메뉴 건너뛰기




Volumn 88, Issue 6, 2005, Pages 4223-4231

Topography and mechanical properties of single molecules of type I collagen using atomic force microscopy

Author keywords

[No Author keywords available]

Indexed keywords

COLLAGEN TYPE 1;

EID: 22244448651     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.104.055228     Document Type: Article
Times cited : (168)

References (37)
  • 1
    • 0027136085 scopus 로고
    • Subfibrillar structure of type I collagen observed by atomic force microscopy
    • Baselt, D., J. Revel, and J. Baldeschwieler. 1993. Subfibrillar structure of type I collagen observed by atomic force microscopy. Biophys. J. 65: 2644-2655.
    • (1993) Biophys. J. , vol.65 , pp. 2644-2655
    • Baselt, D.1    Revel, J.2    Baldeschwieler, J.3
  • 2
    • 0030947539 scopus 로고    scopus 로고
    • Effects of ionic strength and cation valence on the elastic response of single DNA molecules
    • Baumann, C. G., S. B. Smith, C. Bustamante, and V. A. Bloomfield. 1997. Effects of ionic strength and cation valence on the elastic response of single DNA molecules. Proc. Natl. Acad. Sci. USA. 94:6185-6197.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 6185-6197
    • Baumann, C.G.1    Smith, S.B.2    Bustamante, C.3    Bloomfield, V.A.4
  • 3
    • 0031657823 scopus 로고    scopus 로고
    • Supercoiled protein motifs: The collagen triple-helix and the alpha-helical coiled coil
    • Beck, K., and B. Brodsky. 1998. Supercoiled protein motifs: the collagen triple-helix and the alpha-helical coiled coil. J. Struct. Biol. 122:17-29.
    • (1998) J. Struct. Biol. , vol.122 , pp. 17-29
    • Beck, K.1    Brodsky, B.2
  • 4
    • 0029645406 scopus 로고
    • Hydration structure of a collagen peptide
    • Bella, J., B. Brodsky, and H. M. Berman. 1995. Hydration structure of a collagen peptide. Structure. 3:893-906.
    • (1995) Structure , vol.3 , pp. 893-906
    • Bella, J.1    Brodsky, B.2    Berman, H.M.3
  • 5
    • 0027996196 scopus 로고
    • Crystal-structure and molecular-structure of a collagen-like peptide at 1.9-Angstrom resolution
    • Bella, J., M. Eaton, B. Brodsky, and H. M. Berman. 1994. Crystal-structure and molecular-structure of a collagen-like peptide at 1.9-Angstrom resolution. Science. 266:75-81.
    • (1994) Science , vol.266 , pp. 75-81
    • Bella, J.1    Eaton, M.2    Brodsky, B.3    Berman, H.M.4
  • 7
    • 84957349865 scopus 로고
    • Atomic force microscope images collagen fibres
    • Chemoff, E. A. G., and D. A. Chemoff. 1992. Atomic force microscope images collagen fibres. J. Vac. Sci. Technol. A. 10:596-599.
    • (1992) J. Vac. Sci. Technol. A , vol.10 , pp. 596-599
    • Chemoff, E.A.G.1    Chemoff, D.A.2
  • 8
    • 0033813556 scopus 로고    scopus 로고
    • Assembly of type I collagen: Fusion of fibril subunits and the influence of fibril diameter on mechanical properties
    • Christiansen, D. L., E. K. Huang, and F. H. Silver. 2000. Assembly of type I collagen: fusion of fibril subunits and the influence of fibril diameter on mechanical properties. Matrix Biol. 19:409-420.
    • (2000) Matrix Biol. , vol.19 , pp. 409-420
    • Christiansen, D.L.1    Huang, E.K.2    Silver, F.H.3
  • 9
    • 0035889096 scopus 로고    scopus 로고
    • The desorption process of macromolecules adsorbed on interfaces: The force spectroscopy approach
    • Conti, M., Y. Bustanji, G. Falini, P. Ferruti, S. Stefoni, and B. Samori, 2001. The desorption process of macromolecules adsorbed on interfaces: the force spectroscopy approach. ChemPhysChem. 2:610-613.
    • (2001) ChemPhysChem , vol.2 , pp. 610-613
    • Conti, M.1    Bustanji, Y.2    Falini, G.3    Ferruti, P.4    Stefoni, S.5    Samori, B.6
  • 11
    • 2142758179 scopus 로고    scopus 로고
    • Force spectroscopy of collagen fibers to investigate their mechanical properties and structural organisation
    • Gutsmann, T., G. E. Fantner, J. H. Kindt, M. Venturoni, S. Danielsen, and P. K. Hansma. 2004. Force spectroscopy of collagen fibers to investigate their mechanical properties and structural organisation. Biophys. J. 86: 3186-3193.
    • (2004) Biophys. J. , vol.86 , pp. 3186-3193
    • Gutsmann, T.1    Fantner, G.E.2    Kindt, J.H.3    Venturoni, M.4    Danielsen, S.5    Hansma, P.K.6
  • 13
    • 0028999930 scopus 로고
    • Cryoatomic force microscopy: A new approach for biological imaging at high resolution
    • Han, W., J. Mou, J. Yang, and Z. Shao. 1995. Cryoatomic force microscopy: a new approach for biological imaging at high resolution. Biochemistry. 34:8215-8220.
    • (1995) Biochemistry , vol.34 , pp. 8215-8220
    • Han, W.1    Mou, J.2    Yang, J.3    Shao, Z.4
  • 14
    • 0002358902 scopus 로고
    • Potential applications of atomic force microscopy of DNA to the human genome project
    • Hansma, H. G., and P. K. Hansma. 1993. Potential applications of atomic force microscopy of DNA to the human genome project. Proc. SPIE Int. Opt. Eng. 1891:66-70.
    • (1993) Proc. SPIE Int. Opt. Eng. , vol.1891 , pp. 66-70
    • Hansma, H.G.1    Hansma, P.K.2
  • 16
    • 0000842390 scopus 로고
    • Calibration of atomic-force microscope tips
    • Hutter, J. L., and J. Bechhoefer. 1993. Calibration of atomic-force microscope tips. Rev. Sci. Instrum. 64:3342.
    • (1993) Rev. Sci. Instrum. , vol.64 , pp. 3342
    • Hutter, J.L.1    Bechhoefer, J.2
  • 17
    • 7444225745 scopus 로고    scopus 로고
    • Assembly of collagen into microribbons: Effects of pH and electrolytes
    • Jiang, F. Z., H. Horber, J. Howard, and D. J. Muller. 2004. Assembly of collagen into microribbons: effects of pH and electrolytes. J. Struct. Biol. 148:268-278.
    • (2004) J. Struct. Biol. , vol.148 , pp. 268-278
    • Jiang, F.Z.1    Horber, H.2    Howard, J.3    Muller, D.J.4
  • 19
    • 0037007051 scopus 로고    scopus 로고
    • Chair-boat transitions in single polysaccharide molecule observed with force-ramp AFM
    • Marszalek, P. E., H. Li, A. F. Oberhauser, and J. M. Fernandez. 2002. Chair-boat transitions in single polysaccharide molecule observed with force-ramp AFM. Proc. Natl. Acad. Sci. USA. 99:4278-4283.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 4278-4283
    • Marszalek, P.E.1    Li, H.2    Oberhauser, A.F.3    Fernandez, J.M.4
  • 20
    • 0031153358 scopus 로고    scopus 로고
    • Scanning force microscopy and geometric analysis of two-dimensional collagen network formation
    • Mertig, M., U. Thiele, J. Bradt, G. Leibiger, W. Pompe, and H. Wendrock. 1997. Scanning force microscopy and geometric analysis of two-dimensional collagen network formation. Surf. Interfac. Anal. 25: 514-521.
    • (1997) Surf. Interfac. Anal. , vol.25 , pp. 514-521
    • Mertig, M.1    Thiele, U.2    Bradt, J.3    Leibiger, G.4    Pompe, W.5    Wendrock, H.6
  • 22
  • 23
    • 0034651554 scopus 로고    scopus 로고
    • The in situ conformation and axial location of the intermolecular cross-linked non-helical telopeptides of type I collagen
    • Orgel, J. P., T. J. Wess, and A. Miller. 2000. The in situ conformation and axial location of the intermolecular cross-linked non-helical telopeptides of type I collagen. Struct. Fold. Des. 8:137-142.
    • (2000) Struct. Fold. Des. , vol.8 , pp. 137-142
    • Orgel, J.P.1    Wess, T.J.2    Miller, A.3
  • 24
    • 0035941338 scopus 로고    scopus 로고
    • Unhydroxylated triple-helical collagen 1 produced in transgenic plants provides new clues on the role of hydroxyproline in collagen folding and fibril formation
    • Perret, S., S. Merle, J. Nettleton, and J. Howard. 2001. Unhydroxylated triple-helical collagen 1 produced in transgenic plants provides new clues on the role of hydroxyproline in collagen folding and fibril formation. J. Biol. Chem. 276:43693-43698.
    • (2001) J. Biol. Chem. , vol.276 , pp. 43693-43698
    • Perret, S.1    Merle, S.2    Nettleton, J.3    Howard, J.4
  • 25
    • 0000523565 scopus 로고
    • Structure of collagen
    • Ramachandra, G. N., and G. Karthan. 1955. Structure of collagen. Nature. 176:593-595.
    • (1955) Nature , vol.176 , pp. 593-595
    • Ramachandra, G.N.1    Karthan, G.2
  • 26
    • 0028223671 scopus 로고
    • Atomic force microscopy study of the collagen fibre structure
    • Revenko, I., F. Sommer, D. T. Minh, R. Garrone, and J. M. Franc. 1994. Atomic force microscopy study of the collagen fibre structure. Biocell. 80:67-69.
    • (1994) Biocell. , vol.80 , pp. 67-69
    • Revenko, I.1    Sommer, F.2    Minh, D.T.3    Garrone, R.4    Franc, J.M.5
  • 27
    • 0031011695 scopus 로고    scopus 로고
    • Reversible unfolding of individual titin immunoglobulin domains by AFM
    • Rief, M., M. Gautel, F. Oesterhelt, J. M. Fernandez, and H. E. Gaub. 1997. Reversible unfolding of individual titin immunoglobulin domains by AFM. Science. 276:1109-1112.
    • (1997) Science , vol.276 , pp. 1109-1112
    • Rief, M.1    Gautel, M.2    Oesterhelt, F.3    Fernandez, J.M.4    Gaub, H.E.5
  • 28
    • 3342993179 scopus 로고    scopus 로고
    • Atomic force microscopy: Mechanical unfolding of proteins
    • Rounsevell, R., J. R. Forman, and J. Clarke. 2004. Atomic force microscopy: mechanical unfolding of proteins. Methods. 34:100-111.
    • (2004) Methods , vol.34 , pp. 100-111
    • Rounsevell, R.1    Forman, J.R.2    Clarke, J.3
  • 29
    • 0030033874 scopus 로고    scopus 로고
    • Vertical dimension of hydrated biological samples in tapping mode scanning force microscopy
    • Schaben, F. A., and J. P. Rabe. 1996. Vertical dimension of hydrated biological samples in tapping mode scanning force microscopy. Biophys. J. 70:1514-1520.
    • (1996) Biophys. J. , vol.70 , pp. 1514-1520
    • Schaben, F.A.1    Rabe, J.P.2
  • 30
    • 0002017332 scopus 로고
    • Electron microscopy investigations of the structure of collagens
    • Schmitt, F. D., C. E. Hall, and M. A. Jakns. 1942. Electron microscopy investigations of the structure of collagens. J. Cell. Comp. Physiol. 20: 11-33.
    • (1942) J. Cell. Comp. Physiol. , vol.20 , pp. 11-33
    • Schmitt, F.D.1    Hall, C.E.2    Jakns, M.A.3
  • 31
    • 0036064087 scopus 로고    scopus 로고
    • Direct quantification of the flexibility of type I collagen monomer
    • Sun, Y., Z. Luo, A. Fertala, and K. An. 2002. Direct quantification of the flexibility of type I collagen monomer. Biochem. Biophys. Res. Commun. 295:382-386.
    • (2002) Biochem. Biophys. Res. Commun. , vol.295 , pp. 382-386
    • Sun, Y.1    Luo, Z.2    Fertala, A.3    An, K.4
  • 32
    • 0031006659 scopus 로고    scopus 로고
    • Elasticity and unfolding of single molecules of the giant muscle protein titin
    • Tskhovrebova, L., J. Trinick, J. A. Sleep, and R. M. Simmons. 1997. Elasticity and unfolding of single molecules of the giant muscle protein titin. Nature. 387:308-312.
    • (1997) Nature , vol.387 , pp. 308-312
    • Tskhovrebova, L.1    Trinick, J.2    Sleep, J.A.3    Simmons, R.M.4
  • 33
    • 0031024293 scopus 로고    scopus 로고
    • Pathology of failure of the rotator cuff tendon
    • Uhthoff, H. K., and H. Sano. 1997. Pathology of failure of the rotator cuff tendon. Orthop. Clin. North Am. 28:31-41.
    • (1997) Orthop. Clin. North Am. , vol.28 , pp. 31-41
    • Uhthoff, H.K.1    Sano, H.2
  • 37
    • 0029845352 scopus 로고    scopus 로고
    • Imaging biological structures with the cryoatomic force microscope
    • Zhang, Y., S. J. Sheng, and Z. Shao. 1996. Imaging biological structures with the cryoatomic force microscope. Biophys. J: 71:2168-2176.
    • (1996) Biophys. J. , vol.71 , pp. 2168-2176
    • Zhang, Y.1    Sheng, S.J.2    Shao, Z.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.