메뉴 건너뛰기




Volumn 61, Issue 5, 2004, Pages 511-524

Amyloid fibrils from the viewpoint of protein folding

Author keywords

Aggregation; Amyloid fibrils; Denatured states; Protein folding

Indexed keywords

AMINO ACID; AMYLOID; ASPARAGINE; BETA 2 MICROGLOBULIN; DEUTERIUM; GLUTAMINE; HYDROGEN; LYSOZYME; PRION PROTEIN; PROTEIN; TTR PROTEIN; UNCLASSIFIED DRUG;

EID: 1642417648     PISSN: 1420682X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00018-003-3264-8     Document Type: Review
Times cited : (144)

References (171)
  • 1
    • 0003166498 scopus 로고    scopus 로고
    • Protein folding in the landscape perspective: Chevron plots and non-Arrhenius kinetics
    • Chan H. S. and Dill K. A. (1998) Protein folding in the landscape perspective: chevron plots and non-Arrhenius kinetics. Proteins 30: 2-33
    • (1998) Proteins , vol.30 , pp. 2-33
    • Chan, H.S.1    Dill, K.A.2
  • 2
    • 1842298212 scopus 로고    scopus 로고
    • From Levinthal to pathways to funnels
    • Dill K. A. and Chan H. S. (1997) From Levinthal to pathways to funnels. Nat. Struct. Biol. 4: 10-19
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 10-19
    • Dill, K.A.1    Chan, H.S.2
  • 3
    • 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
  • 4
    • 0025910229 scopus 로고
    • Molecular biology of prion diseases
    • Prusiner S. B. (1991) Molecular biology of prion diseases. Science 252: 1515-1522
    • (1991) Science , vol.252 , pp. 1515-1522
    • Prusiner, S.B.1
  • 5
    • 0014211846 scopus 로고
    • Does the agent of scrapie replicate without nucleic acid?
    • Alper T., Cramp W. A., Haig D. A. and Clarke M. C. (1967) Does the agent of scrapie replicate without nucleic acid? Nature 214: 764-766
    • (1967) Nature , vol.214 , pp. 764-766
    • Alper, T.1    Cramp, W.A.2    Haig, D.A.3    Clarke, M.C.4
  • 6
    • 0014190760 scopus 로고
    • Self-replication and scrapie
    • Griffith J. S. (1967) Self-replication and scrapie. Nature 215: 1043-1044
    • (1967) Nature , vol.215 , pp. 1043-1044
    • Griffith, J.S.1
  • 7
    • 0020321767 scopus 로고
    • Novel proteinaceous infectious particles cause scrapie
    • Prusiner S. B. (1982) Novel proteinaceous infectious particles cause scrapie. Science 216: 136-144
    • (1982) Science , vol.216 , pp. 136-144
    • Prusiner, S.B.1
  • 8
    • 0015150725 scopus 로고
    • Creation of 'amyloid' fibrils from Bence Jones proteins in vitro
    • Glenner G. G., Ein D., Eanes E. D., Bladen H. A., Terry W. and Page D. L. (1971) Creation of 'amyloid' fibrils from Bence Jones proteins in vitro. Science 174: 712-714
    • (1971) Science , vol.174 , pp. 712-714
    • Glenner, G.G.1    Ein, D.2    Eanes, E.D.3    Bladen, H.A.4    Terry, W.5    Page, D.L.6
  • 10
    • 0017040042 scopus 로고
    • In vitro synthesis of 'amyloid' fibrils from insulin, calcitonin and parathormone
    • Kedar I., Ravid M. and Sohar E. (1976) In vitro synthesis of 'amyloid' fibrils from insulin, calcitonin and parathormone. Isr. J. Med. Sci. 12: 1137-1140
    • (1976) Isr. J. Med. Sci. , vol.12 , pp. 1137-1140
    • Kedar, I.1    Ravid, M.2    Sohar, E.3
  • 11
    • 0025801516 scopus 로고
    • Normal transthyretin and synthetic transthyretin fragments form amyloid-like fibrils in vitro
    • Gustavsson A., Engstrom U. and Westermark P. (1991) Normal transthyretin and synthetic transthyretin fragments form amyloid-like fibrils in vitro. Biochem. Biophys. Res. Commun. 175: 1159-1164
    • (1991) Biochem. Biophys. Res. Commun. , vol.175 , pp. 1159-1164
    • Gustavsson, A.1    Engstrom, U.2    Westermark, P.3
  • 12
    • 0023425365 scopus 로고
    • Synthetic peptide homologous to beta protein from Alzheimer disease forms amyloid-like fibrils in vitro
    • Kirschner D. A., Inouye H., Duffy L. K., Sinclair A., Lind M. and Selkoe D. J. (1987) Synthetic peptide homologous to beta protein from Alzheimer disease forms amyloid-like fibrils in vitro. Proc. Natl. Acad. Sci. USA 84: 6953-6957
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 6953-6957
    • Kirschner, D.A.1    Inouye, H.2    Duffy, L.K.3    Sinclair, A.4    Lind, M.5    Selkoe, D.J.6
  • 13
    • 0022878817 scopus 로고
    • In vitro formation of amyloid fibrils from two synthetic peptides of different lengths homologous to Alzheimer's disease beta-protein
    • Castano E. M., Ghiso J., Prelli F., Gorevic P. D., Migheli A. and Frangione B. (1986) In vitro formation of amyloid fibrils from two synthetic peptides of different lengths homologous to Alzheimer's disease beta-protein. Biochem. Biophys. Res. Commun. 141: 782-789
    • (1986) Biochem. Biophys. Res. Commun. , vol.141 , pp. 782-789
    • Castano, E.M.1    Ghiso, J.2    Prelli, F.3    Gorevic, P.D.4    Migheli, A.5    Frangione, B.6
  • 14
    • 0027259274 scopus 로고
    • Molecular characteristics of a protease-resistant, amyloidogenic and neurotoxic peptide homologous to residues 106-126 of the prion protein
    • Selvaggini C., De Gioia L., Cantu L., Ghibaudi E., Diomede L., Passerini F. et al. (1993) Molecular characteristics of a protease-resistant, amyloidogenic and neurotoxic peptide homologous to residues 106-126 of the prion protein. Biochem. Biophys. Res. Commun. 194: 1380-1386
    • (1993) Biochem. Biophys. Res. Commun. , vol.194 , pp. 1380-1386
    • Selvaggini, C.1    De Gioia, L.2    Cantu, L.3    Ghibaudi, E.4    Diomede, L.5    Passerini, F.6
  • 15
    • 0026675307 scopus 로고
    • Partial denaturation of transthyretin is sufficient for amyloid fibril formation in vitro
    • Colon W. and Kelly J. W. (1992) Partial denaturation of transthyretin is sufficient for amyloid fibril formation in vitro. Biochemistry 31: 8654-8660
    • (1992) Biochemistry , vol.31 , pp. 8654-8660
    • Colon, W.1    Kelly, J.W.2
  • 17
    • 0005431368 scopus 로고    scopus 로고
    • Formation of amyloid fibrils by peptides derived from the bacterial cold shock protein CspB
    • Gross M., Wilkins D. K., Pitkeathly M. C., Chung E. W., Higham C., Clark A. et al. (1999) Formation of amyloid fibrils by peptides derived from the bacterial cold shock protein CspB. Protein Sci. 8: 1350-1357
    • (1999) Protein Sci. , vol.8 , pp. 1350-1357
    • Gross, M.1    Wilkins, D.K.2    Pitkeathly, M.C.3    Chung, E.W.4    Higham, C.5    Clark, A.6
  • 18
    • 0034647438 scopus 로고    scopus 로고
    • Formation and seeding of amyloid fibrils from wild-type hen lysozyme and a peptide fragment from the beta-domain
    • Krebs M. R., Wilkins D. K., Chung E. W., Pitkeathly M. C., Chamberlain A. K., Zurdo J. et al. (2000) Formation and seeding of amyloid fibrils from wild-type hen lysozyme and a peptide fragment from the beta-domain. J. Mol. Biol. 300: 541-549
    • (2000) J. Mol. Biol. , vol.300 , pp. 541-549
    • Krebs, M.R.1    Wilkins, D.K.2    Chung, E.W.3    Pitkeathly, M.C.4    Chamberlain, A.K.5    Zurdo, J.6
  • 19
    • 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
  • 21
    • 0000504561 scopus 로고
    • Sur les propriétés optiques de l'amyloide
    • Divry P. and Florkin M. ( 1927) Sur les propriétés optiques de l'amyloide. C. R. Soc. Biol. 97: 1808-1810
    • (1927) C. R. Soc. Biol. , vol.97 , pp. 1808-1810
    • Divry, P.1    Florkin, M.2
  • 22
    • 0032855483 scopus 로고    scopus 로고
    • Quantifying amyloid by congo red spectral shift assay
    • Klunk W. E., Jacob R. F. and Mason RP. (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
  • 23
    • 0027502784 scopus 로고
    • Thioflavine T interaction with synthetic Alzheimer's disease beta-amyloid peptides: Detection of amyloid aggregation in solution
    • LeVine H. 3rd (1993). Thioflavine T interaction with synthetic Alzheimer's disease beta-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
  • 24
    • 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
  • 26
    • 0001611370 scopus 로고
    • Electron microscopic observation on a fibrous component in amyloid of diverse origins
    • Cohen A. S. and Calkins E. (1959) Electron microscopic observation on a fibrous component in amyloid of diverse origins. Nature 183: 1202-1203
    • (1959) Nature , vol.183 , pp. 1202-1203
    • Cohen, A.S.1    Calkins, E.2
  • 28
    • 0014351967 scopus 로고
    • X-ray diffraction studies on amyloid filaments
    • Eanes E. D. and Glenner G. G. (1968) X-ray diffraction studies on amyloid filaments. J. Histochem. Cytochem. 16: 673-677
    • (1968) J. Histochem. Cytochem. , vol.16 , pp. 673-677
    • Eanes, E.D.1    Glenner, G.G.2
  • 29
    • 0014578835 scopus 로고
    • Characterization of the amyloid fibril as a cross-beta protein
    • Bonar L., Cohen A. S. and Skinner M. M. (1969) Characterization of the amyloid fibril as a cross-beta protein. Proc. Soc. Exp. Biol. Med. 131: 1373-1375
    • (1969) Proc. Soc. Exp. Biol. Med. , vol.131 , pp. 1373-1375
    • Bonar, L.1    Cohen, A.S.2    Skinner, M.M.3
  • 30
    • 0000573263 scopus 로고
    • Configuration of polypeptide chains with favoured orientation around single bonds: Two new pleated sheets
    • Pauling L. and Corey R. (1951) Configuration of polypeptide chains with favoured orientation around single bonds: two new pleated sheets. Proc. Natl. Acad. Sci. USA 37: 729-739
    • (1951) Proc. Natl. Acad. Sci. USA , vol.37 , pp. 729-739
    • Pauling, L.1    Corey, R.2
  • 32
    • 0021879172 scopus 로고
    • Secondary structure of endocrine amyloid: Infrared spectroscopy of medullary carcinoma of the thyroid
    • O'Leary T. J. and Levin I. W. (1985) Secondary structure of endocrine amyloid: infrared spectroscopy of medullary carcinoma of the thyroid. Lab. Invest. 53: 240-242
    • (1985) Lab. Invest. , vol.53 , pp. 240-242
    • O'Leary, T.J.1    Levin, I.W.2
  • 33
    • 0024386063 scopus 로고
    • The secondary structure of human amyloid deposits as determined by circular dichroism spectroscopy
    • Cascio M., Glazer P. A. and Wallace B. A. (1989) The secondary structure of human amyloid deposits as determined by circular dichroism spectroscopy. Biochem. Biophys. Res. Commun. 162: 1162-1166
    • (1989) Biochem. Biophys. Res. Commun. , vol.162 , pp. 1162-1166
    • Cascio, M.1    Glazer, P.A.2    Wallace, B.A.3
  • 34
    • 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 P. T. Jr (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
  • 35
    • 9044229145 scopus 로고    scopus 로고
    • On the nucleation and growth of amyloid beta-protein fibrils: Detection of nuclei and quantitation of rate constants
    • Lomakin A., Chung D. S., Benedek G. B., Kirschner D. A. and Teplow D. B. (1996) On the nucleation and growth of amyloid beta-protein fibrils: detection of nuclei and quantitation of rate constants. Proc. Natl. Acad. Sci. USA 93: 1125-1129
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 1125-1129
    • Lomakin, A.1    Chung, D.S.2    Benedek, G.B.3    Kirschner, D.A.4    Teplow, D.B.5
  • 37
    • 0029257497 scopus 로고
    • The core Alzheimer's peptide NAC forms amyloid fibrils which seed and are seeded by beta-amyloid: Is NAC a common trigger or target in neurodegenerative disease?
    • Han H., Weinreb P. H. and Lansbury P. T. Jr (1995) The core Alzheimer's peptide NAC forms amyloid fibrils which seed and are seeded by beta-amyloid: is NAC a common trigger or target in neurodegenerative disease? Chem. Biol. 2: 163-169
    • (1995) Chem. Biol. , vol.2 , pp. 163-169
    • Han, H.1    Weinreb, P.H.2    Lansbury Jr., P.T.3
  • 38
    • 0034636976 scopus 로고    scopus 로고
    • Solution conformation and amyloid-like fibril formation of a polar peptide derived from a beta-hairpin in the Ospa single-layer beta-sheet
    • Ohnishi S., Koide A. and Koide S. (2000) Solution conformation and amyloid-like fibril formation of a polar peptide derived from a beta-hairpin in the OspA single-layer beta-sheet. J. Mol. Biol. 301: 477-489
    • (2000) J. Mol. Biol. , vol.301 , pp. 477-489
    • Ohnishi, S.1    Koide, A.2    Koide, S.3
  • 39
    • 0033538541 scopus 로고    scopus 로고
    • Alpha-synuclein fibrillogenesis is nucleation-dependent. Implications for the pathogenesis of Parkinson's disease
    • Wood S. J., Wypych J., Steavenson S., Louis J. C., Citron, M. and Biere A. L. (1999) alpha-synuclein fibrillogenesis is nucleation-dependent. Implications for the pathogenesis of Parkinson's disease. J. Biol. Chem. 274: 19509-19512
    • (1999) J. Biol. Chem. , vol.274 , pp. 19509-19512
    • Wood, S.J.1    Wypych, J.2    Steavenson, S.3    Louis, J.C.4    Citron, M.5    Biere, A.L.6
  • 40
    • 0028172208 scopus 로고
    • The Alzheimer a beta peptide develops protease resistance in association with its polymerization into fibrils
    • Nordstedt C., Naslund J., Tjernberg L. O., Karlstrom, A. R., Thyberg J. and Terenius L. (1994) The Alzheimer A beta peptide develops protease resistance in association with its polymerization into fibrils. J. Biol. Chem. 269: 30773-30776
    • (1994) J. Biol. Chem. , vol.269 , pp. 30773-30776
    • Nordstedt, C.1    Naslund, J.2    Tjernberg, L.O.3    Karlstrom, A.R.4    Thyberg, J.5    Terenius, L.6
  • 41
    • 0017824077 scopus 로고
    • Structure of prealbumin: Secondary, tertiary and quaternary interactions determined by Fourier refinement at 1.8 A
    • Blake C. C., Geisow M. J., Oatley S. J., Rerat B. and Rerat C. (1978) Structure of prealbumin: secondary, tertiary and quaternary interactions determined by Fourier refinement at 1.8 A. J. Mol. Biol. 121: 339-356
    • (1978) J. Mol. Biol. , vol.121 , pp. 339-356
    • Blake, C.C.1    Geisow, M.J.2    Oatley, S.J.3    Rerat, B.4    Rerat, C.5
  • 42
    • 0030004644 scopus 로고    scopus 로고
    • The acid-mediated denaturation pathway of transthyretin yields a conformational intermediate that can self-assemble into amyloid
    • Lai Z., Colon W. and Kelly J. W. (1996) The acid-mediated denaturation pathway of transthyretin yields a conformational intermediate that can self-assemble into amyloid. Biochemistry 35: 6470-6482
    • (1996) Biochemistry , vol.35 , pp. 6470-6482
    • Lai, Z.1    Colon, W.2    Kelly, J.W.3
  • 44
    • 0028969996 scopus 로고
    • Transthyretin mutations in health and disease
    • Saraiva M. J. (1995) Transthyretin mutations in health and disease. Hum. Mutat. 5: 191-196
    • (1995) Hum. Mutat. , vol.5 , pp. 191-196
    • Saraiva, M.J.1
  • 45
    • 0027363264 scopus 로고
    • Transthyretin mutation Leu-55-Pro significantly alters tetramer stability and increases amyloidogenicity
    • McCutchen S. L., Colon W. and Kelly J. W. (1993) Transthyretin mutation Leu-55-Pro significantly alters tetramer stability and increases amyloidogenicity. Biochemistry 32: 12119-12127
    • (1993) Biochemistry , vol.32 , pp. 12119-12127
    • McCutchen, S.L.1    Colon, W.2    Kelly, J.W.3
  • 46
    • 0030874395 scopus 로고    scopus 로고
    • Guanidine hydrochloride-induced denaturation and refolding of transthyretin exhibits a marked hysteresis: Equilibria with high kinetic barriers
    • Lai Z., McCulloch J., Lashuel H. A. and Kelly J. W. (1997) Guanidine hydrochloride-induced denaturation and refolding of transthyretin exhibits a marked hysteresis: equilibria with high kinetic barriers. Biochemistry 36: 10230-10239
    • (1997) Biochemistry , vol.36 , pp. 10230-10239
    • Lai, Z.1    McCulloch, J.2    Lashuel, H.A.3    Kelly, J.W.4
  • 47
    • 0035949632 scopus 로고    scopus 로고
    • Anion shielding of electrostatic repulsions in transthyretin modulates stability and amyloidosis: Insight into the chaotrope unfolding dichotomy
    • Hammarstrom P., Jiang X., Deechongkit S. and Kelly J. W. (2001) Anion shielding of electrostatic repulsions in transthyretin modulates stability and amyloidosis: insight into the chaotrope unfolding dichotomy. Biochemistry 40: 11453-11459
    • (2001) Biochemistry , vol.40 , pp. 11453-11459
    • Hammarstrom, P.1    Jiang, X.2    Deechongkit, S.3    Kelly, J.W.4
  • 48
    • 0035964955 scopus 로고    scopus 로고
    • Trans-suppression of misfolding in an amyloid disease
    • Hammarstrom P., Schneider F. and Kelly J. W. (2001) Trans-suppression of misfolding in an amyloid disease. Science 293: 2459-2462
    • (2001) Science , vol.293 , pp. 2459-2462
    • Hammarstrom, P.1    Schneider, F.2    Kelly, J.W.3
  • 49
    • 0037473750 scopus 로고    scopus 로고
    • Prevention of transthyretin amyloid disease by changing protein misfolding energetics
    • Hammarstrom P., Wiseman R. L., Powers E. T. and Kelly J. W. (2003) Prevention of transthyretin amyloid disease by changing protein misfolding energetics. Science 299: 713-716
    • (2003) Science , vol.299 , pp. 713-716
    • Hammarstrom, P.1    Wiseman, R.L.2    Powers, E.T.3    Kelly, J.W.4
  • 50
    • 0033813424 scopus 로고    scopus 로고
    • A glimpse of a possible amyloidogenic intermediate of transthyretin
    • Liu K., Cho H. S., Lashuel H. A., Kelly J. W. and Wemmer D. E. (2000) A glimpse of a possible amyloidogenic intermediate of transthyretin. Nat. Struct. Biol. 7: 754-757
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 754-757
    • Liu, K.1    Cho, H.S.2    Lashuel, H.A.3    Kelly, J.W.4    Wemmer, D.E.5
  • 51
    • 0036306257 scopus 로고    scopus 로고
    • Native state hydrogen exchange study of suppressor and pathogenic variants of transthyretin
    • Liu K., Kelly J. W. and Wemmer D. E. (2002) Native state hydrogen exchange study of suppressor and pathogenic variants of transthyretin. J. Mol. Biol. 320: 821-832
    • (2002) J. Mol. Biol. , vol.320 , pp. 821-832
    • Liu, K.1    Kelly, J.W.2    Wemmer, D.E.3
  • 53
    • 0033281401 scopus 로고    scopus 로고
    • Hereditary renal amyloidosis associated with variant lysozyme in a large English family
    • Gillmore J. D., Booth D. R., Madhoo S., Pepys M. B. and Hawkins P. N. (1999) Hereditary renal amyloidosis associated with variant lysozyme in a large English family. Nephrol. Dial. Transplant. 14: 2639-2644
    • (1999) Nephrol. Dial. Transplant. , vol.14 , pp. 2639-2644
    • Gillmore, J.D.1    Booth, D.R.2    Madhoo, S.3    Pepys, M.B.4    Hawkins, P.N.5
  • 54
    • 0036189848 scopus 로고    scopus 로고
    • Hereditary renal amyloidosis caused by a new variant lysozyme W64R in a French family
    • Valleix S., Drunat S., Philit J. B., Adoue D., Piette J. C., Droz D. et al. (2002) Hereditary renal amyloidosis caused by a new variant lysozyme W64R in a French family. Kidney Int. 61: 907-912
    • (2002) Kidney Int. , vol.61 , pp. 907-912
    • Valleix, S.1    Drunat, S.2    Philit, J.B.3    Adoue, D.4    Piette, J.C.5    Droz, D.6
  • 55
    • 0242500842 scopus 로고    scopus 로고
    • A novel lysozyme mutation Phe57Ile associated with hereditary renal amyloidosis
    • Yazaki M., Farrell S. A. and Benson M. D. (2003) A novel lysozyme mutation Phe57Ile associated with hereditary renal amyloidosis. Kidney Int. 63: 1652-1657
    • (2003) Kidney Int. , vol.63 , pp. 1652-1657
    • Yazaki, M.1    Farrell, S.A.2    Benson, M.D.3
  • 56
    • 0030474922 scopus 로고    scopus 로고
    • The structure, stability and folding process of amyloidogenic mutant human lysozyme
    • Funahashi J., Takano K., Ogasahara K., Yamagata Y. and Yutani K. (1996) The structure, stability and folding process of amyloidogenic mutant human lysozyme. J. Biochem. 120: 1216-1223
    • (1996) J. Biochem. , vol.120 , pp. 1216-1223
    • Funahashi, J.1    Takano, K.2    Ogasahara, K.3    Yamagata, Y.4    Yutani, K.5
  • 57
    • 0031056829 scopus 로고    scopus 로고
    • Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis
    • Booth D. R., Sunde M., Bellotti V., Robinson C. V., Hutchinson W. L., Fraser P. E. et al. (1997) Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis. Nature 385: 787-793
    • (1997) Nature , vol.385 , pp. 787-793
    • Booth, D.R.1    Sunde, M.2    Bellotti, V.3    Robinson, C.V.4    Hutchinson, W.L.5    Fraser, P.E.6
  • 58
    • 0033580657 scopus 로고    scopus 로고
    • Mechanistic studies of the folding of human lysozyme and the origin of amyloidogenic behavior in its disease-related variants
    • Canet D., Sunde M., Last A. M., Miranker A., Spencer A., Robinson C. V. et al. (1999) Mechanistic studies of the folding of human lysozyme and the origin of amyloidogenic behavior in its disease-related variants. Biochemistry 38: 6419-6427
    • (1999) Biochemistry , vol.38 , pp. 6419-6427
    • Canet, D.1    Sunde, M.2    Last, A.M.3    Miranker, A.4    Spencer, A.5    Robinson, C.V.6
  • 59
    • 0035165190 scopus 로고    scopus 로고
    • The stability and folding process of amyloidogenic mutant human lysozymes
    • Takano K., Funahashi J. and Yutani K. (2001) The stability and folding process of amyloidogenic mutant human lysozymes. Eur. J. Biochem. 268: 155-159
    • (2001) Eur. J. Biochem. , vol.268 , pp. 155-159
    • Takano, K.1    Funahashi, J.2    Yutani, K.3
  • 60
    • 0035177019 scopus 로고    scopus 로고
    • Characterization of the structure and dynamics of amyloidogenic variants of human lysozyme by NMR spectroscopy
    • Chamberlain A. K., Receveur V., Spencer A., Redfield C. and Dobson C. M. (2001) Characterization of the structure and dynamics of amyloidogenic variants of human lysozyme by NMR spectroscopy. Protein Sci. 10: 2525-2530
    • (2001) Protein Sci. , vol.10 , pp. 2525-2530
    • Chamberlain, A.K.1    Receveur, V.2    Spencer, A.3    Redfield, C.4    Dobson, C.M.5
  • 61
    • 0033849915 scopus 로고    scopus 로고
    • Amyloid fibril formation and seeding by wild-type human lysozyme and its disease-related mutational variants
    • Morozova-Roche L. A., Zurdo J., Spencer A., Noppe W., Receveur V., Archer D. B. et al. (2000) Amyloid fibril formation and seeding by wild-type human lysozyme and its disease-related mutational variants. J. Struct. Biol. 130: 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
  • 62
    • 0036220131 scopus 로고    scopus 로고
    • Local cooperativity in the unfolding of an amyloidogenic variant of human lysozyme
    • Canet D., Last A. M., Tito P., Sunde M., Spencer A., Archer D. B. et al. (2002) Local cooperativity in the unfolding of an amyloidogenic variant of human lysozyme. Nat. Struct. Biol. 9: 308-315
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 308-315
    • Canet, D.1    Last, A.M.2    Tito, P.3    Sunde, M.4    Spencer, A.5    Archer, D.B.6
  • 63
    • 0036775896 scopus 로고    scopus 로고
    • Elongation in a beta-structure promotes amyloid-like fibril formation of human lysozyme
    • Tokyo
    • Goda S., Takano K., Yamagata Y., Maki S., Namba K. and Yutani K. (2002) Elongation in a beta-structure promotes amyloid-like fibril formation of human lysozyme. J. Biochem. (Tokyo) 132: 655-661
    • (2002) J. Biochem. , vol.132 , pp. 655-661
    • Goda, S.1    Takano, K.2    Yamagata, Y.3    Maki, S.4    Namba, K.5    Yutani, K.6
  • 66
    • 0030050003 scopus 로고    scopus 로고
    • Beta-2-microglobulin-associated amyloidosis
    • Floege J. and Ehlerding G. ( 1996) Beta-2-microglobulin-associated amyloidosis. Nephron 72: 9-26
    • (1996) Nephron , vol.72 , pp. 9-26
    • Floege, J.1    Ehlerding, G.2
  • 67
    • 18244412979 scopus 로고    scopus 로고
    • Removal of the N-terminal hexapeptide from human beta2-microglobulin facilitates protein aggregation and fibril formation
    • Esposito G., Michelutti R., Verdone G., Viglino P., Hernandez H., Robinson C. V. et al. (2000) Removal of the N-terminal hexapeptide from human beta2-microglobulin facilitates protein aggregation and fibril formation. Protein Sci. 9: 831-845
    • (2000) Protein Sci. , vol.9 , pp. 831-845
    • Esposito, G.1    Michelutti, R.2    Verdone, G.3    Viglino, P.4    Hernandez, H.5    Robinson, C.V.6
  • 68
    • 0037059764 scopus 로고    scopus 로고
    • Investigation of a peptide responsible for amyloid fibril formation of beta 2-microglobulin by achromobacter protease I
    • Kozhukh G. V., Hagihara Y., Kawakami T., Hasegawa K., Naiki H. and Goto Y. (2002) Investigation of a peptide responsible for amyloid fibril formation of beta 2-microglobulin by achromobacter protease I. J. Biol. Chem. 277: 1310-1315
    • (2002) J. Biol. Chem. , vol.277 , pp. 1310-1315
    • Kozhukh, G.V.1    Hagihara, Y.2    Kawakami, T.3    Hasegawa, K.4    Naiki, H.5    Goto, Y.6
  • 70
    • 0035955555 scopus 로고    scopus 로고
    • Beta(2)-microglobulin and its deamidated variant, N17D form amyloid fibrils with a range of morphologies in vitro
    • Kad N. M., Thomson N. H., Smith D. P., Smith D. A. and Radford S. E. (2001) Beta(2)-microglobulin and its deamidated variant, N17D form amyloid fibrils with a range of morphologies in vitro. J. Mol. Biol. 313: 559-571
    • (2001) J. Mol. Biol. , vol.313 , pp. 559-571
    • Kad, N.M.1    Thomson, N.H.2    Smith, D.P.3    Smith, D.A.4    Radford, S.E.5
  • 72
    • 0035367287 scopus 로고    scopus 로고
    • Kidney dialysis-associated amyloidosis: A molecular role for copper in fiber formation
    • Morgan C. J., Gelfand M., Atreya C. and Miranker A. D. (2001) Kidney dialysis-associated amyloidosis: a molecular role for copper in fiber formation. J. Mol. Biol. 309: 339-345
    • (2001) J. Mol. Biol. , vol.309 , pp. 339-345
    • Morgan, C.J.1    Gelfand, M.2    Atreya, C.3    Miranker, A.D.4
  • 73
    • 0037183496 scopus 로고    scopus 로고
    • Formation of a copper specific binding site in non-native states of beta-2-microglobulin
    • Eakin C. M., Knight J. D., Morgan C. J., Gelfand M. A. and Miranker A. D. (2002) Formation of a copper specific binding site in non-native states of beta-2-microglobulin. Biochemistry 41: 10646-10656
    • (2002) Biochemistry , vol.41 , pp. 10646-10656
    • Eakin, C.M.1    Knight, J.D.2    Morgan, C.J.3    Gelfand, M.A.4    Miranker, A.D.5
  • 74
    • 18244378561 scopus 로고    scopus 로고
    • The solution structure of human beta2-microglobulin reveals the prodromes of its amyloid transition
    • Verdone G., Corazza A., Viglino P., Pettirossi F., Giorgetti S., Mangione P. et al. (2002) The solution structure of human beta2-microglobulin reveals the prodromes of its amyloid transition. Protein Sci. 11: 487-499
    • (2002) Protein Sci. , vol.11 , pp. 487-499
    • Verdone, G.1    Corazza, A.2    Viglino, P.3    Pettirossi, F.4    Giorgetti, S.5    Mangione, P.6
  • 76
  • 79
    • 0028308104 scopus 로고
    • URE3 as an altered URE2 protein: Evidence for a prion analog in Saccharomyces cerevisiae
    • Wickner R. B. (1994) [URE3] as an altered URE2 protein: evidence for a prion analog in Saccharomyces cerevisiae. Science 264: 566-569
    • (1994) Science , vol.264 , pp. 566-569
    • Wickner, R.B.1
  • 81
    • 0034160086 scopus 로고    scopus 로고
    • Protein-only inheritance in yeast: Something to get [PSI+]-ched about
    • Serio T. R. and Lindquist S. L. (2000) Protein-only inheritance in yeast: something to get [PSI+]-ched about. Trends Cell Biol. 10: 98-105
    • (2000) Trends Cell Biol. , vol.10 , pp. 98-105
    • Serio, T.R.1    Lindquist, S.L.2
  • 82
    • 0028859540 scopus 로고
    • Prion-inducing domain of yeast Ure2p and protease resistance of Ure2p in prion-containing cells
    • Masison D. C. and Wickner R. B. (1995) Prion-inducing domain of yeast Ure2p and protease resistance of Ure2p in prion-containing cells. Science 270: 93-95
    • (1995) Science , vol.270 , pp. 93-95
    • Masison, D.C.1    Wickner, R.B.2
  • 83
    • 0032568793 scopus 로고    scopus 로고
    • A critical role for amino-terminal glutamine/asparagine repeats in the formation and propagation of a yeast prion
    • DePace A. H., Santoso A., Hillner P. and Weissman J. S. (1998) A critical role for amino-terminal glutamine/asparagine repeats in the formation and propagation of a yeast prion. Cell 93: 1241-1252
    • (1998) Cell , vol.93 , pp. 1241-1252
    • Depace, A.H.1    Santoso, A.2    Hillner, P.3    Weissman, J.S.4
  • 84
    • 0034710897 scopus 로고    scopus 로고
    • A census of glutamine/asparagine-rich regions: Implications for their conserved function and the prediction of novel prions
    • Michelitsch M. D. and Weissman J. S. (2000) A census of glutamine/asparagine-rich regions: implications for their conserved function and the prediction of novel prions. Proc. Natl. Acad. Sci. USA 97: 11910-11915
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 11910-11915
    • Michelitsch, M.D.1    Weissman, J.S.2
  • 85
    • 0027332116 scopus 로고
    • Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins. Proc
    • Pan K. M., Baldwin M., Nguyen J., Gasset M., Serban A., Groth D. et al. (1993) Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins. Proc. Natl. Acad. Sci. USA 90: 10962-10966
    • (1993) Natl. Acad. Sci. USA , vol.90 , pp. 10962-10966
    • Pan, K.M.1    Baldwin, M.2    Nguyen, J.3    Gasset, M.4    Serban, A.5    Groth, D.6
  • 86
    • 0035312586 scopus 로고    scopus 로고
    • Interactions between prion protein isoforms: The kiss of death?
    • Caughey B. (2001) Interactions between prion protein isoforms: the kiss of death? Trends Biochem. Sci. 26: 235-242
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 235-242
    • Caughey, B.1
  • 88
    • 0030967895 scopus 로고    scopus 로고
    • Solution structure of a 142-residue recombinant prion protein corresponding to the infectious fragment of the scrapie isoform
    • James T. L., Liu H., Ulyanov N. B., Fair-Jones S., Zhang H., Donne D. G. et al. (1997) Solution structure of a 142-residue recombinant prion protein corresponding to the infectious fragment of the scrapie isoform. Proc. Natl. Acad. Sci. USA 94: 10086-10091
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 10086-10091
    • James, T.L.1    Liu, H.2    Ulyanov, N.B.3    Fair-Jones, S.4    Zhang, H.5    Donne, D.G.6
  • 90
    • 0032979289 scopus 로고    scopus 로고
    • Extremely rapid folding of the C-terminal domain of the prion protein without kinetic intermediates
    • Wildegger G., Liemann S. and Glockshuber R. (1999) Extremely rapid folding of the C-terminal domain of the prion protein without kinetic intermediates. Nat. Struct. Biol. 6: 550-553
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 550-553
    • Wildegger, G.1    Liemann, S.2    Glockshuber, R.3
  • 91
    • 0033574161 scopus 로고    scopus 로고
    • Influence of amino acid substitutions related to inherited human prion diseases on the thermodynamic stability of the cellular prion protein
    • Liemann S. and Glockshuber R. (1999) Influence of amino acid substitutions related to inherited human prion diseases on the thermodynamic stability of the cellular prion protein. Biochemistry 38: 3258-3267
    • (1999) Biochemistry , vol.38 , pp. 3258-3267
    • Liemann, S.1    Glockshuber, R.2
  • 92
    • 0030781922 scopus 로고    scopus 로고
    • pH-dependent stability and conformation of the recombinant human prion protein PrP(90-231)
    • Swietnicki W., Petersen R., Gambetti P. and Surewicz W. K. (1997) pH-dependent stability and conformation of the recombinant human prion protein PrP(90-231). J. Biol. Chem. 272: 27517-27520
    • (1997) J. Biol. Chem. , vol.272 , pp. 27517-27520
    • Swietnicki, W.1    Petersen, R.2    Gambetti, P.3    Surewicz, W.K.4
  • 93
    • 0032568592 scopus 로고    scopus 로고
    • A scrapie-like unfolding intermediate of the prion protein domain PrP(121-231) induced by acidic pH
    • Hornemann S. and Glockshuber R. (1998) A scrapie-like unfolding intermediate of the prion protein domain PrP(121-231) induced by acidic pH. Proc. Natl. Acad. Sci. USA 95: 6010-6014
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 6010-6014
    • Hornemann, S.1    Glockshuber, R.2
  • 96
    • 0034610180 scopus 로고    scopus 로고
    • Abeta amyloid fibrils possess a core structure highly resistant to hydrogen exchange
    • Kheterpal I., Zhou S., Cook K. D. and Wetzel R. (2000) Abeta amyloid fibrils possess a core structure highly resistant to hydrogen exchange. Proc. Natl. Acad. Sci. USA 97: 13597-13601
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 13597-13601
    • Kheterpal, I.1    Zhou, S.2    Cook, K.D.3    Wetzel, R.4
  • 97
    • 0036414287 scopus 로고    scopus 로고
    • Identification and characterization of a novel molecular-recognition and self-assembly domain within the islet amyloid polypeptide
    • Mazor Y., Gilead S., Benhar I. and Gazit E. (2002) Identification and characterization of a novel molecular-recognition and self-assembly domain within the islet amyloid polypeptide. J. Mol. Biol. 322: 1013-1024
    • (2002) J. Mol. Biol. , vol.322 , pp. 1013-1024
    • Mazor, Y.1    Gilead, S.2    Benhar, I.3    Gazit, E.4
  • 98
    • 0034700129 scopus 로고    scopus 로고
    • Multiple quantum solid-state NMR indicates a parallel, not antiparallel, organization of beta-sheets in Alzheimer's beta-amyloid fibrils
    • Antzutkin O. N., Balbach J. J., Leapman R. D., Rizzo N. W., Reed J. and Tycko R. (2000) Multiple quantum solid-state NMR indicates a parallel, not antiparallel, organization of beta-sheets in Alzheimer's beta-amyloid fibrils. Proc. Natl. Acad. Sci. USA 97: 13045-13050
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 13045-13050
    • Antzutkin, O.N.1    Balbach, J.J.2    Leapman, R.D.3    Rizzo, N.W.4    Reed, J.5    Tycko, R.6
  • 99
    • 0034649352 scopus 로고    scopus 로고
    • Amyloid fibril formation by a beta 16-22, a seven-residue fragment of the Alzheimer's beta-amyloid peptide, and structural characterization by solid state NMR
    • Balbach J. J., Ishii Y., Antzutkin O. N., Leapman R. D., Rizzo N. W., Dyda F. et al. (2000) Amyloid fibril formation by A beta 16-22, a seven-residue fragment of the Alzheimer's beta-amyloid peptide, and structural characterization by solid state NMR. Biochemistry 39: 13748-13759
    • (2000) Biochemistry , vol.39 , pp. 13748-13759
    • Balbach, J.J.1    Ishii, Y.2    Antzutkin, O.N.3    Leapman, R.D.4    Rizzo, N.W.5    Dyda, F.6
  • 100
    • 0037168655 scopus 로고    scopus 로고
    • A structural model for Alzheimer's beta -amyloid fibrils based on experimental constraints from solid state NMR
    • Petkova A. T., Ishii Y., Balbach J. J., Antzutkin O. N., Leapman R. D., Delaglio F. et al. (2002) A structural model for Alzheimer's beta -amyloid fibrils based on experimental constraints from solid state NMR. Proc. Natl. Acad. Sci. USA 99: 16742-16747
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 16742-16747
    • Petkova, A.T.1    Ishii, Y.2    Balbach, J.J.3    Antzutkin, O.N.4    Leapman, R.D.5    Delaglio, F.6
  • 101
    • 0028818272 scopus 로고
    • Tertiary structure of an amyloid immunoglobulin light chain protein: A proposed model for amyloid fibril formation
    • Schormann N., Murrell J. R., Liepnieks J. J. and Benson M. D. (1995) Tertiary structure of an amyloid immunoglobulin light chain protein: a proposed model for amyloid fibril formation. Proc. Natl. Acad. Sci. USA 92: 9490-9494
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 9490-9494
    • Schormann, N.1    Murrell, J.R.2    Liepnieks, J.J.3    Benson, M.D.4
  • 102
    • 0025139469 scopus 로고
    • Finnish hereditary amyloidosis. Amino acid sequence homology between the amyloid fibril protein and human plasma gelsoline
    • Maury C. P., Alli K. and Baumann M. (1990) Finnish hereditary amyloidosis. Amino acid sequence homology between the amyloid fibril protein and human plasma gelsoline. FEBS Lett. 260: 85-87
    • (1990) FEBS Lett. , vol.260 , pp. 85-87
    • Maury, C.P.1    Alli, K.2    Baumann, M.3
  • 103
    • 0033793872 scopus 로고    scopus 로고
    • Mechanisms of amyloidogenesis
    • Kelly J. W. (2000) Mechanisms of amyloidogenesis. Nat. Struct. Biol. 7: 824-826
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 824-826
    • Kelly, J.W.1
  • 104
    • 0034714351 scopus 로고    scopus 로고
    • Nucleated conformational conversion and the replication of conformational information by a prion determinant
    • Serio T. R., Cashikar A. G., Kowal A. S., Sawicki G. J., Moslehi J. J., Serpell L. et al. (2000) Nucleated conformational conversion and the replication of conformational information by a prion determinant. Science 289: 1317-1321
    • (2000) Science , vol.289 , pp. 1317-1321
    • Serio, T.R.1    Cashikar, A.G.2    Kowal, A.S.3    Sawicki, G.J.4    Moslehi, J.J.5    Serpell, L.6
  • 105
    • 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
  • 106
    • 0037066715 scopus 로고    scopus 로고
    • Elucidation of the molecular mechanism during the early events in immunoglobulin light chain amyloid fibrillation. Evidence for an off-pathway oligomer at acidic pH
    • Souillac P. O., Uversky V. N., Millett I. S., Khurana R., Doniach S. and Fink A. L. (2002) Elucidation of the molecular mechanism during the early events in immunoglobulin light chain amyloid fibrillation. Evidence for an off-pathway oligomer at acidic pH. J. Biol. Chem. 277: 12666-12679
    • (2002) J. Biol. Chem. , vol.277 , pp. 12666-12679
    • Souillac, P.O.1    Uversky, V.N.2    Millett, I.S.3    Khurana, R.4    Doniach, S.5    Fink, A.L.6
  • 107
    • 0034875603 scopus 로고    scopus 로고
    • A mathematical model of the kinetics of beta-amyloid fibril growth from the denatured state
    • Pallitto M. M. and Murphy R. M. (2001) A mathematical model of the kinetics of beta-amyloid fibril growth from the denatured state. Biophys. J. 81: 1805-1822
    • (2001) Biophys. J. , vol.81 , pp. 1805-1822
    • Pallitto, M.M.1    Murphy, R.M.2
  • 108
    • 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
    • Yonezawa Y., Tanaka S., Kubota T., Wakabayashi K.,Yutani K. and Fujiwara S. (2002) 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: 237-251
    • (2002) J. Mol. Biol. , vol.323 , pp. 237-251
    • Yonezawa, Y.1    Tanaka, S.2    Kubota, T.3    Wakabayashi, K.4    Yutani, K.5    Fujiwara, S.6
  • 109
    • 0242668337 scopus 로고    scopus 로고
    • Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
    • Kayed R., Head E., Thompson J. L., Mclntire T. M., Milton S. C., Cotman C. W. et al. (2003) Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 300: 486-489
    • (2003) Science , vol.300 , pp. 486-489
    • Kayed, R.1    Head, E.2    Thompson, J.L.3    Mclntire, T.M.4    Milton, S.C.5    Cotman, C.W.6
  • 110
    • 0027988041 scopus 로고
    • Polar zippers: Their role in human disease
    • Perutz M. (1994) Polar zippers: their role in human disease. Protein Sci. 3: 1629-1637
    • (1994) Protein Sci. , vol.3 , pp. 1629-1637
    • Perutz, M.1
  • 111
    • 0028283985 scopus 로고
    • Glutamine repeats as polar zippers: Their possible role in inherited neurodegenerative diseases
    • Perutz M. F., Johnson T., Suzuki M. and Finch J. T. (1994) Glutamine repeats as polar zippers: their possible role in inherited neurodegenerative diseases. Proc. Natl. Acad. Sci. USA 91: 5355-5358
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 5355-5358
    • Perutz, M.F.1    Johnson, T.2    Suzuki, M.3    Finch, J.T.4
  • 112
    • 0033522983 scopus 로고    scopus 로고
    • Induction of beta-sheet structure in amyloidogenic peptides by neutralization of aspartate: A model for amyloid nucleation
    • Orpiszewski J. and Benson M. D. (1999) Induction of beta-sheet structure in amyloidogenic peptides by neutralization of aspartate: a model for amyloid nucleation. J. Mol. Biol. 289: 413-428
    • (1999) J. Mol. Biol. , vol.289 , pp. 413-428
    • Orpiszewski, J.1    Benson, M.D.2
  • 113
    • 0030853453 scopus 로고    scopus 로고
    • Polyalanine-based peptides as models for self-associated beta-pleated-sheet complexes
    • Blondelle S. E., Forood B., Houghten R. A. and Perez-Paya E. (1997) Polyalanine-based peptides as models for self-associated beta-pleated-sheet complexes. Biochemistry 36: 8393-8400
    • (1997) Biochemistry , vol.36 , pp. 8393-8400
    • Blondelle, S.E.1    Forood, B.2    Houghten, R.A.3    Perez-Paya, E.4
  • 114
    • 0036108484 scopus 로고    scopus 로고
    • 3D domain swapping: As domains continue to swap
    • Liu Y. and Eisenberg D. (2002) 3D domain swapping: as domains continue to swap. Protein Sci. 11: 1285-1299
    • (2002) Protein Sci. , vol.11 , pp. 1285-1299
    • Liu, Y.1    Eisenberg, D.2
  • 115
    • 0030770294 scopus 로고    scopus 로고
    • Oligomer formation by 3D domain swapping: A model for protein assembly and misassembly
    • Schlunegger M. P., Bennett M. J. and Eisenberg D. (1997) Oligomer formation by 3D domain swapping: a model for protein assembly and misassembly. Adv. Protein Chem. 50: 61-122
    • (1997) Adv. Protein Chem. , vol.50 , pp. 61-122
    • Schlunegger, M.P.1    Bennett, M.J.2    Eisenberg, D.3
  • 117
    • 0035069135 scopus 로고    scopus 로고
    • Human cystatin C, an amyloidogenic protein, dimerizes through three-dimensional domain swapping
    • Janowski R., Kozak M., Jankowska E., Grzonka Z., Grubb A., Abrahamson M. et al. (2001) Human cystatin C, an amyloidogenic protein, dimerizes through three-dimensional domain swapping. Nat. Struct. Biol. 8: 316-320
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 316-320
    • Janowski, R.1    Kozak, M.2    Jankowska, E.3    Grzonka, Z.4    Grubb, A.5    Abrahamson, M.6
  • 118
    • 0035801540 scopus 로고    scopus 로고
    • Three-dimensional domain swapping in the folded and molten-globule states of cystatins, an amyloid-forming structural superfamily
    • Staniforth R. A., Giannini S., Higgins L. D., Conroy M. J., Hounslow A. M., Jerala R. et al. (2001) Three-dimensional domain swapping in the folded and molten-globule states of cystatins, an amyloid-forming structural superfamily. EMBO J. 20: 4774-4781
    • (2001) EMBO J. , vol.20 , pp. 4774-4781
    • Staniforth, R.A.1    Giannini, S.2    Higgins, L.D.3    Conroy, M.J.4    Hounslow, A.M.5    Jerala, R.6
  • 119
    • 0035826713 scopus 로고    scopus 로고
    • Three-dimensional domain swapping in p13suc1 occurs in the unfolded state and is controlled by conserved proline residues
    • Rousseau F., Schymkowitz J. W., Wilkinson H. R. and Itzhaki L. S. (2001) Three-dimensional domain swapping in p13suc1 occurs in the unfolded state and is controlled by conserved proline residues. Proc. Natl. Acad. Sci. USA 98: 5596-5601
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 5596-5601
    • Rousseau, F.1    Schymkowitz, J.W.2    Wilkinson, H.R.3    Itzhaki, L.S.4
  • 120
    • 0035127031 scopus 로고    scopus 로고
    • A domain-swapped RNase a dimer with implications for amyloid formation
    • Liu Y., Gotte G., Libonati M. and Eisenberg D. (2001) A domain-swapped RNase A dimer with implications for amyloid formation. Nat. Struct. Biol. 8: 211-214
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 211-214
    • Liu, Y.1    Gotte, G.2    Libonati, M.3    Eisenberg, D.4
  • 121
    • 0034646573 scopus 로고    scopus 로고
    • Chemical dissection and reassembly of amyloid fibrils formed by a peptide fragment of transthyretin
    • MacPhee C. E. and Dobson C. M. (2000) Chemical dissection and reassembly of amyloid fibrils formed by a peptide fragment of transthyretin. J. Mol. Biol. 297: 1203-1215
    • (2000) J. Mol. Biol. , vol.297 , pp. 1203-1215
    • MacPhee, C.E.1    Dobson, C.M.2
  • 123
    • 0034723150 scopus 로고    scopus 로고
    • Identification of a penta- and hexapeptide of islet amyloid polypeptide (IAPP) with amyloidogenic and cytotoxic properties
    • Tenidis K., Waldner M., Bernhagen J., Fischle W., Bergmann M., Weber M. et al. (2000) Identification of a penta-and hexapeptide of islet amyloid polypeptide (IAPP) with amyloidogenic and cytotoxic properties. J. Mol. Biol. 295: 1055-1071
    • (2000) J. Mol. Biol. , vol.295 , pp. 1055-1071
    • Tenidis, K.1    Waldner, M.2    Bernhagen, J.3    Fischle, W.4    Bergmann, M.5    Weber, M.6
  • 124
    • 0033579545 scopus 로고    scopus 로고
    • Analysis of amylin cleavage products provides new insights into the amyloidogenic region of human amylin
    • Nilsson M. R. and Raleigh D. P. (1999) Analysis of amylin cleavage products provides new insights into the amyloidogenic region of human amylin. J. Mol. Biol. 294: 1375-1385
    • (1999) J. Mol. Biol. , vol.294 , pp. 1375-1385
    • Nilsson, M.R.1    Raleigh, D.P.2
  • 125
    • 0037022563 scopus 로고    scopus 로고
    • Natural beta-sheet proteins use negative design to avoid edge-to-edge aggregation
    • Richardson J. S. and Richardson D. C. (2002) Natural beta-sheet proteins use negative design to avoid edge-to-edge aggregation. Proc. Natl. Acad. Sci. USA 99: 2754-2759
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 2754-2759
    • Richardson, J.S.1    Richardson, D.C.2
  • 126
    • 0032972592 scopus 로고    scopus 로고
    • Effects of sequential proline substitutions on amyloid formation by human amylin20-29
    • Moriarty D. F. and Raleigh D. P. (1999) Effects of sequential proline substitutions on amyloid formation by human amylin20-29. Biochemistry 38: 1811-1818
    • (1999) Biochemistry , vol.38 , pp. 1811-1818
    • Moriarty, D.F.1    Raleigh, D.P.2
  • 127
    • 0037022661 scopus 로고    scopus 로고
    • Rationally designed mutations convert de novo amyloid-like fibrils into monomeric beta-sheet proteins
    • Wang W. and Hecht M. H. (2002) Rationally designed mutations convert de novo amyloid-like fibrils into monomeric beta-sheet proteins. Proc. Natl. Acad. Sci. USA 99: 2760-2765
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 2760-2765
    • Wang, W.1    Hecht, M.H.2
  • 129
    • 0035804936 scopus 로고    scopus 로고
    • Identification of a novel human islet amyloid polypeptide beta-sheet domain and factors influencing fibrillogenesis
    • Jaikaran E. T., Higham C. E., Serpell L. C., Zurdo J., Gross M., Clark A. et al. (2001) Identification of a novel human islet amyloid polypeptide beta-sheet domain and factors influencing fibrillogenesis. J. Mol. Biol. 308: 515-525
    • (2001) J. Mol. Biol. , vol.308 , pp. 515-525
    • Jaikaran, E.T.1    Higham, C.E.2    Serpell, L.C.3    Zurdo, J.4    Gross, M.5    Clark, A.6
  • 131
    • 0035956924 scopus 로고    scopus 로고
    • An amyloid-forming peptide from the yeast prion Sup35 reveals a dehydrated beta-sheet structure for amyloid
    • Balbirnie M., Grothe R. and Eisenberg D. S. (2001) An amyloid-forming peptide from the yeast prion Sup35 reveals a dehydrated beta-sheet structure for amyloid. Proc. Natl. Acad. Sci. USA 98: 2375-2380
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 2375-2380
    • Balbirnie, M.1    Grothe, R.2    Eisenberg, D.S.3
  • 132
  • 133
    • 0036845354 scopus 로고    scopus 로고
    • The behaviour of polyamino acids reveals an inverse side chain effect in amyloid structure formation
    • Fandrich M. and Dobson C. M. (2002) The behaviour of polyamino acids reveals an inverse side chain effect in amyloid structure formation. EMBO J. 21: 5682-5690
    • (2002) EMBO J. , vol.21 , pp. 5682-5690
    • Fandrich, M.1    Dobson, C.M.2
  • 134
    • 0016259873 scopus 로고
    • Crystal structure of polyglycine I
    • Lotz B. (1974) Crystal structure of polyglycine I. J. Mol. Biol. 87: 169-180
    • (1974) J. Mol. Biol. , vol.87 , pp. 169-180
    • Lotz, B.1
  • 135
    • 0029863697 scopus 로고    scopus 로고
    • Acetylcholinesterase accelerates assembly of amyloid-beta-peptides into Alzheimer's fibrils: Possible role of the peripheral site of the enzyme
    • Inestrosa N. C., Alvarez A., Perez C. A., Moreno R. D., Vicente M., Linker C. et al. (1996) Acetylcholinesterase accelerates assembly of amyloid-beta-peptides into Alzheimer's fibrils: possible role of the peripheral site of the enzyme. Neuron 16: 881-891
    • (1996) Neuron , vol.16 , pp. 881-891
    • Inestrosa, N.C.1    Alvarez, A.2    Perez, C.A.3    Moreno, R.D.4    Vicente, M.5    Linker, C.6
  • 136
    • 0032559003 scopus 로고    scopus 로고
    • Apolipoprotein e and antioxidants have different mechanisms of inhibiting Alzheimer's beta-amyloid fibril formation in vitro
    • Naiki H., Hasegawa K., Yamaguchi I., Nakamura H., Gejyo F. and Nakakuki K. (1998) Apolipoprotein E and antioxidants have different mechanisms of inhibiting Alzheimer's beta-amyloid fibril formation in vitro. Biochemistry 37: 17882-17889
    • (1998) Biochemistry , vol.37 , pp. 17882-17889
    • Naiki, H.1    Hasegawa, K.2    Yamaguchi, I.3    Nakamura, H.4    Gejyo, F.5    Nakakuki, K.6
  • 137
    • 0028180518 scopus 로고
    • A model for beta-amyloid aggregation and neurotoxicity based on free radical generation by the peptide: Relevance to Alzheimer disease
    • Hensley K., Carney J. M., Mattson M. P., Aksenova M., Harris M., Wu J. F. et al. (1994) A model for beta-amyloid aggregation and neurotoxicity based on free radical generation by the peptide: relevance to Alzheimer disease. Proc. Natl. Acad. Sci. USA 91: 3270-3274
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 3270-3274
    • Hensley, K.1    Carney, J.M.2    Mattson, M.P.3    Aksenova, M.4    Harris, M.5    Wu, J.F.6
  • 138
    • 0035916279 scopus 로고    scopus 로고
    • Amyloid-induced aggregation and precipitation of soluble proteins: An electrostatic contribution of the Alzheimer's beta(25-35) amyloid fibril
    • Konno T. (2001) Amyloid-induced aggregation and precipitation of soluble proteins: an electrostatic contribution of the Alzheimer's beta(25-35) amyloid fibril. Biochemistry 40: 2148-2154
    • (2001) Biochemistry , vol.40 , pp. 2148-2154
    • Konno, T.1
  • 139
    • 0028260192 scopus 로고
    • Nativelike secondary structure in interleukin1 beta inclusion bodies by attenuated total reflectance FTIR
    • Oberg K., Chrunyk B. A., Wetzel R. and Fink A. L. (1994) Nativelike secondary structure in interleukin1 beta inclusion bodies by attenuated total reflectance FTIR. Biochemistry 33: 2628-2634
    • (1994) Biochemistry , vol.33 , pp. 2628-2634
    • Oberg, K.1    Chrunyk, B.A.2    Wetzel, R.3    Fink, A.L.4
  • 140
    • 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
  • 141
    • 0035957228 scopus 로고    scopus 로고
    • Partially folded intermediates as critical precursors of light chain amyloid fibrils and amorphous aggregates
    • Khurana R., Gillespie J. R., Talapatra A., Minert L. J., Ionescu-Zanetti C., Millett I. et al. (2001) Partially folded intermediates as critical precursors of light chain amyloid fibrils and amorphous aggregates. Biochemistry 40: 3525-3535
    • (2001) Biochemistry , vol.40 , pp. 3525-3535
    • Khurana, R.1    Gillespie, J.R.2    Talapatra, A.3    Minert, L.J.4    Ionescu-Zanetti, C.5    Millett, I.6
  • 142
    • 0019536747 scopus 로고
    • Infrared and laser-Raman spectroscopic studies of thermally-induced globular protein gels
    • Clark A. H., Saunderson D. H. and Suggett A. (1981) 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
  • 143
    • 0001109729 scopus 로고
    • Formation of intermolecular beta-sheet structure during heat denaturation of ovalbumin
    • Kato A. and Takagi T. (1988) Formation of intermolecular beta-sheet structure during heat denaturation of ovalbumin. J. Agric. Food Chem. 36: 1156-1159
    • (1988) J. Agric. Food Chem. , vol.36 , pp. 1156-1159
    • Kato, A.1    Takagi, T.2
  • 144
    • 0026642332 scopus 로고
    • Aggregation of chymotrypsinogen: Portrait by infrared spectroscopy. Biochim
    • 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) Biophys. Acta , vol.1121 , pp. 183-188
    • Ismail, A.A.1    Manisch, H.H.2    Wong, P.T.3
  • 145
    • 0033059275 scopus 로고    scopus 로고
    • Amyloid-like aggregates of a plant protein: A case of a sweet-tasting protein, monellin
    • Konno T., Murata K. and Nagayama K. (1999) Amyloid-like aggregates of a plant protein: a case of a sweet-tasting protein, monellin. FEBS Lett. 454: 122-126
    • (1999) FEBS Lett. , vol.454 , pp. 122-126
    • Konno, T.1    Murata, K.2    Nagayama, K.3
  • 146
    • 0037166276 scopus 로고    scopus 로고
    • Amyloid-like fibril formation in an all beta-barrel protein involves the formation of partially structured intermediate(s)
    • Srisailam S., Wang H. M., Kumar T. K., Rajalingam D., Sivaraja V, Sheu H. S. et al. (2002) Amyloid-like fibril formation in an all beta-barrel protein involves the formation of partially structured intermediate(s). J. Biol. Chem. 277: 19027-19036
    • (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
  • 147
    • 0031149603 scopus 로고    scopus 로고
    • Kinetics and mechanism of amyloid formation by the prion protein H1 peptide as determined by time-dependent ESR
    • Lundberg K. M., Stenland C. J., Cohen F. E., Prusiner S. B. and Millhauser G. L. (1997) Kinetics and mechanism of amyloid formation by the prion protein H1 peptide as determined by time-dependent ESR. Chem. Biol. 4: 345-355
    • (1997) Chem. Biol. , vol.4 , pp. 345-355
    • Lundberg, K.M.1    Stenland, C.J.2    Cohen, F.E.3    Prusiner, S.B.4    Millhauser, G.L.5
  • 148
    • 0034758223 scopus 로고    scopus 로고
    • Conformational change, aggregation and fibril formation induced by detergent treatments of cellular prion protein
    • Xiong L. W., Raymond L. D., Hayes S. F., Raymond G. J. and Caughey B. (2001) Conformational change, aggregation and fibril formation induced by detergent treatments of cellular prion protein. J. Neurochem. 79: 669-678
    • (2001) J. Neurochem. , vol.79 , pp. 669-678
    • Xiong, L.W.1    Raymond, L.D.2    Hayes, S.F.3    Raymond, G.J.4    Caughey, B.5
  • 149
    • 0037178811 scopus 로고    scopus 로고
    • Kinetics and energetics of assembly, nucleation and growth of aggregates and fibrils for an amyloidogenic protein. Insights into transition states from pressure, temperature and co-solute studies
    • Kim Y. S., Randolph T. W., Stevens F. J. and Carpenter J. F. (2002) Kinetics and energetics of assembly, nucleation and growth of aggregates and fibrils for an amyloidogenic protein. Insights into transition states from pressure, temperature and co-solute studies. J. Biol. Chem. 277: 27240-27246
    • (2002) J. Biol. Chem. , vol.277 , pp. 27240-27246
    • Kim, Y.S.1    Randolph, T.W.2    Stevens, F.J.3    Carpenter, J.F.4
  • 150
    • 0033869084 scopus 로고    scopus 로고
    • Characterization of the oligomeric states of insulin in self-assembly and amyloid fibril formation by mass spectrometry
    • Nettleton E. J., Tito P., Sunde M., Bouchard M., Dobson C. M. and Robinson C. V. (2000) Characterization of the oligomeric states of insulin in self-assembly and amyloid fibril formation by mass spectrometry. Biophys. J. 79: 1053-1065
    • (2000) Biophys. J. , vol.79 , pp. 1053-1065
    • Nettleton, E.J.1    Tito, P.2    Sunde, M.3    Bouchard, M.4    Dobson, C.M.5    Robinson, C.V.6
  • 151
    • 0031885491 scopus 로고    scopus 로고
    • A stable single-layer beta-sheet without a hydrophobic core
    • Pham T. N., Koide A. and Koide S. (1998) A stable single-layer beta-sheet without a hydrophobic core. Nat. Struct. Biol. 5: 115-119
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 115-119
    • Pham, T.N.1    Koide, A.2    Koide, S.3
  • 152
    • 0034808069 scopus 로고    scopus 로고
    • The roles of turn formation and cross-strand interactions in fibrillization of peptides derived from the OspA single-layer beta-sheet
    • Ohnishi S., Koide A. and Koide S. (2001) The roles of turn formation and cross-strand interactions in fibrillization of peptides derived from the OspA single-layer beta-sheet. Protein Sci. 10: 2083-2092
    • (2001) Protein Sci. , vol.10 , pp. 2083-2092
    • Ohnishi, S.1    Koide, A.2    Koide, S.3
  • 154
    • 0036411969 scopus 로고    scopus 로고
    • Insights into the origin of the tendency of the PI3-SH3 domain to form amyloid fibrils
    • Ventura S., Lacroix E. and Serrano L. (2002) Insights into the origin of the tendency of the PI3-SH3 domain to form amyloid fibrils. J. Mol. Biol. 322: 1147-1158
    • (2002) J. Mol. Biol. , vol.322 , pp. 1147-1158
    • Ventura, S.1    Lacroix, E.2    Serrano, L.3
  • 155
    • 0026672305 scopus 로고
    • NMR determination of residual structure in a urea-denatured protein, the 434-repressor
    • Neri D., Billeter M., Wider G. and Wuthrich K. (1992) NMR determination of residual structure in a urea-denatured protein, the 434-repressor. Science 257: 1559-1563
    • (1992) Science , vol.257 , pp. 1559-1563
    • Neri, D.1    Billeter, M.2    Wider, G.3    Wuthrich, K.4
  • 156
    • 0027772180 scopus 로고
    • Urea-induced unfolding of the alpha subunit of tryptophan synthase: One-dimensional proton NMR evidence for residual structure near histidine-92 at high denaturant concentration
    • Saab-Rincon G., Froebe C. L. and Matthews C. R. (1993) Urea-induced unfolding of the alpha subunit of tryptophan synthase: one-dimensional proton NMR evidence for residual structure near histidine-92 at high denaturant concentration. Biochemistry 32: 13981-13990
    • (1993) Biochemistry , vol.32 , pp. 13981-13990
    • Saab-Rincon, G.1    Froebe, C.L.2    Matthews, C.R.3
  • 157
    • 0028349704 scopus 로고
    • Amide hydrogen exchange in a highly denatured state. Hen egg-white lysozyme in urea
    • Buck M., Radford S. E. and Dobson C. M. (1994) Amide hydrogen exchange in a highly denatured state. Hen egg-white lysozyme in urea. J. Mol. Biol. 237: 247-254
    • (1994) J. Mol. Biol. , vol.237 , pp. 247-254
    • Buck, M.1    Radford, S.E.2    Dobson, C.M.3
  • 158
    • 0028856228 scopus 로고
    • The equilibrium folding pathway of staphylococcal nuclease: Identification of the most stable chain-chain interactions by NMR and CD spectroscopy
    • Wang Y. and Shortle D. (1995) The equilibrium folding pathway of staphylococcal nuclease: identification of the most stable chain-chain interactions by NMR and CD spectroscopy. Biochemistry 34: 15895-15905
    • (1995) Biochemistry , vol.34 , pp. 15895-15905
    • Wang, Y.1    Shortle, D.2
  • 159
    • 0033551039 scopus 로고    scopus 로고
    • pKa values and the pH dependent stability of the N-terminal domain of L9 as probes of electrostatic interactions in the denatured state. Differentiation between local and nonlocal interactions
    • Kuhlman B., Luisi D. L., Young P. and Raleigh D. P. (1999) pKa values and the pH dependent stability of the N-terminal domain of L9 as probes of electrostatic interactions in the denatured state. Differentiation between local and nonlocal interactions. Biochemistry 38: 4896-4903
    • (1999) Biochemistry , vol.38 , pp. 4896-4903
    • Kuhlman, B.1    Luisi, D.L.2    Young, P.3    Raleigh, D.P.4
  • 160
    • 0037048655 scopus 로고    scopus 로고
    • Most of the structural elements of the globular domain of murine prion protein form fibrils with predominant beta-sheet structure
    • Jamin N., Coic Y. M., Landon C., Ovtracht L., Baleux F., Neumann J. M. et al. (2002) Most of the structural elements of the globular domain of murine prion protein form fibrils with predominant beta-sheet structure. FEBS Lett. 529: 256-260
    • (2002) FEBS Lett. , vol.529 , pp. 256-260
    • Jamin, N.1    Coic, Y.M.2    Landon, C.3    Ovtracht, L.4    Baleux, F.5    Neumann, J.M.6
  • 161
    • 0033730431 scopus 로고    scopus 로고
    • The Flory isolated-pair hypothesis is not valid for polypeptide chains: Implications for protein folding
    • Pappu R. V, Srinivasan R. and Rose G. D. (2000) The Flory isolated-pair hypothesis is not valid for polypeptide chains: implications for protein folding. Proc. Natl. Acad. Sci. USA 97: 12565-12570
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 12565-12570
    • Pappu, R.V.1    Srinivasan, R.2    Rose, G.D.3
  • 162
    • 0036394906 scopus 로고    scopus 로고
    • Native-like mean structure in the unfolded ensemble of small proteins
    • Zagrovic B., Snow C. D., Khaliq S., Shirts M. R. and Pande V. S. (2002) Native-like mean structure in the unfolded ensemble of small proteins. J. Mol. Biol. 323: 153-164
    • (2002) J. Mol. Biol. , vol.323 , pp. 153-164
    • Zagrovic, B.1    Snow, C.D.2    Khaliq, S.3    Shirts, M.R.4    Pande, V.S.5
  • 163
    • 0035919635 scopus 로고    scopus 로고
    • Persistence of native-like topology in a denatured protein in 8 M urea
    • Shortle D. and Ackerman M. S. (2001 ) Persistence of native-like topology in a denatured protein in 8 M urea. Science 293: 487-489
    • (2001) Science , vol.293 , pp. 487-489
    • Shortle, D.1    Ackerman, M.S.2
  • 164
    • 0037137257 scopus 로고    scopus 로고
    • Robustness of the long-range structure in denatured staphylococcal nuclease to changes in amino acid sequence
    • Ackerman M. S. and Shortle D. (2002) Robustness of the long-range structure in denatured staphylococcal nuclease to changes in amino acid sequence. Biochemistry 41: 13791-13797
    • (2002) Biochemistry , vol.41 , pp. 13791-13797
    • Ackerman, M.S.1    Shortle, D.2
  • 165
    • 0035119625 scopus 로고    scopus 로고
    • Chemical shifts in denatured proteins: Resonance assignments for denatured ubiquitin and comparisons with other denatured proteins
    • Peti W., Smith L. J., Redfield C. and Schwalbe H. (2001) Chemical shifts in denatured proteins: resonance assignments for denatured ubiquitin and comparisons with other denatured proteins. J. Biomol. NMR 19: 153-165
    • (2001) J. Biomol. NMR , vol.19 , pp. 153-165
    • Peti, W.1    Smith, L.J.2    Redfield, C.3    Schwalbe, H.4
  • 166
    • 0037340833 scopus 로고    scopus 로고
    • Observation of residual dipolar couplings in short peptides
    • Ohnishi S. and Shortle D. (2003) Observation of residual dipolar couplings in short peptides. Proteins 50: 546-551
    • (2003) Proteins , vol.50 , pp. 546-551
    • Ohnishi, S.1    Shortle, D.2
  • 167
    • 0034628913 scopus 로고    scopus 로고
    • Towards a complete description of the structural and dynamic properties of the denatured state of barnase and the role of residual structure in folding
    • Wong K. B., Clarke J., Bond C. J., Neira J. L., Freund S. M., Fersht A. R. et al. (2000) Towards a complete description of the structural and dynamic properties of the denatured state of barnase and the role of residual structure in folding. J. Mol. Biol. 296: 1257-1282
    • (2000) J. Mol. Biol. , vol.296 , pp. 1257-1282
    • Wong, K.B.1    Clarke, J.2    Bond, C.J.3    Neira, J.L.4    Freund, S.M.5    Fersht, A.R.6
  • 168
    • 0037633964 scopus 로고    scopus 로고
    • Effects of denaturants and substitutions of hydrophobic residues on backbone dynamics of denatured staphylococcal nuclease
    • Ohnishi S. and Shortle D. (2003) Effects of denaturants and substitutions of hydrophobic residues on backbone dynamics of denatured staphylococcal nuclease. Protein Sci. 12: 1530-1537
    • (2003) Protein Sci. , vol.12 , pp. 1530-1537
    • Ohnishi, S.1    Shortle, D.2
  • 169
    • 0029867797 scopus 로고    scopus 로고
    • Identification of pentosidine as a native structure for advanced glycation end products in beta-2-microglobulin-containing amyloid fibrils in patients with dialysis-related amyloidosis
    • Miyata T., Taneda S., Kawai R., Ueda Y., Horiuchi S., Hara M. et al. (1996) Identification of pentosidine as a native structure for advanced glycation end products in beta-2-microglobulin-containing amyloid fibrils in patients with dialysis-related amyloidosis. Proc. Natl. Acad. Sci. USA 93: 2353-2358
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 2353-2358
    • Miyata, T.1    Taneda, S.2    Kawai, R.3    Ueda, Y.4    Horiuchi, S.5    Hara, M.6
  • 170
    • 0037168446 scopus 로고    scopus 로고
    • Supramolecular structural constraints on Alzheimer's beta-amyloid fibrils from electron microscopy and solid-state nuclear magnetic resonance
    • Antzutkin O. N., Leapman R. D., Balbach J. J. and Tycko R. (2002) Supramolecular structural constraints on Alzheimer's beta-amyloid fibrils from electron microscopy and solid-state nuclear magnetic resonance. Biochemistry 41: 15436-15450
    • (2002) Biochemistry , vol.41 , pp. 15436-15450
    • Antzutkin, O.N.1    Leapman, R.D.2    Balbach, J.J.3    Tycko, R.4
  • 171
    • 0037960361 scopus 로고    scopus 로고
    • Site-specific identification of non-beta-srrand conformations in Alzheimer's beta-amyloid fibrils by solid-state NMR
    • Antzutkin O. N., Balbach J. J. and Tycko R. (2003) Site-specific identification of non-beta-srrand conformations in Alzheimer's beta-amyloid fibrils by solid-state NMR. Biophys. J. 84: 3326-3335
    • (2003) Biophys. J. , vol.84 , pp. 3326-3335
    • Antzutkin, O.N.1    Balbach, J.J.2    Tycko, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.