메뉴 건너뛰기




Volumn 426, Issue 6968, 2003, Pages 884-890

Protein folding and misfolding

Author keywords

[No Author keywords available]

Indexed keywords

AGGLOMERATION; AMINO ACIDS; CELLS; DISEASES; QUALITY CONTROL; SYNTHESIS (CHEMICAL);

EID: 0347357617     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/nature02261     Document Type: Review
Times cited : (4057)

References (71)
  • 1
    • 0043236283 scopus 로고    scopus 로고
    • Protein folding and misfolding: A paradigm of self-assembly and regulation in complex biogical systems
    • Vendruscolo, M., Zurdo, J., MacPhee, C. E. & Dobson, C. M. Protein folding and misfolding: a paradigm of self-assembly and regulation in complex biogical systems. Phil. Trans. R. Soc. Lond. 361, 1205-1222 (2003).
    • (2003) Phil. Trans. R. Soc. Lond. , vol.361 , pp. 1205-1222
    • Vendruscolo, M.1    Zurdo, J.2    MacPhee, C.E.3    Dobson, C.M.4
  • 2
    • 0033617266 scopus 로고    scopus 로고
    • From computer simulations to human disease: Emerging themes in protein folding
    • Radford, S. E. & Dobson, C. M. From computer simulations to human disease: emerging themes in protein folding. Cell 97, 291-298 (1999).
    • (1999) Cell , vol.97 , pp. 291-298
    • Radford, S.E.1    Dobson, C.M.2
  • 3
    • 0344301982 scopus 로고    scopus 로고
    • Protein folding: A perspective from theory and experiment
    • Dobson, C. M., Sali, A. & Karplus, M. Protein folding: a perspective from theory and experiment. Angew. Chem. Int. Ed. Eng. 37, 868-893 (1998).
    • (1998) Angew. Chem. Int. Ed. Eng. , vol.37 , pp. 868-893
    • Dobson, C.M.1    Sali, A.2    Karplus, M.3
  • 5
    • 1842298212 scopus 로고    scopus 로고
    • From Levinthal to pathways to funnels
    • Dill, K. A. & Chan, H. S. From Levinthal to pathways to funnels. Nature Struct. Biol. 4, 10-19 (1997).
    • (1997) Nature Struct. Biol. , vol.4 , pp. 10-19
    • Dill, K.A.1    Chan, H.S.2
  • 6
    • 0009586942 scopus 로고    scopus 로고
    • Understanding protein folding via free energy surfaces from theory and experiment
    • Dinner, A. R., Sali, A., Smith, L. J., Dobson, C. M. & Karplus, M. Understanding protein folding via free energy surfaces from theory and experiment. Trends Biochem. Sci. 25, 331-339 (2000).
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 331-339
    • Dinner, A.R.1    Sali, A.2    Smith, L.J.3    Dobson, C.M.4    Karplus, M.5
  • 7
    • 0028776642 scopus 로고
    • Protein folding: Matching speed and stability
    • Baldwin, R. L. Protein folding: matching speed and stability. Nature 369, 183-184 (1994).
    • (1994) Nature , vol.369 , pp. 183-184
    • Baldwin, R.L.1
  • 8
    • 0542397796 scopus 로고    scopus 로고
    • Kinetics and dynamics of loops, α-helices, β-hairpins, and fast-folding proteins
    • Eaton, W. A., Munoz, V., Thompson, P. A., Henry, E. R. & Hofrichter, J. Kinetics and dynamics of loops, α-helices, β-hairpins, and fast-folding proteins. Acc. Chem. Res. 31, 745-753 (1998).
    • (1998) Acc. Chem. Res. , vol.31 , pp. 745-753
    • Eaton, W.A.1    Munoz, V.2    Thompson, P.A.3    Henry, E.R.4    Hofrichter, J.5
  • 9
    • 0037038372 scopus 로고    scopus 로고
    • Absolute comparison of simulated and experimental protein-folding dynamics
    • Snow, C. D., Nguyen, H., Pande, V. S. & Gruebele, M. Absolute comparison of simulated and experimental protein-folding dynamics. Nature 420, 102-106 (2002).
    • (2002) Nature , vol.420 , pp. 102-106
    • Snow, C.D.1    Nguyen, H.2    Pande, V.S.3    Gruebele, M.4
  • 10
    • 0038329308 scopus 로고    scopus 로고
    • Folding at the speed limit
    • Yang, W. Y. & Gruebele, M. Folding at the speed limit. Nature 423, 193-197 (2003).
    • (2003) Nature , vol.423 , pp. 193-197
    • Yang, W.Y.1    Gruebele, M.2
  • 11
    • 0037456298 scopus 로고    scopus 로고
    • The complete folding pathway of a protein from nanoseconds to microseconds
    • Mayor, U. et al. The complete folding pathway of a protein from nanoseconds to microseconds. Nature 421, 863-867 (2003).
    • (2003) Nature , vol.421 , pp. 863-867
    • Mayor, U.1
  • 12
    • 0032502839 scopus 로고    scopus 로고
    • Contact order, transition state placement and the refolding rates of single domain proteins
    • Plaxco, K. W., Simons, K. T. & Baker, D. Contact order, transition state placement and the refolding rates of single domain proteins. J. Mol. Biol. 277, 985-994 (1998).
    • (1998) J. Mol. Biol. , vol.277 , pp. 985-994
    • Plaxco, K.W.1    Simons, K.T.2    Baker, D.3
  • 13
    • 0037126290 scopus 로고    scopus 로고
    • Probing the free-energy surface for protein folding with single-molecule fluorescence spectroscopy
    • Schuler, B., Lipman, E. A. & Eaton, W. A. Probing the free-energy surface for protein folding with single-molecule fluorescence spectroscopy. Nature 419, 743-747 (2002).
    • (2002) Nature , vol.419 , pp. 743-747
    • Schuler, B.1    Lipman, E.A.2    Eaton, W.A.3
  • 15
    • 0034652206 scopus 로고    scopus 로고
    • Transition-state structure as a unifying basis in protein-folding mechanisms: Contact order, chain topology, stability, and the extended nucleus mechanism
    • Fersht, A. R. Transition-state structure as a unifying basis in protein-folding mechanisms: contact order, chain topology, stability, and the extended nucleus mechanism. Proc. Natl Acad. Sci. USA 97, 1525-1529 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 1525-1529
    • Fersht, A.R.1
  • 16
    • 0034743155 scopus 로고    scopus 로고
    • From folding surfaces to folding proteins: A review and assessment of simulation studies of protein folding and unfolding
    • Shea, J. E. & Brooks, C. L. From folding surfaces to folding proteins: a review and assessment of simulation studies of protein folding and unfolding. Annu. Rev. Phys. Chem. 52, 499-535 (2001).
    • (2001) Annu. Rev. Phys. Chem. , vol.52 , pp. 499-535
    • Shea, J.E.1    Brooks, C.L.2
  • 17
    • 0037154980 scopus 로고    scopus 로고
    • Protein folding and unfolding at atomic resolution
    • Fersht, A. R. & Daggett, V. Protein folding and unfolding at atomic resolution. Cell 108, 573-582 (2002).
    • (2002) Cell , vol.108 , pp. 573-582
    • Fersht, A.R.1    Daggett, V.2
  • 18
    • 0035252350 scopus 로고    scopus 로고
    • Three key residues form a critical contact network in a transition state for protein folding
    • Vendruscolo, M., Paci, E., Dobson, C. M. & Karplus, M. Three key residues form a critical contact network in a transition state for protein folding. Nature 409, 641-646 (2001).
    • (2001) Nature , vol.409 , pp. 641-646
    • Vendruscolo, M.1    Paci, E.2    Dobson, C.M.3    Karplus, M.4
  • 19
    • 0037215268 scopus 로고    scopus 로고
    • The topomer search model: A simple, quantitative theory of two-state protein folding kinetics
    • Makarov, D. E. & Plaxco, K. W. The topomer search model: a simple, quantitative theory of two-state protein folding kinetics. Protein Sci. 12, 17-26 (2003).
    • (2003) Protein Sci. , vol.12 , pp. 17-26
    • Makarov, D.E.1    Plaxco, K.W.2
  • 20
    • 0034604105 scopus 로고    scopus 로고
    • A surprising simplicity to protein folding
    • Baker, D. A surprising simplicity to protein folding. Nature 405, 39-42 (2000).
    • (2000) Nature , vol.405 , pp. 39-42
    • Baker, D.1
  • 21
    • 0031055942 scopus 로고    scopus 로고
    • Kinetic role of early intermediates in protein folding
    • Roder, H. & Colon, W. Kinetic role of early intermediates in protein folding. Curr. Opin. Struct. Biol. 7, 15-28 (1997).
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 15-28
    • Roder, H.1    Colon, W.2
  • 22
    • 0037225280 scopus 로고    scopus 로고
    • Evidence for sequential barriers and obligatory intermediates in apparent two-state protein folding
    • Sanchez, I. E. & Kiefhaber, T. Evidence for sequential barriers and obligatory intermediates in apparent two-state protein folding. J. Mol. Biol. 325, 367-376 (2003).
    • (2003) J. Mol. Biol. , vol.325 , pp. 367-376
    • Sanchez, I.E.1    Kiefhaber, T.2
  • 24
    • 0345598912 scopus 로고    scopus 로고
    • Structures and relative free energies of partially folded states of proteins
    • Vendruscolo, M., Paci, E., Karplus, M. & Dobson, C. M. Structures and relative free energies of partially folded states of proteins. Proc. Natl Acad. Sci. USA 100, 14817-14821 (2003).
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 14817-14821
    • Vendruscolo, M.1    Paci, E.2    Karplus, M.3    Dobson, C.M.4
  • 25
    • 0037154268 scopus 로고    scopus 로고
    • Protein folding mediated by solvation: Water expulsion and formation of the hydrophobic core occur after the structural collapse
    • Cheung, M. S., Garcia, A. E. & Onuchic, J. N. Protein folding mediated by solvation: water expulsion and formation of the hydrophobic core occur after the structural collapse. Proc. Natl Acad. Sci. USA 99, 685-690 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 685-690
    • Cheung, M.S.1    Garcia, A.E.2    Onuchic, J.N.3
  • 27
    • 0032489016 scopus 로고    scopus 로고
    • The Hsp70 and Hsp60 chaperone machines
    • Bukau, B. & Horwich, A. L. The Hsp70 and Hsp60 chaperone machines. Cell 92, 351-366 (1998).
    • (1998) Cell , vol.92 , pp. 351-366
    • Bukau, B.1    Horwich, A.L.2
  • 28
    • 0037040541 scopus 로고    scopus 로고
    • Molecular chaperones in the cytosol: From nascent chain to folded protein
    • Hartl, F. U. & Hayer-Hartl, M. Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 295, 1852-1858 (2002).
    • (2002) Science , vol.295 , pp. 1852-1858
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 29
    • 0035253217 scopus 로고    scopus 로고
    • Macromolecular crowding: An important but neglected aspect of the intra cellular environment
    • Ellis, R. J. Macromolecular crowding: an important but neglected aspect of the intracellular environment. Curr. Opin. Struct. Biol. 11, 114-119 (2001).
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 114-119
    • Ellis, R.J.1
  • 30
    • 0033952307 scopus 로고    scopus 로고
    • Enzymes that catalyse the restructuring of proteins
    • Schiene, C. & Fischer, G. Enzymes that catalyse the restructuring of proteins. Curr. Opin. Struct. Biol. 10, 4O-45 (2000).
    • (2000) Curr. Opin. Struct. Biol. , vol.10
    • Schiene, C.1    Fischer, G.2
  • 31
    • 0029094253 scopus 로고
    • Quality control in the secretory pathway
    • Hammon, C. & Helenius, A. Quality control in the secretory pathway. Curr. Opin. Cell. Biol. 7, 523-529 (1995).
    • (1995) Curr. Opin. Cell. Biol. , vol.7 , pp. 523-529
    • Hammon, C.1    Helenius, A.2
  • 32
    • 0036086064 scopus 로고    scopus 로고
    • The unfolded protein response in nutrient sensing and differentiation
    • Kaufman, R. J. et al. The unfolded protein response in nutrient sensing and differentiation. Nature Rev. Mol. Cell Biol. 3, 411-421 (2002).
    • (2002) Nature Rev. Mol. Cell Biol. , vol.3 , pp. 411-421
    • Kaufman, R.J.1
  • 34
    • 0034643336 scopus 로고    scopus 로고
    • Rapid degradation of a large fraction of newly synthesized proteins by proteasomes
    • Schubert, U. et al. Rapid degradation of a large fraction of newly synthesized proteins by proteasomes. Nature 404, 770-774 (2000).
    • (2000) Nature , vol.404 , pp. 770-774
    • Schubert, U.1
  • 35
    • 0035947372 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system by protein aggregation
    • Bence, N. F., Sampat, R. M. & Kopito, R. R. Impairment of the ubiquitin-proteasome system by protein aggregation. Science 292, 1552-1555 (2001).
    • (2001) Science , vol.292 , pp. 1552-1555
    • Bence, N.F.1    Sampat, R.M.2    Kopito, R.R.3
  • 36
    • 0028856292 scopus 로고
    • Defective protein folding as a basis of human disease
    • Thomas, P. J., Qu, B. H. & Pedersen, P. L. Defective protein folding as a basis of human disease. Trends Biochem. Sci. 20, 456-459 (1995).
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 456-459
    • Thomas, P.J.1    Qu, B.H.2    Pedersen, P.L.3
  • 37
    • 0035961329 scopus 로고    scopus 로고
    • The structural basis of protein folding and its links with human disease
    • Dobson, C. M. The structural basis of protein folding and its links with human disease. Phil. Trans. R. Soc. Lond. B356, 133-145 (2001).
    • (2001) Phil. Trans. R. Soc. Lond. B , vol.356 , pp. 133-145
    • Dobson, C.M.1
  • 38
    • 0036841958 scopus 로고    scopus 로고
    • Protein aggregation in disease: A role for folding intermediates forming specific multimeric interactions
    • Horwich, A. Protein aggregation in disease: a role for folding intermediates forming specific multimeric interactions. J. Clin. Invest. 110, 1221-1232 (2002).
    • (2002) J. Clin. Invest. , vol.110 , pp. 1221-1232
    • Horwich, A.1
  • 39
    • 0035496607 scopus 로고    scopus 로고
    • Rescuing the functions of mutant p53
    • Bullock, A. N. & Fersht, A. R. Rescuing the functions of mutant p53. Nature Rev. Cancer 1, 68-76 (2001).
    • (2001) Nature Rev. Cancer , vol.1 , pp. 68-76
    • Bullock, A.N.1    Fersht, A.R.2
  • 41
    • 0032006678 scopus 로고    scopus 로고
    • Alternative conformation of amyloidogenic proteins and their multi-step assembly pathways
    • Kelly, J. W. Alternative conformation of amyloidogenic proteins and their multi-step assembly pathways. Curr. Opin. Struct. Biol. 8, 101-106 (1998).
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 101-106
    • Kelly, J.W.1
  • 42
    • 0030801746 scopus 로고    scopus 로고
    • The structure of amyloid fibrils by electron microscopy and X-ray diffraction
    • Sunde, M. & Blake, C. C. F. The structure of amyloid fibrils by electron microscopy and X-ray diffraction. Adv. Protein Chem. 50, 123-159 (1997).
    • (1997) Adv. Protein Chem. , vol.50 , pp. 123-159
    • Sunde, M.1    Blake, C.C.F.2
  • 43
    • 0033200063 scopus 로고    scopus 로고
    • Protein misfolding, evolution and disease
    • Dobson, C. M. Protein misfolding, evolution and disease. Trends Biochem. Sci. 24, 329-332 (1999).
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 329-332
    • Dobson, C.M.1
  • 44
    • 0036845354 scopus 로고    scopus 로고
    • The behaviour of polyamino acids reveals an inverse side-chain effect in amyloid structure formation
    • Fändrich, M. & Dobson, C. M. The behaviour of polyamino acids reveals an inverse side-chain effect in amyloid structure formation. EMBO J. 21, 5682-5690 (2002).
    • (2002) EMBO J. , vol.21 , pp. 5682-5690
    • Fändrich, M.1    Dobson, C.M.2
  • 45
    • 0042847751 scopus 로고    scopus 로고
    • Cryo-electron microscopy of an SH3 amyloid fibril and model of the molecular packing
    • Jiménez, J. L. et al. Cryo-electron microscopy of an SH3 amyloid fibril and model of the molecular packing. EMBO J. 18, 815-821 (1999).
    • (1999) EMBO J. , vol.18 , pp. 815-821
    • Jiménez, J.L.1
  • 46
    • 0037168655 scopus 로고    scopus 로고
    • A structural model for Alzheimer's β-amyloid fibrils based on experimental constraints from solid state NMR
    • Petkova, A. T. et al. A structural model for Alzheimer's β-amyloid fibrils based on experimental constraints from solid state NMR. Proc. Natl Acad. Sci. USA 99, 16742-16747 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 16742-16747
    • Petkova, A.T.1
  • 47
    • 0042467550 scopus 로고    scopus 로고
    • Rationalization of mutational effects on protein aggregation rates
    • Chiti, F., Stefani, M., Taddei, N., Ramponi, G. & Dobson, C. M. Rationalization of mutational effects on protein aggregation rates. Nature 424, 805-808 (2003).
    • (2003) Nature , vol.424 , pp. 805-808
    • Chiti, F.1    Stefani, M.2    Taddei, N.3    Ramponi, G.4    Dobson, C.M.5
  • 48
    • 0037551741 scopus 로고    scopus 로고
    • Protofibrils, pores, fibrils, and neurode generation: Separating the responsible protein aggregates from the innocent bystanders
    • Caughey, B. & Lansbury, P. T. Jr. Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders. Annu. Rev. Neurosci. 26, 267-298 (2003).
    • (2003) Annu. Rev. Neurosci. , vol.26 , pp. 267-298
    • Caughey, B.1    Lansbury Jr., P.T.2
  • 49
    • 0037422540 scopus 로고    scopus 로고
    • Amyloid β-protein (Aβ) assembly: Aβ40 and Aβ42 oligomerize through distinct pathways
    • Bitan, G. et al. Amyloid β-protein (Aβ) assembly: Aβ40 and Aβ42 oligomerize through distinct pathways. Proc. Natl Acad. Sci. USA 100, 330-335 (2003).
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 330-335
    • Bitan, G.1
  • 50
    • 0036145439 scopus 로고    scopus 로고
    • Low levels of asparagine deamidation can have a dramatic effect on aggregation of amyloidogenic peptides: Implications for the study of amyloid formation
    • Nilsson, M. R., Driscoll, M. & Raleigh, D. P. Low levels of asparagine deamidation can have a dramatic effect on aggregation of amyloidogenic peptides: implications for the study of amyloid formation. Protein Sci. 11, 342-349 (2002).
    • (2002) Protein Sci. , vol.11 , pp. 342-349
    • Nilsson, M.R.1    Driscoll, M.2    Raleigh, D.P.3
  • 51
    • 0030770294 scopus 로고    scopus 로고
    • Oligomer formation by 3D domain swapping: A model for protein assembly and misassembly
    • Schlunegger, M. P., Bennett, M. J. & Eisenberg, D. Oligomer formation by 3D domain swapping: a model for protein assembly and misassembly. Adv. Protein Chem. 50, 50, 61-122 (1997).
    • (1997) Adv. Protein Chem. , vol.50 , Issue.50 , pp. 61-122
    • Schlunegger, M.P.1    Bennett, M.J.2    Eisenberg, D.3
  • 52
    • 0037041420 scopus 로고    scopus 로고
    • Inherent cytotoxicity of aggregates implies a common origin for protein misfolding diseases
    • Bucciantini, M. et al. Inherent cytotoxicity of aggregates implies a common origin for protein misfolding diseases. Nature 416, 507-511 (2002).
    • (2002) Nature , vol.416 , pp. 507-511
    • Bucciantini, M.1
  • 53
    • 0037130174 scopus 로고    scopus 로고
    • Neurodegenerative disease: Amyloid pores from pathogenic mutations
    • Lashuet, H. A., Hartley, D., Petre, B. M., Walz, T. & Lansbury, P. T. Jr. Neurodegenerative disease: amyloid pores from pathogenic mutations. Nature 418, 291 (2002).
    • (2002) Nature , vol.418 , pp. 291
    • Lashuet, H.A.1    Hartley, D.2    Petre, B.M.3    Walz, T.4    Lansbury Jr., P.T.5
  • 54
    • 0037317334 scopus 로고    scopus 로고
    • Protein folding and disease: A view from the First Horizon Symposium
    • Dobson, C. M. Protein folding and disease: a view from the First Horizon Symposium. Nature Rev. Drug Discov. 2, 154-160 (2003).
    • (2003) Nature Rev. Drug Discov. , vol.2 , pp. 154-160
    • Dobson, C.M.1
  • 55
    • 0034727077 scopus 로고    scopus 로고
    • A yeast prion provides a mechanism for genetic variation and phenotypic diversity
    • True, H. L. & Lindquist, S. L. A yeast prion provides a mechanism for genetic variation and phenotypic diversity. Nature 407, 477-483 (2000).
    • (2000) Nature , vol.407 , pp. 477-483
    • True, H.L.1    Lindquist, S.L.2
  • 56
    • 0036468673 scopus 로고    scopus 로고
    • Role of escherichia coli curli operons in directing amyloid fiber formation
    • Chapman, M. R. et al. Role of escherichia coli curli operons in directing amyloid fiber formation. Science 295, 851-855 (2002).
    • (2002) Science , vol.295 , pp. 851-855
    • Chapman, M.R.1
  • 57
    • 0038612852 scopus 로고    scopus 로고
    • Amyloid as a natural product
    • Kelly, J. W. & Balch, W. E. Amyloid as a natural product. J. Cell Biol. 161, 461-462 (2003).
    • (2003) J. Cell Biol. , vol.161 , pp. 461-462
    • Kelly, J.W.1    Balch, W.E.2
  • 58
    • 0034598954 scopus 로고    scopus 로고
    • Nature disfavours sequences of alternating polar and non-polar amino acids: Implications for amyloidogenesis
    • Broome, B. M. & Hecht, M. H. Nature disfavours sequences of alternating polar and non-polar amino acids: implications for amyloidogenesis. J. Mol. Biol. 296, 961-968 (2000).
    • (2000) J. Mol. Biol. , vol.296 , pp. 961-968
    • Broome, B.M.1    Hecht, M.H.2
  • 59
    • 0036166319 scopus 로고    scopus 로고
    • Kinetic partitioning of protein folding and aggregation
    • Chiti, F. et al. Kinetic partitioning of protein folding and aggregation. Nature Struct. Biol. 9, 137-143 (2002).
    • (2002) Nature Struct. Biol. , vol.9 , pp. 137-143
    • Chiti, F.1
  • 60
    • 0036549108 scopus 로고    scopus 로고
    • Sick chaperones and ageing: A perspective
    • Macario, A. J. L. & Macario, E. C. Sick chaperones and ageing: a perspective. Ageing Res. Rev. 1, 295-311 (2002).
    • (2002) Ageing Res. Rev. , vol.1 , pp. 295-311
    • Macario, A.J.L.1    Macario, E.C.2
  • 61
    • 0034255027 scopus 로고    scopus 로고
    • A systematic exploration of the influence of the protein stability on amyloid fibril formation in vitro
    • Ramirez-Alvarado, M., Merkel, J. S. & Regan, L. A systematic exploration of the influence of the protein stability on amyloid fibril formation in vitro. Proc. Natl Acad. Sci. USA 97, 8979-8984 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 8979-8984
    • Ramirez-Alvarado, M.1    Merkel, J.S.2    Regan, L.3
  • 62
    • 0042467574 scopus 로고    scopus 로고
    • A camelid antibody fragment inhibits amyloid fibril formation by human lysozyme
    • Dumoulin, M. et al. A camelid antibody fragment inhibits amyloid fibril formation by human lysozyme. Nature 424, 783-788 (2003).
    • (2003) Nature , vol.424 , pp. 783-788
    • Dumoulin, M.1
  • 63
    • 0030822582 scopus 로고    scopus 로고
    • Prion diseases and the BSE crisis
    • Prusiner S. B. Prion diseases and the BSE crisis. Science 278, 245-251 (1997).
    • (1997) Science , vol.278 , pp. 245-251
    • Prusiner, S.B.1
  • 64
    • 0037077040 scopus 로고    scopus 로고
    • Toxic proteins in neurodegenerative disease
    • Taylor, J. P., Hardy, J. & Fischbeck, K. H. Toxic proteins in neurodegenerative disease. Science 296, 1991-1995 (2002).
    • (2002) Science , vol.296 , pp. 1991-1995
    • Taylor, J.P.1    Hardy, J.2    Fischbeck, K.H.3
  • 65
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo
    • Walsh, D. M. et al. Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo. Nature 416, 535-539 (2002).
    • (2002) Nature , vol.416 , pp. 535-539
    • Walsh, D.M.1
  • 66
    • 0242668337 scopus 로고    scopus 로고
    • Common structure of soluble amyloid oligomers implies common mechanisms of pathogenesis
    • Kayed, R. et al. Common structure of soluble amyloid oligomers implies common mechanisms of pathogenesis. Science 300, 486-489 (2003).
    • (2003) Science , vol.300 , pp. 486-489
    • Kayed, R.1
  • 67
    • 0344944630 scopus 로고    scopus 로고
    • Protein aggregation and aggregate toxicity: New insights into protein folding, misfolding diseases and biological evolution
    • Stefani, M. & Dobson, C. M. Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution. J. Mol. 81, 678-699 (2003).
    • (2003) J. Mol. , vol.81 , pp. 678-699
    • Stefani, M.1    Dobson, C.M.2
  • 68
    • 0035139109 scopus 로고    scopus 로고
    • Cellular defenses against unfolded proteins: A cell biologist thinks about neurodegenerative diseases
    • Sherman, M. Y. & Goldberg, A. L. Cellular defenses against unfolded proteins: a cell biologist thinks about neurodegenerative diseases. Neuron 29, 15-32 (2001).
    • (2001) Neuron , vol.29 , pp. 15-32
    • Sherman, M.Y.1    Goldberg, A.L.2
  • 69
    • 0034608868 scopus 로고    scopus 로고
    • Hsp70 and Hsp40 chaperones can can inhibit self-assembly of polyglutamine proteins into amyloid-like fibrils
    • Muchowski, P. J. et al. Hsp70 and Hsp40 chaperones can can inhibit self-assembly of polyglutamine proteins into amyloid-like fibrils. Proc. Natl Acad. Sci. USA 97, 7841-7846 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 7841-7846
    • Muchowski, P.J.1
  • 70
    • 0035576876 scopus 로고    scopus 로고
    • Chaperone overload is a possible contributor to 'civilization diseases'
    • Cserniely, P. Chaperone overload is a possible contributor to 'civilization diseases'. Trends Genet. 17, 701-704 (2001).
    • (2001) Trends Genet. , vol.17 , pp. 701-704
    • Cserniely, P.1
  • 71
    • 0037102362 scopus 로고    scopus 로고
    • Getting out of shape-protein misfolding diseases
    • Dobson, C. M. Getting out of shape-protein misfolding diseases. Nature 418, 729-730 (2002).
    • (2002) Nature , vol.418 , pp. 729-730
    • Dobson, C.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.