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Volumn 287, Issue 5, 2012, Pages 3241-3248

Fluorescence correlation spectroscopy to monitor Kai protein-based circadian oscillations in real time

Author keywords

[No Author keywords available]

Indexed keywords

CIRCADIAN CLOCK; CIRCADIAN OSCILLATIONS; COMPLEX FORMATIONS; CONFOCAL FLUORESCENCE; DEPHOSPHORYLATIONS; DETECTION SYSTEM; DYNAMIC PROTEINS; FLUORESCENCE CORRELATION SPECTROSCOPY; FLUORESCENT PROBES; HIGH TEMPERATURE; IN-VITRO; LASER EXPOSURE; MONITORING METHODS; NANOMOLAR CONCENTRATION; NONINVASIVE METHODS; OSCILLATORY SYSTEM; PROTEIN-PROTEIN INTERACTIONS; REAL TIME; REGULATORY SYSTEMS; SHORT TERM; TEMPERATURE CHANGES; WILD TYPES;

EID: 84856241465     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.265777     Document Type: Article
Times cited : (12)

References (29)
  • 3
    • 0037435030 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics
    • Aebersold, R., and Mann, M. (2003) Mass spectrometry-based proteomics. Nature 422, 198-207
    • (2003) Nature , vol.422 , pp. 198-207
    • Aebersold, R.1    Mann, M.2
  • 5
    • 17244373578 scopus 로고    scopus 로고
    • Reconstitution of circadian oscillation of cyanobacterial KaiC phosphorylation in vitro
    • Nakajima, M., Imai, K., Ito, H., Nishiwaki, T., Murayama, Y., Iwasaki, H., Oyama, T., and Kondo, T. (2005) Reconstitution of circadian oscillation of cyanobacterial KaiC phosphorylation in vitro. Science 308, 414-415
    • (2005) Science , vol.308 , pp. 414-415
    • Nakajima, M.1    Imai, K.2    Ito, H.3    Nishiwaki, T.4    Murayama, Y.5    Iwasaki, H.6    Oyama, T.7    Kondo, T.8
  • 7
    • 34548382214 scopus 로고    scopus 로고
    • A sequential program of dual phosphorylation of KaiC as a basis for circadian rhythm in cyanobacteria
    • Nishiwaki, T., Satomi, Y., Kitayama, Y., Terauchi, K., Kiyohara, R., Takao, T., and Kondo, T. (2007) A sequential program of dual phosphorylation of KaiC as a basis for circadian rhythm in cyanobacteria. EMBO J. 26, 4029-4037
    • (2007) EMBO J. , vol.26 , pp. 4029-4037
    • Nishiwaki, T.1    Satomi, Y.2    Kitayama, Y.3    Terauchi, K.4    Kiyohara, R.5    Takao, T.6    Kondo, T.7
  • 8
    • 33746147001 scopus 로고    scopus 로고
    • Cyanobacterial circadian pacemaker. Kai protein complex dynamics in the KaiC phosphorylation cycle in vitro
    • Kageyama, H., Nishiwaki, T., Nakajima, M., Iwasaki, H., Oyama, T., and Kondo, T. (2006) Cyanobacterial circadian pacemaker. Kai protein complex dynamics in the KaiC phosphorylation cycle in vitro. Mol. Cell 23, 161-171
    • (2006) Mol. Cell , vol.23 , pp. 161-171
    • Kageyama, H.1    Nishiwaki, T.2    Nakajima, M.3    Iwasaki, H.4    Oyama, T.5    Kondo, T.6
  • 10
    • 60849095555 scopus 로고    scopus 로고
    • Nonparametric entrainment of the in vitro circadian phosphorylation rhythm of cyanobacterial KaiC by temperature cycle
    • Yoshida, T., Murayama, Y., Ito, H., Kageyama, H., and Kondo, T. (2009) Nonparametric entrainment of the in vitro circadian phosphorylation rhythm of cyanobacterial KaiC by temperature cycle. Proc. Natl. Acad. Sci. U.S.A. 106, 1648-1653
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 1648-1653
    • Yoshida, T.1    Murayama, Y.2    Ito, H.3    Kageyama, H.4    Kondo, T.5
  • 12
    • 0037462789 scopus 로고    scopus 로고
    • Circadian formation of clock protein complexes by KaiA, KaiB, KaiC, and SasA in cyanobacteria
    • Kageyama, H., Kondo, T., and Iwasaki, H. (2003) Circadian formation of clock protein complexes by KaiA, KaiB, KaiC, and SasA in cyanobacteria. J. Biol. Chem. 278, 2388-2395
    • (2003) J. Biol. Chem. , vol.278 , pp. 2388-2395
    • Kageyama, H.1    Kondo, T.2    Iwasaki, H.3
  • 13
    • 0037881861 scopus 로고    scopus 로고
    • KaiB functions as an attenuator of KaiC phosphorylation in the cyanobacterial circadian clock system
    • Kitayama, Y., Iwasaki, H., Nishiwaki, T., and Kondo, T. (2003) KaiB functions as an attenuator of KaiC phosphorylation in the cyanobacterial circadian clock system. EMBO J. 22, 2127-2134
    • (2003) EMBO J. , vol.22 , pp. 2127-2134
    • Kitayama, Y.1    Iwasaki, H.2    Nishiwaki, T.3    Kondo, T.4
  • 14
    • 40849145295 scopus 로고    scopus 로고
    • Assembly and disassembly dynamics of the cyanobacterial periodosome
    • Akiyama, S., Nohara, A., Ito, K., and Maéda, Y. (2008) Assembly and disassembly dynamics of the cyanobacterial periodosome. Mol. Cell 29, 703-716
    • (2008) Mol. Cell , vol.29 , pp. 703-716
    • Akiyama, S.1    Nohara, A.2    Ito, K.3    Maéda, Y.4
  • 16
    • 13844277017 scopus 로고    scopus 로고
    • New methodologies for measuring protein interactions in vivo and in vitro
    • Piehler, J. (2005) New methodologies for measuring protein interactions in vivo and in vitro. Curr. Opin. Struct. Biol. 15, 4-14
    • (2005) Curr. Opin. Struct. Biol. , vol.15 , pp. 4-14
    • Piehler, J.1
  • 17
    • 0142138241 scopus 로고    scopus 로고
    • Analysis of protein interactions using fluorescence technologies
    • Yan, Y., and Marriott, G. (2003) Analysis of protein interactions using fluorescence technologies. Curr. Opin. Chem. Biol. 7, 635-640
    • (2003) Curr. Opin. Chem. Biol. , vol.7 , pp. 635-640
    • Yan, Y.1    Marriott, G.2
  • 19
    • 77953123601 scopus 로고    scopus 로고
    • Incorporation of fluorescent non-natural amino acids into N-terminal tag of proteins in cell-free translation and its dependence on position and neighboring codons
    • Abe, R., Shiraga, K., Ebisu, S., Takagi, H., and Hohsaka, T. (2010) Incorporation of fluorescent non-natural amino acids into N-terminal tag of proteins in cell-free translation and its dependence on position and neighboring codons. J. Biosci. Bioeng. 110, 32-38
    • (2010) J. Biosci. Bioeng. , vol.110 , pp. 32-38
    • Abe, R.1    Shiraga, K.2    Ebisu, S.3    Takagi, H.4    Hohsaka, T.5
  • 20
    • 0346895290 scopus 로고    scopus 로고
    • High fidelity SNP genotyping using sequence-specific primer elongation and fluorescence correlation spectroscopy
    • Hori, K., Shin, W. S., Hemmi, C., Toyo-oka, T., and Makino, T. (2003) High fidelity SNP genotyping using sequence-specific primer elongation and fluorescence correlation spectroscopy. Curr. Pharm. Biotechnol. 4, 477-484
    • (2003) Curr. Pharm. Biotechnol. , vol.4 , pp. 477-484
    • Hori, K.1    Shin, W.S.2    Hemmi, C.3    Toyo-oka, T.4    Makino, T.5
  • 21
    • 0036900746 scopus 로고    scopus 로고
    • Incorporation of non-natural amino acids into proteins
    • Hohsaka, T., and Sisido, M. (2002) Incorporation of non-natural amino acids into proteins. Curr. Opin. Chem. Biol. 6, 809-815
    • (2002) Curr. Opin. Chem. Biol. , vol.6 , pp. 809-815
    • Hohsaka, T.1    Sisido, M.2
  • 22
    • 65849133747 scopus 로고    scopus 로고
    • A protease inhibitor discovery method using fluorescence correlation spectroscopy with position-specific labeled protein substrates
    • Nakata, H., Ohtsuki, T., and Sisido, M. (2009) A protease inhibitor discovery method using fluorescence correlation spectroscopy with position-specific labeled protein substrates. Anal. Biochem. 390, 121-125
    • (2009) Anal. Biochem. , vol.390 , pp. 121-125
    • Nakata, H.1    Ohtsuki, T.2    Sisido, M.3
  • 23
    • 0033021689 scopus 로고    scopus 로고
    • Resolution of fluorescence correlation measurements
    • Meseth, U., Wohland, T., Rigler, R., and Vogel, H. (1999) Resolution of fluorescence correlation measurements. Biophys. J. 76, 1619-1631
    • (1999) Biophys. J. , vol.76 , pp. 1619-1631
    • Meseth, U.1    Wohland, T.2    Rigler, R.3    Vogel, H.4
  • 24
    • 0141743940 scopus 로고    scopus 로고
    • (Dunlap, J. C., Loros, J. J., and DeCoursey, P. J., eds) Sinauer Associates, Sunderland, MA
    • Johnson, C. H., Elliott, J., Foster, R., Honma, K., and Kronauer, R. (2004) in Biological Timekeeping (Dunlap, J. C., Loros, J. J., and DeCoursey, P. J., eds) pp. 67-105, Sinauer Associates, Sunderland, MA
    • (2004) Biological Timekeeping , pp. 67-105
    • Johnson, C.H.1    Elliott, J.2    Foster, R.3    Honma, K.4    Kronauer, R.5
  • 25
    • 0036405341 scopus 로고    scopus 로고
    • Temperature effect on entrainment, phase shifting, and amplitude of circadian clocks and its molecular bases
    • Rensing, L., and Ruoff, P. (2002) Temperature effect on entrainment, phase shifting, and amplitude of circadian clocks and its molecular bases. Chronobiol. Int. 19, 807-864
    • (2002) Chronobiol. Int. , vol.19 , pp. 807-864
    • Rensing, L.1    Ruoff, P.2
  • 28
    • 22144485495 scopus 로고    scopus 로고
    • Evolutions in science triggered by green fluorescent protein (GFP)
    • Schmid, J. A., and Neumeier, H. (2005) Evolutions in science triggered by green fluorescent protein (GFP). Chembiochem 6, 1149-1156
    • (2005) Chembiochem , vol.6 , pp. 1149-1156
    • Schmid, J.A.1    Neumeier, H.2
  • 29
    • 28544446072 scopus 로고    scopus 로고
    • One-step analysis of protein complexes in microliters of cell lysate
    • Stoevesandt, O., Köhler, K., Fischer, R., Johnston, I. C., and Brock, R. (2005) One-step analysis of protein complexes in microliters of cell lysate. Nat. Methods 2, 833-835
    • (2005) Nat. Methods , vol.2 , pp. 833-835
    • Stoevesandt, O.1    Köhler, K.2    Fischer, R.3    Johnston, I.C.4    Brock, R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.