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Volumn 43, Issue 24, 2004, Pages 7808-7815

Oligomeric assembly of native-like precursors precedes amyloid formation by β-2 microglobulin

Author keywords

[No Author keywords available]

Indexed keywords

COPPER; DIMERS; MOLECULAR STRUCTURE; MONOMERS; NATURAL FIBERS; OLIGOMERS;

EID: 2942748436     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi049792q     Document Type: Article
Times cited : (113)

References (39)
  • 3
    • 0030908095 scopus 로고    scopus 로고
    • Models of amyloid seeding in Alzheimer's disease and scrapie: Mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins
    • Harper, J. D., and Lansbury, P. T., Jr. (1997) Models of amyloid seeding in Alzheimer's disease and scrapie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins, Annu. Rev. Biochem. 66, 385-407.
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 385-407
    • Harper, J.D.1    Lansbury Jr., P.T.2
  • 4
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • Hardy, J., and Selkoe, D. J. (2002) The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics, Science 297, 353-356.
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 5
    • 0030050003 scopus 로고    scopus 로고
    • Beta-2-microglobulin-associated amyloidosis
    • Floege, J., and Ehlerding, G. (1996) Beta-2-microglobulin-associated amyloidosis, Nephron 72, 9-26.
    • (1996) Nephron , vol.72 , pp. 9-26
    • Floege, J.1    Ehlerding, G.2
  • 8
    • 0032693874 scopus 로고    scopus 로고
    • Chronic lymphocytic leukemia
    • Keating, M. J. (1999) Chronic lymphocytic leukemia, Semin. Oncol. 26, 107-114.
    • (1999) Semin. Oncol. , vol.26 , pp. 107-114
    • Keating, M.J.1
  • 9
    • 0035367287 scopus 로고    scopus 로고
    • Kidney dialysis-associated amyloidosis: A molecular role for copper in fiber formation
    • Morgan, C. J., Gelfand, M., Atreya, C., and Miranker, A. D. (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
  • 10
    • 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., and Miranker, A. D. (2002) Formation of a copper specific binding site in non-native states of beta-2-microglobulin, Biochemistry 41, 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
  • 13
    • 0037188472 scopus 로고    scopus 로고
    • The galvanization of beta-amyloid in Alzheimer's disease
    • Bush, A. I., and Tanzi, R. E. (2002) The galvanization of beta-amyloid in Alzheimer's disease, Proc. Natl. Acad. Sci. U.S.A. 99, 7317-7319.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 7317-7319
    • Bush, A.I.1    Tanzi, R.E.2
  • 14
    • 0035941201 scopus 로고    scopus 로고
    • Metal-triggered structural transformations, aggregation, and fibrillation of human alpha-synuclein. A possible molecular NK between Parkinson's disease and heavy metal exposure
    • Uversky, V. N., Li, J., and Fink, A. L. (2001) Metal-triggered structural transformations, aggregation, and fibrillation of human alpha-synuclein. A possible molecular NK between Parkinson's disease and heavy metal exposure, J. Biol. Chem. 276, 44284-44296.
    • (2001) J. Biol. Chem. , vol.276 , pp. 44284-44296
    • Uversky, V.N.1    Li, J.2    Fink, A.L.3
  • 15
    • 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., Raffen, R., Stevens, F. J., and Argon, Y. (2001) Both the environment and somatic mutations govern the aggregation pathway of pathogenic immunoglobulin light chain, J. Mol. Biol. 313, 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    Raffen, R.7    Stevens, F.J.8    Argon, Y.9
  • 16
    • 0027502784 scopus 로고
    • Thioflavine T interaction with synthetic Alzheimer's disease beta-amyloid peptides: Detection of amyloid aggregation in solution
    • LeVine, H., 3rd. (1993) Thioflavine T interaction with synthetic Alzheimer's disease beta-amyloid peptides: detection of amyloid aggregation in solution, Protein Sci. 2, 404-410.
    • (1993) Protein Sci , vol.2 , pp. 404-410
    • LeVine III, H.1
  • 17
    • 0034009520 scopus 로고    scopus 로고
    • Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and lamm equation modeling
    • Schuck, P. (2000) Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and lamm equation modeling, Biophys. J. 78, 1606-1619.
    • (2000) Biophys. J. , vol.78 , pp. 1606-1619
    • Schuck, P.1
  • 18
    • 0026951903 scopus 로고
    • Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions
    • Piotto, M., Saudek, V., and Sklenar, V. (1992) Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions, J. Biomol. NMR 2, 661-665.
    • (1992) J. Biomol. NMR , vol.2 , pp. 661-665
    • Piotto, M.1    Saudek, V.2    Sklenar, V.3
  • 19
    • 0031241810 scopus 로고    scopus 로고
    • Measurement of diffusion constants for nucleic acids by NMR
    • Lapham, J., Rife, J. P., Moore, P. B., and Crothers, D. M. (1997) Measurement of diffusion constants for nucleic acids by NMR, J. Biomol. NMR 10, 255-262.
    • (1997) J. Biomol. NMR , vol.10 , pp. 255-262
    • Lapham, J.1    Rife, J.P.2    Moore, P.B.3    Crothers, D.M.4
  • 20
    • 0036128797 scopus 로고    scopus 로고
    • Natively unfolded proteins: A point where biology waits for physics
    • Uversky, V. N. (2002) Natively unfolded proteins: a point where biology waits for physics, Protein Sci. 11, 739-756.
    • (2002) Protein Sci. , vol.11 , pp. 739-756
    • Uversky, V.N.1
  • 21
    • 0018339835 scopus 로고
    • The interpretation of near-ultraviolet circular dichroism
    • Kahn, P. C. (1979) The interpretation of near-ultraviolet circular dichroism, Methods Enzymol. 61, 339-378.
    • (1979) Methods Enzymol. , vol.61 , pp. 339-378
    • Kahn, P.C.1
  • 23
    • 0033041421 scopus 로고    scopus 로고
    • Quality of water used for haemodialysis: Bacteriological and chemical parameters
    • Vorbeck-Meister, I., Sommer, R., Vorbeck, F., and Horl, W. H. (1999) Quality of water used for haemodialysis: bacteriological and chemical parameters, Nephrol. Dial. Transplant. 14, 666-675.
    • (1999) Nephrol. Dial. Transplant. , vol.14 , pp. 666-675
    • Vorbeck-Meister, I.1    Sommer, R.2    Vorbeck, F.3    Horl, W.H.4
  • 25
    • 0022575638 scopus 로고
    • End-to-end annealing of microtubules in vitro
    • Rothwell, S. W., Grasser, W. A., and Murphy, D. B. (1986) End-to-end annealing of microtubules in vitro, J. Cell Biol. 102, 619-627.
    • (1986) J. Cell Biol. , vol.102 , pp. 619-627
    • Rothwell, S.W.1    Grasser, W.A.2    Murphy, D.B.3
  • 26
    • 0036108484 scopus 로고    scopus 로고
    • 3D domain swapping: As domains continue to swap
    • Liu, Y., and Eisenberg, D. (2002) 3D domain swapping: as domains continue to swap, Protein Sci. 11, 1285-1299.
    • (2002) Protein Sci. , vol.11 , pp. 1285-1299
    • Liu, Y.1    Eisenberg, D.2
  • 27
    • 0035037143 scopus 로고    scopus 로고
    • A proposed structural model for amyloid fibril elongation: Domain swapping forms an interdigitating beta-structure polymer
    • Sinha, N., Tsai, C. J., and Nussinov, R. (2001) A proposed structural model for amyloid fibril elongation: domain swapping forms an interdigitating beta-structure polymer, Protein Eng. 14, 93-103.
    • (2001) Protein Eng. , vol.14 , pp. 93-103
    • Sinha, N.1    Tsai, C.J.2    Nussinov, R.3
  • 28
    • 0035127031 scopus 로고    scopus 로고
    • A domain-swapped RNase A dimer with implications for amyloid formation
    • Liu, Y., Gotte, G., Libonati, M., and Eisenberg, D. (2001) A domain-swapped RNase A dimer with implications for amyloid formation, Nat. Struct. Biol. 8, 211-214.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 211-214
    • Liu, Y.1    Gotte, G.2    Libonati, M.3    Eisenberg, D.4
  • 29
    • 0031711595 scopus 로고    scopus 로고
    • Pathologic conformations of prion proteins
    • Cohen, F. E., and Prusiner, S. B. (1998) Pathologic conformations of prion proteins, Annu. Rev. Biochem. 67, 793-819.
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 793-819
    • Cohen, F.E.1    Prusiner, S.B.2
  • 31
    • 0035801540 scopus 로고    scopus 로고
    • Three-dimensional domain swapping in the folded and molten-globule states of cystatins, an amyloid-forming structural superfamily
    • Staniforth, R. A., Giannini, S., Higgins, L. D., Conroy, M. J., Hounslow, A. M., Jerala, R., Craven, C. J., and Waltho, J. P. (2001) Three-dimensional domain swapping in the folded and molten-globule states of cystatins, an amyloid-forming structural superfamily, EMBO J. 20, 4774-4781.
    • (2001) EMBO J. , vol.20 , pp. 4774-4781
    • Staniforth, R.A.1    Giannini, S.2    Higgins, L.D.3    Conroy, M.J.4    Hounslow, A.M.5    Jerala, R.6    Craven, C.J.7    Waltho, J.P.8
  • 33
    • 0038351889 scopus 로고    scopus 로고
    • Role of the N-and C-terminal strands of beta 2-microglobulin in amyloid formation at neutral pH
    • Jones, S., Smith, D. P., and Radford, S. E. (2003) Role of the N-and C-terminal strands of beta 2-microglobulin in amyloid formation at neutral pH, J. Mol. Biol. 330, 935-941.
    • (2003) J. Mol. Biol. , vol.330 , pp. 935-941
    • Jones, S.1    Smith, D.P.2    Radford, S.E.3
  • 35
    • 0036240398 scopus 로고    scopus 로고
    • Structural properties of an amyloid precursor of beta-(2)-microglobulin
    • McParland, V. J., Kalverda, A. P., Homans, S. W., and Radford, S. E. (2002) Structural properties of an amyloid precursor of beta-(2)-microglobulin, Nat. Struct. Biol. 9, 326-331.
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 326-331
    • McParland, V.J.1    Kalverda, A.P.2    Homans, S.W.3    Radford, S.E.4
  • 36
    • 0035253047 scopus 로고    scopus 로고
    • Zinc finger proteins: New insights into structural and functional diversity
    • Laity, J. H., Lee, B. M., and Wright, P. E. (2001) Zinc finger proteins: new insights into structural and functional diversity, Curr. Opin. Struct. Biol. 11, 39-46.
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 39-46
    • Laity, J.H.1    Lee, B.M.2    Wright, P.E.3
  • 37
    • 0034643831 scopus 로고    scopus 로고
    • Metal binding modes of Alzheimer's amyloid beta-peptide in insoluble aggregates and soluble complexes
    • Miura, T., Suzuki, K., Kohata, N., and Takeuchi, H. (2000) Metal binding modes of Alzheimer's amyloid beta-peptide in insoluble aggregates and soluble complexes, Biochemistry 39, 7024-7031.
    • (2000) Biochemistry , vol.39 , pp. 7024-7031
    • Miura, T.1    Suzuki, K.2    Kohata, N.3    Takeuchi, H.4
  • 39
    • 0035872476 scopus 로고    scopus 로고
    • Copper and prion disease
    • Brown, D. R. (2001) Copper and prion disease, Brain Res. Bull. 55, 165-173.
    • (2001) Brain Res. Bull. , vol.55 , pp. 165-173
    • Brown, D.R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.