메뉴 건너뛰기




Volumn 135, Issue 6, 2011, Pages

Nucleated polymerization with secondary pathways. I. Time evolution of the principal moments

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID FIBRIL; ANALYTICAL APPROACH; ANALYTICAL EXPRESSIONS; CLOSED FORM; EXPERIMENTAL MEASUREMENTS; FIRST-PRINCIPLES; FITTING PROCEDURE; FIXED POINT ANALYSIS; FREE END; GENERAL ANALYTICAL SOLUTION; GROWTH LAWS; GROWTH SITES; KINETIC EQUATIONS; LAG TIME; LINEAR STRUCTURES; MOLECULAR LEVELS; NON-LINEAR; NUCLEATED POLYMERIZATION; SELF ASSEMBLY PROCESS; SELF-CONSISTENT SOLUTION; TIME EVOLUTIONS;

EID: 80051866825     PISSN: 00219606     EISSN: None     Source Type: Journal    
DOI: 10.1063/1.3608916     Document Type: Article
Times cited : (285)

References (109)
  • 4
    • 0000306723 scopus 로고
    • 10.1002/and19354150405
    • I. N. Stranski and R. Kaischew, Z. Phys. 36, 393 (1935). 10.1002/andp.19354150405
    • (1935) Z. Phys. , vol.36 , pp. 393
    • Stranski, I.N.1    Kaischew, R.2
  • 5
    • 84934935637 scopus 로고
    • 10.1002/and19354160806
    • R. Becker and W. Dring, Ann. Phys. 26 (5), 719 (1935). 10.1002/andp.19354160806
    • (1935) Ann. Phys. , vol.26 , Issue.5 , pp. 719
    • Becker, R.1    Dring, W.2
  • 6
    • 0342869049 scopus 로고
    • 10.1063/1.1750380
    • M. Avrami, J. Chem. Phys. 7 (12), 1103 (1939). 10.1063/1.1750380
    • (1939) J. Chem. Phys. , vol.7 , Issue.12 , pp. 1103
    • Avrami, M.1
  • 7
    • 0001336124 scopus 로고
    • 10.1063/1.1750631
    • M. Avrami, J. Chem. Phys. 8 (2), 212 (1940). 10.1063/1.1750631
    • (1940) J. Chem. Phys. , vol.8 , Issue.2 , pp. 212
    • Avrami, M.1
  • 11
    • 33947613349 scopus 로고
    • 10.1016/S0022-2836(62)80112-0
    • F. Oosawa and M. Kasai, J. Mol. Biol. 4, 10 (1962). 10.1016/S0022- 2836(62)80112-0
    • (1962) J. Mol. Biol. , vol.4 , pp. 10
    • Oosawa, F.1    Kasai, M.2
  • 12
    • 0021099326 scopus 로고
    • 10.1097/00006254-198305000-00024
    • L. S. Tobacman and E. D. Korn, J. Biol. Chem. 258, 3207 (1983). 10.1097/00006254-198305000-00024
    • (1983) J. Biol. Chem. , vol.258 , pp. 3207
    • Tobacman, L.S.1    Korn, E.D.2
  • 14
    • 0016698509 scopus 로고
    • 10.1016/0301-4622(75)80013-5
    • A. Wegner and J. Engel, Biophys. Chem. 3, 215 (1975). 10.1016/0301-4622(75)80013-5
    • (1975) Biophys. Chem. , vol.3 , pp. 215
    • Wegner, A.1    Engel, J.2
  • 16
    • 0033200063 scopus 로고    scopus 로고
    • Protein misfolding, evolution and disease
    • DOI 10.1016/S0968-0004(99)01445-0, PII S0968000499014450
    • C. M. Dobson, Trends Biochem. Sci. 24, 329 (1999). 10.1016/S0968-0004(99) 01445-0 (Pubitemid 29421804)
    • (1999) Trends in Biochemical Sciences , vol.24 , Issue.9 , pp. 329-332
    • Dobson, C.M.1
  • 17
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • DOI 10.1146/annurev.biochem.75.101304.123901
    • F. Chiti and C. M. Dobson, Annu. Rev. Biochem. 75, 333 (2006). 10.1146/annurev.biochem.75.101304.123901 (Pubitemid 44118036)
    • (2006) Annual Review of Biochemistry , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 18
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • DOI 10.1038/nature02261
    • C. M. Dobson, Nature (London) 426, 884 (2003). 10.1038/nature02261 (Pubitemid 38056880)
    • (2003) Nature , vol.426 , Issue.6968 , pp. 884-890
    • Dobson, C.M.1
  • 19
    • 0346727128 scopus 로고    scopus 로고
    • Therapeutic approaches to protein-misfolding diseases
    • DOI 10.1038/nature02265
    • F. E. Cohen and J. W. Kelly, Nature (London) 426, 905 (2003). 10.1038/nature02265 (Pubitemid 38056884)
    • (2003) Nature , vol.426 , Issue.6968 , pp. 905-909
    • Cohen, F.E.1    Kelly, J.W.2
  • 20
    • 0347987853 scopus 로고    scopus 로고
    • Folding proteins in fatal ways
    • DOI 10.1038/nature02264
    • D. J. Selkoe, Nature (London) 426, 900 (2003). 10.1038/nature02264 (Pubitemid 38056883)
    • (2003) Nature , vol.426 , Issue.6968 , pp. 900-904
    • Selkoe, D.J.1
  • 21
    • 33750361540 scopus 로고    scopus 로고
    • A century-old debate on protein aggregation and neurodegeneration enters the clinic
    • DOI 10.1038/nature05290, PII NATURE05290
    • P. T. Lansbury and H. A. Lashuel, Nature (London) 443, 774 (2006). 10.1038/nature05290 (Pubitemid 44622681)
    • (2006) Nature , vol.443 , Issue.7113 , pp. 774-779
    • Lansbury, P.T.1    Lashuel, H.A.2
  • 23
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • DOI 10.1126/science.1072994
    • J. Hardy and D. J. Selkoe, Science 297, 353 (2002). 10.1126/science. 1072994 (Pubitemid 34790756)
    • (2002) Science , vol.297 , Issue.5580 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 25
    • 0025910229 scopus 로고
    • 10.1126/science.1675487
    • S. B. Prusiner, Science 252, 1515 (1991). 10.1126/science.1675487
    • (1991) Science , vol.252 , pp. 1515
    • Prusiner, S.B.1
  • 27
    • 0242300624 scopus 로고    scopus 로고
    • Games Played by Rogue Proteins in Prion Disorders and Alzheimer's Disease
    • DOI 10.1126/science.1087348
    • A. Aguzzi and C. Haass, Science 302, 814 (2003). 10.1126/science.1087348 (Pubitemid 37339613)
    • (2003) Science , vol.302 , Issue.5646 , pp. 814-818
    • Aguzzi, A.1    Haass, C.2
  • 33
    • 33745757474 scopus 로고    scopus 로고
    • The kinetics of nucleated polymerizations at high concentrations: Amyloid fibril formation near and above the "supercritical concentration"
    • DOI 10.1529/biophysj.105.073767
    • E. T. Powers and D. L. Powers, Biophys. J. 91, 122 (2006). 10.1529/biophysj.105.073767 (Pubitemid 44015313)
    • (2006) Biophysical Journal , vol.91 , Issue.1 , pp. 122-132
    • Powers, E.T.1    Powers, D.L.2
  • 36
    • 0021527508 scopus 로고
    • 10.1016/S0006-3495(84)84062-X
    • M. F. Bishop and F. A. Ferrone, Biophys. J. 46, 631 (1984). 10.1016/S0006-3495(84)84062-X
    • (1984) Biophys. J. , vol.46 , pp. 631
    • Bishop, M.F.1    Ferrone, F.A.2
  • 37
    • 0020431149 scopus 로고
    • Kinetic analysis of actin assembly suggests that tropomyosin inhibits spontaneous fragmentation of actin filaments
    • DOI 10.1016/0022-2836(82)90149-8
    • A. Wegner, J. Mol. Biol. 161, 217 (1982). 10.1016/0022-2836(82)90149-8 (Pubitemid 13253152)
    • (1982) Journal of Molecular Biology , vol.161 , Issue.2 , pp. 217-227
    • Wegner, A.1
  • 38
    • 0019968097 scopus 로고
    • Spontaneous fragmentation of actin filaments in physiological conditions
    • DOI 10.1038/296266a0
    • A. Wegner, Nature (London) 296, 266 (1982). 10.1038/296266a0 (Pubitemid 12072147)
    • (1982) Nature , vol.296 , Issue.5854 , pp. 266-267
    • Wegner, A.1
  • 39
    • 0021837479 scopus 로고
    • Kinetics of sickle hemoglobin polymerization. II. A double nucleation mechanism
    • DOI 10.1016/0022-2836(85)90175-5
    • F. A. Ferrone, J. Hofrichter, and W. A. Eaton, J. Mol. Biol. 183, 611 (1985). 10.1016/0022-2836(85)90175-5 (Pubitemid 15036851)
    • (1985) Journal of Molecular Biology , vol.183 , Issue.4 , pp. 611-631
    • Ferrone, F.A.1    Hofrichter, J.2    Eaton, W.A.3
  • 41
    • 0021815445 scopus 로고
    • Kinetics of sickle hemoglobin polymerization. I. Studies using temperature-jump and laser photolysis techniques
    • DOI 10.1016/0022-2836(85)90174-3
    • F. A. Ferrone, J. Hofrichter, and W. A. Eaton, J. Mol. Biol. 183, 591 (1985). 10.1016/0022-2836(85)90174-3 (Pubitemid 15036850)
    • (1985) Journal of Molecular Biology , vol.183 , Issue.4 , pp. 591-610
    • Ferrone, F.A.1    Hofrichter, J.2    Eaton, W.A.3
  • 43
    • 0023042358 scopus 로고
    • 10.1016/0022-2836(86)90324-4
    • J. Hofrichter, J. Mol. Biol. 189, 553 (1986). 10.1016/0022-2836(86)90324- 4
    • (1986) J. Mol. Biol. , vol.189 , pp. 553
    • Hofrichter, J.1
  • 45
    • 8844247180 scopus 로고    scopus 로고
    • Mechanism of prion propagation: Amyloid growth occurs by monomer addition
    • DOI 10.1371/journal.pbio.0020321
    • S. R. Collins, A. Douglass, R. D. Vale, and J. S. Weissman, PLoS Biol. 2, e321 (2004). 10.1371/journal.pbio.0020321 (Pubitemid 39532919)
    • (2004) PLoS Biology , vol.2 , Issue.10
    • Collins, S.R.1    Douglass, A.2    Vale, R.D.3    Weissman, J.S.4
  • 46
    • 33746698975 scopus 로고    scopus 로고
    • The physical basis of how prion conformations determine strain phenotypes
    • DOI 10.1038/nature04922, PII NATURE04922
    • M. Tanaka, S. R. Collins, B. H. Toyama, and J. S. Weissman, Nature (London) 442, 585 (2006). 10.1038/nature04922 (Pubitemid 44167919)
    • (2006) Nature , vol.442 , Issue.7102 , pp. 585-589
    • Tanaka, M.1    Collins, S.R.2    Toyama, B.H.3    Weissman, J.S.4
  • 49
    • 0027195933 scopus 로고
    • Seeding 'one-dimensional crystallization' of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie?
    • DOI 10.1016/0092-8674(93)90635-4
    • J. T. Jarrett and P. T. Lansbury, Cell 73, 1055 (1993). 10.1016/0092-8674(93)90635-4 (Pubitemid 23180480)
    • (1993) Cell , vol.73 , Issue.6 , pp. 1055-1058
    • Jarrett, J.T.1    Lansbury Jr., P.T.2
  • 51
    • 0001863511 scopus 로고    scopus 로고
    • 10.1002/(SICI)15 20-6602(19 98)1:13::AID-INB I23.0.CO;2-9
    • M. A. Nowak, D. C. Krakauer, A. Klug, and R. M. May, Integr. Biol. 1, 3 (1998). 10.1002/(SICI)1520-6602(1998)1:13::AID-INBI23.0.CO;2-9
    • (1998) Integr. Biol. , vol.1 , pp. 3
    • Nowak, M.A.1    Krakauer, D.C.2    Klug, A.3    May, R.M.4
  • 52
    • 36049020231 scopus 로고    scopus 로고
    • A general model of prion strains and their pathogenicity
    • DOI 10.1126/science.1138718
    • J. Collinge and A. R. Clarke, Science 318, 930 (2007). 10.1126/science.1138718 (Pubitemid 350098981)
    • (2007) Science , vol.318 , Issue.5852 , pp. 930-936
    • Collinge, J.1    Clarke, A.R.2
  • 53
    • 34447639279 scopus 로고    scopus 로고
    • Branched chain mechanism of polymerization and ultrastructure of prion protein amyloid fibrils
    • DOI 10.1111/j.1742-4658.2007.05916.x
    • I. V. Baskakov, FEBS J. 274, 3756 (2007). 10.1111/j.1742-4658.2007.05916. x (Pubitemid 47087672)
    • (2007) FEBS Journal , vol.274 , Issue.15 , pp. 3756-3765
    • Baskakov, I.V.1
  • 54
    • 0842332840 scopus 로고    scopus 로고
    • Silent Prions Lying in Wait: A Two-hit Model of Prion/Amyloid Formation and Infection
    • DOI 10.1016/j.jmb.2003.12.004
    • D. Hall and H. Edskes, J. Mol. Biol. 336, 775 (2004). 10.1016/j.jmb.2003.12.004 (Pubitemid 38183028)
    • (2004) Journal of Molecular Biology , vol.336 , Issue.3 , pp. 775-786
    • Hall, D.1    Edskes, H.2
  • 57
    • 28644437048 scopus 로고    scopus 로고
    • The importance of sequence diversity in the aggregation and evolution of proteins
    • DOI 10.1038/nature04195
    • C. F. Wright, S. A. Teichmann, J. Clarke, and C. M. Dobson, Nature (London) 438, 878 (2005). 10.1038/nature04195 (Pubitemid 41753072)
    • (2005) Nature , vol.438 , Issue.7069 , pp. 878-881
    • Wright, C.F.1    Teichmann, S.A.2    Clarke, J.3    Dobson, C.M.4
  • 58
    • 0032877134 scopus 로고    scopus 로고
    • Analysis of protein aggregation kinetics
    • DOI 10.1016/S0076-6879(99)09019-9
    • F. Ferrone, Methods Enzymol. 309, 256 (1999). 10.1016/S0076-6879(99) 09019-9 (Pubitemid 29446454)
    • (1999) Methods in Enzymology , vol.309 , pp. 256-274
    • Ferrone, F.1
  • 61
    • 0034875603 scopus 로고    scopus 로고
    • 10.1016/S0006-3495(01)75831-6
    • M. M. Pallitto and R. M. Murphy, Biophys. J. 81, 1805 (2001). 10.1016/S0006-3495(01)75831-6
    • (2001) Biophys. J. , vol.81 , pp. 1805
    • Pallitto, M.M.1    Murphy, R.M.2
  • 64
    • 0025206430 scopus 로고
    • 10.1021/j100364a063
    • M. E. Cates, J. Phys. Chem. 94, 371 (1990). 10.1021/j100364a063
    • (1990) J. Phys. Chem. , vol.94 , pp. 371
    • Cates, M.E.1
  • 72
    • 0032968132 scopus 로고    scopus 로고
    • Quantifying the kinetic parameters of prion replication
    • DOI 10.1016/S0301-4622(99)00016-2, PII S0301462299000162
    • J. Masel, V. A. Jansen, and M. A. Nowak, Biophys. Chem. 77, 139 (1999). 10.1016/S0301-4622(99)00016-2 (Pubitemid 29206647)
    • (1999) Biophysical Chemistry , vol.77 , Issue.2-3 , pp. 139-152
    • Masel, J.1    Jansen, V.A.A.2    Nowak, M.A.3
  • 77
    • 0037046151 scopus 로고    scopus 로고
    • Islet amyloid: Phase partitioning and secondary nucleation are central to the mechanism of fibrillogenesis
    • DOI 10.1021/bi0160462
    • S. B. Padrick and A. D. Miranker, Biochemistry 41, 4694 (2002). 10.1021/bi0160462 (Pubitemid 34275671)
    • (2002) Biochemistry , vol.41 , Issue.14 , pp. 4694-4703
    • Padrick, S.B.1    Miranker, A.D.2
  • 80
    • 28844482969 scopus 로고    scopus 로고
    • The kinetic behavior of insulin fibrillation is determined by heterogeneous nucleation pathways
    • DOI 10.1110/ps.051692305
    • F. Librizzi and C. Rischel, Protein Sci. 14, 3129 (2005). 10.1110/ps.051692305 (Pubitemid 41770153)
    • (2005) Protein Science , vol.14 , Issue.12 , pp. 3129-3134
    • Librizzi, F.1    Rischel, C.2
  • 84
    • 39749112546 scopus 로고    scopus 로고
    • Fitting neurological protein aggregation kinetic data via a 2-step, minimal/"Ockham's razor" model: The Finke-Watzky mechanism of nucleation followed by autocatalytic surface growth
    • DOI 10.1021/bi701899y
    • A. M. Morris, M. A. Watzky, J. N. Agar, and R. G. Finke, Biochemistry 47, 2413 (2008). 10.1021/bi701899y (Pubitemid 351304547)
    • (2008) Biochemistry , vol.47 , Issue.8 , pp. 2413-2427
    • Morris, A.M.1    Watzky, M.A.2    Agar, J.N.3    Finke, R.G.4
  • 85
  • 89
    • 33749597429 scopus 로고    scopus 로고
    • Nucleation: The Connections Between Equilibrium and Kinetic Behavior
    • DOI 10.1016/S0076-6879(06)12017-0, PII S0076687906120170
    • F. A. Ferrone, Methods Enzymol. 412, 285 (2006). 10.1016/S0076-6879(06) 12017-0 (Pubitemid 44548586)
    • (2006) Methods in Enzymology , vol.412 , pp. 285-299
    • Ferrone, F.A.1
  • 91
    • 0022799567 scopus 로고
    • 10.1016/S0006-3495(86)83498-1
    • R. F. Goldstein and L. Stryer, Biophys. J. 50, 583 (1986). 10.1016/S0006-3495(86)83498-1
    • (1986) Biophys. J. , vol.50 , pp. 583
    • Goldstein, R.F.1    Stryer, L.2
  • 92
    • 0027697983 scopus 로고
    • 10.1557/JMR.1993.2889
    • M. Ataka and T. Ogawa, J. Mater. Res. 11, 2889 (1993). 10.1557/JMR.1993.2889
    • (1993) J. Mater. Res. , vol.11 , pp. 2889
    • Ataka, M.1    Ogawa, T.2
  • 96
    • 33749824175 scopus 로고    scopus 로고
    • 10.1021/ar050069h
    • R. Wetzel, Acc. Chem. Res. 39, 671 (2006). 10.1021/ar050069h
    • (2006) Acc. Chem. Res. , vol.39 , pp. 671
    • Wetzel, R.1
  • 97
    • 34250834054 scopus 로고    scopus 로고
    • A Lumry-Eyring nucleated polymerization model of protein aggregation kinetics: 1. Aggregation with pre-equilibrated unfolding
    • DOI 10.1021/jp070212j
    • J. M. Andrews and C. J. Roberts, J. Phys. Chem. B 111, 7897 (2007). 10.1021/jp070212j (Pubitemid 47169702)
    • (2007) Journal of Physical Chemistry B , vol.111 , Issue.27 , pp. 7897-7913
    • Andrews, J.M.1    Roberts, C.J.2
  • 103
    • 33846005437 scopus 로고    scopus 로고
    • Absolute Correlation between Lag Time and Growth Rate in the Spontaneous Formation of Several Amyloid-like Aggregates and Fibrils
    • DOI 10.1016/j.jmb.2006.11.009, PII S0022283606015385
    • M. Fndrich, J. Mol. Biol. 365, 1266 (2007). 10.1016/j.jmb.2006.11.009 (Pubitemid 46048846)
    • (2007) Journal of Molecular Biology , vol.365 , Issue.5 , pp. 1266-1270
    • Fandrich, M.1
  • 106
    • 0035814918 scopus 로고    scopus 로고
    • Bidirectional amyloid fiber growth for a yeast prion determinant
    • DOI 10.1016/S0960-9822(01)00099-9
    • T. Scheibel, A. S. Kowal, J. D. Bloom, and S. L. Lindquist, Curr. Biol. 11, 366 (2001). 10.1016/S0960-9822(01)00099-9 (Pubitemid 32200741)
    • (2001) Current Biology , vol.11 , Issue.5 , pp. 366-369
    • Scheibel, T.1    Kowal, A.S.2    Bloom, J.D.3    Lindquist, S.L.4
  • 107
    • 0036233931 scopus 로고    scopus 로고
    • Origins and kinetic consequences of diversity in Sup35 yeast prion fibers
    • DOI 10.1038/nsb786
    • A. H. DePace and J. S. Weissman, Nat. Struct. Biol. 9, 389 (2002). 10.1038/nsb786 (Pubitemid 34462559)
    • (2002) Nature Structural Biology , vol.9 , Issue.5 , pp. 389-396
    • DePace, A.H.1    Weissman, J.S.2
  • 109
    • 1842577741 scopus 로고    scopus 로고
    • Onset of heterogeneous crystal nucleation in colloidal suspensions
    • DOI 10.1038/nature02397
    • A. Cacciuto, S. Auer, and D. Frenkel, Nature (London) 428, 404 (2004). 10.1038/nature02397 (Pubitemid 38419681)
    • (2004) Nature , vol.428 , Issue.6981 , pp. 404-406
    • Cacciuto, A.1    Auer, S.2    Frenkei, D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.