메뉴 건너뛰기




Volumn 135, Issue 5, 2011, Pages

An effective continuum approach for modeling non-equilibrium structural evolution of protein nanofiber networks

Author keywords

[No Author keywords available]

Indexed keywords

CHARACTERISTIC LENGTH; CHARACTERISTIC TIME; CHEMICAL ENVIRONMENT; CHEMICAL FLUX; CONTINUUM EQUATION; EXTERNAL LOADING; FIRST-ORDER; GROWTH MEASUREMENT; MODELING FRAMEWORKS; MODELING TOOL; MONOMER STRUCTURES; NANO SCALE; NON EQUILIBRIUM; NON-LINEAR FINITE ELEMENTS; NUMERICAL MODELS; PHASE-FIELD MODELING; PROTEIN EVOLUTION; QUANTITATIVE PREDICTION; RATE MEASUREMENTS; SEED PARTICLE; SELF-ASSEMBLING; SELF-ASSEMBLY BEHAVIORS; STRUCTURAL EVOLUTION; THEORETICAL FRAMEWORK; TIME-DEPENDENT; TIME-SCALES; VECTOR ORDER PARAMETER;

EID: 80051696463     PISSN: 00219606     EISSN: None     Source Type: Journal    
DOI: 10.1063/1.3622489     Document Type: Article
Times cited : (8)

References (53)
  • 1
    • 33748770352 scopus 로고    scopus 로고
    • Slow release of molecules in self-assembling peptide nanofiber scaffold
    • DOI 10.1016/j.jconrel.2006.06.031, PII S0168365906003270
    • Y. Nagai, L. D. Unsworth, S. Koutsopoulos, and S. Zhang, J. Controlled Release 115, 18 (2006). 10.1016/j.jconrel.2006.06.031 (Pubitemid 44415076)
    • (2006) Journal of Controlled Release , vol.115 , Issue.1 , pp. 18-25
    • Nagai, Y.1    Unsworth, L.D.2    Koutsopoulos, S.3    Zhang, S.4
  • 6
    • 0022419375 scopus 로고
    • 10.1126/science.3892686
    • S. K. Burleyand and G. A. Petsko, Science 229, 23 (1985). 10.1126/science.3892686
    • (1985) Science , vol.229 , pp. 23
    • Burleyand, S.K.1    Petsko, G.A.2
  • 9
    • 39049132284 scopus 로고    scopus 로고
    • Self-assembling peptide nanofiber scaffolds accelerate wound healing
    • DOI 10.1371/journal.pone.0001410
    • A. Schneider, J. A. Garlick, and C. Egles, PLoS ONE 3 (1), 1410 (2008). 10.1371/journal.pone.0001410 (Pubitemid 351234508)
    • (2008) PLoS ONE , vol.3 , Issue.1
    • Schneider, A.1    Garlick, J.A.2    Egles, C.3
  • 14
    • 8844247180 scopus 로고    scopus 로고
    • Mechanism of prion propagation: Amyloid growth occurs by monomer addition
    • DOI 10.1371/journal.pbio.0020321
    • S. Collins, A. Douglass, R. Vale, and J. Weissman, PLoS Biology 2, 1582 (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
  • 25
    • 33748604047 scopus 로고    scopus 로고
    • PROFASI: A Monte Carlo simulation package for protein folding and aggregation
    • DOI 10.1002/jcc.20452
    • A. Irbck and S. Mohanty, J. Comput. Chem. 27, 1548 (2006). 10.1002/jcc.20452 (Pubitemid 44375668)
    • (2006) Journal of Computational Chemistry , vol.27 , Issue.13 , pp. 1548-1555
    • Irback, A.1    Mohanty, S.2
  • 27
    • 0031555024 scopus 로고    scopus 로고
    • 10.1002/(SICI)1097-0282(19971005)42:4399::AID-BIP33.0.CO;2-L
    • P. Gupta and C. K. Hall, Biopolymers 42, 399 (1997). 10.1002/(SICI)1097- 0282(19971005)42:4399::AID-BIP33.0.CO;2-L
    • (1997) Biopolymers , vol.42 , pp. 399
    • Gupta, P.1    Hall, C.K.2
  • 29
    • 0037203044 scopus 로고    scopus 로고
    • Effect of rate of chemical or thermal renaturation on refolding and aggregation of a simple lattice protein
    • DOI 10.1002/bit.10448
    • C. K. H. Hung D. Nguyen, Biotechnology and Bioengineering 80, 823 (2002). 10.1002/bit.10448 (Pubitemid 35423756)
    • (2002) Biotechnology and Bioengineering , vol.80 , Issue.7 , pp. 823-834
    • Nguyen, H.D.1    Hall, C.K.2
  • 30
    • 29144520935 scopus 로고    scopus 로고
    • 10.1016/j.jc2005.07.020
    • Q. Du, C. Liu, and X. Wang, J. Comput. Phys. 212, 757 (2006). 10.1016/j.jcp.2005.07.020
    • (2006) J. Comput. Phys. , vol.212 , pp. 757
    • Du, Q.1    Liu, C.2    Wang, X.3
  • 31
    • 33750293016 scopus 로고    scopus 로고
    • Dual fluorescence and laser emissions from fluorescein-Na and eosin-B
    • DOI 10.1016/j.jlumin.2005.11.013, PII S0022231305002966
    • Q. Du and L. Zhu, J. Comput. Math. 24, 265 (2006). 10.1016/j.jlumin.2005. 11.013 (Pubitemid 44633062)
    • (2006) Journal of Luminescence , vol.121 , Issue.2 SPEC. ISS. , pp. 475-487
    • Math, N.N.1    Naik, L.R.2    Suresh, H.M.3    Inamdar, S.R.4
  • 34
    • 64049116424 scopus 로고    scopus 로고
    • 10.1016/j.jc2009.02.034
    • L. Gao, X. Feng, and H. Gao, J. Comput. Phys. 228, 4162 (2009). 10.1016/j.jcp.2009.02.034
    • (2009) J. Comput. Phys. , vol.228 , pp. 4162
    • Gao, L.1    Feng, X.2    Gao, H.3
  • 35
    • 0032877134 scopus 로고
    • 10.1016/S0076-6879(99)09019-9
    • F. Ferrone, Methods Enzymol. 309, 256 (1987). 10.1016/S0076-6879(99) 09019-9
    • (1987) Methods Enzymol. , vol.309 , pp. 256
    • Ferrone, F.1
  • 36
    • 0001158204 scopus 로고    scopus 로고
    • 10.1016/0167-2789(95)00173-5
    • M. E. Gurtin, Physica D 92, 178 (1996). 10.1016/0167-2789(95)00173-5
    • (1996) Physica D , vol.92 , pp. 178
    • Gurtin, M.E.1
  • 37
    • 33845227062 scopus 로고    scopus 로고
    • Continuum thermodynamics of ferroelectric domain evolution: Theory, finite element implementation, and application to domain wall pinning
    • DOI 10.1016/j.jmps.2006.07.006, PII S0022509606001256
    • Y. Su and C. M. Landis, J. Mech. Phys. Solids 55, 280 (2007). 10.1016/j.jmps.2006.07.006 (Pubitemid 44855782)
    • (2007) Journal of the Mechanics and Physics of Solids , vol.55 , Issue.2 , pp. 280-305
    • Su, Y.1    Landis, C.M.2
  • 38
    • 0036497120 scopus 로고    scopus 로고
    • 10.1103/PhysRevB.65.104111
    • B. Meyer and D. Vanderbilt, Phys. Rev. B 65, 104111 (2002). 10.1103/PhysRevB.65.104111
    • (2002) Phys. Rev. B , vol.65 , pp. 104111
    • Meyer, B.1    Vanderbilt, D.2
  • 41
    • 26544469625 scopus 로고
    • 10.1016/0167-2789(94)90234-8
    • E. Fried and M. E. Gurtin, Physica D 72, 287 (1994). 10.1016/0167- 2789(94)90234-8
    • (1994) Physica D , vol.72 , pp. 287
    • Fried, E.1    Gurtin, M.E.2
  • 43
    • 43449102981 scopus 로고
    • 10.1016/0001-6160(61)90182-1
    • J. Cahn, Acta Metall. 9, 795 (1961). 10.1016/0001-6160(61)90182-1
    • (1961) Acta Metall. , vol.9 , pp. 795
    • Cahn, J.1
  • 50
    • 17644397372 scopus 로고    scopus 로고
    • Aβ40-lactam(D23/K28) models a conformation highly favorable for nucleation of amyloid
    • DOI 10.1021/bi0474867
    • K. L. Sciarretta, D. J. Gordon, A. T. Petkova, R. Tycko, and S. C. Meredith, Biochemistry 44, 6003 (2005). 10.1021/bi0474867 (Pubitemid 40570694)
    • (2005) Biochemistry , vol.44 , Issue.16 , pp. 6003-6014
    • Sciarretta, K.L.1    Gordon, D.J.2    Petkova, A.T.3    Tycko, R.4    Meredith, S.C.5
  • 52
    • 1642417648 scopus 로고    scopus 로고
    • Amyloid fibrils from the viewpoint of protein folding
    • DOI 10.1007/s00018-003-3264-8
    • S. Ohnishi and K. Takano, Cell. Mol. Life Sci. 61, 511 (2004). 10.1007/s00018-003-3264-8 (Pubitemid 38372906)
    • (2004) Cellular and Molecular Life Sciences , vol.61 , Issue.5 , pp. 511-524
    • Ohnishi, S.1    Takano, K.2
  • 53
    • 77949262233 scopus 로고    scopus 로고
    • 10.1038/nnano.2010.28
    • M. J. Buehler, Nat. Nanotechnol. 5, 172 (2010). 10.1038/nnano.2010.28
    • (2010) Nat. Nanotechnol. , vol.5 , pp. 172
    • Buehler, M.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.