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Volumn 584, Issue 15, 2010, Pages 3348-3353

The amyloid fibrils of the constant domain of immunoglobulin light chain

Author keywords

2 Microglobulin; AL amyloidosis; Amyloid fibril; Dialysis related amyloidosis; Immunoglobulin domain

Indexed keywords

AMYLOID; BETA 2 MICROGLOBULIN;

EID: 77955280729     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2010.06.019     Document Type: Article
Times cited : (18)

References (40)
  • 1
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • Dobson C.M. Protein folding and misfolding. Nature 2003, 426:884-890.
    • (2003) Nature , vol.426 , pp. 884-890
    • Dobson, C.M.1
  • 2
    • 0346727128 scopus 로고    scopus 로고
    • Therapeutic approaches to protein-misfolding diseases
    • Cohen F.E., Kelly J.W. Therapeutic approaches to protein-misfolding diseases. Nature 2003, 426:905-909.
    • (2003) Nature , vol.426 , pp. 905-909
    • Cohen, F.E.1    Kelly, J.W.2
  • 3
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • Chiti F., Dobson C.M. Protein misfolding, functional amyloid, and human disease. Annu. Rev. Biochem. 2006, 75:333-366.
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 4
    • 27744454828 scopus 로고    scopus 로고
    • Historical background and clinical treatment of dialysis-related amyloidosis
    • Yamamoto S., Gejyo F. Historical background and clinical treatment of dialysis-related amyloidosis. Biochim. Biophys. Acta 2005, 1753:4-10.
    • (2005) Biochim. Biophys. Acta , vol.1753 , pp. 4-10
    • Yamamoto, S.1    Gejyo, F.2
  • 5
    • 0028305304 scopus 로고
    • A role for destabilizing amino acid replacements in light-chain amyloidosis
    • Hurle M.R., Helms L.R., Li L., Chan W., Wetzel R. A role for destabilizing amino acid replacements in light-chain amyloidosis. Proc. Natl. Acad. Sci. USA 1994, 91:5446-5450.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 5446-5450
    • Hurle, M.R.1    Helms, L.R.2    Li, L.3    Chan, W.4    Wetzel, R.5
  • 7
    • 0037137135 scopus 로고    scopus 로고
    • Establishment of a first-order kinetic model of light chain-associated amyloid fibril extension in vitro
    • Takahashi N., Hasegawa K., Yamaguchi I., Okada H., Ueda T., Gejyo F., Naiki H. Establishment of a first-order kinetic model of light chain-associated amyloid fibril extension in vitro. Biochim. Biophys. Acta 2002, 1601:110-120.
    • (2002) Biochim. Biophys. Acta , vol.1601 , pp. 110-120
    • Takahashi, N.1    Hasegawa, K.2    Yamaguchi, I.3    Okada, H.4    Ueda, T.5    Gejyo, F.6    Naiki, H.7
  • 8
    • 0033855656 scopus 로고    scopus 로고
    • Review: immunoglobulin light chain amyloidosis - the archetype of structural and pathogenic variability
    • Bellotti V., Mangione P., Merlini G. Review: immunoglobulin light chain amyloidosis - the archetype of structural and pathogenic variability. J. Struct. Biol. 2000, 130:280-289.
    • (2000) J. Struct. Biol. , vol.130 , pp. 280-289
    • Bellotti, V.1    Mangione, P.2    Merlini, G.3
  • 9
    • 0033051717 scopus 로고    scopus 로고
    • Phase II trial of high-dose dexamethasone for previously treated immunoglobulin light-chain amyloidosis
    • Gertz M.A., Lacy M.Q., Lust J.A., Greipp P.R., Witzig T.E., Kyle R.A. Phase II trial of high-dose dexamethasone for previously treated immunoglobulin light-chain amyloidosis. Am. J. Hematol. 1999, 61:115-119.
    • (1999) Am. J. Hematol. , vol.61 , pp. 115-119
    • Gertz, M.A.1    Lacy, M.Q.2    Lust, J.A.3    Greipp, P.R.4    Witzig, T.E.5    Kyle, R.A.6
  • 15
    • 67651087325 scopus 로고    scopus 로고
    • Ultrasonication-dependent production and breakdown lead to minimum-sized amyloid fibrils
    • Chatani E., Lee Y.H., Yagi H., Yoshimura Y., Naiki H., Goto Y. Ultrasonication-dependent production and breakdown lead to minimum-sized amyloid fibrils. Proc. Natl. Acad. Sci. USA 2009, 106:11119-11124.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 11119-11124
    • Chatani, E.1    Lee, Y.H.2    Yagi, H.3    Yoshimura, Y.4    Naiki, H.5    Goto, Y.6
  • 21
    • 0029843044 scopus 로고    scopus 로고
    • Cysteine scanning mutagenesis at 40 of 76 positions in villin headpiece maps the F-actin binding site and structural features of the domain
    • Doering D.S., Matsudaira P. Cysteine scanning mutagenesis at 40 of 76 positions in villin headpiece maps the F-actin binding site and structural features of the domain. Biochemistry 1996, 35:12677-12685.
    • (1996) Biochemistry , vol.35 , pp. 12677-12685
    • Doering, D.S.1    Matsudaira, P.2
  • 22
    • 21644434170 scopus 로고    scopus 로고
    • Cellular quality control screening to identify amino acid pairs for substituting the disulfide bonds in immunoglobulin fold domains
    • Hagihara Y., Matsuda T., Yumoto N. Cellular quality control screening to identify amino acid pairs for substituting the disulfide bonds in immunoglobulin fold domains. J. Biol. Chem. 2005, 280:24752-24758.
    • (2005) J. Biol. Chem. , vol.280 , pp. 24752-24758
    • Hagihara, Y.1    Matsuda, T.2    Yumoto, N.3
  • 23
    • 0014109212 scopus 로고
    • Spectroscopic determination of tryptophan and tyrosine in proteins
    • Edelhoch H. Spectroscopic determination of tryptophan and tyrosine in proteins. Biochemistry 1967, 6:1948-1954.
    • (1967) Biochemistry , vol.6 , pp. 1948-1954
    • Edelhoch, H.1
  • 26
    • 0000079910 scopus 로고    scopus 로고
    • Establishment of a kinetic model of dialysis-related amyloid fibril extension in vitro
    • Naiki H., Hashimoto N., Suzuki S., Kimura H., Nakakuki K., Gejyo F. Establishment of a kinetic model of dialysis-related amyloid fibril extension in vitro. Amyloid 1997, 4:223-232.
    • (1997) Amyloid , vol.4 , pp. 223-232
    • Naiki, H.1    Hashimoto, N.2    Suzuki, S.3    Kimura, H.4    Nakakuki, K.5    Gejyo, F.6
  • 27
    • 0035859102 scopus 로고    scopus 로고
    • Sensitive detection of pathological prion protein by cyclic amplification of protein misfolding
    • Saborio G.P., Permanne B., Soto C. Sensitive detection of pathological prion protein by cyclic amplification of protein misfolding. Nature 2001, 411:810-813.
    • (2001) Nature , vol.411 , pp. 810-813
    • Saborio, G.P.1    Permanne, B.2    Soto, C.3
  • 28
    • 33845944898 scopus 로고    scopus 로고
    • Ultra-efficient replication of infectious prions by automated protein misfolding cyclic amplification
    • Saa P., Castilla J., Soto C. Ultra-efficient replication of infectious prions by automated protein misfolding cyclic amplification. J. Biol. Chem. 2006, 281:35245-35252.
    • (2006) J. Biol. Chem. , vol.281 , pp. 35245-35252
    • Saa, P.1    Castilla, J.2    Soto, C.3
  • 29
    • 0032536194 scopus 로고    scopus 로고
    • Group additive contributions to the alcohol-induced α-helix formation of melittin: implication for the mechanism of the alcohol effects on proteins
    • Hirota N., Mizuno K., Goto Y. Group additive contributions to the alcohol-induced α-helix formation of melittin: implication for the mechanism of the alcohol effects on proteins. J. Mol. Biol. 1998, 275:365-378.
    • (1998) J. Mol. Biol. , vol.275 , pp. 365-378
    • Hirota, N.1    Mizuno, K.2    Goto, Y.3
  • 30
    • 33748943122 scopus 로고    scopus 로고
    • 2-microglobulin fragment are induced by fluorine-substituted alcohols
    • 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
  • 31
    • 0018721964 scopus 로고
    • The role of the intrachain disulfide bond in the conformation and stability of the constant fragment of the immunoglobulin light chain
    • Goto Y., Hamaguchi K. The role of the intrachain disulfide bond in the conformation and stability of the constant fragment of the immunoglobulin light chain. J. Biochem. 1979, 86:1433-1441.
    • (1979) J. Biochem. , vol.86 , pp. 1433-1441
    • Goto, Y.1    Hamaguchi, K.2
  • 34
    • 0025195499 scopus 로고
    • Mechanism of acid-induced folding of proteins
    • Goto Y., Takahashi N., Fink A.L. Mechanism of acid-induced folding of proteins. Biochemistry 1990, 29:3480-3488.
    • (1990) Biochemistry , vol.29 , pp. 3480-3488
    • Goto, Y.1    Takahashi, N.2    Fink, A.L.3
  • 35
    • 35148899284 scopus 로고    scopus 로고
    • Effect of different salt ions on the propensity of aggregation and on the structure of Alzheimer's Aβ(1-40) amyloid fibrils
    • Klement K., Wieligmann K., Meinhardt J., Hortschansky P., Richter W., Fandrich M. Effect of different salt ions on the propensity of aggregation and on the structure of Alzheimer's Aβ(1-40) amyloid fibrils. J. Mol. Biol. 2007, 373:1321-1333.
    • (2007) J. Mol. Biol. , vol.373 , pp. 1321-1333
    • Klement, K.1    Wieligmann, K.2    Meinhardt, J.3    Hortschansky, P.4    Richter, W.5    Fandrich, M.6
  • 36
    • 58149326746 scopus 로고    scopus 로고
    • Molecular mechanism of thioflavin-T binding to the surface of β-rich peptide self-assemblies
    • Biancalana M., Makabe K., Koide A., Koide S. Molecular mechanism of thioflavin-T binding to the surface of β-rich peptide self-assemblies. J. Mol. Biol. 2009, 385:1052-1063.
    • (2009) J. Mol. Biol. , vol.385 , pp. 1052-1063
    • Biancalana, M.1    Makabe, K.2    Koide, A.3    Koide, S.4
  • 37
    • 70449518987 scopus 로고    scopus 로고
    • Binding modes of thioflavin-T to the single-layer β-sheet of the peptide self-assembly mimics
    • Wu C., Biancalana M., Koide S., Shea J.E. Binding modes of thioflavin-T to the single-layer β-sheet of the peptide self-assembly mimics. J. Mol. Biol. 2009, 394:627-633.
    • (2009) J. Mol. Biol. , vol.394 , pp. 627-633
    • Wu, C.1    Biancalana, M.2    Koide, S.3    Shea, J.E.4
  • 38
    • 77952320068 scopus 로고    scopus 로고
    • Molecular mechanism of thioflavin-T binding to amyloid fibrils
    • Biancalana M., Koide S. Molecular mechanism of thioflavin-T binding to amyloid fibrils. Biochim. Biophys. Acta 2010, 1804:1405-1412.
    • (2010) Biochim. Biophys. Acta , vol.1804 , pp. 1405-1412
    • Biancalana, M.1    Koide, S.2
  • 39
    • 33845747314 scopus 로고    scopus 로고
    • Influence of the internal disulfide bridge on the folding pathway of the CL antibody domain
    • Feige M.J., Hagn F., Esser J., Kessler H., Buchner J. Influence of the internal disulfide bridge on the folding pathway of the CL antibody domain. J. Mol. Biol. 2007, 365:1232-1244.
    • (2007) J. Mol. Biol. , vol.365 , pp. 1232-1244
    • Feige, M.J.1    Hagn, F.2    Esser, J.3    Kessler, H.4    Buchner, J.5
  • 40
    • 77649240855 scopus 로고    scopus 로고
    • Identifying the amylome, proteins capable of forming amyloid-like fibrils
    • Goldschmidt L., Teng P.K., Riek R., Eisenberg D. Identifying the amylome, proteins capable of forming amyloid-like fibrils. Proc. Natl. Acad. Sci. USA 2010, 107:3487-3492.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 3487-3492
    • Goldschmidt, L.1    Teng, P.K.2    Riek, R.3    Eisenberg, D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.