메뉴 건너뛰기




Volumn 13, Issue 11, 2004, Pages 3017-3027

Sonication of proteins causes formation of aggregates that resemble amyloid

Author keywords

structure; Amyloid; Fibrils; Protein aggregation; Protein conformational disorder; Protein misfolding; Sonication; Ultrasound radiation

Indexed keywords

AMYLOID; CONGO RED; PROTEIN; THIOFLAVINE;

EID: 7244256224     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.04831804     Document Type: Article
Times cited : (367)

References (71)
  • 1
    • 0035882202 scopus 로고    scopus 로고
    • The preparation of magnetic proteinaceous microspheres using the sonochemical method
    • Avivi, S., Felner, I., Novik, I., and Gedanken, A. 2001. The preparation of magnetic proteinaceous microspheres using the sonochemical method. Biochim. Biophys. Acta 1527: 123-129.
    • (2001) Biochim. Biophys. Acta , vol.1527 , pp. 123-129
    • Avivi, S.1    Felner, I.2    Novik, I.3    Gedanken, A.4
  • 2
    • 0032078388 scopus 로고    scopus 로고
    • Recombinant human erythropoietin (rhEPO) loaded poly(lactide-co- glycolide) microspheres: Influence of the encapsulation technique and polymer purity on microsphere characteristics
    • Bittner, B., Morlock, M., Koll, H., Winter, G., and Kissel, T. 1998. Recombinant human erythropoietin (rhEPO) loaded poly(lactide-co-glycolide) microspheres: Influence of the encapsulation technique and polymer purity on microsphere characteristics. Eur. J. Pharm. Biopharm. 45: 295-305.
    • (1998) Eur. J. Pharm. Biopharm. , vol.45 , pp. 295-305
    • Bittner, B.1    Morlock, M.2    Koll, H.3    Winter, G.4    Kissel, T.5
  • 5
    • 0035800572 scopus 로고    scopus 로고
    • Polyglutamine aggregation behavior in vitro supports a recruitment mechanism of cytotoxicity
    • Chen, S., Berthelier, V., Yang, W., and Wetzel, R. 2001. Polyglutamine aggregation behavior in vitro supports a recruitment mechanism of cytotoxicity. J. Mol. Biol. 311: 173-182.
    • (2001) J. Mol. Biol. , vol.311 , pp. 173-182
    • Chen, S.1    Berthelier, V.2    Yang, W.3    Wetzel, R.4
  • 6
    • 0035187228 scopus 로고    scopus 로고
    • Solution conditions can promote formation of either amyloid protofilaments or mature fibrils from the HypF N-terminal domain
    • Chiti, F., Bucciantini, M., Capanni, C., Taddei, N., Dobson, C.M., and Stefani, M. 2001. Solution conditions can promote formation of either amyloid protofilaments or mature fibrils from the HypF N-terminal domain. Protein Sci. 10: 2541-2547.
    • (2001) Protein Sci. , vol.10 , pp. 2541-2547
    • Chiti, F.1    Bucciantini, M.2    Capanni, C.3    Taddei, N.4    Dobson, C.M.5    Stefani, M.6
  • 8
    • 0019536747 scopus 로고
    • Infrared and laser-Raman spectroscopic studies of thermally-induced globular protein gels
    • Clark, A.H., Saunderson, D.H., and Suggett, A. 1981b. Infrared and laser-Raman spectroscopic studies of thermally-induced globular protein gels. Int. J. Pept. Protein Res. 17: 353-364.
    • (1981) Int. J. Pept. Protein Res. , vol.17 , pp. 353-364
    • Clark, A.H.1    Saunderson, D.H.2    Suggett, A.3
  • 10
    • 0034623286 scopus 로고    scopus 로고
    • Entrapping intermediates of thermal aggregation in α-helical proteins with low concentration of guanidine hydrochloride
    • Dong, A., Randolph, T.W., and Carpenter, J.F. 2000. Entrapping intermediates of thermal aggregation in α-helical proteins with low concentration of guanidine hydrochloride. J. Biol. Chem. 275: 27689-27693.
    • (2000) J. Biol. Chem. , vol.275 , pp. 27689-27693
    • Dong, A.1    Randolph, T.W.2    Carpenter, J.F.3
  • 11
    • 0035826234 scopus 로고    scopus 로고
    • Amyloid fibrils from muscle myoglobin
    • Fandrich, M., Fletcher, M.A., and Dobson, C.M. 2001. Amyloid fibrils from muscle myoglobin. Nature 410: 165-166.
    • (2001) Nature , vol.410 , pp. 165-166
    • Fandrich, M.1    Fletcher, M.A.2    Dobson, C.M.3
  • 13
    • 0031932169 scopus 로고    scopus 로고
    • Protein aggregation: Folding aggregates, inclusion bodies and amyloid
    • Fink, A.L. 1998. Protein aggregation: Folding aggregates, inclusion bodies and amyloid. Fold. Des. 3: R9-R23.
    • (1998) Fold. Des. , vol.3
    • Fink, A.L.1
  • 14
    • 0030712145 scopus 로고    scopus 로고
    • Self-seeded fibers formed by Sup35, the protein determinant of [PSI+], a heritable prion-like factor of S. cerevisiae
    • Glover, J.R., Kowal, A.S., Schirmer, E.C., Patino, M.M., Liu, J.J., and Lindquist, S. 1997. Self-seeded fibers formed by Sup35, the protein determinant of [PSI+], a heritable prion-like factor of S. cerevisiae. Cell 89: 811-819.
    • (1997) Cell , vol.89 , pp. 811-819
    • Glover, J.R.1    Kowal, A.S.2    Schirmer, E.C.3    Patino, M.M.4    Liu, J.J.5    Lindquist, S.6
  • 15
    • 0034005357 scopus 로고    scopus 로고
    • Amyloid 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. Amyloid 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
  • 16
    • 0025773848 scopus 로고
    • Air-filled proteinaceous microbubbles: Synthesis of an echo-contrast agent
    • Grinstaff, M.W. and Suslick, K.S. 1991. Air-filled proteinaceous microbubbles: Synthesis of an echo-contrast agent. Proc. Natl. Acad. Sci. 88: 7708-7710.
    • (1991) Proc. Natl. Acad. Sci. , vol.88 , pp. 7708-7710
    • Grinstaff, M.W.1    Suslick, K.S.2
  • 18
    • 0030908095 scopus 로고    scopus 로고
    • Models of amyloid seeding in Alzheimer's disease and scrapie: Mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins
    • Harper, J.D. and Lansbury Jr., P.T. 1997. Models of amyloid seeding in Alzheimer's disease and scrapie: Mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins. Annu. Rev. Biochem. 66: 385-407.
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 385-407
    • Harper, J.D.1    Lansbury Jr., P.T.2
  • 19
    • 0035795180 scopus 로고    scopus 로고
    • Generation and propagation of radical reactions on proteins
    • Hawkins, C.L. and Davies, M.J. 2001. Generation and propagation of radical reactions on proteins. Biochim. Biophys. Acta 1504: 196-219.
    • (2001) Biochim. Biophys. Acta , vol.1504 , pp. 196-219
    • Hawkins, C.L.1    Davies, M.J.2
  • 20
    • 0026642332 scopus 로고
    • Aggregation of chymotrypsinogen: Portrait by infrared spectroscopy
    • Ismail, A.A., Manisch, H.H., and Wong, P.T. 1992. Aggregation of chymotrypsinogen: Portrait by infrared spectroscopy. Biochim. Biophys. Acta 1121: 183-188.
    • (1992) Biochim. Biophys. Acta , vol.1121 , pp. 183-188
    • Ismail, A.A.1    Manisch, H.H.2    Wong, P.T.3
  • 21
    • 0027006436 scopus 로고
    • Amyloid fibril formation requires a chemically discriminating nucleation event: Studies of an amyloidogenic sequence from the bacterial protein OsmB
    • Jarrett, J.T. and Lansbury Jr., P.T. 1992. Amyloid fibril formation requires a chemically discriminating nucleation event: Studies of an amyloidogenic sequence from the bacterial protein OsmB. Biochemistry 31: 12345-12352.
    • (1992) Biochemistry , vol.31 , pp. 12345-12352
    • Jarrett, J.T.1    Lansbury Jr., P.T.2
  • 22
    • 0027258525 scopus 로고
    • The carboxy terminus of the β amyloid protein is critical for the seeding of amyloid formation: Implications for the pathogenesis of Alzheimer's disease
    • Jarrett, J.T., Berger, E.P., and Lansbury Jr., P.T. 1993. The carboxy terminus of the β amyloid protein is critical for the seeding of amyloid formation: Implications for the pathogenesis of Alzheimer's disease. Biochemistry 32: 4693-4697.
    • (1993) Biochemistry , vol.32 , pp. 4693-4697
    • Jarrett, J.T.1    Berger, E.P.2    Lansbury Jr., P.T.3
  • 23
    • 0037335355 scopus 로고    scopus 로고
    • Preparation and in vitro/in vivo evaluation of insulin-loaded poly(acryloyl-hydroxyethyl starch)-PLGA composite microspheres
    • Jiang, G., Qiu, W., and DeLuca, P.P. 2003. Preparation and in vitro/in vivo evaluation of insulin-loaded poly(acryloyl-hydroxyethyl starch)-PLGA composite microspheres. Pharm. Res. 20: 452-459.
    • (2003) Pharm. Res. , vol.20 , pp. 452-459
    • Jiang, G.1    Qiu, W.2    DeLuca, P.P.3
  • 24
    • 0038344725 scopus 로고    scopus 로고
    • Conformational stability of a model protein (bovine serum albumin) during primary emulsification process of PLGA microspheres synthesis
    • Kang, F. and Singh, J. 2003. Conformational stability of a model protein (bovine serum albumin) during primary emulsification process of PLGA microspheres synthesis. Int. J. Pharm. 260: 149-156.
    • (2003) Int. J. Pharm. , vol.260 , pp. 149-156
    • Kang, F.1    Singh, J.2
  • 25
    • 0008452276 scopus 로고    scopus 로고
    • Heat-induced gelation of globular proteins: Part 3. Molecular studies on low pH β-lactoglobulin gels
    • Kavanagh, G.M., Clark, A.H., and Ross-Murphy, S.B. 2000. Heat-induced gelation of globular proteins: Part 3. Molecular studies on low pH β-lactoglobulin gels. Int. J. Biol. Macromol. 28: 41-50.
    • (2000) Int. J. Biol. Macromol. , vol.28 , pp. 41-50
    • Kavanagh, G.M.1    Clark, A.H.2    Ross-Murphy, S.B.3
  • 26
    • 0032006678 scopus 로고    scopus 로고
    • The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways
    • Kelly, J.W. 1998. The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways. Curr. Opin. Struct. Biol. 8: 101-106.
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 101-106
    • Kelly, J.W.1
  • 27
    • 0032855483 scopus 로고    scopus 로고
    • Quantifying amyloid by congo red spectral shift assay
    • Klunk, W.E., Jacob, R.F., and Mason, R.P. 1999. Quantifying amyloid by congo red spectral shift assay. Methods Enzymol. 309: 285-305.
    • (1999) Methods Enzymol. , vol.309 , pp. 285-305
    • Klunk, W.E.1    Jacob, R.F.2    Mason, R.P.3
  • 28
    • 36849103950 scopus 로고
    • Analysis of macromolecular polydispersity in intensity correlation spectroscopy: The method of cumulants
    • Koppel, D.E. 1972. Analysis of macromolecular polydispersity in intensity correlation spectroscopy: The method of cumulants. J. Chem. Phys. 57: 4818-4820.
    • (1972) J. Chem. Phys. , vol.57 , pp. 4818-4820
    • Koppel, D.E.1
  • 29
    • 0041341887 scopus 로고    scopus 로고
    • Amyloid-forming peptides selected proteolytically from phage display library
    • Koscielska-Kasprzak, K. and Otlewski, J. 2003. Amyloid-forming peptides selected proteolytically from phage display library. Protein Sci. 12: 1675-1685.
    • (2003) Protein Sci. , vol.12 , pp. 1675-1685
    • Koscielska-Kasprzak, K.1    Otlewski, J.2
  • 31
    • 0042320356 scopus 로고    scopus 로고
    • Seeded conversion of recombinant prion protein to a disulfide-bonded oligomer by a reduction-oxidation process
    • Lee, S. and Eisenberg, D. 2003. Seeded conversion of recombinant prion protein to a disulfide-bonded oligomer by a reduction-oxidation process. Nat. Struct. Biol. 10: 725-730.
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 725-730
    • Lee, S.1    Eisenberg, D.2
  • 32
    • 0027502784 scopus 로고
    • Thioflavine T interaction with synthetic Alzheimer's disease β-amyloid peptides: Detection of amyloid aggregation in solution
    • LeVine III, H. 1993. Thioflavine T interaction with synthetic Alzheimer's disease β-amyloid peptides: Detection of amyloid aggregation in solution. Protein Sci. 2: 404-410.
    • (1993) Protein Sci. , vol.2 , pp. 404-410
    • LeVine III, H.1
  • 33
    • 0032849874 scopus 로고    scopus 로고
    • Quantification of β-sheet amyloid fibril structures with thioflavin T
    • _. 1999. Quantification of β-sheet amyloid fibril structures with thioflavin T. Methods Enzymol. 309: 274-284.
    • (1999) Methods Enzymol. , vol.309 , pp. 274-284
  • 34
    • 0142210080 scopus 로고    scopus 로고
    • Gene transfer with echo-enhanced contrast agents: Comparison between Albunex, Optison, and Levovist in mice - Initial results
    • Li, T., Tachibana, K., and Kuroki, M. 2003. Gene transfer with echo-enhanced contrast agents: Comparison between Albunex, Optison, and Levovist in mice - Initial results. Radiology 229: 423-428.
    • (2003) Radiology , vol.229 , pp. 423-428
    • Li, T.1    Tachibana, K.2    Kuroki, M.3
  • 36
    • 0036168995 scopus 로고    scopus 로고
    • DICHROWEB: An interactive website for the analysis of protein secondary structure from circular dichroism spectra
    • Lobley, A., Whitmore, L., and Wallace, B.A. 2002. DICHROWEB: An interactive website for the analysis of protein secondary structure from circular dichroism spectra. Bioinformatics 18: 211-212.
    • (2002) Bioinformatics , vol.18 , pp. 211-212
    • Lobley, A.1    Whitmore, L.2    Wallace, B.A.3
  • 37
    • 0036789017 scopus 로고    scopus 로고
    • Serpinopathies and the conformational dementias
    • Lomas, D.A. and Carrell, R.W. 2002. Serpinopathies and the conformational dementias. Nat. Rev. Genet. 3: 759-768.
    • (2002) Nat. Rev. Genet. , vol.3 , pp. 759-768
    • Lomas, D.A.1    Carrell, R.W.2
  • 39
    • 0036231272 scopus 로고    scopus 로고
    • Comparative Fourier transform infrared spectroscopy study of cold-, pressure-, and heat-induced unfolding and aggregation of myoglobin
    • Meersman, F., Smeller, L., and Heremans, K. 2002. Comparative Fourier transform infrared spectroscopy study of cold-, pressure-, and heat-induced unfolding and aggregation of myoglobin. Biophys. J. 82: 2635-2644.
    • (2002) Biophys. J. , vol.82 , pp. 2635-2644
    • Meersman, F.1    Smeller, L.2    Heremans, K.3
  • 41
    • 0024509805 scopus 로고
    • Fluorometric determination of amyloid fibrils in vitro using the fluorescent dye, thioflavin T1
    • Naiki, H., Higuchi, K., Hosokawa, M., and Takeda, T. 1989. Fluorometric determination of amyloid fibrils in vitro using the fluorescent dye, thioflavin T1. Anal. Biochem. 177: 244-249.
    • (1989) Anal. Biochem. , vol.177 , pp. 244-249
    • Naiki, H.1    Higuchi, K.2    Hosokawa, M.3    Takeda, T.4
  • 43
    • 2342444028 scopus 로고    scopus 로고
    • Seeding specificity in amyloid growth induced by heterologous fibrils
    • O'Nuallain, B., Williams, A.D., Westermark, P., and Wetzel, R. 2004. Seeding specificity in amyloid growth induced by heterologous fibrils. J. Biol. Chem. 279: 17490-17499.
    • (2004) J. Biol. Chem. , vol.279 , pp. 17490-17499
    • O'Nuallain, B.1    Williams, A.D.2    Westermark, P.3    Wetzel, R.4
  • 44
    • 0020176708 scopus 로고
    • CONTIN: A general purpose constrained regularization program for inverting noisy linear algebraic and integral equations
    • Provencher, S.W. 1982. CONTIN: A general purpose constrained regularization program for inverting noisy linear algebraic and integral equations. Comput. Phys. Commun. 27: 201-209.
    • (1982) Comput. Phys. Commun. , vol.27 , pp. 201-209
    • Provencher, S.W.1
  • 46
    • 0034255027 scopus 로고    scopus 로고
    • A systematic exploration of the influence of the protein stability on amyloid fibril formation in vitro
    • Ramirez-Alvarado, M., Merkel, J.S., and Regan, L. 2000. A systematic exploration of the influence of the protein stability on amyloid fibril formation in vitro. Proc. Natl. Acad. Sci. 97: 8979-8984.
    • (2000) Proc. Natl. Acad. Sci. , vol.97 , pp. 8979-8984
    • Ramirez-Alvarado, M.1    Merkel, J.S.2    Regan, L.3
  • 48
    • 0035859102 scopus 로고    scopus 로고
    • Sensitive detection of pathological prion protein by cyclic amplification of protein misfolding
    • Saborio, G.P., Permanne, B., and Soto, C. 2001. Sensitive detection of pathological prion protein by cyclic amplification of protein misfolding. Nature 411: 810-813.
    • (2001) Nature , vol.411 , pp. 810-813
    • Saborio, G.P.1    Permanne, B.2    Soto, C.3
  • 49
    • 0036396073 scopus 로고    scopus 로고
    • Sonication induced sheet formation at the air-water interface
    • Satheeshkumar, K.S. and Jayakumar, R. 2002. Sonication induced sheet formation at the air-water interface. Chem. Commun. (Camb.) 19: 2244-2245.
    • (2002) Chem. Commun. (Camb.) , vol.19 , pp. 2244-2245
    • Satheeshkumar, K.S.1    Jayakumar, R.2
  • 51
    • 0141746349 scopus 로고    scopus 로고
    • The role of protein stability, solubility, and net charge in amyloid fibril formation
    • Schmittschmitt, J.P. and Scholtz, J.M. 2003. The role of protein stability, solubility, and net charge in amyloid fibril formation. Protein Sci. 12: 2374-2378.
    • (2003) Protein Sci. , vol.12 , pp. 2374-2378
    • Schmittschmitt, J.P.1    Scholtz, J.M.2
  • 52
    • 0030610918 scopus 로고    scopus 로고
    • Destabilization of the Ca2+-ATPase of sarcoplasmic reticulum by thiol-specific, heat shock inducers results in thermal denaturation at 37 degrees C
    • Senisterra, G.A., Huntley, S.A., Escaravage, M., Sekhar, K.R., Freeman, M.L., Borrelli, M., and Lepock, J.R. 1997. Destabilization of the Ca2+-ATPase of sarcoplasmic reticulum by thiol-specific, heat shock inducers results in thermal denaturation at 37 degrees C. Biochemistry 36: 11002-11011.
    • (1997) Biochemistry , vol.36 , pp. 11002-11011
    • Senisterra, G.A.1    Huntley, S.A.2    Escaravage, M.3    Sekhar, K.R.4    Freeman, M.L.5    Borrelli, M.6    Lepock, J.R.7
  • 53
    • 0037195958 scopus 로고    scopus 로고
    • Tryptophanyl substitutions in apomyoglobin determine protein aggregation and amyloid-like fibril formation at physiological pH
    • Epub 42002 Sep 45819
    • Sirangelo, I., Malmo, C., Casillo, M., Mezzogiorao, A., Papa, M., and Irace, G. 2002. Tryptophanyl substitutions in apomyoglobin determine protein aggregation and amyloid-like fibril formation at physiological pH. J. Biol. Chem. 277: 45887-45891 [Epub 42002 Sep 45819].
    • (2002) J. Biol. Chem. , vol.277 , pp. 45887-45891
    • Sirangelo, I.1    Malmo, C.2    Casillo, M.3    Mezzogiorao, A.4    Papa, M.5    Irace, G.6
  • 54
    • 0035827318 scopus 로고    scopus 로고
    • Protein misfolding and disease; protein refolding and therapy
    • Soto, C. 2001. Protein misfolding and disease; protein refolding and therapy. FEBS Lett. 498: 204-207.
    • (2001) FEBS Lett. , vol.498 , pp. 204-207
    • Soto, C.1
  • 55
    • 0036680112 scopus 로고    scopus 로고
    • Cyclic amplification of protein misfolding: Application to prion-related disorders and beyond
    • Soto, C., Saborio, G.P., and Anderes, L. 2002. Cyclic amplification of protein misfolding: Application to prion-related disorders and beyond. Trends Neurosci. 25: 390-394.
    • (2002) Trends Neurosci. , vol.25 , pp. 390-394
    • Soto, C.1    Saborio, G.P.2    Anderes, L.3
  • 56
    • 0034672325 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: Comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set
    • Sreerama, N. and Woody, R.W. 2000. Estimation of protein secondary structure from circular dichroism spectra: Comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set. Anal. Biochem. 287: 252-260.
    • (2000) Anal. Biochem. , vol.287 , pp. 252-260
    • Sreerama, N.1    Woody, R.W.2
  • 57
    • 0037166276 scopus 로고    scopus 로고
    • Amyloid-like fibril formation in an all β-barrel protein involves the formation of partially structured intermediate(s)
    • Epub 12002 Mar 19024
    • Srisailam, S., Wang, H.M., Kumar, T.K., Rajalingam, D., Sivaraja, V., Sheu, H.S., Chang, Y.C., and Yu, C. 2002. Amyloid-like fibril formation in an all β-barrel protein involves the formation of partially structured intermediate(s). J. Biol. Chem. 277: 19027-19036 [Epub 12002 Mar 19024].
    • (2002) J. Biol. Chem. , vol.277 , pp. 19027-19036
    • Srisailam, S.1    Wang, H.M.2    Kumar, T.K.3    Rajalingam, D.4    Sivaraja, V.5    Sheu, H.S.6    Chang, Y.C.7    Yu, C.8
  • 59
    • 0344944630 scopus 로고    scopus 로고
    • Protein aggregation and aggregate toxicity: New insights into protein folding, misfolding diseases and biological evolution
    • Stefani, M. and Dobson, C.M. 2003. Protein aggregation and aggregate toxicity: New insights into protein folding, misfolding diseases and biological evolution. J. Mol. Med. 81: 678-699.
    • (2003) J. Mol. Med. , vol.81 , pp. 678-699
    • Stefani, M.1    Dobson, C.M.2
  • 60
    • 0030801746 scopus 로고    scopus 로고
    • The structure of amyloid fibrils by electron microscopy and X-ray diffraction
    • Sunde, M. and Blake, C. 1997. The structure of amyloid fibrils by electron microscopy and X-ray diffraction. Adv. Protein Chem. 50: 123-159.
    • (1997) Adv. Protein Chem. , vol.50 , pp. 123-159
    • Sunde, M.1    Blake, C.2
  • 61
    • 0037072274 scopus 로고    scopus 로고
    • The effects of aggregation-inducing motifs on amyloid formation of model proteins related to neurodegenerative diseases
    • Tanaka, M., Machida, Y., Nishikawa, Y., Akagi, T., Morishima, I., Hashikawa, T., Fujisawa, T., and Nukina, N. 2002. The effects of aggregation-inducing motifs on amyloid formation of model proteins related to neurodegenerative diseases. Biochemistry 41: 10277-10286.
    • (2002) Biochemistry , vol.41 , pp. 10277-10286
    • Tanaka, M.1    Machida, Y.2    Nishikawa, Y.3    Akagi, T.4    Morishima, I.5    Hashikawa, T.6    Fujisawa, T.7    Nukina, N.8
  • 62
    • 0036403732 scopus 로고    scopus 로고
    • Prions as protein-based genetic elements
    • Uptain, S.M. and Lindquist, S. 2002. Prions as protein-based genetic elements. Annu. Rev. Microbiol 56: 703-741.
    • (2002) Annu. Rev. Microbiol , vol.56 , pp. 703-741
    • Uptain, S.M.1    Lindquist, S.2
  • 63
    • 0033635054 scopus 로고    scopus 로고
    • Protein instability in poly(lactic-co-glycolic acid) microparticles
    • van de Weert, M., Hennink, W.E., and Jiskoot, W. 2000. Protein instability in poly(lactic-co-glycolic acid) microparticles. Pharm. Res. 17: 1159-1167.
    • (2000) Pharm. Res. , vol.17 , pp. 1159-1167
    • Van De Weert, M.1    Hennink, W.E.2    Jiskoot, W.3
  • 64
    • 0042236699 scopus 로고    scopus 로고
    • Fourier transform IR attenuated total reflectance spectroscopy studies of cysteine-induced changes in secondary conformations of bovine serum albumin after UV-B irradiation
    • Wei, Y.S., Lin, S.Y., Wang, S.L., Li, M.J., and Cheng, W.T. 2003. Fourier transform IR attenuated total reflectance spectroscopy studies of cysteine-induced changes in secondary conformations of bovine serum albumin after UV-B irradiation. Biopolymers 72: 345-351.
    • (2003) Biopolymers , vol.72 , pp. 345-351
    • Wei, Y.S.1    Lin, S.Y.2    Wang, S.L.3    Li, M.J.4    Cheng, W.T.5
  • 65
    • 0032855076 scopus 로고    scopus 로고
    • Staining methods for identification of amyloid in tissue
    • Westermark, G.T., Johnson, K.H., and Westermark, P. 1999. Staining methods for identification of amyloid in tissue. Methods Enzymol. 309: 3-25.
    • (1999) Methods Enzymol. , vol.309 , pp. 3-25
    • Westermark, G.T.1    Johnson, K.H.2    Westermark, P.3
  • 66
    • 0037473475 scopus 로고    scopus 로고
    • Stabilisation and determination of the biological activity of L-asparaginase in poly(D,L-lactide-co-glycolide) nanospheres
    • Wolf, M., Wirth, M., Pittner, F., and Gabor, F. 2003. Stabilisation and determination of the biological activity of L-asparaginase in poly(D,L-lactide-co-glycolide) nanospheres. Int. J. Pharm. 256: 141-152.
    • (2003) Int. J. Pharm. , vol.256 , pp. 141-152
    • Wolf, M.1    Wirth, M.2    Pittner, F.3    Gabor, F.4
  • 67
    • 0013846588 scopus 로고
    • The cause of the green polarization color of amyloid stained with Congo red
    • Wolman, M. and Bubis, J.J. 1965. The cause of the green polarization color of amyloid stained with Congo red. Histochemie 4: 351-356.
    • (1965) Histochemie , vol.4 , pp. 351-356
    • Wolman, M.1    Bubis, J.J.2
  • 68
    • 0029213247 scopus 로고
    • Sonochemically produced hemoglobin microbubbles
    • (eds. D.L. Wilcox et al.), Fall 1994, Material Research Society, Pittsburgh, PA
    • Wong, M. and Suslick, K.S. 1995. Sonochemically produced hemoglobin microbubbles. In Material Research Society Symposium Proceedings (eds. D.L. Wilcox et al.), Fall 1994, Vol. 372, pp. 89-94. Material Research Society, Pittsburgh, PA.
    • (1995) Material Research Society Symposium Proceedings , vol.372 , pp. 89-94
    • Wong, M.1    Suslick, K.S.2
  • 69
    • 0000554465 scopus 로고
    • The physical and biological effects of high frequency sound waves of great intensity
    • Wood, R.W. and Loomis, A.L. 1927. The physical and biological effects of high frequency sound waves of great intensity. Philos. Mag. 4: 414-436.
    • (1927) Philos. Mag. , vol.4 , pp. 414-436
    • Wood, R.W.1    Loomis, A.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.