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Volumn 93, Issue 5, 2007, Pages 1452-1463

Effect of the ionic strength and pH on the equilibrium structure of a neurofilament brush

Author keywords

[No Author keywords available]

Indexed keywords

NEUROFILAMENT H PROTEIN; NEUROFILAMENT L PROTEIN; NEUROFILAMENT M PROTEIN; NEUROFILAMENT PROTEIN; POLYELECTROLYTE; SOLVENT; UNCLASSIFIED DRUG;

EID: 34548612850     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.107.104695     Document Type: Article
Times cited : (39)

References (29)
  • 1
    • 7944236911 scopus 로고    scopus 로고
    • The cytoskeleton in neurodegenerative diseases
    • Caims, N. J., V. M.-Y. Lee, and J. Q. Trojanowski. 2004. The cytoskeleton in neurodegenerative diseases. J. Pathol. 204:438-449.
    • (2004) J. Pathol , vol.204 , pp. 438-449
    • Caims, N.J.1    Lee, V.M.-Y.2    Trojanowski, J.Q.3
  • 2
    • 0032821709 scopus 로고    scopus 로고
    • Neurofilament functions in health and disease
    • Julien, J. P. 1999. Neurofilament functions in health and disease. Curr. Opin. Neurobiol. 9:554-560.
    • (1999) Curr. Opin. Neurobiol , vol.9 , pp. 554-560
    • Julien, J.P.1
  • 4
    • 0034618118 scopus 로고    scopus 로고
    • Intermediate filaments on the move
    • Chou, Y.-H., and R. D. Goldman. 2000. Intermediate filaments on the move. J. Cell Biol. 150:F101-F105.
    • (2000) J. Cell Biol , vol.150
    • Chou, Y.-H.1    Goldman, R.D.2
  • 7
    • 0025269889 scopus 로고
    • Molecular architecture of the neurofilament. I. Subunit arrangement of neurofilament L protein in the intermediate-sized filament
    • Hisanaga, S.-I., A. Ikai, and N. Hirokawa. 1990. Molecular architecture of the neurofilament. I. Subunit arrangement of neurofilament L protein in the intermediate-sized filament. J. Mol. Biol. 211:857-869.
    • (1990) J. Mol. Biol , vol.211 , pp. 857-869
    • Hisanaga, S.-I.1    Ikai, A.2    Hirokawa, N.3
  • 8
    • 0025280187 scopus 로고
    • Molecular architecture of the neurofilament. II. Reassembly process of neurofilament L protein in vitro
    • Hisanaga, S.-I., and N. Hirokawa. 1990. Molecular architecture of the neurofilament. II. Reassembly process of neurofilament L protein in vitro. J. Mol. Biol. 211:871-882.
    • (1990) J. Mol. Biol , vol.211 , pp. 871-882
    • Hisanaga, S.-I.1    Hirokawa, N.2
  • 9
    • 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
  • 10
    • 0036226094 scopus 로고    scopus 로고
    • Relating interactions between neurofilaments to the structure of axonal neurofilament distribution through polymer brush models
    • Kumar, S., X. Yin, B. D. Trapp, J. H. Hoh, and M. E. Paulatis. 2002. Relating interactions between neurofilaments to the structure of axonal neurofilament distribution through polymer brush models. Biophys. J. 82:2360-2372.
    • (2002) Biophys. J , vol.82 , pp. 2360-2372
    • Kumar, S.1    Yin, X.2    Trapp, B.D.3    Hoh, J.H.4    Paulatis, M.E.5
  • 11
    • 0030708555 scopus 로고
    • Entropic exclusion of neurofilament side arms: A mechanism for maintaining interfilament spacing
    • Brown, H. G., and J. H. Hoh. 1977. Entropic exclusion of neurofilament side arms: a mechanism for maintaining interfilament spacing. Biochemistry. 36:15035-15040.
    • (1977) Biochemistry , vol.36 , pp. 15035-15040
    • Brown, H.G.1    Hoh, J.H.2
  • 12
    • 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
  • 13
    • 0035929161 scopus 로고    scopus 로고
    • AFM force measurements on microtubule-associated proteins: The projection domain exerts a longrange repulsive force
    • Mukhopadhyay, R., and J. H. Hoh. 2001. AFM force measurements on microtubule-associated proteins: the projection domain exerts a longrange repulsive force. FEBS Lett. 505:374-382.
    • (2001) FEBS Lett , vol.505 , pp. 374-382
    • Mukhopadhyay, R.1    Hoh, J.H.2
  • 14
    • 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
  • 15
    • 0029992051 scopus 로고    scopus 로고
    • Self-consistent field modeling of adsorbed β-casein: Effects of pH and ionic strength on surface converge and density profile
    • Leermakers, F. A. M., P. J. Atkinson, E. Dickinson, and D. S. Horne. 1996. Self-consistent field modeling of adsorbed β-casein: effects of pH and ionic strength on surface converge and density profile. J. Colloid Int. Sci. 178:681-693.
    • (1996) J. Colloid Int. Sci , vol.178 , pp. 681-693
    • Leermakers, F.A.M.1    Atkinson, P.J.2    Dickinson, E.3    Horne, D.S.4
  • 17
    • 18844434621 scopus 로고    scopus 로고
    • Molecular modeling of lipid bilayers and the effect of protein-like inclusions
    • Kik, R. A., F. A. M. Leermakers, and J. M. Kleijn. 2005. Molecular modeling of lipid bilayers and the effect of protein-like inclusions. Phys. Chem. Chem. Phys. 7:1996-2005.
    • (2005) Phys. Chem. Chem. Phys , vol.7 , pp. 1996-2005
    • Kik, R.A.1    Leermakers, F.A.M.2    Kleijn, J.M.3
  • 18
    • 0020326774 scopus 로고
    • Cross-linker system between neurofilaments, microtubules and membranous organelles in frog axons revealed by the quick-freeze, deep-etching method
    • Hirokawa, N. 1982. Cross-linker system between neurofilaments, microtubules and membranous organelles in frog axons revealed by the quick-freeze, deep-etching method. J. Cell Biol. 94:129-142.
    • (1982) J. Cell Biol , vol.94 , pp. 129-142
    • Hirokawa, N.1
  • 19
    • 0033677861 scopus 로고    scopus 로고
    • The C-terminal tail domain of neurofilament protein -H (NF-H) forms the cross bridges and regulates neurofilament bundle formation
    • Chen, J. G., T. Nakata, Z. Z. Zhang, and N. Hirokawa. 2000. The C-terminal tail domain of neurofilament protein -H (NF-H) forms the cross bridges and regulates neurofilament bundle formation. J. Cell Sci. 113:3861-3869.
    • (2000) J. Cell Sci , vol.113 , pp. 3861-3869
    • Chen, J.G.1    Nakata, T.2    Zhang, Z.Z.3    Hirokawa, N.4
  • 21
    • 0034722377 scopus 로고    scopus 로고
    • Local control of neurofilament accumulation during radial growth of myelinating axons in vivo: Selective role of site-specific phosphorylation
    • Sanchez, I., L. Hassinger, R. K. Sihag, D. W. Cleveland, P. Mohan, and R. A. Nixon. 2000. Local control of neurofilament accumulation during radial growth of myelinating axons in vivo: selective role of site-specific phosphorylation. J. Cell Biol. 151:1013-1024.
    • (2000) J. Cell Biol , vol.151 , pp. 1013-1024
    • Sanchez, I.1    Hassinger, L.2    Sihag, R.K.3    Cleveland, D.W.4    Mohan, P.5    Nixon, R.A.6
  • 22
    • 0023520075 scopus 로고
    • Monoclonal antibodies distinguish several differentially phosphorylated states of the two largest rat neurofilament subunits (NF-H and NF-M) and demonstrate their existence in the normal nervous system of adult rats
    • Lee, V. M.-Y., M. J. Carden, W. W. Schlaepfer, and J. Q. Trojanowski. 1987. Monoclonal antibodies distinguish several differentially phosphorylated states of the two largest rat neurofilament subunits (NF-H and NF-M) and demonstrate their existence in the normal nervous system of adult rats. J. Neurosci. 7:3478-3488.
    • (1987) J. Neurosci , vol.7 , pp. 3478-3488
    • Lee, V.M.-Y.1    Carden, M.J.2    Schlaepfer, W.W.3    Trojanowski, J.Q.4
  • 23
    • 0023515543 scopus 로고
    • Two-stage expression of neurofilament polypeptides during rat neurogenesis with early establishment of adult phosphorylation patterns
    • Carden, M. J., J. Q. Trojanowski, W. W. Schlaepfer, and V. M.-Y. Lee. 1987. Two-stage expression of neurofilament polypeptides during rat neurogenesis with early establishment of adult phosphorylation patterns. J. Neurosci. 7:3499-3504.
    • (1987) J. Neurosci , vol.7 , pp. 3499-3504
    • Carden, M.J.1    Trojanowski, J.Q.2    Schlaepfer, W.W.3    Lee, V.M.-Y.4
  • 24
    • 0017524356 scopus 로고
    • Adsorption of chain molecules with a polar head - a scaling description
    • Alexander, S. 1977. Adsorption of chain molecules with a polar head - a scaling description. J. Phys. (Paris). 38:983-987.
    • (1977) J. Phys. (Paris) , vol.38 , pp. 983-987
    • Alexander, S.1
  • 25
    • 0026153027 scopus 로고
    • Colloid stabilization with grafted polyelectrolytes
    • Pincus, P. 1991. Colloid stabilization with grafted polyelectrolytes. Macromolecules. 24:2912-2919.
    • (1991) Macromolecules , vol.24 , pp. 2912-2919
    • Pincus, P.1
  • 26
  • 27
    • 0030588089 scopus 로고    scopus 로고
    • Kappa-casein as a polyelectrolyte brush on the surface of casein micelles
    • De Kruif, C. G., and E. B. Zhulina. 1996. Kappa-casein as a polyelectrolyte brush on the surface of casein micelles. Colloid Surf. A. 117:151-159.
    • (1996) Colloid Surf. A , vol.117 , pp. 151-159
    • De Kruif, C.G.1    Zhulina, E.B.2
  • 28
    • 1142298544 scopus 로고    scopus 로고
    • Sensitivity, speci-ficity and hybridization isotherms of DNA chips
    • Halperin, A., A. Buhot, and E. B. Zhulina. 2004. Sensitivity, speci-ficity and hybridization isotherms of DNA chips. Biophys. J. 86:718-730.
    • (2004) Biophys. J , vol.86 , pp. 718-730
    • Halperin, A.1    Buhot, A.2    Zhulina, E.B.3
  • 29
    • 21144442981 scopus 로고    scopus 로고
    • Cylindrical molecular brushes under poor solvent conditions: Microscopic observation and scaling analysis
    • Sheiko, S. S., O. V. Borisov, S. A. Prokhorova, and M. Möller. 2004. Cylindrical molecular brushes under poor solvent conditions: microscopic observation and scaling analysis. Eur. Phys. J. E. 13:125-131.
    • (2004) Eur. Phys. J. E , vol.13 , pp. 125-131
    • Sheiko, S.S.1    Borisov, O.V.2    Prokhorova, S.A.3    Möller, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.