메뉴 건너뛰기




Volumn 32, Issue , 2015, Pages 92-101

Neurofilament assembly and function during neuronal development

Author keywords

[No Author keywords available]

Indexed keywords

NEUROFILAMENT PROTEIN; INTERMEDIATE FILAMENT PROTEIN;

EID: 84922130219     PISSN: 09550674     EISSN: 18790410     Source Type: Journal    
DOI: 10.1016/j.ceb.2015.01.003     Document Type: Review
Times cited : (99)

References (76)
  • 1
    • 38449114878 scopus 로고    scopus 로고
    • Nestin in central nervous system cells
    • Gilyarov A.V. Nestin in central nervous system cells. Neurosci Behav Physiol 2008, 38:165-169.
    • (2008) Neurosci Behav Physiol , vol.38 , pp. 165-169
    • Gilyarov, A.V.1
  • 3
    • 0028288886 scopus 로고
    • Expression of the gene for the neuronal intermediate filament protein alpha-internexin coincides with the onset of neuronal differentiation in the developing rat nervous system
    • Fliegner K.H., Kaplan M.P., Wood T.L., Pintar J.E., Liem R.K. Expression of the gene for the neuronal intermediate filament protein alpha-internexin coincides with the onset of neuronal differentiation in the developing rat nervous system. J Comp Neurol 1994, 342:161-173.
    • (1994) J Comp Neurol , vol.342 , pp. 161-173
    • Fliegner, K.H.1    Kaplan, M.P.2    Wood, T.L.3    Pintar, J.E.4    Liem, R.K.5
  • 4
    • 84875444206 scopus 로고    scopus 로고
    • Neurofilaments: properties, functions, and regulation
    • Springer
    • Perrot R., Eyer J. Neurofilaments: properties, functions, and regulation. The Cytoskeleton 2013, 171-236. Springer.
    • (2013) The Cytoskeleton , pp. 171-236
    • Perrot, R.1    Eyer, J.2
  • 5
    • 77955919760 scopus 로고    scopus 로고
    • Distal to proximal development of peripheral nerves requires the expression of neurofilament heavy
    • Shen H., Barry D.M., Garcia M.L. Distal to proximal development of peripheral nerves requires the expression of neurofilament heavy. Neuroscience 2010, 170:16-21.
    • (2010) Neuroscience , vol.170 , pp. 16-21
    • Shen, H.1    Barry, D.M.2    Garcia, M.L.3
  • 6
    • 84862849287 scopus 로고    scopus 로고
    • Peripherin is a subunit of peripheral nerve neurofilaments: implications for differential vulnerability of CNS and peripheral nervous system axons
    • Yuan A., Sasaki T., Kumar A., Peterhoff C.M., Rao M.V., Liem R.K., Julien J.-P., Nixon R.A. Peripherin is a subunit of peripheral nerve neurofilaments: implications for differential vulnerability of CNS and peripheral nervous system axons. J Neurosci 2012, 32:8501-8508.
    • (2012) J Neurosci , vol.32 , pp. 8501-8508
    • Yuan, A.1    Sasaki, T.2    Kumar, A.3    Peterhoff, C.M.4    Rao, M.V.5    Liem, R.K.6    Julien, J.-P.7    Nixon, R.A.8
  • 7
    • 73149102061 scopus 로고    scopus 로고
    • Peripherin and ATF3 genes are differentially regulated in regenerating and non-regenerating primary sensory neurons
    • Reid A.J., Welin D., Wiberg M., Terenghi G., Novikov L.N. Peripherin and ATF3 genes are differentially regulated in regenerating and non-regenerating primary sensory neurons. Brain Res 2010, 1310:1-7.
    • (2010) Brain Res , vol.1310 , pp. 1-7
    • Reid, A.J.1    Welin, D.2    Wiberg, M.3    Terenghi, G.4    Novikov, L.N.5
  • 8
    • 77953230609 scopus 로고    scopus 로고
    • Synemin isoforms in astroglial and neuronal cells from human central nervous system
    • Izmiryan A., Peltekian E., Federici T., Paulin D., Li Z.L., Xue Z.G. Synemin isoforms in astroglial and neuronal cells from human central nervous system. Neurochem Res 2010, 35:881-887.
    • (2010) Neurochem Res , vol.35 , pp. 881-887
    • Izmiryan, A.1    Peltekian, E.2    Federici, T.3    Paulin, D.4    Li, Z.L.5    Xue, Z.G.6
  • 9
    • 59849099824 scopus 로고    scopus 로고
    • Synemin isoforms during mouse development: multiplicity of partners in vascular and neuronal systems
    • Izmiryan A., Franco C.A., Paulin D., Li Z., Xue Z. Synemin isoforms during mouse development: multiplicity of partners in vascular and neuronal systems. Exp Cell Res 2009, 315:769-783.
    • (2009) Exp Cell Res , vol.315 , pp. 769-783
    • Izmiryan, A.1    Franco, C.A.2    Paulin, D.3    Li, Z.4    Xue, Z.5
  • 10
    • 68849112456 scopus 로고    scopus 로고
    • Intermediate filaments: primary determinants of cell architecture and plasticity
    • Herrmann H., Strelkov S.V., Burkhard P., Aebi U. Intermediate filaments: primary determinants of cell architecture and plasticity. J Clin Invest 2009, 119:1772-1783.
    • (2009) J Clin Invest , vol.119 , pp. 1772-1783
    • Herrmann, H.1    Strelkov, S.V.2    Burkhard, P.3    Aebi, U.4
  • 11
    • 84865305368 scopus 로고    scopus 로고
    • Atomic structure of the vimentin central α-helical domain and its implications for intermediate filament assembly
    • Chernyatina A.A., Nicolet S., Aebi U., Herrmann H., Strelkov S.V. Atomic structure of the vimentin central α-helical domain and its implications for intermediate filament assembly. Proc Natl Acad Sci U S A 2012, 109:13620-13625.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 13620-13625
    • Chernyatina, A.A.1    Nicolet, S.2    Aebi, U.3    Herrmann, H.4    Strelkov, S.V.5
  • 12
    • 84865204718 scopus 로고    scopus 로고
    • The structure of vimentin linker 1 and rod 1B domains characterized by site-directed spin-labeling electron paramagnetic resonance (SDSL-EPR) and X-ray crystallography
    • Aziz A., Hess J.F., Budamagunta M.S., Voss J.C., Kuzin A.P., Huang Y.J., Xiao R., Montelione G.T., FitzGerald P.G., Hunt J.F. The structure of vimentin linker 1 and rod 1B domains characterized by site-directed spin-labeling electron paramagnetic resonance (SDSL-EPR) and X-ray crystallography. J Biol Chem 2012, 287:28349-28361.
    • (2012) J Biol Chem , vol.287 , pp. 28349-28361
    • Aziz, A.1    Hess, J.F.2    Budamagunta, M.S.3    Voss, J.C.4    Kuzin, A.P.5    Huang, Y.J.6    Xiao, R.7    Montelione, G.T.8    FitzGerald, P.G.9    Hunt, J.F.10
  • 13
    • 33749177577 scopus 로고    scopus 로고
    • Alpha-internexin is structurally and functionally associated with the neurofilament triplet proteins in the mature CNS
    • Yuan A., Rao M.V., Sasaki T., Chen Y., Kumar A., Veeranna Liem R.K.H., Eyer J., Peterson A.C., Julien J.-P., et al. Alpha-internexin is structurally and functionally associated with the neurofilament triplet proteins in the mature CNS. J Neurosci 2006, 26:10006-10019.
    • (2006) J Neurosci , vol.26 , pp. 10006-10019
    • Yuan, A.1    Rao, M.V.2    Sasaki, T.3    Chen, Y.4    Kumar, A.5    Veeranna Liem, R.K.H.6    Eyer, J.7    Peterson, A.C.8    Julien, J.-P.9
  • 14
    • 0032570802 scopus 로고    scopus 로고
    • Neurofilament (NF) assembly; divergent characteristics of human and rodent NF-L subunits
    • Carter J., Gragerov A., Konvicka K., Elder G., Weinstein H., Lazzarini R.A. Neurofilament (NF) assembly; divergent characteristics of human and rodent NF-L subunits. J Biol Chem 1998, 273:5101-5108.
    • (1998) J Biol Chem , vol.273 , pp. 5101-5108
    • Carter, J.1    Gragerov, A.2    Konvicka, K.3    Elder, G.4    Weinstein, H.5    Lazzarini, R.A.6
  • 15
    • 60749102885 scopus 로고    scopus 로고
    • Neurofilament subunit (NFL) head domain phosphorylation regulates axonal transport of neurofilaments
    • Yates D.M., Manser C., De Vos K.J., Shaw C.E., McLoughlin D.M., Miller C.C.J. Neurofilament subunit (NFL) head domain phosphorylation regulates axonal transport of neurofilaments. Eur J Cell Biol 2009, 88:193-202.
    • (2009) Eur J Cell Biol , vol.88 , pp. 193-202
    • Yates, D.M.1    Manser, C.2    De Vos, K.J.3    Shaw, C.E.4    McLoughlin, D.M.5    Miller, C.C.J.6
  • 17
    • 0032901910 scopus 로고    scopus 로고
    • Serine-23 is a major protein kinase A phosphorylation site on the amino-terminal head domain of the middle molecular mass subunit of neurofilament proteins
    • Sihag R.K., Jaffe H., Nixon R.A., Rong X. Serine-23 is a major protein kinase A phosphorylation site on the amino-terminal head domain of the middle molecular mass subunit of neurofilament proteins. J Neurochem 1999, 72:491-499.
    • (1999) J Neurochem , vol.72 , pp. 491-499
    • Sihag, R.K.1    Jaffe, H.2    Nixon, R.A.3    Rong, X.4
  • 18
    • 0027328373 scopus 로고
    • Glycosylation of mammalian neurofilaments. Localization of multiple O-linked N-acetylglucosamine moieties on neurofilament polypeptides L and M
    • Dong D.L., Xu Z.S., Chevrier M.R., Cotter R.J., Cleveland D.W., Hart G.W. Glycosylation of mammalian neurofilaments. Localization of multiple O-linked N-acetylglucosamine moieties on neurofilament polypeptides L and M. J Biol Chem 1993, 268:16679-16687.
    • (1993) J Biol Chem , vol.268 , pp. 16679-16687
    • Dong, D.L.1    Xu, Z.S.2    Chevrier, M.R.3    Cotter, R.J.4    Cleveland, D.W.5    Hart, G.W.6
  • 19
    • 0029786683 scopus 로고    scopus 로고
    • Cytoplasmic O-GlcNAc modification of the head domain and the KSP repeat motif of the neurofilament protein neurofilament-H
    • Dong D.L., Xu Z.S., Hart G.W., Cleveland D.W. Cytoplasmic O-GlcNAc modification of the head domain and the KSP repeat motif of the neurofilament protein neurofilament-H. J Biol Chem 1996, 271:20845-20852.
    • (1996) J Biol Chem , vol.271 , pp. 20845-20852
    • Dong, D.L.1    Xu, Z.S.2    Hart, G.W.3    Cleveland, D.W.4
  • 21
    • 77649233213 scopus 로고    scopus 로고
    • Aluminum induces neurofilament aggregation by stabilizing cross-bridging of phosphorylated c-terminal sidearms
    • Kushkuley J., Metkar S., Chan W.K.-H., Lee S., Shea T.B. Aluminum induces neurofilament aggregation by stabilizing cross-bridging of phosphorylated c-terminal sidearms. Brain Res 2010, 1322:118-123.
    • (2010) Brain Res , vol.1322 , pp. 118-123
    • Kushkuley, J.1    Metkar, S.2    Chan, W.K.-H.3    Lee, S.4    Shea, T.B.5
  • 22
    • 0002918293 scopus 로고
    • Monoclonal antibodies distinguish phosphorylated and nonphosphorylated forms of neurofilaments in situ
    • Sternberger L.A., Sternberger N.H. Monoclonal antibodies distinguish phosphorylated and nonphosphorylated forms of neurofilaments in situ. Proc Natl Acad Sci U S A 1983, 80:6126-6130.
    • (1983) Proc Natl Acad Sci U S A , vol.80 , pp. 6126-6130
    • Sternberger, L.A.1    Sternberger, N.H.2
  • 23
    • 0037591990 scopus 로고    scopus 로고
    • Phosphorylation of the head domain of neurofilament protein (NF-M): a factor regulating topographic phosphorylation of NF-M tail domain KSP sites in neurons
    • Zheng Y.-L., Li B.-S., Veeranna Pant H.C. Phosphorylation of the head domain of neurofilament protein (NF-M): a factor regulating topographic phosphorylation of NF-M tail domain KSP sites in neurons. J Biol Chem 2003, 278:24026-24032.
    • (2003) J Biol Chem , vol.278 , pp. 24026-24032
    • Zheng, Y.-L.1    Li, B.-S.2    Veeranna Pant, H.C.3
  • 24
    • 38049121347 scopus 로고    scopus 로고
    • Regulation between O-GlcNAcylation and phosphorylation of neurofilament-M and their dysregulation in Alzheimer disease
    • Deng Y., Li B., Liu F., Iqbal K., Grundke-Iqbal I., Brandt R., Gong C.-X. Regulation between O-GlcNAcylation and phosphorylation of neurofilament-M and their dysregulation in Alzheimer disease. FASEB J 2008, 22:138-145.
    • (2008) FASEB J , vol.22 , pp. 138-145
    • Deng, Y.1    Li, B.2    Liu, F.3    Iqbal, K.4    Grundke-Iqbal, I.5    Brandt, R.6    Gong, C.-X.7
  • 25
    • 24744457321 scopus 로고    scopus 로고
    • O-glycosylation of the tail domain of neurofilament protein M in human neurons and in spinal cord tissue of a rat model of amyotrophic lateral sclerosis (ALS)
    • Lüdemann N., Clement A., Hans V.H., Leschik J., Behl C., Brandt R. O-glycosylation of the tail domain of neurofilament protein M in human neurons and in spinal cord tissue of a rat model of amyotrophic lateral sclerosis (ALS). J Biol Chem 2005, 280:31648-31658.
    • (2005) J Biol Chem , vol.280 , pp. 31648-31658
    • Lüdemann, N.1    Clement, A.2    Hans, V.H.3    Leschik, J.4    Behl, C.5    Brandt, R.6
  • 26
    • 0034474025 scopus 로고    scopus 로고
    • Fast transport of neurofilament protein along microtubules in squid axoplasm
    • Prahlad V., Helfand B.T., Langford G.M., Vale R.D., Goldman R.D. Fast transport of neurofilament protein along microtubules in squid axoplasm. J Cell Sci 2000, 113:3939-3946.
    • (2000) J Cell Sci , vol.113 , pp. 3939-3946
    • Prahlad, V.1    Helfand, B.T.2    Langford, G.M.3    Vale, R.D.4    Goldman, R.D.5
  • 27
    • 84862942453 scopus 로고    scopus 로고
    • Axonal transport of neurofilaments: a single population of intermittently moving polymers
    • Li Y., Jung P., Brown A. Axonal transport of neurofilaments: a single population of intermittently moving polymers. J Neurosci 2012, 32:746-758.
    • (2012) J Neurosci , vol.32 , pp. 746-758
    • Li, Y.1    Jung, P.2    Brown, A.3
  • 28
    • 70349097723 scopus 로고    scopus 로고
    • Neurofilaments form a highly stable stationary cytoskeleton after reaching a critical level in axons
    • Yuan A., Sasaki T., Rao M.V., Kumar A., Kanumuri V., Dunlop D.S., Liem R.K., Nixon R.A. Neurofilaments form a highly stable stationary cytoskeleton after reaching a critical level in axons. J Neurosci 2009, 29:11316-11329.
    • (2009) J Neurosci , vol.29 , pp. 11316-11329
    • Yuan, A.1    Sasaki, T.2    Rao, M.V.3    Kumar, A.4    Kanumuri, V.5    Dunlop, D.S.6    Liem, R.K.7    Nixon, R.A.8
  • 29
    • 0035164218 scopus 로고    scopus 로고
    • The predominant form in which neurofilament subunits undergo axonal transport varies during axonal initiation, elongation, and maturation
    • Yabe J.T., Chan W.K., Chylinski T.M., Lee S., Pimenta A.F., Shea T.B. The predominant form in which neurofilament subunits undergo axonal transport varies during axonal initiation, elongation, and maturation. Cell Motil Cytoskeleton 2001, 48:61-83.
    • (2001) Cell Motil Cytoskeleton , vol.48 , pp. 61-83
    • Yabe, J.T.1    Chan, W.K.2    Chylinski, T.M.3    Lee, S.4    Pimenta, A.F.5    Shea, T.B.6
  • 30
    • 84872595572 scopus 로고    scopus 로고
    • A critical reevaluation of the stationary axonal cytoskeleton hypothesis
    • Brown A., Jung P. A critical reevaluation of the stationary axonal cytoskeleton hypothesis. Cytoskeleton (Hoboken) 2013, 70:1-11.
    • (2013) Cytoskeleton (Hoboken) , vol.70 , pp. 1-11
    • Brown, A.1    Jung, P.2
  • 31
    • 84897541945 scopus 로고    scopus 로고
    • Deciphering the axonal transport kinetics of neurofilaments using the fluorescence photoactivation pulse-escape method
    • Li Y., Brown A., Jung P. Deciphering the axonal transport kinetics of neurofilaments using the fluorescence photoactivation pulse-escape method. Phys Biol 2014, 11:026001.
    • (2014) Phys Biol , vol.11 , pp. 026001
    • Li, Y.1    Brown, A.2    Jung, P.3
  • 32
    • 84863785565 scopus 로고    scopus 로고
    • Neurofilaments are flexible polymers that often fold and unfold, but they move in a fully extended configuration
    • Taylor N.J., Wang L., Brown A. Neurofilaments are flexible polymers that often fold and unfold, but they move in a fully extended configuration. Cytoskeleton (Hoboken) 2012, 69:535-544.
    • (2012) Cytoskeleton (Hoboken) , vol.69 , pp. 535-544
    • Taylor, N.J.1    Wang, L.2    Brown, A.3
  • 33
    • 0026580004 scopus 로고
    • Local modulation of neurofilament phosphorylation, axonal caliber, and slow axonal transport by myelinating Schwann cells
    • De Waegh S.M., Lee V.M.-Y., Brady S.T. Local modulation of neurofilament phosphorylation, axonal caliber, and slow axonal transport by myelinating Schwann cells. Cell 1992, 68:451-463.
    • (1992) Cell , vol.68 , pp. 451-463
    • De Waegh, S.M.1    Lee, V.M.-Y.2    Brady, S.T.3
  • 34
    • 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. Absence of the mid-sized neurofilament subunit decreases axonal calibers, levels of light neurofilament (NF-L), and neurofilament content. J Cell Biol 1998, 141:727-739.
    • (1998) J Cell Biol , vol.141 , pp. 727-739
    • Elder, G.A.1
  • 35
    • 0031263931 scopus 로고    scopus 로고
    • Delayed maturation of regenerating myelinated axons in mice lacking neurofilaments
    • Zhu Q., Couillard-Després S., Julien J.P. Delayed maturation of regenerating myelinated axons in mice lacking neurofilaments. Exp Neurol 1997, 148:299-316.
    • (1997) Exp Neurol , vol.148 , pp. 299-316
    • Zhu, Q.1    Couillard-Després, S.2    Julien, J.P.3
  • 37
    • 0032487502 scopus 로고    scopus 로고
    • Requirement of heavy neurofilament subunit in the development of axons with large calibers
    • Elder G.A. Requirement of heavy neurofilament subunit in the development of axons with large calibers. J Cell Biol 1998, 143:195-205.
    • (1998) J Cell Biol , vol.143 , pp. 195-205
    • Elder, G.A.1
  • 39
    • 84860318065 scopus 로고    scopus 로고
    • Expansion of neurofilament medium C terminus increases axonal diameter independent of increases in conduction velocity or myelin thickness
    • Barry D.M., Stevenson W., Bober B.G., Wiese P.J., Dale J.M., Barry G.S., Byers N.S., Strope J.D., Chang R., Schulz D.J., et al. Expansion of neurofilament medium C terminus increases axonal diameter independent of increases in conduction velocity or myelin thickness. J Neurosci 2012, 32:6209-6219.
    • (2012) J Neurosci , vol.32 , pp. 6209-6219
    • Barry, D.M.1    Stevenson, W.2    Bober, B.G.3    Wiese, P.J.4    Dale, J.M.5    Barry, G.S.6    Byers, N.S.7    Strope, J.D.8    Chang, R.9    Schulz, D.J.10
  • 40
    • 70350365509 scopus 로고    scopus 로고
    • Targeted inactivation of a developmentally regulated neural plectin isoform (plectin 1c) in mice leads to reduced motor nerve conduction velocity
    • Fuchs P., Zörer M., Reipert S., Rezniczek G.A., Propst F., Walko G., Fischer I., Bauer J., Leschnik M.W., Lüscher B., et al. Targeted inactivation of a developmentally regulated neural plectin isoform (plectin 1c) in mice leads to reduced motor nerve conduction velocity. J Biol Chem 2009, 284:26502-26509.
    • (2009) J Biol Chem , vol.284 , pp. 26502-26509
    • Fuchs, P.1    Zörer, M.2    Reipert, S.3    Rezniczek, G.A.4    Propst, F.5    Walko, G.6    Fischer, I.7    Bauer, J.8    Leschnik, M.W.9    Lüscher, B.10
  • 41
    • 0034576145 scopus 로고    scopus 로고
    • Electrophysiological properties of axons in mice lacking neurofilament subunit genes: disparity between conduction velocity and axon diameter in absence of NF-H
    • Križ J., Zhu Q., Julien J.-P., Padjen A.L. Electrophysiological properties of axons in mice lacking neurofilament subunit genes: disparity between conduction velocity and axon diameter in absence of NF-H. Brain Res 2000, 885:32-44.
    • (2000) Brain Res , vol.885 , pp. 32-44
    • Križ, J.1    Zhu, Q.2    Julien, J.-P.3    Padjen, A.L.4
  • 43
    • 76249091047 scopus 로고    scopus 로고
    • The polymer brush model of neurofilament projections: effect of protein composition
    • Zhulina E.B., Leermakers F.A.M. The polymer brush model of neurofilament projections: effect of protein composition. Biophys J 2010, 98:462-469.
    • (2010) Biophys J , vol.98 , pp. 462-469
    • Zhulina, E.B.1    Leermakers, F.A.M.2
  • 44
    • 77955660310 scopus 로고    scopus 로고
    • How the projection domains of NF-L and alpha-internexin determine the conformations of NF-M and NF-H in neurofilaments
    • Leermakers F.A.M., Zhulina E.B. How the projection domains of NF-L and alpha-internexin determine the conformations of NF-M and NF-H in neurofilaments. Eur Biophys J 2010, 39:1323-1334.
    • (2010) Eur Biophys J , vol.39 , pp. 1323-1334
    • Leermakers, F.A.M.1    Zhulina, E.B.2
  • 45
    • 79251595937 scopus 로고    scopus 로고
    • Phosphorylation-mediated conformational changes in the mouse neurofilament architecture: insight from a neurofilament brush model
    • Stevenson W., Chang R., Gebremichael Y. Phosphorylation-mediated conformational changes in the mouse neurofilament architecture: insight from a neurofilament brush model. J Mol Biol 2011, 405:1101-1118.
    • (2011) J Mol Biol , vol.405 , pp. 1101-1118
    • Stevenson, W.1    Chang, R.2    Gebremichael, Y.3
  • 46
    • 84872064426 scopus 로고    scopus 로고
    • Effects of molecular model, ionic strength, divalent ions, and hydrophobic interaction on human neurofilament conformation
    • Lee J., Kim S., Chang R., Jayanthi L., Gebremichael Y. Effects of molecular model, ionic strength, divalent ions, and hydrophobic interaction on human neurofilament conformation. J Chem Phys 2013, 138:015103.
    • (2013) J Chem Phys , vol.138 , pp. 015103
    • Lee, J.1    Kim, S.2    Chang, R.3    Jayanthi, L.4    Gebremichael, Y.5
  • 47
    • 67651172762 scopus 로고    scopus 로고
    • Structural properties of neurofilament sidearms: sequence-based modeling of neurofilament architecture
    • Chang R., Kwak Y., Gebremichael Y. Structural properties of neurofilament sidearms: sequence-based modeling of neurofilament architecture. J Mol Biol 2009, 391:648-660.
    • (2009) J Mol Biol , vol.391 , pp. 648-660
    • Chang, R.1    Kwak, Y.2    Gebremichael, Y.3
  • 48
    • 84922110205 scopus 로고    scopus 로고
    • Monte-Carlo Simulation of Neurofilament Brush
    • (in press)
    • Jeong S.M., Zhou X., Zhulina E.B., Jho Y. Monte-Carlo Simulation of Neurofilament Brush. Israel J chem 2014, (in press). 10.1002/ijch.201400139.
    • (2014) Israel J chem
    • Jeong, S.M.1    Zhou, X.2    Zhulina, E.B.3    Jho, Y.4
  • 49
    • 79958775126 scopus 로고    scopus 로고
    • Interactions between planar grafted neurofilament side-arms
    • Stevens M.J., Hoh J.H. Interactions between planar grafted neurofilament side-arms. J Phys Chem B 2011, 115:7541-7549.
    • (2011) J Phys Chem B , vol.115 , pp. 7541-7549
    • Stevens, M.J.1    Hoh, J.H.2
  • 50
    • 77954523044 scopus 로고    scopus 로고
    • Conformational dynamics of neurofilament side-arms
    • Stevens M.J., Hoh J.H. Conformational dynamics of neurofilament side-arms. J Phys Chem B 2010, 114:8879-8886.
    • (2010) J Phys Chem B , vol.114 , pp. 8879-8886
    • Stevens, M.J.1    Hoh, J.H.2
  • 51
    • 84879553420 scopus 로고    scopus 로고
    • Conformational properties of interacting neurofilaments: Monte Carlo simulations of cylindrically grafted apposing neurofilament brushes
    • Jayanthi L., Stevenson W., Kwak Y., Chang R., Gebremichael Y. Conformational properties of interacting neurofilaments: Monte Carlo simulations of cylindrically grafted apposing neurofilament brushes. J Biol Phys 2013, 39:343-362.
    • (2013) J Biol Phys , vol.39 , pp. 343-362
    • Jayanthi, L.1    Stevenson, W.2    Kwak, Y.3    Chang, R.4    Gebremichael, Y.5
  • 52
    • 72449208673 scopus 로고    scopus 로고
    • Gel-expanded to gel-condensed transition in neurofilament networks revealed by direct force measurements
    • Beck R., Deek J., Jones J.B., Safinya C.R. Gel-expanded to gel-condensed transition in neurofilament networks revealed by direct force measurements. Nat Mater 2010, 9:40-46.
    • (2010) Nat Mater , vol.9 , pp. 40-46
    • Beck, R.1    Deek, J.2    Jones, J.B.3    Safinya, C.R.4
  • 53
    • 47749130759 scopus 로고    scopus 로고
    • Interplay between liquid crystalline and isotropic gels in self-assembled neurofilament networks
    • Jones J.B., Safinya C.R. Interplay between liquid crystalline and isotropic gels in self-assembled neurofilament networks. Biophys J 2008, 95:823-835.
    • (2008) Biophys J , vol.95 , pp. 823-835
    • Jones, J.B.1    Safinya, C.R.2
  • 54
    • 84881170268 scopus 로고    scopus 로고
    • Neurofilament sidearms modulate parallel and crossed-filament orientations inducing nematic to isotropic and re-entrant birefringent hydrogels
    • Deek J., Chung P.J., Kayser J., Bausch A.R., Safinya C.R. Neurofilament sidearms modulate parallel and crossed-filament orientations inducing nematic to isotropic and re-entrant birefringent hydrogels. Nat Commun 2013, 4:2224.
    • (2013) Nat Commun , vol.4 , pp. 2224
    • Deek, J.1    Chung, P.J.2    Kayser, J.3    Bausch, A.R.4    Safinya, C.R.5
  • 55
    • 84866714885 scopus 로고    scopus 로고
    • Structures and interactions in bottlebrush neurofilaments: the role of charged disordered proteins in forming hydrogel networks
    • Beck R., Deek J., Safinya C.R. Structures and interactions in bottlebrush neurofilaments: the role of charged disordered proteins in forming hydrogel networks. Biochem Soc Trans 2012, 40:1027-1031.
    • (2012) Biochem Soc Trans , vol.40 , pp. 1027-1031
    • Beck, R.1    Deek, J.2    Safinya, C.R.3
  • 56
  • 58
    • 77951525622 scopus 로고    scopus 로고
    • Nanomechanics of vimentin intermediate filament networks
    • Köster S., Lin Y.-C., Herrmann H., Weitz D.A. Nanomechanics of vimentin intermediate filament networks. Soft Matter 2010, 6:1910.
    • (2010) Soft Matter , vol.6 , pp. 1910
    • Köster, S.1    Lin, Y.-C.2    Herrmann, H.3    Weitz, D.A.4
  • 59
    • 84877756059 scopus 로고    scopus 로고
    • Nonlinear elasticity from single chain to networks and gels
    • Carrillo J.-M.Y., MacKintosh F.C., Dobrynin A.V. Nonlinear elasticity from single chain to networks and gels. Macromolecules 2013, 46:3679-3692.
    • (2013) Macromolecules , vol.46 , pp. 3679-3692
    • Carrillo, J.-M.Y.1    MacKintosh, F.C.2    Dobrynin, A.V.3
  • 61
    • 84897597282 scopus 로고    scopus 로고
    • Impact of ion valency on the assembly of vimentin studied by quantitative small angle X-ray scattering
    • Brennich M.E., Bauch S., Vainio U., Wedig T., Herrmann H., Köster S. Impact of ion valency on the assembly of vimentin studied by quantitative small angle X-ray scattering. Soft Matter 2014, 10:2059.
    • (2014) Soft Matter , vol.10 , pp. 2059
    • Brennich, M.E.1    Bauch, S.2    Vainio, U.3    Wedig, T.4    Herrmann, H.5    Köster, S.6
  • 63
    • 84888321129 scopus 로고    scopus 로고
    • Material control of stem cell differentiation: challenges in nano-characterization
    • Dingal P.D.P., Discher D.E. Material control of stem cell differentiation: challenges in nano-characterization. Curr Opin Biotechnol 2014, 28:46-50.
    • (2014) Curr Opin Biotechnol , vol.28 , pp. 46-50
    • Dingal, P.D.P.1    Discher, D.E.2
  • 64
    • 84891771576 scopus 로고    scopus 로고
    • Substrate stiffness regulates solubility of cellular vimentin
    • Murray M.E., Mendez M.G., Janmey P.A. Substrate stiffness regulates solubility of cellular vimentin. Mol Biol Cell 2014, 25:87-94.
    • (2014) Mol Biol Cell , vol.25 , pp. 87-94
    • Murray, M.E.1    Mendez, M.G.2    Janmey, P.A.3
  • 65
    • 0021950978 scopus 로고
    • Transient expression of a neurofilament protein by replicating neuroepithelial cells of the embryonic chick brain
    • Bennett G.S., DiLullo C. Transient expression of a neurofilament protein by replicating neuroepithelial cells of the embryonic chick brain. Dev Biol 1985, 107:107-127.
    • (1985) Dev Biol , vol.107 , pp. 107-127
    • Bennett, G.S.1    DiLullo, C.2
  • 66
    • 84876465628 scopus 로고    scopus 로고
    • Molecular cloning and characterization of chicken neuronal intermediate filament protein α-internexin
    • Liu C.-H., Chien C.-L. Molecular cloning and characterization of chicken neuronal intermediate filament protein α-internexin. J Comp Neurol 2013, 521:2147-2164.
    • (2013) J Comp Neurol , vol.521 , pp. 2147-2164
    • Liu, C.-H.1    Chien, C.-L.2
  • 67
    • 0025190642 scopus 로고
    • CNS stem cells express a new class of intermediate filament protein
    • Lendahl U., Zimmerman L.B., McKay R.D.G. CNS stem cells express a new class of intermediate filament protein. Cell 1990, 60:585-595.
    • (1990) Cell , vol.60 , pp. 585-595
    • Lendahl, U.1    Zimmerman, L.B.2    McKay, R.D.G.3
  • 68
    • 0019968002 scopus 로고
    • Differential expression of neurofilament triplet proteins in brain development
    • Shaw G., Weber K. Differential expression of neurofilament triplet proteins in brain development. Nature 1982, 298:277-279.
    • (1982) Nature , vol.298 , pp. 277-279
    • Shaw, G.1    Weber, K.2
  • 70
    • 0029670953 scopus 로고    scopus 로고
    • α-Internexin is the only neuronal intermediate filament expressed in developing cerebellar granule neurons
    • Chien C.L., Mason C.A., Liem R.K. α-Internexin is the only neuronal intermediate filament expressed in developing cerebellar granule neurons. J Neurobiol 1996, 29:304-318.
    • (1996) J Neurobiol , vol.29 , pp. 304-318
    • Chien, C.L.1    Mason, C.A.2    Liem, R.K.3
  • 71
    • 41949103193 scopus 로고    scopus 로고
    • The type III neurofilament peripherin is expressed in the tuberomammillary neurons of the mouse
    • Eriksson K.S., Zhang S., Lin L., Larivière R.C., Julien J.-P., Mignot E. The type III neurofilament peripherin is expressed in the tuberomammillary neurons of the mouse. BMC Neurosci 2008, 9:26.
    • (2008) BMC Neurosci , vol.9 , pp. 26
    • Eriksson, K.S.1    Zhang, S.2    Lin, L.3    Larivière, R.C.4    Julien, J.-P.5    Mignot, E.6
  • 72
    • 0021261943 scopus 로고
    • Organization of mammalian neurofilament polypeptides within the neuronal cytoskeleton
    • Hirokawa N., Glicksman M.A., Willard M.B. Organization of mammalian neurofilament polypeptides within the neuronal cytoskeleton. J Cell Biol 1984, 98:1523-1536.
    • (1984) J Cell Biol , vol.98 , pp. 1523-1536
    • Hirokawa, N.1    Glicksman, M.A.2    Willard, M.B.3
  • 73
    • 0344096498 scopus 로고    scopus 로고
    • Characterization of distinct early assembly units of different intermediate filament proteins
    • Herrmann H., Häner M., Brettel M., Ku N.O., Aebi U. Characterization of distinct early assembly units of different intermediate filament proteins. J Mol Biol 1999, 286:1403-1420.
    • (1999) J Mol Biol , vol.286 , pp. 1403-1420
    • Herrmann, H.1    Häner, M.2    Brettel, M.3    Ku, N.O.4    Aebi, U.5
  • 75
    • 0023689454 scopus 로고
    • Structure of the peripheral domains of neurofilaments revealed by low angle rotary shadowing
    • Hisanaga S., Hirokawa N. Structure of the peripheral domains of neurofilaments revealed by low angle rotary shadowing. J Mol Biol 1988, 202:297-305.
    • (1988) J Mol Biol , vol.202 , pp. 297-305
    • Hisanaga, S.1    Hirokawa, N.2
  • 76
    • 73449137883 scopus 로고    scopus 로고
    • Post-transcriptional control of neurofilaments: new roles in development, regeneration and neurodegenerative disease
    • Szaro B.G., Strong M.J. Post-transcriptional control of neurofilaments: new roles in development, regeneration and neurodegenerative disease. Trends Neurosci 2010, 33:27-37.
    • (2010) Trends Neurosci , vol.33 , pp. 27-37
    • Szaro, B.G.1    Strong, M.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.