메뉴 건너뛰기




Volumn 110, Issue 9, 2002, Pages 1221-1232

Protein aggregation in disease: A role for folding intermediates forming specific multimeric interactions

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; AMYLOID; AMYLOID BETA PROTEIN; CHAPERONIN;

EID: 0036841958     PISSN: 00219738     EISSN: None     Source Type: Journal    
DOI: 10.1172/JCI0216781     Document Type: Review
Times cited : (210)

References (80)
  • 1
    • 0003023429 scopus 로고    scopus 로고
    • The hemoglobinopathies
    • C. Scriver, A. Beaudet, D. Valle, and W. Sly, editors. McGraw-Hill. New York, New York, USA
    • Weatherall, D.J., Clegg, J.B., Higgs, D.R., and Wood, W.G. 2001. The hemoglobinopathies. In Metabolic and Molecular Bases of Inherited Disease. C. Scriver, A. Beaudet, D. Valle, and W. Sly, editors. McGraw-Hill. New York, New York, USA. 4571-4636.
    • (2001) Metabolic and Molecular Bases of Inherited Disease , pp. 4571-4636
    • Weatherall, D.J.1    Clegg, J.B.2    Higgs, D.R.3    Wood, W.G.4
  • 2
    • 85047683832 scopus 로고    scopus 로고
    • 1-antitrypsin deficiency: Role of autophagy and mitochondrial injury in response to aggregated protein in the endoplasmic reticulum
    • In press
    • 1-antitrypsin deficiency: Role of autophagy and mitochondrial injury in response to aggregated protein in the endoplasmic reticulum. J. Clin. Invest. In press.
    • (2002) J. Clin. Invest.
    • Perlmutter, D.H.1
  • 3
    • 0002468969 scopus 로고    scopus 로고
    • 1-antitrypsin deficiency
    • C. Scriver, A. Beaudet, D. Valle, and W. Sly, editors. McGraw-Hill. New York, New York, USA
    • 1-antitrypsin deficiency. In Metabolic and Molecular Bases of Inherited Disease. C. Scriver, A. Beaudet, D. Valle, and W. Sly, editors. McGraw-Hill. New York, New York, USA. 5559-5584.
    • (2001) Metabolic and Molecular Bases of Inherited Disease , pp. 5559-5584
    • Cox, D.W.1
  • 4
    • 0036855661 scopus 로고    scopus 로고
    • Deciphering the genesis and fate of amyloid-β protein yields novel therapies for Alzheimer disease
    • In press
    • Selkoe, D.J. 2002. Deciphering the genesis and fate of amyloid-β protein yields novel therapies for Alzheimer disease. J. Clin. Invest. In press.
    • (2002) J. Clin. Invest.
    • Selkoe, D.J.1
  • 5
    • 0002053403 scopus 로고    scopus 로고
    • Cellular and molecular biology of the beta-amyloid precursor protein and Alzheimer's disease
    • R.N. Rosenberg, S.B. Prusiner, S. DiMauro, and R.L. Barchi, editors. Butterworth-Heinemann, Boston, Massachusetts, USA
    • Selkoe, D. 1997. Cellular and molecular biology of the beta-amyloid precursor protein and Alzheimer's disease. In The Molecular and Genetic Basis of Neurological Disease. R.N. Rosenberg, S.B. Prusiner, S. DiMauro, and R.L. Barchi, editors. Butterworth-Heinemann, Boston, Massachusetts, USA. 601-611.
    • (1997) The Molecular and Genetic Basis of Neurological Disease , pp. 601-611
    • Selkoe, D.1
  • 6
    • 0003041278 scopus 로고    scopus 로고
    • Molecular neuropathology of prion diseases
    • R.N. Rosenberg, S.B. Prusiner, S. DiMauro, and R.L. Barchi, editors. Butterworth-Heinemann, Boston, Massachusetts, USA
    • DeArmond, S.J., and Prusiner, S.B. 1997. Molecular neuropathology of prion diseases. In The Molecular and Genetic Basis of Neurological Disease. R.N. Rosenberg, S.B. Prusiner, S. DiMauro, and R.L. Barchi, editors. Butterworth-Heinemann, Boston, Massachusetts, USA. 145-163.
    • (1997) The Molecular and Genetic Basis of Neurological Disease , pp. 145-163
    • DeArmond, S.J.1    Prusiner, S.B.2
  • 7
    • 0030752709 scopus 로고    scopus 로고
    • Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain
    • DiFiglia, M., et al. 1997. Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain. Science. 277:1990-1993.
    • (1997) Science , vol.277 , pp. 1990-1993
    • DiFiglia, M.1
  • 8
    • 18544400323 scopus 로고    scopus 로고
    • Huntintin-encoded polyglutamine expansions form amyloid-like protein aggregates in vitro and in vivo
    • Scherzinger, E., et al. 1997. Huntintin-encoded polyglutamine expansions form amyloid-like protein aggregates in vitro and in vivo. Cell. 90:549-558.
    • (1997) Cell , vol.90 , pp. 549-558
    • Scherzinger, E.1
  • 9
    • 0034646391 scopus 로고    scopus 로고
    • Fibrils formed in vitro from α-synuclein and two mutant forms linked to Parkinson's disease are typical amyloid
    • Conway, K.A., Harper, J.D., and Lansbury, P.T. 2000. Fibrils formed in vitro from α-synuclein and two mutant forms linked to Parkinson's disease are typical amyloid. Biochemistry. 39:2552-2563.
    • (2000) Biochemistry , vol.39 , pp. 2552-2563
    • Conway, K.A.1    Harper, J.D.2    Lansbury, P.T.3
  • 10
    • 0034712918 scopus 로고    scopus 로고
    • Fiber diffraction of synthetic α-synuclein filaments shows amyloid-like cross-β conformation
    • Serpell, L.C., Berriman, J., Jakes, R., Goedert, M., and Crowther, R.A. 2000. Fiber diffraction of synthetic α-synuclein filaments shows amyloid-like cross-β conformation. Proc. Natl. Acad. Sci. USA. 97:4897-4902.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 4897-4902
    • Serpell, L.C.1    Berriman, J.2    Jakes, R.3    Goedert, M.4    Crowther, R.A.5
  • 11
    • 0015859467 scopus 로고
    • Principles that govern the folding of protein chains
    • Anfinsen, C.B. 1973. Principles that govern the folding of protein chains. Science. 181:223-230.
    • (1973) Science , vol.181 , pp. 223-230
    • Anfinsen, C.B.1
  • 12
    • 0028958601 scopus 로고
    • Characterizing transition states in protein folding: An essential step in the puzzle
    • Fersht, A.R. 1995. Characterizing transition states in protein folding: An essential step in the puzzle. Curr. Opin. Struct. Biol. 5:79-84.
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 79-84
    • Fersht, A.R.1
  • 13
    • 0034604105 scopus 로고    scopus 로고
    • A surprising simplicity to protein folding
    • Baker, D. 2000. A surprising simplicity to protein folding. Nature. 405:39-42.
    • (2000) Nature , vol.405 , pp. 39-42
    • Baker, D.1
  • 14
    • 0025345415 scopus 로고
    • Intermediates in the folding reactions of small proteins
    • Kim, P.S., and Baldwin, R.L. 1990. Intermediates in the folding reactions of small proteins. Annu. Rev. Biochem. 59:631-660.
    • (1990) Annu. Rev. Biochem. , vol.59 , pp. 631-660
    • Kim, P.S.1    Baldwin, R.L.2
  • 15
    • 0032878322 scopus 로고    scopus 로고
    • Formation of short-lived protein aggregates directly from the coil in two-state folding
    • Silow, M., Tan, Y.-J., Fersht, A.R., and Oliveberg, M. 1999. Formation of short-lived protein aggregates directly from the coil in two-state folding. Biochemistry. 38:13006-13012.
    • (1999) Biochemistry , vol.38 , pp. 13006-13012
    • Silow, M.1    Tan, Y.-J.2    Fersht, A.R.3    Oliveberg, M.4
  • 16
    • 0016206102 scopus 로고
    • Renaturation of Escherichia coli tryptophanase after exposure to 8 M urea
    • London, J., Skrzynia, C., and Goldberg, M.E. 1974. Renaturation of Escherichia coli tryptophanase after exposure to 8 M urea. Eur. J. Biochem. 47:409-415.
    • (1974) Eur. J. Biochem. , vol.47 , pp. 409-415
    • London, J.1    Skrzynia, C.2    Goldberg, M.E.3
  • 17
    • 0018788361 scopus 로고
    • Reconstitution of lactic dehydrogenase. Noncovalent aggregation vs. reactivation
    • Zettlmeissl, G., Rudolph, R., and Jaenicke, R. 1979. Reconstitution of lactic dehydrogenase. Noncovalent aggregation vs. reactivation. Biochemistry. 18:5567-5571.
    • (1979) Biochemistry , vol.18 , pp. 5567-5571
    • Zettlmeissl, G.1    Rudolph, R.2    Jaenicke, R.3
  • 18
    • 0023657520 scopus 로고
    • Quasi-irreversibility in the unfolding-refolding transition of phosphoglycerate kinase induced by guanidine hydrochloride
    • Mitraki, A., Betton, J.-M., Desmadril, M., and Yon, J.M. 1987. Quasi-irreversibility in the unfolding-refolding transition of phosphoglycerate kinase induced by guanidine hydrochloride. Eur. J. Biochem. 163:29-34.
    • (1987) Eur. J. Biochem. , vol.163 , pp. 29-34
    • Mitraki, A.1    Betton, J.-M.2    Desmadril, M.3    Yon, J.M.4
  • 19
    • 0023950869 scopus 로고
    • Solubility of different folding conformers of bovine growth hormone
    • Brems, D.N. 1988. Solubility of different folding conformers of bovine growth hormone. Biochemistry. 27:4541-4546.
    • (1988) Biochemistry , vol.27 , pp. 4541-4546
    • Brems, D.N.1
  • 20
    • 0028095571 scopus 로고
    • Crystal structure of P22 tailspike protein: Interdigitated subunits in a thermostable trimer
    • Steinbacher, S., et al. 1994. Crystal structure of P22 tailspike protein: Interdigitated subunits in a thermostable trimer. Science. 265:383-386.
    • (1994) Science , vol.265 , pp. 383-386
    • Steinbacher, S.1
  • 21
    • 0023883586 scopus 로고
    • Formation of aggregates from a thermolabile in vivo folding intermediate in P22 tailspike maturation
    • Haase-Pettingell, C.A., and King, J. 1988. Formation of aggregates from a thermolabile in vivo folding intermediate in P22 tailspike maturation. J. Biol. Chem. 263:4977-4983.
    • (1988) J. Biol. Chem. , vol.263 , pp. 4977-4983
    • Haase-Pettingell, C.A.1    King, J.2
  • 22
    • 0030063114 scopus 로고    scopus 로고
    • Thermolabile folding intermediates: Inclusion body precursors and chaperonin substrates
    • King, J., Haase-Pettingell, C., Robinson, A.S., Speed, M., and Mitraki, A. 1996. Thermolabile folding intermediates: Inclusion body precursors and chaperonin substrates. FASEB J. 10:57-66.
    • (1996) FASEB J. , vol.10 , pp. 57-66
    • King, J.1    Haase-Pettingell, C.2    Robinson, A.S.3    Speed, M.4    Mitraki, A.5
  • 23
    • 0025850262 scopus 로고
    • Global suppression of protein folding defects and inclusion body formation
    • Mitraki, A., Fane, B., Haase-Pettingell, C., Sturtevant, J., and King, J. 1991. Global suppression of protein folding defects and inclusion body formation. Science. 253:54-58.
    • (1991) Science , vol.253 , pp. 54-58
    • Mitraki, A.1    Fane, B.2    Haase-Pettingell, C.3    Sturtevant, J.4    King, J.5
  • 24
    • 0027210999 scopus 로고
    • Temperature-sensitive mutations in the phage P22 coat protein which interfere with polypeptide chain folding
    • Gordon, C.L., and King, J. 1993. Temperature-sensitive mutations in the phage P22 coat protein which interfere with polypeptide chain folding. J. Biol. Chem. 268:9358-9368.
    • (1993) J. Biol. Chem. , vol.268 , pp. 9358-9368
    • Gordon, C.L.1    King, J.2
  • 25
    • 0029785453 scopus 로고    scopus 로고
    • Specific aggregation of partially folded polypeptide chains: The molecular basis of inclusion body composition
    • Speed, M.A., Wang, D.I.C., and King, J. 1996. Specific aggregation of partially folded polypeptide chains: The molecular basis of inclusion body composition. Nat. Biotechnol. 14:1283-1287.
    • (1996) Nat. Biotechnol. , vol.14 , pp. 1283-1287
    • Speed, M.A.1    Wang, D.I.C.2    King, J.3
  • 26
    • 0028204771 scopus 로고
    • Domain swapping: Entangling alliances between proteins
    • Bennett, M.J., Choe, S., and Eisenberg, D. 1994. Domain swapping: Entangling alliances between proteins. Proc. Natl. Acad. Sci. USA. 91:3127-3131.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 3127-3131
    • Bennett, M.J.1    Choe, S.2    Eisenberg, D.3
  • 27
    • 0028865843 scopus 로고
    • 3D domain swapping: A mechanism for oligomer assembly
    • Bennett, MJ., Schlunegger, M.P., and Eisenberg, D. 1995. 3D domain swapping: A mechanism for oligomer assembly. Protein Sci. 4:2455-2468.
    • (1995) Protein Sci. , vol.4 , pp. 2455-2468
    • Bennett, M.J.1    Schlunegger, M.P.2    Eisenberg, D.3
  • 28
    • 85047684827 scopus 로고    scopus 로고
    • 1-antitrypsin polymerization and the serpinopath: pathobiology and prospects for therapy
    • In press
    • 1-antitrypsin polymerization and the serpinopath: pathobiology and prospects for therapy. J. Clin. Invest. In press.
    • (2002) J. Clin. Invest.
    • Lomas, D.1    Mahadeva, R.2
  • 30
    • 0022969885 scopus 로고
    • Speculations on the functions of the major heat shock and glucose-regulated proteins
    • Pelham, H.R. 1986. Speculations on the functions of the major heat shock and glucose-regulated proteins. Cell. 46:959-961.
    • (1986) Cell , vol.46 , pp. 959-961
    • Pelham, H.R.1
  • 31
    • 0032489016 scopus 로고    scopus 로고
    • The Hsp70 and Hsp60 chaperone machines
    • Bukau, B., and Horwich, A.L. 1998. The Hsp70 and Hsp60 chaperone machines. Cell. 92:351-366.
    • (1998) Cell , vol.92 , pp. 351-366
    • Bukau, B.1    Horwich, A.L.2
  • 32
    • 0024972083 scopus 로고
    • Mitochondrial heat-shock protein Hsp60 is essential for assembly of proteins imported into yeast mitochondria
    • Cheng, M.Y., et al. 1989. Mitochondrial heat-shock protein Hsp60 is essential for assembly of proteins imported into yeast mitochondria. Nature. 337:620-625.
    • (1989) Nature , vol.337 , pp. 620-625
    • Cheng, M.Y.1
  • 33
    • 0024820705 scopus 로고
    • Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and MgATP
    • Goloubinoff, P., Christeller, J.T., Gatenby, A.A., and Lorimer, G.H. 1989. Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and MgATP. Nature. 342:884-889.
    • (1989) Nature , vol.342 , pp. 884-889
    • Goloubinoff, P.1    Christeller, J.T.2    Gatenby, A.A.3    Lorimer, G.H.4
  • 34
    • 0026416043 scopus 로고
    • Chaperonin-mediated protein folding at the surface of groEL through a "molten globule"-like intermediate
    • Martin, J., et al. 1991. Chaperonin-mediated protein folding at the surface of groEL through a "molten globule"-like intermediate. Nature. 352:36-42.
    • (1991) Nature , vol.352 , pp. 36-42
    • Martin, J.1
  • 35
    • 0029087065 scopus 로고
    • Chaperonins can catalyze the reversal of early aggregations steps when a protein misfolds
    • Ranson, N.A., Dunster, N.J., Burston, S.G., and Clarke, A.R. 1995. Chaperonins can catalyze the reversal of early aggregations steps when a protein misfolds. J. Mol. Biol. 250:581-586.
    • (1995) J. Mol. Biol. , vol.250 , pp. 581-586
    • Ranson, N.A.1    Dunster, N.J.2    Burston, S.G.3    Clarke, A.R.4
  • 36
    • 0027943510 scopus 로고
    • The crystal structure of the bacterial chaperonin GroEL at 2.8 Å
    • Braig, K., et al. 1994. The crystal structure of the bacterial chaperonin GroEL at 2.8 Å. Nature. 371:578-586.
    • (1994) Nature , vol.371 , pp. 578-586
    • Braig, K.1
  • 38
    • 0030870719 scopus 로고    scopus 로고
    • The crystal structure of the asymmetric GroEL-GroES-(ADP)-chaperonin complex
    • Xu, Z., Horwich, A.L., and Sigler, P.B. 1997. The crystal structure of the asymmetric GroEL-GroES-(ADP)-chaperonin complex. Nature. 388:741-750.
    • (1997) Nature , vol.388 , pp. 741-750
    • Xu, Z.1    Horwich, A.L.2    Sigler, P.B.3
  • 39
    • 0028004372 scopus 로고
    • Selective in vivo rescue by GroEL-ES of thermolabile folding intermediate to phage P22 structural proteins
    • Gordon, C.L., Sather, S.K., Casjens, S., and King, J. 1994. Selective in vivo rescue by GroEL-ES of thermolabile folding intermediate to phage P22 structural proteins. J. Biol. Chem. 269:27941-27951.
    • (1994) J. Biol. Chem. , vol.269 , pp. 27941-27951
    • Gordon, C.L.1    Sather, S.K.2    Casjens, S.3    King, J.4
  • 40
    • 0032503968 scopus 로고    scopus 로고
    • Hsp104, Hsp70, and Hsp40: A novel chaperone system that rescues previously aggregated proteins
    • Glover, J.R., and Lindquist, S. 1998. Hsp104, Hsp70, and Hsp40: A novel chaperone system that rescues previously aggregated proteins. Cell. 94:73-82.
    • (1998) Cell , vol.94 , pp. 73-82
    • Glover, J.R.1    Lindquist, S.2
  • 41
    • 0027996115 scopus 로고
    • Protein disaggregation mediated by heat-shock protein Hsp104
    • Parsell, D.A., Kowal, A.S., Singer, M.A., and Lindquist, S. 1994. Protein disaggregation mediated by heat-shock protein Hsp104. Nature. 372:475-478.
    • (1994) Nature , vol.372 , pp. 475-478
    • Parsell, D.A.1    Kowal, A.S.2    Singer, M.A.3    Lindquist, S.4
  • 42
    • 0036853914 scopus 로고    scopus 로고
    • Orchestrating the unfolded protein response in health and disease
    • In press
    • Kaufman, R. 2002. Orchestrating the unfolded protein response in health and disease. J. Clin. Invest. In press.
    • (2002) J. Clin. Invest.
    • Kaufman, R.1
  • 43
    • 0034711439 scopus 로고    scopus 로고
    • Biochemical basis of oxidative protein folding in the endoplasmic reticulum
    • Tu, B.P., Ho-Schleyer, S.C., Travers, KJ., and Weissman, J.S. 2000. Biochemical basis of oxidative protein folding in the endoplasmic reticulum. Science. 290:1571-1574.
    • (2000) Science , vol.290 , pp. 1571-1574
    • Tu, B.P.1    Ho-Schleyer, S.C.2    Travers, K.J.3    Weissman, J.S.4
  • 44
    • 0035937408 scopus 로고    scopus 로고
    • Protein disulfide isomerase acts as a redox-dependent chaperone to unfold cholera toxin
    • Tsai, B., Rodighiero, C., Lencer, W.I., and Rapoport, T.A. 2001. Protein disulfide isomerase acts as a redox-dependent chaperone to unfold cholera toxin. Cell. 104:937-948.
    • (2001) Cell , vol.104 , pp. 937-948
    • Tsai, B.1    Rodighiero, C.2    Lencer, W.I.3    Rapoport, T.A.4
  • 45
    • 0035937505 scopus 로고    scopus 로고
    • Intracellular functions of N-linked glycans
    • Helenius, A., and Aebi, M. 2001. Intracellular functions of N-linked glycans. Science. 291:2364-2369.
    • (2001) Science , vol.291 , pp. 2364-2369
    • Helenius, A.1    Aebi, M.2
  • 46
    • 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
  • 47
    • 0014098295 scopus 로고
    • High-resolution electron microscopic analysis of the amyloid fibril
    • Shirahama, T., and Cohen, A.S. 1967. High-resolution electron microscopic analysis of the amyloid fibril. J. Cell Biol. 33:679-708.
    • (1967) J. Cell Biol. , vol.33 , pp. 679-708
    • Shirahama, T.1    Cohen, A.S.2
  • 48
    • 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
  • 49
    • 0014578835 scopus 로고
    • Characterization of the amyloid fibril as a cross-β protein
    • Bonar, L., Cohen, A.S., and Skinner, M.M. 1969. Characterization of the amyloid fibril as a cross-β 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
  • 51
    • 0019153066 scopus 로고
    • Amyloid deposits and amyloidosis: The β-fibrilloses
    • Glenner, G.G. 1980. Amyloid deposits and amyloidosis: The β-fibrilloses. N. Engl. J. Med. 302:1283-1292
    • (1980) N. Engl. J. Med. , vol.302 , pp. 1283-1292
    • Glenner, G.G.1
  • 52
    • 0029981197 scopus 로고    scopus 로고
    • Alternative conformations of amyloidogenic proteins govern their behaviour
    • Kelly, J.W. 1996. Alternative conformations of amyloidogenic proteins govern their behaviour. Curr. Opin. Struct. Biol. 6:11-17.
    • (1996) Curr. Opin. Struct. Biol. , vol.6 , pp. 11-17
    • Kelly, J.W.1
  • 53
    • 0035826234 scopus 로고    scopus 로고
    • Amyloid fibrils from muscle myloglobin
    • Fandrich, M., Fletcher, M.A., and Dobson, C.M. 2001. Amyloid fibrils from muscle myloglobin. Nature. 410:165-166.
    • (2001) Nature , vol.410 , pp. 165-166
    • Fandrich, M.1    Fletcher, M.A.2    Dobson, C.M.3
  • 54
    • 0033200063 scopus 로고    scopus 로고
    • Protein misfolding, evolution and disease
    • Dobson, C.M. 1999. Protein misfolding, evolution and disease. Trends Biochem. Sci. 24:329-332.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 329-332
    • Dobson, C.M.1
  • 55
    • 0030586945 scopus 로고    scopus 로고
    • Synchrotron X-ray studies suggest that the core of the transthyretin amyloid fibril is a continuous β-sheet helix
    • Blake, C., and Serpell, L. 1996. Synchrotron X-ray studies suggest that the core of the transthyretin amyloid fibril is a continuous β-sheet helix Structure. 4:989-998.
    • (1996) Structure , vol.4 , pp. 989-998
    • Blake, C.1    Serpell, L.2
  • 56
    • 0042847751 scopus 로고    scopus 로고
    • Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing
    • Jimenez, J.L., et al. 1999. Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing. EMBO J. 18:815-821.
    • (1999) EMBO J. , vol.18 , pp. 815-821
    • Jimenez, J.L.1
  • 57
    • 0030712145 scopus 로고    scopus 로고
    • Self-seeded fibers formed by Sup35, the protein determinant of [PS1], a heritable prion-like factor of S. cerevisiae
    • Glover, J.R., et al. 1997. Self-seeded fibers formed by Sup35, the protein determinant of [PS1], a heritable prion-like factor of S. cerevisiae. Cell. 89:811-819.
    • (1997) Cell , vol.89 , pp. 811-819
    • Glover, J.R.1
  • 58
    • 0028305304 scopus 로고
    • A role for destabilizing amino acid replacements in light-chain amyloidosis
    • Hurle, M.R., Helms, L.R., Li, L., Chan, W., and Wetzel, R. 1994. A role for destabilizing amino acid replacements in light-chain amyloidosis. Proc. Natl. Acad Sci. USA. 91:5446-5450.
    • (1994) Proc. Natl. Acad Sci. USA , vol.91 , pp. 5446-5450
    • Hurle, M.R.1    Helms, L.R.2    Li, L.3    Chan, W.4    Wetzel, R.5
  • 59
    • 0031056829 scopus 로고    scopus 로고
    • Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis
    • Booth, D.R., 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
  • 60
    • 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
  • 61
    • 0026675307 scopus 로고
    • Partial denaturation off transthyretin is sufficient for amyloid fibril formation in vitro
    • Colon, W., and Kelly, J.W. 1992. Partial denaturation off 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
  • 62
    • 0028839438 scopus 로고
    • Comparison of lethal and nonlethal transthyretin variants and their relationship to amyloid disease
    • McCutchen, S.L., Lai, Z., Miroy, G.J., Kelly, J.W., and Colon, W. 1995. Comparison of lethal and nonlethal transthyretin variants and their relationship to amyloid disease. Biochemistry. 34:13527-13536.
    • (1995) Biochemistry , vol.34 , pp. 13527-13536
    • McCutchen, S.L.1    Lai, Z.2    Miroy, G.J.3    Kelly, J.W.4    Colon, W.5
  • 63
    • 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
  • 64
    • 0035949432 scopus 로고    scopus 로고
    • An engineered transthyretin monomer that is nonamyloidogenic, unless it is partially denatured
    • Jiang, X., et al. 2001. An engineered transthyretin monomer that is nonamyloidogenic, unless it is partially denatured. Biochemistry. 40:11442-11452.
    • (2001) Biochemistry , vol.40 , pp. 11442-11452
    • Jiang, X.1
  • 65
    • 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
  • 66
    • 0035909981 scopus 로고    scopus 로고
    • The V122I cardiomyophathy variant of transthyretin increases the velocity of rate-limiting tetramer dissociation, resulting in accelerated amyloidosis
    • Jiang, X., Buxbaum, J.N., and Kelly, J.W. 2001. The V122I cardiomyophathy variant of transthyretin increases the velocity of rate-limiting tetramer dissociation, resulting in accelerated amyloidosis. Proc. Natl. Acad. Sci. USA. 98:14943-14948.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 14943-14948
    • Jiang, X.1    Buxbaum, J.N.2    Kelly, J.W.3
  • 67
    • 0032553530 scopus 로고    scopus 로고
    • Familial mutations and the thermodynamic stability of the recombinant human prion protein
    • Swietnicki, W., Petersen, R.B., Gambetti, P., and Surewicz, W.K. 1998. Familial mutations and the thermodynamic stability of the recombinant human prion protein. J. Biol. Chem. 273:31048-31052.
    • (1998) J. Biol. Chem. , vol.273 , pp. 31048-31052
    • Swietnicki, W.1    Petersen, R.B.2    Gambetti, P.3    Surewicz, W.K.4
  • 68
    • 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
  • 69
    • 0035827614 scopus 로고    scopus 로고
    • Folding of prion protein to its native alpha-helical conformation is under kinetic control
    • Baskakov, I.V., Legname, G., Prusiner, S.B., and Cohen, F.E. 2001. Folding of prion protein to its native alpha-helical conformation is under kinetic control. J. Biol. Chem. 276:19687-19690.
    • (2001) J. Biol. Chem. , vol.276 , pp. 19687-19690
    • Baskakov, I.V.1    Legname, G.2    Prusiner, S.B.3    Cohen, F.E.4
  • 70
    • 0030908095 scopus 로고    scopus 로고
    • Models of amyloid seeding in Alzheimer's disease and scrapie
    • Harper, J.D., and Lansbury, P.T. 1997. Models of amyloid seeding in Alzheimer's disease and scrapie. Annu. Rev. Biochem. 66:385-407.
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 385-407
    • Harper, J.D.1    Lansbury, P.T.2
  • 71
    • 0037041420 scopus 로고    scopus 로고
    • Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases
    • Bucciantini, M., Giannoni, E., Chiti, F., Baroni, F., and Formigli, L. 2002. Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases. Nature. 416:507-511.
    • (2002) Nature , vol.416 , pp. 507-511
    • Bucciantini, M.1    Giannoni, E.2    Chiti, F.3    Baroni, F.4    Formigli, L.5
  • 72
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid protein potently inhibit hippocampal long-term potentiation in vivo
    • Walsh, D.M., et al. 2002. Naturally secreted oligomers of amyloid protein potently inhibit hippocampal long-term potentiation in vivo. Nature. 416:535-539.
    • (2002) Nature , vol.416 , pp. 535-539
    • Walsh, D.M.1
  • 73
    • 0036166319 scopus 로고    scopus 로고
    • Kinetic partitioning of protein folding and aggregation
    • Chiti, F., et al. 2002. Kinetic partitioning of protein folding and aggregation. Nat. Struct. Biol. 9:137-143.
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 137-143
    • Chiti, F.1
  • 74
    • 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
  • 75
    • 0035947372 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system by protein aggregation
    • Bence, N.F., Sampat, R.M., and Kopito, R.R. 2001. Impairment of the ubiquitin-proteasome system by protein aggregation. Science. 292:1552-1555.
    • (2001) Science , vol.292 , pp. 1552-1555
    • Bence, N.F.1    Sampat, R.M.2    Kopito, R.R.3
  • 76
    • 0035902194 scopus 로고    scopus 로고
    • Shattuck lecture: Neurodegenerative diseases and prions
    • Prusiner, S.B. 2001. Shattuck lecture: Neurodegenerative diseases and prions. N. Engl. J. Med. 244:1516-1526.
    • (2001) N. Engl. J. Med. , vol.244 , pp. 1516-1526
    • Prusiner, S.B.1
  • 77
    • 0030447882 scopus 로고    scopus 로고
    • Inhibiting transthyretin amyloid fibril formation via protein stabilization
    • Miroy, G.J., et al. 1996. Inhibiting transthyretin amyloid fibril formation via protein stabilization. Proc. Natl. Acad. Sci. USA. 93:15051-15056.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 15051-15056
    • Miroy, G.J.1
  • 78
    • 0034127176 scopus 로고    scopus 로고
    • Rational design of potent human transthyretin amyloid disease inhibitors
    • Klabunde, T., et al. 2000. Rational design of potent human transthyretin amyloid disease inhibitors. Nat. Struct. Biol. 7:312-321.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 312-321
    • Klabunde, T.1
  • 79
    • 0035859806 scopus 로고    scopus 로고
    • Acridine and phenothiazine derivatives as pharmacotherapeutics for prion disease
    • Korth, C., May, B.C.H., Cohen, F.E., and Prusiner, S.B. 2001. Acridine and phenothiazine derivatives as pharmacotherapeutics for prion disease. Proc. Natl. Acad. Sci. USA. 98:9836-9841.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 9836-9841
    • Korth, C.1    May, B.C.H.2    Cohen, F.E.3    Prusiner, S.B.4
  • 80
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.