메뉴 건너뛰기




Volumn 401, Issue 2, 2010, Pages 286-297

Folding and fibrillogenesis: Clues from β2-microglobulin

Author keywords

Amyloid fibrils; Dialysis related amyloidosis; Folding intermediate; Protein thermodynamics

Indexed keywords

ALCOHOL; AMYLOID; BETA 2 MICROGLOBULIN; MUTANT PROTEIN; TRIFLUOROETHANOL; TRYPTOPHAN;

EID: 77955086949     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.06.016     Document Type: Article
Times cited : (33)

References (39)
  • 1
    • 0022391603 scopus 로고
    • A new form of amyloid protein associated with chronic hemodialysis was identified as beta2-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 beta2-microglobulin. Biochem. Biophys. Res. Commun. 1985, 129:701-706.
    • (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
  • 2
    • 0035896018 scopus 로고    scopus 로고
    • Detection of two partially structured species in the folding process of the amyloidogenic protein beta2-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 beta2-microglobulin. J. Mol. Biol. 2001, 307:379-391.
    • (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
  • 4
    • 41949130213 scopus 로고    scopus 로고
    • The controlling roles of Trp60 and Trp95 in β2-microglobulin function, folding and amyloid aggregation properties
    • Esposito G., Ricagno S., Corazza A., Rennella E., Gümral D., Mimmi M.C., et al. The controlling roles of Trp60 and Trp95 in β2-microglobulin function, folding and amyloid aggregation properties. J. Mol. Biol. 2008, 378:885-895.
    • (2008) J. Mol. Biol. , vol.378 , pp. 885-895
    • Esposito, G.1    Ricagno, S.2    Corazza, A.3    Rennella, E.4    Gümral, D.5    Mimmi, M.C.6
  • 5
    • 34547463005 scopus 로고    scopus 로고
    • Protein folding and unfolding studied at atomic resolution by fast two-dimensional NMR spectroscopy
    • Schanda P., Forge V., Brutscher B. Protein folding and unfolding studied at atomic resolution by fast two-dimensional NMR spectroscopy. Proc. Natl Acad. Sci. USA 2007, 104:11257-11262.
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 11257-11262
    • Schanda, P.1    Forge, V.2    Brutscher, B.3
  • 6
    • 77949320904 scopus 로고    scopus 로고
    • Native-unlike long-lived intermediates along the folding pathway of the amyloidogenic protein {beta}2-microglobulin revealed by real time 2D NMR
    • Corazza A., Rennella E., Schanda P., Mimmi M.C., Cutuil T., Raimondi S., et al. Native-unlike long-lived intermediates along the folding pathway of the amyloidogenic protein {beta}2-microglobulin revealed by real time 2D NMR. J. Biol. Chem. 2010, 285:5827-5835.
    • (2010) J. Biol. Chem. , vol.285 , pp. 5827-5835
    • Corazza, A.1    Rennella, E.2    Schanda, P.3    Mimmi, M.C.4    Cutuil, T.5    Raimondi, S.6
  • 7
    • 16244398884 scopus 로고    scopus 로고
    • Nuclear magnetic resonance characterization of the refolding intermediate of beta2-microglobulin trapped by non-native prolyl peptide bond
    • Kameda A., Hoshino M., Higurashi T., Takahashi S., Naiki H., Goto Y. Nuclear magnetic resonance characterization of the refolding intermediate of beta2-microglobulin trapped by non-native prolyl peptide bond. J. Mol. Biol. 2005, 348:383-397.
    • (2005) J. Mol. Biol. , vol.348 , pp. 383-397
    • Kameda, A.1    Hoshino, M.2    Higurashi, T.3    Takahashi, S.4    Naiki, H.5    Goto, Y.6
  • 8
    • 0346103697 scopus 로고    scopus 로고
    • Glycosaminoglycans enhance the trifluoroethanol-induced extension of beta2-microglobulin-related amyloid fibrils at a neutral pH
    • Yamamoto S., Yamaguchi I., Hasegawa K., Tsutsumi S., Goto Y., Gejyo F., Naiki H. Glycosaminoglycans enhance the trifluoroethanol-induced extension of beta2-microglobulin-related amyloid fibrils at a neutral pH. J. Am. Soc. Nephrol. 2004, 15:126-133.
    • (2004) J. Am. Soc. Nephrol. , vol.15 , pp. 126-133
    • Yamamoto, S.1    Yamaguchi, I.2    Hasegawa, K.3    Tsutsumi, S.4    Goto, Y.5    Gejyo, F.6    Naiki, H.7
  • 9
    • 0035980019 scopus 로고    scopus 로고
    • Conformational intermediate of the amyloidogenic protein beta 2-microglobulin at neutral pH
    • Heegaard N.H., Sen J.W., Kaarsholm N.C., Nissen M.H. Conformational intermediate of the amyloidogenic protein beta 2-microglobulin at neutral pH. J. Biol. Chem. 2001, 276:32657-32662.
    • (2001) J. Biol. Chem. , vol.276 , pp. 32657-32662
    • Heegaard, N.H.1    Sen, J.W.2    Kaarsholm, N.C.3    Nissen, M.H.4
  • 10
    • 33144467755 scopus 로고    scopus 로고
    • Amyloid formation under physiological conditions proceeds via a native-like folding intermediate
    • Jahn T.R., Parker M.J., Homans S.W., Radford S.E. Amyloid formation under physiological conditions proceeds via a native-like folding intermediate. Nat. Struct. Mol. Biol. 2006, 13:195-201.
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 195-201
    • Jahn, T.R.1    Parker, M.J.2    Homans, S.W.3    Radford, S.E.4
  • 11
    • 10744219788 scopus 로고    scopus 로고
    • Properties of some variants of human beta2-microglobulin and amyloidogenesis
    • Corazza A., Pettirossi F., Viglino P., Verdone G., Garcia J., Dumy P., et al. Properties of some variants of human beta2-microglobulin and amyloidogenesis. J. Biol. Chem. 2004, 279:9176-9189.
    • (2004) J. Biol. Chem. , vol.279 , pp. 9176-9189
    • Corazza, A.1    Pettirossi, F.2    Viglino, P.3    Verdone, G.4    Garcia, J.5    Dumy, P.6
  • 12
    • 0032444658 scopus 로고    scopus 로고
    • Trifluoroethanol and colleagues: co-solvents come of age. Recent studies with peptides and proteins
    • Buck M. Trifluoroethanol and colleagues: co-solvents come of age. Recent studies with peptides and proteins. Q. Rev. Biophys. 1998, 31:297-355.
    • (1998) Q. Rev. Biophys. , vol.31 , pp. 297-355
    • Buck, M.1
  • 13
    • 33748943122 scopus 로고    scopus 로고
    • Mechanism by which the amyloid-like fibrils of a beta 2-microglobulin fragment are induced by fluorine-substituted alcohols
    • Yamaguchi K., Naiki H., Goto Y. Mechanism by which the amyloid-like fibrils of a beta 2-microglobulin fragment are induced by fluorine-substituted alcohols. J. Mol. Biol. 2006, 363:279-288.
    • (2006) J. Mol. Biol. , vol.363 , pp. 279-288
    • Yamaguchi, K.1    Naiki, H.2    Goto, Y.3
  • 14
    • 33144471714 scopus 로고    scopus 로고
    • A systematic study of the effect of physiological factors on beta2-microglobulin amyloid formation at neutral pH
    • Myers S.L., Jones S., Jahn T.R., Morten I.J., Tennent G.A., Hewitt E.W., Radford S.E. A systematic study of the effect of physiological factors on beta2-microglobulin amyloid formation at neutral pH. Biochemistry 2006, 45:2311-2321.
    • (2006) Biochemistry , vol.45 , pp. 2311-2321
    • Myers, S.L.1    Jones, S.2    Jahn, T.R.3    Morten, I.J.4    Tennent, G.A.5    Hewitt, E.W.6    Radford, S.E.7
  • 15
    • 18244378561 scopus 로고    scopus 로고
    • The solution structure of human beta2-microglobulin reveals the prodromes of its amyloid transition
    • Verdone G., Corazza A., Viglino P., Pettirossi F., Giorgetti S., Mangione P., et al. The solution structure of human beta2-microglobulin reveals the prodromes of its amyloid transition. Protein Sci. 2002, 11:487-499.
    • (2002) Protein Sci. , vol.11 , pp. 487-499
    • Verdone, G.1    Corazza, A.2    Viglino, P.3    Pettirossi, F.4    Giorgetti, S.5    Mangione, P.6
  • 16
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: a program for display and analysis of macromolecular structures
    • Koradi R., Billeter M., Wüthrich K. MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graphics 1996, 14:51-55.
    • (1996) J. Mol. Graphics , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 17
    • 33646358424 scopus 로고    scopus 로고
    • HET-SOFAST NMR for fast detection of structural compactness and heterogeneity along polypeptide chains
    • Schanda P., Forge V., Brutscher B. HET-SOFAST NMR for fast detection of structural compactness and heterogeneity along polypeptide chains. Magn. Reson. Chem. 2006, 44:S177-S184.
    • (2006) Magn. Reson. Chem. , vol.44
    • Schanda, P.1    Forge, V.2    Brutscher, B.3
  • 18
    • 0038575395 scopus 로고    scopus 로고
    • A systematic investigation into the effect of protein destabilisation on beta 2-microglobulin amyloid formation
    • Smith D.P., Jones S., Serpell L.C., Sunde M., Radford S.E. A systematic investigation into the effect of protein destabilisation on beta 2-microglobulin amyloid formation. J. Mol. Biol. 2003, 330:943-954.
    • (2003) J. Mol. Biol. , vol.330 , pp. 943-954
    • Smith, D.P.1    Jones, S.2    Serpell, L.C.3    Sunde, M.4    Radford, S.E.5
  • 19
    • 67749124075 scopus 로고    scopus 로고
    • NMR-based characterization of a refolding intermediate of beta2-microglobulin labeled using a wheat germ cell-free system
    • Kameda A., Morita E.H., Sakurai K., Naiki H., Goto Y. NMR-based characterization of a refolding intermediate of beta2-microglobulin labeled using a wheat germ cell-free system. Protein Sci. 2009, 18:1592-1601.
    • (2009) Protein Sci. , vol.18 , pp. 1592-1601
    • Kameda, A.1    Morita, E.H.2    Sakurai, K.3    Naiki, H.4    Goto, Y.5
  • 20
    • 33644813233 scopus 로고    scopus 로고
    • A native to amyloidogenic transition regulated by a backbone trigger
    • Eakin C.M., Berman A.J., Miranker A.D. A native to amyloidogenic transition regulated by a backbone trigger. Nat. Struct. Mol. Biol. 2006, 13:202-208.
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 202-208
    • Eakin, C.M.1    Berman, A.J.2    Miranker, A.D.3
  • 21
    • 0035942986 scopus 로고    scopus 로고
    • Apolipoprotein E inhibits the depolymerization of beta2-microglobulin-related amyloid fibrils at a neutral pH
    • Yamaguchi I., Hasegawa K., Takahashi N., Gejyo F., Naiki H. Apolipoprotein E inhibits the depolymerization of beta2-microglobulin-related amyloid fibrils at a neutral pH. Biochemistry 2001, 40:8499-8507.
    • (2001) Biochemistry , vol.40 , pp. 8499-8507
    • Yamaguchi, I.1    Hasegawa, K.2    Takahashi, N.3    Gejyo, F.4    Naiki, H.5
  • 22
    • 52449088570 scopus 로고    scopus 로고
    • Lysophospholipids induce the nucleation and extension of beta2-microglobulin-related amyloid fibrils at a neutral pH
    • Ookoshi T., Hasegawa K., Ohhashi Y., Kimura H., Takahashi N., Yoshida H., et al. Lysophospholipids induce the nucleation and extension of beta2-microglobulin-related amyloid fibrils at a neutral pH. Nephrol. Dial. Transplant. 2008, 23:3247-3255.
    • (2008) Nephrol. Dial. Transplant. , vol.23 , pp. 3247-3255
    • Ookoshi, T.1    Hasegawa, K.2    Ohhashi, Y.3    Kimura, H.4    Takahashi, N.5    Yoshida, H.6
  • 23
    • 58149314012 scopus 로고    scopus 로고
    • Growth of beta(2)-microglobulin-related amyloid fibrils by non-esterified fatty acids at a neutral pH
    • Hasegawa K., Tsutsumi-Yasuhara S., Ookoshi T., Ohhashi Y., Kimura H., Takahashi N., et al. Growth of beta(2)-microglobulin-related amyloid fibrils by non-esterified fatty acids at a neutral pH. Biochem. J. 2008, 416:307-315.
    • (2008) Biochem. J. , vol.416 , pp. 307-315
    • Hasegawa, K.1    Tsutsumi-Yasuhara, S.2    Ookoshi, T.3    Ohhashi, Y.4    Kimura, H.5    Takahashi, N.6
  • 24
    • 18244412979 scopus 로고    scopus 로고
    • Removal of the N-terminal hexapeptide from human beta2-microglobulin facilitates protein aggregation and fibril formation
    • Esposito G., Michelutti R., Verdone G., Viglino P., Hernández H., Robinson C.V., et al. Removal of the N-terminal hexapeptide from human beta2-microglobulin facilitates protein aggregation and fibril formation. Protein Sci. 2000, 9:831-845.
    • (2000) Protein Sci. , vol.9 , pp. 831-845
    • Esposito, G.1    Michelutti, R.2    Verdone, G.3    Viglino, P.4    Hernández, H.5    Robinson, C.V.6
  • 25
    • 0344448273 scopus 로고
    • Coherence transfer by isotropic mixing: application to proton correlation spectroscopy
    • Braunschweiler L., Ernst R.R. Coherence transfer by isotropic mixing: application to proton correlation spectroscopy. J. Magn. Reson. 1983, 53:521-528.
    • (1983) J. Magn. Reson. , vol.53 , pp. 521-528
    • Braunschweiler, L.1    Ernst, R.R.2
  • 26
    • 0000195671 scopus 로고
    • Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopy
    • Bodenhausen G., Ruben D.J. Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopy. Chem. Phys. Lett. 1980, 69:185-189.
    • (1980) Chem. Phys. Lett. , vol.69 , pp. 185-189
    • Bodenhausen, G.1    Ruben, D.J.2
  • 27
    • 0000470905 scopus 로고
    • Heteronuclear three-dimensional NMR spectroscopy. A strategy for the simplification of homonuclear two-dimensional NMR spectra
    • Fesik S.W., Zuiderweg E.R.P. Heteronuclear three-dimensional NMR spectroscopy. A strategy for the simplification of homonuclear two-dimensional NMR spectra. J. Magn. Reson. 1988, 78:588-593.
    • (1988) J. Magn. Reson. , vol.78 , pp. 588-593
    • Fesik, S.W.1    Zuiderweg, E.R.P.2
  • 28
    • 77955087390 scopus 로고    scopus 로고
    • The computer-aided resonance assignment tutorial CARA, Cantina Verlag, Goldau, Switzerland
    • Keller, R. (2000) The computer-aided resonance assignment tutorial CARA, Cantina Verlag, Goldau, Switzerland.
    • (2000)
    • Keller, R.1
  • 29
    • 0038612578 scopus 로고
    • Wideband excitation with polychromatic pulses
    • Kupce E., Freeman R. Wideband excitation with polychromatic pulses. J. Magn. Reson., Ser. A 1994, 108:268-273.
    • (1994) J. Magn. Reson., Ser. A , vol.108 , pp. 268-273
    • Kupce, E.1    Freeman, R.2
  • 30
    • 44949280676 scopus 로고
    • Band-selective radiofrequency pulses
    • Geen H., Freeman R. Band-selective radiofrequency pulses. J. Magn. Reson. 1991, 93:93-141.
    • (1991) J. Magn. Reson. , vol.93 , pp. 93-141
    • Geen, H.1    Freeman, R.2
  • 31
    • 0001534324 scopus 로고
    • Frequency-switched composite pulses for decoupling carbon-13 spins over ultrabroad bandwidths
    • Fujiwara T., Anai T., Kurihara N., Nagayama K. Frequency-switched composite pulses for decoupling carbon-13 spins over ultrabroad bandwidths. J. Magn. Reson., Ser. A 1993, 104:103-105.
    • (1993) J. Magn. Reson., Ser. A , vol.104 , pp. 103-105
    • Fujiwara, T.1    Anai, T.2    Kurihara, N.3    Nagayama, K.4
  • 32
    • 0001424822 scopus 로고    scopus 로고
    • Suppression of convection artifacts in stimulated-echo diffusion experiments. Double-stimulated-echo experiments
    • Jerschow A., Müller N. Suppression of convection artifacts in stimulated-echo diffusion experiments. Double-stimulated-echo experiments. J. Magn. Reson. 1997, 125:372-375.
    • (1997) J. Magn. Reson. , vol.125 , pp. 372-375
    • Jerschow, A.1    Müller, N.2
  • 33
    • 0033554852 scopus 로고    scopus 로고
    • Hydrodynamic radii of native and denatured proteins measured by pulse field gradient NMR techniques
    • Wilkins D.K., Grimshaw S.B., Receveur V., Dobson C.M., Jones J.A., Smith L.J. Hydrodynamic radii of native and denatured proteins measured by pulse field gradient NMR techniques. Biochemistry 1999, 38:16424-16431.
    • (1999) Biochemistry , vol.38 , pp. 16424-16431
    • Wilkins, D.K.1    Grimshaw, S.B.2    Receveur, V.3    Dobson, C.M.4    Jones, J.A.5    Smith, L.J.6
  • 36
    • 45249127991 scopus 로고
    • Rapid recording of 2D NMR spectra without phase cycling. Application to the study of hydrogen exchange in proteins
    • Marion D., Ikura M., Tschudin R., Bax A. Rapid recording of 2D NMR spectra without phase cycling. Application to the study of hydrogen exchange in proteins. J. Magn. Reson. 1989, 85:393-399.
    • (1989) J. Magn. Reson. , vol.85 , pp. 393-399
    • Marion, D.1    Ikura, M.2    Tschudin, R.3    Bax, A.4
  • 38
    • 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 1988, 27:8063-8068.
    • (1988) Biochemistry , vol.27 , pp. 8063-8068
    • Santoro, M.M.1    Bolen, D.W.2
  • 39
    • 0027502784 scopus 로고
    • Thioflavine T interaction with synthetic Alzheimer's disease beta-amyloid peptides: detection of amyloid aggregation in solution
    • LeVine H. Thioflavine T interaction with synthetic Alzheimer's disease beta-amyloid peptides: detection of amyloid aggregation in solution. Protein Sci. 1993, 2:404-410.
    • (1993) Protein Sci. , vol.2 , pp. 404-410
    • LeVine, H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.