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Volumn 3, Issue 10, 2002, Pages 759-768

Serpinopathies and the conformational dementias

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA 1 ANTITRYPSIN; ALPHA SYNUCLEIN; AMYLOID BETA PROTEIN; CHAPERONE; DOPAMINE; HUNTINGTIN; POLYMER; PRION PROTEIN; SERINE PROTEINASE INHIBITOR; TAU PROTEIN;

EID: 0036789017     PISSN: 14710056     EISSN: None     Source Type: Journal    
DOI: 10.1038/nrg907     Document Type: Review
Times cited : (204)

References (100)
  • 1
    • 0030841343 scopus 로고    scopus 로고
    • Conformational diseases
    • Carrell, R. W. & Lomas, D. A. Conformational diseases. Lancet 350, 134-138 (1997).
    • (1997) Lancet , vol.350 , pp. 134-138
    • Carrell, R.W.1    Lomas, D.A.2
  • 3
    • 0037011795 scopus 로고    scopus 로고
    • α-antitrypsin deficiency: A model for canformational diseases
    • Carrell, R. W. & Lomas, D. A. α-antitrypsin deficiency: a model for canformational diseases. N. Engl. J. Med. 346, 45-53 (2002).
    • (2002) N. Engl. J. Med. , vol.346 , pp. 45-53
    • Carrell, R.W.1    Lomas, D.A.2
  • 4
    • 0033134869 scopus 로고    scopus 로고
    • Aggregates in neurodegenerative disease: Crowds and power?
    • Tran, P. B. & Miller, R. J. Aggregates in neurodegenerative disease: crowds and power? Trends Neurosci. 22, 194-197 (1999).
    • (1999) Trends Neurosci. , vol.22 , pp. 194-197
    • Tran, P.B.1    Miller, R.J.2
  • 5
  • 6
    • 0034687422 scopus 로고    scopus 로고
    • Structure of a serpin-protease complex shows inhibition by deformation
    • The long-sought-after structure of the final complex of a serpin with its target proteinase.
    • Huntington, J. A., Read, R. J. & Carrell, R. W. Structure of a serpin-protease complex shows inhibition by deformation. Nature 407, 923-926 (2000). The long-sought-after structure of the final complex of a serpin with its target proteinase.
    • (2000) Nature , vol.407 , pp. 923-926
    • Huntington, J.A.1    Read, R.J.2    Carrell, R.W.3
  • 7
    • 0025828198 scopus 로고
    • Analysis of the plasma elimination kinetics and conformational stabilities of native, proteinase-complexed, and reactive site cleaved serpins: Comparison of α-proteinase inhibitor, α-antichymotrypsin, antithrombin III, α-antiplasmin, angiotensinogen, and ovalbumin
    • Mast, A. E., Enghild, J. J., Pizzo, S. V. & Salvesen, G. Analysis of the plasma elimination kinetics and conformational stabilities of native, proteinase-complexed, and reactive site cleaved serpins: comparison of α-proteinase inhibitor, α-antichymotrypsin, antithrombin III, α-antiplasmin, angiotensinogen, and ovalbumin. Biochemistry 30, 1729-1730 (1991).
    • (1991) Biochemistry , vol.30 , pp. 1729-1730
    • Mast, A.E.1    Enghild, J.J.2    Pizzo, S.V.3    Salvesen, G.4
  • 8
    • 0026755363 scopus 로고
    • 1-antitrypsin accumulation in the liver
    • 1-antitrypsin accumulates in the liver by loop-sheet polymerization.
    • 1-antitrypsin accumulates in the liver by loop-sheet polymerization.
    • (1992) Nature , vol.357 , pp. 605-607
    • Lomas, D.A.1    Evans, D.L.2    Finch, J.T.3    Carrell, R.W.4
  • 9
    • 0029589824 scopus 로고
    • What do dysfunctional serpins tell us about molecular mobility and disease?
    • Stein, P. E. & Carrell, R. W. What do dysfunctional serpins tell us about molecular mobility and disease? Nature Struct. Biol. 2, 96-113 (1995).
    • (1995) Nature Struct. Biol. , vol.2 , pp. 96-113
    • Stein, P.E.1    Carrell, R.W.2
  • 11
    • 0023898432 scopus 로고
    • Molecular basis of α1-antitrypsin deficiency
    • Brantly, M., Nukiwa, T. & Crystal, R. G. Molecular basis of α1-antitrypsin deficiency. Am. J. Med. 84 (Suppl. 6A), 13-31 (1988).
    • (1988) Am. J. Med. , vol.84 , Issue.SUPPL. 6A , pp. 13-31
    • Brantly, M.1    Nukiwa, T.2    Crystal, R.G.3
  • 12
    • 0034918677 scopus 로고    scopus 로고
    • 1-Antitrypsin PI phenotypes S and Z in Europe: An analysis of the published surveys
    • 1-Antitrypsin PI phenotypes S and Z in Europe: an analysis of the published surveys. Clin. Genet. 60, 31-41 (2001).
    • (2001) Clin. Genet. , vol.60 , pp. 31-41
    • Blanco, I.1    Fernández, E.2    Bustillo, E.F.3
  • 13
    • 0014530551 scopus 로고
    • Cirrhosis associated with α1-antitrypsin deficiency: A previously unrecognised inherited disorder
    • Sharp, H. L., Bridges, R. A., Krivit, W. & Freier, E. F. Cirrhosis associated with α1-antitrypsin deficiency: a previously unrecognised inherited disorder. J. Lab. Clin. Med. 73, 934-939 (1969).
    • (1969) J. Lab. Clin. Med. , vol.73 , pp. 934-939
    • Sharp, H.L.1    Bridges, R.A.2    Krivit, W.3    Freier, E.F.4
  • 14
    • 0024238708 scopus 로고
    • 1-antitrypsin deficient children
    • 1-antitrypsin deficient children. Acta Paediatr. Scand. 77, 847-851 (1988).
    • (1988) Acta Paediatr. Scand. , vol.77 , pp. 847-851
    • Sveger, T.1
  • 16
    • 0019978932 scopus 로고
    • 1-antitrypsin
    • 1-antitrypsin. Nature 298, 329-334 (1982).
    • (1982) Nature , vol.298 , pp. 329-334
    • Carrell, R.W.1
  • 17
    • 0018128288 scopus 로고
    • 1-antitrypsin deficiency, PiZ
    • 1-antitrypsin deficiency, PiZ. Acta Med. Scand. 204, 345-351 (1978).
    • (1978) Acta Med. Scand. , vol.204 , pp. 345-351
    • Larsson, C.1
  • 20
    • 0034602778 scopus 로고    scopus 로고
    • 1-antichymotrypsin indicates two stage insertion of the reactive loop; implications for inhibitory function and conformational disease
    • 1-antichymotrypsin indicates two stage insertion of the reactive loop; implications for inhibitory function and conformational disease. Proc. Natl Acad. Sci. USA 97, 67-72 (2000).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 67-72
    • Gooptu, B.1
  • 21
    • 0036510604 scopus 로고    scopus 로고
    • Six-mer peptide selectively anneals to a pathogenic serpin conformation and blocks polymerisation: Implications for the prevention of Z a-antitrypsin related cirrhosis
    • Mahadeva, R., Dafforn, T. R., Carrell, R. W. & Lomas, D. A. Six-mer peptide selectively anneals to a pathogenic serpin conformation and blocks polymerisation: implications for the prevention of Z a-antitrypsin related cirrhosis. J. Biol. Chem. 277, 6771-6774 (2002).]
    • (2002) J. Biol. Chem. , vol.277 , pp. 6771-6774
    • Mahadeva, R.1    Dafforn, T.R.2    Carrell, R.W.3    Lomas, D.A.4
  • 23
    • 0025258970 scopus 로고
    • 1-antitrypsin within the hepatic endoplasmic reticulum does not elevate the steady-state level of grp78/BiP
    • 1-antitrypsin within the hepatic endoplasmic reticulum does not elevate the steady-state level of grp78/BiP. J. Biol. Chem. 265, 20463-20468 (1990).
    • (1990) J. Biol. Chem. , vol.265 , pp. 20463-20468
    • Graham, K.S.1    Le, A.2    Sifers, R.N.3
  • 24
    • 0037135563 scopus 로고    scopus 로고
    • Detection of circulating and endothelial cell polymers of Z and wildtype α1-antitrypsin by a monoclonal antibody
    • Janciauskiene, S., Dominaitiene, R., Sternby, N. H., Piitulainen, E. & Eriksson, S. Detection of circulating and endothelial cell polymers of Z and wildtype α1-antitrypsin by a monoclonal antibody. J. Biol. Chem. 277, 26540-26546 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 26540-26546
    • Janciauskiene, S.1    Dominaitiene, R.2    Sternby, N.H.3    Piitulainen, E.4    Eriksson, S.5
  • 26
    • 0032538299 scopus 로고    scopus 로고
    • Implications for function and therapy of a 2.9Å structure of binary-complexed antithrombin
    • Skinner, R. et al. Implications for function and therapy of a 2.9Å structure of binary-complexed antithrombin. J. Mol. Biol. 283, 9-14 (1998).
    • (1998) J. Mol. Biol. , vol.283 , pp. 9-14
    • Skinner, R.1
  • 27
    • 0026570248 scopus 로고
    • Soluble aggregates of the human PiZ α- antitrypsin variant are degraded within the endoplasmic reticulum by a mechanism sensitive to inhibitors of protein synthesis
    • Le, A., Ferrell, G. A., Dishon, D. S., Quyen-Quyen, A. L. & Sifers, R. N. Soluble aggregates of the human PiZ α- antitrypsin variant are degraded within the endoplasmic reticulum by a mechanism sensitive to inhibitors of protein synthesis. J. Biol. Chem. 287, 1072-1080 (1992).
    • (1992) J. Biol. Chem. , vol.287 , pp. 1072-1080
    • Le, A.1    Ferrell, G.A.2    Dishon, D.S.3    Quyen-Quyen, A.L.4    Sifers, R.N.5
  • 29
    • 0028593988 scopus 로고
    • 1-antitrypsin correlates with liver disease phenotype in homozygous PiZZ α-antitrypsin deficiency
    • 1-antitrypsin-related liver disease (as opposed to those with plasma deficiency) have a lag in degrading the retained protein, which indicates that the handling of the polymers is likely to be important in determining which patients develop juvenile cirrhosis
    • 1-antitrypsin-related liver disease (as opposed to those with plasma deficiency) have a lag in degrading the retained protein, which indicates that the handling of the polymers is likely to be important in determining which patients develop juvenile cirrhosis.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 9014-9018
    • Wu, Y.1
  • 31
    • 0027999955 scopus 로고
    • Thromboembolic disease due to thermolabile conformational changes of antithrombin Rouen VI (187 Asn→Asp)
    • Bruce, D., Perry, D. J., Borg, J.-Y., Carrell, R. W. & Wardell, M. R. Thromboembolic disease due to thermolabile conformational changes of antithrombin Rouen VI (187 Asn→Asp). J. Clin. Invest. 94, 2265-2274 (1994).
    • (1994) J. Clin. Invest. , vol.94 , pp. 2265-2274
    • Bruce, D.1    Perry, D.J.2    Borg, J.-Y.3    Carrell, R.W.4    Wardell, M.R.5
  • 32
    • 0032532347 scopus 로고    scopus 로고
    • Antithrombins wibble and wobble (T85M/K): Archetypal conformational diseases with in vivo latent-transition, thrombosis and heparin activation
    • Beauchamp, N. J. et al. Antithrombins wibble and wobble (T85M/K): archetypal conformational diseases with in vivo latent-transition, thrombosis and heparin activation. Blood 92, 2696-2706 (1998).
    • (1998) Blood , vol.92 , pp. 2696-2706
    • Beauchamp, N.J.1
  • 33
    • 0033570979 scopus 로고    scopus 로고
    • Formation of the antithrombin heterodimer and the onset of thrombosis
    • Zhou, A., Huntington, J. A. & Carrell, R. W. Formation of the antithrombin heterodimer and the onset of thrombosis. Blood 94, 3388-3396 (1999).
    • (1999) Blood , vol.94 , pp. 3388-3396
    • Zhou, A.1    Huntington, J.A.2    Carrell, R.W.3
  • 34
    • 0003228455 scopus 로고    scopus 로고
    • Molecular characterization of the first homozygous heparin co-factor II deficiency. Involvement in conformational disease
    • Corral, J. at al. Molecular characterization of the first homozygous heparin co-factor II deficiency. Involvement in conformational disease. Thrombosis Haemostasis (Suppl.) (2001).
    • (2001) Thrombosis Haemostasis , Issue.SUPPL.
    • Corral, J.1
  • 35
    • 0033578917 scopus 로고    scopus 로고
    • Constitutive activation of toll-mediated antifungal defense in serpin-deficient Drosophila
    • Levashina, E. A. et al. Constitutive activation of toll-mediated antifungal defense in serpin-deficient Drosophila. Science 285, 1917-1919 (1999).
    • (1999) Science , vol.285 , pp. 1917-1919
    • Levashina, E.A.1
  • 36
    • 0025923680 scopus 로고
    • Siiyama(serine 53 (TCC) tophenylaianine 53 (TTC)). A new α1-antitrypsin-deficient variant with mutation on a predicted conserved residue of the serpin backbone
    • Seyama, K. et al. Siiyama(serine 53 (TCC) tophenylaianine 53 (TTC)). A new α1-antitrypsin-deficient variant with mutation on a predicted conserved residue of the serpin backbone. J. Biol Chem. 266, 12627-12632 (1991).
    • (1991) J. Biol Chem. , vol.266 , pp. 12627-12632
    • Seyama, K.1
  • 37
    • 0021151426 scopus 로고
    • Occurrence of α1-antitrypsin deficiency in 155 patients with alcoholic liver disease
    • Roberts, E. A., Cox, D. W., Medline, A. & Wanless, I. R. Occurrence of α1-antitrypsin deficiency in 155 patients with alcoholic liver disease. Am. J. Clin. Pathol. 82, 424-427 (1984).
    • (1984) Am. J. Clin. Pathol. , vol.82 , pp. 424-427
    • Roberts, E.A.1    Cox, D.W.2    Medline, A.3    Wanless, I.R.4
  • 40
    • 0029012309 scopus 로고
    • 53Phe deleted) forms loop-sheet polymers in vivo: Evidence for the C sheet mechanism of polymerisation
    • 53Phe deleted) forms loop-sheet polymers in vivo: evidence for the C sheet mechanism of polymerisation. J. Biol. Chem. 270, 16864-16870 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 16864-16870
    • Lomas, D.A.1
  • 41
    • 0028092121 scopus 로고
    • Three novel missense mutations in the antithrombin III (AT3) gene causing recurrent venous thrombosis
    • Millar, D. S. et al. Three novel missense mutations in the antithrombin III (AT3) gene causing recurrent venous thrombosis. Hum. Genet. 94, 509-512 (1994).
    • (1994) Hum. Genet. , vol.94 , pp. 509-512
    • Millar, D.S.1
  • 42
    • 0027923966 scopus 로고
    • 436φThr) results in nonsubstrate-like behavior and in polymerization of the molecule
    • 436φThr) results in nonsubstrate-like behavior and in polymerization of the molecule. J. Biol. Chem. 268, 18088-18094 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 18088-18094
    • Aulak, K.S.1
  • 43
    • 0028855465 scopus 로고
    • COOH-terminal substitutions in the serpin C1 inhibitor that cause loop overinsertion and subsequent multimerization
    • Elderng, E., Verpy, E., Roem, D., Meo, T. & Tosi, M. COOH-terminal substitutions in the serpin C1 inhibitor that cause loop overinsertion and subsequent multimerization. J. Biol. Chem. 270, 2579-2587 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 2579-2587
    • Elderng, E.1    Verpy, E.2    Roem, D.3    Meo, T.4    Tosi, M.5
  • 44
    • 0027328108 scopus 로고
    • 1-antichymotrypsin allele associated with familial obstructive lung disease
    • 1-antichymotrypsin allele associated with familial obstructive lung disease. Genomics 17, 740-743 (1993).
    • (1993) Genomics , vol.17 , pp. 740-743
    • Poller, W.1
  • 46
    • 0032900570 scopus 로고    scopus 로고
    • 1-antitrypsin and liver cirrhosis
    • 1-antitrypsin and liver cirrhosis. J. Clin. Invest. 103, 999-1006 (1999).
    • (1999) J. Clin. Invest. , vol.103 , pp. 999-1006
    • Mahadeva, R.1
  • 47
    • 0032794402 scopus 로고    scopus 로고
    • Familial encephalopathy with neuroserpin inclusion bodies (FEN1B)
    • Davis, R. L. et al. Familial encephalopathy with neuroserpin inclusion bodies (FEN1B). Am. J. Pathol. 155, 1901-1913 (1999).
    • (1999) Am. J. Pathol. , vol.155 , pp. 1901-1913
    • Davis, R.L.1
  • 48
    • 0033598346 scopus 로고    scopus 로고
    • Familial dementia caused by polymerisation of mutant neuroserpin
    • 1-antitrypsin in hepatocytes to cause cirrhosis
    • 1-antitrypsin in hepatocytes to cause cirrhosis.
    • (1999) Nature , vol.401 , pp. 376-379
    • Davis, R.L.1
  • 49
    • 0034857852 scopus 로고    scopus 로고
    • Cognitive deficits associated with a recently reported familial neurodegenerative disease
    • Bradshaw, C. B. et al. Cognitive deficits associated with a recently reported familial neurodegenerative disease. Arch. Neurol. 58, 1429-1434 (2001).
    • (2001) Arch. Neurol. , vol.58 , pp. 1429-1434
    • Bradshaw, C.B.1
  • 50
    • 0037053323 scopus 로고    scopus 로고
    • Mutant neuroserpin (S49P) that causes familial encephalopathy with neuroserpin inclusion bodies is a poor proteinase inhibitor and readily forms polymers in vitro
    • Belorgey, D., Crowther, D. C., Mahadeva, R. & Lomas, D. A. Mutant neuroserpin (S49P) that causes familial encephalopathy with neuroserpin inclusion bodies is a poor proteinase inhibitor and readily forms polymers in vitro. J. Biol. Chem. 277, 17367-17373 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 17367-17373
    • Belorgey, D.1    Crowther, D.C.2    Mahadeva, R.3    Lomas, D.A.4
  • 51
    • 0037193809 scopus 로고    scopus 로고
    • Association between conformational mutations in neuroserpin and onset and seventy of dementia
    • Davis, R. L. et al. Association between conformational mutations in neuroserpin and onset and seventy of dementia. Lancet 359, 2242-2247 (2002).
    • (2002) Lancet , vol.359 , pp. 2242-2247
    • Davis, R.L.1
  • 52
    • 0027976996 scopus 로고
    • Increased body temperature accelerates aggregation of the Leu-68oGln mutant cystatin C, the amyloid-forming protein in hereditary cystatin C amyloid angiopathy
    • Abrahamson, M. & Grubb, A. Increased body temperature accelerates aggregation of the Leu-68oGln mutant cystatin C, the amyloid-forming protein in hereditary cystatin C amyloid angiopathy. Proc. Natl Acad. Sci. USA 91, 1416-1420 (1994).
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 1416-1420
    • Abrahamson, M.1    Grubb, A.2
  • 53
    • 0035069135 scopus 로고    scopus 로고
    • Human cystatin C, an amyloidogenic protein dimerizes through three-dimensional domain swapping
    • Janowski, R. et al. Human cystatin C, an amyloidogenic protein dimerizes through three-dimensional domain swapping. Nature Struct Biol. 8, 316-320 (2001).
    • (2001) Nature Struct Biol. , vol.8 , pp. 316-320
    • Janowski, R.1
  • 54
    • 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. et al. Three-dimensional domain swapping in the folded and molten-globule states of cystatins, an amyloid-forming structural superfamily. EMBO J. 20, 4774-4781 (2001).
    • (2001) EMBO J. , vol.20 , pp. 4774-4781
    • Staniforth, R.A.1
  • 56
    • 0031056829 scopus 로고    scopus 로고
    • Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis
    • Booth, D. R. et al. Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis. Nature 385, 787-793 (1997).
    • (1997) Nature , vol.385 , pp. 787-793
    • Booth, D.R.1
  • 57
    • 0033550075 scopus 로고    scopus 로고
    • The most pathogenic transthyretin variant, L 55P forms amyloid fibrils under acidic conditions and protofilaments under physiological conditions
    • Lashuel, H. A., Wurth, C., Woo, L. & Kelly, J. W. The most pathogenic transthyretin variant, L55P forms amyloid fibrils under acidic conditions and protofilaments under physiological conditions. Biochemistry 12, 13560-13573 (1999).
    • (1999) Biochemistry , vol.12 , pp. 13560-13573
    • Lashuel, H.A.1    Wurth, C.2    Woo, L.3    Kelly, J.W.4
  • 58
    • 0014351967 scopus 로고
    • X-ray diffraction studies on amyloid filaments
    • Eanes, E. D. & Glenner, G. G. X-ray diffraction studies on amyloid filaments. J. Histochem. Cytochem. 16, 673-677 (1968).
    • (1968) J. Histochem. Cytochem. , vol.16 , pp. 673-677
    • Eanes, E.D.1    Glenner, G.G.2
  • 59
    • 0030586945 scopus 로고    scopus 로고
    • Synchrotron X-ray studies suggest that the core of the transthyretin amyloid fibril is a continuous α-sheet helix
    • Interpretation of the diffraction pattern of amyloid fibrils, with a satisfying model for their structure
    • Blake, C. & Serpell, L. Synchrotron X-ray studies suggest that the core of the transthyretin amyloid fibril is a continuous α-sheet helix. Structure 4, 989-998 (1996). Interpretation of the diffraction pattern of amyloid fibrils, with a satisfying model for their structure.
    • (1996) Structure , vol.4 , pp. 989-998
    • Blake, C.1    Serpell, L.2
  • 60
    • 0031592945 scopus 로고    scopus 로고
    • Common core structure of amyloid fibrils by synchrotron X-ray diffraction
    • Sunde, M. et al. Common core structure of amyloid fibrils by synchrotron X-ray diffraction. J. Mol. Biol. 273, 729-739 (1997).
    • (1997) J. Mol. Biol. , vol.273 , pp. 729-739
    • Sunde, M.1
  • 61
    • 0035961291 scopus 로고    scopus 로고
    • Pathogenesis, diagnosis and treatment of systemic amyloidosis
    • Pepys, M. B. Pathogenesis, diagnosis and treatment of systemic amyloidosis. Phil. Trans. R. Soc. Lond. B Biol. Sci. 356, 203-210 (2001).
    • (2001) Phil. Trans. R. Soc. Lond. B Biol. Sci. , vol.356 , pp. 203-210
    • Pepys, M.B.1
  • 62
    • 0030799122 scopus 로고    scopus 로고
    • Amyloid β-protein fibrillogenesis. Detection of a protofibrillar intermediate
    • Walsh, D. M., Lomakin, A., Benedek, G. B., Condron, M. M. & Teplow, D. B. Amyloid β-protein fibrillogenesis. Detection of a protofibrillar intermediate. J. Biol. Chem. 272, 22364-22372 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 22364-22372
    • Walsh, D.M.1    Lomakin, A.2    Benedek, G.B.3    Condron, M.M.4    Teplow, D.B.5
  • 63
    • 0033771793 scopus 로고    scopus 로고
    • Is there a cause-and-effect relationship between α-synuclein fibrillization and Parkinson's disease?
    • Goldberg, M. S. & Lansbury, P. T. J. Is there a cause-and-effect relationship between α-synuclein fibrillization and Parkinson's disease? Nature Cell Biol. 2, E115-E119 (2002).
    • (2002) Nature Cell Biol. , vol.2
    • Goldberg, M.S.1    Lansbury, P.T.J.2
  • 64
    • 0026453127 scopus 로고
    • Fibril formation by primate, rodent, and Dutch-hemorrhagic analogues of Alzheimer amyloid β-protein
    • Fraser, P. E. et al. Fibril formation by primate, rodent, and Dutch-hemorrhagic analogues of Alzheimer amyloid β-protein. Biochemistry 31, 10716-10723 (1992).
    • (1992) Biochemistry , vol.31 , pp. 10716-10723
    • Fraser, P.E.1
  • 66
    • 0030744876 scopus 로고    scopus 로고
    • Mutations in the α-synuclein gene identified in families with Parkinson's disease
    • Polymeropoulos, M. H. et al. Mutations in the α-synuclein gene identified in families with Parkinson's disease. Science 276, 2045-2047 (1997).
    • (1997) Science , vol.276 , pp. 2045-2047
    • Polymeropoulos, M.H.1
  • 67
    • 0031990490 scopus 로고    scopus 로고
    • Ala30Pro mutation in the gene encoding α-synuclein in Parkinson's disease
    • Kruger, R. et al. Ala30Pro mutation in the gene encoding α-synuclein in Parkinson's disease. Nature Genet. 18, 106-108 (1998).
    • (1998) Nature Genet. , vol.18 , pp. 106-108
    • Kruger, R.1
  • 68
    • 0032568534 scopus 로고    scopus 로고
    • α-Synuclein in filamentous inclusions of Lewy bodies from Parkinson's disease and dementia with lewy bodies
    • Spillantini, M. G., Crowther, R. A., Jakes, R., Hasegawa, M. & Goedert, M. α-Synuclein in filamentous inclusions of Lewy bodies from Parkinson's disease and dementia with lewy bodies. Proc. Natl Acad. Sci. USA 95, 6469-6473 (1998).
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 6469-6473
    • Spillantini, M.G.1    Crowther, R.A.2    Jakes, R.3    Hasegawa, M.4    Goedert, M.5
  • 69
    • 0034681163 scopus 로고    scopus 로고
    • Acceleration of oligomerization, not fibrillization, is a shared property of both α-synuclein mutations linked to early-onset Parkinson's disease: Implications for pathogenesis and therapy
    • Conway, K. A. et al. Acceleration of oligomerization, not fibrillization, is a shared property of both α-synuclein mutations linked to early-onset Parkinson's disease: implications for pathogenesis and therapy. Proc. Natl Acad. Sci. USA 97, 571-576 (2000).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 571-576
    • Conway, K.A.1
  • 70
    • 0034869693 scopus 로고    scopus 로고
    • Crystal structure of the human prion protein reveals a mechanism of oligomerization
    • Knaus, K. J. et al. Crystal structure of the human prion protein reveals a mechanism of oligomerization. Nature Struct. Biol. 8, 770-774 (2001).
    • (2001) Nature Struct. Biol. , vol.8 , pp. 770-774
    • Knaus, K.J.1
  • 71
    • 0028036911 scopus 로고
    • A phenylalanine 402 to leucine mutation is responsible for a stable inactive conformation of antithrombin
    • Emmerich, J. et al. A phenylalanine 402 to leucine mutation is responsible for a stable inactive conformation of antithrombin. Thromb. Res. 76, 307-315 (1994).
    • (1994) Thromb. Res. , vol.76 , pp. 307-315
    • Emmerich, J.1
  • 72
    • 0033793872 scopus 로고    scopus 로고
    • Mechanisms of amyloidogenesis
    • Kelly, J. W. Mechanisms of amyloidogenesis. Nature Struct. Biol. 7, 824-826 (2000).
    • (2000) Nature Struct. Biol. , vol.7 , pp. 824-826
    • Kelly, J.W.1
  • 73
    • 0037124337 scopus 로고    scopus 로고
    • The yeast prion Ure2p retains its native alpha-helical conformation upon assembly into protein fibrils in vitro
    • Bousset, L., Thomson, N. H., Radford, S. E. & Melki, R. The yeast prion Ure2p retains its native alpha-helical conformation upon assembly into protein fibrils in vitro. EMBO J. 21, 2903-2911 (2002).
    • (2002) EMBO J. , vol.21 , pp. 2903-2911
    • Bousset, L.1    Thomson, N.H.2    Radford, S.E.3    Melki, R.4
  • 74
    • 0032589794 scopus 로고    scopus 로고
    • A 2.6Å structure of a serpin polymer and implications for conformational disease
    • Huntington, J. A. et. at al. A 2.6Å structure of a serpin polymer and implications for conformational disease. J. Mol. Biol. 293, 449-455 (1999).
    • (1999) J. Mol. Biol. , vol.293 , pp. 449-455
    • Huntington, J.A.1
  • 75
    • 0034000728 scopus 로고    scopus 로고
    • Cleaved antitrypsin polymers at atomic resolution
    • Dunstone, M. A. et al. Cleaved antitrypsin polymers at atomic resolution. Protein Sci. 9, 417-420 (2000).
    • (2000) Protein Sci. , vol.9 , pp. 417-420
    • Dunstone, M.A.1
  • 76
    • 0035947207 scopus 로고    scopus 로고
    • Metabolic regulation of brain Aβ by nepnysin
    • Iwata, N. et al. Metabolic regulation of brain Aβ by nepnysin. Science 292, 1550-1552 (2001).
    • (2001) Science , vol.292 , pp. 1550-1552
    • Iwata, N.1
  • 77
    • 0032499264 scopus 로고    scopus 로고
    • Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism
    • Kitada, T. et al. Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism. Nature 392, 505-608 (1998).
    • (1998) Nature , vol.392 , pp. 505-608
    • Kitada, T.1
  • 78
    • 0027535111 scopus 로고
    • β-Amyloid peptide and a 3-kDa fragment are derived by distinct cellular mechanisms
    • Haass, C., Hung, A. Y., Schlossmacher, M. G., Teplow, D. B. & Selkoe, D. J. β-Amyloid peptide and a 3-kDa fragment are derived by distinct cellular mechanisms. J. Biol. Chem. 268, 3021-3024 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 3021-3024
    • Haass, C.1    Hung, A.Y.2    Schlossmacher, M.G.3    Teplow, D.B.4    Selkoe, D.J.5
  • 79
    • 0026646604 scopus 로고
    • Amyloid β-peptide is produced by cultured cells during normal metabolism
    • Haass, C. et al. Amyloid β-peptide is produced by cultured cells during normal metabolism. Nature 359, 322-325 (1992).
    • (1992) Nature , vol.359 , pp. 322-325
    • Haass, C.1
  • 80
    • 0026760261 scopus 로고
    • Production of the Alzheimer amyloid β protein by normal proteolytic processing
    • Shoji, M. et al. Production of the Alzheimer amyloid β protein by normal proteolytic processing. Science 258, 126-129 (1992).
    • (1992) Science , vol.258 , pp. 126-129
    • Shoji, M.1
  • 81
    • 0035066332 scopus 로고    scopus 로고
    • Alzheimer's disease: Genes, proteins and therapy
    • Selkoe, D. J. Alzheimer's disease: genes, proteins and therapy. Physiol. Rev. 81, 741-766 (2001).
    • (2001) Physiol. Rev. , vol.81 , pp. 741-766
    • Selkoe, D.J.1
  • 82
    • 0033535553 scopus 로고    scopus 로고
    • Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and β-secretase activity
    • Wolfe, M. S. et al. Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and β-secretase activity. Nature 398, 513-517 (1999).
    • (1999) Nature , vol.398 , pp. 513-517
    • Wolfe, M.S.1
  • 83
    • 0034621824 scopus 로고    scopus 로고
    • Photoactivated β-secretase inhibitors directed to the active site covalently label presenilin 1
    • Li, Y.-M. et al. Photoactivated β-secretase inhibitors directed to the active site covalently label presenilin 1. Nature 405, 689-694 (2000).
    • (2000) Nature , vol.405 , pp. 689-694
    • Li, Y.-M.1
  • 84
    • 0033518251 scopus 로고    scopus 로고
    • Purification and cloning of amyloid precursor protein β-secretase from human brain
    • Sinha, S. et al. Purification and cloning of amyloid precursor protein β-secretase from human brain. Nature 402, 537-540 (1999).
    • (1999) Nature , vol.402 , pp. 537-540
    • Sinha, S.1
  • 85
    • 0033518264 scopus 로고    scopus 로고
    • Membrane-anchored aspartyl protease with Alzheimer's disease β-secretase activity
    • Yan, R. et al. Membrane-anchored aspartyl protease with Alzheimer's disease β-secretase activity. Nature 402, 533-537 (1999).
    • (1999) Nature , vol.402 , pp. 533-537
    • Yan, R.1
  • 86
    • 0033595706 scopus 로고    scopus 로고
    • Beta-secretase cleavage of Alzheimer's amyloid precursor protein by the transmembrane aspartic protease BACE
    • Vassar, R. et al. Beta-secretase cleavage of Alzheimer's amyloid precursor protein by the transmembrane aspartic protease BACE. Science 286, 735-741 (1999).
    • (1999) Science , vol.286 , pp. 735-741
    • Vassar, R.1
  • 87
    • 0033382226 scopus 로고    scopus 로고
    • Identification of a novel aspartic protease (Asp 2) as β-secretase
    • Hussain, I. et al. Identification of a novel aspartic protease (Asp 2) as β-secretase. Mol. Cell. Neurosci. 14, 419-427 (1999).
    • (1999) Mol. Cell. Neurosci. , vol.14 , pp. 419-427
    • Hussain, I.1
  • 88
    • 0034608868 scopus 로고    scopus 로고
    • Hsp70 and Hsp40 chaperones can inhibit self assembly of polyglutamine proteins into amyloid-like fibrils
    • Muchowski, P. J. et al. Hsp70 and Hsp40 chaperones can inhibit self assembly of polyglutamine proteins into amyloid-like fibrils. Proc. Natl Acad. Sci. USA 97, 7841-7846 (2002).
    • (2002) Proc. Natl Acad. Sci. USA , vol.97 , pp. 7841-7846
    • Muchowski, P.J.1
  • 89
    • 0030470459 scopus 로고    scopus 로고
    • Glutamine repeats and inherited neurodegenerative diseases: Molecular aspects
    • Perutz, M. F. Glutamine repeats and inherited neurodegenerative diseases: molecular aspects. Curr. Opin. Struct. Biol. 6, 848-858 (1996).
    • (1996) Curr. Opin. Struct. Biol. , vol.6 , pp. 848-858
    • Perutz, M.F.1
  • 91
    • 0031873102 scopus 로고    scopus 로고
    • β-Sheet breaker peptides inhibit fibrillogenesis in a rat brain model of amyloidosis: Implications for Alzheimer's therapy
    • Demonstration that small peptides can block the β-strand linkage of the peptide that is thought to cause Alzheimer disease and so reduce plaque formation in an animal model
    • Soto, C. et al. β-Sheet breaker peptides inhibit fibrillogenesis in a rat brain model of amyloidosis: implications for Alzheimer's therapy. Nature Med. 4, 822-825 (1998). Demonstration that small peptides can block the β-strand linkage of the peptide that is thought to cause Alzheimer disease and so reduce plaque formation in an animal model.
    • (1998) Nature Med. , vol.4 , pp. 822-825
    • Soto, C.1
  • 93
    • 0037118028 scopus 로고    scopus 로고
    • Targeted pharmacological depletion of serum amyloid P component for treatment of human amyloidosis
    • Elegant demonstration of the use of rational drug design to develop a drug for the treatment of the amyloidoses.
    • Pepys, M. B. et al. Targeted pharmacological depletion of serum amyloid P component for treatment of human amyloidosis. Nature 417, 254-259 (2002). Elegant demonstration of the use of rational drug design to develop a drug for the treatment of the amyloidoses.
    • (2002) Nature , vol.417 , pp. 254-259
    • Pepys, M.B.1
  • 94
    • 0033835996 scopus 로고    scopus 로고
    • Peripherally administered antibodies against amyloid β-peptide enter the central nervous system and reduce pathology in a mouse model of Alzheimer disease
    • Bard, F. et al. Peripherally administered antibodies against amyloid β-peptide enter the central nervous system and reduce pathology in a mouse model of Alzheimer disease. Nature Med. 6, 916-919 (2000).
    • (2000) Nature Med. , vol.6 , pp. 916-919
    • Bard, F.1
  • 95
  • 96
    • 84984755327 scopus 로고    scopus 로고
    • Aβ peptide vaccination prevents memory loss in an animal model of Alzheimer's disease
    • Morgan, D. et al. Aβ peptide vaccination prevents memory loss in an animal model of Alzheimer's disease. Nature 408, 982-985 (2000).
    • (2000) Nature , vol.408 , pp. 982-985
    • Morgan, D.1
  • 97
    • 0030819064 scopus 로고    scopus 로고
    • Mechanisms of antithrombin polymerisation and heparin activation probed by insertion of synthetic reactive loop peptides
    • Fitton, H. L., Pike, R. N., Carrell, R. W. & Chang, W.-S. W. Mechanisms of antithrombin polymerisation and heparin activation probed by insertion of synthetic reactive loop peptides. Biol. Chem. 378, 1059-1063 (1997).
    • (1997) Biol. Chem. , vol.378 , pp. 1059-1063
    • Fitton, H.L.1    Pike, R.N.2    Carrell, R.W.3    Chang, W.-S.W.4
  • 98
    • 0029866947 scopus 로고    scopus 로고
    • Probing serpin reactive loop conformations by proteolytic cleavage
    • Chang, W.-S. W., Wardell, M. R., Lomas, D. A. & Carrell, R. W. Probing serpin reactive loop conformations by proteolytic cleavage. Biochem. J. 314, 647-653 (1996).
    • (1996) Biochem. J. , vol.314 , pp. 647-653
    • Chang, W.-S.W.1    Wardell, M.R.2    Lomas, D.A.3    Carrell, R.W.4
  • 99
    • 0343193210 scopus 로고    scopus 로고
    • Topography of a 2.0Å structure of α1-antitrypsin reveals targets for rational drug design to prevent conformational disease
    • Elliott, P. R., Pei, X. Y., Dafforn, T. R. & Lomas, D. A. Topography of a 2.0Å structure of α1-antitrypsin reveals targets for rational drug design to prevent conformational disease. Protein Sci. 9, 1274-1281 (2000).
    • (2000) Protein Sci. , vol.9 , pp. 1274-1281
    • Elliott, P.R.1    Pei, X.Y.2    Dafforn, T.R.3    Lomas, D.A.4
  • 100
    • 0031889082 scopus 로고    scopus 로고
    • A pilot clinical trial of oral sodium 4-phenylbutyrate (Buphenyl) in ΔF508-homozygous cystic fibrosis patients: Partial restoration of nasal epithelial CFTR function
    • Rubenstein, R. C. & Zeitlin, P. L. A pilot clinical trial of oral sodium 4-phenylbutyrate (Buphenyl) in ΔF508-homozygous cystic fibrosis patients: partial restoration of nasal epithelial CFTR function Am. J. Respir. Crit. Care Med. 157, 484-490 (1998).
    • (1998) Am. J. Respir. Crit. Care Med. , vol.157 , pp. 484-490
    • Rubenstein, R.C.1    Zeitlin, P.L.2


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