메뉴 건너뛰기




Volumn 330, Issue 5, 2003, Pages 943-954

A systematic investigation into the effect of protein destabilisation on beta 2-microglobulin amyloid formation

Author keywords

Amyloidosis; Intermediates; Stability; Thioflavin T; 2 microglobulin

Indexed keywords

AMYLOID; BETA 2 MICROGLOBULIN; CONGO RED; THIOFLAVINE;

EID: 0038575395     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(03)00687-9     Document Type: Article
Times cited : (136)

References (52)
  • 1
    • 0033200063 scopus 로고    scopus 로고
    • Protein misfolding, evolution and disease
    • Dobson C.M. Protein misfolding, evolution and disease. Trends Biochem. Sci. 24:1999;329-332.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 329-332
    • Dobson, C.M.1
  • 3
    • 0036377156 scopus 로고    scopus 로고
    • Amyloid-fibril formation
    • Zerovnik A. Amyloid-fibril formation. Eur. J. Biochem. 269:2002;3362-3371.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 3362-3371
    • Zerovnik, A.1
  • 5
    • 0035826234 scopus 로고    scopus 로고
    • Amyloid fibrils from muscle myoglobin
    • Fandrich M., Fletcher M.A., Dobson C.M. Amyloid fibrils from muscle myoglobin. Nature. 410:2001;165-166.
    • (2001) Nature , vol.410 , pp. 165-166
    • Fandrich, M.1    Fletcher, M.A.2    Dobson, C.M.3
  • 8
    • 0030801746 scopus 로고    scopus 로고
    • The structure of amyloid fibrils by electron microscopy and X-ray diffraction
    • Sunde M., Blake C. The structure of amyloid fibrils by electron microscopy and X-ray diffraction. Advan. Protein Chem. 50:1997;123-159.
    • (1997) Advan. Protein Chem. , vol.50 , pp. 123-159
    • Sunde, M.1    Blake, C.2
  • 9
    • 0032849874 scopus 로고    scopus 로고
    • Quantification of beta-sheet amyloid fibril structures with thioflavin T
    • LeVine H. Quantification of beta-sheet amyloid fibril structures with thioflavin T. Methods Enzymol. 309:1999;274-284.
    • (1999) Methods Enzymol. , vol.309 , pp. 274-284
    • LeVine, H.1
  • 11
    • 0030004644 scopus 로고    scopus 로고
    • The acid-mediated denaturation pathway of transthyretin yields a conformational intermediate that can self-assemble into amyloid
    • Lai Z.H., Colon W., Kelly J.W. The acid-mediated denaturation pathway of transthyretin yields a conformational intermediate that can self-assemble into amyloid. Biochemistry. 35:1996;6470-6482.
    • (1996) Biochemistry , vol.35 , pp. 6470-6482
    • Lai, Z.H.1    Colon, W.2    Kelly, J.W.3
  • 14
    • 0031056829 scopus 로고    scopus 로고
    • Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis
    • Booth D.R., Sunde M., Bellotti V., Robinson C.V., Hutchinson W.L., Fraser P.E., et al. Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis. Nature. 385:1997;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
  • 15
    • 0036396520 scopus 로고    scopus 로고
    • Does the location of mutations determine the ability to form amyloid fibrils
    • Ramirez-Alvarado M., Regan L. Does the location of mutations determine the ability to form amyloid fibrils. J. Mol. Biol. 323:2002;17-22.
    • (2002) J. Mol. Biol. , vol.323 , pp. 17-22
    • Ramirez-Alvarado, M.1    Regan, L.2
  • 17
    • 0022391603 scopus 로고
    • A new form of amyloid protein associated with chronic hemodialysis was identified as beta-2-microglobulin
    • Gejyo F., Yamada T., Odani S., Nakagawa Y., Arakawa M., Kunitomo T., et al. A new form of amyloid protein associated with chronic hemodialysis was identified as beta-2-microglobulin. Biochem. Biophys. Res. Commun. 129:1985;701-706.
    • (1985) Biochem. Biophys. Res. Commun. , vol.129 , pp. 701-706
    • Gejyo, F.1    Yamada, T.2    Odani, S.3    Nakagawa, Y.4    Arakawa, M.5    Kunitomo, T.6
  • 18
    • 0000877963 scopus 로고    scopus 로고
    • Beta 2-microglobulin amyloidosis
    • Argiles A. Beta 2-microglobulin amyloidosis. Nephrology. 2:1996;373-386.
    • (1996) Nephrology , vol.2 , pp. 373-386
    • Argiles, A.1
  • 19
    • 0035128916 scopus 로고    scopus 로고
    • Beta-2-microglobulin-derived amyloidosis: An update
    • Floege J., Ketteler M. Beta-2-microglobulin-derived amyloidosis: an update. Kidney Int. 59:2001;164-171.
    • (2001) Kidney Int. , vol.59 , pp. 164-171
    • Floege, J.1    Ketteler, M.2
  • 20
    • 0025831493 scopus 로고
    • Refined structure of the human histocompatibility antigen HLA-A2 at 2.6 Å resolution
    • Saper M.A., Bjorkman P.J., Wiley D.C. Refined structure of the human histocompatibility antigen HLA-A2 at 2.6 Å resolution. J. Mol. Biol. 219:1991;277-319.
    • (1991) J. Mol. Biol. , vol.219 , pp. 277-319
    • Saper, M.A.1    Bjorkman, P.J.2    Wiley, D.C.3
  • 21
    • 0037162520 scopus 로고    scopus 로고
    • Crystal structure of monomeric human beta-2-microglobulin reveals clues to its amyloidogenic properties
    • Trinh C.H., Smith D.P., Kalverda A.P., Phillips S.E., Radford S.E. Crystal structure of monomeric human beta-2-microglobulin reveals clues to its amyloidogenic properties. Proc. Natl Acad. Sci. USA. 99:2002;9771-9776.
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 9771-9776
    • Trinh, C.H.1    Smith, D.P.2    Kalverda, A.P.3    Phillips, S.E.4    Radford, S.E.5
  • 22
    • 0024307776 scopus 로고
    • Collagen-binding affinity of beta-2-microglobulin, a preprotein of hemodialysis-associated amyloidosis
    • Homma N., Gejyo F., Isemura M., Arakawa M. Collagen-binding affinity of beta-2-microglobulin, a preprotein of hemodialysis-associated amyloidosis. Nephron. 53:1989;37-40.
    • (1989) Nephron , vol.53 , pp. 37-40
    • Homma, N.1    Gejyo, F.2    Isemura, M.3    Arakawa, M.4
  • 23
    • 0032532946 scopus 로고    scopus 로고
    • Beta-2-microglobulin can be refolded into a native state from ex vivo amyloid fibrils
    • Bellotti V., Stoppini M., Mangione P., Sunde M., Robinson C., Asti L., et al. Beta-2-microglobulin can be refolded into a native state from ex vivo amyloid fibrils. Eur. J. Biochem. 258:1998;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
  • 25
    • 0035955555 scopus 로고    scopus 로고
    • Beta-2-microglobulin and its deamidated variant, N17D form amyloid fibrils with a range of morphologies in vitro
    • Kad N.M., Thomson N.H., Smith D.P., Smith D.A., Radford S.E. Beta-2-microglobulin and its deamidated variant, N17D form amyloid fibrils with a range of morphologies in vitro. J. Mol. Biol. 313:2001;559-571.
    • (2001) J. Mol. Biol. , vol.313 , pp. 559-571
    • Kad, N.M.1    Thomson, N.H.2    Smith, D.P.3    Smith, D.A.4    Radford, S.E.5
  • 26
    • 0034846252 scopus 로고    scopus 로고
    • Role of the single disulphide bond of beta-2-microglobulin in amyloidosis in vitro
    • Smith D.P., Radford S.E. Role of the single disulphide bond of beta-2-microglobulin in amyloidosis in vitro. Protein Sci. 10:2001;1775-1784.
    • (2001) Protein Sci. , vol.10 , pp. 1775-1784
    • Smith, D.P.1    Radford, S.E.2
  • 27
    • 0037077209 scopus 로고    scopus 로고
    • Conformation of beta-2-microglobulin amyloid fibrils analyzed by reduction of the disulfide bond
    • Hong D.P., Gozu M., Hasegawa K., Naiki H., Goto Y. Conformation of beta-2-microglobulin amyloid fibrils analyzed by reduction of the disulfide bond. J. Biol. Chem. 277:2002;21554-21560.
    • (2002) J. Biol. Chem. , vol.277 , pp. 21554-21560
    • Hong, D.P.1    Gozu, M.2    Hasegawa, K.3    Naiki, H.4    Goto, Y.5
  • 29
    • 0036708005 scopus 로고    scopus 로고
    • The role of disulfide bond in the amyloidogenic state of beta 2-microglobulin studied by heteronuclear NMR
    • Katou H., Kanno T., Hoshino M., Hagihara Y., Tanaka H., Kawai T., et al. The role of disulfide bond in the amyloidogenic state of beta 2-microglobulin studied by heteronuclear NMR. Protein Sci. 11:2002;2218-2229.
    • (2002) Protein Sci. , vol.11 , pp. 2218-2229
    • Katou, H.1    Kanno, T.2    Hoshino, M.3    Hagihara, Y.4    Tanaka, H.5    Kawai, T.6
  • 30
    • 0037819879 scopus 로고    scopus 로고
    • Hierarchical assembly of beta-2-microglobulin amyloid in vitro revealed by atomic force microscopy
    • Kad, N. M., Smith, D. P., Myers, S. L., Smith, D. A., Radford, S. E., Thomson, N. H. (2003) Hierarchical assembly of beta-2-microglobulin amyloid in vitro revealed by atomic force microscopy. J. Mol. Biol. 330, 935-941.
    • (2003) J. Mol. Biol. , vol.330 , pp. 935-941
    • Kad, N.M.1    Smith, D.P.2    Myers, S.L.3    Smith, D.A.4    Radford, S.E.5    Thomson, N.H.6
  • 31
    • 18244412979 scopus 로고    scopus 로고
    • Removal of the N-terminal hexapeptide from human beta-2-microglobulin facilitates protein aggregation and fibril formation
    • Esposito G., Michelutti R., Verdone G., Viglino P., Hernandez H., Robinson C.V., et al. Removal of the N-terminal hexapeptide from human beta-2-microglobulin facilitates protein aggregation and fibril formation. Protein Sci. 9:2000;831-845.
    • (2000) Protein Sci. , vol.9 , pp. 831-845
    • Esposito, G.1    Michelutti, R.2    Verdone, G.3    Viglino, P.4    Hernandez, H.5    Robinson, C.V.6
  • 32
    • 0035367287 scopus 로고    scopus 로고
    • Kidney dialysis-associated amyloidosis: A molecular role for copper in fibre formation
    • Morgan C.J., Gelfand M., Atreya C., Miranker A.D. Kidney dialysis-associated amyloidosis: a molecular role for copper in fibre formation. J. Mol. Biol. 309:2001;339-345.
    • (2001) J. Mol. Biol. , vol.309 , pp. 339-345
    • Morgan, C.J.1    Gelfand, M.2    Atreya, C.3    Miranker, A.D.4
  • 33
    • 0035861649 scopus 로고    scopus 로고
    • A partially structured species of beta 2-microglobulin is significantly populated under physiological conditions and involved in fibrillogenesis
    • Chiti F., De Lorenzi E., Grossi S., Mangione P., Giorgetti S., Caccialanza G., et al. A partially structured species of beta 2-microglobulin is significantly populated under physiological conditions and involved in fibrillogenesis. J. Biol. Chem. 276:2001;46714-46721.
    • (2001) J. Biol. Chem. , vol.276 , pp. 46714-46721
    • Chiti, F.1    De Lorenzi, E.2    Grossi, S.3    Mangione, P.4    Giorgetti, S.5    Caccialanza, G.6
  • 34
    • 0036172742 scopus 로고    scopus 로고
    • The intrachain disulfide bond of beta-2-microglobulin is not essential for the immunoglobulin fold at neutral pH, but is essential for amyloid fibril formation at acidic pH
    • Ohashi Y., Hagihara Y., Kozhukh G., Hoshino M., Hasegawa K., Yamaguchi I., et al. The intrachain disulfide bond of beta-2-microglobulin is not essential for the immunoglobulin fold at neutral pH, but is essential for amyloid fibril formation at acidic pH. J. Biochem. 131:2002;45-52.
    • (2002) J. Biochem. , vol.131 , pp. 45-52
    • Ohashi, Y.1    Hagihara, Y.2    Kozhukh, G.3    Hoshino, M.4    Hasegawa, K.5    Yamaguchi, I.6
  • 35
    • 0037227173 scopus 로고    scopus 로고
    • Amyloid-forming peptides from beta 2-microglobulin - Insights into the mechanism of fibril formation in vitro
    • Jones S., Manning J., Kad N.M., Radford S.E. Amyloid-forming peptides from beta 2-microglobulin - insights into the mechanism of fibril formation in vitro. J. Mol. Biol. 325:2003;249-257.
    • (2003) J. Mol. Biol. , vol.325 , pp. 249-257
    • Jones, S.1    Manning, J.2    Kad, N.M.3    Radford, S.E.4
  • 37
    • 0035896018 scopus 로고    scopus 로고
    • Detection of two partially structured species in the folding process of the amyloidogenic protein beta 2-microglobulin
    • Chiti F., Mangione P., Andreola A., Giorgetti S., Stefani M., Dobson C.M., et al. Detection of two partially structured species in the folding process of the amyloidogenic protein beta 2-microglobulin. J. Mol. Biol. 307:2001;379-391.
    • (2001) J. Mol. Biol. , vol.307 , pp. 379-391
    • Chiti, F.1    Mangione, P.2    Andreola, A.3    Giorgetti, S.4    Stefani, M.5    Dobson, C.M.6
  • 39
    • 0028305304 scopus 로고
    • A role for destabilizing amino-acid replacements in light-chain amyloidosis
    • Hurle M.R., Helms L.R., Li L., Chan W.N., Wetzel R. A role for destabilizing amino-acid replacements in light-chain amyloidosis. Proc. Natl Acad. Sci. USA. 91:1994;5446-5450.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 5446-5450
    • Hurle, M.R.1    Helms, L.R.2    Li, L.3    Chan, W.N.4    Wetzel, R.5
  • 40
    • 0033020141 scopus 로고    scopus 로고
    • Physicochemical consequences of amino acid variations that contribute to fibril formation by immunoglobulin light chains
    • Raffen R., Dieckman L.J., Szpunar M., Wunschl C., Pokkuluri P.R., Dave P., et al. Physicochemical consequences of amino acid variations that contribute to fibril formation by immunoglobulin light chains. Protein Sci. 8:1999;509-517.
    • (1999) Protein Sci. , vol.8 , pp. 509-517
    • Raffen, R.1    Dieckman, L.J.2    Szpunar, M.3    Wunschl, C.4    Pokkuluri, P.R.5    Dave, P.6
  • 41
    • 0035902492 scopus 로고    scopus 로고
    • Probing the mechanism of insulin fibril formation with insulin mutants
    • Nielsen L., Frokjaer S., Brange J., Uversky V.N., Fink A.L. Probing the mechanism of insulin fibril formation with insulin mutants. Biochemistry. 40:2001;8397-8409.
    • (2001) Biochemistry , vol.40 , pp. 8397-8409
    • Nielsen, L.1    Frokjaer, S.2    Brange, J.3    Uversky, V.N.4    Fink, A.L.5
  • 42
    • 0037058942 scopus 로고    scopus 로고
    • Sequence-dependent denaturation energetics: A major determinant in amyloid disease diversity
    • Dec 10; 99 Suppl, 4, 16427-16432
    • Hammarstrom P., Jiang X., Hurshman A.R., Powers E.T., Kelly J.W. Sequence-dependent denaturation energetics: a major determinant in amyloid disease diversity. Proc. Natl Acad. Sci. USA. 99:2002;16427-16432. Dec 10; 99 Suppl, 4, 16427-16432.
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 16427-16432
    • Hammarstrom, P.1    Jiang, X.2    Hurshman, A.R.3    Powers, E.T.4    Kelly, J.W.5
  • 43
    • 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. 97:2000;8979-8984.
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 8979-8984
    • Ramirez-Alvarado, M.1    Merkel, J.S.2    Regan, L.3
  • 44
    • 0037183496 scopus 로고    scopus 로고
    • Formation of a copper specific binding site in non-native states of beta-2-microglobulin
    • Eakin C.M., Knight J.D., Morgan C.J., Gelfand M.A., Miranker A.D. Formation of a copper specific binding site in non-native states of beta-2-microglobulin. Biochemistry. 41:2002;10646-10656.
    • (2002) Biochemistry , vol.41 , pp. 10646-10656
    • Eakin, C.M.1    Knight, J.D.2    Morgan, C.J.3    Gelfand, M.A.4    Miranker, A.D.5
  • 45
    • 0035834456 scopus 로고    scopus 로고
    • Both the environment and somatic mutations govern the aggregation pathway of pathogenic immunoglobulin light chain
    • Davis D.P., Gallo G., Vogen S.M., Dul J.L., Sciarretta K.L., Kumar A., et al. Both the environment and somatic mutations govern the aggregation pathway of pathogenic immunoglobulin light chain. J. Mol. Biol. 313:2001;1021-1034.
    • (2001) J. Mol. Biol. , vol.313 , pp. 1021-1034
    • Davis, D.P.1    Gallo, G.2    Vogen, S.M.3    Dul, J.L.4    Sciarretta, K.L.5    Kumar, A.6
  • 48
    • 0024448151 scopus 로고
    • Calculation of protein extinction coeffients from amino acid sequence data
    • Gill S., Von Hippel P.H. Calculation of protein extinction coeffients from amino acid sequence data. Anal. Biochem. 182:1989;319-326.
    • (1989) Anal. Biochem. , vol.182 , pp. 319-326
    • Gill, S.1    Von Hippel, P.H.2
  • 49
    • 0023697408 scopus 로고
    • Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants
    • Santoro M.M., Bolen D.W. Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants. Biochemistry. 27:1988;8063-8068.
    • (1988) Biochemistry , vol.27 , pp. 8063-8068
    • Santoro, M.M.1    Bolen, D.W.2
  • 50
    • 0034660206 scopus 로고    scopus 로고
    • The structure and stability of an HLA-A*0201/octameric tax peptide complex with an empty conserved peptide-N-terminal binding site
    • Khan A.R., Baker B.M., Ghosh P., Biddison W.E., Wiley D.C. The structure and stability of an HLA-A*0201/octameric tax peptide complex with an empty conserved peptide-N-terminal binding site. J. Immunol. 164:2000;6398-6405.
    • (2000) J. Immunol. , vol.164 , pp. 6398-6405
    • Khan, A.R.1    Baker, B.M.2    Ghosh, P.3    Biddison, W.E.4    Wiley, D.C.5
  • 52
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W., Sander C. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers. 22:1983;2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.