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of special interest. A comprehensive, up-to-date review on the biology and pathobiology of neurofilaments and related neuronal intermediate filaments.
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Lee MK, Cleveland DW. Neuronal intermediate filaments. of special interest Annu Rev Neurosci. 19:1996;187-217 A comprehensive, up-to-date review on the biology and pathobiology of neurofilaments and related neuronal intermediate filaments.
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Phosphorylation on carboxyl terminus domains of neurofilament proteins in retinal ganglion cell neurons in vivo: Influences on regional neurofilament accumulation, interneurofilament spacing, and axon caliber
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Nixon RA, Paskevich PA, Sihag RK, Thayer CY. Phosphorylation on carboxyl terminus domains of neurofilament proteins in retinal ganglion cell neurons in vivo: influences on regional neurofilament accumulation, interneurofilament spacing, and axon caliber. J Cell Biol. 126:1994;1031-1046.
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Hsieh S-T, Kidd GJ, Crawford TO, Xu Z, Lin W-M, Trapp BD, Cleveland DW, Griffin JW. Regional modulation of neurofilament organization by myelination in normal axons. J Neurosci. 14:1994;6392-6401.
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7
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0029781743
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Oligodendroglia regulate the regional expansion of axon caliber and local accumulation of neurofilaments during development independently of myelin formation
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of special interest. A three-fold caliber expansion and commensurate local neurofilament accumulation occur within 24 hours after optic axons are recruited for myelination. Analyses of myelin-deficient mutant mice show that focal oligodendroglial contact, and not myelin, provides the signal for neurofilaments to accumulate locally within axons.
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Sanchez I, Hassinger L, Paskevich PA, Shine HD, Nixon RA. Oligodendroglia regulate the regional expansion of axon caliber and local accumulation of neurofilaments during development independently of myelin formation. of special interest J Neurosci. 16:1996;5095-5105 A three-fold caliber expansion and commensurate local neurofilament accumulation occur within 24 hours after optic axons are recruited for myelination. Analyses of myelin-deficient mutant mice show that focal oligodendroglial contact, and not myelin, provides the signal for neurofilaments to accumulate locally within axons.
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Sanchez, I.1
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8
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85030300790
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The dynamic behavior and organization of cytoskeletal proteins in neurons: Reconciling old and new findings
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of special interest. A critical re-evaluation of existing axonal transport data and new structural studies. The concept of a stationary but dynamic axon cytoskeleton is discussed as a model for slow transport that accommodates old and new findings
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Nixon RA. The dynamic behavior and organization of cytoskeletal proteins in neurons: reconciling old and new findings. of special interest Bioessays. 1997; A critical re-evaluation of existing axonal transport data and new structural studies. The concept of a stationary but dynamic axon cytoskeleton is discussed as a model for slow transport that accommodates old and new findings.
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Bioessays
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Nixon, R.A.1
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9
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0031558020
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The axons as a metabolic compartment: Protein degradation, transport, and maximum length of an axon
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of special interest. A provocative reconsideration of earlier data is the basis of a model, with predictive value, that relates steady-state levels of cytoskeletal proteins to the rates of slow transport and protein degradation along axons.
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Miller KE, Samuels DC. The axons as a metabolic compartment: protein degradation, transport, and maximum length of an axon. of special interest J Theor Biol. 186:1997;373-379 A provocative reconsideration of earlier data is the basis of a model, with predictive value, that relates steady-state levels of cytoskeletal proteins to the rates of slow transport and protein degradation along axons.
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Miller, K.E.1
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10
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0030028366
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Selective stabilization of tau in axons and microtubule-associated protein 2C in cell bodies and dendrites contributes to polarized localization of cytoskeletal proteins in mature neurons
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of special interest. Differential localization of mRNA and suppression of transport have previously been identified as mechanisms governing the polarized localization of MAP2 and tau in neurons. Here, microinjected biotinylated tau and MAP2C were shown to be resistant to proteolysis only within the neuronal compartments within which they are normally localized, emphasizing the role of selective protein turnover in regulating cytoskeleton composition.
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Hirokawa N, Funakoski T, Sato-Harada R, Kanil Y. Selective stabilization of tau in axons and microtubule-associated protein 2C in cell bodies and dendrites contributes to polarized localization of cytoskeletal proteins in mature neurons. of special interest J Cell Biol. 132:1996;667-679 Differential localization of mRNA and suppression of transport have previously been identified as mechanisms governing the polarized localization of MAP2 and tau in neurons. Here, microinjected biotinylated tau and MAP2C were shown to be resistant to proteolysis only within the neuronal compartments within which they are normally localized, emphasizing the role of selective protein turnover in regulating cytoskeleton composition.
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Hirokawa, N.1
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Xu Z, Marszalek JR, Lee MK, Wong PC, Folmer J, Crawford O, Hsieh ST, Griffin JW, Cleveland DW. Subunit composition of neurofilaments specifies axonal diameter. J Cell Biol. 133:1996;1061-1069.
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Mechanical effects of neurofilament cross-bridges. Modulation by phosphorylation, lipids, and interactions with F-actin
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of outstanding interest. Single neurofilaments were shown to be flexible coiled structures which unravel into long filaments when allowed to form viscoelastic networks spontaneously in vitro - a process modulated by phosphorylation and involving the formation of extensive cross-bridges between the sidearms of neighboring filaments. The results imply that neurofilaments are intrinsically interactive.
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Leterrier JF, Kas J, Vegners R, Janmey PA. Mechanical effects of neurofilament cross-bridges. Modulation by phosphorylation, lipids, and interactions with F-actin. of outstanding interest J Biol Chem. 271:1996;15687-15694 Single neurofilaments were shown to be flexible coiled structures which unravel into long filaments when allowed to form viscoelastic networks spontaneously in vitro - a process modulated by phosphorylation and involving the formation of extensive cross-bridges between the sidearms of neighboring filaments. The results imply that neurofilaments are intrinsically interactive.
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Leterrier, J.F.1
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Burgoyne R.D. New York: Alan R Liss, Inc
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Hirokawa N. Molecular architecture and dynamics of the neuronal cytoskeleton. Burgoyne RD. The Neuronal Cytoskeleton. 1991;5-74 Alan R Liss, Inc, New York.
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Hirokawa, N.1
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14
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0023766743
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MAP2c is a component of crossbridges between microtubules and neurofilaments in vivo and in vitro. Quick-freeze, deep-etch immunoelectron microscopy and reconstitution studies
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Hirokawa N, Hisanaga S, Shiomura Y. MAP2c is a component of crossbridges between microtubules and neurofilaments in vivo and in vitro. Quick-freeze, deep-etch immunoelectron microscopy and reconstitution studies. J Neurosci. 8:1988;2769-2779.
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Cross-linker system between neurofilaments, microtubules, and membranous organelles in frog axons revealed by the quick-freeze, deep-etching method
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An essential cytoskeletal linker protein connecting actin microfilaments to intermediate filaments
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of outstanding interest. A neuronal splice variant of the BPAG-1 gene (BPAG-1n), which is defective in dystonia musculorum mice, was localized to sensory axons. BPAG-1 was shown to bind actin at its amino terminus and intermediate filaments at its carboxyl terminus, as well as to establish a neurofilament - microfilament network in transfected cells. Sensory neurons of BPAG-1-null mice display disrupted axonal architecture and ultimately degenerate, suggesting an important cross-linking role for BPAG-1 in axons.
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Yang Y, Dowling J, Yu QC, Kouklis P, Cleveland DW, Fuchs E. An essential cytoskeletal linker protein connecting actin microfilaments to intermediate filaments. of outstanding interest Cell. 86:1996;655-665 A neuronal splice variant of the BPAG-1 gene (BPAG-1n), which is defective in dystonia musculorum mice, was localized to sensory axons. BPAG-1 was shown to bind actin at its amino terminus and intermediate filaments at its carboxyl terminus, as well as to establish a neurofilament - microfilament network in transfected cells. Sensory neurons of BPAG-1-null mice display disrupted axonal architecture and ultimately degenerate, suggesting an important cross-linking role for BPAG-1 in axons.
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Yang, Y.1
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of special interest. A concise summary of evidence supporting a slow axonal transport model in which cytoskeletal protein subunits are viewed as the precursors to a large stationary axonal cytoskeleton.
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Hirokawa N, Terada S, Funakoshi T, Takeda S. Slow axonal transport: the subunit transport model. of special interest Trends Cell Biol. 7:1997;384-388 A concise summary of evidence supporting a slow axonal transport model in which cytoskeletal protein subunits are viewed as the precursors to a large stationary axonal cytoskeleton.
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Hirokawa, N.1
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21
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of special interest. A concise summary of evidence supporting a slow axonal transport model in which the axonal cytoskeleton is viewed as a continuously moving structure composed of sliding cytoskeletal polymers.
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Baas PW, Brown A. Slow axonal transport: the polymer transport model. of special interest Trends Cell Biol. 7:1997;380-384 A concise summary of evidence supporting a slow axonal transport model in which the axonal cytoskeleton is viewed as a continuously moving structure composed of sliding cytoskeletal polymers.
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Baas, P.W.1
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Neurofilament subunit NF-H modulates axonal diameter by selectively slowing neurofilament transport
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of outstanding interest. Neurofilament transport is selectively retarded, neurofilaments accumulate, and caliber expands modestly when wild-type mouse NFH is overexpressed twofold in transgenic mice, implying a role for NFH in determining transport rate. Higher expression causes a more exaggerated effect proximally, with distal atrophy but no cell loss as seen in mice overexpressing human NFH.
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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. of outstanding interest J Cell Biol. 135:1996;711-724 Neurofilament transport is selectively retarded, neurofilaments accumulate, and caliber expands modestly when wild-type mouse NFH is overexpressed twofold in transgenic mice, implying a role for NFH in determining transport rate. Higher expression causes a more exaggerated effect proximally, with distal atrophy but no cell loss as seen in mice overexpressing human NFH.
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Marszalek, J.R.1
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24
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Giasson BI, Mushynski WE. Okadaic acid reversibly inhibits neurite outgrowth in embryonic dorsal root ganglion neurons. J Neurobiol. 32:1997;193-201.
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Sihag RK, Nixon RA. 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. 266:1991;18861-18867.
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0030065110
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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
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of special interest. Although neurofilaments are usually considered to be irreversible polymers, these experiments demonstrate that increasing the phosphorylation state of the amino terminus of NFL - a domain known to regulate assembly - fragments neurofilaments into oligomeric structures within intact neurons.
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Giasson BI, Cromlish JA, Athlan ES, Mushynski WE. 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. of special interest J Neurochem. 66:1996;113-120 Although neurofilaments are usually considered to be irreversible polymers, these experiments demonstrate that increasing the phosphorylation state of the amino terminus of NFL - a domain known to regulate assembly - fragments neurofilaments into oligomeric structures within intact neurons.
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Visualization of slow axonal transport in vivo
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of outstanding interest. Neurons of transgenic mice lacking axonal neurofilaments were infected with a recombinant adenoviral vector encoding epitope-tagged NFM. Confocal and electron microscopy revealed that virally encoded subunits were transported in unpolymerized form at a typical slow rate along microtubules, supporting the idea that subunits could serve as transport intermediates for axonal neurofilaments.
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Terada S, Nakata T, Peterson AC, Hirokawa N. Visualization of slow axonal transport in vivo. of outstanding interest Science. 273:1996;784-788 Neurons of transgenic mice lacking axonal neurofilaments were infected with a recombinant adenoviral vector encoding epitope-tagged NFM. Confocal and electron microscopy revealed that virally encoded subunits were transported in unpolymerized form at a typical slow rate along microtubules, supporting the idea that subunits could serve as transport intermediates for axonal neurofilaments.
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Terada, S.1
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0030973429
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Triton-soluble phosphovariants of the heavy subunit in developing and mature mouse CNS
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of special interest. A substantial pool of extensively phosphorylated NFH subunits exists in developing neurons and persists in the perikarya of mature neurons, consistent with the evidence that NFH may have a more dynamic association with neurofilaments than the other subunits do.
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Shea TB, Nixon RA, Dahl DA, Fischer I. Triton-soluble phosphovariants of the heavy subunit in developing and mature mouse CNS. of special interest J Neurosci Res. 48:1997;515-523 A substantial pool of extensively phosphorylated NFH subunits exists in developing neurons and persists in the perikarya of mature neurons, consistent with the evidence that NFH may have a more dynamic association with neurofilaments than the other subunits do.
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J Neurosci Res
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Shea, T.B.1
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Fischer, I.4
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Increased solubility of high-molecular-mass neurofilament subunit by suppression of dephosphorylation: Its relation to axonal transport
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of special interest. Analyses of neurofilaments isolated from peripheral nerves in the presence of phosphatase inhibitors revealed that 20% of the total NFH was Triton soluble and, in in vivo pulse-radiolabeling studies, migrated within the leading edge of the NFH transport wave.
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Tsuda M, Tashiro T, Komiya Y. Increased solubility of high-molecular-mass neurofilament subunit by suppression of dephosphorylation: its relation to axonal transport. of special interest J Neurochem. 68:1997;2558-2565 Analyses of neurofilaments isolated from peripheral nerves in the presence of phosphatase inhibitors revealed that 20% of the total NFH was Triton soluble and, in in vivo pulse-radiolabeling studies, migrated within the leading edge of the NFH transport wave.
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J Neurochem
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Dynamic microtubule ends are required for growth cone turning to avoid an inhibitory guidance cue
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of special interest. Low concentrations of taxol or vinblastine that block microtubule assembly in cultured dorsal root ganglion neurons reduced the rate of neurite elongation and completely inhibited growth cone turning, highlighting the importance of local microtubule assembly in these processes.
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Challacombe JF, Snow DM, LeTourneau PC. Dynamic microtubule ends are required for growth cone turning to avoid an inhibitory guidance cue. of special interest J Neurosci. 17:1997;3085-3095 Low concentrations of taxol or vinblastine that block microtubule assembly in cultured dorsal root ganglion neurons reduced the rate of neurite elongation and completely inhibited growth cone turning, highlighting the importance of local microtubule assembly in these processes.
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Challacombe, J.F.1
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Microtubule stability decreases axon elongation but not axoplasm production
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of special interest. Nocodozole treatment of superior cervical ganglion cell neurons decreased the dynamic instability, but not the net assembly, of microtubules and reduced axon elongation.
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Rochlin MW, Wickline KM, Bridgman PC. Microtubule stability decreases axon elongation but not axoplasm production. of special interest J Neurosci. 16:1996;3236-3246 Nocodozole treatment of superior cervical ganglion cell neurons decreased the dynamic instability, but not the net assembly, of microtubules and reduced axon elongation.
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Rochlin, M.W.1
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Microtubule transport and assembly during axon growth
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of special interest. After biotinylated tubulin is injected into cultured neurons that are extending axons, a small fraction of the microtubules appearing in the newly grown axon are unlabeled, consistent with the authors' view that these are axonal microtubules formed before the injection that had translocated into the growing axon.
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Wenqian YU, Schwei MJ, Baas PW. Microtubule transport and assembly during axon growth. of special interest J Cell Biol. 133:1996;151-157 After biotinylated tubulin is injected into cultured neurons that are extending axons, a small fraction of the microtubules appearing in the newly grown axon are unlabeled, consistent with the authors' view that these are axonal microtubules formed before the injection that had translocated into the growing axon.
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Rapid transport of foreign particles microinjected into crab axons
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Adams RJ, Bray D. Rapid transport of foreign particles microinjected into crab axons. Nature. 303:1983;718-720.
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Nature
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Adams, R.J.1
Bray, D.2
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40
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0030003894
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Tubulin transport in neurons
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of outstanding interest. Fluorescent tubulin injected into neurons in the presence of vinblastine moved from the cell body as a discrete wave of tubulin subunits, and microinjected fluorescent microtubules stabilized against depolymerization remained stationary within the cell body.
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Miller KE, Joshi HC. Tubulin transport in neurons. of outstanding interest J Cell Biol. 133:1996;1355-1366 Fluorescent tubulin injected into neurons in the presence of vinblastine moved from the cell body as a discrete wave of tubulin subunits, and microinjected fluorescent microtubules stabilized against depolymerization remained stationary within the cell body.
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(1996)
J Cell Biol
, vol.133
, pp. 1355-1366
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Miller, K.E.1
Joshi, H.C.2
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41
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0023837441
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Polewards chromosome movement driven by microtubule depolymerization in vitro
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Koshland DE, Mitchison TJ, Kirschner MW. Polewards chromosome movement driven by microtubule depolymerization in vitro. Nature. 331:1988;499-504.
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(1988)
Nature
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Koshland, D.E.1
Mitchison, T.J.2
Kirschner, M.W.3
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42
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0031010658
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Microtubule release from the centrosome
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Keating TJ, Poloquin JG, Rodionov VI, Momcilovic D, Borisy GG. Microtubule release from the centrosome. Proc Natl Acad Sci USA. 94:1997;5078-5083.
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Proc Natl Acad Sci USA
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Keating, T.J.1
Poloquin, J.G.2
Rodionov, V.I.3
Momcilovic, D.4
Borisy, G.G.5
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43
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0029849616
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Delivery of newly synthesized tubulin to rapidly growing distal axons of rat sympathetic neurons in compartmented cultures
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of outstanding interest. In a compartmentalized neuronal paradigm, more than 90% of the pulse-radiolabeled tubulin arrives at terminal regions of growing sensory neurons at a rate ocnsistent with movement of soluble monomers, thus supporting earlier findings that microtubules are actively assembled at the distal ends of growing axons.
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Campenot RB, Lund K, Senger DL. Delivery of newly synthesized tubulin to rapidly growing distal axons of rat sympathetic neurons in compartmented cultures. of outstanding interest J Cell Biol. 135:1996;701-709 In a compartmentalized neuronal paradigm, more than 90% of the pulse-radiolabeled tubulin arrives at terminal regions of growing sensory neurons at a rate ocnsistent with movement of soluble monomers, thus supporting earlier findings that microtubules are actively assembled at the distal ends of growing axons.
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(1996)
J Cell Biol
, vol.135
, pp. 701-709
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Campenot, R.B.1
Lund, K.2
Senger, D.L.3
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44
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0029898806
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Active transport of photoactivated tubulin molecules in growing axons revealed by a new electron microscopic analysis
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of special interest. Immunogold electron microscopic analysis of fluorescein-labeled free tubulin and microtubules within photobleached zones along axons showed that soluble tubulin, but not microtubules, moved in an anterograde direction, in support of the subunit hypothesis of microtubule transport.
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Funakoshi T, Takeda S, Hirokawa N. Active transport of photoactivated tubulin molecules in growing axons revealed by a new electron microscopic analysis. of special interest J Cell Biol. 133:1996;1347-1353 Immunogold electron microscopic analysis of fluorescein-labeled free tubulin and microtubules within photobleached zones along axons showed that soluble tubulin, but not microtubules, moved in an anterograde direction, in support of the subunit hypothesis of microtubule transport.
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(1996)
J Cell Biol
, vol.133
, pp. 1347-1353
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Funakoshi, T.1
Takeda, S.2
Hirokawa, N.3
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45
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0029799252
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Slow axonal transport of soluble actin with actin depolymerizing factor, cofilin, and profilin suggests actin moves in an unassembled form
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of special interest. After the pulse-radiolabeling of chick motor neurons, a two- to threefold higher specific radioactivity of soluble actin compared with that of particulate actin in sciatic nerves suggests that labeled soluble monomer exchanged with subunits of unlabeled stationary microfilaments present in axons before isotope injection.
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Mills RG, Minamide LS, Yuan A, Bamburg JR, Bray JJ. Slow axonal transport of soluble actin with actin depolymerizing factor, cofilin, and profilin suggests actin moves in an unassembled form. of special interest J Neurochem. 67:1996;1225-1234 After the pulse-radiolabeling of chick motor neurons, a two- to threefold higher specific radioactivity of soluble actin compared with that of particulate actin in sciatic nerves suggests that labeled soluble monomer exchanged with subunits of unlabeled stationary microfilaments present in axons before isotope injection.
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(1996)
J Neurochem
, vol.67
, pp. 1225-1234
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Mills, R.G.1
Minamide, L.S.2
Yuan, A.3
Bamburg, J.R.4
Bray, J.J.5
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46
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0029588380
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Three distinct axonal transport rates for tau, tubulin, and other microtubule-associated proteins
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Mercken M, Fischer I, Kosik KS, Nixon RA. Three distinct axonal transport rates for tau, tubulin, and other microtubule-associated proteins. J Neurosci. 15:1995;8259-8267.
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(1995)
J Neurosci
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Mercken, M.1
Fischer, I.2
Kosik, K.S.3
Nixon, R.A.4
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47
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0030813929
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Selective destruction of stable microtubules and axons by inhibitors of protein serine/threonine phosphatases in cultured human neurons (NT2N cells)
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of special interest. Okadaic acid treatment of NT2N cells increased tau phosphorylation, decreased the binding of tau to microtubules, and selectively depolymerized the more stable detyrosinated axonal microtubules, implying a role for phosphorylation in regulating microtubule assembly in axons.
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Merrick SE, Tjojanowski JQ, Lee VMY. Selective destruction of stable microtubules and axons by inhibitors of protein serine/threonine phosphatases in cultured human neurons (NT2N cells). of special interest J Neurosci. 17:1997;5726-5737 Okadaic acid treatment of NT2N cells increased tau phosphorylation, decreased the binding of tau to microtubules, and selectively depolymerized the more stable detyrosinated axonal microtubules, implying a role for phosphorylation in regulating microtubule assembly in axons.
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(1997)
J Neurosci
, vol.17
, pp. 5726-5737
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Merrick, S.E.1
Tjojanowski, J.Q.2
Lee, V.M.Y.3
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48
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0027531842
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The regulation of neurofilament protein dynamics by phosphorylation: Clues to neurofibrillary pathobiology
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Nixon RA. The regulation of neurofilament protein dynamics by phosphorylation: clues to neurofibrillary pathobiology. Brain Pathol. 3:1993;29-38.
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(1993)
Brain Pathol
, vol.3
, pp. 29-38
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Nixon, R.A.1
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49
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0028900588
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Two distinct functions of the carboxyl terminal tail domain of NF-M upon neurofilament assembly: Cross-bridge formation and longitudinal elongation of filaments
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Nakagawa T, Chen J, Zhang Z, Kanai Y, Hirokawa N. Two distinct functions of the carboxyl terminal tail domain of NF-M upon neurofilament assembly: cross-bridge formation and longitudinal elongation of filaments. J Cell Biol. 129:1995;411-429.
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(1995)
J Cell Biol
, vol.129
, pp. 411-429
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Nakagawa, T.1
Chen, J.2
Zhang, Z.3
Kanai, Y.4
Hirokawa, N.5
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50
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85058206382
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Local accumulation and increased spacing of neurofilaments accompanying axon caliber growth are associated in district NFH phosphorylation events [abstract]
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Sanchez I, Hassinger L, Paskevich PA, Nixon RA. Local accumulation and increased spacing of neurofilaments accompanying axon caliber growth are associated in district NFH phosphorylation events [abstract]. Mol Biol Cell. 6:1995;100a.
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(1995)
Mol Biol Cell
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Sanchez, I.1
Hassinger, L.2
Paskevich, P.A.3
Nixon, R.A.4
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51
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0010635682
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Ultrastructural localization, expression, and activation state of neurofilament kinases during CNS development [abstract]
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Sanchez I, Hassinger L, Wheelock T, Santeufemio C, Hauser G, Nixon RA. Ultrastructural localization, expression, and activation state of neurofilament kinases during CNS development [abstract]. Soc Neurosci. 22:1996;1977.
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(1996)
Soc Neurosci
, vol.22
, pp. 1977
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Sanchez, I.1
Hassinger, L.2
Wheelock, T.3
Santeufemio, C.4
Hauser, G.5
Nixon, R.A.6
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53
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0030071079
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Cytoplasmic dynein is associated with slow axonal transport
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of special interest. The axonal transport of pulse-radiolabeled dynein, a retrograde transport motor, was studied in optic axons in vivo. Nearly 80% of the immunoprecipitated labeled dynein was found associated with the SCb phase of slow transport and can bind microtubules in an ATP-dependent manner in vitro, suggesting that it may be functionally active during its anterograde migration, possibly as an anterograde microtubule motor.
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Dillman JF, Dabney LP, Pfister KK. Cytoplasmic dynein is associated with slow axonal transport. of special interest Proc Natl Acad Sci USA. 93:1996;141-144 The axonal transport of pulse-radiolabeled dynein, a retrograde transport motor, was studied in optic axons in vivo. Nearly 80% of the immunoprecipitated labeled dynein was found associated with the SCb phase of slow transport and can bind microtubules in an ATP-dependent manner in vitro, suggesting that it may be functionally active during its anterograde migration, possibly as an anterograde microtubule motor.
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(1996)
Proc Natl Acad Sci USA
, vol.93
, pp. 141-144
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Dillman, J.F.1
Dabney, L.P.2
Pfister, K.K.3
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54
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0028304474
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Ultrastructural analysis of the dynactin complex: An actin-related protein is a component of a filament that resembles F-actin
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Schafer DA, Gill SR, Copper JA, Heuser JE, Schroer TA. Ultrastructural analysis of the dynactin complex: an actin-related protein is a component of a filament that resembles F-actin. J Cell Biol. 126:1994;403-412.
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(1994)
J Cell Biol
, vol.126
, pp. 403-412
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Schafer, D.A.1
Gill, S.R.2
Copper, J.A.3
Heuser, J.E.4
Schroer, T.A.5
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55
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0029926565
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Functional analysis of dynactin and cytoplasmic dynein in slow axonal transport
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of special interest. Dynactin, an activator of the cytoplasmic motor protein dynein, binds dynein and possibly microfilaments. In vivo pulse-radiolabeled components of dynactin, like dynein, were shown to migrate along optic axons, principally at rate of transport, raising suspicions that a dynactin - dynein linkage to the SCb complex could be involved in anterograde transport of microtubules.
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Dillman JF, Dabney LP, Karki S, Paschal BM, Holzbaur ELF, Pfister KK. Functional analysis of dynactin and cytoplasmic dynein in slow axonal transport. of special interest J Neurosci. 16:1996;6742-6752 Dynactin, an activator of the cytoplasmic motor protein dynein, binds dynein and possibly microfilaments. In vivo pulse-radiolabeled components of dynactin, like dynein, were shown to migrate along optic axons, principally at rate of transport, raising suspicions that a dynactin - dynein linkage to the SCb complex could be involved in anterograde transport of microtubules.
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(1996)
J Neurosci
, vol.16
, pp. 6742-6752
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Dillman, J.F.1
Dabney, L.P.2
Karki, S.3
Paschal, B.M.4
Holzbaur, E.L.F.5
Pfister, K.K.6
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56
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0029367097
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Neurofilament phosphorylation
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Pant HC, Veeranna. Neurofilament phosphorylation. Biochem Cell Biol. 73:1995;575-592.
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(1995)
Biochem Cell Biol
, vol.73
, pp. 575-592
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Pant, H.C.1
Veeranna2
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