메뉴 건너뛰기




Volumn 360, Issue 3, 2015, Pages 609-620

Neurofilament dynamics and involvement in neurological disorders

Author keywords

Amyotrophic Lateral Sclerosis; Charcot Marie Tooth disease; Neurofilaments; Peripheral neuropathies

Indexed keywords

HEAT SHOCK PROTEIN 27; NEUROFILAMENT PROTEIN; PROTEIN KINASE N; UBIQUITIN PROTEIN LIGASE E3;

EID: 84930274621     PISSN: 0302766X     EISSN: 14320878     Source Type: Journal    
DOI: 10.1007/s00441-014-2082-7     Document Type: Review
Times cited : (75)

References (161)
  • 2
    • 31144453053 scopus 로고    scopus 로고
    • A mutation in the small heat-shock protein HSPB1 leading to distal hereditary motor neuronopathy disrupts neurofilament assembly and the axonal transport of specific cellular cargoes
    • COI: 1:CAS:528:DC%2BD28XktF2ltQ%3D%3D, PID: 16368711
    • Ackerley S, James PA, Kalli A, French S, Davies KE, Talbot K (2006) A mutation in the small heat-shock protein HSPB1 leading to distal hereditary motor neuronopathy disrupts neurofilament assembly and the axonal transport of specific cellular cargoes. Hum Mol Genet 15:347–354
    • (2006) Hum Mol Genet , vol.15 , pp. 347-354
    • Ackerley, S.1    James, P.A.2    Kalli, A.3    French, S.4    Davies, K.E.5    Talbot, K.6
  • 5
    • 0030698718 scopus 로고    scopus 로고
    • Heterodimeric associations between neuronal intermediate filament proteins
    • COI: 1:CAS:528:DyaK2sXnvFSktL4%3D, PID: 9388258
    • Athlan ES, Mushynski WE (1997) Heterodimeric associations between neuronal intermediate filament proteins. J Biol Chem 272:31073–31078
    • (1997) J Biol Chem , vol.272 , pp. 31073-31078
    • Athlan, E.S.1    Mushynski, W.E.2
  • 6
    • 69449090498 scopus 로고    scopus 로고
    • Mutation of SYNE-1, encoding an essential component of the nuclear lamina, is responsible for autosomal recessive arthrogryposis
    • COI: 1:CAS:528:DC%2BD1MXhtVehurbO, PID: 19542096
    • Attali R, Warwar N, Israel A, Gurt I, McNally E, Puckelwartz M, Glick B, Nevo Y, Ben-Neriah Z, Melki J (2009) Mutation of SYNE-1, encoding an essential component of the nuclear lamina, is responsible for autosomal recessive arthrogryposis. Hum Mol Genet 18:3462–3469
    • (2009) Hum Mol Genet , vol.18 , pp. 3462-3469
    • Attali, R.1    Warwar, N.2    Israel, A.3    Gurt, I.4    McNally, E.5    Puckelwartz, M.6    Glick, B.7    Nevo, Y.8    Ben-Neriah, Z.9    Melki, J.10
  • 7
    • 0025313509 scopus 로고
    • Individual microtubules in the axon consist of domains that differ in both composition and stability
    • COI: 1:CAS:528:DyaK3cXkvFGiur8%3D, PID: 2199458
    • Baas PW, Black MM (1990) Individual microtubules in the axon consist of domains that differ in both composition and stability. J Cell Biol 111:495–509
    • (1990) J Cell Biol , vol.111 , pp. 495-509
    • Baas, P.W.1    Black, M.M.2
  • 8
    • 0027510394 scopus 로고
    • Sites of microtubule stabilization for the axon
    • COI: 1:STN:280:DyaK3s3ktVagtQ%3D%3D, PID: 8478694
    • Baas PW, Ahmad FJ, Pienkowski TP, Brown A, Black MM (1993) Sites of microtubule stabilization for the axon. J Neurosci 13:2177–2185
    • (1993) J Neurosci , vol.13 , pp. 2177-2185
    • Baas, P.W.1    Ahmad, F.J.2    Pienkowski, T.P.3    Brown, A.4    Black, M.M.5
  • 9
    • 50149093632 scopus 로고    scopus 로고
    • Deficiency in ubiquitin ligase TRIM2 causes accumulation of neurofilament light chain and neurodegeneration
    • COI: 1:CAS:528:DC%2BD1cXhtVChu7%2FF, PID: 18687884
    • Balastik M, Ferraguti F, Pires-da Silva A, Lee TH, Alvarez-Bolado G, Lu KP, Gruss P (2008) Deficiency in ubiquitin ligase TRIM2 causes accumulation of neurofilament light chain and neurodegeneration. Proc Natl Acad Sci U S A 105:12016–12021
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 12016-12021
    • Balastik, M.1    Ferraguti, F.2    Pires-da Silva, A.3    Lee, T.H.4    Alvarez-Bolado, G.5    Lu, K.P.6    Gruss, P.7
  • 11
    • 0005541930 scopus 로고    scopus 로고
    • Association of actin filaments with axonal microtubule tracts
    • COI: 1:CAS:528:DC%2BD3cXht1Kmu7w%3D, PID: 10590510
    • Bearer EL, Reese TS (1999) Association of actin filaments with axonal microtubule tracts. J Neurocytol 28:85–98
    • (1999) J Neurocytol , vol.28 , pp. 85-98
    • Bearer, E.L.1    Reese, T.S.2
  • 12
    • 0033213289 scopus 로고    scopus 로고
    • Squid axoplasm supports the retrograde axonal transport of herpes simplex virus
    • COI: 1:STN:280:DC%2BD3c%2FktFWguw%3D%3D, PID: 10573844
    • Bearer EL, Schlief ML, Breakefield XO, Schuback DE, Reese TS, LaVail JH (1999) Squid axoplasm supports the retrograde axonal transport of herpes simplex virus. Biol Bull 197:257–258
    • (1999) Biol Bull , vol.197 , pp. 257-258
    • Bearer, E.L.1    Schlief, M.L.2    Breakefield, X.O.3    Schuback, D.E.4    Reese, T.S.5    LaVail, J.H.6
  • 13
    • 0037118933 scopus 로고    scopus 로고
    • Induction of peripherin expression in subsets of brain neurons after lesion injury or cerebral ischemia
    • COI: 1:CAS:528:DC%2BD38Xls1ansrY%3D, PID: 12137917
    • Beaulieu JM, Kriz J, Julien JP (2002) Induction of peripherin expression in subsets of brain neurons after lesion injury or cerebral ischemia. Brain Res 946:153–161
    • (2002) Brain Res , vol.946 , pp. 153-161
    • Beaulieu, J.M.1    Kriz, J.2    Julien, J.P.3
  • 14
    • 72449208673 scopus 로고    scopus 로고
    • Gel-expanded to gel-condensed transition in neurofilament networks revealed by direct force measurements
    • COI: 1:CAS:528:DC%2BD1MXhsFOnsrvL, PID: 19915555
    • Beck R, Deek J, Jones JB, Safinya CR (2010) Gel-expanded to gel-condensed transition in neurofilament networks revealed by direct force measurements. Nat Mater 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
  • 15
    • 0028022870 scopus 로고
    • Copper/zinc superoxide dismutase mRNA levels are increased in sporadic amyotrophic lateral sclerosis motorneurons
    • COI: 1:CAS:528:DyaK2cXmt1Oru7s%3D, PID: 7820674
    • Bergeron C, Muntasser S, Somerville MJ, Weyer L, Percy ME (1994) Copper/zinc superoxide dismutase mRNA levels are increased in sporadic amyotrophic lateral sclerosis motorneurons. Brain Res 659:272–276
    • (1994) Brain Res , vol.659 , pp. 272-276
    • Bergeron, C.1    Muntasser, S.2    Somerville, M.J.3    Weyer, L.4    Percy, M.E.5
  • 16
    • 0026502693 scopus 로고
    • Peripherin: an islet antigen that is cross-reactive with nonobese diabetic mouse class II gene products
    • COI: 1:CAS:528:DyaK38XhtVChsLY%3D, PID: 1729686
    • Boitard C, Villa MC, Becourt C, Gia HP, Huc C, Sempe P, Portier MM, Bach JF (1992) Peripherin: an islet antigen that is cross-reactive with nonobese diabetic mouse class II gene products. Proc Natl Acad Sci U S A 89:172–176
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 172-176
    • Boitard, C.1    Villa, M.C.2    Becourt, C.3    Gia, H.P.4    Huc, C.5    Sempe, P.6    Portier, M.M.7    Bach, J.F.8
  • 17
    • 0018766158 scopus 로고
    • Electromyography and nerve conduction studies in Friedreich’s ataxia and autosomal recessive spastic ataxia of Charlevoix-Saguenay (ARSACS)
    • COI: 1:STN:280:DyaL3c%2Fit1CmsA%3D%3D, PID: 487308
    • Bouchard JP, Barbeau A, Bouchard R, Bouchard RW (1979) Electromyography and nerve conduction studies in Friedreich’s ataxia and autosomal recessive spastic ataxia of Charlevoix-Saguenay (ARSACS). Can J Neurol Sci 6:185–189
    • (1979) Can J Neurol Sci , vol.6 , pp. 185-189
    • Bouchard, J.P.1    Barbeau, A.2    Bouchard, R.3    Bouchard, R.W.4
  • 19
    • 0030930279 scopus 로고    scopus 로고
    • Visualization of single neurofilaments by immunofluorescence microscopy of splayed axonal cytoskeletons
    • COI: 1:STN:280:DyaK2svntVOmug%3D%3D, PID: 9331218
    • Brown A (1997) Visualization of single neurofilaments by immunofluorescence microscopy of splayed axonal cytoskeletons. Cell Motil Cytoskeleton 38:133–145
    • (1997) Cell Motil Cytoskeleton , vol.38 , pp. 133-145
    • Brown, A.1
  • 20
    • 0027537548 scopus 로고
    • Composite microtubules of the axon: quantitative analysis of tyrosinated and acetylated tubulin along individual axonal microtubules
    • COI: 1:CAS:528:DyaK3sXktVGnu7o%3D, PID: 8505364
    • Brown A, Li Y, Slaughter T, Black MM (1993) Composite microtubules of the axon: quantitative analysis of tyrosinated and acetylated tubulin along individual axonal microtubules. J Cell Sci 104(Pt 2):339–352
    • (1993) J Cell Sci , vol.104 , pp. 339-352
    • Brown, A.1    Li, Y.2    Slaughter, T.3    Black, M.M.4
  • 21
    • 0031718564 scopus 로고    scopus 로고
    • Neurofilament-L homopolymers are less mechanically stable than native neurofilaments
    • COI: 1:CAS:528:DyaK1cXms1Wit7Y%3D
    • Brown HG, Troncoso JC, Hoh JH (1998) Neurofilament-L homopolymers are less mechanically stable than native neurofilaments. J Microsc 191:229–237
    • (1998) J Microsc , vol.191 , pp. 229-237
    • Brown, H.G.1    Troncoso, J.C.2    Hoh, J.H.3
  • 22
    • 24344435089 scopus 로고    scopus 로고
    • Stochastic simulation of neurofilament transport in axons: the “stop-and-go” hypothesis
    • COI: 1:CAS:528:DC%2BD2MXpvFKlsbs%3D, PID: 16000374
    • Brown A, Wang L, Jung P (2005) Stochastic simulation of neurofilament transport in axons: the “stop-and-go” hypothesis. Mol Biol Cell 16:4243–4255
    • (2005) Mol Biol Cell , vol.16 , pp. 4243-4255
    • Brown, A.1    Wang, L.2    Jung, P.3
  • 24
    • 0026544718 scopus 로고
    • Neurofilaments are prominent in bullfrog olfactory axons but are rarely seen in those of the tiger salamander, Ambystoma tigrinum
    • COI: 1:STN:280:DyaK383ltV2lug%3D%3D, PID: 1578003
    • Burton PR, Wentz MA (1992) Neurofilaments are prominent in bullfrog olfactory axons but are rarely seen in those of the tiger salamander, Ambystoma tigrinum. J Comp Neurol 317:396–406
    • (1992) J Comp Neurol , vol.317 , pp. 396-406
    • Burton, P.R.1    Wentz, M.A.2
  • 25
    • 0022550636 scopus 로고    scopus 로고
    • Eagles PAM(1986) Chemical cross-linking analyses of ox neurofilaments
    • Carden MJ, Eagles PAM(1986) Chemical cross-linking analyses of ox neurofilaments. Biochem J 234:587–591
    • Biochem J , vol.234 , pp. 587-591
    • Carden, M.J.1
  • 26
    • 0014336826 scopus 로고
    • Proximal axonal enlargement in motor neuron disease
    • COI: 1:STN:280:DyaF1M%2FisFektA%3D%3D, PID: 4176657
    • Carpenter S (1968) Proximal axonal enlargement in motor neuron disease. Neurology 18:841–851
    • (1968) Neurology , vol.18 , pp. 841-851
    • Carpenter, S.1
  • 27
    • 69749110327 scopus 로고    scopus 로고
    • The proteasome-associated deubiquitinating enzyme Usp14 is essential for the maintenance of synaptic ubiquitin levels and the development of neuromuscular junctions
    • Chen PC, Qin LN, Li XM, Walters BJ, Wilson JA, Mei L, Wilson SM (2009) The proteasome-associated deubiquitinating enzyme Usp14 is essential for the maintenance of synaptic ubiquitin levels and the development of neuromuscular junctions. J Neurosci: Off J Soc Neurosci 29:10909–10919
    • (2009) J Neurosci: Off J Soc Neurosci , vol.29 , pp. 10909-10919
    • Chen, P.C.1    Qin, L.N.2    Li, X.M.3    Walters, B.J.4    Wilson, J.A.5    Mei, L.6    Wilson, S.M.7
  • 29
    • 0021137693 scopus 로고
    • Initial expression of neurofilaments and vimentin in the central and peripheral nervous system of the mouse embryo in vivo
    • COI: 1:STN:280:DyaL2c3ptFGqtw%3D%3D, PID: 6432971
    • Cochard P, Paulin D (1984) Initial expression of neurofilaments and vimentin in the central and peripheral nervous system of the mouse embryo in vivo. J Neurosci 4:2080–2094
    • (1984) J Neurosci , vol.4 , pp. 2080-2094
    • Cochard, P.1    Paulin, D.2
  • 30
    • 0023657192 scopus 로고
    • Discrete soluble forms of middle and high molecular weight neurofilament proteins in dilute aqueous buffers
    • COI: 1:CAS:528:DyaL2sXmtFekt7s%3D, PID: 3119596
    • Cohlberg JA, Hajarian H, Sainte-Marie S (1987) Discrete soluble forms of middle and high molecular weight neurofilament proteins in dilute aqueous buffers. J Biol Chem 262:17009–17015
    • (1987) J Biol Chem , vol.262 , pp. 17009-17015
    • Cohlberg, J.A.1    Hajarian, H.2    Sainte-Marie, S.3
  • 31
    • 0028930701 scopus 로고
    • Neurofilament protein heterotetramers as assembly intermediates
    • COI: 1:CAS:528:DyaK2MXlt1ajt7c%3D, PID: 7721855
    • Cohlberg JA, Hajarian H, Tran T, Alipourjeddi P, Noveen A (1995) Neurofilament protein heterotetramers as assembly intermediates. J Biol Chem 270:9334–9339
    • (1995) J Biol Chem , vol.270 , pp. 9334-9339
    • Cohlberg, J.A.1    Hajarian, H.2    Tran, T.3    Alipourjeddi, P.4    Noveen, A.5
  • 32
    • 66349104792 scopus 로고    scopus 로고
    • Intermediate filaments exchange subunits along their length and elongate by end-to-end annealing
    • COI: 1:CAS:528:DC%2BD1MXntVCit7s%3D, PID: 19468066
    • Colakoglu G, Brown A (2009) Intermediate filaments exchange subunits along their length and elongate by end-to-end annealing. J Cell Biol 185:769–777
    • (2009) J Cell Biol , vol.185 , pp. 769-777
    • Colakoglu, G.1    Brown, A.2
  • 33
    • 65249107203 scopus 로고    scopus 로고
    • Microtubule assembly, organization and dynamics in axons and dendrites
    • COI: 1:CAS:528:DC%2BD1MXks12ktbk%3D, PID: 19377501
    • Conde C, Caceres A (2009) Microtubule assembly, organization and dynamics in axons and dendrites. Nat Rev Neurosci 10:319–332
    • (2009) Nat Rev Neurosci , vol.10 , pp. 319-332
    • Conde, C.1    Caceres, A.2
  • 35
    • 84868528423 scopus 로고    scopus 로고
    • Neurofilament phosphorylation during development and disease: which came first, the phosphorylation or the accumulation?
    • PID: 22570767
    • Dale JM, Garcia ML (2012) Neurofilament phosphorylation during development and disease: which came first, the phosphorylation or the accumulation? J Amino Acids 2012:382107
    • (2012) J Amino Acids , vol.2012 , pp. 382107
    • Dale, J.M.1    Garcia, M.L.2
  • 36
    • 0242304102 scopus 로고    scopus 로고
    • Monitoring of S100 homodimerization and heterodimeric interactions by the yeast two-hybrid system
    • COI: 1:CAS:528:DC%2BD3sXjt1ajsL0%3D, PID: 12645004
    • Deloulme JC, Gentil BJ, Baudier J (2003) Monitoring of S100 homodimerization and heterodimeric interactions by the yeast two-hybrid system. Microsc Res Tech 60:560–568
    • (2003) Microsc Res Tech , vol.60 , pp. 560-568
    • Deloulme, J.C.1    Gentil, B.J.2    Baudier, J.3
  • 37
    • 0030022780 scopus 로고    scopus 로고
    • Activation of protein kinase C induces neurofilament fragmentation, hyperphosphorylation of perikaryal neurofilaments and proximal dendritic swellings in cultured motor neurons
    • COI: 1:CAS:528:DyaK28XhsF2kurY%3D, PID: 8786383
    • Doroudchi MM, Durham HD (1996) Activation of protein kinase C induces neurofilament fragmentation, hyperphosphorylation of perikaryal neurofilaments and proximal dendritic swellings in cultured motor neurons. J Neuropathol Exp Neurol 55:246–256
    • (1996) J Neuropathol Exp Neurol , vol.55 , pp. 246-256
    • Doroudchi, M.M.1    Durham, H.D.2
  • 38
    • 0037324941 scopus 로고    scopus 로고
    • Proapoptosis and antiapoptosis-related molecules during postnatal pancreas development in control and nonobese diabetic mice: relationship with innervation
    • PID: 12594237
    • Durant S, Geutskens S, Van Blokland SC, Coulaud J, Alves V, Pleau JM, Versnel M, Drexhage HA, Homo-Delarche F (2003) Proapoptosis and antiapoptosis-related molecules during postnatal pancreas development in control and nonobese diabetic mice: relationship with innervation. Lab Investig 83:227–239
    • (2003) Lab Investig , vol.83 , pp. 227-239
    • Durant, S.1    Geutskens, S.2    Van Blokland, S.C.3    Coulaud, J.4    Alves, V.5    Pleau, J.M.6    Versnel, M.7    Drexhage, H.A.8    Homo-Delarche, F.9
  • 39
    • 0030777650 scopus 로고    scopus 로고
    • Aggregation of mutant Cu/Zn superoxide dismutase proteins in a culture model of ALS
    • COI: 1:CAS:528:DyaK2sXjt1Gmsb4%3D, PID: 9143265
    • Durham HD, Roy J, Dong L, Figlewicz DA (1997) Aggregation of mutant Cu/Zn superoxide dismutase proteins in a culture model of ALS. J Neuropathol Exp Neurol 56:523–530
    • (1997) J Neuropathol Exp Neurol , vol.56 , pp. 523-530
    • Durham, H.D.1    Roy, J.2    Dong, L.3    Figlewicz, D.A.4
  • 40
    • 0031972719 scopus 로고    scopus 로고
    • Splice variant-specific interaction of the NMDA receptor subunit NR1 with neuronal intermediate filaments
    • COI: 1:CAS:528:DyaK1cXlsFaisw%3D%3D, PID: 9425014
    • Ehlers MD, Fung ET, O’Brien RJ, Huganir RL (1998) Splice variant-specific interaction of the NMDA receptor subunit NR1 with neuronal intermediate filaments. J Neurosci 18:720–730
    • (1998) J Neurosci , vol.18 , pp. 720-730
    • Ehlers, M.D.1    Fung, E.T.2    O’Brien, R.J.3    Huganir, R.L.4
  • 41
    • 0032482231 scopus 로고    scopus 로고
    • Absence of the mid-sized neurofilament subunit decreases axonal calibers, levels of light neurofilament (NF-L), and neurofilament content
    • COI: 1:CAS:528:DyaK1cXivVGjsbk%3D, PID: 9566972
    • Elder GA, Friedrich VL Jr, Bosco P, Kang C, Gourov A, Tu PH, Lee VM, Lazzarini RA (1998a) 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, V.L.2    Bosco, P.3    Kang, C.4    Gourov, A.5    Tu, P.H.6    Lee, V.M.7    Lazzarini, R.A.8
  • 44
    • 0025246192 scopus 로고
    • Differential expression of two neuronal intermediate-filament proteins, peripherin and the low-molecular-mass neurofilament protein (NF-L), during the development of the rat
    • COI: 1:CAS:528:DyaK3cXitFChu7s%3D, PID: 2108230
    • Escurat M, Djabali K, Gumpel M, Gros F, Portier MM (1990) Differential expression of two neuronal intermediate-filament proteins, peripherin and the low-molecular-mass neurofilament protein (NF-L), during the development of the rat. J Neurosci 10:764–784
    • (1990) J Neurosci , vol.10 , pp. 764-784
    • Escurat, M.1    Djabali, K.2    Gumpel, M.3    Gros, F.4    Portier, M.M.5
  • 46
    • 1942473714 scopus 로고    scopus 로고
    • Giant axon and neurofilament accumulation in Charcot-Marie-Tooth disease type 2E
    • COI: 1:STN:280:DC%2BD2c3htlyhsA%3D%3D, PID: 15111691
    • Fabrizi GM, Cavallaro T, Angiari C, Bertolasi L, Cabrini I, Ferrarini M, Rizzuto N (2004) Giant axon and neurofilament accumulation in Charcot-Marie-Tooth disease type 2E. Neurology 62:1429–1431
    • (2004) Neurology , vol.62 , pp. 1429-1431
    • Fabrizi, G.M.1    Cavallaro, T.2    Angiari, C.3    Bertolasi, L.4    Cabrini, I.5    Ferrarini, M.6    Rizzuto, N.7
  • 48
    • 0033001088 scopus 로고    scopus 로고
    • Aberrant neurofilament phosphorylation in sensory neurons of rats with diabetic neuropathy
    • COI: 1:CAS:528:DyaK1MXitFCqtb4%3D, PID: 10102707
    • Fernyhough P, Gallagher A, Averill SA, Priestley JV, Hounsom L, Patel J, Tomlinson DR (1999) Aberrant neurofilament phosphorylation in sensory neurons of rats with diabetic neuropathy. Diabetes 48:881–889
    • (1999) Diabetes , vol.48 , pp. 881-889
    • Fernyhough, P.1    Gallagher, A.2    Averill, S.A.3    Priestley, J.V.4    Hounsom, L.5    Patel, J.6    Tomlinson, D.R.7
  • 49
    • 0020394540 scopus 로고
    • Cytoplasmic actin in neuronal processes as a possible mediator of synaptic plasticity
    • COI: 1:CAS:528:DyaL38Xlsl2htb4%3D, PID: 6890558
    • Fifkova E, Delay RJ (1982) Cytoplasmic actin in neuronal processes as a possible mediator of synaptic plasticity. J Cell Biol 95:345–350
    • (1982) J Cell Biol , vol.95 , pp. 345-350
    • Fifkova, E.1    Delay, R.J.2
  • 50
    • 0028001606 scopus 로고
    • Variants of the heavy neurofilament subunit are associated with the development of amyotrophic lateral sclerosis
    • COI: 1:CAS:528:DyaK2cXmslels74%3D, PID: 7849698
    • Figlewicz DA, Krizus A, Martinoli MG, Meininger V, Dib M, Rouleau GA, Julien JP (1994) Variants of the heavy neurofilament subunit are associated with the development of amyotrophic lateral sclerosis. Hum Mol Genet 3:1757–1761
    • (1994) Hum Mol Genet , vol.3 , pp. 1757-1761
    • Figlewicz, D.A.1    Krizus, A.2    Martinoli, M.G.3    Meininger, V.4    Dib, M.5    Rouleau, G.A.6    Julien, J.P.7
  • 51
    • 0023840076 scopus 로고
    • Cytoskeleton-associated plectin: in situ localization, in vitro reconstitution, and binding to immobilized intermediate filament proteins
    • COI: 1:CAS:528:DyaL1cXhs1emsbs%3D, PID: 3346324
    • Foisner R, Leichtfried FE, Herrmann H, Small JV, Lawson D, Wiche G (1988) Cytoskeleton-associated plectin: in situ localization, in vitro reconstitution, and binding to immobilized intermediate filament proteins. J Cell Biol 106:723–733
    • (1988) J Cell Biol , vol.106 , pp. 723-733
    • Foisner, R.1    Leichtfried, F.E.2    Herrmann, H.3    Small, J.V.4    Lawson, D.5    Wiche, G.6
  • 55
    • 0027976066 scopus 로고
    • Isolation of nonobese diabetic mouse T-cells that recognize novel autoantigens involved in the early events of diabetes
    • COI: 1:CAS:528:DyaK2cXlt1Ghuw%3D%3D, PID: 8262314
    • Gelber C, Paborsky L, Singer S, McAteer D, Tisch R, Jolicoeur C, Buelow R, McDevitt H, Fathman CG (1994) Isolation of nonobese diabetic mouse T-cells that recognize novel autoantigens involved in the early events of diabetes. Diabetes 43:33–39
    • (1994) Diabetes , vol.43 , pp. 33-39
    • Gelber, C.1    Paborsky, L.2    Singer, S.3    McAteer, D.4    Tisch, R.5    Jolicoeur, C.6    Buelow, R.7    McDevitt, H.8    Fathman, C.G.9
  • 56
    • 84857708526 scopus 로고    scopus 로고
    • Normal role of the low-molecular-weight neurofilament protein in mitochondrial dynamics and disruption in Charcot-Marie-Tooth disease
    • PID: 22155564
    • Gentil BJ, Minotti S, Beange M, Baloh RH, Julien JP, Durham HD (2011) Normal role of the low-molecular-weight neurofilament protein in mitochondrial dynamics and disruption in Charcot-Marie-Tooth disease. FASEB J 26:1194–1203
    • (2011) FASEB J , vol.26 , pp. 1194-1203
    • Gentil, B.J.1    Minotti, S.2    Beange, M.3    Baloh, R.H.4    Julien, J.P.5    Durham, H.D.6
  • 57
    • 84878934230 scopus 로고    scopus 로고
    • Heterogeneity in the properties of NEFL mutants causing Charcot-Marie-Tooth disease results in differential effects on neurofilament assembly and susceptibility to intervention by the chaperone-inducer, celastrol
    • COI: 1:CAS:528:DC%2BC3sXptVyqs7w%3D, PID: 23618875
    • Gentil BJ, Mushynski WE, Durham HD (2013) Heterogeneity in the properties of NEFL mutants causing Charcot-Marie-Tooth disease results in differential effects on neurofilament assembly and susceptibility to intervention by the chaperone-inducer, celastrol. Int J Biochem Cell Biol 45:1499–1508
    • (2013) Int J Biochem Cell Biol , vol.45 , pp. 1499-1508
    • Gentil, B.J.1    Mushynski, W.E.2    Durham, H.D.3
  • 58
    • 84915811391 scopus 로고    scopus 로고
    • A two-hybrid screen identifies an unconventional role for the intermediate filament peripherin in regulating the subcellular distribution of the SNAP25 interacting protein, SIP30
    • COI: 1:CAS:528:DC%2BC2cXitVamtb3P, PID: 25113441
    • Gentil BJ, McLean JR, Xiao S, Zhao B, Durham HD, Robertson J (2014) A two-hybrid screen identifies an unconventional role for the intermediate filament peripherin in regulating the subcellular distribution of the SNAP25 interacting protein, SIP30. J Neurochem 131(5):588–601
    • (2014) J Neurochem , vol.131 , Issue.5 , pp. 588-601
    • Gentil, B.J.1    McLean, J.R.2    Xiao, S.3    Zhao, B.4    Durham, H.D.5    Robertson, J.6
  • 59
    • 0029846873 scopus 로고    scopus 로고
    • Aberrant stress-induced phosphorylation of perikaryal neurofilaments
    • COI: 1:CAS:528:DyaK28XntlamsLc%3D, PID: 8940004
    • Giasson BI, Mushynski WE (1996) Aberrant stress-induced phosphorylation of perikaryal neurofilaments. J Biol Chem 271:30404–30409
    • (1996) J Biol Chem , vol.271 , pp. 30404-30409
    • Giasson, B.I.1    Mushynski, W.E.2
  • 60
    • 0031958195 scopus 로고    scopus 로고
    • Intermediate filament disassembly in cultured dorsal root ganglion neurons is associated with amino-terminal head domain phosphorylation of specific subunits
    • COI: 1:CAS:528:DyaK1cXislSqsrs%3D, PID: 9572270
    • Giasson BI, Mushynski WE (1998) Intermediate filament disassembly in cultured dorsal root ganglion neurons is associated with amino-terminal head domain phosphorylation of specific subunits. J Neurochem 70:1869–1875
    • (1998) J Neurochem , vol.70 , pp. 1869-1875
    • Giasson, B.I.1    Mushynski, W.E.2
  • 61
    • 0030065110 scopus 로고    scopus 로고
    • Activation of cyclic AMP-dependent protein kinase in okadaic acid-treated neurons potentiates neurofilament fragmentation and stimulates phosphorylation of Ser2 in the low-molecular-mass neurofilament subunit
    • COI: 1:CAS:528:DyaK28Xht1Ohsbg%3D, PID: 8769885
    • Giasson BI, Cromlish JA, Athlan ES, Mushynski WE (1996) Activation of cyclic AMP-dependent protein kinase in okadaic acid-treated neurons potentiates neurofilament fragmentation and stimulates phosphorylation of Ser2 in the low-molecular-mass neurofilament subunit. J Neurochem 66:1207–1213
    • (1996) J Neurochem , vol.66 , pp. 1207-1213
    • Giasson, B.I.1    Cromlish, J.A.2    Athlan, E.S.3    Mushynski, W.E.4
  • 62
    • 0030046672 scopus 로고    scopus 로고
    • Assembly properties of neurofilament light chain Ser55 mutants in transfected mammalian cells
    • COI: 1:CAS:528:DyaK28Xht1Ohtrc%3D, PID: 8769898
    • Gibb BJ, Robertson J, Miller CC (1996) Assembly properties of neurofilament light chain Ser55 mutants in transfected mammalian cells. J Neurochem 66:1306–1311
    • (1996) J Neurochem , vol.66 , pp. 1306-1311
    • Gibb, B.J.1    Robertson, J.2    Miller, C.C.3
  • 63
    • 0031890760 scopus 로고    scopus 로고
    • Neuropathological abnormalities in transgenic mice harbouring a phosphorylation mutant neurofilament transgene
    • COI: 1:CAS:528:DyaK1cXmtFaltw%3D%3D, PID: 9453542
    • Gibb BJ, Brion JP, Brownlees J, Anderton BH, Miller CC (1998) Neuropathological abnormalities in transgenic mice harbouring a phosphorylation mutant neurofilament transgene. J Neurochem 70:492–500
    • (1998) J Neurochem , vol.70 , pp. 492-500
    • Gibb, B.J.1    Brion, J.P.2    Brownlees, J.3    Anderton, B.H.4    Miller, C.C.5
  • 67
    • 0025239701 scopus 로고
    • The coiled coil of in vitro assembled keratin filaments is a heterodimer of type I and II keratins: use of site-specific mutagenesis and recombinant protein expression
    • COI: 1:CAS:528:DyaK3cXhvFCju7s%3D, PID: 1691189
    • Hatzfeld M, Weber K (1990) The coiled coil of in vitro assembled keratin filaments is a heterodimer of type I and II keratins: use of site-specific mutagenesis and recombinant protein expression. J Cell Biol 110:1199–1210
    • (1990) J Cell Biol , vol.110 , pp. 1199-1210
    • Hatzfeld, M.1    Weber, K.2
  • 69
    • 0033960790 scopus 로고    scopus 로고
    • Intermediate filaments and their associates: multi-talented structural elements specifying cyto architecture and cytodynamics
    • Herrmann H, Aebi U (2000) Intermediate filaments and their associates: multi-talented structural elements specifying cyto architecture and cytodynamics. Curr Opin Cell Biol 12:79–90
    • (2000) Curr Opin Cell Biol , vol.12 , pp. 79-90
    • Herrmann, H.1    Aebi, U.2
  • 70
    • 0344096498 scopus 로고    scopus 로고
    • Characterization of distinct early assembly units of different intermediate filament proteins
    • COI: 1:CAS:528:DyaK1MXhsVCltLc%3D, PID: 10064706
    • Herrmann H, Haner M, Brettel M, Ku NO, Aebi U (1999) Characterization of distinct early assembly units of different intermediate filament proteins. J Mol Biol 286:1403–1420
    • (1999) J Mol Biol , vol.286 , pp. 1403-1420
    • Herrmann, H.1    Haner, M.2    Brettel, M.3    Ku, N.O.4    Aebi, U.5
  • 71
    • 0016541063 scopus 로고
    • The slow component of axonal transport. Identification of major structural polypeptides of the axon and their generality among mammalian neurons
    • COI: 1:CAS:528:DyaE2MXkvFaltLY%3D, PID: 49355
    • Hoffman PN, Lasek RJ (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
  • 72
    • 84879607430 scopus 로고    scopus 로고
    • Charcot-Marie-Tooth causing HSPB1 mutations increase Cdk5-mediated phosphorylation of neurofilaments
    • COI: 1:CAS:528:DC%2BC3sXhtVahurvK, PID: 23728742
    • Holmgren A, Bouhy D, De Winter V, Asselbergh B, Timmermans JP, Irobi J, Timmerman V (2013) Charcot-Marie-Tooth causing HSPB1 mutations increase Cdk5-mediated phosphorylation of neurofilaments. Acta Neuropathol 126:93–108
    • (2013) Acta Neuropathol , vol.126 , pp. 93-108
    • Holmgren, A.1    Bouhy, D.2    De Winter, V.3    Asselbergh, B.4    Timmermans, J.P.5    Irobi, J.6    Timmerman, V.7
  • 73
    • 0035882526 scopus 로고    scopus 로고
    • Attenuated neurodegenerative disease phenotype in tau transgenic mouse lacking neurofilaments
    • COI: 1:CAS:528:DC%2BD3MXlvFKmsL0%3D, PID: 11487626
    • Ishihara T, Higuchi M, Zhang B, Yoshiyama Y, Hong M, Trojanowski JQ, Lee VM (2001) Attenuated neurodegenerative disease phenotype in tau transgenic mouse lacking neurofilaments. J Neurosci 21:6026–6035
    • (2001) J Neurosci , vol.21 , pp. 6026-6035
    • Ishihara, T.1    Higuchi, M.2    Zhang, B.3    Yoshiyama, Y.4    Hong, M.5    Trojanowski, J.Q.6    Lee, V.M.7
  • 74
    • 84898606538 scopus 로고    scopus 로고
    • Analysis of novel NEFL mRNA targeting microRNAs in amyotrophic lateral sclerosis
    • PID: 24454911
    • Ishtiaq M, Campos-Melo D, Volkening K, Strong MJ (2014) Analysis of novel NEFL mRNA targeting microRNAs in amyotrophic lateral sclerosis. PLoS ONE 9:e85653
    • (2014) PLoS ONE , vol.9 , pp. e85653
    • Ishtiaq, M.1    Campos-Melo, D.2    Volkening, K.3    Strong, M.J.4
  • 75
    • 0026499998 scopus 로고
    • Phosphorylated high molecular weight neurofilament protein in the peripheral motor, sensory and sympathetic neuronal perikarya: system-dependent normal variations and changes in amyotrophic lateral sclerosis and multiple system atrophy
    • COI: 1:STN:280:DyaK383hsVSktg%3D%3D, PID: 1557955
    • Itoh T, Sobue G, Ken E, Mitsuma T, Takahashi A, Trojanowski JQ (1992) Phosphorylated high molecular weight neurofilament protein in the peripheral motor, sensory and sympathetic neuronal perikarya: system-dependent normal variations and changes in amyotrophic lateral sclerosis and multiple system atrophy. Acta Neuropathol 83:240–245
    • (1992) Acta Neuropathol , vol.83 , pp. 240-245
    • Itoh, T.1    Sobue, G.2    Ken, E.3    Mitsuma, T.4    Takahashi, A.5    Trojanowski, J.Q.6
  • 76
    • 0032817551 scopus 로고    scopus 로고
    • Disruption of type IV intermediate filament network in mice lacking the neurofilament medium and heavy subunits
    • COI: 1:CAS:528:DyaK1MXlsVOitrw%3D, PID: 10461886
    • Jacomy H, Zhu Q, Couillard-Despres S, Beaulieu JM, Julien JP (1999) Disruption of type IV intermediate filament network in mice lacking the neurofilament medium and heavy subunits. J Neurochem 73:972–984
    • (1999) J Neurochem , vol.73 , pp. 972-984
    • Jacomy, H.1    Zhu, Q.2    Couillard-Despres, S.3    Beaulieu, J.M.4    Julien, J.P.5
  • 78
  • 79
    • 78650884653 scopus 로고    scopus 로고
    • Which way to go? Cytoskeletal organization and polarized transport in neurons
    • COI: 1:CAS:528:DC%2BC3MXktF2rtA%3D%3D, PID: 20817096
    • Kapitein LC, Hoogenraad CC (2011) Which way to go? Cytoskeletal organization and polarized transport in neurons. Mol Cell Neurosci 46:9–20
    • (2011) Mol Cell Neurosci , vol.46 , pp. 9-20
    • Kapitein, L.C.1    Hoogenraad, C.C.2
  • 80
    • 0025469588 scopus 로고
    • Alpha-internexin, a novel neuronal intermediate filament protein, precedes the low molecular weight neurofilament protein (NF-L) in the developing rat brain
    • COI: 1:CAS:528:DyaK3cXmtVyrsb8%3D, PID: 2201753
    • Kaplan MP, Chin SS, Fliegner KH, Liem RK (1990) Alpha-internexin, a novel neuronal intermediate filament protein, precedes the low molecular weight neurofilament protein (NF-L) in the developing rat brain. J Neurosci 10:2735–2748
    • (1990) J Neurosci , vol.10 , pp. 2735-2748
    • Kaplan, M.P.1    Chin, S.S.2    Fliegner, K.H.3    Liem, R.K.4
  • 81
    • 0024270741 scopus 로고
    • A hypothesis for the pathogenesis of amyotrophic lateral sclerosis
    • COI: 1:STN:280:DyaL1M7mtFKktg%3D%3D, PID: 3231956
    • Karpati G, Carpenter S, Durham H (1988) A hypothesis for the pathogenesis of amyotrophic lateral sclerosis. Rev Neurol 144:672–675
    • (1988) Rev Neurol , vol.144 , pp. 672-675
    • Karpati, G.1    Carpenter, S.2    Durham, H.3
  • 83
    • 0032498856 scopus 로고    scopus 로고
    • Antagonistic roles of neurofilament subunits NF-H and NF-M against NF-L in shaping dendritic arborization in spinal motor neurons
    • COI: 1:CAS:528:DyaK1cXhslOjsro%3D, PID: 9490729
    • Kong J, Tung VW, Aghajanian J, Xu Z (1998) Antagonistic roles of neurofilament subunits NF-H and NF-M against NF-L in shaping dendritic arborization in spinal motor neurons. J Cell Biol 140:1167–1176
    • (1998) J Cell Biol , vol.140 , pp. 1167-1176
    • Kong, J.1    Tung, V.W.2    Aghajanian, J.3    Xu, Z.4
  • 84
    • 80054110241 scopus 로고    scopus 로고
    • Identification of novel NPRAP/delta-catenin-interacting proteins and the direct association of NPRAP with dynamin 2
    • COI: 1:CAS:528:DC%2BC3MXhsVCju7vP, PID: 22022388
    • Koutras C, Levesque G (2011) Identification of novel NPRAP/delta-catenin-interacting proteins and the direct association of NPRAP with dynamin 2. PLoS ONE 6:e25379
    • (2011) PLoS ONE , vol.6 , pp. e25379
    • Koutras, C.1    Levesque, G.2
  • 85
    • 27744588225 scopus 로고    scopus 로고
    • Exploring the mechanical behavior of single intermediate filaments
    • COI: 1:CAS:528:DC%2BD2MXht1ejsrzP, PID: 16257415
    • Kreplak L, Bar H, Leterrier JF, Herrmann H, Aebi U (2005) Exploring the mechanical behavior of single intermediate filaments. J Mol Biol 354:569–577
    • (2005) J Mol Biol , vol.354 , pp. 569-577
    • Kreplak, L.1    Bar, H.2    Leterrier, J.F.3    Herrmann, H.4    Aebi, U.5
  • 87
    • 0036316794 scopus 로고    scopus 로고
    • Reduced number of unmyelinated sensory axons in peripherin null mice
    • COI: 1:CAS:528:DC%2BD38XjsFGkt7w%3D, PID: 12065660
    • Lariviere RC, Nguyen MD, Ribeiro-da-Silva A, Julien JP (2002) Reduced number of unmyelinated sensory axons in peripherin null mice. J Neurochem 81:525–532
    • (2002) J Neurochem , vol.81 , pp. 525-532
    • Lariviere, R.C.1    Nguyen, M.D.2    Ribeiro-da-Silva, A.3    Julien, J.P.4
  • 89
    • 0026535236 scopus 로고
    • Slow axonal transport mechanisms move neurofilaments relentlessly in mouse optic axons
    • COI: 1:CAS:528:DyaK38XitFWltLY%3D, PID: 1374068
    • Lasek RJ, Paggi P, Katz MJ (1992) Slow axonal transport mechanisms move neurofilaments relentlessly in mouse optic axons. J Cell Biol 117:607–616
    • (1992) J Cell Biol , vol.117 , pp. 607-616
    • Lasek, R.J.1    Paggi, P.2    Katz, M.J.3
  • 90
    • 84922481787 scopus 로고    scopus 로고
    • Dissection of genetic factors associated with amyotrophic lateral sclerosis
    • PID: 24780888
    • Leblond CS, Kaneb HM, Dion PA, Rouleau GA (2014) Dissection of genetic factors associated with amyotrophic lateral sclerosis. Exp Neurol. doi:10.1016/j.expneurol.2014.04.013
    • (2014) Exp Neurol
    • Leblond, C.S.1    Kaneb, H.M.2    Dion, P.A.3    Rouleau, G.A.4
  • 91
    • 17544371921 scopus 로고    scopus 로고
    • Characterization of interactions between the neurofilament triplet proteins by the yeast two-hybrid system
    • COI: 1:CAS:528:DyaK28Xjs1Oisbg%3D, PID: 8663004
    • Leung CL, Liem RK (1996) Characterization of interactions between the neurofilament triplet proteins by the yeast two-hybrid system. J Biol Chem 271:14041–14044
    • (1996) J Biol Chem , vol.271 , pp. 14041-14044
    • Leung, C.L.1    Liem, R.K.2
  • 92
    • 0032936972 scopus 로고    scopus 로고
    • No requirement of alpha-internexin for nervous system development and for radial growth of axons
    • COI: 1:CAS:528:DyaK1MXjsVShurg%3D, PID: 10350642
    • Levavasseur F, Zhu Q, Julien JP (1999) No requirement of alpha-internexin for nervous system development and for radial growth of axons. Brain Res Mol Brain Res 69:104–112
    • (1999) Brain Res Mol Brain Res , vol.69 , pp. 104-112
    • Levavasseur, F.1    Zhu, Q.2    Julien, J.P.3
  • 93
    • 0020488844 scopus 로고
    • Purification of individual components of the neurofilament triplet: filament assembly from the 70 000-dalton subunit
    • COI: 1:CAS:528:DyaL38XktF2hu74%3D, PID: 7201852
    • Liem RK, Hutchison SB (1982) Purification of individual components of the neurofilament triplet: filament assembly from the 70 000-dalton subunit. Biochemistry 21:3221–3226
    • (1982) Biochemistry , vol.21 , pp. 3221-3226
    • Liem, R.K.1    Hutchison, S.B.2
  • 94
    • 0034694151 scopus 로고    scopus 로고
    • Movement of mitochondria in the axons and dendrites of cultured hippocampal neurons
    • COI: 1:STN:280:DC%2BD3M%2FmvV2ltg%3D%3D, PID: 11054697
    • Ligon LA, Steward O (2000a) Movement of mitochondria in the axons and dendrites of cultured hippocampal neurons. J Comp Neurol 427:340–350
    • (2000) J Comp Neurol , vol.427 , pp. 340-350
    • Ligon, L.A.1    Steward, O.2
  • 95
    • 0034694152 scopus 로고    scopus 로고
    • Role of microtubules and actin filaments in the movement of mitochondria in the axons and dendrites of cultured hippocampal neurons
    • COI: 1:STN:280:DC%2BD3M%2FmvV2ltw%3D%3D, PID: 11054698
    • Ligon LA, Steward O (2000b) Role of microtubules and actin filaments in the movement of mitochondria in the axons and dendrites of cultured hippocampal neurons. J Comp Neurol 427:351–361
    • (2000) J Comp Neurol , vol.427 , pp. 351-361
    • Ligon, L.A.1    Steward, O.2
  • 96
  • 100
    • 0022738435 scopus 로고
    • Actin filament organization within dendrites and dendritic spines during development
    • COI: 1:STN:280:DyaL283hslaksw%3D%3D, PID: 3708380
    • Markham JA, Fifkova E (1986) Actin filament organization within dendrites and dendritic spines during development. Brain Res 392:263–269
    • (1986) Brain Res , vol.392 , pp. 263-269
    • Markham, J.A.1    Fifkova, E.2
  • 101
    • 79951552495 scopus 로고    scopus 로고
    • Nesprins LINC the nucleus and cytoskeleton
    • COI: 1:CAS:528:DC%2BC3MXit12jurc%3D, PID: 21177090
    • Mellad JA, Warren DT, Shanahan CM (2011) Nesprins LINC the nucleus and cytoskeleton. Curr Opin Cell Biol 23:47–54
    • (2011) Curr Opin Cell Biol , vol.23 , pp. 47-54
    • Mellad, J.A.1    Warren, D.T.2    Shanahan, C.M.3
  • 103
    • 84878393110 scopus 로고    scopus 로고
    • Overexpression of USP14 protease reduces I-kappaB protein levels and increases cytokine release in lung epithelial cells
    • COI: 1:CAS:528:DC%2BC3sXosFyqurw%3D, PID: 23615914
    • Mialki RK, Zhao J, Wei J, Mallampalli DF, Zhao Y (2013) Overexpression of USP14 protease reduces I-kappaB protein levels and increases cytokine release in lung epithelial cells. J Biol Chem 288:15437–15441
    • (2013) J Biol Chem , vol.288 , pp. 15437-15441
    • Mialki, R.K.1    Zhao, J.2    Wei, J.3    Mallampalli, D.F.4    Zhao, Y.5
  • 104
    • 14244266089 scopus 로고    scopus 로고
    • [35S]Methionine metabolic labeling to study axonal transport of neuronal intermediate filament proteins in vivo
    • COI: 1:CAS:528:DC%2BD2MXptVCrsQ%3D%3D, PID: 15646631
    • Millecamps S, Julien JP (2004) [35S]Methionine metabolic labeling to study axonal transport of neuronal intermediate filament proteins in vivo. Methods Cell Biol 78:555–571
    • (2004) Methods Cell Biol , vol.78 , pp. 555-571
    • Millecamps, S.1    Julien, J.P.2
  • 105
    • 34247890153 scopus 로고    scopus 로고
    • Conditional NF-L transgene expression in mice for in vivo analysis of turnover and transport rate of neurofilaments
    • COI: 1:CAS:528:DC%2BD2sXlsV2rt78%3D, PID: 17475803
    • Millecamps S, Gowing G, Corti O, Mallet J, Julien JP (2007) Conditional NF-L transgene expression in mice for in vivo analysis of turnover and transport rate of neurofilaments. J Neurosci 27:4947–4956
    • (2007) J Neurosci , vol.27 , pp. 4947-4956
    • Millecamps, S.1    Gowing, G.2    Corti, O.3    Mallet, J.4    Julien, J.P.5
  • 107
    • 33645985470 scopus 로고    scopus 로고
    • Spontaneous and evoked neuronal activities regulate movements of single neuronal mitochondria
    • COI: 1:CAS:528:DC%2BD28XjvFarsLs%3D, PID: 16485263
    • Mironov SL (2006) Spontaneous and evoked neuronal activities regulate movements of single neuronal mitochondria. Synapse 59:403–411
    • (2006) Synapse , vol.59 , pp. 403-411
    • Mironov, S.L.1
  • 108
    • 33845912670 scopus 로고    scopus 로고
    • ER vesicles and mitochondria move and communicate at synapses
    • COI: 1:CAS:528:DC%2BD2sXivFeisQ%3D%3D, PID: 17105774
    • Mironov SL, Symonchuk N (2006) ER vesicles and mitochondria move and communicate at synapses. J Cell Sci 119:4926–4934
    • (2006) J Cell Sci , vol.119 , pp. 4926-4934
    • Mironov, S.L.1    Symonchuk, N.2
  • 110
    • 0033951171 scopus 로고    scopus 로고
    • Major phosphorylation site (Ser55) of neurofilament L by cyclic AMP-dependent protein kinase in rat primary neuronal culture
    • COI: 1:CAS:528:DC%2BD3cXhtlChs74%3D, PID: 10693925
    • Nakamura Y, Hashimoto R, Kashiwagi Y, Aimoto S, Fukusho E, Matsumoto N, Kudo T, Takeda M (2000) Major phosphorylation site (Ser55) of neurofilament L by cyclic AMP-dependent protein kinase in rat primary neuronal culture. J Neurochem 74:949–959
    • (2000) J Neurochem , vol.74 , pp. 949-959
    • Nakamura, Y.1    Hashimoto, R.2    Kashiwagi, Y.3    Aimoto, S.4    Fukusho, E.5    Matsumoto, N.6    Kudo, T.7    Takeda, M.8
  • 111
    • 0023070785 scopus 로고
    • Atrophic cell processes of large motor neurons in the anterior horn in amyotrophic lateral sclerosis: observation with silver impregnation method
    • COI: 1:STN:280:DyaL2s%2FosFOjsQ%3D%3D, PID: 2432193
    • Nakano I, Hirano A (1987) Atrophic cell processes of large motor neurons in the anterior horn in amyotrophic lateral sclerosis: observation with silver impregnation method. J Neuropathol Exp Neurol 46:40–49
    • (1987) J Neuropathol Exp Neurol , vol.46 , pp. 40-49
    • Nakano, I.1    Hirano, A.2
  • 112
    • 0022617701 scopus 로고
    • Multiple fates of newly synthesized neurofilament proteins: evidence for a stationary neurofilament network distributed nonuniformly along axons of retinal ganglion cell neurons
    • COI: 1:CAS:528:DyaL28XhtVOjtLs%3D, PID: 2418034
    • Nixon RA, Logvinenko KB (1986) Multiple fates of newly synthesized neurofilament proteins: evidence for a stationary neurofilament network distributed nonuniformly along axons of retinal ganglion cell neurons. J Cell Biol 102:647–659
    • (1986) J Cell Biol , vol.102 , pp. 647-659
    • Nixon, R.A.1    Logvinenko, K.B.2
  • 113
    • 0024237394 scopus 로고
    • Dephosphorylation of neurofilament proteins enhances their susceptibility to degradation by calpain
    • COI: 1:CAS:528:DyaL1MXitVSquw%3D%3D, PID: 2851997
    • Pant HC (1988) Dephosphorylation of neurofilament proteins enhances their susceptibility to degradation by calpain. Biochem J 256:665–668
    • (1988) Biochem J , vol.256 , pp. 665-668
    • Pant, H.C.1
  • 114
    • 0037115722 scopus 로고    scopus 로고
    • Effects of Charcot-Marie-Tooth-linked mutations of the neurofilament light subunit on intermediate filament formation
    • COI: 1:CAS:528:DC%2BD3sXis1Kqug%3D%3D, PID: 12432080
    • Perez-Olle R, Leung CL, Liem RK (2002) Effects of Charcot-Marie-Tooth-linked mutations of the neurofilament light subunit on intermediate filament formation. J Cell Sci 115:4937–4946
    • (2002) J Cell Sci , vol.115 , pp. 4937-4946
    • Perez-Olle, R.1    Leung, C.L.2    Liem, R.K.3
  • 115
    • 5444267945 scopus 로고    scopus 로고
    • Phenotypic analysis of neurofilament light gene mutations linked to Charcot-Marie-Tooth disease in cell culture models
    • COI: 1:CAS:528:DC%2BD2cXns1Onu7w%3D, PID: 15282209
    • Perez-Olle R, Jones ST, Liem RK (2004) Phenotypic analysis of neurofilament light gene mutations linked to Charcot-Marie-Tooth disease in cell culture models. Hum Mol Genet 13:2207–2220
    • (2004) Hum Mol Genet , vol.13 , pp. 2207-2220
    • Perez-Olle, R.1    Jones, S.T.2    Liem, R.K.3
  • 116
    • 84875130745 scopus 로고    scopus 로고
    • Ubiquitinated proteins activate the proteasomal ATPases by binding to Usp14 or Uch37 homologs
    • COI: 1:CAS:528:DC%2BC3sXktVKgtb0%3D
    • Peth A, Kukushkin N, Bosse M, Goldberg AL (2013) Ubiquitinated proteins activate the proteasomal ATPases by binding to Usp14 or Uch37 homologs. J Biolo Chem 288:7781–7790
    • (2013) J Biolo Chem , vol.288 , pp. 7781-7790
    • Peth, A.1    Kukushkin, N.2    Bosse, M.3    Goldberg, A.L.4
  • 117
    • 0027422823 scopus 로고
    • Evidence for antigen driven selection in two monoclonal auto-antibodies derived from nonobese diabetic mice
    • COI: 1:CAS:528:DyaK3sXms1yrt74%3D, PID: 8413326
    • Pleau JM, Marche PN, Serrano MP, Boitard C, Bach JF (1993) Evidence for antigen driven selection in two monoclonal auto-antibodies derived from nonobese diabetic mice. Mol Immunol 30:1257–1264
    • (1993) Mol Immunol , vol.30 , pp. 1257-1264
    • Pleau, J.M.1    Marche, P.N.2    Serrano, M.P.3    Boitard, C.4    Bach, J.F.5
  • 120
    • 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
    • COI: 1:CAS:528:DC%2BD38XmsVSnur4%3D, PID: 12186852
    • Rao MV, Garcia ML, Miyazaki Y, Gotow T, Yuan A, Mattina S, Ward CM, Calcutt NA, Uchiyama Y, Nixon RA, Cleveland DW (2002b) 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    Miyazaki, Y.3    Gotow, T.4    Yuan, A.5    Mattina, S.6    Ward, C.M.7    Calcutt, N.A.8    Uchiyama, Y.9    Nixon, R.A.10    Cleveland, D.W.11
  • 121
    • 0346849719 scopus 로고    scopus 로고
    • The neurofilament middle molecular mass subunit carboxyl-terminal tail domains is essential for the radial growth and cytoskeletal architecture of axons but not for regulating neurofilament transport rate
    • COI: 1:CAS:528:DC%2BD3sXpvVaks70%3D, PID: 14662746
    • Rao MV, Campbell J, Yuan A, Kumar A, Gotow T, Uchiyama Y, Nixon RA (2003) The neurofilament middle molecular mass subunit carboxyl-terminal tail domains is essential for the radial growth and cytoskeletal architecture of axons but not for regulating neurofilament transport rate. J Cell Biol 163:1021–1031
    • (2003) J Cell Biol , vol.163 , pp. 1021-1031
    • Rao, M.V.1    Campbell, J.2    Yuan, A.3    Kumar, A.4    Gotow, T.5    Uchiyama, Y.6    Nixon, R.A.7
  • 122
    • 79951891241 scopus 로고    scopus 로고
    • The myosin Va head domain binds to the neurofilament-L rod and modulates endoplasmic reticulum (ER) content and distribution within axons
    • COI: 1:CAS:528:DC%2BC3MXislChu7c%3D, PID: 21359212
    • Rao MV, Mohan PS, Kumar A, Yuan A, Montagna L, Campbell J, Veeranna EEM, Julien JP, Nixon RA (2011) The myosin Va head domain binds to the neurofilament-L rod and modulates endoplasmic reticulum (ER) content and distribution within axons. PLoS ONE 6:e17087
    • (2011) PLoS ONE , vol.6 , pp. e17087
    • Rao, M.V.1    Mohan, P.S.2    Kumar, A.3    Yuan, A.4    Montagna, L.5    Campbell, J.6    Veeranna, E.E.M.7    Julien, J.P.8    Nixon, R.A.9
  • 124
    • 0030786038 scopus 로고    scopus 로고
    • Axonal cytoskeletal pathology in aged and diabetic human sympathetic autonomic ganglia
    • COI: 1:CAS:528:DyaK2sXlvVKmt7k%3D, PID: 9374210
    • Schmidt RE, Beaudet LN, Plurad SB, Dorsey DA (1997a) Axonal cytoskeletal pathology in aged and diabetic human sympathetic autonomic ganglia. Brain Res 769:375–383
    • (1997) Brain Res , vol.769 , pp. 375-383
    • Schmidt, R.E.1    Beaudet, L.N.2    Plurad, S.B.3    Dorsey, D.A.4
  • 125
    • 0030967761 scopus 로고    scopus 로고
    • Dystrophic axonal swellings develop as a function of age and diabetes in human dorsal root ganglia
    • COI: 1:STN:280:DyaK2svjslCisw%3D%3D, PID: 9291944
    • Schmidt RE, Dorsey D, Parvin CA, Beaudet LN, Plurad SB, Roth KA (1997b) Dystrophic axonal swellings develop as a function of age and diabetes in human dorsal root ganglia. J Neuropathol Exp Neurol 56:1028–1043
    • (1997) J Neuropathol Exp Neurol , vol.56 , pp. 1028-1043
    • Schmidt, R.E.1    Dorsey, D.2    Parvin, C.A.3    Beaudet, L.N.4    Plurad, S.B.5    Roth, K.A.6
  • 126
    • 0022238110 scopus 로고
    • Characterization of mammalian neurofilament triplet proteins. Subunit stoichiometry and morphology of native and reconstituted filaments
    • COI: 1:CAS:528:DyaL2MXltlOgu7o%3D, PID: 2993286
    • Scott D, Smith KE, O’Brien BJ, Angelides KJ (1985) Characterization of mammalian neurofilament triplet proteins. Subunit stoichiometry and morphology of native and reconstituted filaments. J Biol Chem 260:10736–10747
    • (1985) J Biol Chem , vol.260 , pp. 10736-10747
    • Scott, D.1    Smith, K.E.2    O’Brien, B.J.3    Angelides, K.J.4
  • 127
    • 0024531851 scopus 로고
    • In vivo phosphorylation of distinct domains of the 70-kilodalton neurofilament subunit involves different protein kinases
    • COI: 1:CAS:528:DyaL1MXlsVylsg%3D%3D, PID: 2491851
    • Sihag RK, Nixon RA (1989) In vivo phosphorylation of distinct domains of the 70-kilodalton neurofilament subunit involves different protein kinases. J Biol Chem 264:457–464
    • (1989) J Biol Chem , vol.264 , pp. 457-464
    • Sihag, R.K.1    Nixon, R.A.2
  • 128
    • 0025257205 scopus 로고
    • Phosphorylation of the amino-terminal head domain of the middle molecular mass 145-kDa subunit of neurofilaments. Evidence for regulation by second messenger-dependent protein kinases
    • COI: 1:CAS:528:DyaK3cXhsFeqtbY%3D, PID: 2105960
    • Sihag RK, Nixon RA (1990) Phosphorylation of the amino-terminal head domain of the middle molecular mass 145-kDa subunit of neurofilaments. Evidence for regulation by second messenger-dependent protein kinases. J Biol Chem 265:4166–4171
    • (1990) J Biol Chem , vol.265 , pp. 4166-4171
    • Sihag, R.K.1    Nixon, R.A.2
  • 129
    • 0025950711 scopus 로고
    • Identification of Ser-55 as a major protein kinase A phosphorylation site on the 70-kDa subunit of neurofilaments. Early turnover during axonal transport
    • COI: 1:CAS:528:DyaK3MXmsFSmtbg%3D, PID: 1717455
    • Sihag RK, Nixon RA (1991) Identification of Ser-55 as a major protein kinase A phosphorylation site on the 70-kDa subunit of neurofilaments. Early turnover during axonal transport. J Biol Chem 266:18861–18867
    • (1991) J Biol Chem , vol.266 , pp. 18861-18867
    • Sihag, R.K.1    Nixon, R.A.2
  • 130
    • 0023916538 scopus 로고
    • Phosphorylation of neurofilament proteins by protein kinase C
    • COI: 1:CAS:528:DyaL1cXktlCns7k%3D, PID: 3384089
    • Sihag RK, Jeng AY, Nixon RA (1988) Phosphorylation of neurofilament proteins by protein kinase C. FEBS Lett 233:181–185
    • (1988) FEBS Lett , vol.233 , pp. 181-185
    • Sihag, R.K.1    Jeng, A.Y.2    Nixon, R.A.3
  • 131
    • 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
    • COI: 1:CAS:528:DyaK1MXmt1yhuw%3D%3D, PID: 9930720
    • Sihag RK, Jaffe H, Nixon RA, Rong X (1999) 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 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
  • 132
    • 0025165101 scopus 로고
    • Phosphorylated high molecular weight neurofilament protein in lower motor neurons in amyotrophic lateral sclerosis and other neurodegenerative diseases involving ventral horn cells
    • COI: 1:STN:280:DyaK3c3lt1GmtQ%3D%3D, PID: 2111074
    • Sobue G, Hashizume Y, Yasuda T, Mukai E, Kumagai T, Mitsuma T, Trojanowski JQ (1990) Phosphorylated high molecular weight neurofilament protein in lower motor neurons in amyotrophic lateral sclerosis and other neurodegenerative diseases involving ventral horn cells. Acta Neuropathol 79:402–408
    • (1990) Acta Neuropathol , vol.79 , pp. 402-408
    • Sobue, G.1    Hashizume, Y.2    Yasuda, T.3    Mukai, E.4    Kumagai, T.5    Mitsuma, T.6    Trojanowski, J.Q.7
  • 133
    • 0025284699 scopus 로고
    • The two-chain coiled-coil molecule of native epidermal keratin intermediate filaments is a type I-type II heterodimer
    • COI: 1:CAS:528:DyaK3cXktVahu7s%3D, PID: 1692836
    • Steinert PM (1990) The two-chain coiled-coil molecule of native epidermal keratin intermediate filaments is a type I-type II heterodimer. J Biol Chem 265:8766–8774
    • (1990) J Biol Chem , vol.265 , pp. 8766-8774
    • Steinert, P.M.1
  • 134
    • 84906318887 scopus 로고    scopus 로고
    • Dendritic retraction, but not atrophy, is consistent in amyotrophic lateral sclerosis-comparison between Onuf’s neurons and other sacral motor neurons
    • PID: 24468079
    • Takeda T, Uchihara T, Nakayama Y, Nakamura A, Sasaki S, Kakei S, Uchiyama S, Duyckaerts C, Yoshida M (2014) Dendritic retraction, but not atrophy, is consistent in amyotrophic lateral sclerosis-comparison between Onuf’s neurons and other sacral motor neurons. Acta Neuropathol Commun 2:11
    • (2014) Acta Neuropathol Commun , vol.2 , pp. 11
    • Takeda, T.1    Uchihara, T.2    Nakayama, Y.3    Nakamura, A.4    Sasaki, S.5    Kakei, S.6    Uchiyama, S.7    Duyckaerts, C.8    Yoshida, M.9
  • 135
    • 67649413406 scopus 로고    scopus 로고
    • Mitochondrial and axonal abnormalities precede disruption of the neurofilament network in a model of Charcot-Marie-Tooth disease type 2E and are prevented by heat shock proteins in a mutant-specific fashion
    • COI: 1:CAS:528:DC%2BD1MXmsFWmtL4%3D, PID: 19458545
    • Tradewell ML, Durham HD, Mushynski WE, Gentil BJ (2009) Mitochondrial and axonal abnormalities precede disruption of the neurofilament network in a model of Charcot-Marie-Tooth disease type 2E and are prevented by heat shock proteins in a mutant-specific fashion. J Neuropathol Exp Neurol 68:642–652
    • (2009) J Neuropathol Exp Neurol , vol.68 , pp. 642-652
    • Tradewell, M.L.1    Durham, H.D.2    Mushynski, W.E.3    Gentil, B.J.4
  • 136
    • 33846423163 scopus 로고    scopus 로고
    • Neurofilaments switch between distinct mobile and stationary states during their transport along axons
    • COI: 1:CAS:528:DC%2BD2sXhtFSktbs%3D, PID: 17234583
    • Trivedi N, Jung P, Brown A (2007) Neurofilaments switch between distinct mobile and stationary states during their transport along axons. J Neurosci 27:507–516
    • (2007) J Neurosci , vol.27 , pp. 507-516
    • Trivedi, N.1    Jung, P.2    Brown, A.3
  • 137
    • 0025185388 scopus 로고
    • Regulation of peripherin and neurofilament expression in regenerating rat motor neurons
    • COI: 1:CAS:528:DyaK3cXmt1yrtLw%3D, PID: 2126481
    • Troy CM, Muma NA, Greene LA, Price DL, Shelanski ML (1990) Regulation of peripherin and neurofilament expression in regenerating rat motor neurons. Brain Res 529:232–238
    • (1990) Brain Res , vol.529 , pp. 232-238
    • Troy, C.M.1    Muma, N.A.2    Greene, L.A.3    Price, D.L.4    Shelanski, M.L.5
  • 138
    • 73949153142 scopus 로고    scopus 로고
    • Tight functional coupling of kinesin-1A and dynein motors in the bidirectional transport of neurofilaments
    • COI: 1:CAS:528:DC%2BC3cXnslWl, PID: 19812246
    • Uchida A, Alami NH, Brown A (2009) Tight functional coupling of kinesin-1A and dynein motors in the bidirectional transport of neurofilaments. Mol Biol Cell 20:4997–5006
    • (2009) Mol Biol Cell , vol.20 , pp. 4997-5006
    • Uchida, A.1    Alami, N.H.2    Brown, A.3
  • 139
    • 84880393651 scopus 로고    scopus 로고
    • Severing and end-to-end annealing of neurofilaments in neurons
    • COI: 1:CAS:528:DC%2BC3sXht1emu7zP, PID: 23821747
    • Uchida A, Colakoglu G, Wang L, Monsma PC, Brown A (2013) Severing and end-to-end annealing of neurofilaments in neurons. Proc Natl Acad Sci U S A 110:E2696–2705
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. E2696-E2705
    • Uchida, A.1    Colakoglu, G.2    Wang, L.3    Monsma, P.C.4    Brown, A.5
  • 141
    • 73949134014 scopus 로고    scopus 로고
    • Tar DNA binding protein of 43 kDa (TDP-43), 14-3-3 proteins and copper/zinc superoxide dismutase (SOD1) interact to modulate NFL mRNA stability. Implications for altered RNA processing in amyotrophic lateral sclerosis (ALS)
    • COI: 1:CAS:528:DC%2BD1MXhsVGntbbO, PID: 19815002
    • Volkening K, Leystra-Lantz C, Yang W, Jaffee H, Strong MJ (2009) Tar DNA binding protein of 43 kDa (TDP-43), 14-3-3 proteins and copper/zinc superoxide dismutase (SOD1) interact to modulate NFL mRNA stability. Implications for altered RNA processing in amyotrophic lateral sclerosis (ALS). Brain Res 1305:168–182
    • (2009) Brain Res , vol.1305 , pp. 168-182
    • Volkening, K.1    Leystra-Lantz, C.2    Yang, W.3    Jaffee, H.4    Strong, M.J.5
  • 142
    • 79951958601 scopus 로고    scopus 로고
    • Carboxyl-terminus of Hsc70 interacting protein mediates 2,5-hexanedione-induced neurofilament medium chain degradation
    • COI: 1:CAS:528:DC%2BC3MXit12jtbs%3D, PID: 21219885
    • Wang Q, Song F, Zhang C, Zhao X, Zhu Z, Yu S, Xie K (2011) Carboxyl-terminus of Hsc70 interacting protein mediates 2,5-hexanedione-induced neurofilament medium chain degradation. Biochem Pharmacol 81:793–799
    • (2011) Biochem Pharmacol , vol.81 , pp. 793-799
    • Wang, Q.1    Song, F.2    Zhang, C.3    Zhao, X.4    Zhu, Z.5    Yu, S.6    Xie, K.7
  • 143
    • 84992236576 scopus 로고    scopus 로고
    • Plectin isoforms as organizers of intermediate filament cytoarchitecture
    • Wiche G, Winter L (2011) Plectin isoforms as organizers of intermediate filament cytoarchitecture. Biogeosciences 1:14–20
    • (2011) Biogeosciences , vol.1 , pp. 14-20
    • Wiche, G.1    Winter, L.2
  • 144
    • 14844362394 scopus 로고    scopus 로고
    • Characterization of the in vitro co-assembly process of the intermediate filament proteins vimentin and desmin: mixed polymers at all stages of assembly
    • COI: 1:CAS:528:DC%2BD2MXktFCisLw%3D, PID: 15819415
    • Wickert U, Mucke N, Wedig T, Muller SA, Aebi U, Herrmann H (2005) Characterization of the in vitro co-assembly process of the intermediate filament proteins vimentin and desmin: mixed polymers at all stages of assembly. Eur J Cell Biol 84:379–391
    • (2005) Eur J Cell Biol , vol.84 , pp. 379-391
    • Wickert, U.1    Mucke, N.2    Wedig, T.3    Muller, S.A.4    Aebi, U.5    Herrmann, H.6
  • 145
    • 84914432794 scopus 로고
    • Neurofilaments and microtubules in anterior horn cells of the rat
    • COI: 1:STN:280:DC%2BD1cvls1agsg%3D%3D, PID: 18631475
    • Wuerker RB, Palay SL (1969) Neurofilaments and microtubules in anterior horn cells of the rat. Tissue Cell 1:387–402
    • (1969) Tissue Cell , vol.1 , pp. 387-402
    • Wuerker, R.B.1    Palay, S.L.2
  • 146
    • 39749188127 scopus 로고    scopus 로고
    • An aggregate-inducing peripherin isoform generated through intron retention is upregulated in amyotrophic lateral sclerosis and associated with disease pathology
    • COI: 1:CAS:528:DC%2BD1cXnvVSrtbw%3D, PID: 18287500
    • Xiao S, Tjostheim S, Sanelli T, McLean JR, Horne P, Fan Y, Ravits J, Strong MJ, Robertson J (2008) An aggregate-inducing peripherin isoform generated through intron retention is upregulated in amyotrophic lateral sclerosis and associated with disease pathology. J Neurosci 28:1833–1840
    • (2008) J Neurosci , vol.28 , pp. 1833-1840
    • Xiao, S.1    Tjostheim, S.2    Sanelli, T.3    McLean, J.R.4    Horne, P.5    Fan, Y.6    Ravits, J.7    Strong, M.J.8    Robertson, J.9
  • 147
    • 0032694199 scopus 로고    scopus 로고
    • Kinesin-mediated transport of neurofilament protein oligomers in growing axons
    • COI: 1:CAS:528:DyaK1MXns1Oltr0%3D, PID: 10523515
    • Yabe JT, Pimenta A, Shea TB (1999) Kinesin-mediated transport of neurofilament protein oligomers in growing axons. J Cell Sci 112(Pt 21):3799–3814
    • (1999) J Cell Sci , vol.112 , pp. 3799-3814
    • Yabe, J.T.1    Pimenta, A.2    Shea, T.B.3
  • 148
    • 0025365347 scopus 로고
    • Reduced myelinated fiber size correlates with loss of axonal neurofilaments in peripheral nerve of chronically streptozotocin diabetic rats
    • COI: 1:STN:280:DyaK3c3ovFyisA%3D%3D, PID: 2141449
    • Yagihashi S, Kamijo M, Watanabe K (1990) Reduced myelinated fiber size correlates with loss of axonal neurofilaments in peripheral nerve of chronically streptozotocin diabetic rats. Am J Pathol 136:1365–1373
    • (1990) Am J Pathol , vol.136 , pp. 1365-1373
    • Yagihashi, S.1    Kamijo, M.2    Watanabe, K.3
  • 149
    • 60749102885 scopus 로고    scopus 로고
    • Neurofilament subunit (NFL) head domain phosphorylation regulates axonal transport of neurofilaments
    • COI: 1:CAS:528:DC%2BD1MXktlejs74%3D, PID: 19147253
    • Yates DM, Manser C, De Vos KJ, Shaw CE, McLoughlin DM, Miller CC (2009) Neurofilament subunit (NFL) head domain phosphorylation regulates axonal transport of neurofilaments. Eur J Cell Biol 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.6
  • 151
    • 0036900365 scopus 로고    scopus 로고
    • Identification of novel sequence variants in the neurofilament-light gene in a Japanese population: analysis of Charcot-Marie-Tooth disease patients and normal individuals
    • COI: 1:CAS:528:DC%2BD3sXpsF2lsbs%3D, PID: 12477167
    • Yoshihara T, Yamamoto M, Hattori N, Misu K, Mori K, Koike H, Sobue G (2002) Identification of novel sequence variants in the neurofilament-light gene in a Japanese population: analysis of Charcot-Marie-Tooth disease patients and normal individuals. J Peripher Nerv Syst 7:221–224
    • (2002) J Peripher Nerv Syst , vol.7 , pp. 221-224
    • Yoshihara, T.1    Yamamoto, M.2    Hattori, N.3    Misu, K.4    Mori, K.5    Koike, H.6    Sobue, G.7
  • 152
    • 0142250822 scopus 로고    scopus 로고
    • Neurofilament transport in vivo minimally requires hetero-oligomer formation
    • COI: 1:CAS:528:DC%2BD3sXos1Gqtb8%3D, PID: 14561875
    • Yuan A, Rao MV, Kumar A, Julien JP, Nixon RA (2003) Neurofilament transport in vivo minimally requires hetero-oligomer formation. J Neurosci 23:9452–9458
    • (2003) J Neurosci , vol.23 , pp. 9452-9458
    • Yuan, A.1    Rao, M.V.2    Kumar, A.3    Julien, J.P.4    Nixon, R.A.5
  • 153
    • 29244471690 scopus 로고    scopus 로고
    • Deleting the phosphorylated tail domain of the neurofilament heavy subunit does not alter neurofilament transport rate in vivo
    • COI: 1:CAS:528:DC%2BD2MXhtlGit77L, PID: 16266786
    • Yuan A, Nixon RA, Rao MV (2006a) Deleting the phosphorylated tail domain of the neurofilament heavy subunit does not alter neurofilament transport rate in vivo. Neurosci Lett 393:264–268
    • (2006) Neurosci Lett , vol.393 , pp. 264-268
    • Yuan, A.1    Nixon, R.A.2    Rao, M.V.3
  • 154
    • 33749177577 scopus 로고    scopus 로고
    • Alpha-internexin is structurally and functionally associated with the neurofilament triplet proteins in the mature CNS
    • COI: 1:CAS:528:DC%2BD28XhtVOmtLbI, PID: 17005864
    • Yuan A, Rao MV, Sasaki T, Chen Y, Kumar A, Veeranna LRK, Eyer J, Peterson AC, Julien JP, Nixon RA (2006b) Alpha-internexin is structurally and functionally associated with the neurofilament triplet proteins in the mature CNS. J Neurosci 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, L.R.K.6    Eyer, J.7    Peterson, A.C.8    Julien, J.P.9    Nixon, R.A.10
  • 155
    • 84862849287 scopus 로고    scopus 로고
    • Peripherin is a subunit of peripheral nerve neurofilaments: implications for differential vulnerability of CNS and peripheral nervous system axons
    • COI: 1:CAS:528:DC%2BC38XpsV2iurc%3D, PID: 22723690
    • Yuan A, Sasaki T, Kumar A, Peterhoff CM, Rao MV, Liem RK, Julien JP, Nixon RA (2012) Peripherin is a subunit of peripheral nerve neurofilaments: implications for differential vulnerability of CNS and peripheral nervous system axons. J Neurosci 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
  • 156
    • 73549086741 scopus 로고    scopus 로고
    • A novel recessive Nefl mutation causes a severe, early-onset axonal neuropathy
    • COI: 1:CAS:528:DC%2BC3cXhtlams7g%3D, PID: 20039262
    • Yum SW, Zhang J, Mo K, Li J, Scherer SS (2009) A novel recessive Nefl mutation causes a severe, early-onset axonal neuropathy. Ann Neurol 66:759–770
    • (2009) Ann Neurol , vol.66 , pp. 759-770
    • Yum, S.W.1    Zhang, J.2    Mo, K.3    Li, J.4    Scherer, S.S.5
  • 157
    • 0038437591 scopus 로고
    • In vitro reconstitution of intermediate filaments form mammalian neurofilament triplet polypeptides
    • COI: 1:CAS:528:DyaL38XhsFOlsbo%3D, PID: 6950425
    • Zackroff RV, Idler WW, Steinert PM, Goldman RD (1982) In vitro reconstitution of intermediate filaments form mammalian neurofilament triplet polypeptides. Proc Natl Acad Sci U S A 79:754–757
    • (1982) Proc Natl Acad Sci U S A , vol.79 , pp. 754-757
    • Zackroff, R.V.1    Idler, W.W.2    Steinert, P.M.3    Goldman, R.D.4
  • 158
    • 36248947271 scopus 로고    scopus 로고
    • Disruption of neurofilament network with aggregation of light neurofilament protein: a common pathway leading to motor neuron degeneration due to Charcot-Marie-Tooth disease-linked mutations in NFL and HSPB1
    • COI: 1:CAS:528:DC%2BD2sXhtlajsrrP, PID: 17881652
    • Zhai J, Lin H, Julien JP, Schlaepfer WW (2007) Disruption of neurofilament network with aggregation of light neurofilament protein: a common pathway leading to motor neuron degeneration due to Charcot-Marie-Tooth disease-linked mutations in NFL and HSPB1. Hum Mol Genet 16:3103–3116
    • (2007) Hum Mol Genet , vol.16 , pp. 3103-3116
    • Zhai, J.1    Lin, H.2    Julien, J.P.3    Schlaepfer, W.W.4
  • 159
    • 0037047506 scopus 로고    scopus 로고
    • Normal dendritic arborization in spinal motoneurons requires neurofilament subunit L
    • COI: 1:CAS:528:DC%2BD38Xmt1OhsLw%3D, PID: 12124759
    • Zhang Z, Casey DM, Julien JP, Xu Z (2002) Normal dendritic arborization in spinal motoneurons requires neurofilament subunit L. J Comp Neurol 450:144–152
    • (2002) J Comp Neurol , vol.450 , pp. 144-152
    • Zhang, Z.1    Casey, D.M.2    Julien, J.P.3    Xu, Z.4
  • 160
    • 0031263931 scopus 로고    scopus 로고
    • Delayed maturation of regenerating myelinated axons in mice lacking neurofilaments
    • COI: 1:CAS:528:DyaK2sXotV2ltbc%3D, PID: 9398473
    • Zhu Q, Couillard-Despres S, Julien JP (1997) Delayed maturation of regenerating myelinated axons in mice lacking neurofilaments. Exp Neurol 148:299–316
    • (1997) Exp Neurol , vol.148 , pp. 299-316
    • Zhu, Q.1    Couillard-Despres, S.2    Julien, J.P.3
  • 161
    • 0347090624 scopus 로고    scopus 로고
    • The novel neurofilament light (NEFL) mutation Glu397Lys is associated with a clinically and morphologically heterogeneous type of Charcot-Marie-Tooth neuropathy
    • PID: 14733962
    • Zuchner S, Vorgerd M, Sindern E, Schroder JM (2004) The novel neurofilament light (NEFL) mutation Glu397Lys is associated with a clinically and morphologically heterogeneous type of Charcot-Marie-Tooth neuropathy. Neuromuscul Disord 14:147–157
    • (2004) Neuromuscul Disord , vol.14 , pp. 147-157
    • Zuchner, S.1    Vorgerd, M.2    Sindern, E.3    Schroder, J.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.