메뉴 건너뛰기




Volumn 9, Issue 7, 2014, Pages 537-541

Amyloid fibrils nucleated and organized by DNA origami constructions

Author keywords

[No Author keywords available]

Indexed keywords

CHEMICAL STABILITY; ELASTIC MODULI; GLYCOPROTEINS; METAL NANOPARTICLES; NANOTUBES; NEURODEGENERATIVE DISEASES; PEPTIDES; YARN;

EID: 84904036284     PISSN: 17483387     EISSN: 17483395     Source Type: Journal    
DOI: 10.1038/nnano.2014.102     Document Type: Article
Times cited : (75)

References (31)
  • 2
    • 79961211353 scopus 로고    scopus 로고
    • Nanomechanics of functional and pathological amyloid materials
    • Knowles, T. P. J. & Buehler, M. J. Nanomechanics of functional and pathological amyloid materials. Nature Nanotech. 6, 469-479 (2011).
    • (2011) Nature Nanotech. , vol.6 , pp. 469-479
    • Knowles, T.P.J.1    Buehler, M.J.2
  • 5
    • 0033616575 scopus 로고    scopus 로고
    • Designing conditions for in vitro formation of amyloid protofilaments and fibrils
    • Chiti, F. et al. Designing conditions for in vitro formation of amyloid protofilaments and fibrils. Proc. Natl Acad. Sci. USA 96, 3590-3594 (1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 3590-3594
    • Chiti, F.1
  • 6
    • 34249739081 scopus 로고    scopus 로고
    • Amyloid fibrils: From disease to design New biomaterial applications for self-Assembling cross-beta fibrils
    • Gras, S. L. Amyloid fibrils: From disease to design. New biomaterial applications for self-Assembling cross-beta fibrils. Aust. J. Chem. 60, 333-342 (2007).
    • (2007) Aust. J. Chem. , vol.60 , pp. 333-342
    • Gras, S.L.1
  • 7
    • 0020373595 scopus 로고
    • Nucleic acid junctions and lattice
    • Seeman, N. C. Nucleic acid junctions and lattice. J. Theor. Biol. 99, 237-247 (1982).
    • (1982) J. Theor. Biol. , vol.99 , pp. 237-247
    • Seeman, N.C.1
  • 8
    • 77953645331 scopus 로고    scopus 로고
    • Nanomaterials based on DNA
    • Seeman, N. C. Nanomaterials based on DNA. Annu. Rev. Biochem. 79, 65-87 (2010).
    • (2010) Annu. Rev. Biochem. , vol.79 , pp. 65-87
    • Seeman, N.C.1
  • 9
    • 0025801516 scopus 로고
    • Normal transthyretin and synthetic transthyretin fragments form amyloid-like fibrils in vitro
    • Gustavsson, A., Engstrom, U. & Westermark, P. Normal transthyretin and synthetic transthyretin fragments form amyloid-like fibrils in vitro. Biochem. Biophys. Res. Commun. 175, 1159-1164 (1991).
    • (1991) Biochem. Biophys. Res. Commun. , vol.175 , pp. 1159-1164
    • Gustavsson, A.1    Engstrom, U.2    Westermark, P.3
  • 10
    • 33645028600 scopus 로고    scopus 로고
    • Folding DNA to create nanoscale shapes and patterns
    • Rothemund, P. W. K. Folding DNA to create nanoscale shapes and patterns. Nature 440, 297-302 (2006).
    • (2006) Nature , vol.440 , pp. 297-302
    • Rothemund, P.W.K.1
  • 11
    • 33744819149 scopus 로고    scopus 로고
    • Design of minimally strained nucleic acid nanotubes
    • Sherman, W. B. & Seeman, N. C. Design of minimally strained nucleic acid nanotubes. Biophys. J. 90, 4546-4547 (2006).
    • (2006) Biophys. J. , vol.90 , pp. 4546-4547
    • Sherman, W.B.1    Seeman, N.C.2
  • 12
    • 84875871051 scopus 로고    scopus 로고
    • Atomic structure and hierarchical assembly of a cross-b amyloid fibril
    • Fitzpatrick, A. W. P. et al. Atomic structure and hierarchical assembly of a cross-b amyloid fibril. Proc. Natl Acad. Sci. USA 110, 5468-5473 (2013).
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. 5468-5473
    • Fitzpatrick, A.W.P.1
  • 14
    • 77958453230 scopus 로고    scopus 로고
    • Accurate determination of interstrand distances and alignment in amyloid fibrils by magic angle spinning NMR
    • Caporini, M. A. et al. Accurate determination of interstrand distances and alignment in amyloid fibrils by magic angle spinning NMR. J. Phys. Chem. B 114, 13555-13561 (2010).
    • (2010) J. Phys. Chem. , vol.B114 , pp. 13555-13561
    • Caporini, M.A.1
  • 15
    • 84863989612 scopus 로고    scopus 로고
    • Noncore residues influence the kinetics of functional TTR105-115-based amyloid fibril assembly
    • Bongiovanni, M. N., Puri, D., Goldie, K. N. & Gras, S. L. Noncore residues influence the kinetics of functional TTR105-115-based amyloid fibril assembly. J. Mol. Biol. 421, 256-269 (2012).
    • (2012) J. Mol. Biol. , vol.421 , pp. 256-269
    • Bongiovanni, M.N.1    Puri, D.2    Goldie, K.N.3    Gras, S.L.4
  • 16
    • 84874407281 scopus 로고    scopus 로고
    • Lysine functionalised amyloid fibrils: The design and assembly of a TTR1-based peptide
    • Bongiovanni, M. N., Caruso, F. & Gras, S. L. Lysine functionalised amyloid fibrils: The design and assembly of a TTR1-based peptide. Soft Matter 9, 3315-3330 (2013).
    • (2013) Soft Matter , vol.9 , pp. 3315-3330
    • Bongiovanni, M.N.1    Caruso, F.2    Gras, S.L.3
  • 17
    • 38749119393 scopus 로고    scopus 로고
    • Functionalized amyloid fibrils for roles in cell adhesion
    • Gras, S. L. et al. Functionalized amyloid fibrils for roles in cell adhesion. Biomaterials 29, 1553-1562 (2008).
    • (2008) Biomaterials , vol.29 , pp. 1553-1562
    • Gras, S.L.1
  • 18
    • 0034722985 scopus 로고    scopus 로고
    • Formation of mixed fibrils demonstrates the generic nature and potential utility of amyloid nanostructures
    • MacPhee, C. E. & Dobson, C. M. Formation of mixed fibrils demonstrates the generic nature and potential utility of amyloid nanostructures. J. Am. Chem. Soc. 122, 12707-12713 (2000).
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 12707-12713
    • MacPhee, C.E.1    Dobson, C.M.2
  • 20
    • 28644437048 scopus 로고    scopus 로고
    • The importance of sequence diversity to the aggregation and evolution of proteins
    • Wright, C. F., Teichmann, S. A., Clark, J. & Dobson, C. M. The importance of sequence diversity to the aggregation and evolution of proteins. Nature 438, 878-881 (2005).
    • (2005) Nature , vol.438 , pp. 878-881
    • Wright, C.F.1    Teichmann, S.A.2    Clark, J.3    Dobson, C.M.4
  • 21
    • 84863989612 scopus 로고    scopus 로고
    • Noncore residues influence the kinetics of functional TTR105-115-based amyloid fibril assembly
    • Bongiovanni, M. N., Puri, D., Goldie, K. N. & Gras, S. L. Noncore residues influence the kinetics of functional TTR105-115-based amyloid fibril assembly. J. Mol. Biol. 421, 256-269 (2012).
    • (2012) J. Mol. Biol. , vol.421 , pp. 256-269
    • Bongiovanni, M.N.1    Puri, D.2    Goldie, K.N.3    Gras, S.L.4
  • 22
    • 17244381236 scopus 로고    scopus 로고
    • Microarrays of peptide fibrils created by electrostatically controlled deposition
    • Mesquida, P., Ammann, D. L., MacPhee, C. E. & McKendry, R. A. Microarrays of peptide fibrils created by electrostatically controlled deposition. Adv. Mater. 17, 893-897 (2005).
    • (2005) Adv. Mater. , vol.17 , pp. 893-897
    • Mesquida, P.1    Ammann, D.L.2    MacPhee, C.E.3    McKendry, R.A.4
  • 23
    • 33751424745 scopus 로고    scopus 로고
    • Patterning amyloid peptide fibrils by AFM charge writing
    • Mesquida, P., Blanco, E. M. & McKendry, R. A. Patterning amyloid peptide fibrils by AFM charge writing. Langmuir 22, 9089-9091 (2006).
    • (2006) Langmuir , vol.22 , pp. 9089-9091
    • Mesquida, P.1    Blanco, E.M.2    McKendry, R.A.3
  • 24
    • 41549137864 scopus 로고    scopus 로고
    • Two-dimensional graphene nanoribbons
    • Yang, X. et al. Two-dimensional graphene nanoribbons. J. Am. Chem. Soc. 130, 4216-4217 (2008).
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 4216-4217
    • Yang, X.1
  • 25
    • 77952861540 scopus 로고    scopus 로고
    • Peptide/graphene hybrid assembly into core/shell nanowires
    • Han, T. H. et al. Peptide/graphene hybrid assembly into core/shell nanowires. Adv. Mater. 22, 2060-2064 (2010).
    • (2010) Adv. Mater. , vol.22 , pp. 2060-2064
    • Han, T.H.1
  • 26
    • 84863715767 scopus 로고    scopus 로고
    • Biodegradable nanocomposites of amyloid fibrils and graphene with shape-memory and enzyme-sensing properties
    • Li, C., Adamcik, J. & Raffaele Mezzenga, R. Biodegradable nanocomposites of amyloid fibrils and graphene with shape-memory and enzyme-sensing properties. Nature Nanotech. 7, 421-427 (2012).
    • (2012) Nature Nanotech. , vol.7 , pp. 421-427
    • Li, C.1    Adamcik, J.2    Raffaele Mezzenga, R.3
  • 27
    • 0025635653 scopus 로고
    • De novo design of sequences for nucleic acid structure engineering
    • Seeman, N. C. De novo design of sequences for nucleic acid structure engineering. J. Biomol. Struct. Dyn. 8, 573-581 (1990).
    • (1990) J. Biomol. Struct. Dyn. , vol.8 , pp. 573-581
    • Seeman, N.C.1
  • 28
    • 20744456789 scopus 로고
    • Solid phase peptide synthesis i the synthesis of a tetrapeptide
    • Merrifield, R. B. Solid phase peptide synthesis. I. The synthesis of a tetrapeptide. J. Am. Chem. Soc. 85, 2149-2154 (1963).
    • (1963) J. Am. Chem. Soc. , vol.85 , pp. 2149-2154
    • Merrifield, R.B.1
  • 29
    • 38749119393 scopus 로고    scopus 로고
    • Functionalized amyloid fibrils for roles in cell adhesion
    • Gras, S. L. et al. Functionalized amyloid fibrils for roles in cell adhesion. Biomaterials 29, 1553-1562 (2008).
    • (2008) Biomaterials , vol.29 , pp. 1553-1562
    • Gras, S.L.1
  • 30
    • 0036849859 scopus 로고    scopus 로고
    • Blu-ice and the distributed control system: Software for data acquisition and instrument control at macromolecular crystallography beamlines
    • McPhillips, T. M. et al. Blu-ice and the distributed control system: Software for data acquisition and instrument control at macromolecular crystallography beamlines. J. Synchrotron Radiat. 9, 401-406 (2002).
    • (2002) J. Synchrotron Radiat. , vol.9 , pp. 401-406
    • McPhillips, T.M.1
  • 31
    • 85029160761 scopus 로고    scopus 로고
    • http://www.nanoengineer-1.com/content/


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.