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Volumn 243, Issue 1-2, 1997, Pages 430-436

Energy-filtered electron microscopy reveals that talin is a highly flexible protein composed of a series of globular domains

Author keywords

Cytoskeletal; Electron microscopy; Electron spectroscopic imaging; Structure; Talin

Indexed keywords

CYTOSKELETON PROTEIN; TALIN;

EID: 0031033956     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1997.0430a.x     Document Type: Article
Times cited : (45)

References (38)
  • 1
    • 4243392875 scopus 로고
    • Electron spectroscopic imaging: An advanced technique for imaging and analysis in transmission electron microscopy
    • Bauer, J. (1988) Electron spectroscopic imaging: an advanced technique for imaging and analysis in transmission electron microscopy, Methods Microbiol. 20, 113-146.
    • (1988) Methods Microbiol. , vol.20 , pp. 113-146
    • Bauer, J.1
  • 2
    • 0023661249 scopus 로고
    • Colocalization of calcium-dependent protease II and one of its substrates at sites of cell adhesion
    • Beckerle, M. C., Burridge, K., DeMartino, G. N. & Croall, D. (1987) Colocalization of calcium-dependent protease II and one of its substrates at sites of cell adhesion, Cell 51, 569-577.
    • (1987) Cell , vol.51 , pp. 569-577
    • Beckerle, M.C.1    Burridge, K.2    DeMartino, G.N.3    Croall, D.4
  • 3
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding, Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 4
    • 0020805412 scopus 로고
    • A new protein of adhesion plaques and membrane ruffles
    • Burridge, K. & Connell, L. (1983a) A new protein of adhesion plaques and membrane ruffles, J. Cell Biol. 97, 359-367.
    • (1983) J. Cell Biol. , vol.97 , pp. 359-367
    • Burridge, K.1    Connell, L.2
  • 5
    • 0020999298 scopus 로고
    • Talin: A cytoskeletal component concentrated in adhesion plaques and other sites of actin-membrane interaction
    • Burridge, K. & Connell, L (1983b) Talin: a cytoskeletal component concentrated in adhesion plaques and other sites of actin-membrane interaction, Cell Motil. 3, 405-417.
    • (1983) Cell Motil. , vol.3 , pp. 405-417
    • Burridge, K.1    Connell, L.2
  • 6
    • 0021214312 scopus 로고
    • An interaction between vinculin and talin
    • Burridge, K. & Mangeat, P. (1984) An interaction between vinculin and talin, Nature 308, 744-746.
    • (1984) Nature , vol.308 , pp. 744-746
    • Burridge, K.1    Mangeat, P.2
  • 10
    • 0020119114 scopus 로고
    • An F-actin- and calmodulin-binding protein from isolated intestinal brush borders has a morphology related to spectrin
    • Glenney, J. R., Glenney, J. R. P., Osborn, M. & Weber, K. (1982) An F-actin- and calmodulin-binding protein from isolated intestinal brush borders has a morphology related to spectrin, Cell 28, 843-854.
    • (1982) Cell , vol.28 , pp. 843-854
    • Glenney, J.R.1    Glenney, J.R.P.2    Osborn, M.3    Weber, K.4
  • 11
    • 8044260325 scopus 로고
    • Rotary shadowing for visualizing rod-shaped proteins
    • Sommerville, J. & Scheer, U., eds IRL Press Limited, Oxford
    • Glenney, J. R. (1987) Rotary shadowing for visualizing rod-shaped proteins, in Electron microscopy in molecular biology: a practical approach (Sommerville, J. & Scheer, U., eds) pp. 167-178, IRL Press Limited, Oxford.
    • (1987) Electron Microscopy in Molecular Biology: A Practical Approach , pp. 167-178
    • Glenney, J.R.1
  • 13
    • 0028067413 scopus 로고
    • Native talin is a dumbbell-shaped homodimer when it interacts with actin
    • Goldmann, W. H., Bremer, A., Haner, M., Aebi, U. & Isenberg, G. (1994) Native talin is a dumbbell-shaped homodimer when it interacts with actin, J. Struct. Biol. 112, 3-10.
    • (1994) J. Struct. Biol. , vol.112 , pp. 3-10
    • Goldmann, W.H.1    Bremer, A.2    Haner, M.3    Aebi, U.4    Isenberg, G.5
  • 14
    • 0019433121 scopus 로고
    • Structure of macrophage actin-binding protein molecules in solution and interacting with actin filaments
    • Hartwig, J. H. & Stossel, T. P. (1981) Structure of macrophage actin-binding protein molecules in solution and interacting with actin filaments, J. Mol. Biol. 145, 563-581.
    • (1981) J. Mol. Biol. , vol.145 , pp. 563-581
    • Hartwig, J.H.1    Stossel, T.P.2
  • 15
    • 0022534722 scopus 로고
    • Interaction of plasma membrane fibronectin receptor with talin - A transmembrane linkage
    • Horwitz, A., Duggan, K., Buck, C., Beckerle, M. C. & Burridge, K. (1986) Interaction of plasma membrane fibronectin receptor with talin - a transmembrane linkage, Nature 320, 531-533.
    • (1986) Nature , vol.320 , pp. 531-533
    • Horwitz, A.1    Duggan, K.2    Buck, C.3    Beckerle, M.C.4    Burridge, K.5
  • 16
    • 0023710857 scopus 로고
    • A precursor of the focal contact in cultured fibroblasts
    • Izzard, C. S. (1988) A precursor of the focal contact in cultured fibroblasts, Cell Motil. Cytoskeleton 10, 137-142.
    • (1988) Cell Motil. Cytoskeleton , vol.10 , pp. 137-142
    • Izzard, C.S.1
  • 18
    • 0030222341 scopus 로고    scopus 로고
    • Crosstalk between cell adhesion molecules
    • Jockusch, B. M. & Rüdiger, M. (1996) Crosstalk between cell adhesion molecules, Trends Cell Biol. 6, 311-315.
    • (1996) Trends Cell Biol. , vol.6 , pp. 311-315
    • Jockusch, B.M.1    Rüdiger, M.2
  • 20
    • 0027433507 scopus 로고
    • Fourier transformed infrared spectroscopic studies of the secondary structure of spectrin under different ionic strength
    • LaBrake, C. C., Wang, L., Keiderling, T. A. & Fung, L. W.-M. (1993) Fourier transformed infrared spectroscopic studies of the secondary structure of spectrin under different ionic strength, Biochemistry 32, 10296-10302.
    • (1993) Biochemistry , vol.32 , pp. 10296-10302
    • LaBrake, C.C.1    Wang, L.2    Keiderling, T.A.3    Fung, L.W.-M.4
  • 21
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophages T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophages T4, Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 23
    • 0022891198 scopus 로고
    • A rapid method for preparing perforated supporting foils for the thin carbon films used in high resolution transmission electron microscopy
    • Lünsdorf, H. & Spiess, E. (1986) A rapid method for preparing perforated supporting foils for the thin carbon films used in high resolution transmission electron microscopy, J. Microsc. (Oxf.) 144, 211-213.
    • (1986) J. Microsc. (Oxf.) , vol.144 , pp. 211-213
    • Lünsdorf, H.1    Spiess, E.2
  • 27
    • 0029050645 scopus 로고
    • Organization of the functional domains in membrane cytoskeletal protein talin
    • Muguruma, M., Nishimuta, S., Tomisaka, Y., Ito, T. & Matsumura, S. (1995) Organization of the functional domains in membrane cytoskeletal protein talin, J. Biochem, 117, 1036-1042.
    • (1995) J. Biochem , vol.117 , pp. 1036-1042
    • Muguruma, M.1    Nishimuta, S.2    Tomisaka, Y.3    Ito, T.4    Matsumura, S.5
  • 28
    • 0028146835 scopus 로고
    • Identification of functional domains in the cytoskeletal protein talin
    • Niggli, V., Kaufmann, S., Goldmann, W. H., Weber, T. & Isenberg, G. (1994) Identification of functional domains in the cytoskeletal protein talin, Eur. J. Biochem. 227, 951-957.
    • (1994) Eur. J. Biochem. , vol.227 , pp. 951-957
    • Niggli, V.1    Kaufmann, S.2    Goldmann, W.H.3    Weber, T.4    Isenberg, G.5
  • 29
    • 0022958824 scopus 로고
    • Purification and assay of vinculin, metavinculin, and talin
    • O'Halloran, T., Molony, L. & Burridge, K. (1986) Purification and assay of vinculin, metavinculin, and talin, Methods Enzymol. 134, 69-77.
    • (1986) Methods Enzymol. , vol.134 , pp. 69-77
    • O'Halloran, T.1    Molony, L.2    Burridge, K.3
  • 30
    • 0024990759 scopus 로고
    • Sequence and domain structure of talin
    • Rees, D. J. G., Ades, S. E., Singer, S. J. & Hynes, R. O. (1990) Sequence and domain structure of talin, Nature 347, 685-689.
    • (1990) Nature , vol.347 , pp. 685-689
    • Rees, D.J.G.1    Ades, S.E.2    Singer, S.J.3    Hynes, R.O.4
  • 31
    • 0029062869 scopus 로고
    • Interaction of the 47 kDa talin fragment and the 32 kDa vinculin fragment with acidic phospholipids: A computer analysis
    • Tempel, M., Goldmann, W. H., Isenberg, H. & Sackmann, E. (1995) Interaction of the 47 kDa talin fragment and the 32 kDa vinculin fragment with acidic phospholipids: a computer analysis, Biophys. J. 69, 228-241.
    • (1995) Biophys. J. , vol.69 , pp. 228-241
    • Tempel, M.1    Goldmann, W.H.2    Isenberg, H.3    Sackmann, E.4
  • 33
    • 0018962392 scopus 로고
    • Structural comparison of several actin-binding macromolecules
    • Tyler, J., Anderson, J. M. & Branton, D. (1980) Structural comparison of several actin-binding macromolecules, J. Cell Biol. 85, 489-495.
    • (1980) J. Cell Biol. , vol.85 , pp. 489-495
    • Tyler, J.1    Anderson, J.M.2    Branton, D.3
  • 34
    • 0018099901 scopus 로고
    • Self-association of human spectrin
    • Ungewickell, E. & Gratzer, W. (1978) Self-association of human spectrin, Eur. J. Biochem. 88, 379-385.
    • (1978) Eur. J. Biochem. , vol.88 , pp. 379-385
    • Ungewickell, E.1    Gratzer, W.2
  • 35
    • 0014301425 scopus 로고
    • Regulation of glutamine synthetase. XII. Electron microscopy of the enzyme from Escherichia coli
    • Valentine, R. C., Shapiro, B. M. & Stadtman, E. R. (1968) Regulation of glutamine synthetase. XII. Electron microscopy of the enzyme from Escherichia coli, Biochemistry 7, 2143-2152.
    • (1968) Biochemistry , vol.7 , pp. 2143-2152
    • Valentine, R.C.1    Shapiro, B.M.2    Stadtman, E.R.3
  • 36
    • 0343058961 scopus 로고    scopus 로고
    • The ultrastructure of chicken gizzard vinculin as visualized by high-resolution electron microscopy
    • Winkler, J., Lünsdorf, H. & Jockusch, B. M. (1996) The ultrastructure of chicken gizzard vinculin as visualized by high-resolution electron microscopy, J. Struct. Biol. 116, 270-277.
    • (1996) J. Struct. Biol. , vol.116 , pp. 270-277
    • Winkler, J.1    Lünsdorf, H.2    Jockusch, B.M.3
  • 37
    • 8044224714 scopus 로고
    • Electron micrographs of protein molecules: Interconversion of size, shape and molecular weight made easy
    • Wrighley, N. G. (1988) Electron micrographs of protein molecules: interconversion of size, shape and molecular weight made easy, Proc. R. Microsc. Soc. 23, 299-302.
    • (1988) Proc. R. Microsc. Soc. , vol.23 , pp. 299-302
    • Wrighley, N.G.1


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