메뉴 건너뛰기




Volumn 98, Issue 3, 2010, Pages 462-469

The polymer brush model of neurofilament projections: Effect of protein composition

Author keywords

[No Author keywords available]

Indexed keywords

ANIMALIA;

EID: 76249091047     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2009.10.033     Document Type: Article
Times cited : (23)

References (27)
  • 1
    • 34548615784 scopus 로고    scopus 로고
    • A self-consistent field analysis of the neurofilament brush with amino-acid resolution
    • Zhulina, E. B., and F. A. M. Leermakers. 2007. A self-consistent field analysis of the neurofilament brush with amino-acid resolution. Biophys. J. 93:1421-1430.
    • (2007) Biophys. J. , vol.93 , pp. 1421-1430
    • Zhulina, E.B.1    Leermakers, F.A.M.2
  • 2
    • 34548612850 scopus 로고    scopus 로고
    • Effect of the ionic strength and pH on the equilibrium structure of a neurofilament brush
    • Zhulina, E. B., and F. A. M. Leermakers. 2007. Effect of the ionic strength and pH on the equilibrium structure of a neurofilament brush. Biophys. J. 93:1452-1463.
    • (2007) Biophys. J. , vol.93 , pp. 1452-1463
    • Zhulina, E.B.1    Leermakers, F.A.M.2
  • 3
    • 62549090988 scopus 로고    scopus 로고
    • Self-consistent field modeling of the neurofilament network
    • Leermakers, F. A. M., and E. B. Zhulina. 2008. Self-consistent field modeling of the neurofilament network. Biophys. Rev. Lett. 3:459-489.
    • (2008) Biophys. Rev. Lett. , vol.3 , pp. 459-489
    • Leermakers, F.A.M.1    Zhulina, E.B.2
  • 4
    • 85031336333 scopus 로고    scopus 로고
    • Reference deleted in proof.
    • Reference deleted in proof.
  • 5
    • 76249086413 scopus 로고    scopus 로고
    • On the polyelectrolyte brush model of neurofilaments
    • Zhulina, E. B., and F. A. M. Leermakers. 2009. On the polyelectrolyte brush model of neurofilaments. Soft Matter. 42:5360-5371.
    • (2009) Soft Matter. , vol.42 , pp. 5360-5371
    • Zhulina, E.B.1    Leermakers, F.A.M.2
  • 6
    • 0032559341 scopus 로고    scopus 로고
    • A structural scaffolding of intermediate filaments in health and disease
    • DOI 10.1126/science.279.5350.514
    • Fuchs, E., and D. W. Cleveland. 1998. A structural scaffolding of intermediate filaments in health and disease. Science. 279:514-519. (Pubitemid 28067272)
    • (1998) Science , vol.279 , Issue.5350 , pp. 514-519
    • Fuchs, E.1    Cleveland, D.W.2
  • 7
    • 0016541063 scopus 로고
    • The slow component of axonal transport. Identification of major structural polypeptides of the axon and their generality among mammalian neurons
    • Hoffman, P. N., and R. J. Lasek. 1975. The slow component of axonal transport. Identification of major structural polypeptides of the axon and their generality among mammalian neurons. J. Cell Biol. 66:351-366.
    • (1975) J. Cell Biol. , vol.66 , pp. 351-366
    • Hoffman, P.N.1    Lasek, R.J.2
  • 8
  • 9
    • 3943078618 scopus 로고    scopus 로고
    • Intermediate Filaments: Molecular structure, assembly mechanism, and integration into functionally distinct intracellular scaffolds
    • DOI 10.1146/annurev.biochem.73.011303.073823
    • Herrmann, H., and U. Aebi. 2004. Intermediate filaments: molecular structure, assembly mechanism, and integration into functionally distinct intracellular scaffolds. Annu. Rev. Biochem. 73:749-789. (Pubitemid 39050385)
    • (2004) Annual Review of Biochemistry , vol.73 , pp. 749-789
    • Herrmann, H.1    Aebi, U.2
  • 11
    • 0019968002 scopus 로고
    • Differential expression of neurofilament triplet proteins in brain development
    • DOI 10.1038/298277a0
    • Shaw, G., and K. Weber. 1982. Differential expression of neurofilament triplet proteins in brain development. Nature. 298:277-279. (Pubitemid 12089413)
    • (1982) Nature , vol.298 , Issue.5871 , pp. 277-279
    • Shaw, G.1    Weber, K.2
  • 12
    • 0021265440 scopus 로고
    • Regional, differences in the neuronal cytoskeleton
    • Drake, P. F., and R. J. Lasek. 1984. Regional, differences in the neuronal cytoskeleton. J. Neurosci. 4:1173-1186.
    • (1984) J. Neurosci. , vol.4 , pp. 1173-1186
    • Drake, P.F.1    Lasek, R.J.2
  • 13
    • 0033977283 scopus 로고    scopus 로고
    • Selective solubilization of high-molecular-mass neurofilament subunit during nerve regeneration
    • DOI 10.1046/j.1471-4159.2000.740860.x
    • Tsuda, M., T. Tashiro, and Y. Komiya. 2000. Selective solubilization of high-molecular-mass neurofilament subunit during nerve regeneration. J. Neurochem. 74:860-868. (Pubitemid 30053760)
    • (2000) Journal of Neurochemistry , vol.74 , Issue.2 , pp. 860-868
    • Tsuda, M.1    Tashiro, T.2    Komiya, Y.3
  • 15
    • 0030708555 scopus 로고    scopus 로고
    • Entropie exclusion by neurofilament sidearms: A mechanism for maintaining interfilament spacing
    • Brown, H. G., and J. H. Hoh. 1997. Entropie exclusion by neurofilament sidearms: a mechanism for maintaining interfilament spacing. Biochemistry. 36:15035-15040.
    • (1997) Biochemistry. , vol.36 , pp. 15035-15040
    • Brown, H.G.1    Hoh, J.H.2
  • 16
    • 4644266178 scopus 로고    scopus 로고
    • Molecular mechanisms for organizing the neuronal cytoskeleton
    • Mukhopadhyay, R., S. Kumar, and J. H. Hoh. 2004. Molecular mechanisms for organizing the neuronal cytoskeleton. Bioessays. 26:1-9.
    • (2004) Bioessays. , vol.26 , pp. 1-9
    • Mukhopadhyay, R.1    Kumar, S.2    Hoh, J.H.3
  • 17
    • 0032147118 scopus 로고    scopus 로고
    • Functional protein domains from the thermally driven motion of polypeptide chains: A proposal
    • Hoh, J. H. 1998. Functional protein domains from the thermally driven motion of polypeptide chains: a proposal. Proteins Struct. Funct. Genet. 32:223-228.
    • (1998) Proteins Struct. Funct. Genet. , vol.32 , pp. 223-228
    • Hoh, J.H.1
  • 18
    • 0036226094 scopus 로고    scopus 로고
    • Relating interactions between neurofilaments to the structure of axonal neurofilament distributions through polymer brush models
    • Kumar, S., X. Yin, M. E. Paulaitis. 2002. Relating interactions between neurofilaments to the structure of axonal neurofilament distributions through polymer brush models. Biophys. J. 82:2360-2372. (Pubitemid 34441277)
    • (2002) Biophysical Journal , vol.82 , Issue.5 , pp. 2360-2372
    • Kumar, S.1    Yin, X.2    Trapp, B.D.3    Hoh, J.H.4    Paulaitis, M.E.5
  • 19
    • 34548361622 scopus 로고    scopus 로고
    • Brushes, cables, and anchors: Recent insights into multiscale assembly and mechanics of cellular structural networks
    • Lele, T. P., and S. Kumar. 2007. Brushes, cables, and anchors: recent insights into multiscale assembly and mechanics of cellular structural networks. Cell Biochem. Biophys. 47:348-360.
    • (2007) Cell Biochem. Biophys. , vol.47 , pp. 348-360
    • Lele, T.P.1    Kumar, S.2
  • 20
    • 0033677861 scopus 로고    scopus 로고
    • The C-terminal tail domain of neurofilament protein-H (NF-H) forms the crossbridges and regulates neurofilament bundle formation
    • Chen, J., T. Nakata, N. Hirokawa. 2000. The C-terminal tail domain of neurofilament protein-H (NF-H) forms the crossbridges and regulates neurofilament bundle formation. J. Cell Sci. 113:3861-3869. (Pubitemid 30943027)
    • (2000) Journal of Cell Science , vol.113 , Issue.21 , pp. 3861-3869
    • Chen, J.1    Nakata, T.2    Zhang, Z.3    Hirokawa, N.4
  • 21
    • 0028900588 scopus 로고
    • Two distinct functions of the carboxyl-terminal tail domain of NF-M upon neurofilament assembly: Cross-bridge formation and longitudinal elongation of filaments
    • Nakagawa, T., J. Chen, N. Hirokawa. 1995. Two distinct functions of the carboxyl-terminal tail domain of NF-M upon neurofilament assembly: cross-bridge formation and longitudinal elongation of filaments. J. Cell Biol. 129:411-429.
    • (1995) J. Cell Biol. , vol.129 , pp. 411-429
    • Nakagawa, T.1    Chen, J.2    Hirokawa, N.3
  • 22
    • 47749130759 scopus 로고    scopus 로고
    • Interplay between liquid crystalline and isotropic gels in self-assembled neurofilament networks
    • Jones, J. B., and C. R. Safinya. 2008. Interplay between liquid crystalline and isotropic gels in self-assembled neurofilament networks. Biophys. J. 95:723-835.
    • (2008) Biophys. J. , vol.95 , pp. 723-835
    • Jones, J.B.1    Safinya, C.R.2
  • 23
    • 0032482231 scopus 로고    scopus 로고
    • Absence of the mid-sized neurofilament subunit decreases axonal calibers, levels of light neurofilament (NF-L), and neurofilament content
    • Elder, G. A., V. L. Friedrich, Jr., R. A. Lazzarini. 1998. Absence of the mid-sized neurofilament subunit decreases axonal calibers, levels of light neurofilament (NF-L), and neurofilament content. J. Cell Biol. 141:727-739.
    • (1998) J. Cell Biol. , vol.141 , pp. 727-739
    • Elder, G.A.1    Friedrich Jr., V.L.2    Lazzarini, R.A.3
  • 24
    • 0032487502 scopus 로고
    • Requirement of heavy neurofilament subunit in the development of axons with large calibers
    • Elder, G. A., V. L. Friedrich, Jr, R. A. Lazzarini. 1988. Requirement of heavy neurofilament subunit in the development of axons with large calibers. J. Cell Biol. 143:195-205.
    • (1988) J. Cell Biol. , vol.143 , pp. 195-205
    • Elder, G.A.1    Friedrich Jr., V.L.2    Lazzarini, R.A.3
  • 25
    • 0037135978 scopus 로고    scopus 로고
    • Gene replacement in mice reveals that the heavily phosphorylated tail of neurofilament heavy subunit does not affect axonal caliber or the transit of cargoes in slow axonal transport
    • Rao, M. V., M. L. Garcia, D. W. Cleveland. 2002. Gene replacement in mice reveals that the heavily phosphorylated tail of neurofilament heavy subunit does not affect axonal caliber or the transit of cargoes in slow axonal transport. J. Cell Biol. 158:681-693.
    • (2002) J. Cell Biol. , vol.158 , pp. 681-693
    • Rao, M.V.1    Garcia, M.L.2    Cleveland, D.W.3
  • 26
    • 10744228738 scopus 로고    scopus 로고
    • NFM is an essential target for the myelin-directed "outside-in" signaling cascade that mediates radial axonal growth
    • Garcia, M. L., C. S. Lobasiger, D. W. Cleveland. 2003. NF-M is an essential target for the myelin-directed "outside-in" signaling cascade that mediates radial axonal growth. J. Cell Biol. 163:1011-1020.
    • (2003) J. Cell Biol. , vol.163 , pp. 1011-1020
    • Garcia, M.L.1    Lobasiger, C.S.2    Cleveland, D.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.