메뉴 건너뛰기




Volumn 402, Issue 6757, 1999, Pages 100-103

Mechanical unfolding intermediates in titin modules

Author keywords

[No Author keywords available]

Indexed keywords

CONNECTIN;

EID: 0033523904     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/47083     Document Type: Article
Times cited : (720)

References (30)
  • 1
    • 0030962748 scopus 로고    scopus 로고
    • Stretching single protein molecules: Titin is a weird spring
    • Erickson, H. P. Stretching single protein molecules: titin is a weird spring. Science 276, 1090-1092 (1997).
    • (1997) Science , vol.276 , pp. 1090-1092
    • Erickson, H.P.1
  • 2
    • 0031006659 scopus 로고    scopus 로고
    • Elasticity and unfolding of single molecules of the giant muscle protein titin
    • Tskhovrebova, L., Trinick, J., Sleep, J. A. & Simmons, R. M. Elasticity and unfolding of single molecules of the giant muscle protein titin. Nature 387, 308-312 (1997).
    • (1997) Nature , vol.387 , pp. 308-312
    • Tskhovrebova, L.1    Trinick, J.2    Sleep, J.A.3    Simmons, R.M.4
  • 3
    • 0031002460 scopus 로고    scopus 로고
    • Folding-unfolding transitions in single titin molecules characterized with laser tweezers
    • Kellermayer, M. S. Z., Smith, S. B., Granzier, H. L. & Bustamante, C. Folding-unfolding transitions in single titin molecules characterized with laser tweezers. Science 276, 1112-1116 (1997).
    • (1997) Science , vol.276 , pp. 1112-1116
    • Kellermayer, M.S.Z.1    Smith, S.B.2    Granzier, H.L.3    Bustamante, C.4
  • 5
    • 0031011695 scopus 로고    scopus 로고
    • Reversible unfolding of individual titin immunoglobulin domains by AFM
    • Rief, M., Gautel, M., Oesterbelt, F., Fernandez, J. M. & Gaub, H. E. Reversible unfolding of individual titin immunoglobulin domains by AFM. Science 76, 1109-1112 (1997).
    • (1997) Science , vol.76 , pp. 1109-1112
    • Rief, M.1    Gautel, M.2    Oesterbelt, F.3    Fernandez, J.M.4    Gaub, H.E.5
  • 6
    • 11544281834 scopus 로고    scopus 로고
    • Elastically coupled two-level-systems as a model for biopolymer extensibility
    • Rief, M., Fernandez, J. M. & Gaub, H. E. Elastically coupled two-level-systems as a model for biopolymer extensibility. Phys. Rev. Lett. 81, 4764-4767 (1998).
    • (1998) Phys. Rev. Lett. , vol.81 , pp. 4764-4767
    • Rief, M.1    Fernandez, J.M.2    Gaub, H.E.3
  • 7
    • 0033616713 scopus 로고    scopus 로고
    • Mechanical and chemical unfolding of a single protein: A comparison
    • Carrion-Vazquez, M. et al. Mechanical and chemical unfolding of a single protein: a comparison. Proc. Natl Acad. Sci. USA 96, 3694-3699 (1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 3694-3699
    • Carrion-Vazquez, M.1
  • 8
    • 0033151955 scopus 로고    scopus 로고
    • Steered molecular dynamics simulations of force-induced protein domain unfolding
    • Lu, H. & Schulten, K. Steered molecular dynamics simulations of force-induced protein domain unfolding. Profeifts Struct. Funct., Genet. 35 1453-463 (1999).
    • (1999) Profeifts Struct. Funct., Genet. , vol.35 , pp. 1453-1463
    • Lu, H.1    Schulten, K.2
  • 9
    • 0030987036 scopus 로고    scopus 로고
    • Molecular dynamics study of unbinding of the avidin-biotin complex
    • Izrailev, I., Stepaniants, S., Baisera, M., Oono, Y. & Schulten, K. Molecular dynamics study of unbinding of the avidin-biotin complex. Biophys. J. 72, 1568-1581 (1997).
    • (1997) Biophys. J. , vol.72 , pp. 1568-1581
    • Izrailev, I.1    Stepaniants, S.2    Baisera, M.3    Oono, Y.4    Schulten, K.5
  • 11
    • 0028834886 scopus 로고
    • The folding and stability of titin immunoglobulin-like modules, with implications for the mechanism of elasticity
    • Politou, A. S., Thomas, D. J. & Pastore, A. The folding and stability of titin immunoglobulin-like modules, with implications for the mechanism of elasticity. Biophys. J. 69, 2601-2610 (1995).
    • (1995) Biophys. J. , vol.69 , pp. 2601-2610
    • Politou, A.S.1    Thomas, D.J.2    Pastore, A.3
  • 12
    • 0030009318 scopus 로고    scopus 로고
    • The elastic I-band region of titin is assembled in a "modular" fashion by weakly interacting Ig-like domains
    • Politou, A. S., Gautel, M., Improta, S., Vangelista, L & Pastore, A. The elastic I-band region of titin is assembled in a "modular" fashion by weakly interacting Ig-like domains. J. Mol. Biol. 255, 604-616 (1996).
    • (1996) J. Mol. Biol. , vol.255 , pp. 604-616
    • Politou, A.S.1    Gautel, M.2    Improta, S.3    Vangelista, L.4    Pastore, A.5
  • 13
    • 0032484034 scopus 로고    scopus 로고
    • The assembly of immunoglobulin-like modules in titin: Implications for muscle elasticity
    • Improta, S. et al. The assembly of immunoglobulin-like modules in titin: implications for muscle elasticity. J. Mol Biol. 284, 761-777 (1998).
    • (1998) J. Mol Biol. , vol.284 , pp. 761-777
    • Improta, S.1
  • 14
    • 0030048904 scopus 로고    scopus 로고
    • Nonuniform elasticity of titin in cardiac myocytes: A study using imnumoelectron microscopy and cellular mechanics
    • Granzier, H., Helmes, M. & Trombitas, K. Nonuniform elasticity of titin in cardiac myocytes: A study using imnumoelectron microscopy and cellular mechanics. Biophys. J. 70, 430-442 (1996).
    • (1996) Biophys. J. , vol.70 , pp. 430-442
    • Granzier, H.1    Helmes, M.2    Trombitas, K.3
  • 15
    • 0030855930 scopus 로고    scopus 로고
    • Titin elasticity and mechanism of passive force development in rat cardiac myocytes probed by thin-filament extraction
    • Granzier, H., Kellermayer, M., Helmes, M. & Trobitas, K. Titin elasticity and mechanism of passive force development in rat cardiac myocytes probed by thin-filament extraction. Biophys. J. 73, 2043-2053 (1997).
    • (1997) Biophys. J. , vol.73 , pp. 2043-2053
    • Granzier, H.1    Kellermayer, M.2    Helmes, M.3    Trobitas, K.4
  • 16
    • 0032559640 scopus 로고    scopus 로고
    • Titin extensibility in situ: Entropic elasticity of permanently folded and permanently unfolded molecular segments
    • Trombitas, K. et al. Titin extensibility in situ: entropic elasticity of permanently folded and permanently unfolded molecular segments. J. Cell Biol. 140, 853-859 (1998).
    • (1998) J. Cell Biol. , vol.140 , pp. 853-859
    • Trombitas, K.1
  • 17
    • 0028824480 scopus 로고
    • Titins: Giant proteins in charge of muscle ultrastructure and elasticity
    • Labeit, S. & Kolmerer, B. Titins: giant proteins in charge of muscle ultrastructure and elasticity. Science 270, 293-296 (1995).
    • (1995) Science , vol.270 , pp. 293-296
    • Labeit, S.1    Kolmerer, B.2
  • 18
    • 0031016596 scopus 로고    scopus 로고
    • The giant protein titin. Emerging roles in physiology and pathophysiology
    • Labeit, S., Kolmerer, B. & Linke, W. A. The giant protein titin. Emerging roles in physiology and pathophysiology. Circ Res. 80, 290-294 (1997).
    • (1997) Circ Res. , vol.80 , pp. 290-294
    • Labeit, S.1    Kolmerer, B.2    Linke, W.A.3
  • 19
    • 0031809493 scopus 로고    scopus 로고
    • Characterizing titin's I-band Ig domain region as an entropic spring
    • Linke, W. A., Stockmeier, M. R., Ivemeyer, M., Hosser, H. & Mundel, P. Characterizing titin's I-band Ig domain region as an entropic spring. J. Cell Sci. 111, 1567-1574 (1998).
    • (1998) J. Cell Sci. , vol.111 , pp. 1567-1574
    • Linke, W.A.1    Stockmeier, M.R.2    Ivemeyer, M.3    Hosser, H.4    Mundel, P.5
  • 20
    • 0029882110 scopus 로고    scopus 로고
    • A molecular map of titin/connectin elasticity reveals two different mechanisms acting in series
    • Gautel, M. & Goulding, D. A molecular map of titin/connectin elasticity reveals two different mechanisms acting in series. FEBS Lett. 385, 11-14 (1996).
    • (1996) FEBS Lett. , vol.385 , pp. 11-14
    • Gautel, M.1    Goulding, D.2
  • 21
    • 0033582763 scopus 로고    scopus 로고
    • Single molecule force spectroscopy of spectrin repeats: Low unfolding forces in helix bundles
    • Rief, M., Pascual, J., Saraste, M. & Gaub, H. E Single molecule force spectroscopy of spectrin repeats: low unfolding forces in helix bundles. J. Mol. Biol. 286, 553-561 (1999).
    • (1999) J. Mol. Biol. , vol.286 , pp. 553-561
    • Rief, M.1    Pascual, J.2    Saraste, M.3    Gaub, H.E.4
  • 22
    • 0032542229 scopus 로고    scopus 로고
    • Polysaccharide elasticity governed by chair-boat transitions of the glucopyranose ring
    • Marszalek, P. E., Oberhauxr, A. F., Pang, Y.-P. & Fernandez, J. M. Polysaccharide elasticity governed by chair-boat transitions of the glucopyranose ring. Nature 396, 661-664 (1998).
    • (1998) Nature , vol.396 , pp. 661-664
    • Marszalek, P.E.1    Oberhauxr, A.F.2    Pang, Y.-P.3    Fernandez, J.M.4
  • 23
    • 0031848099 scopus 로고    scopus 로고
    • Unfolding of titin immunoglobulin domains by steered molecular dynamics simulation
    • Lu, H., Isralewitz, B., Krammer, A., Vogel, V. & Schulten, K. Unfolding of titin immunoglobulin domains by steered molecular dynamics simulation. Biophys. J. 75, 662-671 (1998).
    • (1998) Biophys. J. , vol.75 , pp. 662-671
    • Lu, H.1    Isralewitz, B.2    Krammer, A.3    Vogel, V.4    Schulten, K.5
  • 24
    • 0032988663 scopus 로고    scopus 로고
    • Strength of a weak bond connecting flexible polymer chains
    • Evans, E. & Ritchie, K. Strength of a weak bond connecting flexible polymer chains. Biophys. J. 76, 2439-2447 (1999).
    • (1999) Biophys. J. , vol.76 , pp. 2439-2447
    • Evans, E.1    Ritchie, K.2
  • 26
    • 0032516205 scopus 로고    scopus 로고
    • The molecular elasticity of the extracellular matrix protein tenascin
    • Oberhauser, A. F., Marszalek, P. E., Erickson, H. P. & Fernandez, J. M. The molecular elasticity of the extracellular matrix protein tenascin. Nature 393, 181-185 (1998).
    • (1998) Nature , vol.393 , pp. 181-185
    • Oberhauser, A.F.1    Marszalek, P.E.2    Erickson, H.P.3    Fernandez, J.M.4
  • 27
    • 0028834673 scopus 로고
    • Sensing specific molecular interactions with the atomic force microscope
    • Florin, E. L. et al. Sensing specific molecular interactions with the atomic force microscope. Biosens. Bioelelectr. 10, 895-901 (1995).
    • (1995) Biosens. Bioelelectr. , vol.10 , pp. 895-901
    • Florin, E.L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.