메뉴 건너뛰기




Volumn 44, Issue 19, 2005, Pages 7266-7274

Aggregation of a slow-folding mutant of a β-clam protein proceeds through a monomeric nucleus

Author keywords

[No Author keywords available]

Indexed keywords

AGGLOMERATION; ESCHERICHIA COLI; FLUORESCENCE; MONOMERS; MUTAGENESIS; NUCLEATION; POLYMERIZATION; X RAY SCATTERING;

EID: 18544387148     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi047404e     Document Type: Article
Times cited : (53)

References (33)
  • 1
    • 0344944630 scopus 로고    scopus 로고
    • Protein aggregation and aggregate toxicity: New insights into protein folding, misfolding diseases and biological evolution
    • Stefani, M., and Dobson, C. M. (2003) Protein aggregation and aggregate toxicity: New insights into protein folding, misfolding diseases and biological evolution, J. Mol. Med. 81, 678-699.
    • (2003) J. Mol. Med. , vol.81 , pp. 678-699
    • Stefani, M.1    Dobson, C.M.2
  • 2
    • 0030572683 scopus 로고    scopus 로고
    • For protein misassembly, it's the "I" decade
    • Wetzel, R. (1996) For protein misassembly, it's the "I" decade, Cell 86, 699-702.
    • (1996) Cell , vol.86 , pp. 699-702
    • Wetzel, R.1
  • 3
    • 0031932169 scopus 로고    scopus 로고
    • Protein aggregation: Folding aggregates, inclusion bodies and amyloid
    • Fink, A. L. (1998) Protein aggregation: Folding aggregates, inclusion bodies and amyloid, Folding Des. 3, 9-23.
    • (1998) Folding Des. , vol.3 , pp. 9-23
    • Fink, A.L.1
  • 4
    • 0033200063 scopus 로고    scopus 로고
    • Protein misfolding, evolution and disease
    • Dobson, C. M. (1999) Protein misfolding, evolution and disease, Trends Biochem. Sci. 24, 329-332.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 329-332
    • Dobson, C.M.1
  • 5
    • 3142514201 scopus 로고    scopus 로고
    • Protein aggregation and neurodegenerative disease
    • Ross, C. A., and Poirier, M. A. (2004) Protein aggregation and neurodegenerative disease, Nat. Med. 10, 10-17.
    • (2004) Nat. Med. , vol.10 , pp. 10-17
    • Ross, C.A.1    Poirier, M.A.2
  • 7
    • 0037372175 scopus 로고    scopus 로고
    • In vitro unfolding, refolding and polymerization of human γD crystallin, a protein involved in cataract formation
    • Kosinski-Collins, M. S., and King, J. (2003) In vitro unfolding, refolding and polymerization of human γD crystallin, a protein involved in cataract formation, Protein Sci. 12, 480-490.
    • (2003) Protein Sci. , vol.12 , pp. 480-490
    • Kosinski-Collins, M.S.1    King, J.2
  • 8
    • 0029785453 scopus 로고    scopus 로고
    • Specific aggregation of partially folded polypeptide chains: The molecular basis of inclusion body composition
    • Speed, M. A., Wang, D. J., and King, J. (1996) Specific aggregation of partially folded polypeptide chains: The molecular basis of inclusion body composition, Nat. Biotechnol. 14, 1283-1287.
    • (1996) Nat. Biotechnol. , vol.14 , pp. 1283-1287
    • Speed, M.A.1    Wang, D.J.2    King, J.3
  • 9
    • 0030063114 scopus 로고    scopus 로고
    • Thermolabile folding intermediates: Inclusion bodies precursors and chaperonin substrates
    • King, J., Haase-Pettingell, C., Robinson, A. S., Speed, M., and Mitraki, A. (1996) Thermolabile folding intermediates: Inclusion bodies precursors and chaperonin substrates, FASEB J. 10, 57-66.
    • (1996) FASEB J. , vol.10 , pp. 57-66
    • King, J.1    Haase-Pettingell, C.2    Robinson, A.S.3    Speed, M.4    Mitraki, A.5
  • 10
    • 0028260192 scopus 로고
    • Native like secondary structure in interleukin-1β inclusion bodies attenuated total reflectance FTIR
    • Oberg, K., Chrunyk, B. A., Wetzel, R., and Fink, A. L. (1994) Native like secondary structure in interleukin-1β inclusion bodies attenuated total reflectance FTIR, Biochemistry 33, 2628-2634.
    • (1994) Biochemistry , vol.33 , pp. 2628-2634
    • Oberg, K.1    Chrunyk, B.A.2    Wetzel, R.3    Fink, A.L.4
  • 11
    • 0028057034 scopus 로고
    • Secondary structure characterization of β-lactamase inclusion bodies
    • Przybycien, T. M., Dunn, J. P., Valx, P., and Georgiou, G. (1994) Secondary structure characterization of β-lactamase inclusion bodies, Protein Eng. 7, 131-136.
    • (1994) Protein Eng. , vol.7 , pp. 131-136
    • Przybycien, T.M.1    Dunn, J.P.2    Valx, P.3    Georgiou, G.4
  • 12
    • 0028865843 scopus 로고
    • 3D domain swapping: A mechanism for oligomer assembly
    • Bennett, M. J., Schlunegger, M. P., and Eisenberg, D. (1994) 3D domain swapping: A mechanism for oligomer assembly, Protein Sci. 4, 2455-2468.
    • (1994) Protein Sci. , vol.4 , pp. 2455-2468
    • Bennett, M.J.1    Schlunegger, M.P.2    Eisenberg, D.3
  • 13
    • 0037015081 scopus 로고    scopus 로고
    • Huntington's disease age-of-onset linked to polyglutamine aggregation nucleation
    • Chen, S., Ferrone, F. A., and Wetzel, R. (2002) Huntington's disease age-of-onset linked to polyglutamine aggregation nucleation, Proc. Natl. Acad. Sci. U.S.A. 99, 11884-11889.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 11884-11889
    • Chen, S.1    Ferrone, F.A.2    Wetzel, R.3
  • 14
    • 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
  • 15
    • 0027195933 scopus 로고
    • Seeding "one-dimensional crystallization" of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie?
    • Jarrett, J. T., and Lansbury, P. J. (1993) Seeding "one-dimensional crystallization" of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie? Cell 73, 1050-1058.
    • (1993) Cell , vol.73 , pp. 1050-1058
    • Jarrett, J.T.1    Lansbury, P.J.2
  • 16
    • 9044229145 scopus 로고    scopus 로고
    • On the nucleation and growth of amyloid β-protein fibrils: Detection of nuclei and quantification of rate constants
    • Lomakin, A., Chung, D. S., Beneder, G. B., Kirschner, D., and Teplow, D. B. (1996) On the nucleation and growth of amyloid β-protein fibrils: Detection of nuclei and quantification of rate constants, Proc. Natl. Acad. Sci. U.S.A. 93, 1125-1129.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 1125-1129
    • Lomakin, A.1    Chung, D.S.2    Beneder, G.B.3    Kirschner, D.4    Teplow, D.B.5
  • 17
    • 0032877134 scopus 로고    scopus 로고
    • Analysis of protein aggregation kinetics
    • Ferrone, F. (1999) Analysis of protein aggregation kinetics, Methods Enzymol. 309, 256-274.
    • (1999) Methods Enzymol. , vol.309 , pp. 256-274
    • Ferrone, F.1
  • 18
    • 2942593931 scopus 로고    scopus 로고
    • Transthyretin aggregation under partially denaturing conditions is a downhill polymerization
    • Hurshman, A. R., White, J. T., Powers, E. T., and Kelly, J. W. (2004) Transthyretin aggregation under partially denaturing conditions is a downhill polymerization, Biochemistry 43, 7365-7381.
    • (2004) Biochemistry , vol.43 , pp. 7365-7381
    • Hurshman, A.R.1    White, J.T.2    Powers, E.T.3    Kelly, J.W.4
  • 20
    • 0037046151 scopus 로고    scopus 로고
    • Islet amyloid: Phase partitioning and secondary nucleation are central to the mechanism of fibrillogenesis
    • Padrick, S. B., and Miranker, A. D. (2002) Islet amyloid: Phase partitioning and secondary nucleation are central to the mechanism of fibrillogenesis, Biochemistry 41, 4694-4703.
    • (2002) Biochemistry , vol.41 , pp. 4694-4703
    • Padrick, S.B.1    Miranker, A.D.2
  • 22
    • 0029929965 scopus 로고    scopus 로고
    • Intrinsic tryptophans of CRABP I as probes of structure and folding
    • Clark, P. L., and Gierasch, L. M. (1996) Intrinsic tryptophans of CRABP I as probes of structure and folding, Protein Sci. 5, 1108-1117.
    • (1996) Protein Sci. , vol.5 , pp. 1108-1117
    • Clark, P.L.1    Gierasch, L.M.2
  • 23
    • 0030716169 scopus 로고    scopus 로고
    • Cavity formation before stable hydrogen bonding in the folding of a β-clam protein
    • Clark, P. L., Liu, Z. P., Rizo, J., and Gierasch, L. M. (1997) Cavity formation before stable hydrogen bonding in the folding of a β-clam protein, Nat. Struct. Biol. 4, 883-886.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 883-886
    • Clark, P.L.1    Liu, Z.P.2    Rizo, J.3    Gierasch, L.M.4
  • 24
    • 0031784567 scopus 로고    scopus 로고
    • Probing the folding pathway of a β-clam protein with single-tryptophan constructs
    • Clark, P. L., Weston, B. F., and Gierasch, L. M. (1998) Probing the folding pathway of a β-clam protein with single-tryptophan constructs, Folding Des. 3, 401-412.
    • (1998) Folding Des. , vol.3 , pp. 401-412
    • Clark, P.L.1    Weston, B.F.2    Gierasch, L.M.3
  • 25
    • 0034682867 scopus 로고    scopus 로고
    • Multiple roles of prolyl residues in structure and folding
    • Eyles, S. J., and Gierasch, L. M. (2000) Multiple roles of prolyl residues in structure and folding, J. Mol. Biol. 301, 737-747.
    • (2000) J. Mol. Biol. , vol.301 , pp. 737-747
    • Eyles, S.J.1    Gierasch, L.M.2
  • 26
    • 0347004717 scopus 로고    scopus 로고
    • Monitoring protein stability and aggregation in vivo by real-time fluorescent labeling
    • Ignatova, Z., and Gierasch, L. M. (2004) Monitoring protein stability and aggregation in vivo by real-time fluorescent labeling, Proc. Natl. Acad. Sci. U.S.A. 101, 523-528.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 523-528
    • Ignatova, Z.1    Gierasch, L.M.2
  • 27
    • 0034581376 scopus 로고    scopus 로고
    • Fluorescent labeling of recombinant proteins in living cells with FlAsH
    • Griffin, B. A., Adams, S. R., Jones, J., and Tsien, R. Y. (2000) Fluorescent labeling of recombinant proteins in living cells with FlAsH, Methods Enzymol. 327, 565-578.
    • (2000) Methods Enzymol. , vol.327 , pp. 565-578
    • Griffin, B.A.1    Adams, S.R.2    Jones, J.3    Tsien, R.Y.4
  • 28
    • 0027273987 scopus 로고
    • Aggregation and denaturation of apomyoglobin in aqueous urea solutions
    • De Young, L. R., Dill, K. A., and Fink, A. L. (1993) Aggregation and denaturation of apomyoglobin in aqueous urea solutions, Biochemistry 32, 3877-3886.
    • (1993) Biochemistry , vol.32 , pp. 3877-3886
    • De Young, L.R.1    Dill, K.A.2    Fink, A.L.3
  • 29
    • 0037168642 scopus 로고    scopus 로고
    • Mutational analysis of the structural organization of polyglutamine aggregates
    • Thakur, A. K., and Wetzel, R. (2002) Mutational analysis of the structural organization of polyglutamine aggregates, Proc. Natl. Acad. Sci. U.S.A. 99, 17014-17019.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 17014-17019
    • Thakur, A.K.1    Wetzel, R.2
  • 30
    • 0035818579 scopus 로고    scopus 로고
    • Specificity in intracellular protein aggregation and inclusion body formation
    • Rajan, R. S., Illing, M. E., Bence, N. F., and Kopito, R. R. (2001) Specificity in intracellular protein aggregation and inclusion body formation, Proc. Natl. Acad. Sci. U.S.A. 98, 13060-13065.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 13060-13065
    • Rajan, R.S.1    Illing, M.E.2    Bence, N.F.3    Kopito, R.R.4
  • 31
    • 0032879438 scopus 로고    scopus 로고
    • X-ray fiber diffraction of amyloid fibrils
    • Serpell, L. C., Fraser, P. E., and Sunde, M. (1999) X-ray fiber diffraction of amyloid fibrils, Methods Enzymol. 309, 526-536.
    • (1999) Methods Enzymol. , vol.309 , pp. 526-536
    • Serpell, L.C.1    Fraser, P.E.2    Sunde, M.3
  • 32
    • 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
  • 33
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo
    • Walsh, D. M., Klyubin, I., Fadeeva, J. V., Cullen, W. K., Anwyl, R., Wolfe, M. S., Rowan, M. J., and Selkoe, D. J. (2002) Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo, Nature 416, 535-539.
    • (2002) Nature , vol.416 , pp. 535-539
    • Walsh, D.M.1    Klyubin, I.2    Fadeeva, J.V.3    Cullen, W.K.4    Anwyl, R.5    Wolfe, M.S.6    Rowan, M.J.7    Selkoe, D.J.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.