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Volumn 13, Issue 3, 2012, Pages 232-257

Characterization of fiber-forming peptides and proteins by means of atomic force microscopy

Author keywords

Antibody recognition imaging; Atomic force microscopy; Peptide fibers; Protein aggregation

Indexed keywords

ALPHA SYNUCLEIN; AMYLOID; AMYLOID BETA PROTEIN; MONOMER; OLIGOMER; PEPTIDES AND PROTEINS; SYNTHETIC PEPTIDE;

EID: 84862584933     PISSN: 13892037     EISSN: 18755550     Source Type: Journal    
DOI: 10.2174/138920312800785058     Document Type: Article
Times cited : (11)

References (230)
  • 3
    • 0028364295 scopus 로고
    • Biomolecular imaging with the atomic force microscope
    • Hansma, H.; Hoh, J. Biomolecular imaging with the atomic force microscope. Annu. Rev. Biophys. Biomol. Struct. 1994, 23, 115-139.
    • (1994) Annu. Rev. Biophys. Biomol. Struct , vol.23 , pp. 115-139
    • Hansma, H.1    Hoh, J.2
  • 4
    • 0029439550 scopus 로고
    • Scanning probe microscopy in microbiology
    • Firtel, M.; Beveridge, T. J. Scanning probe microscopy in microbiology. Micron, 1995, 26, 347-362.
    • (1995) Micron , vol.26 , pp. 347-362
    • Firtel, M.1    Beveridge, T.J.2
  • 5
    • 43449133266 scopus 로고    scopus 로고
    • Atomic force microscopy as a multifunctional molecular toolbox in nanobiotechnology
    • Müller, D. J.; Dufrêne, Y. F. Atomic force microscopy as a multifunctional molecular toolbox in nanobiotechnology. Nat. Nanotechnol. 2008, 3, 261-1269.
    • (2008) Nat. Nanotechnol , vol.3 , pp. 261-1269
    • Müller, D.J.1    Dufrêne, Y.F.2
  • 8
    • 1242271244 scopus 로고    scopus 로고
    • An overview of the biophysical applications of atomic force microscopy
    • Santos, N. C.; Castanho, M. R. B. An overview of the biophysical applications of atomic force microscopy. Biophys. Chem. 2004, 107, 133-149.
    • (2004) Biophys. Chem , vol.107 , pp. 133-149
    • Santos, N.C.1    Castanho, M.R.B.2
  • 9
    • 0032177654 scopus 로고    scopus 로고
    • Atomic force microscopy and other scanning probe microscopies
    • Hansma, H.; Pietrasanta, L. Atomic force microscopy and other scanning probe microscopies. Curr. Opin. Chem. Biol. 1998, 579-584.
    • (1998) Curr. Opin. Chem. Biol , pp. 579-584
    • Hansma, H.1    Pietrasanta, L.2
  • 10
    • 22944466397 scopus 로고    scopus 로고
    • Imaging proteins with atomic force microscopy: An overview
    • Silva, L. P. Imaging proteins with atomic force microscopy: an overview. Curr. Protein Pept. Sci. 2005, 6, 387-395.
    • (2005) Curr. Protein Pept. Sci , vol.6 , pp. 387-395
    • Silva, L.P.1
  • 12
    • 0036712485 scopus 로고    scopus 로고
    • Dynamic atomic force microscopy methods
    • García, R. Dynamic atomic force microscopy methods. Surf. Sci.Rep.2002, 47, 197-301.
    • (2002) Surf. Sci.Rep , vol.47 , pp. 197-301
    • García, R.1
  • 14
    • 0031122070 scopus 로고    scopus 로고
    • Phase imaging and stiffness in tapping-mode atomic force microscopy
    • Magonov, S. N, Elings, V.; Whangbo, M.-H. Phase imaging and stiffness in tapping-mode atomic force microscopy. Surf. Sci. 1997, 375, L385-L391.
    • (1997) Surf. Sci , vol.375
    • Magonov, S.N.1    Elings, V.2    Whangbo, M.-H.3
  • 15
    • 16644390418 scopus 로고    scopus 로고
    • Relationship between phase shift and energy dissipation in tapping-mode scanning force microscopy
    • Tamayo, J.; Garc, R. Relationship between phase shift and energy dissipation in tapping-mode scanning force microscopy. Appl. Phys. Lett. 1998, 73, 2926-2928.
    • (1998) Appl. Phys. Lett , vol.73 , pp. 2926-2928
    • Tamayo, J.1    Garc, R.2
  • 16
    • 0029637281 scopus 로고
    • Atomic resolution of the silicon (111)-(7x7) surface by atomic force microscopy
    • Giessibl, F. J. Atomic resolution of the silicon (111)-(7x7) surface by atomic force microscopy. Science 1995, 267, 68-71.
    • (1995) Science , vol.267 , pp. 68-71
    • Giessibl, F.J.1
  • 17
    • 0141990921 scopus 로고    scopus 로고
    • Advances in atomic force microscopy
    • Giessibl, F. J. Advances in atomic force microscopy. Rev. Mod. Phys. 2003, 75, 949-983.
    • (2003) Rev. Mod. Phys , vol.75 , pp. 949-983
    • Giessibl, F.J.1
  • 20
    • 0026899890 scopus 로고
    • Force measurement with a piezoelectric cantilever in a scanning force microscope
    • Tansock, J.; Williams, C. Force measurement with a piezoelectric cantilever in a scanning force microscope. Ultramicroscopy 1992, 42-44, 1464-1469.
    • (1992) Ultramicroscopy , vol.42-44 , pp. 1464-1469
    • Tansock, J.1    Williams, C.2
  • 21
    • 0033153911 scopus 로고    scopus 로고
    • Force-distance curves by atomic force microscopy
    • Cappella, B.; Dietler, G. Force-distance curves by atomic force microscopy. Surf. Sci. Rep. 1999, 34, 1-104.
    • (1999) Surf. Sci. Rep , vol.34 , pp. 1-104
    • Cappella, B.1    Dietler, G.2
  • 22
    • 0029292717 scopus 로고
    • Nanotribology: Friction, wear and lubrication at the atomic scale
    • Bhushan, B. Israelachvili, J. N.; Landman, U. Nanotribology: friction, wear and lubrication at the atomic scale. Nature 1995, 374, 607-616.
    • (1995) Nature , vol.374 , pp. 607-616
    • Bhushan, B.1    Israelachvili, J.N.2    Landman, U.3
  • 23
    • 0030234766 scopus 로고    scopus 로고
    • Determination of the spring constants of probes for force microscopy/spectroscopy
    • Gibson, C. T. Watson, G. S.; Myhra, S. Determination of the spring constants of probes for force microscopy/spectroscopy. Nanotechnology 1996, 7, 259-262.
    • (1996) Nanotechnology , vol.7 , pp. 259-262
    • Gibson, C.T.1    Watson, G.S.2    Myhra, S.3
  • 24
    • 0031390745 scopus 로고    scopus 로고
    • Scanning force microscopy- calibrative procedures for "best practice
    • Gibson, C. T. Watson, G. S.; Myhra, S. Scanning force microscopy- calibrative procedures for "best practice. Scanning 2006, 19, 564-581.
    • (2006) Scanning , vol.19 , pp. 564-581
    • Gibson, C.T.1    Watson, G.S.2    Myhra, S.3
  • 25
    • 0034530126 scopus 로고    scopus 로고
    • Single molecule force spectroscopy in biology using the atomic force microscope
    • Zlatanova, J. Lindsay, S. M.; Leuba, S. H. Single molecule force spectroscopy in biology using the atomic force microscope. Prog. Biophys. Mol. Biol.2000, 74, 37-61.
    • (2000) Prog. Biophys. Mol. Biol , vol.74 , pp. 37-61
    • Zlatanova, J.1    Lindsay, S.M.2    Leuba, S.H.3
  • 26
    • 0020804837 scopus 로고
    • On two methods of calculation of the force of sticking of an elastic sphere to a rigid plane
    • Muller, V. Derjaguin, B.; Toporov, Y. P. On two methods of calculation of the force of sticking of an elastic sphere to a rigid plane. Colloids Surf.1983, 7, 251-259.
    • (1983) Colloids Surf , vol.7 , pp. 251-259
    • Muller, V.1    Derjaguin, B.2    Toporov, Y.P.3
  • 29
    • 27744587245 scopus 로고    scopus 로고
    • Force measurements with the atomic force microscope: Technique, interpretation and applications
    • Butt, H. Cappella, B.; Kappl, M. Force measurements with the atomic force microscope: Technique, interpretation and applications. Surf. Sci. Rep. 2005, 59, 1-152.
    • (2005) Surf. Sci. Rep , vol.59 , pp. 1-152
    • Butt, H.1    Cappella, B.2    Kappl, M.3
  • 30
    • 0031106327 scopus 로고    scopus 로고
    • Measuring the elastic properties of biological samples with the AFM
    • Radmacher, M. Measuring the elastic properties of biological samples with the AFM. IEEE Eng. Med. Biol. Mag.1997, 16, 47-57.
    • (1997) IEEE Eng. Med. Biol. Mag , vol.16 , pp. 47-57
    • Radmacher, M.1
  • 31
    • 0027540056 scopus 로고
    • A nondestructive method for determining the spring constant of cantilevers for scanning force microscopy
    • Cleveland, J. P. Manne, S. Bocek, D.; Hansma, P. K. A nondestructive method for determining the spring constant of cantilevers for scanning force microscopy. Rev. Sci. Instrum. 1993, 64, 403.
    • (1993) Rev. Sci. Instrum , vol.64 , pp. 403
    • Cleveland, J.P.1    Manne, S.2    Bocek, D.3    Hansma, P.K.4
  • 32
    • 36449007442 scopus 로고
    • Calibration of atomic-force microscope tips
    • Hutter, J. L.; Bechhoefer, J. Calibration of atomic-force microscope tips. Rev. Sci. Instrum. 1993, 64, 1868.
    • (1993) Rev. Sci. Instrum , vol.64 , pp. 1868
    • Hutter, J.L.1    Bechhoefer, J.2
  • 34
    • 0001155528 scopus 로고    scopus 로고
    • Calibration of rectangular atomic force microscope cantilevers
    • Sader, J. E. Chon, J. W. M.; Mulvaney, P. Calibration of rectangular atomic force microscope cantilevers. Rev. Sci. Instrum. 1999, 70, 3967.
    • (1999) Rev. Sci. Instrum , vol.70 , pp. 3967
    • Sader, J.E.1    Chon, J.W.M.2    Mulvaney, P.3
  • 35
    • 78751563522 scopus 로고    scopus 로고
    • Force calibration in lateral force microscopy: A review of the experimental methods
    • Munz, M. Force calibration in lateral force microscopy: a review of the experimental methods. J. Phys. D. Appl. Phys.2010, 43, 063001.
    • (2010) J. Phys. D. Appl. Phys , vol.43 , pp. 063001
    • Munz, M.1
  • 36
    • 84861420982 scopus 로고    scopus 로고
    • Cantilever Spring-Constant Calibration in Atomic Force Microscopy
    • Cumpson, P. Clifford, C.; Portoles, J. Cantilever Spring-Constant Calibration in Atomic Force Microscopy. Probe Methods 8 2008.
    • (2008) Probe Methods , pp. 8
    • Cumpson, P.1    Clifford, C.2    Portoles, J.3
  • 37
    • 84862554916 scopus 로고    scopus 로고
    • T Functionalization of Probe Tips and Supports For Single-molecule Recognition Force Microscopy
    • Ebner, A. Wildling, L. Zhu, R. Rankl, C.; T Functionalization of probe tips and supports for single-molecule recognition force microscopy. STM and AFM Studies 2008.
    • (2008) STM and AFM Studies
    • Ebner, A.1    Wildling, L.2    Zhu, R.3    Rankl, C.4
  • 38
    • 65249131066 scopus 로고    scopus 로고
    • Simple, clickable protocol for atomic force microscopy tip modification and its application for trace ricin detection by recognition imaging
    • Chen, G. Ning, X. Park, B. Boons, G.J., Xu, B. Simple, clickable protocol for atomic force microscopy tip modification and its application for trace ricin detection by recognition imaging. Langmuir 2009, 25, 2860-2864.
    • (2009) Langmuir , vol.25 , pp. 2860-2864
    • Chen, G.1    Ning, X.2    Park, B.3    Boons, G.J.4    Xu, B.5
  • 40
    • 34447632456 scopus 로고    scopus 로고
    • Comparison of different aminofunctionalization strategies for attachment of single antibodies to AFM cantilevers
    • Ebner, A. Hinterdorfer, P.; Gruber, H. Comparison of different aminofunctionalization strategies for attachment of single antibodies to AFM cantilevers. Ultramicroscopy 2007, 107, 922-927.
    • (2007) Ultramicroscopy , vol.107 , pp. 922-927
    • Ebner, A.1    Hinterdorfer, P.2    Gruber, H.3
  • 41
    • 41049093662 scopus 로고    scopus 로고
    • Chemical modifications of AFM tips for the study of molecular recognition events
    • Barattin, R.; Voyer, N. Chemical modifications of AFM tips for the study of molecular recognition events. Chem. Commun.2008.
    • (2008) Chem. Commun
    • Barattin, R.1    Voyer, N.2
  • 43
    • 0342350248 scopus 로고    scopus 로고
    • Dynamic force spectroscopy of molecular adhesion bonds
    • Heymann, B.; Grubmüller, H. Dynamic force spectroscopy of molecular adhesion bonds. Phys. Rev. Lett.2000, 84, 6126-6129.
    • (2000) Phys. Rev. Lett , vol.84 , pp. 6126-6129
    • Heymann, B.1    Grubmüller, H.2
  • 44
    • 33947207859 scopus 로고    scopus 로고
    • Atomic force microscopy: Determination of unbinding force, off rate and energy barrier for protein-ligand interaction
    • Lee, C. K. Wang, Y. M. Huang, L. S., Lin, S. Atomic force microscopy: determination of unbinding force, off rate and energy barrier for protein-ligand interaction. Micron 2007, 38, 446-461.
    • (2007) Micron , vol.38 , pp. 446-461
    • Lee, C.K.1    Wang, Y.M.2    Huang, L.S.3    Lin, S.4
  • 45
    • 0031001349 scopus 로고    scopus 로고
    • Dynamic strength of molecular adhesion bonds
    • Evans, E.; Ritchie, K. Dynamic strength of molecular adhesion bonds. Biophys. J.1997, 72, 1541-1555.
    • (1997) Biophys. J , vol.72 , pp. 1541-1555
    • Evans, E.1    Ritchie, K.2
  • 47
    • 0035206306 scopus 로고    scopus 로고
    • Intermolecular forces in biology
    • Leckband, D., Israelachvili, J. Intermolecular forces in biology. Q. Rev. Biophys. 2001; Vol. 34, pp. 105-267.
    • (2001) Q. Rev. Biophys , vol.34 , pp. 105-267
    • Leckband, D.1    Israelachvili, J.2
  • 48
    • 33344476773 scopus 로고    scopus 로고
    • Molecular recognition imaging and force spectroscopy of single biomolecules
    • Kienberger, F, Ebner, A, Gruber, H. J.; Hinterdorfer, P. Molecular recognition imaging and force spectroscopy of single biomolecules. Acc. Chem. Res. 2006, 39, 29-36.
    • (2006) Acc. Chem. Res , vol.39 , pp. 29-36
    • Kienberger, F.1    Ebner, A.2    Gruber, H.J.3    Hinterdorfer, P.4
  • 49
    • 33646021951 scopus 로고    scopus 로고
    • Detection and localization of single molecular recognition events using atomic force microscopy
    • Hinterdorfer, P., Dufrêne, Y. F. Detection and localization of single molecular recognition events using atomic force microscopy. Nat. Methods 2006, 3, 347-355.
    • (2006) Nat. Methods , vol.3 , pp. 347-355
    • Hinterdorfer, P.1    Dufrêne, Y.F.2
  • 51
    • 0031019894 scopus 로고    scopus 로고
    • Atomic force microscope imaging contrast based on molecular recognition
    • Ludwig, M., Dettmann, W., Gaub, H. Atomic force microscope imaging contrast based on molecular recognition. Biophys. J.1997, 72, 445-448.
    • (1997) Biophys. J , vol.72 , pp. 445-448
    • Ludwig, M.1    Dettmann, W.2    Gaub, H.3
  • 52
    • 0028853559 scopus 로고
    • The relationship between ligand-binding thermodynamics and protein-ligand interaction forces measured by atomic force microscopy
    • Chilkoti, A., Boland, T, Ratner, B. D., Stayton, P. S. The relationship between ligand-binding thermodynamics and protein-ligand interaction forces measured by atomic force microscopy. Biophys. J.1995, 69, 2125-2130.
    • (1995) Biophys. J , vol.69 , pp. 2125-2130
    • Chilkoti, A.1    Boland, T.2    Ratner, B.D.3    Stayton, P.S.4
  • 53
    • 0037180006 scopus 로고    scopus 로고
    • Temperature Dependence of the Biotin-Avidin Bond-Rupture Force Studied by Atomic Force Microscopy
    • Lo, Y.-shiu; Simons, J.; Beebe, T. P. Temperature Dependence of the Biotin-Avidin Bond-Rupture Force Studied by Atomic Force Microscopy. J. Phys. Chem. B 2002, 9847-9852.
    • (2002) J. Phys. Chem. B , pp. 9847-9852
    • Lo, Y.-S.1    Simons, J.2    Beebe, T.P.3
  • 54
    • 0034043222 scopus 로고    scopus 로고
    • Cross-linking of cell surface receptors enhances cooperativity of molecular adhesion
    • Chen, A; Moy, V. T. Cross-linking of cell surface receptors enhances cooperativity of molecular adhesion. Biophys. J.2000, 78, 2814-2820.
    • (2000) Biophys. J , vol.78 , pp. 2814-2820
    • Chen, A.1    Moy, V.T.2
  • 55
    • 0033621525 scopus 로고    scopus 로고
    • Direct force measurements of the streptavidin-biotin interaction
    • Wong, J, Chilkoti, A; Moy, V. T. Direct force measurements of the streptavidin-biotin interaction. Biomol. Eng.1999, 16, 45-55.
    • (1999) Biomol. Eng , vol.16 , pp. 45-55
    • Wong, J.1    Chilkoti, A.2    Moy, V.T.3
  • 57
    • 29844448752 scopus 로고    scopus 로고
    • The AFM measured force required to rupture the dithiolate linkage of thioctic acid to gold is less than the rupture force of a simple goldalkyl thiolate bond
    • Langry, K. C. Ratto, T. V. Rudd, R. E.; McElfresh, M. W. The AFM measured force required to rupture the dithiolate linkage of thioctic acid to gold is less than the rupture force of a simple goldalkyl thiolate bond. Langmuir 2005, 21, 12064-12067.
    • (2005) Langmuir , vol.21 , pp. 12064-12067
    • Langry, K.C.1    Ratto, T.V.2    Rudd, R.E.3    McElfresh, M.W.4
  • 59
    • 33847764116 scopus 로고    scopus 로고
    • Molecular recognition forces between immunoglobulin G and a surface protein adhesin on living Staphylococcus aureus
    • Touhami, A. Jericho, M. H.; Beveridge, T. J. Molecular recognition forces between immunoglobulin G and a surface protein adhesin on living Staphylococcus aureus. Langmuir 2007, 23, 2755-2760.
    • (2007) Langmuir , vol.23 , pp. 2755-2760
    • Touhami, A.1    Jericho, M.H.2    Beveridge, T.J.3
  • 60
    • 0037420277 scopus 로고    scopus 로고
    • Simple test system for single molecule recognition force microscopy
    • Riener, C. Simple test system for single molecule recognition force microscopy. Anal. Chim. Acta. 2003, 479, 59-75.
    • (2003) Anal. Chim. Acta , vol.479 , pp. 59-75
    • Riener, C.1
  • 68
    • 28844471878 scopus 로고    scopus 로고
    • Single molecule adhesion measurements reveal two homophilic neural cell adhesion molecule bonds with mechanically distinct properties
    • Wieland, J., Gewirth, A., Leckband, D. E. Single molecule adhesion measurements reveal two homophilic neural cell adhesion molecule bonds with mechanically distinct properties. J. Biol. Chem.2005, 280, 41037-41046.
    • (2005) J. Biol. Chem , vol.280 , pp. 41037-41046
    • Wieland, J.1    Gewirth, A.2    Leckband, D.E.3
  • 69
    • 0037408412 scopus 로고    scopus 로고
    • Analytical investigation of the chemical reactivity and stability of aminopropyl-grafted silica in aqueous medium
    • Etienne, M.; Walcarius, A. Analytical investigation of the chemical reactivity and stability of aminopropyl-grafted silica in aqueous medium. Talanta 2003, 59, 1173-1188.
    • (2003) Talanta , vol.59 , pp. 1173-1188
    • Etienne, M.1    Walcarius, A.2
  • 70
    • 0001381024 scopus 로고    scopus 로고
    • Formation of Uniform Aminosilane Thin Layers: An Imine Formation To Measure Relative Surface Density of the Amine Group
    • Moon, J. H. Shin, J. W. Kim, S. Y.; Park, J. W. Formation of Uniform Aminosilane Thin Layers: An Imine Formation To Measure Relative Surface Density of the Amine Group. Langmuir 1996, 7463, 4621-4624.
    • (1996) Langmuir , vol.7463 , pp. 4621-4624
    • Moon, J.H.1    Shin, J.W.2    Kim, S.Y.3    Park, J.W.4
  • 71
    • 0035397452 scopus 로고    scopus 로고
    • Functionalization of self-assembled monolayers on glass and oxidized silicon wafers by surface reactions
    • Flink, S, van Veggel, F. C. J. M.; Reinhoudt, D. N. Functionalization of self-assembled monolayers on glass and oxidized silicon wafers by surface reactions. J. Phys. Org. Chem. 2001, 14, 407-415.
    • (2001) J. Phys. Org. Chem , vol.14 , pp. 407-415
    • Flink, S.1    van Veggel, F.C.J.M.2    Reinhoudt, D.N.3
  • 73
    • 0032532286 scopus 로고    scopus 로고
    • TM-AFM Threshold Analysis of Macromolecular Orientation: A Study of the Orientation of IgG and IgE on Mica Surfaces
    • Bergkvist, M. Carlsson, J. Karlsson, T.; Oscarsson, S. TM-AFM Threshold Analysis of Macromolecular Orientation: A Study of the Orientation of IgG and IgE on Mica Surfaces. J. Colloid Interface Sci.1998, 206, 475-481.
    • (1998) J. Colloid Interface Sci , vol.206 , pp. 475-481
    • Bergkvist, M.1    Carlsson, J.2    Karlsson, T.3    Oscarsson, S.4
  • 75
    • 77956590971 scopus 로고    scopus 로고
    • Detecting protein aggregates on untreated human tissue samples by atomic force microscopy recognition imaging
    • Creasey, R. Sharma, S. Craig, J. E. Gibson, C. T. Ebner, A. Hinterdorfer, P.; Voelcker, N. H. Detecting protein aggregates on untreated human tissue samples by atomic force microscopy recognition imaging. Biophys. J.2010, 99, 1660-1667.
    • (2010) Biophys. J , vol.99 , pp. 1660-1667
    • Creasey, R.1    Sharma, S.2    Craig, J.E.3    Gibson, C.T.4    Ebner, A.5    Hinterdorfer, P.6    Voelcker, N.H.7
  • 77
    • 80053310708 scopus 로고    scopus 로고
    • Chemical functionalization and bioconjugation strategies for atomic force microscope cantilevers
    • (Clifton, N.J.); Mark, S. S., Ed. Humana Press: Totowa, NJ
    • Bergkvist, M.; Cady, N. C. Chemical functionalization and bioconjugation strategies for atomic force microscope cantilevers. In Methods in Mol Biol (Clifton, N.J.); Mark, S. S., Ed. Humana Press: Totowa, NJ, 2011; Vol. 751, 381-400.
    • (2011) Methods In Mol Biol , vol.751 , pp. 381-400
    • Bergkvist, M.1    Cady, N.C.2
  • 78
    • 36449000136 scopus 로고
    • Tip artifacts of microfabricated force sensors for atomic force microscopy
    • Grutter, P. Zimmermann-Edling, W.; Brodbeck, D. Tip artifacts of microfabricated force sensors for atomic force microscopy. Appl Phys Lett. 1992, 60, 2741.
    • (1992) Appl Phys Lett , vol.60 , pp. 2741
    • Grutter, P.1    Zimmermann-Edling, W.2    Brodbeck, D.3
  • 81
    • 33846381911 scopus 로고    scopus 로고
    • MAC mode atomic force microscopy studies of living samples, ranging from cells to fresh tissue
    • Ge, G. Han, D. Lin, D. Chu, W. Sun, Y. Jiang, L. Ma, W.; Wang, C. MAC mode atomic force microscopy studies of living samples, ranging from cells to fresh tissue. Ultramicroscopy 2007, 107, 299-307.
    • (2007) Ultramicroscopy , vol.107 , pp. 299-307
    • Ge, G.1    Han, D.2    Lin, D.3    Chu, W.4    Sun, Y.5    Jiang, L.6    Ma, W.7    Wang, C.8
  • 82
    • 74249086852 scopus 로고    scopus 로고
    • Biomolecules under mechanical force
    • Kumar, S.; Li, M. S. Biomolecules under mechanical force. Phys. Rep.2010, 486, 1-74.
    • (2010) Phys. Rep , vol.486 , pp. 1-74
    • Kumar, S.1    Li, M.S.2
  • 83
    • 80051704115 scopus 로고    scopus 로고
    • Direct measurement and control of peak tapping forces in atomic force microscopy for improved height measurements
    • Sikora, A.; Bednarz, L. Direct measurement and control of peak tapping forces in atomic force microscopy for improved height measurements. Meas. Sci. Technol.2011, 22, 094005.
    • (2011) Meas. Sci. Technol , vol.22 , pp. 094005
    • Sikora, A.1    Bednarz, L.2
  • 84
    • 34247223253 scopus 로고    scopus 로고
    • An atomic force microscope for the study of the effects of tip-sample interactions on dimensional metrology
    • Yacoot, A. Koenders, L.; Wolff, H. An atomic force microscope for the study of the effects of tip-sample interactions on dimensional metrology. Meas. Sci. Technol.2007, 18, 350-359.
    • (2007) Meas. Sci. Technol , vol.18 , pp. 350-359
    • Yacoot, A.1    Koenders, L.2    Wolff, H.3
  • 85
    • 0026206391 scopus 로고
    • Reconstruction of STM and AFM images distorted by finite-size tips
    • Keller, D. Reconstruction of STM and AFM images distorted by finite-size tips. Surf. Sci.1991, 253, 353-364.
    • (1991) Surf. Sci , vol.253 , pp. 353-364
    • Keller, D.1
  • 86
    • 4344678675 scopus 로고    scopus 로고
    • Ultrastructural organization of ex vivo amyloid fibrils formed by the apolipoprotein A-I Leu174Ser variant: An atomic force microscopy study
    • Relini, A. Rolandi, R. Bolognesi, M. Aboudan, M. Merlini, G. Bellotti, V.; Gliozzi, A. Ultrastructural organization of ex vivo amyloid fibrils formed by the apolipoprotein A-I Leu174Ser variant: an atomic force microscopy study. Biochim. Biophys. Acta 2004, 1690, 33-41.
    • (2004) Biochim. Biophys. Acta , vol.1690 , pp. 33-41
    • Relini, A.1    Rolandi, R.2    Bolognesi, M.3    Aboudan, M.4    Merlini, G.5    Bellotti, V.6    Gliozzi, A.7
  • 90
    • 77949622855 scopus 로고    scopus 로고
    • Phase imaging atomic force microscopy in the characterization of biomaterials
    • Ye, Z.; Zhao, X. Phase imaging atomic force microscopy in the characterization of biomaterials. J Microsc. 2010, 238, 27-35.
    • (2010) J Microsc , vol.238 , pp. 27-35
    • Ye, Z.1    Zhao, X.2
  • 91
  • 92
    • 32144433377 scopus 로고    scopus 로고
    • Simultaneous Topography and RECognition Mapping with PicoTRECTM: A powerful new technology that can be used to map nanometer-scale molecular binding sites on a variety of surfaces
    • Johnson, W. Kada, G. Stroh, C. Gruber, H. Wang, H. Kienberger, F. Ebner, A. Lindsay, S.; Hinterdorfer, P. Simultaneous Topography and RECognition Mapping with PicoTRECTM: A powerful new technology that can be used to map nanometer-scale molecular binding sites on a variety of surfaces. NSTI-Nanotech 2005, 2, 679-682.
    • (2005) NSTI-Nanotech , vol.2 , pp. 679-682
    • Johnson, W.K.1    Stroh, G.2    Gruber, C.3    Wang, H.4    Kienberger, H.5    Ebner, F.6    Lindsay, A.S.7    Hinterdorfer, P.8
  • 93
    • 82655177891 scopus 로고    scopus 로고
    • Nanomechanical properties of α-synuclein amyloid fibrils: A comparative study by nanoindentation, harmonic force microscopy, and Peakforce QNM
    • Sweers, K. van der Werf, K. Bennink, M.; Subramaniam, V. Nanomechanical properties of α-synuclein amyloid fibrils: a comparative study by nanoindentation, harmonic force microscopy, and Peakforce QNM. Nanoscale Res. Lett. 2011, 6, 270.
    • (2011) Nanoscale Res. Lett , vol.6 , pp. 270
    • Sweers, K.1    van der Werf, K.2    Bennink, M.3    Subramaniam, V.4
  • 94
    • 79959631028 scopus 로고    scopus 로고
    • Single-step direct measurement of amyloid fibrils stiffness by peak force quantitative nanomechanical atomic force microscopy
    • Adamcik, J. Berquand, A.; Mezzenga, R. Single-step direct measurement of amyloid fibrils stiffness by peak force quantitative nanomechanical atomic force microscopy. Appl. Phys. Lett. 2011, 98, 193701.
    • (2011) Appl. Phys. Lett , vol.98 , pp. 193701
    • Adamcik, J.1    Berquand, A.2    Mezzenga, R.3
  • 96
    • 84862576339 scopus 로고    scopus 로고
    • Nanoprobing of α-synuclein Misfolding and Aggregation With Atomic Force Microscopy
    • Yu, J, Warnke, J.; Lyubchenko, Y. L. Nanoprobing of α-synuclein misfolding and aggregation with atomic force microscopy. Nanomedicine 2010.
    • (2010) Nanomedicine
    • Yu, J.1    Warnke, J.2    Lyubchenko, Y.L.3
  • 97
    • 60549100886 scopus 로고    scopus 로고
    • Early stages for Parkinson's development: Alpha-synuclein misfolding and aggregation
    • Yu, J.; Lyubchenko, Y. L. Early stages for Parkinson's development: alpha-synuclein misfolding and aggregation. J Neuroimmune Pharmacol. 2009, 4, 10-16.
    • (2009) J Neuroimmune Pharmacol , vol.4 , pp. 10-16
    • Yu, J.1    Lyubchenko, Y.L.2
  • 99
    • 0033973107 scopus 로고    scopus 로고
    • Data analysis of interaction forces measured with the atomic force microscope
    • Baumgartner, W. Hinterdorfer, P.; Schindler, H. Data analysis of interaction forces measured with the atomic force microscope. Ultramicroscopy 2000, 82, 85-95.
    • (2000) Ultramicroscopy , vol.82 , pp. 85-95
    • Baumgartner, W.1    Hinterdorfer, P.2    Schindler, H.3
  • 103
    • 77955667712 scopus 로고    scopus 로고
    • Material Properties of Lipid Microdomains: Force-Volume Imaging Study of the Effect of Cholesterol on Lipid Microdomain Rigidity
    • An, H. Nussio, M. R. Huson, M. G. Voelcker, N. H.; Shapter, J. G. Material Properties of Lipid Microdomains: Force-Volume Imaging Study of the Effect of Cholesterol on Lipid Microdomain Rigidity. Biophys. J.2010, 99, 834-844.
    • (2010) Biophys. J , vol.99 , pp. 834-844
    • An, H.1    Nussio, M.R.2    Huson, M.G.3    Voelcker, N.H.4    Shapter, J.G.5
  • 104
    • 77951572333 scopus 로고    scopus 로고
    • Detecting cell-adhesive sites in extracellular matrix using force spectroscopy mapping
    • Chirasatitsin, S.; Engler, A. J. Detecting cell-adhesive sites in extracellular matrix using force spectroscopy mapping. J. Phys. Condens. Matter 2010, 22, 194102.
    • (2010) J. Phys. Condens. Matter , vol.22 , pp. 194102
    • Chirasatitsin, S.1    Engler, A.J.2
  • 106
    • 33645663597 scopus 로고    scopus 로고
    • Investigation of angiotensin II type 1 receptor by atomic force microscopy with functionalized tip
    • Li, G. Xi, N.; Wang, D. H. Investigation of angiotensin II type 1 receptor by atomic force microscopy with functionalized tip. Nanomedicine 2005, 1, 306-312.
    • (2005) Nanomedicine , vol.1 , pp. 306-312
    • Li, G.1    Xi, N.2    Wang, D.H.3
  • 107
    • 33645669939 scopus 로고    scopus 로고
    • Probing membrane proteins using atomic force microscopy
    • Li, G. Xi, N.; Wang, D. H. Probing membrane proteins using atomic force microscopy. J. Cell. Biochem. 2006, 97, 1191-1197.
    • (2006) J. Cell. Biochem , vol.97 , pp. 1191-1197
    • Li, G.1    Xi, N.2    Wang, D.H.3
  • 108
    • 67649194544 scopus 로고    scopus 로고
    • Simultaneous topography and recognition imaging: Physical aspects and optimal imaging conditions
    • Preiner, J. Ebner, A. Chtcheglova, L. Zhu, R.; Hinterdorfer, P. Simultaneous topography and recognition imaging: physical aspects and optimal imaging conditions. Nanotechnology 2009, 20, 215103.
    • (2009) Nanotechnology , vol.20 , pp. 215103
    • Preiner, J.1    Ebner, A.2    Chtcheglova, L.3    Zhu, R.4    Hinterdorfer, P.5
  • 110
    • 43149089348 scopus 로고    scopus 로고
    • Localization of the ergtoxin-1 receptors on the voltage sensing domain of hERG K+ channel by AFM recognition imaging
    • Chtcheglova, L. A. Atalar, F. Ozbek, U. Wildling, L. Ebner, A.; Hinterdorfer, P. Localization of the ergtoxin-1 receptors on the voltage sensing domain of hERG K+ channel by AFM recognition imaging. Pflugers Arch. 2008, 456, 247-254.
    • (2008) Pflugers Arch , vol.456 , pp. 247-254
    • Chtcheglova, L.A.1    Atalar, F.2    Ozbek, U.3    Wildling, L.4    Ebner, A.5    Hinterdorfer, P.6
  • 113
    • 80052804535 scopus 로고    scopus 로고
    • Mechanical mapping of single membrane proteins at submolecular resolution
    • Rico, F, Su, C.; Scheuring, S. Mechanical mapping of single membrane proteins at submolecular resolution. Nano lett. 2011, 11, 3983-3986.
    • (2011) Nano Lett , vol.11 , pp. 3983-3986
    • Rico, F.1    Su, C.2    Scheuring, S.3
  • 114
    • 0033605231 scopus 로고    scopus 로고
    • The structure of bacteriorhodopsin at 3.0 Å resolution based on electron crystallography: Implication of the charge distribution
    • Mitsuoka, K. Hirai, T. Murata, K. Miyazawa, A. Kidera, A. Kimura, Y.; Fujiyoshi, Y. The structure of bacteriorhodopsin at 3.0 Å resolution based on electron crystallography: implication of the charge distribution. J. Mol. Biol.1999, 286, 861-882.
    • (1999) J. Mol. Biol , vol.286 , pp. 861-882
    • Mitsuoka, K.1    Hirai, T.2    Murata, K.3    Miyazawa, A.4    Kidera, A.5    Kimura, Y.6    Fujiyoshi, Y.7
  • 115
    • 72949119728 scopus 로고    scopus 로고
    • DNA nanomechanics allows direct digital detection of complementary DNA and microRNA targets
    • Husale, S. Persson, H. H. J.; Sahin, O. DNA nanomechanics allows direct digital detection of complementary DNA and microRNA targets. Nature 2009, 462, 1075-1078.
    • (2009) Nature , vol.462 , pp. 1075-1078
    • Husale, S.1    Persson, H.H.J.2    Sahin, O.3
  • 116
    • 77955230701 scopus 로고    scopus 로고
    • Understanding amyloid aggregation by statistical analysis of atomic force microscopy images. Nat
    • Adamcik, J. Jung, J.-M. Flakowski, J. De Los Rios, P. Dietler, G.; Mezzenga, R. Understanding amyloid aggregation by statistical analysis of atomic force microscopy images. Nat. Nanotechnol. 2010, 5, 423-428.
    • (2010) Nanotechnol , vol.5 , pp. 423-428
    • Adamcik, J.1    Jung, J.-M.2    Flakowski, J.3    de Los, R.P.4    Dietler, G.5    Mezzenga, R.6
  • 117
    • 84862532667 scopus 로고    scopus 로고
    • The Combined Application of AFM and LSCMα: Changing the Way We Look At Innate Immunity
    • Adams, E. L.; Czymmek, K. J. The combined application of AFM and LSCMα: Changing the way we look at innate immunity. Imaging 2007, 68-76.
    • (2007) Imaging , pp. 68-76
    • Adams, E.L.1    Czymmek, K.J.2
  • 118
    • 38349101591 scopus 로고    scopus 로고
    • Novel combination of atomic force microscopy and epifluorescence microscopy for visualization of leaching bacteria on pyrite
    • Mangold, S, Harneit, K, Rohwerder, T, Claus, G.; Sand, W. Novel combination of atomic force microscopy and epifluorescence microscopy for visualization of leaching bacteria on pyrite. Appl. Microbiol. 2008, 74, 410-415.
    • (2008) Appl. Microbiol , vol.74 , pp. 410-415
    • Mangold, S.1    Harneit, K.2    Rohwerder, T.3    Claus, G.4    Sand, W.5
  • 121
    • 28844441969 scopus 로고    scopus 로고
    • Secondary structure of alpha-synuclein oligomers: Characterization by raman and atomic force microscopy
    • Apetri, M. M. Maiti, N. C. Zagorski, M. G. Carey, P. R.; Anderson, V. E. Secondary structure of alpha-synuclein oligomers: characterization by raman and atomic force microscopy. J. Mol. Biol. 2006, 355, 63-71.
    • (2006) J. Mol. Biol , vol.355 , pp. 63-71
    • Apetri, M.M.1    Maiti, N.C.2    Zagorski, M.G.3    Carey, P.R.4    Anderson, V.E.5
  • 122
    • 84906093734 scopus 로고    scopus 로고
    • Combined AFM / Raman Microspectroscopy For Characterization of Living Cells In Near Physiological Conditions
    • Zhou, A. H. McEwen, G. D.; Wu, Y. Z. Combined AFM / Raman microspectroscopy for characterization of living cells in near physiological conditions. Exposure 2010, 515-522.
    • (2010) Exposure , pp. 515-522
    • Zhou, A.H.1    McEwen, G.D.2    Wu, Y.Z.3
  • 124
    • 0033200063 scopus 로고    scopus 로고
    • Protein misfolding, evolution and disease
    • Dobson, C. M. Protein misfolding, evolution and disease. Trends Biochem. Sci. 1999, 24, 329-332.
    • (1999) Trends Biochem. Sci , vol.24 , pp. 329-332
    • Dobson, C.M.1
  • 125
    • 78650081316 scopus 로고    scopus 로고
    • Protein aggregation from inclusion bodies to amyloid and biomaterials
    • Mitraki, A. Protein aggregation from inclusion bodies to amyloid and biomaterials. Adv Protein Chem Struct Biol 2010, 79, 89-125.
    • (2010) Adv Protein Chem Struct Biol , vol.79 , pp. 89-125
    • Mitraki, A.1
  • 126
    • 59649108278 scopus 로고    scopus 로고
    • Unraveling the mysteries of protein folding and misfolding
    • Ecroyd, H.; Carver, J. A. Unraveling the mysteries of protein folding and misfolding. IUBMB life 2008, 60, 769-774.
    • (2008) IUBMB Life , vol.60 , pp. 769-774
    • Ecroyd, H.1    Carver, J.A.2
  • 127
    • 33746377894 scopus 로고    scopus 로고
    • Protein Misfolding, Functional Amyloid, and Human Disease
    • Chiti, F.; Dobson, C. M. Protein Misfolding, Functional Amyloid, and Human Disease. Annu. Rev. Biochem. 2006, 75, 333-366.
    • (2006) Annu. Rev. Biochem , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 128
    • 59349083966 scopus 로고    scopus 로고
    • Protein aggregation kinetics, mechanism, and curve-fitting: A review of the literature
    • Morris, A. M. Watzky, M.; Finke, R. G. Protein aggregation kinetics, mechanism, and curve-fitting: a review of the literature. Biochim. Biophys. Acta 2009, 1794, 375-597.
    • (2009) Biochim. Biophys. Acta , vol.1794 , pp. 375-597
    • Morris, A.M.1    Watzky, M.2    Finke, R.G.3
  • 129
    • 77951498805 scopus 로고    scopus 로고
    • Protein aggregation-pathways and influencing factors
    • Wang, W, Nema, S.; Teagarden, D. Protein aggregation-pathways and influencing factors. Int. J. Pharm.2010, 390, 89-99.
    • (2010) Int. J. Pharm , vol.390 , pp. 89-99
    • Wang, W.1    Nema, S.2    Teagarden, D.3
  • 130
  • 131
    • 70449702059 scopus 로고    scopus 로고
    • Mechanism of amyloidogenesis: Nucleation-dependent fibrillation versus double-concerted fibrillation
    • Bhak, G. Choe, Y.-J.; Paik, S. R. Mechanism of amyloidogenesis: nucleation-dependent fibrillation versus double-concerted fibrillation. BMB reports 2009, 42, 541-551.
    • (2009) BMB Reports , vol.42 , pp. 541-551
    • Bhak, G.1    Choe, Y.-J.2    Paik, S.R.3
  • 132
    • 84862530274 scopus 로고    scopus 로고
    • Merriam-Webster.com, accessed Oct 7, 2011
    • Merriam-Webster.com "Fiber" http://www.merriamwebster.com/dictionary/fiber?show=0&t=1317942787 (accessed Oct 7, 2011).
    • Fiber
  • 133
    • 28244484729 scopus 로고    scopus 로고
    • Structures for amyloid fibrils
    • Makin, O. S.; Serpell, L. C. Structures for amyloid fibrils. FEBS J 2005, 272, 5950-5961.
    • (2005) FEBS J , vol.272 , pp. 5950-5961
    • Makin, O.S.1    Serpell, L.C.2
  • 134
    • 35148865232 scopus 로고    scopus 로고
    • On the structural definition of amyloid fibrils and other polypeptide aggregates
    • Fändrich, M. On the structural definition of amyloid fibrils and other polypeptide aggregates. Cell. Mol. Life Sci. 2007, 64, 2066-2078.
    • (2007) Cell. Mol. Life Sci , vol.64 , pp. 2066-2078
    • Fändrich, M.1
  • 135
    • 0842307665 scopus 로고    scopus 로고
    • Amyloidosis of Alzheimer's Abeta peptides: Solid-state nuclear magnetic resonance, electron paramagnetic resonance, transmission electron microscopy, scanning transmission electron microscopy and atomic force microscopy studies
    • Antzutkin, O. N. Amyloidosis of Alzheimer's Abeta peptides: solid-state nuclear magnetic resonance, electron paramagnetic resonance, transmission electron microscopy, scanning transmission electron microscopy and atomic force microscopy studies. Magn. Reson. Chem. 2004, 42, 231-246.
    • (2004) Magn. Reson. Chem , vol.42 , pp. 231-246
    • Antzutkin, O.N.1
  • 137
    • 0038386274 scopus 로고    scopus 로고
    • Zeroing in on the pathogenic form of alpha-synuclein and its mechanism of neurotoxicity in Parkinson's disease
    • Volles, M. J.; Lansbury, P. T. Zeroing in on the pathogenic form of alpha-synuclein and its mechanism of neurotoxicity in Parkinson's disease. Biochemistry 2003, 42, 7871-7878.
    • (2003) Biochemistry , vol.42 , pp. 7871-7878
    • Volles, M.J.1    Lansbury, P.T.2
  • 138
    • 0031444010 scopus 로고    scopus 로고
    • Atomic force microscopic imaging of seeded fibril formation and fibril branching by the Alzheimer's disease amyloid-α protein
    • Harper, J. D, Lieber, C. M.; Lansbury Jr, P. T. Atomic force microscopic imaging of seeded fibril formation and fibril branching by the Alzheimer's disease amyloid-α protein. Chem. Biol. 1997, 4, 951-959.
    • (1997) Chem. Biol , vol.4 , pp. 951-959
    • Harper, J.D.1    Lieber, C.M.2    Lansbury, P.T.3
  • 140
    • 0034681163 scopus 로고    scopus 로고
    • Acceleration of oligomerization, not fibrillization, is a shared property of both a-synuclein mutations linked to early-onset Parkinson's disease: Implications for pathogenesis and therapy
    • Conway, K, Lee, S.-Jae; Rochet, J.-Christophe; Ding, T.; Williamson, R. Acceleration of oligomerization, not fibrillization, is a shared property of both a-synuclein mutations linked to early-onset Parkinson's disease: Implications for pathogenesis and therapy. Proc. Natl Acad. Sci. USA 2000, 99, 571-576.
    • (2000) Proc. Natl Acad. Sci. USA , vol.99 , pp. 571-576
    • Conway, K.1    Lee, S.-J.2    Rochet, J.-C.3    Ding, T.4    Williamson, R.5
  • 141
    • 2942592408 scopus 로고    scopus 로고
    • Rapid selfassembly of alpha-synuclein observed by in situ atomic force microscopy
    • Hoyer, W. Cherny, D. Subramaniam, V.; Jovin, T. M. Rapid selfassembly of alpha-synuclein observed by in situ atomic force microscopy. J. Mol. Biol.2004, 340, 127-139.
    • (2004) J. Mol. Biol , vol.340 , pp. 127-139
    • Hoyer, W.1    Cherny, D.2    Subramaniam, V.3    Jovin, T.M.4
  • 143
    • 79959886270 scopus 로고    scopus 로고
    • Amyloid precursor protein processing and Alzheimer's disease
    • O'Brien, R. J.; Wong, P. C. Amyloid precursor protein processing and Alzheimer's disease. Annu. Rev. Neurosci. 2011, 34, 185-204.
    • (2011) Annu. Rev. Neurosci , vol.34 , pp. 185-204
    • O'Brien, R.J.1    Wong, P.C.2
  • 144
    • 79958058969 scopus 로고    scopus 로고
    • Recent progress in understanding Alzheimer's α-amyloid structures
    • Fändrich, M. Schmidt, M.; Grigorieff, N. Recent progress in understanding Alzheimer's α-amyloid structures. Trends Biochem. Sci. 2011, 36, 338-345.
    • (2011) Trends Biochem. Sci , vol.36 , pp. 338-345
    • Fändrich, M.1    Schmidt, M.2    Grigorieff, N.3
  • 145
    • 0033855775 scopus 로고    scopus 로고
    • Review: Model peptides and the physicochemical approach to beta-amyloids
    • Lynn, D. G.; Meredith, S. C. Review: Model peptides and the physicochemical approach to beta-amyloids. J. Struct. Biol. 2000, 130, 153-173.
    • (2000) J. Struct. Biol , vol.130 , pp. 153-173
    • Lynn, D.G.1    Meredith, S.C.2
  • 146
    • 0025910229 scopus 로고
    • Molecular biology of prion diseases
    • Prusiner, S. B. Molecular biology of prion diseases. Science 1991, 252, 1515-1522.
    • (1991) Science , vol.252 , pp. 1515-1522
    • Prusiner, S.B.1
  • 147
    • 42049122359 scopus 로고    scopus 로고
    • Systematic review of therapeutic interventions in human prion disease
    • Stewart, L. Rydzewska, L. H. M. Keogh, G. F.; Knight, R. S. G. Systematic review of therapeutic interventions in human prion disease. Neurol. 2008, 70, 1272-1281.
    • (2008) Neurol , vol.70 , pp. 1272-1281
    • Stewart, L.1    Rydzewska, L.H.M.2    Keogh, G.F.3    Knight, R.S.G.4
  • 148
    • 0035066332 scopus 로고    scopus 로고
    • Alzheimer's disease: Genes, proteins, and therapy
    • Selkoe, D. Alzheimer's disease: Genes, proteins, and therapy. Physiol. Rev.2001, 741-766.
    • (2001) Physiol. Rev , pp. 741-766
    • Selkoe, D.1
  • 149
    • 67650325176 scopus 로고    scopus 로고
    • The interplay of catalysis and toxicity by amyloid intermediates on lipid bilayers: Insights from type II diabetes
    • Hebda, J.; Miranker, A. D. The interplay of catalysis and toxicity by amyloid intermediates on lipid bilayers: insights from type II diabetes. Annu. Rev. Biophys. 2009, 38, 125-152.
    • (2009) Annu. Rev. Biophys , vol.38 , pp. 125-152
    • Hebda, J.1    Miranker, A.D.2
  • 152
    • 79953245314 scopus 로고    scopus 로고
    • Amyloid structure: Conformational diversity and consequences
    • Toyama, B. H.; Weissman, J. S. Amyloid structure: conformational diversity and consequences. Annu. Rev. Biochem. 2011, 80, 557-585.
    • (2011) Annu. Rev. Biochem , vol.80 , pp. 557-585
    • Toyama, B.H.1    Weissman, J.S.2
  • 154
    • 12544257523 scopus 로고    scopus 로고
    • In vitro conversion of full-length mammalian prion protein produces amyloid form with physical properties of PrP(Sc)
    • Bocharova, O. V. Breydo, L. Parfenov, A. S. Salnikov, V. V.; Baskakov, I. V. In vitro conversion of full-length mammalian prion protein produces amyloid form with physical properties of PrP(Sc). J. Mol. Biol. 2005, 346, 645-659.
    • (2005) J. Mol. Biol , vol.346 , pp. 645-659
    • Bocharova, O.V.1    Breydo, L.2    Parfenov, A.S.3    Salnikov, V.V.4    Baskakov, I.V.5
  • 155
    • 33646093028 scopus 로고    scopus 로고
    • Polymorphism and ultrastructural organization of prion protein amyloid fibrils: An insight from high resolution atomic force microscopy
    • Anderson, M, Bocharova, O. V, Makarava, N, Breydo, L, Salnikov, V. V.; Baskakov, I. V. Polymorphism and ultrastructural organization of prion protein amyloid fibrils: An insight from high resolution atomic force microscopy. J. Mol. Biol. 2006, 358, 580-596.
    • (2006) J. Mol. Biol , vol.358 , pp. 580-596
    • Anderson, M.1    Bocharova, O.V.2    Makarava, N.3    Breydo, L.4    Salnikov, V.V.5    Baskakov, I.V.6
  • 156
    • 15444367176 scopus 로고    scopus 로고
    • Correlations among morphology, beta-sheet stability, and molecular structure in prion peptide aggregates
    • Petty, S. Adalsteinsson, T.; Decatur, S. M. Correlations among morphology, beta-sheet stability, and molecular structure in prion peptide aggregates. Biochemistry 2005, 44, 4720-4726.
    • (2005) Biochemistry , vol.44 , pp. 4720-4726
    • Petty, S.1    Adalsteinsson, T.2    Decatur, S.M.3
  • 157
    • 33646199155 scopus 로고    scopus 로고
    • Early events in insulin fibrillization studied by time-lapse atomic force microscopy
    • Podestà, A. Tiana, G. Milani, P.; Manno, M. Early events in insulin fibrillization studied by time-lapse atomic force microscopy. Biophys. J. 2006, 90, 589-597.
    • (2006) Biophys. J , vol.90 , pp. 589-597
    • Podestà, A.1    Tiana, G.2    Milani, P.3    Manno, M.4
  • 159
    • 0033534397 scopus 로고    scopus 로고
    • Watching amyloid fibrils grow by time-lapse atomic force microscopy
    • Goldsbury, C. Kistler, J. Aebi, U. Arvinte, T.; Cooper, G. J. Watching amyloid fibrils grow by time-lapse atomic force microscopy. J. Mol. Biol.1999, 285, 33-39.
    • (1999) J. Mol. Biol , vol.285 , pp. 33-39
    • Goldsbury, C.1    Kistler, J.2    Aebi, U.3    Arvinte, T.4    Cooper, G.J.5
  • 160
    • 24044507958 scopus 로고    scopus 로고
    • A Multiple assembly pathways underlie amyloid-beta fibril polymorphisms
    • Goldsbury, C. Frey, P. Olivieri, V. Aebi, U.; Müller, S. A Multiple assembly pathways underlie amyloid-beta fibril polymorphisms. J. Mol. Biol. 2005, 352, 282-298.
    • (2005) J. Mol. Biol , vol.352 , pp. 282-298
    • Goldsbury, C.1    Frey, P.2    Olivieri, V.3    Aebi, U.4    Müller, S.5
  • 161
    • 0030614627 scopus 로고    scopus 로고
    • Observation of metastable beta amyloid protofibrils by atomic force microscopy
    • Harper, J. D. Wong, S. S. Lieber, C. M.; Lansbury, P. T. Observation of metastable beta amyloid protofibrils by atomic force microscopy. Chem. Biol. 1997, 4, 119-125.
    • (1997) Chem. Biol , vol.4 , pp. 119-125
    • Harper, J.D.1    Wong, S.S.2    Lieber, C.M.3    Lansbury, P.T.4
  • 162
    • 70350133393 scopus 로고    scopus 로고
    • Structural insights into alternate aggregated prion protein forms
    • Polano, M. Bek, A. Benetti, F. Lazzarino, M.; Legname, G. Structural insights into alternate aggregated prion protein forms. J. Mol. Biol. 2009, 393, 1033-1042.
    • (2009) J. Mol. Biol , vol.393 , pp. 1033-1042
    • Polano, M.1    Bek, A.2    Benetti, F.3    Lazzarino, M.4    Legname, G.5
  • 163
    • 39049119728 scopus 로고    scopus 로고
    • Conformational stability of PrP amyloid fibrils controls their smallest possible fragment size
    • Sun, Y. Makarava, N. Lee, C.-I. Laksanalamai, P. Robb, F. T.; Baskakov, I. V. Conformational stability of PrP amyloid fibrils controls their smallest possible fragment size. J. Mol. Biol. 2008, 376, 1155-1167.
    • (2008) J. Mol. Biol , vol.376 , pp. 1155-1167
    • Sun, Y.1    Makarava, N.2    Lee, C.-I.3    Laksanalamai, P.4    Robb, F.T.5    Baskakov, I.V.6
  • 164
  • 166
    • 61849170573 scopus 로고    scopus 로고
    • Highly accelerated self-assembly and fibrillation of prion peptides on solid surfaces
    • Ku, S. H.; Park, C. B. Highly accelerated self-assembly and fibrillation of prion peptides on solid surfaces. Langmuir 2008, 24, 13822-13827.
    • (2008) Langmuir , vol.24 , pp. 13822-13827
    • Ku, S.H.1    Park, C.B.2
  • 167
    • 33747182874 scopus 로고    scopus 로고
    • Ex situ atomic force microscopy analysis of beta-amyloid self-assembly and deposition on a synthetic template
    • Ha, C.; Park, C. B. Ex situ atomic force microscopy analysis of beta-amyloid self-assembly and deposition on a synthetic template. Langmuir 2006, 22, 6977-6985.
    • (2006) Langmuir , vol.22 , pp. 6977-6985
    • Ha, C.1    Park, C.B.2
  • 168
    • 0345688752 scopus 로고    scopus 로고
    • Influence of hydrophobic Teflon particles on the structure of amyloid beta-peptide
    • Giacomelli, C. E.; Norde, W. Influence of hydrophobic Teflon particles on the structure of amyloid beta-peptide. Biomacromolecules 4, 1719-1726.
    • Biomacromolecules , vol.4 , pp. 1719-1726
    • Giacomelli, C.E.1    Norde, W.2
  • 170
    • 0033616587 scopus 로고    scopus 로고
    • In situ atomic force microscopy study of Alzheimer's α-amyloid peptide on different substrates: New insights into mechanism of α-sheet formation
    • Kowalewski, T.; Holtzman, D. M. In situ atomic force microscopy study of Alzheimer's α-amyloid peptide on different substrates: New insights into mechanism of α-sheet formation. Proc. Natl. Acad. Sci. U.S.A. 1999, 96, 3688.
    • (1999) Proc. Natl. Acad. Sci. U.S.A , vol.96 , pp. 3688
    • Kowalewski, T.1    Holtzman, D.M.2
  • 171
    • 0038204160 scopus 로고    scopus 로고
    • AFM and STM study of beta-amyloid aggregation on graphite
    • Wang, Z. Zhou, C. Wang, C. Wan, L. Fang, X.; Bai, C. AFM and STM study of beta-amyloid aggregation on graphite. Ultramicroscopy 2003, 97, 73-79.
    • (2003) Ultramicroscopy , vol.97 , pp. 73-79
    • Wang, Z.1    Zhou, C.2    Wang, C.3    Wan, L.4    Fang, X.5    Bai, C.6
  • 172
    • 67349128044 scopus 로고    scopus 로고
    • Amyloid beta (1-42) folding multiplicity and singlemolecule binding behavior studied with STM
    • Ma, X, Liu, L, Mao, X., Niu, L., Deng, K., Wu, W., Li, Y., Yang, Y.; Wang, C. Amyloid beta (1-42) folding multiplicity and singlemolecule binding behavior studied with STM. J. Mol. Biol. 2009, 388, 894-901.
    • (2009) J. Mol. Biol , vol.388 , pp. 894-901
    • Ma, X.1    Liu, L.2    Mao, X.3    Niu, L.4    Deng, K.5    Wu, W.6    Li, Y.7    Yang, Y.8    Wang, C.9
  • 173
    • 0037462946 scopus 로고    scopus 로고
    • Alternate aggregation pathways of the Alzheimer beta-amyloid peptide: Abeta association kinetics at endosomal pH
    • Gorman, P. M. Yip, C. M. Fraser, P. E.; Chakrabartty, A. Alternate aggregation pathways of the Alzheimer beta-amyloid peptide: Abeta association kinetics at endosomal pH. J. Mol. Biol. 2003, 325, 743-757.
    • (2003) J. Mol. Biol , vol.325 , pp. 743-757
    • Gorman, P.M.1    Yip, C.M.2    Fraser, P.E.3    Chakrabartty, A.4
  • 174
    • 4444292588 scopus 로고    scopus 로고
    • Atomic force microscopy reveals defects within mica supported lipid bilayers induced by the amyloidogenic human amylin peptide
    • Green, J. D. Kreplak, L. Goldsbury, C. Li Blatter, X. Stolz, M. Cooper, G. S. Seelig, A; Kistler, J.; Aebi, U. Atomic force microscopy reveals defects within mica supported lipid bilayers induced by the amyloidogenic human amylin peptide. J. Mol. Biol. 2004, 342, 877-887.
    • (2004) J. Mol. Biol , vol.342 , pp. 877-887
    • Green, J.D.1    Kreplak, L.2    Goldsbury, C.3    Li-Blatter, X.4    Stolz, M.5    Cooper, G.S.6    Seelig, A.7    Kistler, J.8    Aebi, U.9
  • 175
    • 33845932931 scopus 로고    scopus 로고
    • Structural properties of prion protein protofibrils and fibrils: An experimental assessment of atomic models
    • DeMarco, M. L. Silveira, J. Caughey, B.; Daggett, V. Structural properties of prion protein protofibrils and fibrils: an experimental assessment of atomic models. Biochemistry 2006, 45, 15573-15582.
    • (2006) Biochemistry , vol.45 , pp. 15573-15582
    • Demarco, M.L.1    Silveira, J.2    Caughey, B.3    Daggett, V.4
  • 177
    • 0037200117 scopus 로고    scopus 로고
    • Oligomeric and fibrillar species of amyloid-beta peptides differentially affect neuronal viability
    • Dahlgren, K. N., Manelli, A. M., Stine, W. B., Baker, L. K., Krafft, G.; LaDu, M. J. Oligomeric and fibrillar species of amyloid-beta peptides differentially affect neuronal viability. J. Biol. Chem.2002, 277, 32046-32053.
    • (2002) J. Biol. Chem , vol.277 , pp. 32046-32053
    • Dahlgren, K.N.1    Manelli, A.M.2    Stine, W.B.3    Baker, L.K.4    Krafft, G.5    Ladu, M.J.6
  • 179
    • 8744220663 scopus 로고    scopus 로고
    • Permeabilization of lipid bilayers is a common conformation-dependent activity of soluble amyloid oligomers in protein misfolding diseases
    • Kayed, R. Sokolov, Y. Edmonds, B. McIntire, T. M. Milton, S. C. Hall, J. E.; Glabe, C. G. Permeabilization of lipid bilayers is a common conformation-dependent activity of soluble amyloid oligomers in protein misfolding diseases. J. Biol. Chem.2004, 279, 46363-46366.
    • (2004) J. Biol. Chem , vol.279 , pp. 46363-46366
    • Kayed, R.1    Sokolov, Y.2    Edmonds, B.3    McIntire, T.M.4    Milton, S.C.5    Hall, J.E.6    Glabe, C.G.7
  • 180
    • 15844403848 scopus 로고    scopus 로고
    • Annular alphasynuclein oligomers are potentially toxic agents in alphasynucleinopathy
    • Pountney, D. L. Voelcker, N. H.; Gai, W. P. Annular alphasynuclein oligomers are potentially toxic agents in alphasynucleinopathy. Hypothesis. Neurotox. Res.2005, 7, 59-67.
    • (2005) Hypothesis. Neurotox. Res , vol.7 , pp. 59-67
    • Pountney, D.L.1    Voelcker, N.H.2    Gai, W.P.3
  • 181
    • 77955312210 scopus 로고    scopus 로고
    • Amyloidogenic protein-membrane interactions: Mechanistic insight from model systems
    • Butterfield, S. M.; Lashuel, H. Amyloidogenic protein-membrane interactions: mechanistic insight from model systems. Angew. Chem. Int. Ed. Engl. 2010, 49, 5628-5654.
    • (2010) Angew. Chem. Int. Ed. Engl , vol.49 , pp. 5628-5654
    • Butterfield, S.M.1    Lashuel, H.2
  • 182
    • 9344233839 scopus 로고    scopus 로고
    • Calcium (II) selectively induces alpha-synuclein annular oligomers via interaction with the C-terminal domain
    • Lowe, R. Pountney, D. L. Jensen, P. H. Gai, W. P.; Voelcker, N. H. Calcium (II) selectively induces alpha-synuclein annular oligomers via interaction with the C-terminal domain. Protein Sci. 2004, 13, 3245-3252.
    • (2004) Protein Sci , vol.13 , pp. 3245-3252
    • Lowe, R.1    Pountney, D.L.2    Jensen, P.H.3    Gai, W.P.4    Voelcker, N.H.5
  • 184
    • 77956072590 scopus 로고    scopus 로고
    • Metalloproteomics and metal toxicology of α-synuclein
    • Santner, A.; Uversky, V. N. Metalloproteomics and metal toxicology of α-synuclein. Metallomics 2010, 2, 378-392.
    • (2010) Metallomics , vol.2 , pp. 378-392
    • Santner, A.1    Uversky, V.N.2
  • 185
    • 3142664614 scopus 로고    scopus 로고
    • Annular alpha-synuclein species from purified multiple system atrophy inclusions
    • Pountney, D. L. Lowe, R. Quilty, M. Vickers, J. C. Voelcker, N. H.; Gai, W. P. Annular alpha-synuclein species from purified multiple system atrophy inclusions. J. Neurochem. 2004, 90, 502-512.
    • (2004) J. Neurochem , vol.90 , pp. 502-512
    • Pountney, D.L.1    Lowe, R.2    Quilty, M.3    Vickers, J.C.4    Voelcker, N.H.5    Gai, W.P.6
  • 186
    • 77949359499 scopus 로고    scopus 로고
    • Ribosylation rapidly induces alpha-synuclein to form highly cytotoxic molten globules of advanced glycation end products
    • Chen, L. Wei, Y. Wang, X.; He, R. Ribosylation rapidly induces alpha-synuclein to form highly cytotoxic molten globules of advanced glycation end products. PloS One 2010, 5, e9052.
    • (2010) PloS One , vol.5
    • Chen, L.1    Wei, Y.2    Wang, X.3    He, R.4
  • 187
    • 22544478124 scopus 로고    scopus 로고
    • Inhibition of alpha-synuclein fibrillization by dopamine analogs via reaction with the amino groups of alpha-synuclein. Implication for dopaminergic neurodegeneration
    • Li, H.-T., Lin, D.-H., Luo, X.-Y., Zhang, F., Ji, L.-N., Du, H.-N., Song, G.-Q., Hu, J., Zhou, J.-W.; Hu, H.-Y. Inhibition of alpha-synuclein fibrillization by dopamine analogs via reaction with the amino groups of alpha-synuclein. Implication for dopaminergic neurodegeneration. FEBS J 2005, 272, 3661-3672.
    • (2005) FEBS J , vol.272 , pp. 3661-3672
    • Li, H.-T.1    Lin, D.-H.2    Luo, X.-Y.3    Zhang, F.4    Ji, L.-N.5    Du, H.-N.6    Song, G.-Q.7    Hu, J.8    Zhou, J.-W.9    Hu, H.-Y.10
  • 188
    • 58149199681 scopus 로고    scopus 로고
    • Smoking and Parkinson's disease: Does nicotine affect alpha-synuclein fibrillation?
    • Hong, D.-P. Fink, A. L.; Uversky, V. N. Smoking and Parkinson's disease: does nicotine affect alpha-synuclein fibrillation? Biochim. Biophys. Acta 2009, 1794, 282-290.
    • (2009) Biochim. Biophys. Acta , vol.1794 , pp. 282-290
    • Hong, D.-P.1    Fink, A.L.2    Uversky, V.N.3
  • 191
    • 33646126278 scopus 로고    scopus 로고
    • New insights into prion structure and toxicity
    • Harris, D.; True, H. L. New insights into prion structure and toxicity. Neuron 2006, 50, 353-357.
    • (2006) Neuron , vol.50 , pp. 353-357
    • Harris, D.1    True, H.L.2
  • 192
    • 77954358960 scopus 로고    scopus 로고
    • Mysterious oligomerization of the amyloidogenic proteins
    • Uversky, V. N. Mysterious oligomerization of the amyloidogenic proteins. FEBS J 2010, 277, 2940-2953.
    • (2010) FEBS J , vol.277 , pp. 2940-2953
    • Uversky, V.N.1
  • 193
    • 77950941375 scopus 로고    scopus 로고
    • Amyloid-beta fibrillogenesis: Structural insight and therapeutic intervention
    • Dasilva, K.; Shaw, J. E.; McLaurin, J. Amyloid-beta fibrillogenesis: structural insight and therapeutic intervention. Exp. Neurol. 2010, 223, 311-321.
    • (2010) Exp. Neurol , vol.223 , pp. 311-321
    • Dasilva, K.1    Shaw, J.E.2    McLaurin, J.3
  • 194
    • 33750365052 scopus 로고    scopus 로고
    • Are amyloid diseases caused by protein aggregates that mimic bacterial pore-forming toxins?
    • Lashuel, H.; Lansbury, P. T. Are amyloid diseases caused by protein aggregates that mimic bacterial pore-forming toxins? Q. Rev. Biophys. 2006, 39, 167-201.
    • (2006) Q. Rev. Biophys , vol.39 , pp. 167-201
    • Lashuel, H.1    Lansbury, P.T.2
  • 195
    • 0037046163 scopus 로고    scopus 로고
    • Vesicle Permeabilization by Protofibrillar α-Synuclein Is Sensitive to Parkinson's Disease-Linked Mutations and Occurs by a Pore-like Mechanism
    • Volles, M. J.; Lansbury, P. T. Vesicle Permeabilization by Protofibrillar α-Synuclein Is Sensitive to Parkinson's Disease-Linked Mutations and Occurs by a Pore-like Mechanism. Biochemistry 2002, 41, 4595-4602.
    • (2002) Biochemistry , vol.41 , pp. 4595-4602
    • Volles, M.J.1    Lansbury, P.T.2
  • 196
    • 33747881813 scopus 로고    scopus 로고
    • Mechanical characterization of nanofibers - A review
    • Tan, E.; Lim, C. Mechanical characterization of nanofibers - A review. Compos Sci Technol 2006, 66, 1102-1111.
    • (2006) Compos Sci Technol , vol.66 , pp. 1102-1111
    • Tan, E.1    Lim, C.2
  • 197
    • 78651262764 scopus 로고    scopus 로고
    • Structural and mechanical properties of TTR105-115 amyloid fibrils from compression experiments
    • Meersman, F., Cabrera, R. Q., McMillan, P. F.; Dmitriev, V. Structural and mechanical properties of TTR105-115 amyloid fibrils from compression experiments. Biophys. J. 2011, 100, 193-197.
    • (2011) Biophys. J , vol.100 , pp. 193-197
    • Meersman, F.1    Cabrera, R.Q.2    McMillan, P.F.3    Dmitriev, V.4
  • 199
    • 79960006769 scopus 로고    scopus 로고
    • Atomic force microscopybased antibody recognition imaging of proteins in the pathological deposits in Pseudoexfoliation Syndrome
    • Creasey, R. Sharma, S. Gibson, C. T. Craig, J. E. Ebner, A. Becker, T. Hinterdorfer, P.; Voelcker, N. H. Atomic force microscopybased antibody recognition imaging of proteins in the pathological deposits in Pseudoexfoliation Syndrome. Ultramicroscopy 2011, 111, 1055-1061.
    • (2011) Ultramicroscopy , vol.111 , pp. 1055-1061
    • Creasey, R.1    Sharma, S.2    Gibson, C.T.3    Craig, J.E.4    Ebner, A.5    Becker, T.6    Hinterdorfer, P.7    Voelcker, N.H.8
  • 201
    • 36349020908 scopus 로고    scopus 로고
    • Cataract and glaucoma surgery in pseudoexfoliation syndrome: A review
    • Drolsum, L. Ringvold, A.; Nicolaissen, B. Cataract and glaucoma surgery in pseudoexfoliation syndrome: a review. Acta Ophthalmol Scand 2007, 85, 810-821.
    • (2007) Acta Ophthalmol Scand , vol.85 , pp. 810-821
    • Drolsum, L.1    Ringvold, A.2    Nicolaissen, B.3
  • 202
    • 56249106138 scopus 로고
    • Pseudoexfoliation of the lens capsule: Relation to true exfoliation of the lens capsule as reported in the literature, and role in the production of glaucoma capsulocuticulare
    • Dvorak-Theobald, G. Pseudoexfoliation of the lens capsule: relation to true exfoliation of the lens capsule as reported in the literature, and role in the production of glaucoma capsulocuticulare. Trans Am Ophthalmol Soc 1953, 51, 385-407.
    • (1953) Trans Am Ophthalmol Soc , vol.51 , pp. 385-407
    • Dvorak-Theobald, G.1
  • 203
    • 0141765883 scopus 로고    scopus 로고
    • Fabrication of novel biomaterials through molecular selfassembly
    • Zhang, S. Fabrication of novel biomaterials through molecular selfassembly. Nat. Biotechnol. 2003, 21, 1171-1178.
    • (2003) Nat. Biotechnol , vol.21 , pp. 1171-1178
    • Zhang, S.1
  • 204
    • 77954946648 scopus 로고    scopus 로고
    • Designer self-assembling peptide nanofiber biological materials
    • Hauser, C. E.; Zhang, S. Designer self-assembling peptide nanofiber biological materials. Chem. Soc. Rev.2010, 2780-2790.
    • (2010) Chem. Soc. Rev , pp. 2780-2790
    • Hauser, C.E.1    Zhang, S.2
  • 205
    • 78651357235 scopus 로고    scopus 로고
    • Cellulose nanowhiskers: Promising materials for advanced applications
    • Eichhorn, S. J. Cellulose nanowhiskers: promising materials for advanced applications. Soft Matter 2011, 7, 303.
    • (2011) Soft Matter , vol.7 , pp. 303
    • Eichhorn, S.J.1
  • 206
    • 84860315046 scopus 로고    scopus 로고
    • Nanomaterials: Amyloids reflect their brighter side
    • Mankar, S. Anoop.; Sen, S.; Maji, S. K. Nanomaterials: amyloids reflect their brighter side. Nano Reviews 2011, 2, 1-12.
    • (2011) Nano Reviews , vol.2 , pp. 1-12
    • Mankar, S.A.1    Sen, S.2    Maji, S.K.3
  • 207
    • 77950342360 scopus 로고    scopus 로고
    • Self-assembly of peptide amphiphiles: From molecules to nanostructures to biomaterials
    • Cui, H. Webber, M. J.; Stupp, S. I. Self-assembly of peptide amphiphiles: from molecules to nanostructures to biomaterials. Biopolymers 2010, 94, 1-18.
    • (2010) Biopolymers , vol.94 , pp. 1-18
    • Cui, H.1    Webber, M.J.2    Stupp, S.I.3
  • 208
    • 60649106342 scopus 로고    scopus 로고
    • Peptide-directed self-assembly of hydrogels
    • Kopecek, J.; Yang, J. Peptide-directed self-assembly of hydrogels. Acta Biomater 2009, 5, 805-816.
    • (2009) Acta Biomater , vol.5 , pp. 805-816
    • Kopecek, J.1    Yang, J.2
  • 210
    • 0034571041 scopus 로고    scopus 로고
    • Self-assembly of a beta-sheet protein governed by relief of electrostatic repulsion relative to van der Waals attraction
    • Caplan, M. R. Moore, P. N. Zhang, S. Kamm, R. D.; Lauffenburger, D. Self-assembly of a beta-sheet protein governed by relief of electrostatic repulsion relative to van der Waals attraction, Biomacromolecules 2000, 1, 627-631.
    • (2000) Biomacromolecules , vol.1 , pp. 627-631
    • Caplan, M.R.1    Moore, P.N.2    Zhang, S.3    Kamm, R.D.4    Lauffenburger, D.5
  • 211
    • 0000590549 scopus 로고    scopus 로고
    • Left-Handed Helical Ribbon Intermediates in the Self-Assembly of a α-Sheet Peptide
    • Marini, D. M. Hwang, W. Lauffenburger, D. A. Zhang, S.; Kamm, R. D. Left-Handed Helical Ribbon Intermediates in the Self-Assembly of a α-Sheet Peptide. Nano Lett. 2002, 2, 295-299.
    • (2002) Nano Lett , vol.2 , pp. 295-299
    • Marini, D.M.1    Hwang, W.2    Lauffenburger, D.A.3    Zhang, S.4    Kamm, R.D.5
  • 212
    • 77952374620 scopus 로고    scopus 로고
    • Structures of selfassembled amphiphilic peptide-heterodimers: Effects of concentration, pH, temperature and ionic strength
    • Luo, Z. Åkerman, B. Zhang, S.; Nordén, B. Structures of selfassembled amphiphilic peptide-heterodimers: effects of concentration, pH, temperature and ionic strength. Soft Matter 2010, 6, 2260.
    • (2010) Soft Matter , vol.6 , pp. 2260
    • Luo, Z.1    Åkerman, B.2    Zhang, S.3    Nordén, B.4
  • 214
    • 20844451602 scopus 로고    scopus 로고
    • Dynamic reassembly of peptide RADA16 nanofiber scaffold
    • Yokoi, H. Kinoshita, T.; Zhang, S. Dynamic reassembly of peptide RADA16 nanofiber scaffold. Proc. Natl. Acad. Sci. U.S.A 2005, 102, 8414-8419.
    • (2005) Proc. Natl. Acad. Sci. U.S.A , vol.102 , pp. 8414-8419
    • Yokoi, H.1    Kinoshita, T.2    Zhang, S.3
  • 215
    • 54049097997 scopus 로고    scopus 로고
    • Self-organization of a chiral D-EAK16 designer peptide into a 3D nanofiber scaffold
    • Luo, Z, Zhao, X.; Zhang, S. Self-organization of a chiral D-EAK16 designer peptide into a 3D nanofiber scaffold. Macromol. Biosci. 2008, 8, 785-791.
    • (2008) Macromol. Biosci , vol.8 , pp. 785-791
    • Luo, Z.1    Zhao, X.2    Zhang, S.3
  • 216
    • 68949107702 scopus 로고    scopus 로고
    • Experimental study on self-assembly of KLD-12 peptide hydrogel and 3-D culture of MSC encapsulated within hydrogel in vitro
    • Sun, J.; Zheng, Q. Experimental study on self-assembly of KLD-12 peptide hydrogel and 3-D culture of MSC encapsulated within hydrogel in vitro. J Huazhong Univ Sci Technolog Med Sci. 2009, 29, 512-816.
    • (2009) J Huazhong Univ Sci Technolog Med Sci , vol.29 , pp. 512-816
    • Sun, J.1    Zheng, Q.2
  • 218
    • 78650319534 scopus 로고    scopus 로고
    • Investigation of Self-assembly Structure and Properties of a Novel Designed Lego-type Peptide with Double Amphiphilic Surfaces
    • Wang, L.; Zhao, X.-J. Investigation of Self-assembly Structure and Properties of a Novel Designed Lego-type Peptide with Double Amphiphilic Surfaces. Bull. Kor. Chem. Soc. 2010, 31, 3740-3744.
    • (2010) Bull. Kor. Chem. Soc , vol.31 , pp. 3740-3744
    • Wang, L.1    Zhao, X.-J.2
  • 222
    • 38049143848 scopus 로고    scopus 로고
    • Dendritic macromers for hydrogel formation: Tailored materials for ophthalmic, orthopedic, and biotech applications
    • Grinstaff, M. Dendritic macromers for hydrogel formation: Tailored materials for ophthalmic, orthopedic, and biotech applications. J Polym Sci A Polym Chem 2008, 46, 383-400.
    • (2008) J Polym Sci a Polym Chem , vol.46 , pp. 383-400
    • Grinstaff, M.1
  • 226
    • 33750528504 scopus 로고    scopus 로고
    • Dendritic Gels-Many Arms Make Light Work
    • Smith, D. K. Dendritic Gels-Many Arms Make Light Work. Adv. Mater. 2006, 18, 2773-2778.
    • (2006) Adv. Mater , vol.18 , pp. 2773-2778
    • Smith, D.K.1
  • 229
    • 0027703505 scopus 로고
    • Self-assembling Organic Nanotubes Based On a Cyclic Peptide Architecture
    • Ghadiri, M. Granja, J. Milligan, R.; McRee, D. Self-assembling organic nanotubes based on a cyclic peptide architecture. Nature 1993.
    • (1993) Nature
    • Ghadiri, M.1    Granja, J.2    Milligan, R.3    McRee, D.4
  • 230
    • 77951613692 scopus 로고    scopus 로고
    • Towards functional bionanomaterials based on self-assembling cyclic peptide nanotubes
    • Brea, R. J. Reiriz, C.; Granja, J. R. Towards functional bionanomaterials based on self-assembling cyclic peptide nanotubes. Chem. Soc. Rev.2010, 39, 1448-1456.
    • (2010) Chem. Soc. Rev , vol.39 , pp. 1448-1456
    • Brea, R.J.1    Reiriz, C.2    Granja, J.R.3


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