus 로고
    • Ionic-strength-dependent transition of hen egg-white lysozyme at low pH to a compact state and its aggregation on thermal denaturation
    • Babu, K. R. and Bhakuni, V. (1997) Ionic-strength-dependent transition of hen egg-white lysozyme at low pH to a compact state and its aggregation on thermal denaturation. Eur. J. Biochem. 245, 781-789
    • (1997) Eur. J. Biochem , vol.245 , pp. 781-789
    • Babu, K.R.1    Bhakuni, V.2
  • 39
    • 38449094348 scopus 로고    scopus 로고
    • Different molten globule-like folding intermediates of hen egg white lysozyme induced by high pH and tertiary butanol
    • Hameed, M., Ahmad. B., Fazili, K. M., Andrabi, K. and Khan, R. H. (2007) Different molten globule-like folding intermediates of hen egg white lysozyme induced by high pH and tertiary butanol. J. Biochem. (Tokyo) 141, 573-583
    • (2007) J. Biochem. (Tokyo) , vol.141 , pp. 573-583
    • Hameed, M.1    Ahmad, B.2    Fazili, K.M.3    Andrabi, K.4    Khan, R.H.5
  • 40
    • 0035960767 scopus 로고    scopus 로고
    • The lysozyme-dodecyl sulfate system. An example of protein-surfactant aggregation
    • Stenstam, A., Khan, A. and Wennerstrom, K. (2001) The lysozyme-dodecyl sulfate system. An example of protein-surfactant aggregation. Langmuir 17, 7513-7520
    • (2001) Langmuir , vol.17 , pp. 7513-7520
    • Stenstam, A.1    Khan, A.2    Wennerstrom, K.3
  • 41
    • 18744405982 scopus 로고
    • Immunological studies on egg white proteins IV. Immunochemical and physical studies of lysozyme
    • Wetter, L. R. and Deutsch, H. F. (1951) Immunological studies on egg white proteins IV. Immunochemical and physical studies of lysozyme. J. Biol. Chem. 192, 237-242
    • (1951) J. Biol. Chem , vol.192 , pp. 237-242
    • Wetter, L.R.1    Deutsch, H.F.2
  • 42
    • 0032598465 scopus 로고    scopus 로고
    • Microstructure of protein-surfactant complexes in gel and solution-an NMR relaxation study
    • Moren, A. K., Nyden, M., Soderman, O. and Khan, A. (1999) Microstructure of protein-surfactant complexes in gel and solution-an NMR relaxation study. Langmuir 15, 5480-5488
    • (1999) Langmuir , vol.15 , pp. 5480-5488
    • Moren, A.K.1    Nyden, M.2    Soderman, O.3    Khan, A.4
  • 43
    • 56749096456 scopus 로고    scopus 로고
    • Kumar, S., Singh, A. K., Krishnamoorthy, G. and Swaminathan, R. (2008) Thioflavin T displays enhanced fluorescence selectively inside anionic micelles and mammalian cells. J. Fluoresc., doi 10.1007/s10895-008-0378-2
    • Kumar, S., Singh, A. K., Krishnamoorthy, G. and Swaminathan, R. (2008) Thioflavin T displays enhanced fluorescence selectively inside anionic micelles and mammalian cells. J. Fluoresc., doi 10.1007/s10895-008-0378-2
  • 44
    • 0029774156 scopus 로고    scopus 로고
    • Artificial chaperone-assisted refolding of denatured-reduced lysozyme: Modulation of the competition between renaturation and aggregation
    • Rozema, D. and Gellman, S. H. (1996) Artificial chaperone-assisted refolding of denatured-reduced lysozyme: modulation of the competition between renaturation and aggregation. Biochemistry 35, 15760-15771
    • (1996) Biochemistry , vol.35 , pp. 15760-15771
    • Rozema, D.1    Gellman, S.H.2
  • 45
    • 25144471718 scopus 로고    scopus 로고
    • Inhibition of amyloid fibril formation of β-amyloid peptides via the amphiphilic surfactants
    • Wang, S. S. S., Chen, Y. T. and Chou, S. W. (2005) Inhibition of amyloid fibril formation of β-amyloid peptides via the amphiphilic surfactants. Biochm. Biophys. Acta 1741, 307-313
    • (2005) Biochm. Biophys. Acta , vol.1741 , pp. 307-313
    • Wang, S.S.S.1    Chen, Y.T.2    Chou, S.W.3
  • 46
    • 34248679167 scopus 로고    scopus 로고
    • Tricine-SDS-PAGE
    • Schagger, H. (2006) Tricine-SDS-PAGE. Nat. Protoc. 1, 16-22
    • (2006) Nat. Protoc , vol.1 , pp. 16-22
    • Schagger, H.1
  • 47
    • 0016537404 scopus 로고    scopus 로고
    • (11975) A new method for disufficle analysis of pepticles
    • Anderson, W. L. and Wetlaufer, D. B. (11975) A new method for disufficle analysis of pepticles. Anal. Biochem. 67, 493-502
    • Anal. Biochem , vol.67 , pp. 493-502
    • Anderson, W.L.1    Wetlaufer, D.B.2
  • 49
    • 0042820167 scopus 로고    scopus 로고
    • Human recombinant resistin protein display a tendency to aggregate by forming intermolecular disufficle linkage
    • Aruna, B., Ghosh, S., Singh. A. K., Mande, S. C., Srinivas, V., Chauhan, R. and Ehtesham, N. Z. (2003) Human recombinant resistin protein display a tendency to aggregate by forming intermolecular disufficle linkage. Biochemistry 42, 10554-10559
    • (2003) Biochemistry , vol.42 , pp. 10554-10559
    • Aruna, B.1    Ghosh, S.2    Singh, A.K.3    Mande, S.C.4    Srinivas, V.5    Chauhan, R.6    Ehtesham, N.Z.7
  • 50
    • 33646486372 scopus 로고    scopus 로고
    • Disultide cross-linking protein represents a significant fraction of ALS-associated Cu, Zn-superoxide dismulase aggregation in spinal cords of model mice
    • Furukawa, Y., Fu, R., Deng, H. X., Siddique, T. and O'Halloran, T. V. (2006) Disultide cross-linking protein represents a significant fraction of ALS-associated Cu, Zn-superoxide dismulase aggregation in spinal cords of model mice. Proc. Natl. Acad. Sci. U.S.A. 103, 7148-7153
    • (2006) Proc. Natl. Acad. Sci. U.S.A , vol.103 , pp. 7148-7153
    • Furukawa, Y.1    Fu, R.2    Deng, H.X.3    Siddique, T.4    O'Halloran, T.V.5
  • 51
    • 33646466296 scopus 로고    scopus 로고
    • Deng, H. X., Shi, Y., Furukawa, Y., Zhai, H., Fu, R.. Liu, E., Gorrie, G. H., Khan, M. S., Hung, W. Y., Bigio, E. H. et al. (2006) Conversion to the amyotrophic lateral sclerosis phenotype is associated with intermolecular linked insoluble aggregates of SOD1 in mitochondria. Proc. Natl. Acad. Sci. U.S.A. 103, 7142-7147
    • Deng, H. X., Shi, Y., Furukawa, Y., Zhai, H., Fu, R.. Liu, E., Gorrie, G. H., Khan, M. S., Hung, W. Y., Bigio, E. H. et al. (2006) Conversion to the amyotrophic lateral sclerosis phenotype is associated with intermolecular linked insoluble aggregates of SOD1 in mitochondria. Proc. Natl. Acad. Sci. U.S.A. 103, 7142-7147
  • 52
    • 33749563294 scopus 로고    scopus 로고
    • Induction of the unfolded protein response in familial amyotrophic lateral sclerosis and association of protein-disulfide isomerase with superoxide dismutase 1
    • Atkin, J. D., Farg, M. A., Turner, B. J., Tomas. D., Lysaght, J. A., Nunan, J., Bembach, A., Nagley, P., Beart, P. M., Cheema, S. S. and Horne, M. K. (2006) Induction of the unfolded protein response in familial amyotrophic lateral sclerosis and association of protein-disulfide isomerase with superoxide dismutase 1. J. Biol. Chem. 281, 30152-30165
    • (2006) J. Biol. Chem , vol.281 , pp. 30152-30165
    • Atkin, J.D.1    Farg, M.A.2    Turner, B.J.3    Tomas, D.4    Lysaght, J.A.5    Nunan, J.6    Bembach, A.7    Nagley, P.8    Beart, P.M.9    Cheema, S.S.10    Horne, M.K.11
  • 53
    • 0032479890 scopus 로고    scopus 로고
    • The importance of disulfide bond in prion protein conversion
    • Herrmann, L. M. and Caughey, B. (1998) The importance of disulfide bond in prion protein conversion. Neuroreport 9, 2457-2461
    • (1998) Neuroreport , vol.9 , pp. 2457-2461
    • Herrmann, L.M.1    Caughey, B.2
  • 55
    • 43049096368 scopus 로고    scopus 로고
    • Mixed macromolecular crowding inhibits amyloid formation of hen egg white lysozyme
    • Zhou, B. R., Zhou, Z., Hu, Q. L., Chen, J. and Liang, Y. (2008) Mixed macromolecular crowding inhibits amyloid formation of hen egg white lysozyme. Biochim. Biophys. Acta 1784, 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
  • 56
    • 34548389339 scopus 로고    scopus 로고
    • 2-microglobulin and hen egg-white lysozyme into amyloid fibrils
    • 2-microglobulin and hen egg-white lysozyme into amyloid fibrils. J. Mol. Biol. 372, 981-991
    • (2007) J. Mol. Biol , vol.372 , pp. 981-991
    • Sasahara, K.1    Yagi, H.2    Naiki, H.3    Goto, Y.4
  • 57
    • 33846562360 scopus 로고    scopus 로고
    • Lysozyme amyloidogenesis is accelerated by specific nicking and fragmentation but decelerated by intact protein binding and conversion
    • Mishra, R., Sorgjerd, K., Nystrom, S., Nordigarden, A., Yu, Y. C. and Hammarstrom, P. (2007) Lysozyme amyloidogenesis is accelerated by specific nicking and fragmentation but decelerated by intact protein binding and conversion. J. Mol. Biol. 366, 1029-1044
    • (2007) J. Mol. Biol , vol.366 , pp. 1029-1044
    • Mishra, R.1    Sorgjerd, K.2    Nystrom, S.3    Nordigarden, A.4    Yu, Y.C.5    Hammarstrom, P.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.