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Volumn 31, Issue 7, 2008, Pages 343-352

Chromatin and nuclear architecture in the nervous system

Author keywords

[No Author keywords available]

Indexed keywords

HISTONE DEACETYLASE INHIBITOR;

EID: 45849146938     PISSN: 01662236     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tins.2008.03.005     Document Type: Review
Times cited : (55)

References (107)
  • 1
    • 18744375181 scopus 로고    scopus 로고
    • Concepts in nuclear architecture
    • Misteli T. Concepts in nuclear architecture. Bioessays 27 (2005) 477-487
    • (2005) Bioessays , vol.27 , pp. 477-487
    • Misteli, T.1
  • 2
    • 16844373902 scopus 로고    scopus 로고
    • PML bodies: a meeting place for genomic loci?
    • Ching R.W., et al. PML bodies: a meeting place for genomic loci?. J. Cell Sci. 118 (2005) 847-854
    • (2005) J. Cell Sci. , vol.118 , pp. 847-854
    • Ching, R.W.1
  • 3
    • 33744831161 scopus 로고    scopus 로고
    • Structure of the '30 nm' chromatin fibre: a key role for the linker histone
    • Robinson P.J., and Rhodes D. Structure of the '30 nm' chromatin fibre: a key role for the linker histone. Curr. Opin. Struct. Biol. 16 (2006) 336-343
    • (2006) Curr. Opin. Struct. Biol. , vol.16 , pp. 336-343
    • Robinson, P.J.1    Rhodes, D.2
  • 4
    • 0348150714 scopus 로고    scopus 로고
    • Maintenance of stable heterochromatin domains by dynamic HP1 binding
    • Cheutin T., et al. Maintenance of stable heterochromatin domains by dynamic HP1 binding. Science 299 (2003) 721-725
    • (2003) Science , vol.299 , pp. 721-725
    • Cheutin, T.1
  • 5
    • 0035793376 scopus 로고    scopus 로고
    • Protein dynamics: implications for nuclear architecture and gene expression
    • Misteli T. Protein dynamics: implications for nuclear architecture and gene expression. Science 291 (2001) 843-847
    • (2001) Science , vol.291 , pp. 843-847
    • Misteli, T.1
  • 6
    • 0034649663 scopus 로고    scopus 로고
    • Dynamic binding of histone H1 to chromatin in living cells
    • Misteli T., et al. Dynamic binding of histone H1 to chromatin in living cells. Nature 408 (2000) 877-881
    • (2000) Nature , vol.408 , pp. 877-881
    • Misteli, T.1
  • 7
    • 0034611785 scopus 로고    scopus 로고
    • High mobility of proteins in the mammalian cell nucleus
    • Phair R.D., and Misteli T. High mobility of proteins in the mammalian cell nucleus. Nature 404 (2000) 604-609
    • (2000) Nature , vol.404 , pp. 604-609
    • Phair, R.D.1    Misteli, T.2
  • 8
    • 0020464770 scopus 로고
    • Analysis of chromosome positions in the interphase nucleus of Chinese hamster cells by laser-UV-microirradiation experiments
    • Cremer T., et al. Analysis of chromosome positions in the interphase nucleus of Chinese hamster cells by laser-UV-microirradiation experiments. Hum. Genet. 62 (1982) 201-209
    • (1982) Hum. Genet. , vol.62 , pp. 201-209
    • Cremer, T.1
  • 9
    • 22944489197 scopus 로고    scopus 로고
    • Silence of the genes - mechanisms of long-term repression
    • Lande-Diner L., and Cedar H. Silence of the genes - mechanisms of long-term repression. Nat. Rev. Genet. 6 (2005) 648-654
    • (2005) Nat. Rev. Genet. , vol.6 , pp. 648-654
    • Lande-Diner, L.1    Cedar, H.2
  • 10
    • 0021235210 scopus 로고
    • Different central nervous system cell types display distinct and nonrandom arrangements of satellite DNA sequences
    • Manuelidis L. Different central nervous system cell types display distinct and nonrandom arrangements of satellite DNA sequences. Proc. Natl. Acad. Sci. U. S. A. 81 (1984) 3123-3127
    • (1984) Proc. Natl. Acad. Sci. U. S. A. , vol.81 , pp. 3123-3127
    • Manuelidis, L.1
  • 11
    • 0021892886 scopus 로고
    • Indications of centromere movement during interphase and differentiation
    • Manuelidis L. Indications of centromere movement during interphase and differentiation. Ann. N. Y. Acad. Sci. 450 (1985) 205-221
    • (1985) Ann. N. Y. Acad. Sci. , vol.450 , pp. 205-221
    • Manuelidis, L.1
  • 12
    • 0025649160 scopus 로고
    • A view of interphase chromosomes
    • Manuelidis L. A view of interphase chromosomes. Science 250 (1990) 1533-1540
    • (1990) Science , vol.250 , pp. 1533-1540
    • Manuelidis, L.1
  • 13
    • 3242748982 scopus 로고    scopus 로고
    • Positional changes of pericentromeric heterochromatin and nucleoli in postmitotic Purkinje cells during murine cerebellum development
    • Solovei I., et al. Positional changes of pericentromeric heterochromatin and nucleoli in postmitotic Purkinje cells during murine cerebellum development. Cytogenet. Genome Res. 105 (2004) 302-310
    • (2004) Cytogenet. Genome Res. , vol.105 , pp. 302-310
    • Solovei, I.1
  • 14
    • 33646514631 scopus 로고    scopus 로고
    • Nuclear organization and dynamics of transcription sites in rat sensory ganglia neurons detected by incorporation of 5′-fluorouridine into nascent RNA
    • Casafont I., et al. Nuclear organization and dynamics of transcription sites in rat sensory ganglia neurons detected by incorporation of 5′-fluorouridine into nascent RNA. Neuroscience 140 (2006) 453-462
    • (2006) Neuroscience , vol.140 , pp. 453-462
    • Casafont, I.1
  • 15
    • 0035809126 scopus 로고    scopus 로고
    • Neuronal body size correlates with the number of nucleoli and Cajal bodies, and with the organization of the splicing machinery in rat trigeminal ganglion neurons
    • Pena E., et al. Neuronal body size correlates with the number of nucleoli and Cajal bodies, and with the organization of the splicing machinery in rat trigeminal ganglion neurons. J. Comp. Neurol. 430 (2001) 250-263
    • (2001) J. Comp. Neurol. , vol.430 , pp. 250-263
    • Pena, E.1
  • 16
    • 0030696889 scopus 로고    scopus 로고
    • Changes in morphology and spatial position of coiled bodies during NGF-induced neuronal differentiation of PC12 cells
    • Janevski J., et al. Changes in morphology and spatial position of coiled bodies during NGF-induced neuronal differentiation of PC12 cells. J. Histochem. Cytochem. 45 (1997) 1523-1531
    • (1997) J. Histochem. Cytochem. , vol.45 , pp. 1523-1531
    • Janevski, J.1
  • 17
    • 0029923029 scopus 로고    scopus 로고
    • Neuronal differentiation in the rat hippocampus involves a stage-specific reorganization of subnuclear structure both in vivo and in vitro
    • Santama N., et al. Neuronal differentiation in the rat hippocampus involves a stage-specific reorganization of subnuclear structure both in vivo and in vitro. Eur. J. Neurosci. 8 (1996) 892-905
    • (1996) Eur. J. Neurosci. , vol.8 , pp. 892-905
    • Santama, N.1
  • 18
    • 33749157645 scopus 로고    scopus 로고
    • Nuclear and chromatin reorganization in the MHC-Oct3/4 locus at developmental phases of embryonic stem cell differentiation
    • Aoto T., et al. Nuclear and chromatin reorganization in the MHC-Oct3/4 locus at developmental phases of embryonic stem cell differentiation. Dev. Biol. 298 (2006) 354-367
    • (2006) Dev. Biol. , vol.298 , pp. 354-367
    • Aoto, T.1
  • 19
    • 2342524701 scopus 로고    scopus 로고
    • PML bodies in reactive sensory ganglion neurons of the Guillain-Barre syndrome
    • Villagra N.T., et al. PML bodies in reactive sensory ganglion neurons of the Guillain-Barre syndrome. Neurobiol. Dis. 16 (2004) 158-168
    • (2004) Neurobiol. Dis. , vol.16 , pp. 158-168
    • Villagra, N.T.1
  • 20
    • 33947679342 scopus 로고    scopus 로고
    • Activity-dependent AIDA-1 nuclear signaling regulates nucleolar numbers and protein synthesis in neurons
    • Jordan B.A., et al. Activity-dependent AIDA-1 nuclear signaling regulates nucleolar numbers and protein synthesis in neurons. Nat. Neurosci. 10 (2007) 427-435
    • (2007) Nat. Neurosci. , vol.10 , pp. 427-435
    • Jordan, B.A.1
  • 21
    • 29744447772 scopus 로고    scopus 로고
    • Hyperdynamic plasticity of chromatin proteins in pluripotent embryonic stem cells
    • Meshorer E., et al. Hyperdynamic plasticity of chromatin proteins in pluripotent embryonic stem cells. Dev. Cell 10 (2006) 105-116
    • (2006) Dev. Cell , vol.10 , pp. 105-116
    • Meshorer, E.1
  • 22
    • 33745865934 scopus 로고    scopus 로고
    • Chromatin in pluripotent embryonic stem cells and differentiation
    • Meshorer E., and Misteli T. Chromatin in pluripotent embryonic stem cells and differentiation. Nat. Rev. Mol. Cell Biol. 7 (2006) 540-546
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 540-546
    • Meshorer, E.1    Misteli, T.2
  • 23
    • 0025802982 scopus 로고
    • Ultrastructural characteristics of human adult and infant cerebral cortical neurons
    • Ong W.Y., and Garey L.J. Ultrastructural characteristics of human adult and infant cerebral cortical neurons. J. Anat. 175 (1991) 79-104
    • (1991) J. Anat. , vol.175 , pp. 79-104
    • Ong, W.Y.1    Garey, L.J.2
  • 24
    • 0017091251 scopus 로고
    • Comparison of the number of RNA initiation sites in rat brain fractions enriched in neuronal or glial nuclei
    • Sarkander H.I., and Uthoff C.G. Comparison of the number of RNA initiation sites in rat brain fractions enriched in neuronal or glial nuclei. FEBS Lett. 72 (1976) 53-56
    • (1976) FEBS Lett. , vol.72 , pp. 53-56
    • Sarkander, H.I.1    Uthoff, C.G.2
  • 25
    • 0028072746 scopus 로고
    • Transcription and motoneuron size
    • Sato S., et al. Transcription and motoneuron size. J. Neurochem. 63 (1994) 1609-1615
    • (1994) J. Neurochem. , vol.63 , pp. 1609-1615
    • Sato, S.1
  • 26
    • 0019312794 scopus 로고
    • Chromatin repeat length correlates with phenotypic expression in hepatoma cells, their dedifferentiated variants, and somatic hybrids
    • Sperling L., and Weiss M.C. Chromatin repeat length correlates with phenotypic expression in hepatoma cells, their dedifferentiated variants, and somatic hybrids. Proc. Natl. Acad. Sci. U. S. A. 77 (1980) 3412-3416
    • (1980) Proc. Natl. Acad. Sci. U. S. A. , vol.77 , pp. 3412-3416
    • Sperling, L.1    Weiss, M.C.2
  • 27
    • 0018142517 scopus 로고
    • The chromatin repeat length of cortical neurons shortens during early postnatal development
    • Ermini M., and Kuenzle C.C. The chromatin repeat length of cortical neurons shortens during early postnatal development. FEBS Lett. 90 (1978) 167-172
    • (1978) FEBS Lett. , vol.90 , pp. 167-172
    • Ermini, M.1    Kuenzle, C.C.2
  • 28
    • 0020341183 scopus 로고
    • The chromatin repeat length of brain cortex and cerebellar neurons changes concomitant with terminal differentiation
    • Jaeger A.W., and Kuenzle C.C. The chromatin repeat length of brain cortex and cerebellar neurons changes concomitant with terminal differentiation. EMBO J. 1 (1982) 811-816
    • (1982) EMBO J. , vol.1 , pp. 811-816
    • Jaeger, A.W.1    Kuenzle, C.C.2
  • 29
    • 0020558835 scopus 로고
    • Chromatin structure in neuronal and neuroglial cell nuclei as a function of age
    • Berkowitz E.M., et al. Chromatin structure in neuronal and neuroglial cell nuclei as a function of age. J. Neurochem. 41 (1983) 516-523
    • (1983) J. Neurochem. , vol.41 , pp. 516-523
    • Berkowitz, E.M.1
  • 30
    • 0019841867 scopus 로고
    • Changes in chromatin structure associated with Alzheimer's disease
    • Lewis P.N., et al. Changes in chromatin structure associated with Alzheimer's disease. J. Neurochem. 37 (1981) 1193-1202
    • (1981) J. Neurochem. , vol.37 , pp. 1193-1202
    • Lewis, P.N.1
  • 31
    • 0025117535 scopus 로고
    • Chromatin structure and gene expression in Alzheimer's disease
    • Lukiw W.J., et al. Chromatin structure and gene expression in Alzheimer's disease. Brain Res. Mol. Brain Res. 7 (1990) 227-233
    • (1990) Brain Res. Mol. Brain Res. , vol.7 , pp. 227-233
    • Lukiw, W.J.1
  • 32
    • 0034630503 scopus 로고    scopus 로고
    • Nuclear topology of murine, cerebellar Purkinje neurons: changes as a function of development
    • Martou G., and De Boni U. Nuclear topology of murine, cerebellar Purkinje neurons: changes as a function of development. Exp. Cell Res. 256 (2000) 131-139
    • (2000) Exp. Cell Res. , vol.256 , pp. 131-139
    • Martou, G.1    De Boni, U.2
  • 33
    • 33747873573 scopus 로고    scopus 로고
    • Cell-type specific proximity of centromeric domains of one homologue each of chromosomes 2 and 11 in nuclei of cerebellar Purkinje neurons
    • Vadakkan K.I., et al. Cell-type specific proximity of centromeric domains of one homologue each of chromosomes 2 and 11 in nuclei of cerebellar Purkinje neurons. Chromosoma 115 (2006) 395-402
    • (2006) Chromosoma , vol.115 , pp. 395-402
    • Vadakkan, K.I.1
  • 34
    • 0024239767 scopus 로고
    • Movement of the X chromosome in epilepsy
    • Borden J., and Manuelidis L. Movement of the X chromosome in epilepsy. Science 242 (1988) 1687-1691
    • (1988) Science , vol.242 , pp. 1687-1691
    • Borden, J.1    Manuelidis, L.2
  • 35
    • 39449123232 scopus 로고    scopus 로고
    • Allele-specific nuclear positioning of the monoallelically expressed astrocyte marker GFAP
    • Takizawa T., et al. Allele-specific nuclear positioning of the monoallelically expressed astrocyte marker GFAP. Genes Dev. 22 (2008) 489-498
    • (2008) Genes Dev. , vol.22 , pp. 489-498
    • Takizawa, T.1
  • 36
    • 1842855742 scopus 로고    scopus 로고
    • Nuclear organization in differentiating oligodendrocytes
    • Nielsen J.A., et al. Nuclear organization in differentiating oligodendrocytes. J. Cell Sci. 115 (2002) 4071-4079
    • (2002) J. Cell Sci. , vol.115 , pp. 4071-4079
    • Nielsen, J.A.1
  • 37
    • 40749122641 scopus 로고    scopus 로고
    • Transcriptional repression mediated by repositioning of genes to the nuclear lamina
    • Reddy K.L., et al. Transcriptional repression mediated by repositioning of genes to the nuclear lamina. Nature 452 (2008) 243-247
    • (2008) Nature , vol.452 , pp. 243-247
    • Reddy, K.L.1
  • 38
    • 41949121084 scopus 로고    scopus 로고
    • Recruitment to the nuclear periphery can alter expression of genes in human cells
    • Finlan L.E., et al. Recruitment to the nuclear periphery can alter expression of genes in human cells. PLoS Genet. 4 (2008) e1000039
    • (2008) PLoS Genet. , vol.4
    • Finlan, L.E.1
  • 39
    • 38349043904 scopus 로고    scopus 로고
    • A genetic locus targeted to the nuclear periphery in living cells maintains its transcriptional competence
    • Kumaran R.I., and Spector D.L. A genetic locus targeted to the nuclear periphery in living cells maintains its transcriptional competence. J. Cell Biol. 180 (2008) 51-65
    • (2008) J. Cell Biol. , vol.180 , pp. 51-65
    • Kumaran, R.I.1    Spector, D.L.2
  • 40
    • 33645814398 scopus 로고    scopus 로고
    • CTCF mediates interchromosomal colocalization between Igf2/H19 and Wsb1/Nf1
    • Ling J.Q., et al. CTCF mediates interchromosomal colocalization between Igf2/H19 and Wsb1/Nf1. Science 312 (2006) 269-272
    • (2006) Science , vol.312 , pp. 269-272
    • Ling, J.Q.1
  • 41
    • 15544382113 scopus 로고    scopus 로고
    • Homologous pairing of 15q11-13 imprinted domains in brain is developmentally regulated but deficient in Rett and autism samples
    • Thatcher K.N., et al. Homologous pairing of 15q11-13 imprinted domains in brain is developmentally regulated but deficient in Rett and autism samples. Hum. Mol. Genet. 14 (2005) 785-797
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 785-797
    • Thatcher, K.N.1
  • 42
    • 24644518545 scopus 로고    scopus 로고
    • Reelin and glutamic acid decarboxylase67 promoter remodeling in an epigenetic methionine-induced mouse model of schizophrenia
    • Dong E., et al. Reelin and glutamic acid decarboxylase67 promoter remodeling in an epigenetic methionine-induced mouse model of schizophrenia. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 12578-12583
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 12578-12583
    • Dong, E.1
  • 43
    • 34248370579 scopus 로고    scopus 로고
    • Histone hyperacetylation induces demethylation of reelin and 67-kDa glutamic acid decarboxylase promoters
    • Dong E., et al. Histone hyperacetylation induces demethylation of reelin and 67-kDa glutamic acid decarboxylase promoters. Proc. Natl. Acad. Sci. U. S. A. 104 (2007) 4676-4681
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 4676-4681
    • Dong, E.1
  • 44
    • 3342989681 scopus 로고    scopus 로고
    • Epigenetic programming by maternal behavior
    • Weaver I.C., et al. Epigenetic programming by maternal behavior. Nat. Neurosci. 7 (2004) 847-854
    • (2004) Nat. Neurosci. , vol.7 , pp. 847-854
    • Weaver, I.C.1
  • 45
    • 33645357786 scopus 로고    scopus 로고
    • Sustained hippocampal chromatin regulation in a mouse model of depression and antidepressant action
    • Tsankova N.M., et al. Sustained hippocampal chromatin regulation in a mouse model of depression and antidepressant action. Nat. Neurosci. 9 (2006) 519-525
    • (2006) Nat. Neurosci. , vol.9 , pp. 519-525
    • Tsankova, N.M.1
  • 46
    • 35648934049 scopus 로고    scopus 로고
    • Histone deacetylase 5 epigenetically controls behavioral adaptations to chronic emotional stimuli
    • Renthal W., et al. Histone deacetylase 5 epigenetically controls behavioral adaptations to chronic emotional stimuli. Neuron 56 (2007) 517-529
    • (2007) Neuron , vol.56 , pp. 517-529
    • Renthal, W.1
  • 47
    • 0037127007 scopus 로고    scopus 로고
    • Alternative splicing and neuritic mRNA translocation under long-term neuronal hypersensitivity
    • Meshorer E., et al. Alternative splicing and neuritic mRNA translocation under long-term neuronal hypersensitivity. Science 295 (2002) 508-512
    • (2002) Science , vol.295 , pp. 508-512
    • Meshorer, E.1
  • 48
    • 33645988822 scopus 로고    scopus 로고
    • Virtues and woes of AChE alternative splicing in stress-related neuropathologies
    • Meshorer E., and Soreq H. Virtues and woes of AChE alternative splicing in stress-related neuropathologies. Trends Neurosci. 29 (2006) 216-224
    • (2006) Trends Neurosci. , vol.29 , pp. 216-224
    • Meshorer, E.1    Soreq, H.2
  • 49
    • 27544499653 scopus 로고    scopus 로고
    • SC35 promotes sustainable stress-induced alternative splicing of neuronal acetylcholinesterase mRNA
    • Meshorer E., et al. SC35 promotes sustainable stress-induced alternative splicing of neuronal acetylcholinesterase mRNA. Mol. Psychiatry 10 (2005) 985-997
    • (2005) Mol. Psychiatry , vol.10 , pp. 985-997
    • Meshorer, E.1
  • 50
    • 0034644473 scopus 로고    scopus 로고
    • Signaling to chromatin through histone modifications
    • Cheung P., et al. Signaling to chromatin through histone modifications. Cell 103 (2000) 263-271
    • (2000) Cell , vol.103 , pp. 263-271
    • Cheung, P.1
  • 51
    • 0036532026 scopus 로고    scopus 로고
    • Histone modifications in transcriptional regulation
    • Berger S.L. Histone modifications in transcriptional regulation. Curr. Opin. Genet. Dev. 12 (2002) 142-148
    • (2002) Curr. Opin. Genet. Dev. , vol.12 , pp. 142-148
    • Berger, S.L.1
  • 52
    • 0037382605 scopus 로고    scopus 로고
    • Functional consequences of histone modifications
    • Iizuka M., and Smith M.M. Functional consequences of histone modifications. Curr. Opin. Genet. Dev. 13 (2003) 154-160
    • (2003) Curr. Opin. Genet. Dev. , vol.13 , pp. 154-160
    • Iizuka, M.1    Smith, M.M.2
  • 53
    • 0033919494 scopus 로고    scopus 로고
    • Querkopf, a MYST family histone acetyltransferase, is required for normal cerebral cortex development
    • Thomas T., et al. Querkopf, a MYST family histone acetyltransferase, is required for normal cerebral cortex development. Development 127 (2000) 2537-2548
    • (2000) Development , vol.127 , pp. 2537-2548
    • Thomas, T.1
  • 54
    • 0037426839 scopus 로고    scopus 로고
    • Rhythmic histone acetylation underlies transcription in the mammalian circadian clock
    • Etchegaray J.P., et al. Rhythmic histone acetylation underlies transcription in the mammalian circadian clock. Nature 421 (2003) 177-182
    • (2003) Nature , vol.421 , pp. 177-182
    • Etchegaray, J.P.1
  • 55
    • 0035873614 scopus 로고    scopus 로고
    • Increased histone acetyltransferase and lysine acetyltransferase activity and biphasic activation of the ERK/RSK cascade in insular cortex during novel taste learning
    • Swank M.W., and Sweatt J.D. Increased histone acetyltransferase and lysine acetyltransferase activity and biphasic activation of the ERK/RSK cascade in insular cortex during novel taste learning. J. Neurosci. 21 (2001) 3383-3391
    • (2001) J. Neurosci. , vol.21 , pp. 3383-3391
    • Swank, M.W.1    Sweatt, J.D.2
  • 56
    • 34248523169 scopus 로고    scopus 로고
    • Recovery of learning and memory is associated with chromatin remodelling
    • Fischer A., et al. Recovery of learning and memory is associated with chromatin remodelling. Nature 447 (2007) 178-182
    • (2007) Nature , vol.447 , pp. 178-182
    • Fischer, A.1
  • 57
    • 0347624644 scopus 로고    scopus 로고
    • Critical loss of CBP/p300 histone acetylase activity by caspase-6 during neurodegeneration
    • Rouaux C., et al. Critical loss of CBP/p300 histone acetylase activity by caspase-6 during neurodegeneration. EMBO J. 22 (2003) 6537-6549
    • (2003) EMBO J. , vol.22 , pp. 6537-6549
    • Rouaux, C.1
  • 58
    • 33749583553 scopus 로고    scopus 로고
    • α-Synuclein acts in the nucleus to inhibit histone acetylation and promote neurotoxicity
    • Kontopoulos E., et al. α-Synuclein acts in the nucleus to inhibit histone acetylation and promote neurotoxicity. Hum. Mol. Genet. 15 (2006) 3012-3023
    • (2006) Hum. Mol. Genet. , vol.15 , pp. 3012-3023
    • Kontopoulos, E.1
  • 59
    • 13844275314 scopus 로고    scopus 로고
    • Transcriptional control of cognitive development
    • Hong E.J., et al. Transcriptional control of cognitive development. Curr. Opin. Neurobiol. 15 (2005) 21-28
    • (2005) Curr. Opin. Neurobiol. , vol.15 , pp. 21-28
    • Hong, E.J.1
  • 60
    • 0036897351 scopus 로고    scopus 로고
    • Histone deacetylase activity is necessary for oligodendrocyte lineage progression
    • Marin-Husstege M., et al. Histone deacetylase activity is necessary for oligodendrocyte lineage progression. J. Neurosci. 22 (2002) 10333-10345
    • (2002) J. Neurosci. , vol.22 , pp. 10333-10345
    • Marin-Husstege, M.1
  • 61
    • 0037707637 scopus 로고    scopus 로고
    • Upregulation of class II histone deacetylases mRNA during neural differentiation of cultured rat hippocampal progenitor cells
    • Ajamian F., et al. Upregulation of class II histone deacetylases mRNA during neural differentiation of cultured rat hippocampal progenitor cells. Neurosci. Lett. 346 (2003) 57-60
    • (2003) Neurosci. Lett. , vol.346 , pp. 57-60
    • Ajamian, F.1
  • 62
    • 9344252804 scopus 로고    scopus 로고
    • Histone deacetylase inhibition-mediated neuronal differentiation of multipotent adult neural progenitor cells
    • Hsieh J., et al. Histone deacetylase inhibition-mediated neuronal differentiation of multipotent adult neural progenitor cells. Proc. Natl. Acad. Sci. U. S. A. 101 (2004) 16659-16664
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 16659-16664
    • Hsieh, J.1
  • 63
    • 0037315344 scopus 로고    scopus 로고
    • Selective E2F-dependent gene transcription is controlled by histone deacetylase activity during neuronal apoptosis
    • Boutillier A.L., et al. Selective E2F-dependent gene transcription is controlled by histone deacetylase activity during neuronal apoptosis. J. Neurochem. 84 (2003) 814-828
    • (2003) J. Neurochem. , vol.84 , pp. 814-828
    • Boutillier, A.L.1
  • 64
    • 26844518082 scopus 로고    scopus 로고
    • Intracellular trafficking of histone deacetylase 4 regulates neuronal cell death
    • Bolger T.A., and Yao T.P. Intracellular trafficking of histone deacetylase 4 regulates neuronal cell death. J. Neurosci. 25 (2005) 9544-9553
    • (2005) J. Neurosci. , vol.25 , pp. 9544-9553
    • Bolger, T.A.1    Yao, T.P.2
  • 65
    • 0033598827 scopus 로고    scopus 로고
    • Neural restrictive silencer factor recruits mSin3 and histone deacetylase complex to repress neuron-specific target genes
    • Naruse Y., et al. Neural restrictive silencer factor recruits mSin3 and histone deacetylase complex to repress neuron-specific target genes. Proc. Natl. Acad. Sci. U. S. A. 96 (1999) 13691-13696
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 13691-13696
    • Naruse, Y.1
  • 66
    • 0033306577 scopus 로고    scopus 로고
    • Transcriptional repression by REST: recruitment of Sin3A and histone deacetylase to neuronal genes
    • Huang Y., et al. Transcriptional repression by REST: recruitment of Sin3A and histone deacetylase to neuronal genes. Nat. Neurosci. 2 (1999) 867-872
    • (1999) Nat. Neurosci. , vol.2 , pp. 867-872
    • Huang, Y.1
  • 67
    • 0037188526 scopus 로고    scopus 로고
    • A core-BRAF35 complex containing histone deacetylase mediates repression of neuronal-specific genes
    • Hakimi M.A., et al. A core-BRAF35 complex containing histone deacetylase mediates repression of neuronal-specific genes. Proc. Natl. Acad. Sci. U. S. A. 99 (2002) 7420-7425
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 7420-7425
    • Hakimi, M.A.1
  • 68
    • 20244368362 scopus 로고    scopus 로고
    • Disruption of the gene euchromatin histone methyl transferase1 (Eu-HMTase1) is associated with the 9q34 subtelomeric deletion syndrome
    • Kleefstra T., et al. Disruption of the gene euchromatin histone methyl transferase1 (Eu-HMTase1) is associated with the 9q34 subtelomeric deletion syndrome. J. Med. Genet. 42 (2005) 299-306
    • (2005) J. Med. Genet. , vol.42 , pp. 299-306
    • Kleefstra, T.1
  • 69
    • 2942631126 scopus 로고    scopus 로고
    • Localized domains of G9a-mediated histone methylation are required for silencing of neuronal genes
    • Roopra A., et al. Localized domains of G9a-mediated histone methylation are required for silencing of neuronal genes. Mol. Cell 14 (2004) 727-738
    • (2004) Mol. Cell , vol.14 , pp. 727-738
    • Roopra, A.1
  • 70
    • 33644823190 scopus 로고    scopus 로고
    • Recruitment of MLL by HMG-domain protein iBRAF promotes neural differentiation
    • Wynder C., et al. Recruitment of MLL by HMG-domain protein iBRAF promotes neural differentiation. Nat. Cell Biol. 7 (2005) 1113-1117
    • (2005) Nat. Cell Biol. , vol.7 , pp. 1113-1117
    • Wynder, C.1
  • 71
    • 0035909999 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors reduce polyglutamine toxicity
    • McCampbell A., et al. Histone deacetylase inhibitors reduce polyglutamine toxicity. Proc. Natl. Acad. Sci. U. S. A. 98 (2001) 15179-15184
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 15179-15184
    • McCampbell, A.1
  • 72
    • 0035047651 scopus 로고    scopus 로고
    • Therapeutic opportunities in polyglutamine disease
    • Hughes R.E., and Olson J.M. Therapeutic opportunities in polyglutamine disease. Nat. Med. 7 (2001) 419-423
    • (2001) Nat. Med. , vol.7 , pp. 419-423
    • Hughes, R.E.1    Olson, J.M.2
  • 73
    • 0034494318 scopus 로고    scopus 로고
    • Interaction of expanded polyglutamine stretches with nuclear transcription factors leads to aberrant transcriptional regulation in polyglutamine diseases
    • Shimohata T., et al. Interaction of expanded polyglutamine stretches with nuclear transcription factors leads to aberrant transcriptional regulation in polyglutamine diseases. Neuropathology 20 (2000) 326-333
    • (2000) Neuropathology , vol.20 , pp. 326-333
    • Shimohata, T.1
  • 74
    • 0033230850 scopus 로고    scopus 로고
    • Expanding our understanding of polyglutamine diseases through mouse models
    • Lin X., et al. Expanding our understanding of polyglutamine diseases through mouse models. Neuron 24 (1999) 499-502
    • (1999) Neuron , vol.24 , pp. 499-502
    • Lin, X.1
  • 75
    • 0142157600 scopus 로고    scopus 로고
    • Histone deacetylase inhibition by sodium butyrate chemotherapy ameliorates the neurodegenerative phenotype in Huntington's disease mice
    • Ferrante R.J., et al. Histone deacetylase inhibition by sodium butyrate chemotherapy ameliorates the neurodegenerative phenotype in Huntington's disease mice. J. Neurosci. 23 (2003) 9418-9427
    • (2003) J. Neurosci. , vol.23 , pp. 9418-9427
    • Ferrante, R.J.1
  • 76
    • 33748928786 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors as therapeutics for polyglutamine disorders
    • Butler R., and Bates G.P. Histone deacetylase inhibitors as therapeutics for polyglutamine disorders. Nat. Rev. Neurosci. 7 (2006) 784-796
    • (2006) Nat. Rev. Neurosci. , vol.7 , pp. 784-796
    • Butler, R.1    Bates, G.P.2
  • 77
    • 28444453738 scopus 로고    scopus 로고
    • Cytoprotective effect of novel histone deacetylase inhibitors against polyglutamine toxicity
    • Kariya S., et al. Cytoprotective effect of novel histone deacetylase inhibitors against polyglutamine toxicity. Neurosci. Lett. 392 (2006) 213-215
    • (2006) Neurosci. Lett. , vol.392 , pp. 213-215
    • Kariya, S.1
  • 78
    • 33749059726 scopus 로고    scopus 로고
    • The neurobiology of multiple sclerosis: genes, inflammation, and neurodegeneration
    • Hauser S.L., and Oksenberg J.R. The neurobiology of multiple sclerosis: genes, inflammation, and neurodegeneration. Neuron 52 (2006) 61-76
    • (2006) Neuron , vol.52 , pp. 61-76
    • Hauser, S.L.1    Oksenberg, J.R.2
  • 79
    • 20444446595 scopus 로고    scopus 로고
    • Transcriptional therapy with the histone deacetylase inhibitor trichostatin A ameliorates experimental autoimmune encephalomyelitis
    • Camelo S., et al. Transcriptional therapy with the histone deacetylase inhibitor trichostatin A ameliorates experimental autoimmune encephalomyelitis. J. Neuroimmunol. 164 (2005) 10-21
    • (2005) J. Neuroimmunol. , vol.164 , pp. 10-21
    • Camelo, S.1
  • 80
    • 3042651448 scopus 로고    scopus 로고
    • Valproic acid reduces brain damage induced by transient focal cerebral ischemia in rats: potential roles of histone deacetylase inhibition and heat shock protein induction
    • Ren M., et al. Valproic acid reduces brain damage induced by transient focal cerebral ischemia in rats: potential roles of histone deacetylase inhibition and heat shock protein induction. J. Neurochem. 89 (2004) 1358-1367
    • (2004) J. Neurochem. , vol.89 , pp. 1358-1367
    • Ren, M.1
  • 81
    • 33751120697 scopus 로고    scopus 로고
    • Pharmacological inhibition of histone deacetylases by suberoylanilide hydroxamic acid specifically alters gene expression and reduces ischemic injury in the mouse brain
    • Faraco G., et al. Pharmacological inhibition of histone deacetylases by suberoylanilide hydroxamic acid specifically alters gene expression and reduces ischemic injury in the mouse brain. Mol. Pharmacol. 70 (2006) 1876-1884
    • (2006) Mol. Pharmacol. , vol.70 , pp. 1876-1884
    • Faraco, G.1
  • 82
    • 34250161829 scopus 로고    scopus 로고
    • Antidepressant-like effects of the histone deacetylase inhibitor, sodium butyrate, in the mouse
    • Schroeder F.A., et al. Antidepressant-like effects of the histone deacetylase inhibitor, sodium butyrate, in the mouse. Biol. Psychiatry 62 (2007) 55-64
    • (2007) Biol. Psychiatry , vol.62 , pp. 55-64
    • Schroeder, F.A.1
  • 83
    • 0037093781 scopus 로고    scopus 로고
    • Stress activation of glutamate neurotransmission in the prefrontal cortex: implications for dopamine-associated psychiatric disorders
    • Moghaddam B. Stress activation of glutamate neurotransmission in the prefrontal cortex: implications for dopamine-associated psychiatric disorders. Biol. Psychiatry 51 (2002) 775-787
    • (2002) Biol. Psychiatry , vol.51 , pp. 775-787
    • Moghaddam, B.1
  • 84
    • 33745079980 scopus 로고    scopus 로고
    • In vitro and ex vivo evaluation of second-generation histone deacetylase inhibitors for the treatment of spinal muscular atrophy
    • Hahnen E., et al. In vitro and ex vivo evaluation of second-generation histone deacetylase inhibitors for the treatment of spinal muscular atrophy. J. Neurochem. 98 (2006) 193-202
    • (2006) J. Neurochem. , vol.98 , pp. 193-202
    • Hahnen, E.1
  • 85
    • 33745686137 scopus 로고    scopus 로고
    • The benzamide M344, a novel histone deacetylase inhibitor, significantly increases SMN2 RNA/protein levels in spinal muscular atrophy cells
    • Riessland M., et al. The benzamide M344, a novel histone deacetylase inhibitor, significantly increases SMN2 RNA/protein levels in spinal muscular atrophy cells. Hum. Genet. 120 (2006) 101-110
    • (2006) Hum. Genet. , vol.120 , pp. 101-110
    • Riessland, M.1
  • 86
    • 0036640628 scopus 로고    scopus 로고
    • On the epigenetic regulation of the human reelin promoter
    • Chen Y., et al. On the epigenetic regulation of the human reelin promoter. Nucleic Acids Res. 30 (2002) 2930-2939
    • (2002) Nucleic Acids Res. , vol.30 , pp. 2930-2939
    • Chen, Y.1
  • 87
    • 33747449599 scopus 로고    scopus 로고
    • Gene silencing through methylation: an epigenetic intervention on Alzheimer disease
    • Scarpa S., et al. Gene silencing through methylation: an epigenetic intervention on Alzheimer disease. J. Alzheimers Dis. 9 (2006) 407-414
    • (2006) J. Alzheimers Dis. , vol.9 , pp. 407-414
    • Scarpa, S.1
  • 88
    • 34347375106 scopus 로고    scopus 로고
    • Epigenetic drugs as pleiotropic agents in cancer treatment: biomolecular aspects and clinical applications
    • Sigalotti L., et al. Epigenetic drugs as pleiotropic agents in cancer treatment: biomolecular aspects and clinical applications. J. Cell. Physiol. 212 (2007) 330-344
    • (2007) J. Cell. Physiol. , vol.212 , pp. 330-344
    • Sigalotti, L.1
  • 89
    • 20844438031 scopus 로고    scopus 로고
    • Remodeling chromatin and stress resistance in the central nervous system: histone deacetylase inhibitors as novel and broadly effective neuroprotective agents
    • Langley B., et al. Remodeling chromatin and stress resistance in the central nervous system: histone deacetylase inhibitors as novel and broadly effective neuroprotective agents. Curr. Drug Targets CNS Neurol. Disord. 4 (2005) 41-50
    • (2005) Curr. Drug Targets CNS Neurol. Disord. , vol.4 , pp. 41-50
    • Langley, B.1
  • 90
    • 33644946604 scopus 로고    scopus 로고
    • HATs and HDACs in neurodegeneration: a tale of disconcerted acetylation homeostasis
    • Saha R.N., and Pahan K. HATs and HDACs in neurodegeneration: a tale of disconcerted acetylation homeostasis. Cell Death Differ. 13 (2006) 539-550
    • (2006) Cell Death Differ. , vol.13 , pp. 539-550
    • Saha, R.N.1    Pahan, K.2
  • 91
    • 33748450288 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: a novel therapeutic approach to Huntington's disease (complex mechanism of neuronal death)
    • Sadri-Vakili G., and Cha J.H. Histone deacetylase inhibitors: a novel therapeutic approach to Huntington's disease (complex mechanism of neuronal death). Curr. Alzheimer Res. 3 (2006) 403-408
    • (2006) Curr. Alzheimer Res. , vol.3 , pp. 403-408
    • Sadri-Vakili, G.1    Cha, J.H.2
  • 92
    • 0034912742 scopus 로고    scopus 로고
    • Histone acetyltransferases
    • Roth S.Y., et al. Histone acetyltransferases. Annu. Rev. Biochem. 70 (2001) 81-120
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 81-120
    • Roth, S.Y.1
  • 93
    • 0041302197 scopus 로고    scopus 로고
    • Histone deacetylases
    • Marks P.A., et al. Histone deacetylases. Curr. Opin. Pharmacol. 3 (2003) 344-351
    • (2003) Curr. Opin. Pharmacol. , vol.3 , pp. 344-351
    • Marks, P.A.1
  • 94
    • 3142674953 scopus 로고    scopus 로고
    • Structure and function of histone methyltransferases
    • Trievel R.C. Structure and function of histone methyltransferases. Crit. Rev. Eukaryot. Gene Expr. 14 (2004) 147-169
    • (2004) Crit. Rev. Eukaryot. Gene Expr. , vol.14 , pp. 147-169
    • Trievel, R.C.1
  • 95
    • 33747455678 scopus 로고    scopus 로고
    • JmjC-domain-containing proteins and histone demethylation
    • Klose R.J., et al. JmjC-domain-containing proteins and histone demethylation. Nat. Rev. Genet. 7 (2006) 715-727
    • (2006) Nat. Rev. Genet. , vol.7 , pp. 715-727
    • Klose, R.J.1
  • 96
    • 33747609801 scopus 로고    scopus 로고
    • Genome-wide patterns of histone modifications in yeast
    • Millar C.B., and Grunstein M. Genome-wide patterns of histone modifications in yeast. Nat. Rev. Mol. Cell Biol. 7 (2006) 657-666
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 657-666
    • Millar, C.B.1    Grunstein, M.2
  • 97
    • 0027986525 scopus 로고
    • Histone shuttling by poly ADP-ribosylation
    • Althaus F.R., et al. Histone shuttling by poly ADP-ribosylation. Mol. Cell. Biochem. 138 (1994) 53-59
    • (1994) Mol. Cell. Biochem. , vol.138 , pp. 53-59
    • Althaus, F.R.1
  • 98
    • 0842304521 scopus 로고    scopus 로고
    • Analysis of histone phosphorylation: coupling intracellular signaling to chromatin remodeling
    • Loury R., and Sassone-Corsi P. Analysis of histone phosphorylation: coupling intracellular signaling to chromatin remodeling. Methods Enzymol. 377 (2004) 197-212
    • (2004) Methods Enzymol. , vol.377 , pp. 197-212
    • Loury, R.1    Sassone-Corsi, P.2
  • 99
    • 0344442779 scopus 로고    scopus 로고
    • Transcriptional regulation by histone ubiquitination and deubiquitination
    • Zhang Y. Transcriptional regulation by histone ubiquitination and deubiquitination. Genes Dev. 17 (2003) 2733-2740
    • (2003) Genes Dev. , vol.17 , pp. 2733-2740
    • Zhang, Y.1
  • 100
    • 0344824404 scopus 로고    scopus 로고
    • Histone sumoylation is associated with transcriptional repression
    • Shiio Y., and Eisenman R.N. Histone sumoylation is associated with transcriptional repression. Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 13225-13230
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 13225-13230
    • Shiio, Y.1    Eisenman, R.N.2
  • 101
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • Jenuwein T., and Allis C.D. Translating the histone code. Science 293 (2001) 1074-1080
    • (2001) Science , vol.293 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 102
    • 0037059081 scopus 로고    scopus 로고
    • Does heterochromatin protein 1 always follow code?
    • Li Y., et al. Does heterochromatin protein 1 always follow code?. Proc. Natl. Acad. Sci. U. S. A. 99 Suppl 4 (2002) 16462-16469
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , Issue.SUPPL. 4 , pp. 16462-16469
    • Li, Y.1
  • 103
    • 0036850325 scopus 로고    scopus 로고
    • Cellular memory and the histone code
    • Turner B.M. Cellular memory and the histone code. Cell 111 (2002) 285-291
    • (2002) Cell , vol.111 , pp. 285-291
    • Turner, B.M.1
  • 104
    • 17244368913 scopus 로고    scopus 로고
    • Genomic characterization reveals a simple histone H4 acetylation code
    • Dion M.F., et al. Genomic characterization reveals a simple histone H4 acetylation code. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 5501-5506
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 5501-5506
    • Dion, M.F.1
  • 105
    • 33845451555 scopus 로고    scopus 로고
    • A profile of histone lysine methylation across transcribed mammalian chromatin
    • Vakoc C.R., et al. A profile of histone lysine methylation across transcribed mammalian chromatin. Mol. Cell. Biol. 26 (2006) 9185-9195
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 9185-9195
    • Vakoc, C.R.1
  • 106
    • 23044457554 scopus 로고    scopus 로고
    • Role of de novo DNA methyltransferases in initiation of genomic imprinting and X-chromosome inactivation
    • Kaneda M., et al. Role of de novo DNA methyltransferases in initiation of genomic imprinting and X-chromosome inactivation. Cold Spring Harb. Symp. Quant. Biol. 69 (2004) 125-129
    • (2004) Cold Spring Harb. Symp. Quant. Biol. , vol.69 , pp. 125-129
    • Kaneda, M.1
  • 107
    • 33846933274 scopus 로고    scopus 로고
    • Gadd45a promotes epigenetic gene activation by repair-mediated DNA demethylation
    • Barreto G., et al. Gadd45a promotes epigenetic gene activation by repair-mediated DNA demethylation. Nature 445 (2007) 671-675
    • (2007) Nature , vol.445 , pp. 671-675
    • Barreto, G.1


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