메뉴 건너뛰기




Volumn 6, Issue 4, 2010, Pages 1337-1341

Fabrication and characterisation of protein fibril-elastomer composites

Author keywords

Anisotropy; Carbon nanotube; Elastomer; Protein fibril; Rigidity

Indexed keywords

CARBON NANOTUBES; ELASTOMERS; ENZYMES; FABRICATION; FILLING; PLASTICS; RIGIDITY; SILICONES; YARN;

EID: 76949103284     PISSN: 17427061     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.actbio.2009.10.013     Document Type: Article
Times cited : (18)

References (20)
  • 1
    • 23144442139 scopus 로고    scopus 로고
    • Self-assembled peptide nanotubes are uniquely rigid bioinspired supramolecular structures
    • Kol N., Adler-Abramovich L., Barlam D., Shneck R.Z., Gazit E., and Rousso I. Self-assembled peptide nanotubes are uniquely rigid bioinspired supramolecular structures. Nano Lett 5 (2005) 1343-1346
    • (2005) Nano Lett , vol.5 , pp. 1343-1346
    • Kol, N.1    Adler-Abramovich, L.2    Barlam, D.3    Shneck, R.Z.4    Gazit, E.5    Rousso, I.6
  • 2
    • 47049100201 scopus 로고    scopus 로고
    • Amyloids: not only pathological agents but also ordered nanomaterials
    • Cherny I., and Gazit E. Amyloids: not only pathological agents but also ordered nanomaterials. Angew Chem Int Ed 47 (2008) 4062-4069
    • (2008) Angew Chem Int Ed , vol.47 , pp. 4062-4069
    • Cherny, I.1    Gazit, E.2
  • 3
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • Dobson C.M. Protein folding and misfolding. Nature 426 (2003) 884-890
    • (2003) Nature , vol.426 , pp. 884-890
    • Dobson, C.M.1
  • 4
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • Chiti F., and Dobson C.M. Protein misfolding, functional amyloid, and human disease. Annu Rev Biochem 75 (2006) 333-366
    • (2006) Annu Rev Biochem , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 5
  • 6
    • 0033200063 scopus 로고    scopus 로고
    • Protein misfolding, evolution, and disease
    • Dobson C.M. Protein misfolding, evolution, and disease. Trends Biochem Sci 24 (1999) 329-332
    • (1999) Trends Biochem Sci , vol.24 , pp. 329-332
    • Dobson, C.M.1
  • 7
    • 0141765883 scopus 로고    scopus 로고
    • Fabrication of novel biomaterials through molecular self-assembly
    • Zhang S. Fabrication of novel biomaterials through molecular self-assembly. Nat Biotechnol 21 (2003) 1171-1177
    • (2003) Nat Biotechnol , vol.21 , pp. 1171-1177
    • Zhang, S.1
  • 8
    • 3242834384 scopus 로고    scopus 로고
    • Exceptionally high young's modulus observed for individual carbon nanotubes
    • Treacy M.M., Ebbesen T.W., and Gibson T.M. Exceptionally high young's modulus observed for individual carbon nanotubes. Nature 381 (1996) 678-680
    • (1996) Nature , vol.381 , pp. 678-680
    • Treacy, M.M.1    Ebbesen, T.W.2    Gibson, T.M.3
  • 9
    • 33645385898 scopus 로고    scopus 로고
    • Mechanical reinforcement of polymers using carbon nanotubes
    • Coleman J.N., Khan U., and Gunko Y.K. Mechanical reinforcement of polymers using carbon nanotubes. Adv Mater 18 (2006) 689-706
    • (2006) Adv Mater , vol.18 , pp. 689-706
    • Coleman, J.N.1    Khan, U.2    Gunko, Y.K.3
  • 10
    • 35948972832 scopus 로고    scopus 로고
    • Direct imaging of single-walled carbon nanotubes in cells
    • Porter A.E., et al. Direct imaging of single-walled carbon nanotubes in cells. Nat Nanotechnol 2 (2007) 713-717
    • (2007) Nat Nanotechnol , vol.2 , pp. 713-717
    • Porter, A.E.1
  • 11
    • 0036897817 scopus 로고    scopus 로고
    • Design of nanostructured biological materials through self-assembly of peptides and proteins
    • Zhang S., Marini D.M., Hwang W., and Santoso S. Design of nanostructured biological materials through self-assembly of peptides and proteins. Curr Opin Chem Biol 6 (2002) 865-871
    • (2002) Curr Opin Chem Biol , vol.6 , pp. 865-871
    • Zhang, S.1    Marini, D.M.2    Hwang, W.3    Santoso, S.4
  • 15
    • 0036468673 scopus 로고    scopus 로고
    • Role of Escherichia coli curli operons in directing amyloid fiber formation
    • Chapman M.R. Role of Escherichia coli curli operons in directing amyloid fiber formation. Science 295 (2002) 851-854
    • (2002) Science , vol.295 , pp. 851-854
    • Chapman, M.R.1
  • 16
    • 33750480868 scopus 로고    scopus 로고
    • Characterization of the nanoscale properties of individual amyloid fibrils
    • Smith J.F., Knowles T.P.J., Dobson C.M., MacPhee C.E., and Welland M.E. Characterization of the nanoscale properties of individual amyloid fibrils. PNAS 103 (2006) 15806-15811
    • (2006) PNAS , vol.103 , pp. 15806-15811
    • Smith, J.F.1    Knowles, T.P.J.2    Dobson, C.M.3    MacPhee, C.E.4    Welland, M.E.5
  • 17
    • 76949097228 scopus 로고    scopus 로고
    • Dispersion and rheology of carbon nanotubes in polymers
    • Huang Y.Y., and Terentjev E.M. Dispersion and rheology of carbon nanotubes in polymers. Int J Mater Form 1 (2006) 63-74
    • (2006) Int J Mater Form , vol.1 , pp. 63-74
    • Huang, Y.Y.1    Terentjev, E.M.2
  • 18
    • 0037008487 scopus 로고    scopus 로고
    • Carbon nanotubes the route toward applications
    • Baughman R.H., Zakhidov A.A., and de Heer W.A. Carbon nanotubes the route toward applications. Science 297 (2002) 787-792
    • (2002) Science , vol.297 , pp. 787-792
    • Baughman, R.H.1    Zakhidov, A.A.2    de Heer, W.A.3
  • 19
    • 33750704606 scopus 로고    scopus 로고
    • Mechanics of prestressed polydimethylsiloxane-carbon nanotubecomposite
    • Paul J., et al. Mechanics of prestressed polydimethylsiloxane-carbon nanotubecomposite. Appl Phys Lett 89 (2006) 184101-184103
    • (2006) Appl Phys Lett , vol.89 , pp. 184101-184103
    • Paul, J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.