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Volumn 125, Issue 3, 2006, Pages 497-508

Circadian Regulator CLOCK Is a Histone Acetyltransferase

Author keywords

[No Author keywords available]

Indexed keywords

DNA; HISTONE ACETYLTRANSFERASE; HISTONE H3; HISTONE H4; STEROID RECEPTOR COACTIVATOR 1; TRANSCRIPTION FACTOR CLOCK;

EID: 33646145721     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cell.2006.03.033     Document Type: Article
Times cited : (699)

References (68)
  • 2
    • 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
  • 4
    • 0032511229 scopus 로고    scopus 로고
    • A serum shock induces circadian gene expression in mammalian tissue culture cells
    • Balsalobre A., Damiola F., and Schibler U. A serum shock induces circadian gene expression in mammalian tissue culture cells. Cell 93 (1998) 929-937
    • (1998) Cell , vol.93 , pp. 929-937
    • Balsalobre, A.1    Damiola, F.2    Schibler, U.3
  • 5
    • 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
  • 6
    • 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
  • 7
    • 0033287749 scopus 로고    scopus 로고
    • An SDS-PAGE-based enzyme activity assay for the detection and identification of histone acetyltransferases
    • Brownell J.E., Mizzen C.A., and Allis C.D. An SDS-PAGE-based enzyme activity assay for the detection and identification of histone acetyltransferases. Methods Mol. Biol. 119 (1999) 343-353
    • (1999) Methods Mol. Biol. , vol.119 , pp. 343-353
    • Brownell, J.E.1    Mizzen, C.A.2    Allis, C.D.3
  • 10
    • 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
  • 11
    • 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
  • 12
    • 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
  • 16
    • 0034940767 scopus 로고    scopus 로고
    • Light-induced phase-delay of the chicken pineal circadian clock is associated with the induction of cE4bp4, a potential transcriptional repressor of cPer2 gene
    • Doi M., Nakajima Y., Okano T., and Fukada Y. Light-induced phase-delay of the chicken pineal circadian clock is associated with the induction of cE4bp4, a potential transcriptional repressor of cPer2 gene. Proc. Natl. Acad. Sci. USA 98 (2001) 8089-8094
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 8089-8094
    • Doi, M.1    Nakajima, Y.2    Okano, T.3    Fukada, Y.4
  • 17
    • 2642560489 scopus 로고    scopus 로고
    • Negative control of circadian clock regulator E4BP4 by casein kinase Iepsilon-mediated phosphorylation
    • Doi M., Okano T., Yujnovsky I., Sassone-Corsi P., and Fukada Y. Negative control of circadian clock regulator E4BP4 by casein kinase Iepsilon-mediated phosphorylation. Curr. Biol. 14 (2004) 975-980
    • (2004) Curr. Biol. , vol.14 , pp. 975-980
    • Doi, M.1    Okano, T.2    Yujnovsky, I.3    Sassone-Corsi, P.4    Fukada, Y.5
  • 18
    • 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
  • 19
    • 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
  • 20
    • 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
  • 21
    • 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
  • 22
    • 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
  • 24
    • 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
  • 25
    • 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
  • 26
    • 22544475560 scopus 로고    scopus 로고
    • Common pathways in circadian and cell cycle clocks: light-dependent activation of Fos/AP-1 in zebrafish controls CRY-1a and WEE-1
    • Hirayama J., Cardone L., Doi M., and Sassone-Corsi P. Common pathways in circadian and cell cycle clocks: light-dependent activation of Fos/AP-1 in zebrafish controls CRY-1a and WEE-1. Proc. Natl. Acad. Sci. USA 102 (2005) 10194-10199
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 10194-10199
    • Hirayama, J.1    Cardone, L.2    Doi, M.3    Sassone-Corsi, P.4
  • 27
    • 0032510778 scopus 로고    scopus 로고
    • The basic-helix-loop-helix-PAS orphan MOP3 forms transcriptionally active complexes with circadian and hypoxia factors
    • Hogenesch J.B., Gu Y.Z., Jain S., and Bradfield C.A. The basic-helix-loop-helix-PAS orphan MOP3 forms transcriptionally active complexes with circadian and hypoxia factors. Proc. Natl. Acad. Sci. USA 95 (1998) 5474-5479
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 5474-5479
    • Hogenesch, J.B.1    Gu, Y.Z.2    Jain, S.3    Bradfield, C.A.4
  • 28
    • 0034677535 scopus 로고    scopus 로고
    • Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase
    • Imai S., Armstrong C.M., Kaeberlein M., and Guarente L. Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase. Nature 403 (2000) 795-800
    • (2000) Nature , vol.403 , pp. 795-800
    • Imai, S.1    Armstrong, C.M.2    Kaeberlein, M.3    Guarente, L.4
  • 29
    • 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
  • 30
    • 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
  • 31
    • 0036843170 scopus 로고    scopus 로고
    • Chromosomal gradient of histone acetylation established by Sas2p and Sir2p functions as a shield against gene silencing
    • Kimura A., Umehara T., and Horikoshi M. Chromosomal gradient of histone acetylation established by Sas2p and Sir2p functions as a shield against gene silencing. Nat. Genet. 32 (2002) 370-377
    • (2002) Nat. Genet. , vol.32 , pp. 370-377
    • Kimura, A.1    Umehara, T.2    Horikoshi, M.3
  • 32
    • 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
  • 34
    • 0042626226 scopus 로고    scopus 로고
    • BMAL1-dependent circadian oscillation of nuclear CLOCK: posttranslational events induced by dimerization of transcriptional activators of the mammalian clock system
    • Kondratov R.V., Chernov M.V., Kondratova A.A., Gorbacheva V.Y., Gudkov A.V., and Antoch M.P. BMAL1-dependent circadian oscillation of nuclear CLOCK: posttranslational events induced by dimerization of transcriptional activators of the mammalian clock system. Genes Dev. 17 (2003) 1921-1932
    • (2003) Genes Dev. , vol.17 , pp. 1921-1932
    • Kondratov, R.V.1    Chernov, M.V.2    Kondratova, A.A.3    Gorbacheva, V.Y.4    Gudkov, A.V.5    Antoch, M.P.6
  • 35
    • 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
  • 36
    • 0032142918 scopus 로고    scopus 로고
    • Roles of histone acetyltransferases and deacetylases in gene regulation
    • Kuo M.H., and Allis C.D. Roles of histone acetyltransferases and deacetylases in gene regulation. Bioessays 20 (1998) 615-626
    • (1998) Bioessays , vol.20 , pp. 615-626
    • Kuo, M.H.1    Allis, C.D.2
  • 38
    • 0035966317 scopus 로고    scopus 로고
    • Posttranslational mechanisms regulate the mammalian circadian clock
    • Lee C., Etchegaray J.P., Cagampang F.R., Loudon A.S., and Reppert S.M. Posttranslational mechanisms regulate the mammalian circadian clock. Cell 107 (2001) 855-867
    • (2001) Cell , vol.107 , pp. 855-867
    • Lee, C.1    Etchegaray, J.P.2    Cagampang, F.R.3    Loudon, A.S.4    Reppert, S.M.5
  • 39
    • 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
  • 40
    • 4544362674 scopus 로고    scopus 로고
    • Mammalian circadian biology: elucidating genome-wide levels of temporal organization
    • Lowrey P.L., and Takahashi J.S. Mammalian circadian biology: elucidating genome-wide levels of temporal organization. Annu. Rev. Genomics Hum. Genet. 5 (2004) 407-441
    • (2004) Annu. Rev. Genomics Hum. Genet. , vol.5 , pp. 407-441
    • Lowrey, P.L.1    Takahashi, J.S.2
  • 42
    • 0035967914 scopus 로고    scopus 로고
    • Regulation of CLOCK and MOP4 by nuclear hormone receptors in the vasculature: A humoral mechanism to reset a peripheral clock
    • McNamara P., Seo S.P., Rudic R.D., Sehgal A., Chakravarti D., and FitzGerald G.A. Regulation of CLOCK and MOP4 by nuclear hormone receptors in the vasculature: A humoral mechanism to reset a peripheral clock. Cell 105 (2001) 877-889
    • (2001) Cell , vol.105 , pp. 877-889
    • McNamara, P.1    Seo, S.P.2    Rudic, R.D.3    Sehgal, A.4    Chakravarti, D.5    FitzGerald, G.A.6
  • 44
    • 0033031978 scopus 로고    scopus 로고
    • Histone acetyltransferases: preparation of substrates and assay procedures
    • Mizzen C.A., Brownell J.E., Cook R.G., and Allis C.D. Histone acetyltransferases: preparation of substrates and assay procedures. Methods Enzymol. 304 (1999) 675-696
    • (1999) Methods Enzymol. , vol.304 , pp. 675-696
    • Mizzen, C.A.1    Brownell, J.E.2    Cook, R.G.3    Allis, C.D.4
  • 45
    • 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
  • 47
    • 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
  • 48
    • 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
  • 49
    • 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
  • 51
    • 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
  • 52
    • 0035997367 scopus 로고    scopus 로고
    • Metabolism and the control of circadian rhythms
    • Rutter J., Reick M., and McKnight S.L. Metabolism and the control of circadian rhythms. Annu. Rev. Biochem. 71 (2002) 307-331
    • (2002) Annu. Rev. Biochem. , vol.71 , pp. 307-331
    • Rutter, J.1    Reick, M.2    McKnight, S.L.3
  • 53
    • 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
  • 54
    • 15044341917 scopus 로고    scopus 로고
    • Cellular oscillators: rhythmic gene expression and metabolism
    • Schibler U., and Naef F. Cellular oscillators: rhythmic gene expression and metabolism. Curr. Opin. Cell Biol. 17 (2005) 223-229
    • (2005) Curr. Opin. Cell Biol. , vol.17 , pp. 223-229
    • Schibler, U.1    Naef, F.2
  • 56
    • 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
  • 57
    • 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
  • 58
    • 0036842129 scopus 로고    scopus 로고
    • Sir2p and Sas2p opposingly regulate acetylation of yeast histone H4 lysine16 and spreading of heterochromatin
    • Suka N., Luo K., and Grunstein M. Sir2p and Sas2p opposingly regulate acetylation of yeast histone H4 lysine16 and spreading of heterochromatin. Nat. Genet. 32 (2002) 378-383
    • (2002) Nat. Genet. , vol.32 , pp. 378-383
    • Suka, N.1    Luo, K.2    Grunstein, M.3
  • 62
    • 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
  • 63
    • 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
  • 64
    • 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
  • 65
    • 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
  • 66
    • 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
  • 68
    • 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


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