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Volumn 25, Issue 3, 2006, Pages 175-184

Understanding the elasticity of fibronectin fibrils: Unfolding strengths of FN-III and GFP domains measured by single molecule force spectroscopy

Author keywords

Protein unfolding; Single molecule force spectroscopy; Wormlike chain

Indexed keywords

FIBRONECTIN; GREEN FLUORESCENT PROTEIN;

EID: 33645417227     PISSN: 0945053X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.matbio.2005.10.007     Document Type: Article
Times cited : (59)

References (41)
  • 2
    • 0035807873 scopus 로고    scopus 로고
    • Coexisting conformations of fibronectin in cell culture imaged using fluorescence resonance energy transfer
    • G. Baneyx, L. Baugh, and V. Vogel Coexisting conformations of fibronectin in cell culture imaged using fluorescence resonance energy transfer Proc. Natl. Acad. Sci. U. S. A. 98 2001 14464 14468
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 14464-14468
    • Baneyx, G.1    Baugh, L.2    Vogel, V.3
  • 3
    • 0037117522 scopus 로고    scopus 로고
    • Fibronectin extension and unfolding within cell matrix fibrils controlled by cytoskeletal tension
    • G. Baneyx, L. Baugh, and V. Vogel Fibronectin extension and unfolding within cell matrix fibrils controlled by cytoskeletal tension Proc. Natl. Acad. Sci. U. S. A. 99 2002 5139 5143
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 5139-5143
    • Baneyx, G.1    Baugh, L.2    Vogel, V.3
  • 4
    • 0034804341 scopus 로고    scopus 로고
    • Can non-mechanical proteins withstand force? Stretching Barnase by atomic force microscopy and molecular dynamic simulation
    • R.B. Best, B. Li, A. Steward, V. Daggett, and J. Clarke Can non-mechanical proteins withstand force? Stretching Barnase by atomic force microscopy and molecular dynamic simulation Biophys. J. 81 2001 2344 2356
    • (2001) Biophys. J. , vol.81 , pp. 2344-2356
    • Best, R.B.1    Li, B.2    Steward, A.3    Daggett, V.4    Clarke, J.5
  • 5
    • 0026644395 scopus 로고
    • Proposed acquisitions of an animal protein domain by bacteria
    • P. Bork, and R.F. Doolittle Proposed acquisitions of an animal protein domain by bacteria Proc. Natl. Acad. Sci. U. S. A. 89 1992 8990 8994
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 8990-8994
    • Bork, P.1    Doolittle, R.F.2
  • 9
    • 9244234443 scopus 로고    scopus 로고
    • Exploring the energy landscape of GFP single-molecule mechanical experiments
    • H. Dietz, and M. Rief Exploring the energy landscape of GFP single-molecule mechanical experiments Proc. Natl. Acad. Sci. U. S. A. 101 2004 16192 16197
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 16192-16197
    • Dietz, H.1    Rief, M.2
  • 11
    • 0021058825 scopus 로고
    • Fibronectin in extended and collapsed conformations, electron microscopy and sedimentation analysis
    • H.P. Erickson, and N.A. Carrell Fibronectin in extended and collapsed conformations, electron microscopy and sedimentation analysis J. Biol. Chem. 258 1983 539 544
    • (1983) J. Biol. Chem. , vol.258 , pp. 539-544
    • Erickson, H.P.1    Carrell, N.A.2
  • 12
    • 0031001349 scopus 로고    scopus 로고
    • Dynamic strength of molecular adhesion bonds
    • E. Evans, and K. Ritchie Dynamic strength of molecular adhesion bonds Biophys. J. 72 1997 1541 1555
    • (1997) Biophys. J. , vol.72 , pp. 1541-1555
    • Evans, E.1    Ritchie, K.2
  • 13
    • 0032988663 scopus 로고    scopus 로고
    • Strength of a weak bond connecting flexible polymer chains
    • E. Evans, and K. Ritchie Strength of a weak bond connecting flexible polymer chains Biophys. J. 76 1999 2439 2447
    • (1999) Biophys. J. , vol.76 , pp. 2439-2447
    • Evans, E.1    Ritchie, K.2
  • 16
    • 0033817704 scopus 로고    scopus 로고
    • Stretching single molecules into novel conformations using the atomic force microscope
    • T.E. Fisher, P.E. Marszalek, and J.M. Fernandez Stretching single molecules into novel conformations using the atomic force microscope Nat. Struct. Biol. 7 2000 719 724
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 719-724
    • Fisher, T.E.1    Marszalek, P.E.2    Fernandez, J.M.3
  • 17
    • 0028926188 scopus 로고
    • Mechanical properties of the extracellular matrix influence fibronectin fibril assembly in vitro
    • N.L. Halliday, and J.J. Tomasek Mechanical properties of the extracellular matrix influence fibronectin fibril assembly in vitro Exp. Cell Res. 217 1995 109 117
    • (1995) Exp. Cell Res. , vol.217 , pp. 109-117
    • Halliday, N.L.1    Tomasek, J.J.2
  • 18
    • 36449007442 scopus 로고
    • Calibration of atomic force microscope tips
    • J.L. Hutter, and J. Bechhoefer Calibration of atomic force microscope tips Rev. Sci. Instrum. 64 1993 1868 1873
    • (1993) Rev. Sci. Instrum. , vol.64 , pp. 1868-1873
    • Hutter, J.L.1    Bechhoefer, J.2
  • 19
    • 0033016468 scopus 로고    scopus 로고
    • The compact conformation of fibronectin is determined by intramolecular ionic interactions
    • K.J. Johnson, H. Sage, G. Briscoe, and H.P. Erickson The compact conformation of fibronectin is determined by intramolecular ionic interactions J. Biol. Chem. 274 1999 15473 15479
    • (1999) J. Biol. Chem. , vol.274 , pp. 15473-15479
    • Johnson, K.J.1    Sage, H.2    Briscoe, G.3    Erickson, H.P.4
  • 20
    • 0030050396 scopus 로고    scopus 로고
    • 2.0 angstrom crystal structure of a four-domain segment of human fibronectin encompassing the RGD loop and synergy region
    • D.J. Leahy, I. Aukhil, and H.P. Erickson 2.0 angstrom crystal structure of a four-domain segment of human fibronectin encompassing the RGD loop and synergy region Cell 84 1996 155 164
    • (1996) Cell , vol.84 , pp. 155-164
    • Leahy, D.J.1    Aukhil, I.2    Erickson, H.P.3
  • 24
    • 10044247452 scopus 로고    scopus 로고
    • Mechanical unfolding intermediates observed by single-molecule force spectroscopy in a fibronectin type III module
    • H. Li, H.H.-L. Huang, C.L. Badilla, and J.M. Fernandez Mechanical unfolding intermediates observed by single-molecule force spectroscopy in a fibronectin type III module J. Mol. Biol. 345 2005 817 826
    • (2005) J. Mol. Biol. , vol.345 , pp. 817-826
    • Li, H.1    Huang, H.H.-L.2    Badilla, C.L.3    Fernandez, J.M.4
  • 27
    • 0344062772 scopus 로고    scopus 로고
    • Single-molecule force spectroscopy of isolated and aggregated fibronectin proteins on negatively charged surfaces in aqueous liquids
    • P.Y. Meadows, J.E. Bemis, and G.C. Walker Single-molecule force spectroscopy of isolated and aggregated fibronectin proteins on negatively charged surfaces in aqueous liquids Langmuir 19 2003 9566 9572
    • (2003) Langmuir , vol.19 , pp. 9566-9572
    • Meadows, P.Y.1    Bemis, J.E.2    Walker, G.C.3
  • 28
    • 0032516205 scopus 로고    scopus 로고
    • The molecular elasticity of the extracellular matrix protein tenascin
    • A.F. Oberhauser, P.E. Marszalek, H.P. Erickson, and J.M. Fernandez The molecular elasticity of the extracellular matrix protein tenascin Nature 393 1998 181 185
    • (1998) Nature , vol.393 , pp. 181-185
    • Oberhauser, A.F.1    Marszalek, P.E.2    Erickson, H.P.3    Fernandez, J.M.4
  • 29
    • 0038368702 scopus 로고    scopus 로고
    • Conformational analysis of native fibronectin by means of force spectroscopy
    • Y. Oberdorfer, H. Fuchs, and A. Janshoff Conformational analysis of native fibronectin by means of force spectroscopy Langmuir 16 2000 9955 9958
    • (2000) Langmuir , vol.16 , pp. 9955-9958
    • Oberdorfer, Y.1    Fuchs, H.2    Janshoff, A.3
  • 31
    • 0033515070 scopus 로고    scopus 로고
    • Dynamics and elasticity of the fibronectin matrix in living cell culture visualized by fibronectin-green fluorescent protein
    • T. Ohashi, D.P. Kiehart, and H.P. Erickson Dynamics and elasticity of the fibronectin matrix in living cell culture visualized by fibronectin-green fluorescent protein Proc. Natl. Acad. Sci. U. S. A. 96 1999 2153 2158
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 2153-2158
    • Ohashi, T.1    Kiehart, D.P.2    Erickson, H.P.3
  • 32
    • 0037087773 scopus 로고    scopus 로고
    • Dual labeling of the fibronectin matrix and actin cytoskeleton with green fluorescent protein variants
    • T. Ohashi, D.P. Kiehart, and H.P. Erickson Dual labeling of the fibronectin matrix and actin cytoskeleton with green fluorescent protein variants J. Cell Sci. 115 2002 1221 1229
    • (2002) J. Cell Sci. , vol.115 , pp. 1221-1229
    • Ohashi, T.1    Kiehart, D.P.2    Erickson, H.P.3
  • 34
    • 0030298383 scopus 로고    scopus 로고
    • Structure and function of fibronectin modules
    • J.R. Potts, and I.D. Campbell Structure and function of fibronectin modules Matrix Biol. 15 1996 313 320
    • (1996) Matrix Biol. , vol.15 , pp. 313-320
    • Potts, J.R.1    Campbell, I.D.2
  • 35
    • 0031011695 scopus 로고    scopus 로고
    • Reversible unfolding of individual titin immunoglobulin domains by AFM
    • M. Rief, M. Gautel, F. Oesterhelt, J.M. Fernandez, and H.E. Gaub Reversible unfolding of individual titin immunoglobulin domains by AFM Science 276 1997 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
  • 36
    • 11544281834 scopus 로고    scopus 로고
    • Elasticity coupled two-level systems as a model for biopolymer extensibility
    • M. Rief, J.M. Fernandez, and H.E. Gaub Elasticity coupled two-level systems as a model for biopolymer extensibility Phys. Rev. Lett. 81 1998 4764
    • (1998) Phys. Rev. Lett. , vol.81 , pp. 4764
    • Rief, M.1    Fernandez, J.M.2    Gaub, H.E.3
  • 37
    • 0031767965 scopus 로고    scopus 로고
    • The mechanical stability of immunoglobulin and fibronectin III domains in the muscle protein titin as measured by AFM
    • M. Rief, M. Gautel, A. Schemmel, and H.E. Gaub The mechanical stability of immunoglobulin and fibronectin III domains in the muscle protein titin as measured by AFM Biophys. J. 75 1998 3008 3014
    • (1998) Biophys. J. , vol.75 , pp. 3008-3014
    • Rief, M.1    Gautel, M.2    Schemmel, A.3    Gaub, H.E.4
  • 38
    • 0033582763 scopus 로고    scopus 로고
    • Single molecule force spectroscopy of spectrin repeats: Low unfolding forces in helix bundles
    • M. Rief, J. Pascual, M. Saraste, and H.E. Gaub Single molecule force spectroscopy of spectrin repeats: low unfolding forces in helix bundles J. Mol. Biol. 286 1999 553 561
    • (1999) J. Mol. Biol. , vol.286 , pp. 553-561
    • Rief, M.1    Pascual, J.2    Saraste, M.3    Gaub, H.E.4
  • 41
    • 0032550177 scopus 로고    scopus 로고
    • Rho-mediated contractility exposes a cryptic site in fibronectin and induces fibronectin matrix assembly
    • C.L. Zhong, M. Chrzanowskawodnicka, J. Brown, A. Shaub, A.M. Belkin, and K. Burridge Rho-mediated contractility exposes a cryptic site in fibronectin and induces fibronectin matrix assembly J. Cell Biol. 141 1998 539 551
    • (1998) J. Cell Biol. , vol.141 , pp. 539-551
    • Zhong, C.L.1    Chrzanowskawodnicka, M.2    Brown, J.3    Shaub, A.4    Belkin, A.M.5    Burridge, K.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.