메뉴 건너뛰기




Volumn 437, Issue 3, 2013, Pages 386-391

Effects of NAD(P)H and its derivatives on the DNA-binding activity of NPAS2, a mammalian circadian transcription factor

Author keywords

Clock genes; DNA binding activity; E box; NAD(P)H cofactor; PAS domain; Transcription

Indexed keywords

HOMODIMER; NICOTINAMIDE; NICOTINIC ACID; PROTEIN BMAL1; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR NPAS2; UNCLASSIFIED DRUG;

EID: 84880941452     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2013.06.086     Document Type: Article
Times cited : (13)

References (22)
  • 1
    • 33749031807 scopus 로고    scopus 로고
    • Molecular components of the mammalian circadian clock
    • Ko C.H., Takahashi J.S. Molecular components of the mammalian circadian clock. Hum. Mol. Genet. 2006, 15:271-277.
    • (2006) Hum. Mol. Genet. , vol.15 , pp. 271-277
    • Ko, C.H.1    Takahashi, J.S.2
  • 2
    • 0035919618 scopus 로고    scopus 로고
    • NPAS2: an analog of clock operative in the mammalian forebrain
    • Reick M., Garcia J.A., Dudley C., McKnight S.L. NPAS2: an analog of clock operative in the mammalian forebrain. Science 2001, 293:506-509.
    • (2001) Science , vol.293 , pp. 506-509
    • Reick, M.1    Garcia, J.A.2    Dudley, C.3    McKnight, S.L.4
  • 3
    • 0041346143 scopus 로고    scopus 로고
    • Clocks on the brain
    • Green C.B., Menaker M. Clocks on the brain. Science 2003, 301:319-320.
    • (2003) Science , vol.301 , pp. 319-320
    • Green, C.B.1    Menaker, M.2
  • 4
    • 34247526990 scopus 로고    scopus 로고
    • CLOCK and NPAS2 have overlapping roles in the suprachiasmatic circadian clock
    • DeBruyne J.P., Weaver D.R., Reppert S.M. CLOCK and NPAS2 have overlapping roles in the suprachiasmatic circadian clock. Nat. Neurosci. 2007, 10:543-545.
    • (2007) Nat. Neurosci. , vol.10 , pp. 543-545
    • DeBruyne, J.P.1    Weaver, D.R.2    Reppert, S.M.3
  • 6
    • 0027910469 scopus 로고
    • Recognition by Max of its cognate DNA through a dimeric b/HLH/Z domain
    • Ferre'-D'Amare A.R., Prendergast G.C., Ziff E.B., Burley S.K. Recognition by Max of its cognate DNA through a dimeric b/HLH/Z domain. Nature 1993, 363:38-45.
    • (1993) Nature , vol.363 , pp. 38-45
    • Ferre'-D'Amare, A.R.1    Prendergast, G.C.2    Ziff, E.B.3    Burley, S.K.4
  • 8
    • 37849019258 scopus 로고    scopus 로고
    • Crystal structure of E47-neurod1/beta2 bHLH domain-DNA complex: heterodimer selectivity and DNA recognition
    • Longo A., Guanga G.P., Rose R.B. Crystal structure of E47-neurod1/beta2 bHLH domain-DNA complex: heterodimer selectivity and DNA recognition. Biochemistry 2008, 47:218-229.
    • (2008) Biochemistry , vol.47 , pp. 218-229
    • Longo, A.1    Guanga, G.P.2    Rose, R.B.3
  • 9
    • 0942298565 scopus 로고    scopus 로고
    • Signal transduction by heme-containing PAS-domain proteins
    • Gilles-Gonzalez M.A., Gonzalez G. Signal transduction by heme-containing PAS-domain proteins. J. Appl. Physiol. 2004, 96:774-783.
    • (2004) J. Appl. Physiol. , vol.96 , pp. 774-783
    • Gilles-Gonzalez, M.A.1    Gonzalez, G.2
  • 12
    • 20444374458 scopus 로고    scopus 로고
    • CO-dependent activity-controlling mechanism of heme-containing CO-sensor protein, neuronal PAS domain protein 2
    • Uchida T., Sato E., Sato A., Sagami I., Shimizu T., Kitagawa T. CO-dependent activity-controlling mechanism of heme-containing CO-sensor protein, neuronal PAS domain protein 2. J. Biol. Chem. 2005, 280:21358-21368.
    • (2005) J. Biol. Chem. , vol.280 , pp. 21358-21368
    • Uchida, T.1    Sato, E.2    Sato, A.3    Sagami, I.4    Shimizu, T.5    Kitagawa, T.6
  • 13
    • 33646682128 scopus 로고    scopus 로고
    • Spectroscopic and DNA-binding characterization of the isolated heme-bound basic helix-loop-helix-PAS-A domain of neuronal PAS domain protein 2 (NPAS2), a transcription activator protein associated with circadian rhythms
    • Mukaiyama Y., Uchida T., Sato E., Sasaki A., Sato Y., Igarashi J., Kurokawa H., Sagami I., Kitagawa T., Shimizu T. Spectroscopic and DNA-binding characterization of the isolated heme-bound basic helix-loop-helix-PAS-A domain of neuronal PAS domain protein 2 (NPAS2), a transcription activator protein associated with circadian rhythms. FEBS J. 2006, 273:2528-2539.
    • (2006) FEBS J. , vol.273 , pp. 2528-2539
    • Mukaiyama, Y.1    Uchida, T.2    Sato, E.3    Sasaki, A.4    Sato, Y.5    Igarashi, J.6    Kurokawa, H.7    Sagami, I.8    Kitagawa, T.9    Shimizu, T.10
  • 14
    • 84863407362 scopus 로고    scopus 로고
    • Effects of bHLH domain on axial coordination of heme in the PAS-A domain of neuronal PAS domain protein 2 (NPAS2): conversion from His119/Cys170 coordination to His119/His171 coordination
    • Uchida T., Sagami I., Shimizu T., Ishimori K., Kitagawa T. Effects of bHLH domain on axial coordination of heme in the PAS-A domain of neuronal PAS domain protein 2 (NPAS2): conversion from His119/Cys170 coordination to His119/His171 coordination. J. Inorg. Biochem. 2012, 108:188-195.
    • (2012) J. Inorg. Biochem. , vol.108 , pp. 188-195
    • Uchida, T.1    Sagami, I.2    Shimizu, T.3    Ishimori, K.4    Kitagawa, T.5
  • 15
    • 39549117367 scopus 로고    scopus 로고
    • Effects of mutations in the heme domain on the transcriptional activity and DNA-binding activity of NPAS2
    • Ishida M., Ueha T., Sagami I. Effects of mutations in the heme domain on the transcriptional activity and DNA-binding activity of NPAS2. Biochem. Biophys. Res. Commun. 2008, 368:292-297.
    • (2008) Biochem. Biophys. Res. Commun. , vol.368 , pp. 292-297
    • Ishida, M.1    Ueha, T.2    Sagami, I.3
  • 16
    • 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., McKnight S.L. Regulation of clock and NPAS2 DNA binding by the redox state of NAD cofactors. Science 2001, 293:510-514.
    • (2001) Science , vol.293 , pp. 510-514
    • Rutter, J.1    Reick, M.2    Wu, L.C.3    McKnight, S.L.4
  • 18
    • 84892677127 scopus 로고    scopus 로고
    • Intermolecular recognition revealed by the complex structure of human CLOCK-BMAL1 basic helix-loop-helix domains with E-box DNA
    • Wang Z., Wu Y., Li L., Su X.D. Intermolecular recognition revealed by the complex structure of human CLOCK-BMAL1 basic helix-loop-helix domains with E-box DNA. Cell Res. 2012, 170:1038.
    • (2012) Cell Res. , vol.170 , pp. 1038
    • Wang, Z.1    Wu, Y.2    Li, L.3    Su, X.D.4
  • 19
    • 33646145721 scopus 로고    scopus 로고
    • Circadian regulator CLOCK is a histone acetyltransferase
    • Doi M., Hirayama J., Sassone-Corsi P. Circadian regulator CLOCK is a histone acetyltransferase. Cell 2006, 125:497-508.
    • (2006) Cell , vol.125 , pp. 497-508
    • Doi, M.1    Hirayama, J.2    Sassone-Corsi, P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.