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Volumn 75, Issue 6, 1998, Pages 3008-3014

The mechanical stability of immunoglobulin and fibronectin III domains in the muscle protein titin measured by atomic force microscopy

Author keywords

[No Author keywords available]

Indexed keywords

CONNECTIN; FIBRONECTIN; IMMUNOGLOBULIN; TENASCIN;

EID: 0031767965     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(98)77741-0     Document Type: Article
Times cited : (284)

References (34)
  • 1
    • 0027474006 scopus 로고
    • Cell- and heparin-binding domains of the hexabrachion arm identified by tenascin expression proteins
    • Aukhil, I., P. Joshi, Y. Yan, and H. P. Erickson. 1993. Cell-and heparin-binding domains of the hexabrachion arm identified by tenascin expression proteins. J. Biol. Chem. 268:2542-2553.
    • (1993) J. Biol. Chem. , vol.268 , pp. 2542-2553
    • Aukhil, I.1    Joshi, P.2    Yan, Y.3    Erickson, H.P.4
  • 2
    • 0018101150 scopus 로고
    • Models for the specific adhesion of cells to cells
    • Bell, G. I. 1978. Models for the specific adhesion of cells to cells. Science. 200:618-627.
    • (1978) Science , vol.200 , pp. 618-627
    • Bell, G.I.1
  • 3
    • 0031258656 scopus 로고    scopus 로고
    • Evidence that the tandem Ig domains near the end of the muscle thick filament form an inelastic part of the I-band titin
    • Bennett, P. M., T. E. Hodkin, and C. Hawkins. 1997. Evidence that the tandem Ig domains near the end of the muscle thick filament form an inelastic part of the I-band titin. J. Struct. Biol. 120:93-104.
    • (1997) J. Struct. Biol. , vol.120 , pp. 93-104
    • Bennett, P.M.1    Hodkin, T.E.2    Hawkins, C.3
  • 5
    • 34347209835 scopus 로고
    • Calculation of thermal noise in atomic force microscopy
    • Butt, H.-J., and M. Jaschke. 1995. Calculation of thermal noise in atomic force microscopy. Nanotechnology. 6:1-7.
    • (1995) Nanotechnology , vol.6 , pp. 1-7
    • Butt, H.-J.1    Jaschke, M.2
  • 6
    • 0031214818 scopus 로고    scopus 로고
    • Folding and stability of a fibronectin type III domain of human tenascin
    • Clarke, J., S. J. Hamill, and C. M. Johnson. 1997. Folding and stability of a fibronectin type III domain of human tenascin. J. Mol. Biol. 270: 771-778.
    • (1997) J. Mol. Biol. , vol.270 , pp. 771-778
    • Clarke, J.1    Hamill, S.J.2    Johnson, C.M.3
  • 7
    • 0001209838 scopus 로고    scopus 로고
    • Scanning tunneling microscopy study of L-cysteine on Au(111)
    • Dakkouri, A. S., D. M. Kolb, R. Edelstein-Shima, and D. Mandler. 1996. Scanning tunneling microscopy study of L-cysteine on Au(111). Langmuir. 12:2849-2852.
    • (1996) Langmuir , vol.12 , pp. 2849-2852
    • Dakkouri, A.S.1    Kolb, D.M.2    Edelstein-Shima, R.3    Mandler, D.4
  • 8
    • 0028028999 scopus 로고
    • Reversible unfolding of fibronectin type III and immunoglobulin domains provides the structural basis for stretch and elasticity of titin and fibronectin
    • Erickson, H. P. 1994. Reversible unfolding of fibronectin type III and immunoglobulin domains provides the structural basis for stretch and elasticity of titin and fibronectin. Proc. Natl. Acad. Sci. USA. 91: 10114-10118.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 10114-10118
    • Erickson, H.P.1
  • 9
    • 0030962748 scopus 로고    scopus 로고
    • Stretching single protein molecules: Titin is a weird spring
    • Erickson, H. P. 1997. Stretching single protein molecules: titin is a weird spring. Science. 276:1090-1092.
    • (1997) Science , vol.276 , pp. 1090-1092
    • Erickson, H.P.1
  • 10
    • 0025847304 scopus 로고
    • Detachment of agglutinin bonded red blood cells. I. Forces to rupture molecular point attachments
    • Evans, E., D. Berk, and A. Leung. 1991. Detachment of agglutinin bonded red blood cells. I. Forces to rupture molecular point attachments. Biophys. J. 59:838-848.
    • (1991) Biophys. J. , vol.59 , pp. 838-848
    • Evans, E.1    Berk, D.2    Leung, A.3
  • 12
    • 0026320866 scopus 로고
    • The energy landscapes and motions of proteins
    • Frauenfelder, H., A. G. Sligar, and P. G. Wolynes. 1991. The energy landscapes and motions of proteins. Science. 1598-1603.
    • (1991) Science , pp. 1598-1603
    • Frauenfelder, H.1    Sligar, A.G.2    Wolynes, P.G.3
  • 13
    • 0030052266 scopus 로고    scopus 로고
    • A molecular map of the interactions of titin and myosin-binding protein C: Implications for sarcomeric assembly in familial hypertrophic cardiomyopathy
    • Freiburg, A., and M. Gautel. 1996. A molecular map of the interactions of titin and myosin-binding protein C: implications for sarcomeric assembly in familial hypertrophic cardiomyopathy. Eur. J. Biochem. 235: 317-323.
    • (1996) Eur. J. Biochem. , vol.235 , pp. 317-323
    • Freiburg, A.1    Gautel, M.2
  • 14
    • 0023924769 scopus 로고
    • The organization of titin filaments in the half-sarcomere revealed by monoclonal antibodies in immunoelectron microscopy; a map of ten non-repetitive epitopes starting at the Z line extends close to the M line
    • Fürst, D. O., M. Osborn, R. Nave, and K. Weber. 1988. The organization of titin filaments in the half-sarcomere revealed by monoclonal antibodies in immunoelectron microscopy; a map of ten non-repetitive epitopes starting at the Z line extends close to the M line. J. Cell Biol. 106: 1563-1572.
    • (1988) J. Cell Biol. , vol.106 , pp. 1563-1572
    • Fürst, D.O.1    Osborn, M.2    Nave, R.3    Weber, K.4
  • 15
    • 0029882110 scopus 로고    scopus 로고
    • A molecular map of titin/connectin elasticity reveals two different mechanisms acting in series
    • Gautel, M., and D. Goulding. 1996. A molecular map of titin/connectin elasticity reveals two different mechanisms acting in series. FEBS Lett. 385:11-14.
    • (1996) FEBS Lett. , vol.385 , pp. 11-14
    • Gautel, M.1    Goulding, D.2
  • 16
    • 0029801781 scopus 로고    scopus 로고
    • Assembly of the cardiac I-band region of titin/connectin: Expression of the cardiac-specific regions and their relation to the elastic segments
    • Gautel, M., E. Lehtonen, and F. Pietruschka. 1996. Assembly of the cardiac I-band region of titin/connectin: expression of the cardiac-specific regions and their relation to the elastic segments. J. Muscle Res. Cell Motil. 17:449-461.
    • (1996) J. Muscle Res. Cell Motil. , vol.17 , pp. 449-461
    • Gautel, M.1    Lehtonen, E.2    Pietruschka, F.3
  • 17
    • 36449007442 scopus 로고
    • Calibration of atomic-force microscope tips
    • Hutter, J. L., and J. Bechhoefer. 1994. Calibration of atomic-force microscope tips. Rev. Sci. Instrum. 64:1868-1873.
    • (1994) Rev. Sci. Instrum. , vol.64 , pp. 1868-1873
    • Hutter, J.L.1    Bechhoefer, J.2
  • 18
    • 0031002460 scopus 로고    scopus 로고
    • Folding-unfolding transitions in single titin molecules characterized with laser tweezers
    • Kellermayer, M. S., S. B. Smith, H. L. Granzier, and C. Bustamante. 1997. Folding-unfolding transitions in single titin molecules characterized with laser tweezers. Science. 276:1112-1116.
    • (1997) Science , vol.276 , pp. 1112-1116
    • Kellermayer, M.S.1    Smith, S.B.2    Granzier, H.L.3    Bustamante, C.4
  • 19
    • 0028824480 scopus 로고
    • Titins, giant proteins in charge of muscle ultrastructure and elasticity
    • Labeit, S., and B. Kolmerer. 1995. Titins, giant proteins in charge of muscle ultrastructure and elasticity. Science. 270:293-296.
    • (1995) Science , vol.270 , pp. 293-296
    • Labeit, S.1    Kolmerer, B.2
  • 20
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head bacteriophage T4. Nature. 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 21
    • 0025191211 scopus 로고
    • Rapid purification of homodimer and heterodimer HIV-1 reverse transcriptase by metal chelate affinity chromatography
    • LeGrice, S. F. J., and F. Grüninger-Leitch. 1990. Rapid purification of homodimer and heterodimer HIV-1 reverse transcriptase by metal chelate affinity chromatography. Eur. J. Biochem. 187:307-314.
    • (1990) Eur. J. Biochem. , vol.187 , pp. 307-314
    • Legrice, S.F.J.1    Grüninger-Leitch, F.2
  • 22
    • 0032481560 scopus 로고    scopus 로고
    • Single-molecule force spectroscopy on xanthan by AFM
    • Li, H., M. Rief, F. Oesterhelt, and H. E. Gaub. 1998. Single-molecule force spectroscopy on xanthan by AFM. Adv. Materials. 10:316-319.
    • (1998) Adv. Materials , vol.10 , pp. 316-319
    • Li, H.1    Rief, M.2    Oesterhelt, F.3    Gaub, H.E.4
  • 24
    • 0030982846 scopus 로고    scopus 로고
    • Connectin/titin, giant elastic protein of muscle
    • Maruyama, K. 1997. Connectin/titin, giant elastic protein of muscle. FASEB J. 11:341-345.
    • (1997) FASEB J. , vol.11 , pp. 341-345
    • Maruyama, K.1
  • 26
    • 0032516205 scopus 로고    scopus 로고
    • The molecular elasticity of the extracellular matrix protein tenascin
    • Oberhauser, A. F., P. E. Marszalek, H. P. Erickson, and J. M. Fernandez. 1998. The molecular elasticity of the extracellular matrix protein tenascin. Nature. 393:181-185.
    • (1998) Nature , vol.393 , pp. 181-185
    • Oberhauser, A.F.1    Marszalek, P.E.2    Erickson, H.P.3    Fernandez, J.M.4
  • 27
    • 0028058747 scopus 로고
    • Immunoglobulin-type domains of titin are stabilized by amino-terminal extension
    • Politou, A. S., M. Gautel, C. Joseph, and A. Pastore. 1994. Immunoglobulin-type domains of titin are stabilized by amino-terminal extension. FEBS Lett. 352:27-31.
    • (1994) FEBS Lett. , vol.352 , pp. 27-31
    • Politou, A.S.1    Gautel, M.2    Joseph, C.3    Pastore, A.4
  • 28
    • 0028834886 scopus 로고
    • The folding and stability of titin immunoglobulin-like modules, with implications for the mechanism of elasticity
    • Politou, A. S., D. J. Thomas, and A. Pastore. 1995. The folding and stability of titin immunoglobulin-like modules, with implications for the mechanism of elasticity. Biophys. J. 69:2601-2610.
    • (1995) Biophys. J. , vol.69 , pp. 2601-2610
    • Politou, A.S.1    Thomas, D.J.2    Pastore, A.3
  • 29
    • 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. 1997a. 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
  • 30
    • 0031042739 scopus 로고    scopus 로고
    • Single molecule force spectroscopy on polysaccharides by AFM
    • Rief, M., F. Oesterhelt, B. Heymann, and H. E. Gaub. 1997b. Single molecule force spectroscopy on polysaccharides by AFM. Science. 275:1295-1297.
    • (1997) Science , vol.275 , pp. 1295-1297
    • Rief, M.1    Oesterhelt, F.2    Heymann, B.3    Gaub, H.E.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
    • 0025816649 scopus 로고
    • Regulation of skeletal muscle stiffness and elasticity by titin isoforms: A test of the segmental extension model of resting tension
    • Wang, K., R. McCarter, J. Wright, J. Beverly, and R. Ramirez-Mitchell. 1991. Regulation of skeletal muscle stiffness and elasticity by titin isoforms: a test of the segmental extension model of resting tension. Proc. Natl. Acad. Sci. USA. 88:7101-7105.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 7101-7105
    • Wang, K.1    McCarter, R.2    Wright, J.3    Beverly, J.4    Ramirez-Mitchell, R.5
  • 34
    • 0011450535 scopus 로고
    • Titin: Major myofibrillar components of striated muscle
    • Wang, K., J. McClure, and A. Tu. 1979. Titin: major myofibrillar components of striated muscle. Proc. Natl. Acad. Sci. USA. 76:3698-3702.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 3698-3702
    • Wang, K.1    McClure, J.2    Tu, A.3


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