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Volumn 19, Issue 2, 2007, Pages 230-237

Signaling to the circadian clock: plasticity by chromatin remodeling

Author keywords

[No Author keywords available]

Indexed keywords

HISTONE; HISTONE ACETYLTRANSFERASE; TRANSCRIPTION FACTOR CLOCK;

EID: 33847732265     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ceb.2007.02.016     Document Type: Review
Times cited : (76)

References (78)
  • 1
    • 0037381213 scopus 로고    scopus 로고
    • Structure and dynamic behavior of nucleosomes
    • Luger K. Structure and dynamic behavior of nucleosomes. Curr Opin Genet Dev 13 (2003) 127-135
    • (2003) Curr Opin Genet Dev , vol.13 , pp. 127-135
    • Luger, K.1
  • 2
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • Strahl B.D., and Allis C.D. The language of covalent histone modifications. Nature 403 (2000) 41-45
    • (2000) Nature , vol.403 , pp. 41-45
    • Strahl, B.D.1    Allis, C.D.2
  • 3
    • 85015069067 scopus 로고    scopus 로고
    • Controlling the double helix
    • Felsenfeld G., and Groudine M. Controlling the double helix. Nature 421 (2003) 448-453
    • (2003) Nature , vol.421 , pp. 448-453
    • Felsenfeld, G.1    Groudine, M.2
  • 4
    • 0034026193 scopus 로고    scopus 로고
    • Promoter targeting and chromatin remodeling by the SWI/SNF complex
    • Peterson C.L., and Workman J.L. Promoter targeting and chromatin remodeling by the SWI/SNF complex. Curr Opin Genet Dev 10 (2000) 187-192
    • (2000) Curr Opin Genet Dev , vol.10 , pp. 187-192
    • Peterson, C.L.1    Workman, J.L.2
  • 5
    • 0034644473 scopus 로고    scopus 로고
    • Signaling to chromatin through histone modifications
    • Cheung P., Allis C.D., and Sassone-Corsi P. Signaling to chromatin through histone modifications. Cell 103 (2000) 263-271
    • (2000) Cell , vol.103 , pp. 263-271
    • Cheung, P.1    Allis, C.D.2    Sassone-Corsi, P.3
  • 6
    • 0030798245 scopus 로고    scopus 로고
    • Histone acetylation in chromatin structure and transcription
    • Grunstein M. Histone acetylation in chromatin structure and transcription. Nature 389 (1997) 349-352
    • (1997) Nature , vol.389 , pp. 349-352
    • Grunstein, M.1
  • 7
    • 1642326716 scopus 로고    scopus 로고
    • Phosphorylation of histone H3: a balancing act between chromosome condensation and transcriptional activation
    • Nowak S.J., and Corces V.G. Phosphorylation of histone H3: a balancing act between chromosome condensation and transcriptional activation. Trends Genet 20 (2004) 214-220
    • (2004) Trends Genet , vol.20 , pp. 214-220
    • Nowak, S.J.1    Corces, V.G.2
  • 8
    • 0035883954 scopus 로고    scopus 로고
    • Transcription regulation by histone methylation: interplay between different covalent modifications of the core histone tails
    • Zhang Y., and Reinberg D. Transcription regulation by histone methylation: interplay between different covalent modifications of the core histone tails. Genes Dev 15 (2001) 2343-2360
    • (2001) Genes Dev , vol.15 , pp. 2343-2360
    • Zhang, Y.1    Reinberg, D.2
  • 9
    • 0035325163 scopus 로고    scopus 로고
    • Histone acetylation and chromatin remodeling
    • Gregory P.D., Wagner K., and Horz W. Histone acetylation and chromatin remodeling. Exp Cell Res 265 (2001) 195-202
    • (2001) Exp Cell Res , vol.265 , pp. 195-202
    • Gregory, P.D.1    Wagner, K.2    Horz, W.3
  • 11
    • 0025872683 scopus 로고
    • Rapid histone H3 phosphorylation in response to growth factors, phorbol esters, okadaic acid, and protein synthesis inhibitors
    • Mahadevan L.C., Willis A.C., and Barratt M.J. Rapid histone H3 phosphorylation in response to growth factors, phorbol esters, okadaic acid, and protein synthesis inhibitors. Cell 65 (1991) 775-783
    • (1991) Cell , vol.65 , pp. 775-783
    • Mahadevan, L.C.1    Willis, A.C.2    Barratt, M.J.3
  • 12
    • 0037188911 scopus 로고    scopus 로고
    • Histone methylation: dynamic or static?
    • Bannister A.J., Schneider R., and Kouzarides T. Histone methylation: dynamic or static?. Cell 109 (2002) 801-806
    • (2002) Cell , vol.109 , pp. 801-806
    • Bannister, A.J.1    Schneider, R.2    Kouzarides, T.3
  • 13
    • 0021921061 scopus 로고
    • Sequential ADP-ribosylation pattern of nucleosomal histones. ADP-ribosylation of nucleosomal histones
    • Huletsky A., Niedergang C., Frechette A., Aubin R., Gaudreau A., and Poirier G.G. Sequential ADP-ribosylation pattern of nucleosomal histones. ADP-ribosylation of nucleosomal histones. Eur J Biochem 146 (1985) 277-285
    • (1985) Eur J Biochem , vol.146 , pp. 277-285
    • Huletsky, A.1    Niedergang, C.2    Frechette, A.3    Aubin, R.4    Gaudreau, A.5    Poirier, G.G.6
  • 14
    • 0344392751 scopus 로고    scopus 로고
    • Histone modifications: Now summoning sumoylation
    • Nathan D., Sterner D.E., and Berger S.L. Histone modifications: Now summoning sumoylation. Proc Natl Acad Sci USA 100 (2003) 13118-13120
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 13118-13120
    • Nathan, D.1    Sterner, D.E.2    Berger, S.L.3
  • 15
    • 0025341218 scopus 로고
    • Level of ubiquitinated histone H2B in chromatin is coupled to ongoing transcription
    • Davie J.R., and Murphy L.C. Level of ubiquitinated histone H2B in chromatin is coupled to ongoing transcription. Biochemistry 29 (1990) 4752-4757
    • (1990) Biochemistry , vol.29 , pp. 4752-4757
    • Davie, J.R.1    Murphy, L.C.2
  • 16
    • 0037019333 scopus 로고    scopus 로고
    • Ubiquitination of histone H2B regulates H3 methylation and gene silencing in yeast
    • Sun Z.W., and Allis C.D. Ubiquitination of histone H2B regulates H3 methylation and gene silencing in yeast. Nature 418 (2002) 104-108
    • (2002) Nature , vol.418 , pp. 104-108
    • Sun, Z.W.1    Allis, C.D.2
  • 19
    • 0033695926 scopus 로고    scopus 로고
    • Light induces chromatin modification in cells of the mammalian circadian clock
    • Crosio C., Cermakian N., Allis C.D., and Sassone-Corsi P. Light induces chromatin modification in cells of the mammalian circadian clock. Nat Neurosci 3 (2000) 1241-1247
    • (2000) Nat Neurosci , vol.3 , pp. 1241-1247
    • Crosio, C.1    Cermakian, N.2    Allis, C.D.3    Sassone-Corsi, P.4
  • 21
    • 0348143169 scopus 로고    scopus 로고
    • Chromatin remodeling and neuronal response: multiple signaling pathways induce specific histone H3 modifications and early gene expression in hippocampal neurons
    • Crosio C., Heitz E., Allis C.D., Borrelli E., and Sassone-Corsi P. Chromatin remodeling and neuronal response: multiple signaling pathways induce specific histone H3 modifications and early gene expression in hippocampal neurons. J Cell Sci 116 (2003) 4905-4914
    • (2003) J Cell Sci , vol.116 , pp. 4905-4914
    • Crosio, C.1    Heitz, E.2    Allis, C.D.3    Borrelli, E.4    Sassone-Corsi, P.5
  • 22
    • 0035839135 scopus 로고    scopus 로고
    • Snf1-a histone kinase that works in concert with the histone acetyltransferase Gcn5 to regulate transcription
    • Lo W.S., Duggan L., Emre N.C., Belotserkovskya R., Lane W.S., Shiekhattar R., and Berger S.L. Snf1-a histone kinase that works in concert with the histone acetyltransferase Gcn5 to regulate transcription. Science 293 (2001) 1142-1146
    • (2001) Science , vol.293 , pp. 1142-1146
    • Lo, W.S.1    Duggan, L.2    Emre, N.C.3    Belotserkovskya, R.4    Lane, W.S.5    Shiekhattar, R.6    Berger, S.L.7
  • 23
    • 0034679625 scopus 로고    scopus 로고
    • Phosphoacetylation of histone H3 on c-fos- and c-jun-associated nucleosomes upon gene activation
    • Clayton A.L., Rose S., Barratt M.J., and Mahadevan L.C. Phosphoacetylation of histone H3 on c-fos- and c-jun-associated nucleosomes upon gene activation. EMBO J 19 (2000) 3714-3726
    • (2000) EMBO J , vol.19 , pp. 3714-3726
    • Clayton, A.L.1    Rose, S.2    Barratt, M.J.3    Mahadevan, L.C.4
  • 24
    • 0033636595 scopus 로고    scopus 로고
    • Synergistic coupling of histone H3 phosphorylation and acetylation in response to epidermal growth factor stimulation
    • Cheung P., Tanner K.G., Cheung W.L., Sassone-Corsi P., Denu J.M., and Allis C.D. Synergistic coupling of histone H3 phosphorylation and acetylation in response to epidermal growth factor stimulation. Mol Cell 5 (2000) 905-915
    • (2000) Mol Cell , vol.5 , pp. 905-915
    • Cheung, P.1    Tanner, K.G.2    Cheung, W.L.3    Sassone-Corsi, P.4    Denu, J.M.5    Allis, C.D.6
  • 25
    • 0033638105 scopus 로고    scopus 로고
    • Phosphorylation of serine 10 in histone H3 is functionally linked in vitro and in vivo to Gcn5-mediated acetylation at lysine 14
    • Lo W.S., Trievel R.C., Rojas J.R., Duggan L., Hsu J.Y., Allis C.D., Marmorstein R., and Berger S.L. Phosphorylation of serine 10 in histone H3 is functionally linked in vitro and in vivo to Gcn5-mediated acetylation at lysine 14. Mol Cell 5 (2000) 917-926
    • (2000) Mol Cell , vol.5 , pp. 917-926
    • Lo, W.S.1    Trievel, R.C.2    Rojas, J.R.3    Duggan, L.4    Hsu, J.Y.5    Allis, C.D.6    Marmorstein, R.7    Berger, S.L.8
  • 26
    • 0034813107 scopus 로고    scopus 로고
    • Mitogen-regulated RSK2-CBP interaction controls their kinase and acetylase activities
    • Merienne K., Pannetier S., Harel-Bellan A., and Sassone-Corsi P. Mitogen-regulated RSK2-CBP interaction controls their kinase and acetylase activities. Mol Cell Biol 21 (2001) 7089-7096
    • (2001) Mol Cell Biol , vol.21 , pp. 7089-7096
    • Merienne, K.1    Pannetier, S.2    Harel-Bellan, A.3    Sassone-Corsi, P.4
  • 27
    • 0141929385 scopus 로고    scopus 로고
    • Binary switches and modification cassettes in histone biology and beyond
    • Fischle W., Wang Y., and Allis C.D. Binary switches and modification cassettes in histone biology and beyond. Nature 425 (2003) 475-479
    • (2003) Nature , vol.425 , pp. 475-479
    • Fischle, W.1    Wang, Y.2    Allis, C.D.3
  • 28
    • 0032030770 scopus 로고    scopus 로고
    • Histone acetylation and transcriptional regulatory mechanisms
    • Struhl K. Histone acetylation and transcriptional regulatory mechanisms. Genes Dev 12 (1998) 599-606
    • (1998) Genes Dev , vol.12 , pp. 599-606
    • Struhl, K.1
  • 29
    • 0030961614 scopus 로고    scopus 로고
    • Histone acetyltransferases in control
    • Wade P.A., and Wolffe A.P. Histone acetyltransferases in control. Curr Biol 7 (1997) R82-R84
    • (1997) Curr Biol , vol.7
    • Wade, P.A.1    Wolffe, A.P.2
  • 30
    • 0031707751 scopus 로고    scopus 로고
    • Alteration of nucleosome structure as a mechanism of transcriptional regulation
    • Workman J.L., and Kingston R.E. Alteration of nucleosome structure as a mechanism of transcriptional regulation. Annu Rev Biochem 67 (1998) 545-579
    • (1998) Annu Rev Biochem , vol.67 , pp. 545-579
    • Workman, J.L.1    Kingston, R.E.2
  • 31
    • 0033000990 scopus 로고    scopus 로고
    • Histone acetylases and deacetylases in cell proliferation
    • Kouzarides T. Histone acetylases and deacetylases in cell proliferation. Curr Opin Genet Dev 9 (1999) 40-48
    • (1999) Curr Opin Genet Dev , vol.9 , pp. 40-48
    • Kouzarides, T.1
  • 32
    • 0034051227 scopus 로고    scopus 로고
    • Acetylation of histones and transcription-related factors
    • Sterner D.E., and Berger S.L. Acetylation of histones and transcription-related factors. Microbiol Mol Biol Rev 64 (2000) 435-459
    • (2000) Microbiol Mol Biol Rev , vol.64 , pp. 435-459
    • Sterner, D.E.1    Berger, S.L.2
  • 33
    • 0029984469 scopus 로고    scopus 로고
    • Tetrahymena histone acetyltransferase A: a homolog to yeast Gcn5p linking histone acetylation to gene activation
    • Brownell J.E., Zhou J., Ranalli T., Kobayashi R., Edmondson D.G., Roth S.Y., and Allis C.D. Tetrahymena histone acetyltransferase A: a homolog to yeast Gcn5p linking histone acetylation to gene activation. Cell 84 (1996) 843-851
    • (1996) Cell , vol.84 , pp. 843-851
    • Brownell, J.E.1    Zhou, J.2    Ranalli, T.3    Kobayashi, R.4    Edmondson, D.G.5    Roth, S.Y.6    Allis, C.D.7
  • 34
    • 0029665857 scopus 로고    scopus 로고
    • A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A
    • Yang X.J., Ogryzko V.V., Nishikawa J., Howard B.H., and Nakatani Y. A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A. Nature 382 (1996) 319-324
    • (1996) Nature , vol.382 , pp. 319-324
    • Yang, X.J.1    Ogryzko, V.V.2    Nishikawa, J.3    Howard, B.H.4    Nakatani, Y.5
  • 35
    • 0030480969 scopus 로고    scopus 로고
    • The CBP co-activator is a histone acetyltransferase
    • Bannister A.J., and Kouzarides T. The CBP co-activator is a histone acetyltransferase. Nature 384 (1996) 641-643
    • (1996) Nature , vol.384 , pp. 641-643
    • Bannister, A.J.1    Kouzarides, T.2
  • 36
    • 0030606239 scopus 로고    scopus 로고
    • The transcriptional coactivators p300 and CBP are histone acetyltransferases
    • Ogryzko V.V., Schiltz R.L., Russanova V., Howard B.H., and Nakatani Y. The transcriptional coactivators p300 and CBP are histone acetyltransferases. Cell 87 (1996) 953-959
    • (1996) Cell , vol.87 , pp. 953-959
    • Ogryzko, V.V.1    Schiltz, R.L.2    Russanova, V.3    Howard, B.H.4    Nakatani, Y.5
  • 38
    • 0030740253 scopus 로고    scopus 로고
    • Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with P/CAF and CBP/p300
    • Chen H., Lin R.J., Schiltz R.L., Chakravarti D., Nash A., Nagy L., Privalsky M.L., Nakatani Y., and Evans R.M. Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with P/CAF and CBP/p300. Cell 90 (1997) 569-580
    • (1997) Cell , vol.90 , pp. 569-580
    • Chen, H.1    Lin, R.J.2    Schiltz, R.L.3    Chakravarti, D.4    Nash, A.5    Nagy, L.6    Privalsky, M.L.7    Nakatani, Y.8    Evans, R.M.9
  • 40
    • 0034636554 scopus 로고    scopus 로고
    • ATF-2 has intrinsic histone acetyltransferase activity which is modulated by phosphorylation
    • Kawasaki H., Schiltz L., Chiu R., Itakura K., Taira K., Nakatani Y., and Yokoyama K.K. ATF-2 has intrinsic histone acetyltransferase activity which is modulated by phosphorylation. Nature 405 (2000) 195-200
    • (2000) Nature , vol.405 , pp. 195-200
    • Kawasaki, H.1    Schiltz, L.2    Chiu, R.3    Itakura, K.4    Taira, K.5    Nakatani, Y.6    Yokoyama, K.K.7
  • 42
    • 0030712311 scopus 로고    scopus 로고
    • Novel substrate specificity of the histone acetyltransferase activity of HIV-1-Tat interactive protein Tip60
    • Yamamoto T., and Horikoshi M. Novel substrate specificity of the histone acetyltransferase activity of HIV-1-Tat interactive protein Tip60. J Biol Chem 272 (1997) 30595-30598
    • (1997) J Biol Chem , vol.272 , pp. 30595-30598
    • Yamamoto, T.1    Horikoshi, M.2
  • 43
    • 0033593306 scopus 로고    scopus 로고
    • Molecular bases for circadian clocks
    • Dunlap J.C. Molecular bases for circadian clocks. Cell 96 (1999) 271-290
    • (1999) Cell , vol.96 , pp. 271-290
    • Dunlap, J.C.1
  • 44
    • 0034042294 scopus 로고    scopus 로고
    • Molecular genetics of circadian rhythms in mammals
    • King D.P., and Takahashi J.S. Molecular genetics of circadian rhythms in mammals. Annu Rev Neurosci 23 (2000) 713-742
    • (2000) Annu Rev Neurosci , vol.23 , pp. 713-742
    • King, D.P.1    Takahashi, J.S.2
  • 46
    • 0035458732 scopus 로고    scopus 로고
    • Time zones: a comparative genetics of circadian clocks
    • Young M.W., and Kay S.A. Time zones: a comparative genetics of circadian clocks. Nat Rev Genet 2 (2001) 702-715
    • (2001) Nat Rev Genet , vol.2 , pp. 702-715
    • Young, M.W.1    Kay, S.A.2
  • 47
    • 0037194790 scopus 로고    scopus 로고
    • Coordination of circadian timing in mammals
    • Reppert S.M., and Weaver D.R. Coordination of circadian timing in mammals. Nature 418 (2002) 935-941
    • (2002) Nature , vol.418 , pp. 935-941
    • Reppert, S.M.1    Weaver, D.R.2
  • 48
    • 0042490526 scopus 로고    scopus 로고
    • A clockwork web: circadian timing in brain and periphery, in health and disease
    • Hastings M.H., Reddy A.B., and Maywood E.S. A clockwork web: circadian timing in brain and periphery, in health and disease. Nat Rev Neurosci 4 (2003) 649-661
    • (2003) Nat Rev Neurosci , vol.4 , pp. 649-661
    • Hastings, M.H.1    Reddy, A.B.2    Maywood, E.S.3
  • 49
    • 0037711399 scopus 로고    scopus 로고
    • The circadian clock: pacemaker and tumour suppressor
    • Fu L., and Lee C.C. The circadian clock: pacemaker and tumour suppressor. Nat Rev Cancer 3 (2003) 350-361
    • (2003) Nat Rev Cancer , vol.3 , pp. 350-361
    • Fu, L.1    Lee, C.C.2
  • 51
    • 0037006807 scopus 로고    scopus 로고
    • Circadian programs of transcriptional activation, signaling, and protein turnover revealed by microarray analysis of mammalian cells
    • Duffield G.E., Best J.D., Meurers B.H., Bittner A., Loros J.J., and Dunlap J.C. Circadian programs of transcriptional activation, signaling, and protein turnover revealed by microarray analysis of mammalian cells. Curr Biol 12 (2002) 551-557
    • (2002) Curr Biol , vol.12 , pp. 551-557
    • Duffield, G.E.1    Best, J.D.2    Meurers, B.H.3    Bittner, A.4    Loros, J.J.5    Dunlap, J.C.6
  • 53
    • 0035969473 scopus 로고    scopus 로고
    • Peripheral clocks and their role in circadian timing: insights from insects
    • Giebultowicz J.M. Peripheral clocks and their role in circadian timing: insights from insects. Philos Trans R Soc Lond B Biol Sci 356 (2001) 1791-1799
    • (2001) Philos Trans R Soc Lond B Biol Sci , vol.356 , pp. 1791-1799
    • Giebultowicz, J.M.1
  • 54
    • 0035910387 scopus 로고    scopus 로고
    • Entrainment of the circadian clock in the liver by feeding
    • Stokkan K.A., Yamazaki S., Tei H., Sakaki Y., and Menaker M. Entrainment of the circadian clock in the liver by feeding. Science 291 (2001) 490-493
    • (2001) Science , vol.291 , pp. 490-493
    • Stokkan, K.A.1    Yamazaki, S.2    Tei, H.3    Sakaki, Y.4    Menaker, M.5
  • 55
    • 0034594904 scopus 로고    scopus 로고
    • Light acts directly on organs and cells in culture to set the vertebrate circadian clock
    • Whitmore D., Foulkes N.S., and Sassone-Corsi P. Light acts directly on organs and cells in culture to set the vertebrate circadian clock. Nature 404 (2000) 87-91
    • (2000) Nature , vol.404 , pp. 87-91
    • Whitmore, D.1    Foulkes, N.S.2    Sassone-Corsi, P.3
  • 56
    • 0037184977 scopus 로고    scopus 로고
    • A web of circadian pacemakers
    • Schibler U., and Sassone-Corsi P. A web of circadian pacemakers. Cell 111 (2002) 919-922
    • (2002) Cell , vol.111 , pp. 919-922
    • Schibler, U.1    Sassone-Corsi, P.2
  • 57
    • 0035930732 scopus 로고    scopus 로고
    • Regulation of daily locomotor activity and sleep by hypothalamic EGF receptor signaling
    • Kramer A., Yang F.C., Snodgrass P., Li X., Scammell T.E., Davis F.C., and Weitz C.J. Regulation of daily locomotor activity and sleep by hypothalamic EGF receptor signaling. Science 294 (2001) 2511-2515
    • (2001) Science , vol.294 , pp. 2511-2515
    • Kramer, A.1    Yang, F.C.2    Snodgrass, P.3    Li, X.4    Scammell, T.E.5    Davis, F.C.6    Weitz, C.J.7
  • 58
    • 0035919479 scopus 로고    scopus 로고
    • Regulation of clock and NPAS2 DNA binding by the redox state of NAD cofactors
    • Rutter J., Reick M., Wu L.C., and McKnight S.L. Regulation of clock and NPAS2 DNA binding by the redox state of NAD cofactors. Science 293 (2001) 510-514
    • (2001) Science , vol.293 , pp. 510-514
    • Rutter, J.1    Reick, M.2    Wu, L.C.3    McKnight, S.L.4
  • 59
    • 33845665236 scopus 로고    scopus 로고
    • A sense of time: how molecular clocks organize metabolism
    • Kohsaka A., and Bass J. A sense of time: how molecular clocks organize metabolism. Trends Endocrinol Metab 18 (2007) 4-11
    • (2007) Trends Endocrinol Metab , vol.18 , pp. 4-11
    • Kohsaka, A.1    Bass, J.2
  • 60
    • 33750938296 scopus 로고    scopus 로고
    • Circadian rhythms: perturbing a food-entrained clock
    • Mistlberger R.E. Circadian rhythms: perturbing a food-entrained clock. Curr Biol 16 (2006) R968-R969
    • (2006) Curr Biol , vol.16
    • Mistlberger, R.E.1
  • 63
    • 0037426839 scopus 로고    scopus 로고
    • Rhythmic histone acetylation underlies transcription in the mammalian circadian clock
    • Etchegaray J.P., Lee C., Wade P.A., and Reppert S.M. 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    Lee, C.2    Wade, P.A.3    Reppert, S.M.4
  • 64
    • 3042709817 scopus 로고    scopus 로고
    • Circadian and light-induced transcription of clock gene Per1 depends on histone acetylation and deacetylation
    • Naruse Y., Oh-hashi K., Iijima N., Naruse M., Yoshioka H., and Tanaka M. Circadian and light-induced transcription of clock gene Per1 depends on histone acetylation and deacetylation. Mol Cell Biol 24 (2004) 6278-6287
    • (2004) Mol Cell Biol , vol.24 , pp. 6278-6287
    • Naruse, Y.1    Oh-hashi, K.2    Iijima, N.3    Naruse, M.4    Yoshioka, H.5    Tanaka, M.6
  • 65
    • 33644617485 scopus 로고    scopus 로고
    • Rhythmic CLOCK-BMAL1 binding to multiple E-box motifs drives circadian Dbp transcription and chromatin transitions
    • Ripperger J.A., and Schibler U. Rhythmic CLOCK-BMAL1 binding to multiple E-box motifs drives circadian Dbp transcription and chromatin transitions. Nat Genet 38 (2006) 369-374
    • (2006) Nat Genet , vol.38 , pp. 369-374
    • Ripperger, J.A.1    Schibler, U.2
  • 66
    • 17044451254 scopus 로고    scopus 로고
    • A mutant Drosophila homolog of mammalian Clock disrupts circadian rhythms and transcription of period and timeless
    • Allada R., White N.E., So W.V., Hall J.C., and Rosbash M. A mutant Drosophila homolog of mammalian Clock disrupts circadian rhythms and transcription of period and timeless. Cell 93 (1998) 791-804
    • (1998) Cell , vol.93 , pp. 791-804
    • Allada, R.1    White, N.E.2    So, W.V.3    Hall, J.C.4    Rosbash, M.5
  • 69
    • 0033534628 scopus 로고    scopus 로고
    • A molecular mechanism regulating rhythmic output from the suprachiasmatic circadian clock
    • Jin X., Shearman L.P., Weaver D.R., Zylka M.J., de Vries G.J., and Reppert S.M. A molecular mechanism regulating rhythmic output from the suprachiasmatic circadian clock. Cell 96 (1999) 57-68
    • (1999) Cell , vol.96 , pp. 57-68
    • Jin, X.1    Shearman, L.P.2    Weaver, D.R.3    Zylka, M.J.4    de Vries, G.J.5    Reppert, S.M.6
  • 71
    • 33646145721 scopus 로고    scopus 로고
    • Circadian regulator CLOCK is a histone acetyltransferase
    • This study demonstrates a direct link between circadian clock control and histone modifications. The central regulator CLOCK is shown to possess intrinsic histone acetyltransferase activity. This finding is of central importance as it establishes a conceptual connection between circadian regulation, chromatin remodeling and cellular metabolism.
    • Doi M., Hirayama J., and Sassone-Corsi P. Circadian regulator CLOCK is a histone acetyltransferase. Cell 125 (2006) 497-508. This study demonstrates a direct link between circadian clock control and histone modifications. The central regulator CLOCK is shown to possess intrinsic histone acetyltransferase activity. This finding is of central importance as it establishes a conceptual connection between circadian regulation, chromatin remodeling and cellular metabolism.
    • (2006) Cell , vol.125 , pp. 497-508
    • Doi, M.1    Hirayama, J.2    Sassone-Corsi, P.3
  • 72
    • 24344450660 scopus 로고    scopus 로고
    • Structural and functional features of transcription factors controlling the circadian clock
    • Hirayama J., and Sassone-Corsi P. Structural and functional features of transcription factors controlling the circadian clock. Curr Opin Genet Dev 15 (2005) 548-556
    • (2005) Curr Opin Genet Dev , vol.15 , pp. 548-556
    • Hirayama, J.1    Sassone-Corsi, P.2
  • 73
    • 0033635283 scopus 로고    scopus 로고
    • Crystal structure of yeast Esa1 suggests a unified mechanism for catalysis and substrate binding by histone acetyltransferases
    • Yan Y., Barlev N.A., Haley R.H., Berger S.L., and Marmorstein R. Crystal structure of yeast Esa1 suggests a unified mechanism for catalysis and substrate binding by histone acetyltransferases. Mol Cell 6 (2000) 1195-1205
    • (2000) Mol Cell , vol.6 , pp. 1195-1205
    • Yan, Y.1    Barlev, N.A.2    Haley, R.H.3    Berger, S.L.4    Marmorstein, R.5
  • 75
    • 0037067652 scopus 로고    scopus 로고
    • Phenotypic rescue of a peripheral clock genetic defect via SCN hierarchical dominance
    • Pando M.P., Morse D., Cermakian N., and Sassone-Corsi P. Phenotypic rescue of a peripheral clock genetic defect via SCN hierarchical dominance. Cell 110 (2002) 107-117
    • (2002) Cell , vol.110 , pp. 107-117
    • Pando, M.P.1    Morse, D.2    Cermakian, N.3    Sassone-Corsi, P.4
  • 76
    • 33646130147 scopus 로고    scopus 로고
    • A clock shock: mouse CLOCK is not required for circadian oscillator function
    • The authors describe the phenotype of Clock-deficient mice generated by homologous recombination. The mild phenotype, in comparison to the c/c mice described in [74], suggests the presence of compensatory mechanisms and functional paralogs of the CLOCK protein.
    • Debruyne J.P., Noton E., Lambert C.M., Maywood E.S., Weaver D.R., and Reppert S.M. A clock shock: mouse CLOCK is not required for circadian oscillator function. Neuron 50 (2006) 465-477. The authors describe the phenotype of Clock-deficient mice generated by homologous recombination. The mild phenotype, in comparison to the c/c mice described in [74], suggests the presence of compensatory mechanisms and functional paralogs of the CLOCK protein.
    • (2006) Neuron , vol.50 , pp. 465-477
    • Debruyne, J.P.1    Noton, E.2    Lambert, C.M.3    Maywood, E.S.4    Weaver, D.R.5    Reppert, S.M.6
  • 77
    • 0035919618 scopus 로고    scopus 로고
    • NPAS2: an analog of clock operative in the mammalian forebrain
    • Reick M., Garcia J.A., Dudley C., and McKnight S.L. NPAS2: an analog of clock operative in the mammalian forebrain. Science 293 (2001) 506-509
    • (2001) Science , vol.293 , pp. 506-509
    • Reick, M.1    Garcia, J.A.2    Dudley, C.3    McKnight, S.L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.