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Volumn 65, Issue , 2012, Pages 165-183

Pathological self-aggregation of β2-microglobulin: A challenge for protein biophysics

Author keywords

Aggregation; 2 Microglobulin ( 2m)

Indexed keywords

BETA 2 MICROGLOBULIN; MULTIPROTEIN COMPLEX;

EID: 84894446315     PISSN: 03060225     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-94-007-5416-4_7     Document Type: Article
Times cited : (9)

References (70)
  • 4
    • 34447503337 scopus 로고    scopus 로고
    • Specific glycosamino-glycans promote unseeded amyloid formation from β-microglobulin fold
    • Borysik AJ, Morten IJ., Radford SE, Hewitt EW (2007) Specific glycosamino-glycans promote unseeded amyloid formation from β-microglobulin fold. Nat Struct Mol Biol 72:174-181
    • (2007) Nat Struct Mol Biol , vol.72 , pp. 174-181
    • Borysik, A.J.1    Morten, I.J.2    Radford, S.E.3    Hewitt, E.W.4
  • 6
    • 0025784163 scopus 로고
    • Structural modifications of human β2-microglobulin treated with oxygen-derived radicals
    • Capeiller-Blandin C, Delaveau T, Descamps-Latscha B (1991) Structural modifications of human β2-microglobulin treated with oxygen-derived radicals. Biochem J 277:175-182
    • (1991) Biochem J , vol.277 , pp. 175-182
    • Capeiller-Blandin, C.1    Delaveau, T.2    Descamps-Latscha, B.3
  • 7
    • 77954620268 scopus 로고    scopus 로고
    • Pre-steady-state analysis of the elongation of amyloid fibrils of β2-microglobulin with tryptophan mutagenesis
    • Chatani E, Ohnishi R, Konuma T, Sakurai K, Naiki H, GotoY (2010) Pre-steady-state analysis of the elongation of amyloid fibrils of β2-microglobulin with tryptophan mutagenesis. J Mol Biol 400:1057-1066
    • (2010) J Mol Biol , vol.400 , pp. 1057-1066
    • Chatani, E.1    Ohnishi, R.2    Konuma, T.3    Sakurai, K.4    Naiki, H.5    Goto, Y.6
  • 8
  • 12
    • 23444441485 scopus 로고    scopus 로고
    • Quantification of cleaved β2-microglobulin in serum from patients undergoing chronic hemodialysis
    • Corlin DB, Sen JW, Ladefoged S, Lund GB, Nissen MH, Heegaard NHH (2005) Quantification of cleaved β2-microglobulin in serum from patients undergoing chronic hemodialysis. Clin Chem 51:1177-1184
    • (2005) Clin Chem , vol.51 , pp. 1177-1184
    • Corlin, D.B.1    Sen, J.W.2    Ladefoged, S.3    Lund, G.B.4    Nissen, M.H.5    Heegaard, N.H.H.6
  • 13
    • 77955045091 scopus 로고    scopus 로고
    • Magic angle spinning NMR analysis of β2-microglobulin amyloid fibrils in two distinct morphologies
    • Debelouchina GT, Platt GW, Bayro MJ, Radford SE, Griffin RG (2010a) Magic angle spinning NMR analysis of β2-microglobulin amyloid fibrils in two distinct morphologies. J Am Chem Soc 132:10414-10423
    • (2010) J Am Chem Soc , vol.132 , pp. 10414-10423
    • Debelouchina, G.T.1    Platt, G.W.2    Bayro, M.J.3    Radford, S.E.4    Griffin, R.G.5
  • 15
    • 33644813233 scopus 로고    scopus 로고
    • A native to amyloidogenic transition regulated by a backbone trigger
    • Eakin CM, Berman AJ, Miranker AD (2006) A native to amyloidogenic transition regulated by a backbone trigger. Nat Struct Mol Biol 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
  • 17
    • 80053596817 scopus 로고    scopus 로고
    • Understanding the complex mechanism of b2-microglobulin amyloid assembly
    • EichnerT, RadfordSE (2011a) Understanding the complex mechanism of b2-microglobulin amyloid assembly. FEBS J 278:3868-3883.
    • (2011) FEBS J , vol.278 , pp. 3868-3883
    • Eichner, T.1    Radford, S.E.2
  • 18
    • 79959887638 scopus 로고    scopus 로고
    • A diversity of assembly mechanisms of a generic amyloid fold
    • Eichner T, Radford SE (2011b) A diversity of assembly mechanisms of a generic amyloid fold. Mol Cell 43:8-18
    • (2011) Mol Cell , vol.43 , pp. 8-18
    • Eichner, T.1    Radford, S.E.2
  • 22
    • 0028872558 scopus 로고
    • Apolipoprotein E is a kinetic but not a thermodynamic inhibitor of amyloid formation: Implications for the pathogenesis and treatment of Alzheimer disease
    • Evans KC, Berger EP, Cho C,Weisgraber KH, Lansbury PT Jr, (1995) Apolipoprotein E is a kinetic but not a thermodynamic inhibitor of amyloid formation: implications for the pathogenesis and treatment of Alzheimer disease. Proc Natl Acad Sci USA 92:763-767
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 763-767
    • Evans, K.C.1    Berger, E.P.2    Cho, C.3    Weisgraber, K.H.4    Lansbury, P.T.5
  • 23
    • 46049088514 scopus 로고    scopus 로고
    • Early stages of misfolding and association of β-microglobulin: Insights from infrared spectroscopy and dynamic light scattering
    • Fabian H, Gast K, Laue M, Misselwitz R, Uchanska-Ziegler B, Ziegler A, Naumann D (2008) Early stages of misfolding and association of β-microglobulin: insights from infrared spectroscopy and dynamic light scattering. Biochemistry 47:6895-6906
    • (2008) Biochemistry , vol.47 , pp. 6895-6906
    • Fabian, H.1    Gast, K.2    Laue, M.3    Misselwitz, R.4    Uchanska-Ziegler, B.5    Ziegler, A.6    Naumann, D.7
  • 24
    • 0035128916 scopus 로고    scopus 로고
    • β2-microglobulin-derived amyloidosis: An update
    • Floege J, Ketteler M (2001) β2-microglobulin-derived amyloidosis: an update. Kidney Int 59:164- 171
    • (2001) Kidney Int , vol.59 , pp. 164-171
    • Floege, J.1    Ketteler, M.2
  • 25
    • 33847785526 scopus 로고    scopus 로고
    • Molecular dynamics simulation suggests possible interaction patterns at early steps of β2-microglobulin aggregation
    • Fogolari F, CorazzaA,Viglino P, Zuccato P, Pieri L, Faccioli P, BellottiV, EspositoG (2007) Molecular dynamics simulation suggests possible interaction patterns at early steps of β2-microglobulin aggregation. Biophys J 92:1673-1681
    • (2007) Biophys J , vol.92 , pp. 1673-1681
    • Fogolari, F.1    Corazza, A.2    Viglino, P.3    Zuccato, P.4    Pieri, L.5    Faccioli, P.6    Bellotti, V.7    Esposito, G.8
  • 30
    • 23444445907 scopus 로고    scopus 로고
    • Competing pathways determine fibril morphology in the selfassembly of β2-microglobulin into amyloid
    • GosalWS,Morten IJ,HewittEW, SmithDA,ThomsonNH,RadfordSE (2005) Competing pathways determine fibril morphology in the selfassembly of β2-microglobulin into amyloid. J Mol Biol 351:850-864
    • (2005) J Mol Biol , vol.351 , pp. 850-864
    • Gosal, W.S.1    Morten, I.J.2    Hewitt, E.W.3    Smith, D.A.4    Thomson, N.H.5    Radford, S.E.6
  • 31
    • 0018418510 scopus 로고
    • Refolding of the immunoglobulin light chain
    • Goto Y, Azuma T, Hamaguchi K (1979) Refolding of the immunoglobulin light chain. J Biochem 85:1427-1438
    • (1979) J Biochem , vol.85 , pp. 1427-1438
    • Goto, Y.1    Azuma, T.2    Hamaguchi, K.3
  • 35
    • 36849083472 scopus 로고    scopus 로고
    • High resolution crystal structure of β2-microglobulin formed at pH 7.0
    • Iwata K, Matsuura T, Sakurai K, Nakagawa A, GotoY (2007) High resolution crystal structure of β2-microglobulin formed at pH 7.0. J Biochem (Tokyo) 142:413-419
    • (2007) J Biochem (Tokyo) , vol.142 , pp. 413-419
    • Iwata, K.1    Matsuura, T.2    Sakurai, K.3    Nakagawa, A.4    Goto, Y.5
  • 36
    • 33144467755 scopus 로고    scopus 로고
    • Amyloid formation under physiological conditions proceeds via a native-like folding intermediate
    • Jahn TR, Parker MJ, Homans SW, Radford SE (2006) Amyloid formation under physiological conditions proceeds via a native-like folding intermediate. Nat Struct Mol Biol 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
  • 37
    • 47749118352 scopus 로고    scopus 로고
    • A common β-sheet architecture underlies in Vitro and in Vivo β-microglobulin amyloid fibrils
    • Jahn TR, Tennent GA, Radford SE (2008) A common β-sheet architecture underlies in Vitro and in Vivo β-microglobulin amyloid fibrils. J Biol Chem 283:17279-17286
    • (2008) J Biol Chem , vol.283 , pp. 17279-17286
    • Jahn, T.R.1    Tennent, G.A.2    Radford, S.E.3
  • 38
    • 16244398884 scopus 로고    scopus 로고
    • Nuclear magnetic resonance characterization of the refolding intermediate of β2- microglobulin trapped by nonnative prolyl peptide bond
    • Kameda A, Hoshino M, Higurashi T, Takahashi S, Naiki H, Goto Y (2005) Nuclear magnetic resonance characterization of the refolding intermediate of β2- microglobulin trapped by nonnative prolyl peptide bond. J Mol Biol 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
  • 39
    • 27744449235 scopus 로고    scopus 로고
    • Structural studies reveal that the diverse morphology of β-microglobulin aggregates is a reflection of difference molecular architectures
    • Kardos J, Okuno D, Kawai T, Hagihara Y, Yumoto N, Kitagawa T, Zavodszky P, Naiki H, Goto Y (2005) Structural studies reveal that the diverse morphology of β-microglobulin aggregates is a reflection of difference molecular architectures. Biochim Biophys Acta 1753:108-120
    • (2005) Biochim Biophys Acta , vol.1753 , pp. 108-120
    • Kardos, J.1    Okuno, D.2    Kawai, T.3    Hagihara, Y.4    Yumoto, N.5    Kitagawa, T.6    Zavodszky, P.7    Naiki, H.8    Goto, Y.9
  • 41
    • 78650909852 scopus 로고    scopus 로고
    • Kinetic intermediates of b2-microglobulin fibril elongation probed by pulse-labeling H/D exchange combined with NMR analysis
    • Konuma T, Chatani E,Yagi M, Sakurai K, Ikegami T, Naiki H, GotoY (2011) Kinetic intermediates of b2-microglobulin fibril elongation probed by pulse-labeling H/D exchange combined with NMR analysis. J Mol Biol 405:851-862
    • (2011) J Mol Biol , vol.405 , pp. 851-862
    • Konuma, T.1    Chatani, E.2    Yagi, M.3    Sakurai, K.4    Ikegami, T.5    Naiki, H.6    Goto, Y.7
  • 42
    • 77952759080 scopus 로고    scopus 로고
    • Stacked sets of parallel, in-register beta-strands of β2-microglobulin in amyloid fibrils revealed by site-directed spin labeling and chemical labeling
    • Ladner CL, Chen M, Smith DP, Platt GW, Radford SE, Langen R (2010) Stacked sets of parallel, in-register beta-strands of β2-microglobulin in amyloid fibrils revealed by site-directed spin labeling and chemical labeling. J Biol Chem 285:17137-17147
    • (2010) J Biol Chem , vol.285 , pp. 17137-17147
    • Ladner, C.L.1    Chen, M.2    Smith, D.P.3    Platt, G.W.4    Radford, S.E.5    Langen, R.6
  • 47
    • 0035367287 scopus 로고    scopus 로고
    • Kidney dialysis-associated amyloidosis: A molecular role for copper in fiber formation
    • Morgan CJ, Gelfand M, Atreya C, Miranker AD (2001) Kidney dialysis-associated amyloidosis: a molecular role for copper in fiber formation. J Mol Biol 309:339-345
    • (2001) J Mol Biol , vol.309 , pp. 339-345
    • Morgan, C.J.1    Gelfand, M.2    Atreya, C.3    Miranker, A.D.4
  • 48
    • 33144471714 scopus 로고    scopus 로고
    • A systematic study of the effect of physiological factors on β2-microglobulin amyloid formation at neutral pH
    • Myers SL, Jones S, Jahn TR, Morten IJ, Tennent GA, Hewitt EW, Radford SE (2006) A systematic study of the effect of physiological factors on β2-microglobulin amyloid formation at neutral pH. Biochemistry 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
  • 50
    • 0026611617 scopus 로고
    • 1H NMR assignments and secondary structure of human β2- microglobulin in solution
    • Okon M, Bray P, Vucelic D (1992) 1H NMR assignments and secondary structure of human β2- microglobulin in solution. Biochemistry 31:8906-8915
    • (1992) Biochemistry , vol.31 , pp. 8906-8915
    • Okon, M.1    Bray, P.2    Vucelic, D.3
  • 52
    • 0032718386 scopus 로고    scopus 로고
    • Salt-induced detour through compact regions of the protein folding landscape
    • Otzen DE Oliveberg M (1999) Salt-induced detour through compact regions of the protein folding landscape. Proc Natl Acad Sci USA 96:11746-11751
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 11746-11751
    • Otzen, D.E.1    Oliveberg, M.2
  • 54
    • 20444403757 scopus 로고    scopus 로고
    • Prediction of aggregation-prone and aggregation-susceptible regions in proteins associated with neurodegenerative diseases
    • Pawar AP, DuBay KF, Zurdo J, Chiti F, Vendruscolo M, Dobson CM (2005) Prediction of aggregation-prone and aggregation-susceptible regions in proteins associated with neurodegenerative diseases. J Mol Biol 350:379-392
    • (2005) J Mol Biol , vol.350 , pp. 379-392
    • Pawar, A.P.1    DuBay, K.F.2    Zurdo, J.3    Chiti, F.4    Vendruscolo, M.5    Dobson, C.M.6
  • 55
    • 33646450413 scopus 로고    scopus 로고
    • Micro-heterogeneity and aggregation in β2-microglobulin solutions: Effects of temperature, pH, and conformational variant addition
    • Piazza R, Pierno M, Iacopini S, Mangione P, Esposito G, Bellotti V (2006) Micro-heterogeneity and aggregation in β2-microglobulin solutions: effects of temperature, pH, and conformational variant addition. Eur Biophys J 35:439-445
    • (2006) Eur Biophys J , vol.35 , pp. 439-445
    • Piazza, R.1    Pierno, M.2    Iacopini, S.3    Mangione, P.4    Esposito, G.5    Bellotti, V.6
  • 59
  • 60
    • 0037022563 scopus 로고    scopus 로고
    • Natural β-sheet proteins use negative design to aviod edgeto- edge aggregation
    • Richardson JS, Richardson DC (2002) Natural β-sheet proteins use negative design to aviod edgeto- edge aggregation. Proc Natl Acad Sci USA 99:2754-2759
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 2754-2759
    • Richardson, J.S.1    Richardson, D.C.2
  • 62
    • 51549116627 scopus 로고    scopus 로고
    • Kinetic coupling of folding and prolyl isomerization of β2-microglobulin studied by mutational analysis
    • Sakata M, Chatani E, KamedaA, Sakurai K, Naiki H, GotoY (2008) Kinetic coupling of folding and prolyl isomerization of β2-microglobulin studied by mutational analysis. J Mol Biol 382:1242- 1255
    • (2008) J Mol Biol , vol.382 , pp. 1242-1255
    • Sakata, M.1    Chatani, E.2    Kameda, A.3    Sakurai, K.4    Naiki, H.5    Goto, Y.6
  • 63
    • 77956244375 scopus 로고    scopus 로고
    • Characterization of amyloid fibrils of human β2- microglobulin by high-resolution Magic-Angle Spinning NMR
    • Skora L, Becker S, Zweckstetter M (2010) Characterization of amyloid fibrils of human β2- microglobulin by high-resolution Magic-Angle Spinning NMR. ChemBioChem. 11:1829-1832
    • (2010) ChemBioChem. , vol.11 , pp. 1829-1832
    • Skora, L.1    Becker, S.2    Zweckstetter, M.3
  • 65
    • 0037162520 scopus 로고    scopus 로고
    • Crystal structure of monomeric human β2-microglobulin reveals clues to its amyloidogenic properties
    • Trinh CH, Smith DP, Kalverda AP, Phillips SE, Radford SE (2002) Crystal structure of monomeric human β2-microglobulin reveals clues to its amyloidogenic properties. Proc Natl Acad Sci USA 99:9771-9776
    • (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
  • 69
    • 4644335370 scopus 로고    scopus 로고
    • Low concentrations of sodium dodecyl sulfate induce the extension of b2-microglobulin-related amyloid fibrils at a neutral pH
    • Yamamoto S, Hasegawa K,Yamaguchi I, Tsutsumi S, Kardos J, GotoY, Gejyo F, Naiki H (2004b) Low concentrations of sodium dodecyl sulfate induce the extension of b2-microglobulin-related amyloid fibrils at a neutral pH. Biochemistry 43:11075-11082
    • (2004) Biochemistry , vol.43 , pp. 11075-11082
    • Yamamoto, S.1    Hasegawa, K.2    Yamaguchi, I.3    Tsutsumi, S.4    Kardos, J.5    Goto, Y.6    Gejyo, F.7    Naiki, H.8
  • 70
    • 0346103697 scopus 로고    scopus 로고
    • Glycosaminoglycans enhance the trifluoroethanol-induced extension of b2-microglobulin-related amyloid fibrils at a neutral pH
    • Yamamoto S, Yamaguchi I, Hasegawa K, Tsutsumi S, Goto Y, Gejyo F, Naiki H (2004a) Glycosaminoglycans enhance the trifluoroethanol-induced extension of b2-microglobulin-related amyloid fibrils at a neutral pH. J Am Soc Nephrol 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


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