메뉴 건너뛰기




Volumn 90, Issue 10, 2006, Pages 3739-3748

Dielectric measurement of individual microtubules using the electroorientation method

Author keywords

[No Author keywords available]

Indexed keywords

ION; POLYELECTROLYTE; PROTEIN;

EID: 33646195450     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.105.071324     Document Type: Article
Times cited : (145)

References (56)
  • 1
    • 0034078008 scopus 로고    scopus 로고
    • Microtubule-based transport systems in neurons: The roles of kinesins and dyneins
    • Goldstein, L. S., and Z. Yang. 2000. Microtubule-based transport systems in neurons: the roles of kinesins and dyneins. Annu. Rev. Neurosci. 23:39-71.
    • (2000) Annu. Rev. Neurosci. , vol.23 , pp. 39-71
    • Goldstein, L.S.1    Yang, Z.2
  • 2
    • 0028945057 scopus 로고
    • Microtubules and microtubule-associated proteins
    • Mandelkow, E., and E. M. Mandelkow. 1995. Microtubules and microtubule-associated proteins. Curr. Opin. Cell Biol. 7:72-81.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 72-81
    • Mandelkow, E.1    Mandelkow, E.M.2
  • 3
    • 0034681137 scopus 로고    scopus 로고
    • Mechanism of the single-headed processivity: Diffusional anchoring between the K-loop of kinesin and the C terminus of tubulin
    • Okada, Y., and N. Hirokawa. 2000. Mechanism of the single-headed processivity: diffusional anchoring between the K-loop of kinesin and the C terminus of tubulin. Proc. Natl. Acad. Sci. USA. 97:640-645.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 640-645
    • Okada, Y.1    Hirokawa, N.2
  • 4
    • 0034722373 scopus 로고    scopus 로고
    • Engineering the processive run length of the kinesin motor
    • Thorn, K. S., J. A. Ubersax, and R. D. Vale. 2000. Engineering the processive run length of the kinesin motor. J. Cell Biol. 151:1093-1100.
    • (2000) J. Cell Biol. , vol.151 , pp. 1093-1100
    • Thorn, K.S.1    Ubersax, J.A.2    Vale, R.D.3
  • 5
    • 0034079578 scopus 로고    scopus 로고
    • The C-terminus of tubulin increases cytoplasmic dynein and kinesin processivity
    • Wang, Z., and M. P. Sheetz. 2000. The C-terminus of tubulin increases cytoplasmic dynein and kinesin processivity. Biophys. J. 78:1955-1964.
    • (2000) Biophys. J. , vol.78 , pp. 1955-1964
    • Wang, Z.1    Sheetz, M.P.2
  • 6
    • 0020434615 scopus 로고
    • The nature of the clear zone around microtubules
    • Stebbings, H., and C. Hunt. 1982. The nature of the clear zone around microtubules. Cell Tissue Res. 227:609-617.
    • (1982) Cell Tissue Res. , vol.227 , pp. 609-617
    • Stebbings, H.1    Hunt, C.2
  • 7
    • 0028118917 scopus 로고
    • Microtubule organization and dynamics dependent on microtubule-associated proteins
    • Hirokawa, N. 1994. Microtubule organization and dynamics dependent on microtubule-associated proteins. Curr. Opin. Cell Biol. 6:74-81.
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 74-81
    • Hirokawa, N.1
  • 8
    • 0026666829 scopus 로고
    • Tau protein induces bundling of microtubules in vitro: Comparison of different tau isoforms and a tau protein fragment
    • Scott, C. W., A. B. Klika, M. M. Lo, T. E. Norris, and C. B. Caputo. 1992. Tau protein induces bundling of microtubules in vitro: comparison of different tau isoforms and a tau protein fragment. J. Neurosci. Res. 33:19-29.
    • (1992) J. Neurosci. Res. , vol.33 , pp. 19-29
    • Scott, C.W.1    Klika, A.B.2    Lo, M.M.3    Norris, T.E.4    Caputo, C.B.5
  • 10
    • 0043032716 scopus 로고    scopus 로고
    • The number of repeat sequences in microtubule-associated protein 4 affects the microtubule surface properties
    • Tokuraku, K., K. Matsushima, T. Matui, H. Nakagawa, M. Katsuki, R. Majima, and S. Kotani. 2003. The number of repeat sequences in microtubule-associated protein 4 affects the microtubule surface properties. J. Biol. Chem. 278:29609-29618.
    • (2003) J. Biol. Chem. , vol.278 , pp. 29609-29618
    • Tokuraku, K.1    Matsushima, K.2    Matui, T.3    Nakagawa, H.4    Katsuki, M.5    Majima, R.6    Kotani, S.7
  • 12
  • 14
    • 0026253815 scopus 로고
    • Condensation of DNA by multivalent cations: Considerations on mechanism
    • Bloomfield, V. A. 1991. Condensation of DNA by multivalent cations: considerations on mechanism. Biopolymers. 31:1471-1481.
    • (1991) Biopolymers , vol.31 , pp. 1471-1481
    • Bloomfield, V.A.1
  • 15
    • 0030012323 scopus 로고    scopus 로고
    • The polyelectrolyte nature of F-actin and the mechanism of actin bundle formation
    • Tang, J. X., and P. A. Janmey. 1996. The polyelectrolyte nature of F-actin and the mechanism of actin bundle formation. J. Biol. Chem. 271:8556-8563.
    • (1996) J. Biol. Chem. , vol.271 , pp. 8556-8563
    • Tang, J.X.1    Janmey, P.A.2
  • 16
    • 0030845631 scopus 로고    scopus 로고
    • Opposite effects of electrostatics and steric exclusion on bundle formation by F-actin and other filamentous polyelectrolytes
    • Tang, J. X., T. Ito, T. Tao, P. Traub, and P. A. Janmey. 1997. Opposite effects of electrostatics and steric exclusion on bundle formation by F-actin and other filamentous polyelectrolytes. Biochemistry. 36:12600-12607.
    • (1997) Biochemistry , vol.36 , pp. 12600-12607
    • Tang, J.X.1    Ito, T.2    Tao, T.3    Traub, P.4    Janmey, P.A.5
  • 18
    • 0036857758 scopus 로고    scopus 로고
    • Electrostatic correlations: From plasma to biology
    • Levin, Y. 2002. Electrostatic correlations: from plasma to biology. Rep. Prog. Phys. 65:1577-1632.
    • (2002) Rep. Prog. Phys. , vol.65 , pp. 1577-1632
    • Levin, Y.1
  • 19
    • 0041306048 scopus 로고    scopus 로고
    • Like-charge attraction between polyelectrolytes induced by counterion charge density waves
    • Angelini, T. E., H. Liang, W. Wriggers, and G. C. Wong. 2003. Like-charge attraction between polyelectrolytes induced by counterion charge density waves. Proc. Natl. Acad. Sci. USA. 100:8634-8637.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 8634-8637
    • Angelini, T.E.1    Liang, H.2    Wriggers, W.3    Wong, G.C.4
  • 21
    • 0032300427 scopus 로고    scopus 로고
    • Electrorotation and dielectrophoresis
    • Goater, A. D., and R. Pethig. 1998. Electrorotation and dielectrophoresis. Parasitology. 117(Suppl.):S177-S189.
    • (1998) Parasitology , vol.117 , Issue.SUPPL.
    • Goater, A.D.1    Pethig, R.2
  • 22
    • 0000733480 scopus 로고
    • The electric polarization of rod-like, charged macromolecules
    • Mandel, M. 1961. The electric polarization of rod-like, charged macromolecules. Mol. Phys. 4:489-496.
    • (1961) Mol. Phys. , vol.4 , pp. 489-496
    • Mandel, M.1
  • 23
    • 0017895903 scopus 로고
    • The molecular theory of polyelectrolyte solutions with applications to the electrostatic properties of polynucleotides
    • Manning, G. S. 1978. The molecular theory of polyelectrolyte solutions with applications to the electrostatic properties of polynucleotides. Q. Rev. Biophys. 11:179-246.
    • (1978) Q. Rev. Biophys. , vol.11 , pp. 179-246
    • Manning, G.S.1
  • 26
    • 0017667806 scopus 로고
    • Dimethyl sulfoxide-induced self-assembly of tubulin lacking associated proteins
    • Himes, R. H., P. R. Burton, and J. M. Gaito. 1977. Dimethyl sulfoxide-induced self-assembly of tubulin lacking associated proteins. J. Biol. Chem. 252:6222-6228.
    • (1977) J. Biol. Chem. , vol.252 , pp. 6222-6228
    • Himes, R.H.1    Burton, P.R.2    Gaito, J.M.3
  • 27
    • 0022534289 scopus 로고
    • Direct observation of steady-state microtubule dynamics
    • Kristofferson, D., T. Mitchison, and M. Kirschner. 1986. Direct observation of steady-state microtubule dynamics. J. Cell Biol. 102:1007-1019.
    • (1986) J. Cell Biol. , vol.102 , pp. 1007-1019
    • Kristofferson, D.1    Mitchison, T.2    Kirschner, M.3
  • 28
    • 0021135071 scopus 로고
    • Controlled proteolysis of tubulin by subtilisin: Localization of the site for MAP2 interaction
    • Serrano, L., J. Avila, and R. B. Maccioni. 1984. Controlled proteolysis of tubulin by subtilisin: localization of the site for MAP2 interaction. Biochemistry. 23:4675-4681.
    • (1984) Biochemistry , vol.23 , pp. 4675-4681
    • Serrano, L.1    Avila, J.2    Maccioni, R.B.3
  • 29
    • 0018464246 scopus 로고
    • Calculation of the concentrations of free cations and cation-ligand complexes in solutions containing multiple divalent cations and ligands
    • Goldstein, D. A. 1979. Calculation of the concentrations of free cations and cation-ligand complexes in solutions containing multiple divalent cations and ligands. Biophys. J. 26:235-242.
    • (1979) Biophys. J. , vol.26 , pp. 235-242
    • Goldstein, D.A.1
  • 30
    • 0001544174 scopus 로고
    • Determination of biological impedances
    • G. Oster, editor. Academic Press, New York
    • Schwan, H. P. 1963. Determination of biological impedances. In Physical Techniques in Biological Research, Vol. 6. G. Oster, editor. Academic Press, New York. 323-407.
    • (1963) Physical Techniques in Biological Research , vol.6 , pp. 323-407
    • Schwan, H.P.1
  • 31
    • 0023540829 scopus 로고
    • Frequency-dependent orientation of ellipsoidal particles in AC electric fields
    • Miller, R. D., and T. B. Jones. 1987. Frequency-dependent orientation of ellipsoidal particles in AC electric fields. Proc. IEEE 9th Annu. EMBS Conf. Boston.:710-711.
    • (1987) Proc. IEEE 9th Annu. EMBS Conf. Boston , pp. 710-711
    • Miller, R.D.1    Jones, T.B.2
  • 32
    • 0026925397 scopus 로고
    • Orientation and transformation of flagella in electrostatic field
    • Washizu, M., M. Shikida, S. Aizawa, and H. Hotani. 1992. Orientation and transformation of flagella in electrostatic field. IEEE Trans. Ind. Appl. 28:1194-1202.
    • (1992) IEEE Trans. Ind. Appl. , vol.28 , pp. 1194-1202
    • Washizu, M.1    Shikida, M.2    Aizawa, S.3    Hotani, H.4
  • 33
    • 0027285263 scopus 로고
    • Electro-orientation of ellipsoidal erythrocytes. Theory and experiment
    • Miller, R. D., and T. B. Jones. 1993. Electro-orientation of ellipsoidal erythrocytes. Theory and experiment. Biophys. J. 64:1588-1595.
    • (1993) Biophys. J. , vol.64 , pp. 1588-1595
    • Miller, R.D.1    Jones, T.B.2
  • 36
    • 0022705194 scopus 로고
    • Calculation of the isoelectric points of polypeptides from the amino acid composition
    • Skoog, B., and A. Wichman. 1986. Calculation of the isoelectric points of polypeptides from the amino acid composition. Trends Anal. Chem. 5:82-83.
    • (1986) Trends Anal. Chem. , vol.5 , pp. 82-83
    • Skoog, B.1    Wichman, A.2
  • 37
    • 0005979938 scopus 로고
    • Complete amino acid sequence of alpha-tubulin from porcine brain
    • Ponstingl, H., E. Krauhs, M. Little, and T. Kempf. 1981. Complete amino acid sequence of alpha-tubulin from porcine brain. Proc. Natl. Acad. Sci. USA. 78:2757-2761.
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 2757-2761
    • Ponstingl, H.1    Krauhs, E.2    Little, M.3    Kempf, T.4
  • 39
    • 0039940808 scopus 로고    scopus 로고
    • Control of the structural stability of the tubulin dimer by one high affinity bound magnesium ion at nucleotide N-site
    • Menendez, M., G. Rivas, J. F. Diaz, and J. M. Andreu. 1998. Control of the structural stability of the tubulin dimer by one high affinity bound magnesium ion at nucleotide N-site. J. Biol. Chem. 273:167-176.
    • (1998) J. Biol. Chem. , vol.273 , pp. 167-176
    • Menendez, M.1    Rivas, G.2    Diaz, J.F.3    Andreu, J.M.4
  • 41
    • 17844401462 scopus 로고    scopus 로고
    • Results of molecular dynamics computations of the structural and electrostatic properties of tubulin and their consequences for microtubules
    • Tuszynski, J. A., T. Luchko, E. J. Carpenter, and E. Crawford. 2004. Results of molecular dynamics computations of the structural and electrostatic properties of tubulin and their consequences for microtubules. J. Comput. Theor. Nanosci. 1:392-397.
    • (2004) J. Comput. Theor. Nanosci. , vol.1 , pp. 392-397
    • Tuszynski, J.A.1    Luchko, T.2    Carpenter, E.J.3    Crawford, E.4
  • 42
    • 0020366962 scopus 로고
    • Parallel arrays of microtubules formed in electric and magnetic fields
    • Vassilev, P. M., R. T. Dronzine, M. P. Vassileva, and G. A. Georgiev. 1982. Parallel arrays of microtubules formed in electric and magnetic fields. Biosci. Rep. 2:1025-1029.
    • (1982) Biosci. Rep. , vol.2 , pp. 1025-1029
    • Vassilev, P.M.1    Dronzine, R.T.2    Vassileva, M.P.3    Georgiev, G.A.4
  • 44
    • 0014179169 scopus 로고
    • Effect of ions on the dielectric relaxation of DNA
    • Takashima, S. 1967. Effect of ions on the dielectric relaxation of DNA. Biopolymers. 5:899-913.
    • (1967) Biopolymers , vol.5 , pp. 899-913
    • Takashima, S.1
  • 45
    • 0034141740 scopus 로고    scopus 로고
    • Dielectric relaxation around a charged colloidal cylinder in an electrolyte
    • Fornés, J. A. 2000. Dielectric relaxation around a charged colloidal cylinder in an electrolyte. J. Colloid Interface Sci. 222:97-102.
    • (2000) J. Colloid Interface Sci. , vol.222 , pp. 97-102
    • Fornés, J.A.1
  • 46
    • 0016813649 scopus 로고
    • Ionic and nucleotide requirements for microtubule polymerization in vitro
    • Olmsted, J. B., and G. G. Borisy. 1975. Ionic and nucleotide requirements for microtubule polymerization in vitro. Biochemistry. 14:2996-3005.
    • (1975) Biochemistry , vol.14 , pp. 2996-3005
    • Olmsted, J.B.1    Borisy, G.G.2
  • 47
    • 19744382442 scopus 로고    scopus 로고
    • Direct observation of charge inversion by multivalent ions as a universal electrostatic phenomenon
    • Besteman, K., M. A. Zevenbergen, H. A. Heering, and S. G. Lemay. 2004. Direct observation of charge inversion by multivalent ions as a universal electrostatic phenomenon. Phys. Rev. Lett. 93:170802.
    • (2004) Phys. Rev. Lett. , vol.93 , pp. 170802
    • Besteman, K.1    Zevenbergen, M.A.2    Heering, H.A.3    Lemay, S.G.4
  • 48
    • 42749101738 scopus 로고    scopus 로고
    • Hydrodynamics within the electric double layer on slipping surfaces
    • Joly, L., C. Ybert, E. Trizac, and L. Bocquet. 2004. Hydrodynamics within the electric double layer on slipping surfaces. Phys. Rev. Lett. 93:257805.
    • (2004) Phys. Rev. Lett. , vol.93 , pp. 257805
    • Joly, L.1    Ybert, C.2    Trizac, E.3    Bocquet, L.4
  • 50
    • 0023025012 scopus 로고
    • Proteolysis of tubulin and the substructure of the tubulin dimer
    • Sackett, D. L., and J. Wolff. 1986. Proteolysis of tubulin and the substructure of the tubulin dimer. J. Biol. Chem. 261:9070-9076.
    • (1986) J. Biol. Chem. , vol.261 , pp. 9070-9076
    • Sackett, D.L.1    Wolff, J.2
  • 51
    • 11644276439 scopus 로고
    • Limiting laws and counterion condensation in polyelectrolyte solutions. I. Colligative Properties
    • Manning, G. S. 1969. Limiting laws and counterion condensation in polyelectrolyte solutions. I. Colligative Properties. J. Chem. Phys. 51:924-933.
    • (1969) J. Chem. Phys. , vol.51 , pp. 924-933
    • Manning, G.S.1
  • 53
    • 0025308916 scopus 로고
    • Ion distributions around DNA and other cylindrical polyions: Theoretical descriptions and physical implications
    • Anderson, C. F., and M. T. Record, Jr. 1990. Ion distributions around DNA and other cylindrical polyions: theoretical descriptions and physical implications. Annu. Rev. Biophys. Biophys. Chem. 19:423-465.
    • (1990) Annu. Rev. Biophys. Biophys. Chem. , vol.19 , pp. 423-465
    • Anderson, C.F.1    Record Jr., M.T.2
  • 54
    • 0032495513 scopus 로고    scopus 로고
    • Structure of the alpha beta tubulin dimer by electron crystallography
    • Nogales, E., S. G. Wolf, and K. H. Downing. 1998. Structure of the alpha beta tubulin dimer by electron crystallography. Nature. 391:199-203.
    • (1998) Nature , vol.391 , pp. 199-203
    • Nogales, E.1    Wolf, S.G.2    Downing, K.H.3
  • 56
    • 0027533269 scopus 로고
    • Flexural rigidity of microtubules and actin filaments measured from thermal fluctuations in shape
    • Gittes, F., B. Mickey, J. Nettleton, and J. Howard. 1993. Flexural rigidity of microtubules and actin filaments measured from thermal fluctuations in shape. J. Cell Biol. 120:923-934.
    • (1993) J. Cell Biol. , vol.120 , pp. 923-934
    • Gittes, F.1    Mickey, B.2    Nettleton, J.3    Howard, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.