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Volumn 16, Issue 12, 2008, Pages 1882-1891

The 3D Structure of Villin as an Unusual F-Actin Crosslinker

Author keywords

CELLBIO; PROTEINS

Indexed keywords

ACTIN; ACTIN BINDING PROTEIN; F ACTIN; GELSOLIN; VILLIN;

EID: 57049099188     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2008.09.015     Document Type: Article
Times cited : (36)

References (62)
  • 3
    • 0018869290 scopus 로고
    • Villin is a major protein of the microvillus cytoskeleton which binds both G and F actin in a calcium-dependent manner
    • Bretscher A., and Weber K. Villin is a major protein of the microvillus cytoskeleton which binds both G and F actin in a calcium-dependent manner. Cell 20 (1980) 839-847
    • (1980) Cell , vol.20 , pp. 839-847
    • Bretscher, A.1    Weber, K.2
  • 4
    • 0023139873 scopus 로고
    • Tropomyosin distinguishes between the two actin-binding sites of villin and affects actin-binding properties of other brush border proteins
    • Burgess D.R., Broschat K.O., and Hayden J.M. Tropomyosin distinguishes between the two actin-binding sites of villin and affects actin-binding properties of other brush border proteins. J. Cell Biol. 104 (1987) 29-40
    • (1987) J. Cell Biol. , vol.104 , pp. 29-40
    • Burgess, D.R.1    Broschat, K.O.2    Hayden, J.M.3
  • 5
    • 0030829385 scopus 로고    scopus 로고
    • The crystal structure of plasma gelsolin: implications for actin severing, capping, and nucleation
    • Burtnick L.D., Koepf E.K., Grimes J., Jones E.Y., Stuart D.I., McLaughlin P.J., and Robinson R.C. The crystal structure of plasma gelsolin: implications for actin severing, capping, and nucleation. Cell 90 (1997) 661-670
    • (1997) Cell , vol.90 , pp. 661-670
    • Burtnick, L.D.1    Koepf, E.K.2    Grimes, J.3    Jones, E.Y.4    Stuart, D.I.5    McLaughlin, P.J.6    Robinson, R.C.7
  • 6
    • 3543012019 scopus 로고    scopus 로고
    • Structure of the N-terminal half of gelsolin bound to actin: roles in severing, apoptosis and FAF
    • Burtnick L.D., Urosev D., Irobi E., Narayan K., and Robinson R.C. Structure of the N-terminal half of gelsolin bound to actin: roles in severing, apoptosis and FAF. EMBO J. 23 (2004) 2713-2722
    • (2004) EMBO J. , vol.23 , pp. 2713-2722
    • Burtnick, L.D.1    Urosev, D.2    Irobi, E.3    Narayan, K.4    Robinson, R.C.5
  • 7
    • 0344120716 scopus 로고    scopus 로고
    • Low-resolution structure refinement in electron microscopy
    • Chen J.Z., Furst J., Chapman M.S., and Grigorieff N. Low-resolution structure refinement in electron microscopy. J. Struct. Biol. 144 (2003) 144-151
    • (2003) J. Struct. Biol. , vol.144 , pp. 144-151
    • Chen, J.Z.1    Furst, J.2    Chapman, M.S.3    Grigorieff, N.4
  • 8
    • 0036923313 scopus 로고    scopus 로고
    • The calcium activation of gelsolin: insights from the 3 Å structure of the G4-G6/actin complex
    • Choe H., Burtnick L.D., Mejillano M., Yin H.L., Robinson R.C., and Choe S. The calcium activation of gelsolin: insights from the 3 Å structure of the G4-G6/actin complex. J. Mol. Biol. 324 (2002) 691-702
    • (2002) J. Mol. Biol. , vol.324 , pp. 691-702
    • Choe, H.1    Burtnick, L.D.2    Mejillano, M.3    Yin, H.L.4    Robinson, R.C.5    Choe, S.6
  • 9
    • 33748264168 scopus 로고    scopus 로고
    • Actin-binding proteins sensitively mediate F-actin bundle stiffness
    • Claessens M.M., Bathe M., Frey E., and Bausch A.R. Actin-binding proteins sensitively mediate F-actin bundle stiffness. Nat. Mater. 5 (2006) 748-753
    • (2006) Nat. Mater. , vol.5 , pp. 748-753
    • Claessens, M.M.1    Bathe, M.2    Frey, E.3    Bausch, A.R.4
  • 11
    • 0017378495 scopus 로고
    • Structure of actin-containing filaments from two types of non-muscle cells
    • DeRosier D., Mandelkow E., and Silliman A. Structure of actin-containing filaments from two types of non-muscle cells. J. Mol. Biol. 113 (1977) 679-695
    • (1977) J. Mol. Biol. , vol.113 , pp. 679-695
    • DeRosier, D.1    Mandelkow, E.2    Silliman, A.3
  • 12
    • 0029843044 scopus 로고    scopus 로고
    • Cysteine scanning mutagenesis at 40 of 76 positions in villin headpiece maps the F-actin binding site and structural features of the domain
    • Doering D.S., and Matsudaira P. Cysteine scanning mutagenesis at 40 of 76 positions in villin headpiece maps the F-actin binding site and structural features of the domain. Biochemistry 35 (1996) 12677-12685
    • (1996) Biochemistry , vol.35 , pp. 12677-12685
    • Doering, D.S.1    Matsudaira, P.2
  • 13
    • 0020477574 scopus 로고
    • F-actin is a helix with a random variable twist
    • Egelman E.H., Francis N., and DeRosier D.J. F-actin is a helix with a random variable twist. Nature 298 (1982) 131-135
    • (1982) Nature , vol.298 , pp. 131-135
    • Egelman, E.H.1    Francis, N.2    DeRosier, D.J.3
  • 14
    • 0024410166 scopus 로고
    • Differential localization of villin and fimbrin during development of the mouse visceral endoderm and intestinal epithelium
    • Ezzell R.M., Chafel M.M., and Matsudaira P.T. Differential localization of villin and fimbrin during development of the mouse visceral endoderm and intestinal epithelium. Development 106 (1989) 407-419
    • (1989) Development , vol.106 , pp. 407-419
    • Ezzell, R.M.1    Chafel, M.M.2    Matsudaira, P.T.3
  • 16
    • 1942423619 scopus 로고    scopus 로고
    • MMTSB Tool Set: enhanced sampling and multiscale modeling methods for applications in structural biology
    • Feig M., Karanicolas J., and Brooks III C.L. MMTSB Tool Set: enhanced sampling and multiscale modeling methods for applications in structural biology. J. Mol. Graph. Model. 22 (2004) 377-395
    • (2004) J. Mol. Graph. Model. , vol.22 , pp. 377-395
    • Feig, M.1    Karanicolas, J.2    Brooks III, C.L.3
  • 18
    • 0026554080 scopus 로고
    • In vivo analysis of functional domains from villin and gelsolin
    • Finidori J., Friederich E., Kwiatkowski D.J., and Louvard D. In vivo analysis of functional domains from villin and gelsolin. J. Cell Biol. 116 (1992) 1145-1155
    • (1992) J. Cell Biol. , vol.116 , pp. 1145-1155
    • Finidori, J.1    Friederich, E.2    Kwiatkowski, D.J.3    Louvard, D.4
  • 19
    • 1542349982 scopus 로고    scopus 로고
    • The NMR structure of dematin headpiece reveals a dynamic loop that is conformationally altered upon phosphorylation at a distal site
    • Frank B.S., Vardar D., Chishti A.H., and McKnight C.J. The NMR structure of dematin headpiece reveals a dynamic loop that is conformationally altered upon phosphorylation at a distal site. J. Biol. Chem. 279 (2004) 7909-7916
    • (2004) J. Biol. Chem. , vol.279 , pp. 7909-7916
    • Frank, B.S.1    Vardar, D.2    Chishti, A.H.3    McKnight, C.J.4
  • 20
    • 0033578936 scopus 로고    scopus 로고
    • Villin function in the organization of the actin cytoskeleton. Correlation of in vivo effects to its biochemical activities in vitro
    • Friederich E., Vancompernolle K., Louvard D., and Vandekerckhove J. Villin function in the organization of the actin cytoskeleton. Correlation of in vivo effects to its biochemical activities in vitro. J. Biol. Chem. 274 (1999) 26751-26760
    • (1999) J. Biol. Chem. , vol.274 , pp. 26751-26760
    • Friederich, E.1    Vancompernolle, K.2    Louvard, D.3    Vandekerckhove, J.4
  • 21
    • 33646182429 scopus 로고    scopus 로고
    • The CH-domain of calponin does not determine the modes of calponin binding to F-actin
    • Galkin V.E., Orlova A., Fattoum A., Walsh M.P., and Egelman E.H. The CH-domain of calponin does not determine the modes of calponin binding to F-actin. J. Mol. Biol. 359 (2006) 478-485
    • (2006) J. Mol. Biol. , vol.359 , pp. 478-485
    • Galkin, V.E.1    Orlova, A.2    Fattoum, A.3    Walsh, M.P.4    Egelman, E.H.5
  • 23
    • 0019088749 scopus 로고
    • Calcium control of the intestinal microvillus cytoskeleton: its implications for the regulation of microfilament organizations
    • Glenney Jr. J.R., Bretscher A., and Weber K. Calcium control of the intestinal microvillus cytoskeleton: its implications for the regulation of microfilament organizations. Proc. Natl. Acad. Sci. USA 77 (1980) 6458-6462
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 6458-6462
    • Glenney Jr., J.R.1    Bretscher, A.2    Weber, K.3
  • 24
    • 0019821604 scopus 로고
    • Demonstration of at least two different actin-binding sites in villin, a calcium-regulated modulator of F-actin organization
    • Glenney Jr. J.R., Geisler N., Kaulfus P., and Weber K. Demonstration of at least two different actin-binding sites in villin, a calcium-regulated modulator of F-actin organization. J. Biol. Chem. 256 (1981) 8156-8161
    • (1981) J. Biol. Chem. , vol.256 , pp. 8156-8161
    • Glenney Jr., J.R.1    Geisler, N.2    Kaulfus, P.3    Weber, K.4
  • 25
    • 0020663602 scopus 로고
    • Demonstration of three distinct calcium-binding sites in villin, a modulator of actin assembly
    • Hesterberg L.K., and Weber K. Demonstration of three distinct calcium-binding sites in villin, a modulator of actin assembly. J. Biol. Chem. 258 (1983) 365-369
    • (1983) J. Biol. Chem. , vol.258 , pp. 365-369
    • Hesterberg, L.K.1    Weber, K.2
  • 26
    • 0020685135 scopus 로고
    • Ligand-induced conformational changes in villin, a calcium-controlled actin-modulating protein
    • Hesterberg L.K., and Weber K. Ligand-induced conformational changes in villin, a calcium-controlled actin-modulating protein. J. Biol. Chem. 258 (1983) 359-364
    • (1983) J. Biol. Chem. , vol.258 , pp. 359-364
    • Hesterberg, L.K.1    Weber, K.2
  • 27
    • 0026170664 scopus 로고
    • Improved transfer of two-dimensional crystals from the air/water interface to specimen support grids for high-resolution analysis by electron microscopy
    • Kubalek E.W., Kornberg R.D., and Darst S.A. Improved transfer of two-dimensional crystals from the air/water interface to specimen support grids for high-resolution analysis by electron microscopy. Ultramicroscopy 35 (1991) 295-304
    • (1991) Ultramicroscopy , vol.35 , pp. 295-304
    • Kubalek, E.W.1    Kornberg, R.D.2    Darst, S.A.3
  • 28
    • 2942530493 scopus 로고    scopus 로고
    • Identification of a functional switch for actin severing by cytoskeletal proteins
    • Kumar N., and Khurana S. Identification of a functional switch for actin severing by cytoskeletal proteins. J. Biol. Chem. 279 (2004) 24915-24918
    • (2004) J. Biol. Chem. , vol.279 , pp. 24915-24918
    • Kumar, N.1    Khurana, S.2
  • 29
  • 30
    • 0025603713 scopus 로고
    • Localization of a new α-actinin binding site in the COOH-terminal part of actin sequence
    • Lebart M.C., Mejean C., Boyer M., Roustan C., and Benyamin Y. Localization of a new α-actinin binding site in the COOH-terminal part of actin sequence. Biochem. Biophys. Res. Commun. 173 (1990) 120-126
    • (1990) Biochem. Biophys. Res. Commun. , vol.173 , pp. 120-126
    • Lebart, M.C.1    Mejean, C.2    Boyer, M.3    Roustan, C.4    Benyamin, Y.5
  • 31
    • 0027416724 scopus 로고
    • Further characterization of the α-actinin-actin interface and comparison with filamin-binding sites on actin
    • Lebart M.C., Mejean C., Roustan C., and Benyamin Y. Further characterization of the α-actinin-actin interface and comparison with filamin-binding sites on actin. J. Biol. Chem. 268 (1993) 5642-5648
    • (1993) J. Biol. Chem. , vol.268 , pp. 5642-5648
    • Lebart, M.C.1    Mejean, C.2    Roustan, C.3    Benyamin, Y.4
  • 32
    • 0033377664 scopus 로고    scopus 로고
    • EMAN: semiautomated software for high-resolution single-particle reconstructions
    • Ludtke S.J., Baldwin P.R., and Chiu W. EMAN: semiautomated software for high-resolution single-particle reconstructions. J. Struct. Biol. 128 (1999) 82-97
    • (1999) J. Struct. Biol. , vol.128 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chiu, W.3
  • 33
    • 0028158904 scopus 로고
    • Solution structure of villin 14T, a domain conserved among actin-severing proteins
    • Markus M.A., Nakayama T., Matsudaira P., and Wagner G. Solution structure of villin 14T, a domain conserved among actin-severing proteins. Protein Sci. 3 (1994) 70-81
    • (1994) Protein Sci. , vol.3 , pp. 70-81
    • Markus, M.A.1    Nakayama, T.2    Matsudaira, P.3    Wagner, G.4
  • 34
    • 0030954481 scopus 로고    scopus 로고
    • Refined structure of villin 14T and a detailed comparison with other actin-severing domains
    • Markus M.A., Matsudaira P., and Wagner G. Refined structure of villin 14T and a detailed comparison with other actin-severing domains. Protein Sci. 6 (1997) 1197-1209
    • (1997) Protein Sci. , vol.6 , pp. 1197-1209
    • Markus, M.A.1    Matsudaira, P.2    Wagner, G.3
  • 35
    • 0018578513 scopus 로고
    • Identification and organization of the components in the isolated microvillus cytoskeleton
    • Matsudaira P.T., and Burgess D.R. Identification and organization of the components in the isolated microvillus cytoskeleton. J. Cell Biol. 83 (1979) 667-673
    • (1979) J. Cell Biol. , vol.83 , pp. 667-673
    • Matsudaira, P.T.1    Burgess, D.R.2
  • 36
    • 0020655456 scopus 로고
    • Role of fimbrin and villin in determining the interfilament distances of actin bundles
    • Matsudaira P., Mandelkow E., Renner W., Hesterberg L.K., and Weber K. Role of fimbrin and villin in determining the interfilament distances of actin bundles. Nature 301 (1983) 209-214
    • (1983) Nature , vol.301 , pp. 209-214
    • Matsudaira, P.1    Mandelkow, E.2    Renner, W.3    Hesterberg, L.K.4    Weber, K.5
  • 37
    • 0028176006 scopus 로고
    • Determination of the α-actinin-binding site on actin filaments by cryoelectron microscopy and image analysis
    • McGough A., Way M., and DeRosier D. Determination of the α-actinin-binding site on actin filaments by cryoelectron microscopy and image analysis. J. Cell Biol. 126 (1994) 433-443
    • (1994) J. Cell Biol. , vol.126 , pp. 433-443
    • McGough, A.1    Way, M.2    DeRosier, D.3
  • 38
    • 0031879577 scopus 로고    scopus 로고
    • Determination of the gelsolin binding site on F-actin: implications for severing and capping
    • McGough A., Chiu W., and Way M. Determination of the gelsolin binding site on F-actin: implications for severing and capping. Biophys. J. 74 (1998) 764-772
    • (1998) Biophys. J. , vol.74 , pp. 764-772
    • McGough, A.1    Chiu, W.2    Way, M.3
  • 39
    • 0031058410 scopus 로고    scopus 로고
    • NMR structure of the 35-residue villin headpiece subdomain
    • McKnight C.J., Matsudaira P.T., and Kim P.S. NMR structure of the 35-residue villin headpiece subdomain. Nat. Struct. Biol. 4 (1997) 180-184
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 180-184
    • McKnight, C.J.1    Matsudaira, P.T.2    Kim, P.S.3
  • 40
    • 0027251071 scopus 로고
    • Structure of gelsolin segment 1-actin complex and the mechanism of filament severing
    • McLaughlin P.J., Gooch J.T., Mannherz H.G., and Weeds A.G. Structure of gelsolin segment 1-actin complex and the mechanism of filament severing. Nature 364 (1993) 685-692
    • (1993) Nature , vol.364 , pp. 685-692
    • McLaughlin, P.J.1    Gooch, J.T.2    Mannherz, H.G.3    Weeds, A.G.4
  • 41
    • 24644519821 scopus 로고    scopus 로고
    • High-resolution crystal structures of villin headpiece and mutants with reduced F-actin binding activity
    • Meng J., Vardar D., Wang Y., Guo H.C., Head J.F., and McKnight C.J. High-resolution crystal structures of villin headpiece and mutants with reduced F-actin binding activity. Biochemistry 44 (2005) 11963-11973
    • (2005) Biochemistry , vol.44 , pp. 11963-11973
    • Meng, J.1    Vardar, D.2    Wang, Y.3    Guo, H.C.4    Head, J.F.5    McKnight, C.J.6
  • 42
    • 0023216026 scopus 로고
    • Further characterization of a conserved actin-binding 27-kDa fragment of actinogelin and α-actinins and mapping of their binding sites on the actin molecule by chemical cross-linking
    • Mimura N., and Asano A. Further characterization of a conserved actin-binding 27-kDa fragment of actinogelin and α-actinins and mapping of their binding sites on the actin molecule by chemical cross-linking. J. Biol. Chem. 262 (1987) 4717-4723
    • (1987) J. Biol. Chem. , vol.262 , pp. 4717-4723
    • Mimura, N.1    Asano, A.2
  • 43
    • 0020021878 scopus 로고
    • Purification of muscle actin
    • Pardee J.D., and Spudich J.A. Purification of muscle actin. Methods Enzymol. 85 Pt B (1982) 164-181
    • (1982) Methods Enzymol. , vol.85 , Issue.PART B , pp. 164-181
    • Pardee, J.D.1    Spudich, J.A.2
  • 45
    • 0031984186 scopus 로고    scopus 로고
    • Targeted disruption of the mouse villin gene does not impair the morphogenesis of microvilli
    • Pinson K.I., Dunbar L., Samuelson L., and Gumucio D.L. Targeted disruption of the mouse villin gene does not impair the morphogenesis of microvilli. Dev. Dyn. 211 (1998) 109-121
    • (1998) Dev. Dyn. , vol.211 , pp. 109-121
    • Pinson, K.I.1    Dunbar, L.2    Samuelson, L.3    Gumucio, D.L.4
  • 46
    • 0028058169 scopus 로고
    • Characterisation of the F-actin binding domains of villin: classification of F-actin binding proteins into two groups according to their binding sites on actin
    • Pope B., Way M., Matsudaira P.T., and Weeds A. Characterisation of the F-actin binding domains of villin: classification of F-actin binding proteins into two groups according to their binding sites on actin. FEBS Lett. 338 (1994) 58-62
    • (1994) FEBS Lett. , vol.338 , pp. 58-62
    • Pope, B.1    Way, M.2    Matsudaira, P.T.3    Weeds, A.4
  • 48
    • 0019987933 scopus 로고
    • The correlation averaging of a regularly arranged bacterial cell envelope protein
    • Saxton W.O., and Baumeister W. The correlation averaging of a regularly arranged bacterial cell envelope protein. J. Microsc. 127 (1982) 127-138
    • (1982) J. Microsc. , vol.127 , pp. 127-138
    • Saxton, W.O.1    Baumeister, W.2
  • 49
    • 0042622380 scopus 로고    scopus 로고
    • SWISS-MODEL: an automated protein homology-modeling server
    • Schwede T., Kopp J., Guex N., and Peitsch M.C. SWISS-MODEL: an automated protein homology-modeling server. Nucleic Acids Res. 31 (2003) 3381-3385
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3381-3385
    • Schwede, T.1    Kopp, J.2    Guex, N.3    Peitsch, M.C.4
  • 50
    • 34250849051 scopus 로고    scopus 로고
    • The isolated sixth gelsolin repeat and headpiece domain of villin bundle F-actin in the presence of calcium and are linked by a 40-residue unstructured sequence
    • Smirnov S.L., Isern N.G., Jiang Z.G., Hoyt D.W., and McKnight C.J. The isolated sixth gelsolin repeat and headpiece domain of villin bundle F-actin in the presence of calcium and are linked by a 40-residue unstructured sequence. Biochemistry 46 (2007) 7488-7496
    • (2007) Biochemistry , vol.46 , pp. 7488-7496
    • Smirnov, S.L.1    Isern, N.G.2    Jiang, Z.G.3    Hoyt, D.W.4    McKnight, C.J.5
  • 51
    • 0032509093 scopus 로고    scopus 로고
    • How to analyze electron micrographs of rafts of actin filaments crosslinked by actin-binding proteins
    • Sukow C., and DeRosier D. How to analyze electron micrographs of rafts of actin filaments crosslinked by actin-binding proteins. J. Mol. Biol. 284 (1998) 1039-1050
    • (1998) J. Mol. Biol. , vol.284 , pp. 1039-1050
    • Sukow, C.1    DeRosier, D.2
  • 52
    • 0027992919 scopus 로고
    • Formation of two-dimensional complexes of F-actin and crosslinking proteins on lipid monolayers: demonstration of unipolar α-actinin-F-actin crosslinking
    • Taylor K.A., and Taylor D.W. Formation of two-dimensional complexes of F-actin and crosslinking proteins on lipid monolayers: demonstration of unipolar α-actinin-F-actin crosslinking. Biophys. J. 67 (1994) 1976-1983
    • (1994) Biophys. J. , vol.67 , pp. 1976-1983
    • Taylor, K.A.1    Taylor, D.W.2
  • 53
    • 0015131317 scopus 로고
    • Actin in the brush-border of epithelial cells of the chicken intestine
    • Tilney L.G., and Mooseker M. Actin in the brush-border of epithelial cells of the chicken intestine. Proc. Natl. Acad. Sci. USA 68 (1971) 2611-2615
    • (1971) Proc. Natl. Acad. Sci. USA , vol.68 , pp. 2611-2615
    • Tilney, L.G.1    Mooseker, M.2
  • 54
    • 0019307051 scopus 로고
    • The organization of actin filaments in the stereocilia of cochlear hair cells
    • Tilney L.G., Derosier D.J., and Mulroy M.J. The organization of actin filaments in the stereocilia of cochlear hair cells. J. Cell Biol. 86 (1980) 244-259
    • (1980) J. Cell Biol. , vol.86 , pp. 244-259
    • Tilney, L.G.1    Derosier, D.J.2    Mulroy, M.J.3
  • 55
    • 0020570679 scopus 로고
    • Actin filaments, stereocilia, and hair cells of the bird cochlea. II. Packing of actin filaments in the stereocilia and in the cuticular plate and what happens to the organization when the stereocilia are bent
    • Tilney L.G., Egelman E.H., DeRosier D.J., and Saunder J.C. Actin filaments, stereocilia, and hair cells of the bird cochlea. II. Packing of actin filaments in the stereocilia and in the cuticular plate and what happens to the organization when the stereocilia are bent. J. Cell Biol. 96 (1983) 822-834
    • (1983) J. Cell Biol. , vol.96 , pp. 822-834
    • Tilney, L.G.1    Egelman, E.H.2    DeRosier, D.J.3    Saunder, J.C.4
  • 56
    • 0033579417 scopus 로고    scopus 로고
    • NMR structure of an F-actin-binding "headpiece" motif from villin
    • Vardar D., Buckley D.A., Frank B.S., and McKnight C.J. NMR structure of an F-actin-binding "headpiece" motif from villin. J. Mol. Biol. 294 (1999) 1299-1310
    • (1999) J. Mol. Biol. , vol.294 , pp. 1299-1310
    • Vardar, D.1    Buckley, D.A.2    Frank, B.S.3    McKnight, C.J.4
  • 58
    • 0035947761 scopus 로고    scopus 로고
    • An atomic model of actin filaments cross-linked by fimbrin and its implications for bundle assembly and function
    • Volkmann N., DeRosier D., Matsudaira P., and Hanein D. An atomic model of actin filaments cross-linked by fimbrin and its implications for bundle assembly and function. J. Cell Biol. 153 (2001) 947-956
    • (2001) J. Cell Biol. , vol.153 , pp. 947-956
    • Volkmann, N.1    DeRosier, D.2    Matsudaira, P.3    Hanein, D.4
  • 59
    • 0026495427 scopus 로고
    • Evidence for functional homology in the F-actin binding domains of gelsolin and α-actinin: implications for the requirements of severing and capping
    • Way M., Pope B., and Weeds A.G. Evidence for functional homology in the F-actin binding domains of gelsolin and α-actinin: implications for the requirements of severing and capping. J. Cell Biol. 119 (1992) 835-842
    • (1992) J. Cell Biol. , vol.119 , pp. 835-842
    • Way, M.1    Pope, B.2    Weeds, A.G.3
  • 60
    • 0033166855 scopus 로고    scopus 로고
    • Multivariate statistical analysis of three-dimensional cross-bridge motifs in insect flight muscle
    • Winkler H., and Taylor K.A. Multivariate statistical analysis of three-dimensional cross-bridge motifs in insect flight muscle. Ultramicroscopy 77 (1999) 141-152
    • (1999) Ultramicroscopy , vol.77 , pp. 141-152
    • Winkler, H.1    Taylor, K.A.2
  • 61
    • 29244462551 scopus 로고    scopus 로고
    • Accurate marker-free alignment with simultaneous geometry determination and reconstruction of tilt series in electron tomography
    • Winkler H., and Taylor K.A. Accurate marker-free alignment with simultaneous geometry determination and reconstruction of tilt series in electron tomography. Ultramicroscopy 106 (2006) 240-254
    • (2006) Ultramicroscopy , vol.106 , pp. 240-254
    • Winkler, H.1    Taylor, K.A.2
  • 62
    • 0018667209 scopus 로고
    • Control of cytoplasmic actin gel-sol transformation by gelsolin, a calcium-dependent regulatory protein
    • Yin H.L., and Stossel T.P. Control of cytoplasmic actin gel-sol transformation by gelsolin, a calcium-dependent regulatory protein. Nature 281 (1979) 583-586
    • (1979) Nature , vol.281 , pp. 583-586
    • Yin, H.L.1    Stossel, T.P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.