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Volumn 55, Issue 6-7, 1999, Pages 977-991

Biological activity and pathological implications of misfolded proteins

Author keywords

Amyloidosis; Apolipoprotein AI; Lysozyme; Protein misfolding; Transthyretin; protein; 2 microglobulin

Indexed keywords

AMYLOID; APOLIPOPROTEIN A1; BETA 2 MICROGLOBULIN; LYSOZYME; POLYMER; PREALBUMIN; PROTEIN;

EID: 0033045668     PISSN: 1420682X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s000180050348     Document Type: Review
Times cited : (108)

References (112)
  • 1
    • 0015859467 scopus 로고
    • Principles that govern the folding of protein chains
    • 1 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
  • 2
    • 0031055820 scopus 로고    scopus 로고
    • Mutations make enzyme polymerize
    • 2 Perutz M. F. (1997) Mutations make enzyme polymerize. Nature 385: 773-774
    • (1997) Nature , vol.385 , pp. 773-774
    • Perutz, M.F.1
  • 3
    • 0031825554 scopus 로고    scopus 로고
    • From the globular to the fibrous state. Protein structure and structural conversion in amyloid formation
    • 3 Sunde M. and Blake C. C. F. (1998) From the globular to the fibrous state. Protein structure and structural conversion in amyloid formation. Quart. Rev. Biophys. 31: 1-39
    • (1998) Quart. Rev. Biophys. , vol.31 , pp. 1-39
    • Sunde, M.1    Blake, C.C.F.2
  • 5
    • 0031056829 scopus 로고    scopus 로고
    • Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis
    • 5 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
  • 6
    • 0025778735 scopus 로고
    • Lysozyme revisited: Crystallographic evidence for distortion of an N-acetylmuramic acid residue bound in site D
    • 6 Strynadka N. C. J. and James M. N. G. (1991) Lysozyme revisited: crystallographic evidence for distortion of an N-acetylmuramic acid residue bound in site D. J. Mol. Biol. 220: 401-424
    • (1991) J. Mol. Biol. , vol.220 , pp. 401-424
    • Strynadka, N.C.J.1    James, M.N.G.2
  • 7
    • 0031576990 scopus 로고    scopus 로고
    • Fast and slow tracks in lysozyme folding process
    • 7 Matagne A., Radford S. E. and Dobson C. M. (1997) Fast and slow tracks in lysozyme folding process. J. Mol. Biol. 267: 1068-1074
    • (1997) J. Mol. Biol. , vol.267 , pp. 1068-1074
    • Matagne, A.1    Radford, S.E.2    Dobson, C.M.3
  • 8
    • 0003481596 scopus 로고
    • W. H. Freeman and Company (ed.), New York
    • 8 Fersht A. (1984) In: Enzyme Structure and Mechanism, pp. 325-361, W. H. Freeman and Company (ed.), New York
    • (1984) Enzyme Structure and Mechanism , pp. 325-361
    • Fersht, A.1
  • 9
    • 0021530861 scopus 로고
    • Characterization of the transition state of lysozyme unfolding. II. Effects of the intrachain crosslinking and the inhibitor binding on the transition state
    • 9 Segawa S. and Sugihara M. (1984) Characterization of the transition state of lysozyme unfolding. II. Effects of the intrachain crosslinking and the inhibitor binding on the transition state. Biopolymers 23: 2489-2498
    • (1984) Biopolymers , vol.23 , pp. 2489-2498
    • Segawa, S.1    Sugihara, M.2
  • 10
    • 0025162617 scopus 로고
    • Effect of inhibitors on conformational changes in hen lysozyme around thermal transition point in solution and solid state
    • 10 Bernard M., Canioni P., Cozzone P., Berthou J. and Jollès P. (1990) Effect of inhibitors on conformational changes in hen lysozyme around thermal transition point in solution and solid state. Int. J. Pept. Protein Res. 36: 46-55
    • (1990) Int. J. Pept. Protein Res. , vol.36 , pp. 46-55
    • Bernard, M.1    Canioni, P.2    Cozzone, P.3    Berthou, J.4    Jollès, P.5
  • 11
    • 0013620922 scopus 로고
    • Production and elimination of plasma lysozyme
    • Osserman E. F., Canfield R. E. and Beychok S. (eds). Academic Press, New York
    • 11 Hansen N. B., Karle H. and Andersen V. (1974) Production and elimination of plasma lysozyme. In: Lysozyme, pp. 307-319, Osserman E. F., Canfield R. E. and Beychok S. (eds). Academic Press, New York
    • (1974) Lysozyme , pp. 307-319
    • Hansen, N.B.1    Karle, H.2    Andersen, V.3
  • 12
    • 0029948723 scopus 로고    scopus 로고
    • Lysozyme binds to elastin and protects elastin from elastase-mediated degradation
    • 12 Park P. W., Biedermann K., Mecham L., Bissett D. L. and Mecham R. P. (1996) Lysozyme binds to elastin and protects elastin from elastase-mediated degradation. J. Invest. Dermatol. 106: 1075-1080
    • (1996) J. Invest. Dermatol. , vol.106 , pp. 1075-1080
    • Park, P.W.1    Biedermann, K.2    Mecham, L.3    Bissett, D.L.A.4    Mecham, R.P.5
  • 14
    • 0002699669 scopus 로고
    • Multiple modes of binding of thyroid hormones and other iodothyronines to human plasma transthyretin
    • Beddell C. R. (ed.), Wiley, New York
    • 14 De la Paz P., Burridge J. M., Oatley S. J. and Blake C. C. F. (1992) Multiple modes of binding of thyroid hormones and other iodothyronines to human plasma transthyretin. In: The Design of Drugs to Macromolecular Targets, pp. 119-172, Beddell C. R. (ed.), Wiley, New York
    • (1992) The Design of Drugs to Macromolecular Targets , pp. 119-172
    • De La Paz, P.1    Burridge, J.M.2    Oatley, S.J.A.3    Blake, C.C.F.4
  • 15
    • 0020518375 scopus 로고
    • The influence of the choroid-plexus on the concentration of prealbumin in CSF
    • 15 Weisner B. and Kauerz U. (1983) The influence of the choroid-plexus on the concentration of prealbumin in CSF. J. Neurol. Sci. 61: 27-35
    • (1983) J. Neurol. Sci. , vol.61 , pp. 27-35
    • Weisner, B.1    Kauerz, U.2
  • 16
    • 0029062667 scopus 로고
    • Structure of a complex of two plasma proteins: Transthyretin and retinol binding protein
    • 16 Monaco H. L., Rizzi M. and Coda A. (1995) Structure of a complex of two plasma proteins: transthyretin and retinol binding protein. Science 268: 1039-1041
    • (1995) Science , vol.268 , pp. 1039-1041
    • Monaco, H.L.1    Rizzi, M.2    Coda, A.3
  • 17
    • 0017824077 scopus 로고
    • Structure of prealbumin (transthyretin): Secondary, tertiary and quaternary interactions determined by Fourier refinement at 1.8 Å
    • 17 Blake C. C. F., Geisow M. J. and Oatley S. J. (1978) Structure of prealbumin (transthyretin): secondary, tertiary and quaternary interactions determined by Fourier refinement at 1.8 Å. J. Mol. Biol. 121: 339-356
    • (1978) J. Mol. Biol. , vol.121 , pp. 339-356
    • Blake, C.C.F.1    Geisow, M.J.A.2    Oatley, S.J.3
  • 18
    • 0028969996 scopus 로고
    • Transthyretin mutations in health and disease
    • 18 Saraiva M. J. M. (1995) Transthyretin mutations in health and disease. Hum. Mutat. 5: 191-196
    • (1995) Hum. Mutat. , vol.5 , pp. 191-196
    • Saraiva, M.J.M.1
  • 19
    • 0026675307 scopus 로고
    • Partial denaturation of transthyretin is sufficient for amyloid fibril formation in vitro
    • 19 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
  • 20
    • 0030004644 scopus 로고    scopus 로고
    • The acid-mediated denaturation pathway of transthyretin yields a conformational intermediate that can self-assemble into amyloid
    • 20 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 15: 6470-6482
    • (1996) Biochemistry , vol.15 , pp. 6470-6482
    • Lai, Z.1    Colon, W.2    Kelly, J.W.3
  • 21
    • 0029981197 scopus 로고    scopus 로고
    • Alternative conformations of amyloidogenic proteins govern their behavior
    • 21 Kelly J. W. (1996) Alternative conformations of amyloidogenic proteins govern their behavior. Curr. Opin. Struct. Biol. 6: 11-17
    • (1996) Curr. Opin. Struct. Biol. , vol.6 , pp. 11-17
    • Kelly, J.W.1
  • 22
    • 0030874395 scopus 로고    scopus 로고
    • Guanidine hydrochloride-induced denaturation and refolding of transthyretin exhibits a marked hysteresis: Equilibria with high kinetic barriers
    • 22 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
  • 23
    • 0030830019 scopus 로고    scopus 로고
    • Transthyretin quaternary and tertiary structural changes facilitate misassembly into amyloid
    • 23 Kelly J. W., Colon W., Lai Z., Lashuel H. A., McCulloch J., McCutchen S. L. et al. (1997) Transthyretin quaternary and tertiary structural changes facilitate misassembly into amyloid. Adv. Protein Chem 50: 161-181
    • (1997) Adv. Protein Chem , vol.50 , pp. 161-181
    • Kelly, J.W.1    Colon, W.2    Lai, Z.3    Lashuel, H.A.4    McCulloch, J.5    McCutchen, S.L.6
  • 24
    • 0028801805 scopus 로고
    • Purification and characterisation of amyloid-related transthyretin associated with familial amyloidotic cardiomyopathy
    • 24 Hermansen L. F., Bergman T., Jornval H., Husby G., Ranlov I. and Sletten K. (1995) Purification and characterisation of amyloid-related transthyretin associated with familial amyloidotic cardiomyopathy. Eur. J. Biochem. 227: 772-779
    • (1995) Eur. J. Biochem. , vol.227 , pp. 772-779
    • Hermansen, L.F.1    Bergman, T.2    Jornval, H.3    Husby, G.4    Ranlov, I.5    Sletten, K.6
  • 25
    • 0028858182 scopus 로고
    • Amyloid fibril composition and transthyretin gene structure in senile systemic amyloidosis
    • 25 Gustavsson A., Jahr H., Tobiassen R., Jacobson D. R., Sletten K. and Westermark P. (1995) Amyloid fibril composition and transthyretin gene structure in senile systemic amyloidosis. Lab. Invest. 73: 703-708
    • (1995) Lab. Invest. , vol.73 , pp. 703-708
    • Gustavsson, A.1    Jahr, H.2    Tobiassen, R.3    Jacobson, D.R.4    Sletten, K.5    Westermark, P.6
  • 26
    • 0028839438 scopus 로고
    • Comparison of lethal and nonlethal transthyretin variants and their relationship to amyloid disease
    • 26 McCutchen S. L., Lai Z., Miroy G., 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.3    Kelly, J.W.A.4    Colon, W.5
  • 27
    • 0032555738 scopus 로고    scopus 로고
    • Protein subunit interactions and structural integrity of amyloidogenic transthyretins: Evidence from electrospray mass spectrometry
    • 27 Nettleton E. J., Sunde M., Lai Z., Kelly J. W., Dobson C. M. and Robinson C. V. (1998) Protein subunit interactions and structural integrity of amyloidogenic transthyretins: evidence from electrospray mass spectrometry. J. Mol. Biol. 281: 553-564
    • (1998) J. Mol. Biol. , vol.281 , pp. 553-564
    • Nettleton, E.J.1    Sunde, M.2    Lai, Z.3    Kelly, J.W.4    Dobson, C.M.A.5    Robinson, C.V.6
  • 28
    • 0027518443 scopus 로고
    • Structure of Met30 variant of transthyretin and its amyloidogenic implications
    • 28 Terry C. J., Damas A. M., Oliveira P., Saraiva M. J. M., Alves I. L., Costa P. P. et al. (1993) Structure of Met30 variant of transthyretin and its amyloidogenic implications. EMBO J. 12: 735-741
    • (1993) EMBO J. , vol.12 , pp. 735-741
    • Terry, C.J.1    Damas, A.M.2    Oliveira, P.3    Saraiva, M.J.M.4    Alves, I.L.5    Costa, P.P.6
  • 29
    • 0027476367 scopus 로고
    • The x-ray crystal structure refinements of normal human transthyretin and the amyloidogenic Val-30→Met variant to 1.7-Å resolution
    • 29 Hamilton J. A., Steinrauf L. K., Braden B. C., Liepnieks J., Benson M. D., Holmgren G. et al. (1993) The x-ray crystal structure refinements of normal human transthyretin and the amyloidogenic Val-30→Met variant to 1.7-Å resolution. J. Biol. Chem. 268: 2416-2424
    • (1993) J. Biol. Chem. , vol.268 , pp. 2416-2424
    • Hamilton, J.A.1    Steinrauf, L.K.2    Braden, B.C.3    Liepnieks, J.4    Benson, M.D.5    Holmgren, G.6
  • 30
    • 0027459456 scopus 로고
    • X-ray crystal structure of the Ala 109 Thr variant of human transthyretin that produces euthyroid hyperthyroxinemia
    • 30 Steinrauf L. K., Hamilton J. S., Braden B. C., Murrel J. R. and Benson M. D. (1993) X-ray crystal structure of the Ala 109 Thr variant of human transthyretin that produces euthyroid hyperthyroxinemia. J. Biol. Chem. 268: 2425-2430
    • (1993) J. Biol. Chem. , vol.268 , pp. 2425-2430
    • Steinrauf, L.K.1    Hamilton, J.S.2    Braden, B.C.3    Murrel, J.R.A.4    Benson, M.D.5
  • 31
    • 0030345867 scopus 로고    scopus 로고
    • Modulating conformalional factors in transthyretin amyloid
    • CIBA Symposium No. 199, Bock G. R. and Goode J. A. (eds), Wiley, Chichester
    • 31 Saraiva M. J. M., Almeida M. R., Alves I. L., Bonifacio M. J., Damas A. M., Palha J. A. et al. (1996) Modulating conformalional factors in transthyretin amyloid. In: CIBA Symposium No. 199, The Nature and Origin of Amyloid Fibrils. pp. 47-57, Bock G. R. and Goode J. A. (eds), Wiley, Chichester
    • (1996) The Nature and Origin of Amyloid Fibrils. , pp. 47-57
    • Saraiva, M.J.M.1    Almeida, M.R.2    Alves, I.L.3    Bonifacio, M.J.4    Damas, A.M.5    Palha, J.A.6
  • 32
    • 0032544408 scopus 로고    scopus 로고
    • The crystal structure of amyloidogenic Leu 55-Pro transthyretin variant reveals a possible pathway for transthyretin polymerization into amyloid fibrils
    • 32 Sebastiao M. P., Saraiva M. J. and Damas A. M. (1998) The crystal structure of amyloidogenic Leu 55-Pro transthyretin variant reveals a possible pathway for transthyretin polymerization into amyloid fibrils. J. Biol. Chem. 273: 24715-24722
    • (1998) J. Biol. Chem. , vol.273 , pp. 24715-24722
    • Sebastiao, M.P.1    Saraiva, M.J.A.2    Damas, A.M.3
  • 33
    • 0028168367 scopus 로고
    • The Ile-84-Ser amino acid substitution in transthyretin interferes with the interaction with plasma Retinol-binding protein
    • 33 Berni R., Malpeli G., Folli C., Murrell J. R., Liepnieks J. J. and Benson M. D. (1994) The Ile-84-Ser amino acid substitution in transthyretin interferes with the interaction with plasma Retinol-binding protein. J. Biol. Chem. 269: 23395-23398
    • (1994) J. Biol. Chem. , vol.269 , pp. 23395-23398
    • Berni, R.1    Malpeli, G.2    Folli, C.3    Murrell, J.R.4    Liepnieks, J.J.A.5    Benson, M.D.6
  • 34
    • 0028801506 scopus 로고
    • Transport of serum transthyretin into chicken oocytes
    • 34 Vieira A. V., Sanders E. J. and Schneider W. J. (1995) Transport of serum transthyretin into chicken oocytes. J. Biol. Chem. 270: 2952-2956
    • (1995) J. Biol. Chem. , vol.270 , pp. 2952-2956
    • Vieira, A.V.1    Sanders, E.J.A.2    Schneider, W.J.3
  • 35
    • 0013565808 scopus 로고    scopus 로고
    • Characterization of receptor mediated internalization of transthyretin
    • Mayo Clinic, Rochester, MN
    • 35 Sousa M. and Saraiva M. J. (1998) Characterization of receptor mediated internalization of transthyretin. VIII International Symposium on Amyloidosis, Mayo Clinic, Rochester, MN. p. 95
    • (1998) VIII International Symposium on Amyloidosis , pp. 95
    • Sousa, M.1    Saraiva, M.J.2
  • 37
    • 0029831901 scopus 로고    scopus 로고
    • Thyroxine binding to transthyretin (TTR) variants-two variants (TTR Pro 55 and TTR Met III) with a particular low binding affinity
    • 37 Almeida M. R. and Saraiva M. J. (1996) Thyroxine binding to transthyretin (TTR) variants-two variants (TTR Pro 55 and TTR Met III) with a particular low binding affinity. Eur. J. Endocrinol. 135: 226-230
    • (1996) Eur. J. Endocrinol. , vol.135 , pp. 226-230
    • Almeida, M.R.1    Saraiva, M.J.2
  • 39
    • 0002914568 scopus 로고
    • Reidenberg M. M. and Erill S. (eds), Praeger, New York
    • 39 Sjöhohm I. (1986) In: Drug Protein Binding. pp. 36-45, Reidenberg M. M. and Erill S. (eds), Praeger, New York
    • (1986) Drug Protein Binding , pp. 36-45
    • Sjöhohm, I.1
  • 41
    • 0027504210 scopus 로고
    • Folding and assembly of major histocompatibility complex class I heterodimers in the endoplasmic reticulum of intact cells precedes the binding of peptide
    • 41 Neefjes J., Hammerling G. and Momburg F. (1993) Folding and assembly of major histocompatibility complex class I heterodimers in the endoplasmic reticulum of intact cells precedes the binding of peptide. J. Exp. Med. 178: 1971-1980
    • (1993) J. Exp. Med. , vol.178 , pp. 1971-1980
    • Neefjes, J.1    Hammerling, G.2    Momburg, F.3
  • 42
    • 0030456367 scopus 로고    scopus 로고
    • Intermediates in the assembly and degradation of class I major histocompalibility complex (MHC) molecules probed with free heavy chain-specific monoclonal antibodies
    • 42 Machold R. P. and Ploegh H. L. (1996) Intermediates in the assembly and degradation of class I major histocompalibility complex (MHC) molecules probed with free heavy chain-specific monoclonal antibodies. J. Exp. Med. 184: 2251-2259
    • (1996) J. Exp. Med. , vol.184 , pp. 2251-2259
    • Machold, R.P.1    Ploegh, H.L.2
  • 43
    • 0028181764 scopus 로고
    • Soluble β2-microglobulin-free class I heavy chains are released from the surface of activated and leukemia cells by a metalloprotease
    • 43 Demaria S., Schawab R., Gottesman S. R. S. and Buskin Y. (1994) Soluble β2-microglobulin-free class I heavy chains are released from the surface of activated and leukemia cells by a metalloprotease. J. Biol. Chem. 269: 6689-6694
    • (1994) J. Biol. Chem. , vol.269 , pp. 6689-6694
    • Demaria, S.1    Schawab, R.2    Gottesman, S.R.S.A.3    Buskin, Y.4
  • 44
    • 0000694354 scopus 로고
    • Amyloidosis
    • Weatherall D. J., Ledingham J. G. and Warrell D. A. (eds), Oxford University Press, Oxford
    • 44 Pepys M. B. (1995) Amyloidosis. In: Oxford Textbook of Medicine, 3rd ed.. pp. 1512-1524, Weatherall D. J., Ledingham J. G. and Warrell D. A. (eds), Oxford University Press, Oxford
    • (1995) Oxford Textbook of Medicine, 3rd Ed.. , pp. 1512-1524
    • Pepys, M.B.1
  • 45
    • 0030823440 scopus 로고    scopus 로고
    • β2-Microglobulin associated amyloidosis: A vanishing complication of long-term haemodialysis
    • 45 Schwalbe S., Holzhauer M., Schaeffer J., Galanski M., Koch K. M. and Floege J. (1997) β2-microglobulin associated amyloidosis: A vanishing complication of long-term haemodialysis. Kidney Int. 52: 1077-1083
    • (1997) Kidney Int. , vol.52 , pp. 1077-1083
    • Schwalbe, S.1    Holzhauer, M.2    Schaeffer, J.3    Galanski, M.4    Koch, K.M.5    Floege, J.6
  • 46
    • 0027254912 scopus 로고
    • Clinical implications of hemodialysis membrane biocompatibility
    • 46 Hakim R. M. (1993) Clinical implications of hemodialysis membrane biocompatibility. Kidney Int. 44: 484-494
    • (1993) Kidney Int. , vol.44 , pp. 484-494
    • Hakim, R.M.1
  • 47
    • 0025087095 scopus 로고
    • Effects of membrane on beta-2 microglobulin production and cellular expression
    • 47 Zaoui P. M., Stone W. J. and Hakim R. M. (1980) Effects of membrane on beta-2 microglobulin production and cellular expression. Kidney Int. 38: 962-968
    • (1980) Kidney Int. , vol.38 , pp. 962-968
    • Zaoui, P.M.1    Stone, W.J.2    Hakim, R.M.3
  • 48
    • 0026709414 scopus 로고
    • The β2-microglobulin dissociation rate is an accurate measure of the stability of MHC class I heterotrimers and depends on which peptide is bound
    • 48 Parker K. C., DiBrino M., Hull L. and Coligan J. E. (1992) The β2-microglobulin dissociation rate is an accurate measure of the stability of MHC class I heterotrimers and depends on which peptide is bound. J. Immunol. 149: 1896-1904
    • (1992) J. Immunol. , vol.149 , pp. 1896-1904
    • Parker, K.C.1    DiBrino, M.2    Hull, L.3    Coligan, J.E.4
  • 49
    • 0030613752 scopus 로고    scopus 로고
    • Use of anti-(β2 microglobulin) mAb to study formation of amyloid fibrils
    • 49 Stoppini M., Bellotti V., Mangione P., Merlini G. and Ferri G. (1997) Use of anti-(β2 microglobulin) mAb to study formation of amyloid fibrils. Eur. J. Bioehem. 249: 21-29
    • (1997) Eur. J. Bioehem. , vol.249 , pp. 21-29
    • Stoppini, M.1    Bellotti, V.2    Mangione, P.3    Merlini, G.4    Ferri, G.5
  • 50
    • 0028929555 scopus 로고
    • Relationship between elevation in the plasma concentration of elastase-alfa I proteinase inhibitor complex (E-alfa-Pi) and haemostatic parameters during haemodialysis
    • 50 Yamazaki M., Asakura H., Saito M., Jokaji H., Uotani C., Kumabashiri I. et al. (1995) Relationship between elevation in the plasma concentration of elastase-alfa I proteinase inhibitor complex (E-alfa-Pi) and haemostatic parameters during haemodialysis. Blood Coagul. Fibrinolysis 6: 5-10
    • (1995) Blood Coagul. Fibrinolysis , vol.6 , pp. 5-10
    • Yamazaki, M.1    Asakura, H.2    Saito, M.3    Jokaji, H.4    Uotani, C.5    Kumabashiri, I.6
  • 51
    • 0028987213 scopus 로고
    • Crystal structure of an H-2Kb-ovalbumin peptide complex reveals the interplay of primary and secondary anchor positions in the major histocompatibility complex binding groove
    • 51 Fremont D. H., Stura E. A., Matsumura M., Peterson P. A. and Wilson I. A. (1995) Crystal structure of an H-2Kb-ovalbumin peptide complex reveals the interplay of primary and secondary anchor positions in the major histocompatibility complex binding groove. Proc. Natl. Acad. Sci. USA 92: 2479-2483
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 2479-2483
    • Fremont, D.H.1    Stura, E.A.2    Matsumura, M.3    Peterson, P.A.A.4    Wilson, I.A.5
  • 52
    • 17644429206 scopus 로고    scopus 로고
    • Secretory processing of amyloid precursor protein is inhibited by increase in cellular cholesterol content
    • 52 Racchi M., Baetta K., Salvietti N., Ianna P., Franceschini G., Paolotti R. et al. (1997) Secretory processing of amyloid precursor protein is inhibited by increase in cellular cholesterol content. Biochem. J. 322: 893-898
    • (1997) Biochem. J. , vol.322 , pp. 893-898
    • Racchi, M.1    Baetta, K.2    Salvietti, N.3    Ianna, P.4    Franceschini, G.5    Paolotti, R.6
  • 53
    • 0024307776 scopus 로고
    • Collagen-binding affinity of beta-2-microglobulin, a preprotein of hemodialysis-associated amyloidosis
    • 53 Homma N., Gejyo F., Isemura M. and Arakawa M. (1989) Collagen-binding affinity of beta-2-microglobulin, a preprotein of hemodialysis-associated amyloidosis. Nephron 53: 37-40
    • (1989) Nephron , vol.53 , pp. 37-40
    • Homma, N.1    Gejyo, F.2    Isemura, M.3    Arakawa, M.4
  • 54
    • 0024604961 scopus 로고
    • Autocrine induction of collagenase by serum amyloid A-like and beta2-microglobulin-like proteins
    • 54 Brinekerhoff C., Mitchel T. I., Karmilowicz M. J., Kluve Beckerman B. and Benson M. (1989) Autocrine induction of collagenase by serum amyloid A-like and beta2-microglobulin-like proteins. Science 243: 655-657
    • (1989) Science , vol.243 , pp. 655-657
    • Brinekerhoff, C.1    Mitchel, T.I.2    Karmilowicz, M.J.3    Kluve Beckerman, B.4    Benson, M.5
  • 55
    • 0023182225 scopus 로고
    • A bone derived growth factor isolated from rat calvariae is beta 2 microglobulin
    • 55 Canalis E., McCarthy T. and Centrella M. (1987) A bone derived growth factor isolated from rat calvariae is beta 2 microglobulin. Endocrinology 121: 1198-1200
    • (1987) Endocrinology , vol.121 , pp. 1198-1200
    • Canalis, E.1    McCarthy, T.2    Centrella, M.3
  • 56
    • 0023839071 scopus 로고
    • Growth factors and the regulation of bone remodelling
    • 56 Canalis E., McCarthy T. and Centrella M. (1988) Growth factors and the regulation of bone remodelling. J. Clin. Invest. 81: 277-281
    • (1988) J. Clin. Invest. , vol.81 , pp. 277-281
    • Canalis, E.1    McCarthy, T.2    Centrella, M.3
  • 60
    • 0032532946 scopus 로고    scopus 로고
    • β2-Microglobulin can be refolded into a native state from ex vivo amyloid fibrils
    • 60 Bellotti V., Stoppini M., Mangione P., Sunde M., Robinson C., Asti L. et al. (1998) β2-microglobulin can be refolded into a native state from ex vivo amyloid fibrils. Eur. J. Biochem. 258: 61-67
    • (1998) Eur. J. Biochem. , vol.258 , pp. 61-67
    • Bellotti, V.1    Stoppini, M.2    Mangione, P.3    Sunde, M.4    Robinson, C.5    Asti, L.6
  • 61
    • 0040973182 scopus 로고
    • The structure and function of immunoglobulin domains: Studies with β2-microglobulin on the role of the intrachain disulfide bond
    • 61 Isenman D. E., Painter R. H. and Dorrington H. J. (1975) The structure and function of immunoglobulin domains: studies with β2-microglobulin on the role of the intrachain disulfide bond. Proc. Natl. Acad. Sci. USA 72: 548-552
    • (1975) Proc. Natl. Acad. Sci. USA , vol.72 , pp. 548-552
    • Isenman, D.E.1    Painter, R.H.2    Dorrington, H.J.3
  • 62
    • 0014264541 scopus 로고
    • The plasma lecithins:Cholesterol acyl-transferase reaction
    • 62 Glomset J. A. (1968) The plasma lecithins:cholesterol acyl-transferase reaction. J. Lipid Res. 9: 155-167
    • (1968) J. Lipid Res. , vol.9 , pp. 155-167
    • Glomset, J.A.1
  • 63
    • 0023178264 scopus 로고
    • Pre-beta-migrating high density lipoprotein: Quantitation in normal and hyperlipidemic plasma by solid phase radioimmunoassay following electrophoretic transfer
    • 63 Ishida B. Y., Frolich J. and Fielding C. J. J. (1987) Pre-beta-migrating high density lipoprotein: quantitation in normal and hyperlipidemic plasma by solid phase radioimmunoassay following electrophoretic transfer. Lipid Res. 28: 778-786
    • (1987) Lipid Res. , vol.28 , pp. 778-786
    • Ishida, B.Y.1    Frolich, J.2    Fielding, C.J.J.3
  • 64
    • 0030732162 scopus 로고    scopus 로고
    • Crystal structure of truncated human apolipoprotein A-1 suggests a lipid-bound conformation
    • 64 Borhani D. W., Rogers D. P., Engler J. A. and Brouillette C. G. (1997) Crystal structure of truncated human apolipoprotein A-1 suggests a lipid-bound conformation. Proc. Natl. Acad. Sci. USA 94: 12291-12296
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 12291-12296
    • Borhani, D.W.1    Rogers, D.P.2    Engler, J.A.3    Brouillette, C.G.4
  • 65
    • 0029864592 scopus 로고    scopus 로고
    • Thermal unfolding of human high-density apolipoprotein A-1: Implications for a lipid-free molten globular stale
    • 65 Gursky O. and Atkinson D. (1996) Thermal unfolding of human high-density apolipoprotein A-1: implications for a lipid-free molten globular stale. Proc. Natl. Acad. Sci. USA 93: 2991-2995
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 2991-2995
    • Gursky, O.1    Atkinson, D.2
  • 67
    • 0025006134 scopus 로고
    • A mutation in apolipoprotein AI in the Iowa type of familial amyloidotic polyneuropathy
    • 67 Nichols W. C., Gregg R. E., Brewer H. B. and Benson M. D. (1990) A mutation in apolipoprotein AI in the Iowa type of familial amyloidotic polyneuropathy. Genomics 8: 318-323
    • (1990) Genomics , vol.8 , pp. 318-323
    • Nichols, W.C.1    Gregg, R.E.2    Brewer, H.B.3    Benson, M.D.4
  • 68
    • 0028267150 scopus 로고
    • Familial nephropathic systemic amyloidosis caused by apolipoprotein AI variant Arg 26
    • 68 Vigushin D. M., Gough J., Allan D., Alguacil A., Penner B., Pettigrevv N. M. et al. (1994) Familial nephropathic systemic amyloidosis caused by apolipoprotein AI variant Arg 26. Q. J. Med. 87: 149-154
    • (1994) Q. J. Med. , vol.87 , pp. 149-154
    • Vigushin, D.M.1    Gough, J.2    Allan, D.3    Alguacil, A.4    Penner, B.5    Pettigrevv, N.M.6
  • 69
    • 0028803995 scopus 로고
    • A new apolipoprotein AI variant, Trp50Arg, causes hereditary amyloidosis
    • 69 Booth D. R., Tan S. Y., Booth S. E., Hsuan J. J., Totty N. F., Nguyen O. et al. (1995) A new apolipoprotein AI variant, Trp50Arg, causes hereditary amyloidosis. Q. J. Med. 88: 695-702
    • (1995) Q. J. Med. , vol.88 , pp. 695-702
    • Booth, D.R.1    Tan, S.Y.2    Booth, S.E.3    Hsuan, J.J.4    Totty, N.F.5    Nguyen, O.6
  • 71
    • 0031907376 scopus 로고    scopus 로고
    • Hereditary nephropathic systemic amyloidosis caused by a novel variant apolipoprotein AI
    • 71 Persey M. R., Booth D. R., Booth S. E., Van Zyl-Smit R., Adam B. K., Fattaar A. B. et al. (1998) Hereditary nephropathic systemic amyloidosis caused by a novel variant apolipoprotein AI. Kidney Int. 53: 276-281
    • (1998) Kidney Int. , vol.53 , pp. 276-281
    • Persey, M.R.1    Booth, D.R.2    Booth, S.E.3    Van Zyl-Smit, R.4    Adam, B.K.5    Fattaar, A.B.6
  • 72
    • 0031907376 scopus 로고    scopus 로고
    • Hereditary hepatic and systemic amyloidosis caused by a novel variant apolipoprotein AI
    • 72 Booth D. R., Tan S. Y., Booth S. E., Tennent G. A., Hutchinson W. L., Hsuan J. J. et al. (1998) Hereditary hepatic and systemic amyloidosis caused by a novel variant apolipoprotein AI. Kidney Int. 53: 276-281
    • (1998) Kidney Int. , vol.53 , pp. 276-281
    • Booth, D.R.1    Tan, S.Y.2    Booth, S.E.3    Tennent, G.A.4    Hutchinson, W.L.5    Hsuan, J.J.6
  • 76
    • 0026462953 scopus 로고
    • Pulmonary vascular amyloidosis in aged dogs: A new form of spontaneously occurring amyloidosis derived from apolipoprotein AI
    • 76 Johnson K. H., Sletten K., Hayden D. W., O'Brien T. D., Roertgen K. E. and Westermark P. (1992) Pulmonary vascular amyloidosis in aged dogs: a new form of spontaneously occurring amyloidosis derived from apolipoprotein AI. Am. J. Pathol. 141: 1013-1019
    • (1992) Am. J. Pathol. , vol.141 , pp. 1013-1019
    • Johnson, K.H.1    Sletten, K.2    Hayden, D.W.3    O'Brien, T.D.4    Roertgen, K.E.5    Westermark, P.6
  • 79
    • 0032548464 scopus 로고    scopus 로고
    • Structural analysis of apolipoprotein AI: Effects of amino and carboxy-terminal deletions on the lipid-free structure
    • 79 Rogers D. P., Roberts L. M., Lebowitz J., Engler J. A. and Brouillette C. G. (1998) Structural analysis of apolipoprotein AI: effects of amino and carboxy-terminal deletions on the lipid-free structure. Biochemistry. 37: 945-955
    • (1998) Biochemistry. , vol.37 , pp. 945-955
    • Rogers, D.P.1    Roberts, L.M.2    Lebowitz, J.3    Engler, J.A.4    Brouillette, C.G.5
  • 80
    • 0026642154 scopus 로고
    • In vivo metabolism of a mutant apolipoprotein. apoA-Iowa, associated with hypoalphalipoproteinemia and hereditary systemic amyloidosis
    • 80 Rader D. J., Gregg R. E., Meng M. S., Schaefer J. R., Zech L. A., Benson M. D. et al. (1992) In vivo metabolism of a mutant apolipoprotein. apoA-Iowa, associated with hypoalphalipoproteinemia and hereditary systemic amyloidosis. J. Lipid Res. 33: 755-763
    • (1992) J. Lipid Res. , vol.33 , pp. 755-763
    • Rader, D.J.1    Gregg, R.E.2    Meng, M.S.3    Schaefer, J.R.4    Zech, L.A.5    Benson, M.D.6
  • 81
    • 0027172984 scopus 로고
    • In vivo metabolism of a mutant form of apolipoprotein A-I, apo A-I Milano, associated with familial hypoalphalipoproteinemia
    • 81 Roma P., Gregg E., Meng M. S., Ronan R., Zech L. A., Franceschini G. et al. (1993) In vivo metabolism of a mutant form of apolipoprotein A-I, apo A-I Milano, associated with familial hypoalphalipoproteinemia. J. Clin. Invest. 91: 1445-1452
    • (1993) J. Clin. Invest. , vol.91 , pp. 1445-1452
    • Roma, P.1    Gregg, E.2    Meng, M.S.3    Ronan, R.4    Zech, L.A.5    Franceschini, G.6
  • 83
    • 0021675938 scopus 로고
    • Sites and mechanisms of uptake and degradation of high density and low density lipoproteins
    • 83 Pittman R. C. and Steiberg D. (1984) Sites and mechanisms of uptake and degradation of high density and low density lipoproteins. J. Lipid. Res. 25: 1577-1585
    • (1984) J. Lipid. Res. , vol.25 , pp. 1577-1585
    • Pittman, R.C.1    Steiberg, D.2
  • 84
    • 0029894150 scopus 로고    scopus 로고
    • Calcium dependent binding of the plasma protein Apolipoprotein A-I to two members of the annexin family
    • 84 Brownawell A. M. and Creutz C. E. (1996) Calcium dependent binding of the plasma protein Apolipoprotein A-I to two members of the annexin family. Biochemistry 35: 6839-6845
    • (1996) Biochemistry , vol.35 , pp. 6839-6845
    • Brownawell, A.M.1    Creutz, C.E.2
  • 87
    • 1542528944 scopus 로고    scopus 로고
    • Protoglycans and the extracellular matrix in amyloidosis
    • 87 Magnus J. H. and Stenstad T. (1997) Protoglycans and the extracellular matrix in amyloidosis. Amyloid: Int. J. Exp. Clin. Invest. 4: 121-134
    • (1997) Amyloid: Int. J. Exp. Clin. Invest. , vol.4 , pp. 121-134
    • Magnus, J.H.1    Stenstad, T.2
  • 88
    • 0028170818 scopus 로고
    • Cell biology of the amyloid beta-protein precursor and the mechanism of Alzheimer's disease
    • 88 Selkoe D. J. (1994) Cell biology of the amyloid beta-protein precursor and the mechanism of Alzheimer's disease. Annu. Rev. Cell Biol. 10: 373-403
    • (1994) Annu. Rev. Cell Biol. , vol.10 , pp. 373-403
    • Selkoe, D.J.1
  • 89
    • 0032084472 scopus 로고    scopus 로고
    • Structural and kinetic features of amyloid β-protein fibrillogenesis
    • 89 Teplow D. B. (1998) Structural and kinetic features of amyloid β-protein fibrillogenesis. Amyloid: Int. J. Exp. Clin. Invest. 5: 121-142
    • (1998) Amyloid: Int. J. Exp. Clin. Invest. , vol.5 , pp. 121-142
    • Teplow, D.B.1
  • 90
    • 0027447286 scopus 로고
    • Neurodegeneration induced by beta-amyloid peptides in vitro: The role of peptide assembly state
    • 90 Pike C. J., Burdick D., Walencewicz A. J., Glabe C. G. and Cotman C. W. (1993) Neurodegeneration induced by beta-amyloid peptides in vitro: the role of peptide assembly state. J. Neurosci. 13: 1676-1687
    • (1993) J. Neurosci. , vol.13 , pp. 1676-1687
    • Pike, C.J.1    Burdick, D.2    Walencewicz, A.J.3    Glabe, C.G.4    Cotman, C.W.5
  • 91
    • 0028172886 scopus 로고
    • β-Amyloid neurotoxicity requires fibril formation and is inhibited by Congo red
    • 91 Lorenzo A, and Yankner B. A. (1994) β-Amyloid neurotoxicity requires fibril formation and is inhibited by Congo red. Proc. Natl. Acad. Sci. USA 91: 12243-12247
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 12243-12247
    • Lorenzo, A.1    Yankner, B.A.2
  • 92
    • 0030808462 scopus 로고    scopus 로고
    • Aggregated Amyloid-β protein induces cortical neuronal apoptosis and concomitant 'apoptotic' pattern of gene induction
    • 92 Estus S., Tucker H. M., van Rooyen C., Wright S., Brigham E. F., Wogulis M. et al. (1997) Aggregated Amyloid-β protein induces cortical neuronal apoptosis and concomitant 'apoptotic' pattern of gene induction. J. Neuroscience 17: 7736-7745
    • (1997) J. Neuroscience , vol.17 , pp. 7736-7745
    • Estus, S.1    Tucker, H.M.2    Van Rooyen, C.3    Wright, S.4    Brigham, E.F.5    Wogulis, M.6
  • 93
    • 0028210761 scopus 로고
    • Increased immunoreactivity for Jun and Fos-related proteins in AD: Association with pathology
    • 93 Anderson A. J., Cummings B. J. and Cotman C. W (1994) Increased immunoreactivity for Jun and Fos-related proteins in AD: association with pathology. Exp. Neurol. 125: 286-295
    • (1994) Exp. Neurol. , vol.125 , pp. 286-295
    • Anderson, A.J.1    Cummings, B.J.2    Cotman, C.W.3
  • 94
    • 0027191973 scopus 로고
    • Apoptosis-mediated neurotoxicity induced by chronic application of β amyloid fragment 25-35
    • 94 Forloni G., Chiesa R., Smiroldo S., Verga L., Salmona M. and Tagliavini F. (1993) Apoptosis-mediated neurotoxicity induced by chronic application of β amyloid fragment 25-35. Neuroreport 4: 523-526
    • (1993) Neuroreport , vol.4 , pp. 523-526
    • Forloni, G.1    Chiesa, R.2    Smiroldo, S.3    Verga, L.4    Salmona, M.5    Tagliavini, F.6
  • 95
    • 0021338217 scopus 로고
    • Phosphorylation affects the ability of tau protein to promote microtubule assembly
    • 95 Lindwall G. and Cole R. D. (1986) Phosphorylation affects the ability of tau protein to promote microtubule assembly. J. Biol. Chem. 259: 5301-5305
    • (1986) J. Biol. Chem. , vol.259 , pp. 5301-5305
    • Lindwall, G.1    Cole, R.D.2
  • 96
    • 0031824782 scopus 로고    scopus 로고
    • Aging renders the brain vulnerable to amyloid b-protein neurotoxicity
    • 96 Geula C., Wu C. K., Saroff D., Lorenzo A., Yuan M. and Yanker B. A. (1998) Aging renders the brain vulnerable to amyloid b-protein neurotoxicity. Nature Med. 4: 827-831
    • (1998) Nature Med. , vol.4 , pp. 827-831
    • Geula, C.1    Wu, C.K.2    Saroff, D.3    Lorenzo, A.4    Yuan, M.5    Yanker, B.A.6
  • 97
    • 0013617842 scopus 로고    scopus 로고
    • Amyloid fibril toxicity
    • CIBA Symposium No. 199, Bock G. R. and Goode J. A. (eds), Wiley, Chichester
    • 97 Pepys M. B. (1996) Amyloid fibril toxicity. In: CIBA Symposium No. 199, The Nature and Origin of Amyloid Fibrils, pp. 44-45, Bock G. R. and Goode J. A. (eds), Wiley, Chichester
    • (1996) The Nature and Origin of Amyloid Fibrils , pp. 44-45
    • Pepys, M.B.1
  • 98
    • 11544279355 scopus 로고    scopus 로고
    • Diffusible non fibrillar ligands derived from AβI 42 are potent central nervous system neurotoxins
    • 98 Lambert M. P., Barlow A. K., Chromy B. A., Edwards C., Freed R. and Liosatos M. (1998) Diffusible non fibrillar ligands derived from AβI 42 are potent central nervous system neurotoxins. Proc. Natl. Acad. Sci. USA 95: 6448-6453
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 6448-6453
    • Lambert, M.P.1    Barlow, A.K.2    Chromy, B.A.3    Edwards, C.4    Freed, R.5    Liosatos, M.6
  • 99
    • 0030723983 scopus 로고    scopus 로고
    • Binding of β-amyloid to the p75 neurotrophin receptor induces apoptosis. A possible mechanism for Alzheimer's disease
    • 99 Yaar M., Zhai S., Pilch P. F., Doyle S. M., Eisenhauer P. B., Fine R. E. et al. (1997) Binding of β-amyloid to the p75 neurotrophin receptor induces apoptosis. A possible mechanism for Alzheimer's disease. J. Clin. Invest. 100: 2333-2340
    • (1997) J. Clin. Invest. , vol.100 , pp. 2333-2340
    • Yaar, M.1    Zhai, S.2    Pilch, P.F.3    Doyle, S.M.4    Eisenhauer, P.B.5    Fine, R.E.6
  • 100
    • 0013615899 scopus 로고    scopus 로고
    • RAGE and amyloid β peptide neurotoxicity in Alzheimer's disease
    • 100 Yan S. D., Chen X., Fu J., Chen M., Zhu H., Roher A. et al. (1996) RAGE and amyloid β peptide neurotoxicity in Alzheimer's disease. Nature 382: 716-719
    • (1996) Nature , vol.382 , pp. 716-719
    • Yan, S.D.1    Chen, X.2    Fu, J.3    Chen, M.4    Zhu, H.5    Roher, A.6
  • 101
    • 0030952217 scopus 로고    scopus 로고
    • Intracellular generation and accumulation of Aβ terminating amino acid 42
    • 101 Wild-Bode C., Yamazaki T., Capell A., Leimer U., Steiner H., Ihara Y. et al. (1997) Intracellular generation and accumulation of Aβ terminating amino acid 42. J. Biol. Chem. 272: 16085-16088
    • (1997) J. Biol. Chem. , vol.272 , pp. 16085-16088
    • Wild-Bode, C.1    Yamazaki, T.2    Capell, A.3    Leimer, U.4    Steiner, H.5    Ihara, Y.6
  • 102
    • 0013079948 scopus 로고    scopus 로고
    • An intracellular protein that binds amyloid-β peptide and mediates neurotoxicity in Alzheimer's disease
    • 102 Yan S. D., Soto C., Chen X., Zhu H., Al-Mohanna F., Collison K. et al. (1997) An intracellular protein that binds amyloid-β peptide and mediates neurotoxicity in Alzheimer's disease. Nature 389: 689-695
    • (1997) Nature , vol.389 , pp. 689-695
    • Yan, S.D.1    Soto, C.2    Chen, X.3    Zhu, H.4    Al-Mohanna, F.5    Collison, K.6
  • 104
    • 0028303844 scopus 로고
    • Pancreatic islet cell toxicity of amylin associated with type-2 diabetes mellitus
    • 104 Lorenzo A., Razzaboni R., Weir G. D. and Yanker B. A. (1994) Pancreatic islet cell toxicity of amylin associated with type-2 diabetes mellitus. Nature 368: 756-760
    • (1994) Nature , vol.368 , pp. 756-760
    • Lorenzo, A.1    Razzaboni, R.2    Weir, G.D.3    Yanker, B.A.4
  • 105
    • 0013620335 scopus 로고    scopus 로고
    • Nascent human islet amyloid polypeptide is more cytotoxic and causes more membrane damage than mature fibrils
    • Mayo Clinic, Rochester, MN
    • 105 Janson J., Ashley R. and Butler P. (1998) Nascent human islet amyloid polypeptide is more cytotoxic and causes more membrane damage than mature fibrils. VIII International Symposium on Amyloidosis, Mayo Clinic, Rochester, MN, p. 199
    • (1998) VIII International Symposium on Amyloidosis , pp. 199
    • Janson, J.1    Ashley, R.2    Butler, P.3
  • 106
    • 0013566367 scopus 로고    scopus 로고
    • Fibriliar human islet amyloid polypeptide 'amylin' is cytotoxic to clonal cells and isolated B-cells but not to pancreatic islet in vitro
    • Mayo Clinic, Rochester, MN
    • 106 Higham C. E., Badman M. K., Morris J. F. and Clark A. (1998) Fibriliar human islet amyloid polypeptide 'amylin' is cytotoxic to clonal cells and isolated B-cells but not to pancreatic islet in vitro. VIII International Symposium on Amyloidosis, Mayo Clinic, Rochester, MN, p. 220
    • (1998) VIII International Symposium on Amyloidosis , pp. 220
    • Higham, C.E.1    Badman, M.K.2    Morris, J.F.A.3    Clark, A.4
  • 107
    • 0028172886 scopus 로고
    • Beta-amyloid neurotoxicity requires fibril formation and is inhibited by Congo red
    • 107 Lorenzo A. and Yankner B. A. (1994) Beta-amyloid neurotoxicity requires fibril formation and is inhibited by Congo red. Proc. Natl. Acad. Sci. USA 91: 12243-12247
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 12243-12247
    • Lorenzo, A.1    Yankner, B.A.2
  • 108
    • 0028914019 scopus 로고
    • Interaction of the anthracycline 4′-iodo-4′-deoxydoxorubicin with amyloid fibrils; inhibition of amyloidogenesis
    • 108 Merlini G., Ascari E., Amboldi N., Bellotti V., Arbustini E., Perfetti V. et al. (1995) Interaction of the anthracycline 4′-iodo-4′-deoxydoxorubicin with amyloid fibrils; inhibition of amyloidogenesis. Proc. Natl. Acad. Sci. USA 92: 2959-2963
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 2959-2963
    • Merlini, G.1    Ascari, E.2    Amboldi, N.3    Bellotti, V.4    Arbustini, E.5    Perfetti, V.6
  • 109
    • 0030905125 scopus 로고    scopus 로고
    • Rifampicin inhibits the toxicity of pre-aggregated peptides by binding to peptide fibrils and preventing amyloid-cell interaction
    • 109 Tomiyama T., Kaneko H., Kataoka K., Asano S. and Endo N. (1997) Rifampicin inhibits the toxicity of pre-aggregated peptides by binding to peptide fibrils and preventing amyloid-cell interaction. Biochem. J. 322: 859-865
    • (1997) Biochem. J. , vol.322 , pp. 859-865
    • Tomiyama, T.1    Kaneko, H.2    Kataoka, K.3    Asano, S.4    Endo, N.5
  • 110
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • 110 Nicholls A., Sharp K. A. and Honig B. (1991) Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins Struct. Funct. Genet. 11: 281-296
    • (1991) Proteins Struct. Funct. Genet. , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 111
    • 0025831493 scopus 로고
    • Refined structure of the human histocompatibility antigen HLA-A2 at 2.6 å resolution
    • 111 Saper M. A., Bjiorkman P. J. and Wiley D. C. (1991) Refined structure of the human histocompatibility antigen HLA-A2 at 2.6 Å resolution. J. Mol. Biol. 219: 277-319
    • (1991) J. Mol. Biol. , vol.219 , pp. 277-319
    • Saper, M.A.1    Bjiorkman, P.J.2    Wiley, D.C.3
  • 112
    • 0013566269 scopus 로고
    • Radiological evaluation of beta-2 microglobulin amyloidosis
    • Gejyo F., Brancaccio D. and Bardin T. (eds), Wichting, Milano
    • 112 Bardin T., Bellini F. and Laredo J.D. (1989) Radiological evaluation of beta-2 microglobulin amyloidosis. In: Dialysis Amyloidosis, pp. 91-100, Gejyo F., Brancaccio D. and Bardin T. (eds), Wichting, Milano
    • (1989) Dialysis Amyloidosis , pp. 91-100
    • Bardin, T.1    Bellini, F.2    Laredo, J.D.3


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