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Volumn 47, Issue 8, 2008, Pages 2397-2403

Nucleation, growth, and activation energies for seeded and unseeded aggregation of α-chymotrypsinogen A

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATION ENERGY; BIOCHEMISTRY; GROWTH KINETICS; NUCLEATION;

EID: 39749110693     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi7019244     Document Type: Article
Times cited : (46)

References (33)
  • 1
    • 11844291300 scopus 로고    scopus 로고
    • Protein aggregation and its inhibition in biopharmaceutics
    • Wang, W. (2005) Protein aggregation and its inhibition in biopharmaceutics, Int. J. Pharm. 289, 1-30.
    • (2005) Int. J. Pharm , vol.289 , pp. 1-30
    • Wang, W.1
  • 2
    • 33645521792 scopus 로고    scopus 로고
    • Protein aggregation and its consequences for human disease
    • Dobson, C. M. (2006) Protein aggregation and its consequences for human disease, Protein Pept. Lett. 13, 219-227.
    • (2006) Protein Pept. Lett , vol.13 , pp. 219-227
    • Dobson, C.M.1
  • 3
    • 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
  • 4
    • 34250834054 scopus 로고    scopus 로고
    • A Lumry-Eyring Nucleated-Polymerization Model of Protein Aggregation Kinetics I. Aggregation with Pre-Equilibrated Unfolding
    • Andrews, J. M., and Roberts, C. J. (2007) A Lumry-Eyring Nucleated-Polymerization Model of Protein Aggregation Kinetics I. Aggregation with Pre-Equilibrated Unfolding, J. Phys. Chem. B 111, 7897-7913.
    • (2007) J. Phys. Chem. B , vol.111 , pp. 7897-7913
    • Andrews, J.M.1    Roberts, C.J.2
  • 5
    • 0037015081 scopus 로고    scopus 로고
    • Huntington's disease age-of-onset linked to polyglutamine aggregation nucleation
    • Chen, S. M., 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.M.1    Ferrone, F.A.2    Wetzel, R.3
  • 6
    • 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, 7365-81.
    • (2004) Biochemistry , vol.43 , pp. 7365-7381
    • Hurshman, A.R.1    White, J.T.2    Powers, E.T.3    Kelly, J.W.4
  • 7
    • 18544387148 scopus 로고    scopus 로고
    • Aggregation of a slow-folding mutant of a beta-clam protein proceeds through a monomelic nucleus
    • Ignatova, Z., and Gierasch, L. M. (2005) Aggregation of a slow-folding mutant of a beta-clam protein proceeds through a monomelic nucleus, Biochemistry 44, 7266-7274.
    • (2005) Biochemistry , vol.44 , pp. 7266-7274
    • Ignatova, Z.1    Gierasch, L.M.2
  • 8
    • 0034875603 scopus 로고    scopus 로고
    • A mathematical model of the kinetics of beta-amyloid fibril growth from the denatured state
    • Pallitto, M. M., and Murphy, R. M. (2001) A mathematical model of the kinetics of beta-amyloid fibril growth from the denatured state, Biophys. J. 81, 1805-1822.
    • (2001) Biophys. J , vol.81 , pp. 1805-1822
    • Pallitto, M.M.1    Murphy, R.M.2
  • 9
    • 0037421836 scopus 로고    scopus 로고
    • Kinetics of irreversible protein aggregation: Analysis of extended Lumry-Eyring models and implications for predicting protein shelf life
    • Roberts, C. J. (2003) Kinetics of irreversible protein aggregation: Analysis of extended Lumry-Eyring models and implications for predicting protein shelf life, J. Phys. Chem. B 107, 1194-1207.
    • (2003) J. Phys. Chem. B , vol.107 , pp. 1194-1207
    • Roberts, C.J.1
  • 10
    • 84919873764 scopus 로고    scopus 로고
    • Non-Native Protein Aggregation: Pathways, Kinetics, and Shelf-Life Prediction
    • Murphy, R. M, and Tsai, A. M, Eds, pp, Springer, New York
    • Roberts, C. J. (2006) Non-Native Protein Aggregation: Pathways, Kinetics, and Shelf-Life Prediction, in Misbehaving Proteins: Protein Misfolding, Aggregation, and Stability (Murphy, R. M., and Tsai, A. M., Eds.) pp 17-46, Springer, New York.
    • (2006) Misbehaving Proteins: Protein Misfolding, Aggregation, and Stability , pp. 17-46
    • Roberts, C.J.1
  • 11
    • 0242684664 scopus 로고    scopus 로고
    • Irreversible aggregation of recombinant bovine Granulocyte-Colony Stimulating Factor (bG-CSF) and implications for predicting protein shelf life
    • Roberts, C. J., Darrington, R. T., and Whitley, M. B. (2003) Irreversible aggregation of recombinant bovine Granulocyte-Colony Stimulating Factor (bG-CSF) and implications for predicting protein shelf life, J. Pharm. Sci. 92, 1095-1111.
    • (2003) J. Pharm. Sci , vol.92 , pp. 1095-1111
    • Roberts, C.J.1    Darrington, R.T.2    Whitley, M.B.3
  • 12
    • 34250870678 scopus 로고    scopus 로고
    • Non-native aggregation of alpha-chymotrypsinogen occurs through nucleation and growth with competing nucleus sizes and negative activation energies
    • Andrews, J. M., and Roberts, C. J. (2007) Non-native aggregation of alpha-chymotrypsinogen occurs through nucleation and growth with competing nucleus sizes and negative activation energies, Biochemistry 46, 7558-7571.
    • (2007) Biochemistry , vol.46 , pp. 7558-7571
    • Andrews, J.M.1    Roberts, C.J.2
  • 13
    • 37349050368 scopus 로고    scopus 로고
    • Nonnative protein polymers: Structure, morphology, and relation to nucleation and growth
    • Weiss, W. F., IV, Hodgdon, T. K., Kaler, E. W., Lenhoff, A. M., and Roberts, C. J. (2007) Nonnative protein polymers: structure, morphology, and relation to nucleation and growth, Biophys. J. 93, 4392-4403.
    • (2007) Biophys. J , vol.93 , pp. 4392-4403
    • Weiss, W.F.I.1    Hodgdon, T.K.2    Kaler, E.W.3    Lenhoff, A.M.4    Roberts, C.J.5
  • 14
    • 0842281551 scopus 로고    scopus 로고
    • Principles of protein folding, misfolding and aggregation
    • Dobson, C. M. (2004) Principles of protein folding, misfolding and aggregation, Semin. Cell Dev. Biol. 15, 3-16.
    • (2004) Semin. Cell Dev. Biol , vol.15 , pp. 3-16
    • Dobson, C.M.1
  • 15
    • 33746237577 scopus 로고    scopus 로고
    • To be or not to be toxic: Aggregations in Huntington and Alzheimer disease
    • Slow, E. J., Graham, R. K., and Hayden, M. R. (2006) To be or not to be toxic: aggregations in Huntington and Alzheimer disease, Trends Genet. 22, 408-411.
    • (2006) Trends Genet , vol.22 , pp. 408-411
    • Slow, E.J.1    Graham, R.K.2    Hayden, M.R.3
  • 18
    • 0141567459 scopus 로고    scopus 로고
    • Physical stability of proteins in aqueous solution: Mechanism and driving forces in nonnative protein aggregation
    • Chi, E. Y., Krishnan, S., Randolph, T. W., and Carpenter, J. F. (2003) Physical stability of proteins in aqueous solution: Mechanism and driving forces in nonnative protein aggregation, Pharm. Res. 20, 1325-1336.
    • (2003) Pharm. Res , vol.20 , pp. 1325-1336
    • Chi, E.Y.1    Krishnan, S.2    Randolph, T.W.3    Carpenter, J.F.4
  • 19
    • 0141750565 scopus 로고    scopus 로고
    • Kinetics of heat- and acidification-induced aggregation of firefly luciferase
    • Wang, K. Y., and Kurganov, B. I. (2003) Kinetics of heat- and acidification-induced aggregation of firefly luciferase, Biophys. Chem. 106, 97-109.
    • (2003) Biophys. Chem , vol.106 , pp. 97-109
    • Wang, K.Y.1    Kurganov, B.I.2
  • 21
    • 36749040335 scopus 로고    scopus 로고
    • Non-native protein aggregation kinetics
    • Roberts, C. J. (2007) Non-native protein aggregation kinetics, Biotechnol. Bioeng. 98, 927-938.
    • (2007) Biotechnol. Bioeng , vol.98 , pp. 927-938
    • Roberts, C.J.1
  • 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, K. C., Berger, E. P., Cho, C. G., Weisgraber, K. H., and Lansbury, P. T. (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. U.S.A. 92, 763-767.
    • (1995) Proc. Natl. Acad. Sci. U.S.A , vol.92 , pp. 763-767
    • Evans, K.C.1    Berger, E.P.2    Cho, C.G.3    Weisgraber, K.H.4    Lansbury, P.T.5
  • 23
    • 33745285736 scopus 로고    scopus 로고
    • The component polypeptide chains of bovine insulin nucleate or inhibit aggregation of the parent protein in a conformation-dependent manner
    • Devlin, G. L., Knowles, T. P. J., Squires, A., McCammon, M. G., Gras, S. L., Nilsson, M. R., Robinson, C. V., Dobson, C. M., and MacPhee, C. E. (2006) The component polypeptide chains of bovine insulin nucleate or inhibit aggregation of the parent protein in a conformation-dependent manner, J. Mol. Biol. 360, 497-509.
    • (2006) J. Mol. Biol , vol.360 , pp. 497-509
    • Devlin, G.L.1    Knowles, T.P.J.2    Squires, A.3    McCammon, M.G.4    Gras, S.L.5    Nilsson, M.R.6    Robinson, C.V.7    Dobson, C.M.8    MacPhee, C.E.9
  • 24
    • 2342444028 scopus 로고    scopus 로고
    • Seeding specificity in amyloid growth induced by heterologous fibrils
    • O'Nuallain, B., Williams, A. D., Westermark, P., and Wetzel, R. (2004) Seeding specificity in amyloid growth induced by heterologous fibrils, J. Biol. Chem. 279, 17490-17499.
    • (2004) J. Biol. Chem , vol.279 , pp. 17490-17499
    • O'Nuallain, B.1    Williams, A.D.2    Westermark, P.3    Wetzel, R.4
  • 25
    • 27344435254 scopus 로고    scopus 로고
    • Polyglutamine aggregation nucleation: Thermodynamics of a highly unfavorable protein folding reaction
    • Bhattacharyya, A. M., Thakur, A. K., and Wetzel, R. (2005) Polyglutamine aggregation nucleation: Thermodynamics of a highly unfavorable protein folding reaction, Proc. Natl. Acad. Sci. U.S.A. 102, 15400-15405.
    • (2005) Proc. Natl. Acad. Sci. U.S.A , vol.102 , pp. 15400-15405
    • Bhattacharyya, A.M.1    Thakur, A.K.2    Wetzel, R.3
  • 28
    • 0009656012 scopus 로고    scopus 로고
    • Thermophysical Properties of Fluid Systems
    • Linstiom, P. J, and Mallard, W. G, Eds, National Institute of Standards and Technology, Gaithersburg, MD
    • Lemmon, E. W., McLinden, M. O., and Friend, D. G. (2005) Thermophysical Properties of Fluid Systems, in NIST Chemistry Webbook, NIST Standard Reference Database Number 69 (Linstiom, P. J., and Mallard, W. G., Eds.), National Institute of Standards and Technology, Gaithersburg, MD.
    • (2005) NIST Chemistry Webbook, NIST Standard Reference Database Number 69
    • Lemmon, E.W.1    McLinden, M.O.2    Friend, D.G.3
  • 29
    • 0035029337 scopus 로고    scopus 로고
    • Effect of anisotropic reactivity on the rate of diffusion-controlled reactions: Comparative analysis of the models of patches and hemispheres
    • Barzykin, A. V., and Shushin, A. I. (2001) Effect of anisotropic reactivity on the rate of diffusion-controlled reactions: Comparative analysis of the models of patches and hemispheres, Biophys. J. 80, 2062-2073.
    • (2001) Biophys. J , vol.80 , pp. 2062-2073
    • Barzykin, A.V.1    Shushin, A.I.2
  • 30
    • 0000786787 scopus 로고
    • Role Of Surface-Chemistry In Primary And Secondary Coagulation And Hetero-Coagulation
    • Prieve, D. C., and Ruckenstein, E. (1980) Role Of Surface-Chemistry In Primary And Secondary Coagulation And Hetero-Coagulation, J. Colloid Interface Sci. 73, 539-555.
    • (1980) J. Colloid Interface Sci , vol.73 , pp. 539-555
    • Prieve, D.C.1    Ruckenstein, E.2
  • 31
    • 0028981210 scopus 로고
    • Negative Activation Enthalpies In The Kinetics Of Protein-Folding
    • Oliveberg, M., Tan, Y. J., and Fersht, A. R. (1995) Negative Activation Enthalpies In The Kinetics Of Protein-Folding, Proc. Natl. Acad. Sci. U.S.A. 92, 8926-8929.
    • (1995) Proc. Natl. Acad. Sci. U.S.A , vol.92 , pp. 8926-8929
    • Oliveberg, M.1    Tan, Y.J.2    Fersht, A.R.3
  • 32
    • 0026675307 scopus 로고
    • Partial Denaturation Of Transthyretin Is Sufficient For Amyloid Fibril Formation In vitro
    • Colon, W., and Kelly, J. W. (1992) Partial Denaturation Of Transthyretin Is Sufficient For Amyloid Fibril Formation In vitro, Biochemistry 31, 8654-8660.
    • (1992) Biochemistry , vol.31 , pp. 8654-8660
    • Colon, W.1    Kelly, J.W.2
  • 33
    • 1642417648 scopus 로고    scopus 로고
    • Amyloid fibrils from the viewpoint of protein folding
    • Ohnishi, S., and Takano, K. (2004) Amyloid fibrils from the viewpoint of protein folding, Cell. Mol. Life Sci. 61, 511-524.
    • (2004) Cell. Mol. Life Sci , vol.61 , pp. 511-524
    • Ohnishi, S.1    Takano, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.