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deWaegh SM, Lee VMY, Brady ST Local modulation of neurofilament phosphorylation, axonal caliber, and slow axonal transport by myelinating Schwann cells. Cell. 68:1992;451-463.
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Neurofilament-dependent radial growth of motor axons and axonal organization of neurofilaments does not require the neurofilament heavy subunit (NF-H) or its phosphorylation
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Many lines of evidence suggested that the carboxyl terminal of NF-H makes side-arm projections that control neurofilament spacing and axon caliber. Surprisingly, this study on NF-H null mice shows that NF-H expression is not required for the radial growth of myelinated motor axons during development. This analysis of NF-H null mice revealed various cytoskeletal changes, such as increases in levels and phosphorylation of NF-M as well as increased tubulin content
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Rao MV, Houseweart MK, Williamson TL, Crawford TO, Folmer J, Cleveland DW Neurofilament-dependent radial growth of motor axons and axonal organization of neurofilaments does not require the neurofilament heavy subunit (NF-H) or its phosphorylation. J Cell Biol. 143:1998;171-181. Many lines of evidence suggested that the carboxyl terminal of NF-H makes side-arm projections that control neurofilament spacing and axon caliber. Surprisingly, this study on NF-H null mice shows that NF-H expression is not required for the radial growth of myelinated motor axons during development. This analysis of NF-H null mice revealed various cytoskeletal changes, such as increases in levels and phosphorylation of NF-M as well as increased tubulin content.
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9
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0032487532
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Disruption of the NF-H gene increases axonal microtubule content and velocity of neurofilament transport: Relief of axonopathy resulting from the toxin beta, beta'-iminodipropionitrile
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••], this paper shows that NF-H is not required for the radial growth of myelinated axons during development. In addition, this paper shows that the absence of NF-H increases the velocity of slow axonal transport and alleviates motor axonopathy caused by the toxin beta, beta′-iminodipropionitrile (IDPN)
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••], this paper shows that NF-H is not required for the radial growth of myelinated axons during development. In addition, this paper shows that the absence of NF-H increases the velocity of slow axonal transport and alleviates motor axonopathy caused by the toxin beta, beta′-iminodipropionitrile (IDPN).
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10
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0032487502
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Requirement of heavy neurofilament subunit in the development of axons with large calibers
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••], this analysis of NF-H null mice showed a reduction of NF-L levels and no changes in NF-M levels. This discrepancy may be attributable to the fact that these different groups used mice with different genetic backgrounds. This study used mice of 129J strain, whereas the two other groups used mice enriched in C57Bl6 background
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••], this analysis of NF-H null mice showed a reduction of NF-L levels and no changes in NF-M levels. This discrepancy may be attributable to the fact that these different groups used mice with different genetic backgrounds. This study used mice of 129J strain, whereas the two other groups used mice enriched in C57Bl6 background.
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Elder, G.A.1
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Tu, P.H.6
Zhang, B.7
Lee, V.M.8
Lazzarini, R.A.9
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11
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0032482231
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Absence of the mid-sized neurofilament subunit decreases axonal calibers, levels of light neurofilament (NF-L), and neurofilament content
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This analysis of NF-M null mice demonstrates for the first time the key role of NF-M protein in the control of neurofilament content and in the radial growth of axons
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Elder GA, Friedrich VL Jr., Bosco P, Kang C, Gourov A, Tu PH, Lee VM, Lazzarini RA Absence of the mid-sized neurofilament subunit decreases axonal calibers, levels of light neurofilament (NF-L), and neurofilament content. J Cell Biol. 141:1998;727-739. This analysis of NF-M null mice demonstrates for the first time the key role of NF-M protein in the control of neurofilament content and in the radial growth of axons.
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J Cell Biol
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Elder, G.A.1
Friedrich V.L., Jr.2
Bosco, P.3
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Tu, P.H.6
Lee, V.M.7
Lazzarini, R.A.8
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12
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0032817551
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Disruption of type IV intermediate filament network in mice lacking the neurofilament medium and heavy subunits
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This study confirms a requirement for NF-M and NF-H for the in vivo assembly of NF-L into neurofilaments and for the radial growth of myelinated axons. The levels of NF-L and α-internexin are dramatically reduced when NF-M and NF-H are absent. The authors also examined axonal transport in NF-M null and double mutant NF-M ; NF-H mice
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Jacomy H, Zhu Q, Couillard-Després S, Beaulieu M, Julien JP Disruption of type IV intermediate filament network in mice lacking the neurofilament medium and heavy subunits. J Neurochem. 73:1999;972-984. This study confirms a requirement for NF-M and NF-H for the in vivo assembly of NF-L into neurofilaments and for the radial growth of myelinated axons. The levels of NF-L and α-internexin are dramatically reduced when NF-M and NF-H are absent. The authors also examined axonal transport in NF-M null and double mutant NF-M ; NF-H mice.
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Jacomy, H.1
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13
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Athlan ES, Mushynski WE Heterodimeric associations between neuronal intermediate filament proteins. J Biol Chem. 272:1997;31073-31078.
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Athlan, E.S.1
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14
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0031718564
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Neurofilament-L homopolymers are less mechanically stable than native neurofilaments
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Brown HG, Troncoso JC, Hoh JH Neurofilament-L homopolymers are less mechanically stable than native neurofilaments. J Microsc. 191:1998;229-237.
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Abumuhor IA, Spencer PH, Cohlberg JA The pathway of assembly of intermediate filaments from recombinant alpha-internexin. J Struct Biol. 123:1998;187-198.
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0028853185
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Reassembly of the 66 kD neurofilament protein in vitro following isolation and purification from bovine spinal cord
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Balin BJ, Miller MH Reassembly of the 66 kD neurofilament protein in vitro following isolation and purification from bovine spinal cord. J Neurosci Res. 40:1995;79-88.
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No requirement of α-internexin for nervous system development and for radial growth of axons
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Levavasseur F, Zhu Q, Julien JP No requirement of α-internexin for nervous system development and for radial growth of axons. Mol Brain Res. 69:1999;104-112.
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18
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0028001606
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Variants of the heavy neurofilament subunit are associated with the development of amyotrophic lateral sclerosis
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Figlewicz DA, Krizus A, Martinoli MG, Meininger V, Dib M, Rouleau GA, Julien JP Variants of the heavy neurofilament subunit are associated with the development of amyotrophic lateral sclerosis. Hum Mol Genet. 3:1994;1757-1761.
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19
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0029970685
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Sequence variants in human neurofilament proteins: Absence of linkage to familial amyotrophic lateral sclerosis
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Vechio JD, Bruijn LI, Xu Z, Brown RH Jr., Cleveland DW Sequence variants in human neurofilament proteins: absence of linkage to familial amyotrophic lateral sclerosis. Ann Neurol. 40:1996;603-610.
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20
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0030000608
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Analysis of the KSP repeat of the neurofilament heavy subunit in familial amyotrophic lateral sclerosis
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Rooke K, Figlewicz DA, Han FY, Rouleau GA Analysis of the KSP repeat of the neurofilament heavy subunit in familial amyotrophic lateral sclerosis. Ann Neurol. 46:1995;789-790.
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Rooke, K.1
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21
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0032926368
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Deletions of the heavy neurofilament subunit tail in amyotrophic lateral sclerosis
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Al-Chalabi A, Andersen PM, Nilsson P, Chioza B, Andersson JL, Russ C, Shaw CE, Powell JF, Leigh PN Deletions of the heavy neurofilament subunit tail in amyotrophic lateral sclerosis. Hum Mol Genet. 8:1999;157-164.
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Al-Chalabi, A.1
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Russ, C.6
Shaw, C.E.7
Powell, J.F.8
Leigh, P.N.9
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22
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0032427646
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Novel insertion in the KSP region of the neurofilament heavy gene in amyotrophic lateral sclerosis (ALS)
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Tomkins J, Usher P, Slade JY, Ince PG, Curtis A, Bushby K, Shaw PJ Novel insertion in the KSP region of the neurofilament heavy gene in amyotrophic lateral sclerosis (ALS). Neuroreport. 9:1998;3967-3970.
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Tomkins, J.1
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Shaw, P.J.7
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23
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1842289165
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Superoxide dismutase catalyzes nitration of tyrosines by peroxynitrite in the rod and head domains of neurofilament-L
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Crow JP, Ye YZ, Strong M, Kirk M, Barnes S, Beckman JS Superoxide dismutase catalyzes nitration of tyrosines by peroxynitrite in the rod and head domains of neurofilament-L. J Neurochem. 69:1997;1945-1953.
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Crow, J.P.1
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24
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0032499878
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Nitration of the low molecular weight neurofilament is equivalent in sporadic amyotrophic lateral sclerosis and control cervical spinal cord
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Strong MJ, Sopper MM, Crow JP, Strong WL, Beckman JS Nitration of the low molecular weight neurofilament is equivalent in sporadic amyotrophic lateral sclerosis and control cervical spinal cord. Biochem Biophys Res Commun. 248:1998;157-164.
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Strong, M.J.1
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Strong, W.L.4
Beckman, J.S.5
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25
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0028353603
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Neurofilament light and polyadenylated mRNA levels are decreased in amyotrophic lateral sclerosis motor neurons
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Bergeron C, Beric-Maskarel K, Muntasser S, Weyer L, Somerville MJ, Percy ME Neurofilament light and polyadenylated mRNA levels are decreased in amyotrophic lateral sclerosis motor neurons. J Neuropathol Exp Neurol. 53:1994;221-230.
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Percy, M.E.6
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26
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0029004898
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Defective axonal transport in a transgenic mouse model of amyotrophic lateral sclerosis
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Collard JF, Côté F, Julien JP Defective axonal transport in a transgenic mouse model of amyotrophic lateral sclerosis. Nature. 375:1995;61-64.
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Collard, J.F.1
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0029807823
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Neurofilament subunit NF-H modulates axonal diameter by selectively slowing neurofilament transport
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Marszalek JR, Williamson TL, Lee MK, Xu Z, Hoffman PN, Becher MW, Crawford TO, Cleveland DW Neurofilament subunit NF-H modulates axonal diameter by selectively slowing neurofilament transport. J Cell Biol. 135:1996;711-724.
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Marszalek, J.R.1
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Becher, M.W.6
Crawford, T.O.7
Cleveland, D.W.8
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28
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0032498856
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Antagonistic roles of neurofilament subunits NF-H and NF-M against NF-L in shaping dendritic arborization in spinal motor neurons
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This paper shows that increasing the levels of NF-H or NF-M reduces the neurofilament content of spinal motor neuron dendrites. These changes can be reversed by overexpressing NF-L together with NF-H or NF-M, emphasizing the importance of the ratio of NF-L to NF-H and NF-M for dendritic arborization in motor neurons
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Kong J, Tung VW, Aghajanian J, Xu Z Antagonistic roles of neurofilament subunits NF-H and NF-M against NF-L in shaping dendritic arborization in spinal motor neurons. J Cell Biol. 140:1998;1167-1176. This paper shows that increasing the levels of NF-H or NF-M reduces the neurofilament content of spinal motor neuron dendrites. These changes can be reversed by overexpressing NF-L together with NF-H or NF-M, emphasizing the importance of the ratio of NF-L to NF-H and NF-M for dendritic arborization in motor neurons.
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J Cell Biol
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Kong, J.1
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Transgenic mice in the study of ALS: The role of neurofilaments
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Julien JP, Couillard-Després S, Meier J Transgenic mice in the study of ALS: the role of neurofilaments. Brain Pathol. 8:1998;759-769.
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Julien, J.P.1
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Meier, J.3
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30
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0033561167
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Overexpression of alpha internexin causes abnormal neurofilamentous accumulations and motor coordination deficits in transgenic mice
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The authors report that overexpression of a wild-type intermediate filament protein can provoke neurofilamentous accumulations and progressive neuronal death
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Ching GY, Chien CL, Flores R, Liem RKH Overexpression of alpha internexin causes abnormal neurofilamentous accumulations and motor coordination deficits in transgenic mice. J Neurosci. 19:1999;2974-2986. The authors report that overexpression of a wild-type intermediate filament protein can provoke neurofilamentous accumulations and progressive neuronal death.
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J Neurosci
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Ching, G.Y.1
Chien, C.L.2
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Liem, R.K.H.4
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31
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0033583561
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Severe neuronal losses with age in the parietal cortex and ventrobasal thalamus of mice transgenic for the human NF-L neurofilament protein
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Ma DM, Descarries L, Micheva KD, Lepage Y, Julien JP, Doucet G Severe neuronal losses with age in the parietal cortex and ventrobasal thalamus of mice transgenic for the human NF-L neurofilament protein. J Comp Neurol. 406:1999;433-448.
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J Comp Neurol
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Ma, D.M.1
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Julien, J.P.5
Doucet, G.6
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32
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0031876839
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Advanced glycation endproducts in neurofilament conglomeration of motoneurons in familial and sporadic amyotrophic lateral sclerosis
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Chou SM, Wang HS, Taniguchi A, Bucala R Advanced glycation endproducts in neurofilament conglomeration of motoneurons in familial and sporadic amyotrophic lateral sclerosis. Mol Med. 4:1998;324-332.
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Chou, S.M.1
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Bucala, R.4
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33
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Persyn, a member of the synuclein family, influences neurofilament network integrity
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This short paper describes the selective degradation of NF-H by calcium-dependent proteases in cultured neurons transfected by persyn, a member of the synuclein family. This interesting observation may have implications for neurodegenerative diseases
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Buchman VL, Adu J, Pinon LG, Ninkina NN, Davies AM Persyn, a member of the synuclein family, influences neurofilament network integrity. Nat Neurosci. 1:1998;101-103. This short paper describes the selective degradation of NF-H by calcium-dependent proteases in cultured neurons transfected by persyn, a member of the synuclein family. This interesting observation may have implications for neurodegenerative diseases.
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Nat Neurosci
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Buchman, V.L.1
Adu, J.2
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Davies, A.M.5
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34
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0032976739
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Expanded polyglutamine domain proteins bind neurofilament and alter the neurofilament network
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Nagai Y, Onodera O, Chun J, Strittmatter WJ, Burke JR Expanded polyglutamine domain proteins bind neurofilament and alter the neurofilament network. Exp Neurol. 155:1999;195-203.
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Exp Neurol
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Nagai, Y.1
Onodera, O.2
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Burke, J.R.5
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35
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0033597898
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Integrators of the cytoskeleton that stabilize microtubules
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Yang Y, Bauer C, Strasser G, Wollman R, Julien JP, Fuchs E Integrators of the cytoskeleton that stabilize microtubules. Cell. 98:1999;229-238.
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Cell
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Yang, Y.1
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Wollman, R.4
Julien, J.P.5
Fuchs, E.6
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36
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0033535053
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The intermediate filament protein peripherin is the specific interaction partner of mouse BPAG1-n (dystonin) in neurons
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This paper reports that peripherin, rather than neurofilament proteins, is the major interaction partner for BPAG1-n (dystonin), which plays a role in sensory neuron function
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Leung CL, Sun D, Liem RKH The intermediate filament protein peripherin is the specific interaction partner of mouse BPAG1-n (dystonin) in neurons. J Cell Biol. 144:1999;435-446. This paper reports that peripherin, rather than neurofilament proteins, is the major interaction partner for BPAG1-n (dystonin), which plays a role in sensory neuron function.
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J Cell Biol
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Leung, C.L.1
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37
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0032809052
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Interactions between peripherin and neurofilaments in cultured cells: Disruption of peripherin assembly by the NF-M and NF-H subunits
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Beaulieu JM, Robertson J, Julien JP Interactions between peripherin and neurofilaments in cultured cells: disruption of peripherin assembly by the NF-M and NF-H subunits. Biochem Cell Biol. 77:1999;41-45.
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Biochem Cell Biol
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Beaulieu, J.M.1
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Julien, J.P.3
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38
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0242671888
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Mutation in neurofilament transgene implicates RNA processing in the pathogenesis of neurodegenerative disease
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This study describes the analysis of transgenic mice expressing a NF-L gene bearing a c-myc insert at the end of the NF-L coding region that contains a stability determinant of NF-L mRNA. The authors propose a novel mechanism of neurodegeneration for enteric and motor neurons based on alterations of RNA processing
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Canete-Soler R, Silberg DG, Gershon MD, Schlaepfer WW Mutation in neurofilament transgene implicates RNA processing in the pathogenesis of neurodegenerative disease. J Neurosci. 19:1999;1273-1283. This study describes the analysis of transgenic mice expressing a NF-L gene bearing a c-myc insert at the end of the NF-L coding region that contains a stability determinant of NF-L mRNA. The authors propose a novel mechanism of neurodegeneration for enteric and motor neurons based on alterations of RNA processing.
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J Neurosci
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Canete-Soler, R.1
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40
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Tu PH, Gurney ME, Julien JP, Lee VM, Trojanowski JQ Oxidative stress, mutant SOD1, and neurofilament pathology in transgenic mouse models of human motor neuron disease. Lab Invest. 76:1997;441-456.
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Lab Invest
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Tu, P.H.1
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SOD1 mutation is associated with accumulation of neurofilaments in amyotrophic lateral sclerosis
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Pathogenesis of two axonopathies does not require axonal neurofilaments
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The authors used mice expressing a NF-H-β-galactosidase fusion protein that causes perikaryal retention of neurofilaments to demonstrate that axonal neurofilaments are not required for disease caused by dystonin and by mutant SOD1
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Eyer J, Cleveland DW, Wong PC, Peterson AC Pathogenesis of two axonopathies does not require axonal neurofilaments. Nature. 391:1998;584-587. The authors used mice expressing a NF-H-β-galactosidase fusion protein that causes perikaryal retention of neurofilaments to demonstrate that axonal neurofilaments are not required for disease caused by dystonin and by mutant SOD1.
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Absence of neurofilaments reduces the selective vulnerability of motor neurons and slows disease caused by a familial amyotrophic lateral sclerosis-linked superoxide dismutase 1 mutant
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••]). The absence of NF-L increased the life span of mice expressing mutant SOD1. This could be attributable to perikaryal increases of NF-H and NF-M subunits and/or to a depletion of axonal neurofilaments
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••]). The absence of NF-L increased the life span of mice expressing mutant SOD1. This could be attributable to perikaryal increases of NF-H and NF-M subunits and/or to a depletion of axonal neurofilaments.
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0032483016
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Protective effect of neurofilament heavy gene overexpression in motor neuron disease induced by mutant superoxide dismutase
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G37R mice by up to 65%. The results suggest a protective effect of perikaryal accumulation of neurofilament proteins in motor neuron disease caused by mutant SOD1
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G37R mice by up to 65%. The results suggest a protective effect of perikaryal accumulation of neurofilament proteins in motor neuron disease caused by mutant SOD1.
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0032402093
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Glutamate potentiates the toxicity of mutant Cu/Zn-superoxide dismutase in motor neurons by postsynaptic calcium-dependent mechanisms
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Splice variant-specific interaction of the NMDA receptor subunit NR1 with neuronal intermediate filaments
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Ehlers MD, Fung ET, O'Brien RJ, Huganir RL Splice variant-specific interaction of the NMDA receptor subunit NR1 with neuronal intermediate filaments. J Neurosci. 18:1998;720-730.
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Slowing of axonal transport is a very early event in the toxicity of ALS-linked SOD1 mutants to motor neurons
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Neurofilaments and orthograde transport are reduced in ventral root axons of transgenic mice that express human SOD1 with a G93A mutation
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Zhang B, Tu P, Abtahian F, Trojanowski JQ, Lee VM Neurofilaments and orthograde transport are reduced in ventral root axons of transgenic mice that express human SOD1 with a G93A mutation. J Cell Biol. 139:1997;1307-1315.
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Aberrant stress-induced phosphorylation of perikaryal neurofilaments
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Giasson BI, Mushynski WE Aberrant stress-induced phosphorylation of perikaryal neurofilaments. J Biol Chem. 271:1996;30404-30409.
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Mitogen-activated protein kinases (Erk1,2) phosphorylate Lys-Ser-Pro (KSP) repeats in neurofilament proteins NF-H and NF-M
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While cyclin-dependent kinase 5 can phosphorylate specifically the KSPXK, where 'X' denotes any amino acid, repeats in NF-H, this paper demonstrates that neuronal Erk1 and Erk2 are capable of phosphorylating serine residues in diverse KSP repeat motifs in NF-M and NF-H proteins
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Veeranna Amin ND, Ahn NG, Jaffe H, Winters CA, Grant P, Pant HC Mitogen-activated protein kinases (Erk1,2) phosphorylate Lys-Ser-Pro (KSP) repeats in neurofilament proteins NF-H and NF-M. J Neurosci. 18:1998;4008-4021. While cyclin-dependent kinase 5 can phosphorylate specifically the KSPXK, where 'X' denotes any amino acid, repeats in NF-H, this paper demonstrates that neuronal Erk1 and Erk2 are capable of phosphorylating serine residues in diverse KSP repeat motifs in NF-M and NF-H proteins.
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Aberrant neurofilament phosphorylation in sensory neurons of rats with diabetic neuropathy
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