메뉴 건너뛰기




Volumn 464, Issue C, 2009, Pages 31-53

Chapter 3 Construction of Cell-Sized Liposomes Encapsulating Actin and Actin-Cross-linking Proteins

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA ACTININ; CYTOSKELETON PROTEIN; F ACTIN; FASCIN; FILAMIN; G ACTIN; LIPOSOME; MEROMYOSIN; MOLECULAR MOTOR; MYOSIN I; OIL; PHOSPHOLIPID;

EID: 71549120126     PISSN: 00766879     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0076-6879(09)64003-9     Document Type: Review
Times cited : (19)

References (69)
  • 1
    • 0017114442 scopus 로고
    • A quantitative description of the extension and retraction of surface protrusions in spreading 3T3 mouse fibroblasts
    • Albrecht-Buehler G., and Lancaster R.M. A quantitative description of the extension and retraction of surface protrusions in spreading 3T3 mouse fibroblasts. J. Cell Biol. 71 (1976) 370-382
    • (1976) J. Cell Biol. , vol.71 , pp. 370-382
    • Albrecht-Buehler, G.1    Lancaster, R.M.2
  • 3
    • 0029444559 scopus 로고
    • Surrogate cells or Trojan horses. The discovery of liposomes
    • Bangham A.D. Surrogate cells or Trojan horses. The discovery of liposomes. BioEssays 17 (1995) 1081-1088
    • (1995) BioEssays , vol.17 , pp. 1081-1088
    • Bangham, A.D.1
  • 4
    • 85012373035 scopus 로고
    • Diffusion of univalent ions across the lamellae of swollen phospholipids
    • Bangham A.D., Standish M.M., and Watkins J.C. Diffusion of univalent ions across the lamellae of swollen phospholipids. J. Mol. Biol. 13 (1965) 238-252
    • (1965) J. Mol. Biol. , vol.13 , pp. 238-252
    • Bangham, A.D.1    Standish, M.M.2    Watkins, J.C.3
  • 5
    • 2942540905 scopus 로고
    • A new cell model-actin networks encaged by giant vesicles
    • Lipowsky R., Richter D., and Kremer K. (Eds), Springer, Heidelberg Springer Proceedings in Physics
    • Bärmann M., Käs J., Kurzmeiser H., and Sackmann E. A new cell model-actin networks encaged by giant vesicles. In: Lipowsky R., Richter D., and Kremer K. (Eds). The Structure and Conformation of Amphiphilic Membranes Vol. 66 (1992), Springer, Heidelberg 137-143 Springer Proceedings in Physics
    • (1992) The Structure and Conformation of Amphiphilic Membranes , vol.66 , pp. 137-143
    • Bärmann, M.1    Käs, J.2    Kurzmeiser, H.3    Sackmann, E.4
  • 6
    • 0025720725 scopus 로고
    • Microfilament structure and function in the cortical cytoskeleton
    • Bretscher A. Microfilament structure and function in the cortical cytoskeleton. Annu. Rev. Cell Biol. 7 (1991) 337-374
    • (1991) Annu. Rev. Cell Biol. , vol.7 , pp. 337-374
    • Bretscher, A.1
  • 7
    • 0020290629 scopus 로고
    • Stress fibers in cells in situ: Immunofluorescence visualization with antiactin, antimyosin, and anti-α-actinin
    • Byers H.R., and Fujikawa K. Stress fibers in cells in situ: Immunofluorescence visualization with antiactin, antimyosin, and anti-α-actinin. J. Cell Biol. 93 (1982) 804-811
    • (1982) J. Cell Biol. , vol.93 , pp. 804-811
    • Byers, H.R.1    Fujikawa, K.2
  • 8
    • 0028269631 scopus 로고
    • Drosophila singed, a fascin homolog, is required for actin bundle formation during oogenesis and bristle extension
    • Cant K., Knowles B.A., Mooseker M.S., and Cooley L. Drosophila singed, a fascin homolog, is required for actin bundle formation during oogenesis and bristle extension. J. Cell Biol. 125 (1994) 369-380
    • (1994) J. Cell Biol. , vol.125 , pp. 369-380
    • Cant, K.1    Knowles, B.A.2    Mooseker, M.S.3    Cooley, L.4
  • 9
    • 33645778010 scopus 로고    scopus 로고
    • Microstructure and viscoelasticity of confined semiflexible polymer networks
    • Claessens M.M.A.E., Tharmann R., Kroy K., and Bausch A.R. Microstructure and viscoelasticity of confined semiflexible polymer networks. Nat. Phys. 2 (2006) 186-189
    • (2006) Nat. Phys. , vol.2 , pp. 186-189
    • Claessens, M.M.A.E.1    Tharmann, R.2    Kroy, K.3    Bausch, A.R.4
  • 10
    • 0025984501 scopus 로고
    • Myosin I: A new insight into the mechanism and cellular significance of actin-based motility
    • Collins K., Sellers J., and Matsudaira P. Myosin I: A new insight into the mechanism and cellular significance of actin-based motility. Adv. Biophys. 27 (1991) 221-226
    • (1991) Adv. Biophys. , vol.27 , pp. 221-226
    • Collins, K.1    Sellers, J.2    Matsudaira, P.3
  • 13
    • 0013789624 scopus 로고
    • Alpha-actinin, a new structural protein from striated muscle. I. Preparation and action on actomyosin-ATP interaction
    • Ebashi S., and Ebashi F. Alpha-actinin, a new structural protein from striated muscle. I. Preparation and action on actomyosin-ATP interaction. J. Biochem. 58 (1965) 7-12
    • (1965) J. Biochem. , vol.58 , pp. 7-12
    • Ebashi, S.1    Ebashi, F.2
  • 14
    • 0028799146 scopus 로고
    • Fascins, a family of actin bundling proteins
    • Edwards R.A., and Bryan J. Fascins, a family of actin bundling proteins. Cell Motil. Cytoskel. 32 (1995) 1-9
    • (1995) Cell Motil. Cytoskel. , vol.32 , pp. 1-9
    • Edwards, R.A.1    Bryan, J.2
  • 15
    • 0028902746 scopus 로고
    • Cloning and expression of a murine fascin homolog from mouse brain
    • Edwards R.A., Herrera-Sosa H., Otto J., and Bryan J. Cloning and expression of a murine fascin homolog from mouse brain. J. Biol. Chem. 270 (1995) 10764-10770
    • (1995) J. Biol. Chem. , vol.270 , pp. 10764-10770
    • Edwards, R.A.1    Herrera-Sosa, H.2    Otto, J.3    Bryan, J.4
  • 16
    • 35548972065 scopus 로고    scopus 로고
    • Formation of giant lipid vesiclelike compartments from a planar lipid membrane by a pulsed jet flow
    • Funakoshi K., Suzuki H., and Takeuchi S. Formation of giant lipid vesiclelike compartments from a planar lipid membrane by a pulsed jet flow. J. Am. Chem. Soc. 129 (2007) 12608-12609
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 12608-12609
    • Funakoshi, K.1    Suzuki, H.2    Takeuchi, S.3
  • 17
    • 0031372605 scopus 로고    scopus 로고
    • Mechanics of microtubule-based membrane extension
    • Fygenson D.K., Marko J.F., and Libchaber A. Mechanics of microtubule-based membrane extension. Phys. Rev. Lett. 79 (1997) 4497-4500
    • (1997) Phys. Rev. Lett. , vol.79 , pp. 4497-4500
    • Fygenson, D.K.1    Marko, J.F.2    Libchaber, A.3
  • 19
    • 0028178829 scopus 로고
    • α-Actinin from chicken gizzard: At low temperature, the onset of actin-gelling activity correlates with actin bundling
    • Grazi E., Trombetta G., Magri E., Cuneo P., and Schwienbacher C. α-Actinin from chicken gizzard: At low temperature, the onset of actin-gelling activity correlates with actin bundling. Biochem. J. 298 (1994) 129-133
    • (1994) Biochem. J. , vol.298 , pp. 129-133
    • Grazi, E.1    Trombetta, G.2    Magri, E.3    Cuneo, P.4    Schwienbacher, C.5
  • 20
    • 11744369500 scopus 로고    scopus 로고
    • Shape changes of self-assembled actin bilayer composite membranes
    • Häckl W., Bärmann M., and Sackmann E. Shape changes of self-assembled actin bilayer composite membranes. Phys. Rev. Lett. 80 (1998) 1786-1789
    • (1998) Phys. Rev. Lett. , vol.80 , pp. 1786-1789
    • Häckl, W.1    Bärmann, M.2    Sackmann, E.3
  • 21
    • 57449084385 scopus 로고    scopus 로고
    • Construction of asymmetric cell-sized lipid vesicles from lipid-coated water-in-oil microdroplets
    • Hamada T., Miura Y., Komatsu Y., Kishimoto Y., Vestergaard M., and Takagi M. Construction of asymmetric cell-sized lipid vesicles from lipid-coated water-in-oil microdroplets. J. Phys. Chem. B 112 (2008) 14678-14681
    • (2008) J. Phys. Chem. B , vol.112 , pp. 14678-14681
    • Hamada, T.1    Miura, Y.2    Komatsu, Y.3    Kishimoto, Y.4    Vestergaard, M.5    Takagi, M.6
  • 23
    • 34547649522 scopus 로고    scopus 로고
    • Structural transition of actin filament in a cell-sized water droplet with a phospholipid membrane
    • Art. no. 104903
    • Hase M., and Yoshikawa K. Structural transition of actin filament in a cell-sized water droplet with a phospholipid membrane. J. Chem. Phys. 124 (2006) Art. no. 104903
    • (2006) J. Chem. Phys. , vol.124
    • Hase, M.1    Yoshikawa, K.2
  • 24
    • 33846876569 scopus 로고    scopus 로고
    • Manipulation of cell-sized phospholipid-coated microdroplets and their use as biochemical microreactors
    • Hase M., Yamada A., Hamada T., Baigl D., and Yoshikawa K. Manipulation of cell-sized phospholipid-coated microdroplets and their use as biochemical microreactors. Langmuir 23 (2007) 348-352
    • (2007) Langmuir , vol.23 , pp. 348-352
    • Hase, M.1    Yamada, A.2    Hamada, T.3    Baigl, D.4    Yoshikawa, K.5
  • 25
    • 0021063003 scopus 로고
    • Phosphorylation of myosin light chain modulates the in vitro movement of fibrils composed of actin and myosin filaments from skeletal muscle
    • Higashi-Fujime S. Phosphorylation of myosin light chain modulates the in vitro movement of fibrils composed of actin and myosin filaments from skeletal muscle. J. Biochem. 94 (1983) 1539-1545
    • (1983) J. Biochem. , vol.94 , pp. 1539-1545
    • Higashi-Fujime, S.1
  • 26
    • 0025053513 scopus 로고
    • Purification of human smooth muscle filamin and characterization of structural domains and functional sites
    • Hock R.S., Davis G., and Speicher D.W. Purification of human smooth muscle filamin and characterization of structural domains and functional sites. Biochemistry 29 (1990) 9441-9451
    • (1990) Biochemistry , vol.29 , pp. 9441-9451
    • Hock, R.S.1    Davis, G.2    Speicher, D.W.3
  • 27
    • 0033605879 scopus 로고    scopus 로고
    • Morphogenesis of liposomes encapsulating actin depends on the type of actin-crosslinking
    • Honda M., Takiguchi K., Ishikawa S., and Hotani H. Morphogenesis of liposomes encapsulating actin depends on the type of actin-crosslinking. J. Mol. Biol. 287 (1999) 293-300
    • (1999) J. Mol. Biol. , vol.287 , pp. 293-300
    • Honda, M.1    Takiguchi, K.2    Ishikawa, S.3    Hotani, H.4
  • 28
    • 0021755796 scopus 로고
    • Transformation pathways of liposomes
    • Hotani H. Transformation pathways of liposomes. J. Mol. Biol. 178 (1984) 113-120
    • (1984) J. Mol. Biol. , vol.178 , pp. 113-120
    • Hotani, H.1
  • 29
    • 0025204589 scopus 로고
    • Dynamic features of microtubules as visualized by dark-field microscopy
    • Hotani H., and Miyamoto H. Dynamic features of microtubules as visualized by dark-field microscopy. Adv. Biophys. 26 (1990) 135-156
    • (1990) Adv. Biophys. , vol.26 , pp. 135-156
    • Hotani, H.1    Miyamoto, H.2
  • 31
    • 0025292782 scopus 로고
    • Brownian motion of inert tracer macromolecules in polymerized and spontaneously bundled mixtures of actin and filamin
    • Hou L., Luby-Phelps K., and Lanni F.J. Brownian motion of inert tracer macromolecules in polymerized and spontaneously bundled mixtures of actin and filamin. J. Cell Biol. 110 (1990) 1645-1654
    • (1990) J. Cell Biol. , vol.110 , pp. 1645-1654
    • Hou, L.1    Luby-Phelps, K.2    Lanni, F.J.3
  • 32
    • 0024278676 scopus 로고
    • Substructure and higher structure of chicken smooth muscle alpha-actinin molecule
    • Imamura M., Endo T., Kuroda M., Tanaka T., and Masaki T. Substructure and higher structure of chicken smooth muscle alpha-actinin molecule. J. Biol. Chem. 263 (1988) 7800-7805
    • (1988) J. Biol. Chem. , vol.263 , pp. 7800-7805
    • Imamura, M.1    Endo, T.2    Kuroda, M.3    Tanaka, T.4    Masaki, T.5
  • 33
    • 0025871812 scopus 로고
    • Modulation of contraction by gelation/solation in a reconstituted motile model
    • Janson L.W., Kolega J., and Taylor D.L. Modulation of contraction by gelation/solation in a reconstituted motile model. J. Cell Biol. 114 (1991) 1005-1015
    • (1991) J. Cell Biol. , vol.114 , pp. 1005-1015
    • Janson, L.W.1    Kolega, J.2    Taylor, D.L.3
  • 34
    • 0031581885 scopus 로고    scopus 로고
    • Three-dimensional structure of brush border myosin-I at approximately 20 Å resolution by electron microscopy and image analysis
    • Jontes J.D., and Milligan R.A. Three-dimensional structure of brush border myosin-I at approximately 20 Å resolution by electron microscopy and image analysis. J. Mol. Biol. 266 (1997) 331-342
    • (1997) J. Mol. Biol. , vol.266 , pp. 331-342
    • Jontes, J.D.1    Milligan, R.A.2
  • 35
    • 0032545175 scopus 로고    scopus 로고
    • Morphological transformation of liposomes caused by assembly of encapsulated tubulin and determination of shape by microtubule-associated proteins (MAPs)
    • Kaneko T., Itoh T.J., and Hotani H. Morphological transformation of liposomes caused by assembly of encapsulated tubulin and determination of shape by microtubule-associated proteins (MAPs). J. Mol. Biol. 284 (1998) 1671-1681
    • (1998) J. Mol. Biol. , vol.284 , pp. 1671-1681
    • Kaneko, T.1    Itoh, T.J.2    Hotani, H.3
  • 37
    • 18744363662 scopus 로고    scopus 로고
    • Polymorphism of cross-linked actin networks in giant vesicles
    • Art. no. 168103
    • Limozin L., and Sackmann E. Polymorphism of cross-linked actin networks in giant vesicles. Phys. Rev. Lett. 89 (2002) Art. no. 168103
    • (2002) Phys. Rev. Lett. , vol.89
    • Limozin, L.1    Sackmann, E.2
  • 38
    • 0037495920 scopus 로고    scopus 로고
    • On the organization of self-assembled actin networks in giant vesicles
    • Limozin L., Bärmann M., and Sackmann E. On the organization of self-assembled actin networks in giant vesicles. Eur. Phys. J. E 10 (2003) 319-330
    • (2003) Eur. Phys. J. E , vol.10 , pp. 319-330
    • Limozin, L.1    Bärmann, M.2    Sackmann, E.3
  • 39
    • 28844435854 scopus 로고    scopus 로고
    • Microviscoelastic moduli of biomimetic cell envelopes
    • Art. no. 178101
    • Limozin L., Roth A., and Sackmann E. Microviscoelastic moduli of biomimetic cell envelopes. Phys. Rev. Lett. 95 (2005) Art. no. 178101
    • (2005) Phys. Rev. Lett. , vol.95
    • Limozin, L.1    Roth, A.2    Sackmann, E.3
  • 40
    • 0025968124 scopus 로고
    • The conformation of membranes
    • Lipowsky R. The conformation of membranes. Nature 349 (1991) 475-481
    • (1991) Nature , vol.349 , pp. 475-481
    • Lipowsky, R.1
  • 41
    • 55549094081 scopus 로고    scopus 로고
    • Morphogenesis of liposomes caused by polycation-induced actin assembly formation
    • Maemichi H., Shikinaka K., Kakugo A., Furukawa H., Osada Y., and Gong J.P. Morphogenesis of liposomes caused by polycation-induced actin assembly formation. Langmuir 24 (2008) 11975-11981
    • (2008) Langmuir , vol.24 , pp. 11975-11981
    • Maemichi, H.1    Shikinaka, K.2    Kakugo, A.3    Furukawa, H.4    Osada, Y.5    Gong, J.P.6
  • 42
    • 0025339009 scopus 로고
    • Bundling of actin filaments by α-actinin depends on its molecular length
    • Meyer R.K., and Aebi U. Bundling of actin filaments by α-actinin depends on its molecular length. J. Cell Biol. 110 (1990) 2013-2024
    • (1990) J. Cell Biol. , vol.110 , pp. 2013-2024
    • Meyer, R.K.1    Aebi, U.2
  • 43
    • 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
  • 44
    • 0030049170 scopus 로고    scopus 로고
    • Actin-based cell motility and cell locomotion
    • Mitchison T.J., and Cramer L.P. Actin-based cell motility and cell locomotion. Cell 84 (1996) 371-379
    • (1996) Cell , vol.84 , pp. 371-379
    • Mitchison, T.J.1    Cramer, L.P.2
  • 45
    • 0024109183 scopus 로고
    • Cytoskeletal dynamics and nerve growth
    • Mitchison T.J., and Kirschner M. Cytoskeletal dynamics and nerve growth. Neuron 1 (1988) 761-772
    • (1988) Neuron , vol.1 , pp. 761-772
    • Mitchison, T.J.1    Kirschner, M.2
  • 46
    • 0026482154 scopus 로고
    • Morphological changes in liposomes caused by polymerization of encapsulated actin and spontaneous formation of actin bundles
    • Miyata H., and Hotani H. Morphological changes in liposomes caused by polymerization of encapsulated actin and spontaneous formation of actin bundles. Proc. Natl. Acad. Sci. USA 89 (1992) 11547-11551
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 11547-11551
    • Miyata, H.1    Hotani, H.2
  • 50
    • 11144220854 scopus 로고    scopus 로고
    • A vesicle bioreactor as a step toward an artificial cell assembly
    • Noireaux V., and Libchaber A. A vesicle bioreactor as a step toward an artificial cell assembly. Proc. Natl. Acad. Sci. USA 101 (2004) 17669-17674
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 17669-17674
    • Noireaux, V.1    Libchaber, A.2
  • 51
    • 0019260574 scopus 로고
    • Redistribution of actin and fascin in sea urchin eggs after fertilization
    • Otto J.J., Kane R.E., and Bryan J. Redistribution of actin and fascin in sea urchin eggs after fertilization. Cell Motil. 1 (1980) 31-40
    • (1980) Cell Motil. , vol.1 , pp. 31-40
    • Otto, J.J.1    Kane, R.E.2    Bryan, J.3
  • 53
    • 0038061507 scopus 로고    scopus 로고
    • Production of unilamellar vesicles using an inverted emulsion
    • Pautot S., Frisken B.J., and Weitz D.A. Production of unilamellar vesicles using an inverted emulsion. Langmuir 19 (2003) 2870-2879
    • (2003) Langmuir , vol.19 , pp. 2870-2879
    • Pautot, S.1    Frisken, B.J.2    Weitz, D.A.3
  • 57
    • 0011014320 scopus 로고
    • Actin in dividing cells: Contractile ring filaments bind heavy meromyosin
    • Schroeder T.E. Actin in dividing cells: Contractile ring filaments bind heavy meromyosin. Proc. Natl. Acad. Sci. USA 70 (1973) 1688-1692
    • (1973) Proc. Natl. Acad. Sci. USA , vol.70 , pp. 1688-1692
    • Schroeder, T.E.1
  • 58
    • 49649113480 scopus 로고    scopus 로고
    • Double emulsion templated monodisperse phospholipid vesicles
    • Shum H.C., Lee D., Yoon I., Kodger T., and Weitz D.A. Double emulsion templated monodisperse phospholipid vesicles. Langmuir 24 (2008) 7651-7653
    • (2008) Langmuir , vol.24 , pp. 7651-7653
    • Shum, H.C.1    Lee, D.2    Yoon, I.3    Kodger, T.4    Weitz, D.A.5
  • 60
    • 0025793710 scopus 로고
    • Heavy meromyosin induces sliding movements between antiparallel actin filaments
    • Takiguchi K. Heavy meromyosin induces sliding movements between antiparallel actin filaments. J. Biochem. 109 (1991) 520-527
    • (1991) J. Biochem. , vol.109 , pp. 520-527
    • Takiguchi, K.1
  • 61
    • 55549106113 scopus 로고    scopus 로고
    • Entrapping desired amounts of actin filaments and molecular motor proteins in giant liposomes
    • Takiguchi K., Yamada A., Negishi M., Tanaka-Takiguchi Y., and Yoshikawa K. Entrapping desired amounts of actin filaments and molecular motor proteins in giant liposomes. Langmuir 24 (2008) 11323-11326
    • (2008) Langmuir , vol.24 , pp. 11323-11326
    • Takiguchi, K.1    Yamada, A.2    Negishi, M.3    Tanaka-Takiguchi, Y.4    Yoshikawa, K.5
  • 62
    • 3342938506 scopus 로고    scopus 로고
    • The elongation and contraction of actin bundles are induced by double-headed myosins in a motor concentration-dependent manner
    • Tanaka-Takiguchi Y., Kakei T., Tanimura A., Takagi A., Honda M., Hotani H., and Takiguchi K. The elongation and contraction of actin bundles are induced by double-headed myosins in a motor concentration-dependent manner. J. Mol. Biol. 341 (2004) 467-476
    • (2004) J. Mol. Biol. , vol.341 , pp. 467-476
    • Tanaka-Takiguchi, Y.1    Kakei, T.2    Tanimura, A.3    Takagi, A.4    Honda, M.5    Hotani, H.6    Takiguchi, K.7
  • 63
    • 0018654598 scopus 로고
    • Cytoplasmic structure and contractility in amoeboid cells
    • Academic Press, New York
    • Taylor D.L., and Condeelis J.S. Cytoplasmic structure and contractility in amoeboid cells. International Review of Cytology Vol. 56 (1979), Academic Press, New York 57-144
    • (1979) International Review of Cytology , vol.56 , pp. 57-144
    • Taylor, D.L.1    Condeelis, J.S.2
  • 64
    • 0027162413 scopus 로고
    • Affinity of α-actinin for actin determines the structure and mechanical properties of actin filament gels
    • Wachsstock D.H., Schwartz W.H., and Pollard T.D. Affinity of α-actinin for actin determines the structure and mechanical properties of actin filament gels. Biophys. J. 65 (1993) 205-214
    • (1993) Biophys. J. , vol.65 , pp. 205-214
    • Wachsstock, D.H.1    Schwartz, W.H.2    Pollard, T.D.3
  • 65
    • 0028265522 scopus 로고
    • Cross-linker dynamics determine the mechanical properties of actin gels
    • Wachsstock D.H., Schwartz W.H., and Pollard T.D. Cross-linker dynamics determine the mechanical properties of actin gels. Biophys. J. 66 (1994) 801-809
    • (1994) Biophys. J. , vol.66 , pp. 801-809
    • Wachsstock, D.H.1    Schwartz, W.H.2    Pollard, T.D.3
  • 66
    • 0032540368 scopus 로고    scopus 로고
    • Dynamic cross-linking by α-actinin determines the mechanical properties of actin filament networks
    • Xu J., Wirtz D., and Pollard T.D. Dynamic cross-linking by α-actinin determines the mechanical properties of actin filament networks. J. Biol. Chem. 273 (1998) 9570-9576
    • (1998) J. Biol. Chem. , vol.273 , pp. 9570-9576
    • Xu, J.1    Wirtz, D.2    Pollard, T.D.3
  • 67
    • 33846122301 scopus 로고    scopus 로고
    • Spontaneous transfer of phospholipid-coated oil-in-oil and water-in-oil micro-droplets through an oil/water interface
    • Yamada A., Yamanaka Y., Hamada T., Hase M., Yoshikawa K., and Baigl D. Spontaneous transfer of phospholipid-coated oil-in-oil and water-in-oil micro-droplets through an oil/water interface. Langmuir 22 (2006) 9824-9828
    • (2006) Langmuir , vol.22 , pp. 9824-9828
    • Yamada, A.1    Yamanaka, Y.2    Hamada, T.3    Hase, M.4    Yoshikawa, K.5    Baigl, D.6
  • 68
    • 0031694209 scopus 로고    scopus 로고
    • Fascin, an actin-bundling protein, induces membrane protrusions and increases cell motility of epithelial cells
    • Yamashiro S., Yamakita Y., Ono S., and Matsumura F. Fascin, an actin-bundling protein, induces membrane protrusions and increases cell motility of epithelial cells. Mol. Biol. Cell 9 (1998) 993-1006
    • (1998) Mol. Biol. Cell , vol.9 , pp. 993-1006
    • Yamashiro, S.1    Yamakita, Y.2    Ono, S.3    Matsumura, F.4
  • 69
    • 0021827569 scopus 로고
    • Purification and characterization of an F-actin-bundling 55-kilodalton protein from HeLa cells
    • Yamashiro-Matsumura S., and Matsumura F. Purification and characterization of an F-actin-bundling 55-kilodalton protein from HeLa cells. J. Biol. Chem. 260 (1985) 5087-5097
    • (1985) J. Biol. Chem. , vol.260 , pp. 5087-5097
    • Yamashiro-Matsumura, S.1    Matsumura, F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.