메뉴 건너뛰기




Volumn 579, Issue 5, 2005, Pages 1067-1071

Quaternary structure of LOV-domain containing polypeptide of Arabidopsis FKF1 protein

Author keywords

FKF1 protein; LOV domain; Photoperiodism; Quaternary structure; Small angle X ray scattering

Indexed keywords

ARABIDOPSIS PROTEIN; DIMER; FLAVIN BINDING KELCH REPEAT F BOX PROTEIN; POLYPEPTIDE; UNCLASSIFIED DRUG;

EID: 13844261202     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2004.12.078     Document Type: Article
Times cited : (37)

References (21)
  • 1
    • 0037136548 scopus 로고    scopus 로고
    • Molecular basis of seasonal time measurement in Arabidopsis
    • M.J. Yanovsky, and S.A. Kay Molecular basis of seasonal time measurement in Arabidopsis Nature 419 2002 308 312
    • (2002) Nature , vol.419 , pp. 308-312
    • Yanovsky, M.J.1    Kay, S.A.2
  • 2
    • 0037381239 scopus 로고    scopus 로고
    • Living by the calendar: How plants know when to flower
    • M.J. Yanovsky, and S.A. Kay Living by the calendar: how plants know when to flower Nat. Rev. Mol. Cell Biol. 4 2003 265 275
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 265-275
    • Yanovsky, M.J.1    Kay, S.A.2
  • 3
    • 0035953691 scopus 로고    scopus 로고
    • CONSTANTS mediates between the circadian clock and the control of flowering in Arabidopsis
    • P. Suarez-Lopez CONSTANTS mediates between the circadian clock and the control of flowering in Arabidopsis Nature 410 2001 1116 1120
    • (2001) Nature , vol.410 , pp. 1116-1120
    • Suarez-Lopez, P.1
  • 4
    • 0344443180 scopus 로고    scopus 로고
    • FKF1 is essential for photoperiodic-specific light signaling in Arabidopsis
    • T. Imaizumi, H.G. Tran, T.E. Swartz, W.R. Briggs, and S.A. Kay FKF1 is essential for photoperiodic-specific light signaling in Arabidopsis Nature 426 2003 302 306
    • (2003) Nature , vol.426 , pp. 302-306
    • Imaizumi, T.1    Tran, H.G.2    Swartz, T.E.3    Briggs, W.R.4    Kay, S.A.5
  • 5
    • 0036583102 scopus 로고    scopus 로고
    • Phototropins 1 and 2: Versatile plant blue-light receptors
    • W.R. Briggs, and J.M. Christie Phototropins 1 and 2: versatile plant blue-light receptors Trend. Plant Sci. 7 2002 204 210
    • (2002) Trend. Plant Sci. , vol.7 , pp. 204-210
    • Briggs, W.R.1    Christie, J.M.2
  • 6
    • 0032990441 scopus 로고    scopus 로고
    • PAS domains: Internal sensors of oxygen, redox potential and light
    • B.L. Taylor, and I.B. Zhulin PAS domains: internal sensors of oxygen, redox potential and light Microbiol. Mol. Biol. Rev. 63 1999 479 506
    • (1999) Microbiol. Mol. Biol. Rev. , vol.63 , pp. 479-506
    • Taylor, B.L.1    Zhulin, I.B.2
  • 7
    • 0034622586 scopus 로고    scopus 로고
    • Photochemical and mutational analysis of the FMN-binding domains of the plant blue light receptor, phototropin
    • M. Salomon, J.M. Christie, E. Kneib, U. Lempert, and W.R. Briggs Photochemical and mutational analysis of the FMN-binding domains of the plant blue light receptor, phototropin Biochemistry 39 2000 9401 9410
    • (2000) Biochemistry , vol.39 , pp. 9401-9410
    • Salomon, M.1    Christie, J.M.2    Kneib, E.3    Lempert, U.4    Briggs, W.R.5
  • 8
    • 0037435618 scopus 로고    scopus 로고
    • The LOV domain family: Photoresponsive signaling modules coupled to diverse output domains
    • S. Crosson, S. Rajagopal, and K. Moffat The LOV domain family: photoresponsive signaling modules coupled to diverse output domains Biochemistry 42 2003 2 10
    • (2003) Biochemistry , vol.42 , pp. 2-10
    • Crosson, S.1    Rajagopal, S.2    Moffat, K.3
  • 9
    • 4143081643 scopus 로고    scopus 로고
    • Dimerization of the plant photoreceptor phototropin is probably mediated by the LOV domain
    • M. Salomon, U. Lempert, and W. Rüdiger Dimerization of the plant photoreceptor phototropin is probably mediated by the LOV domain FEBS Lett. 572 2004 8 10
    • (2004) FEBS Lett. , vol.572 , pp. 8-10
    • Salomon, M.1    Lempert, U.2    Rüdiger, W.3
  • 10
    • 9744263917 scopus 로고    scopus 로고
    • Light-induced structural changes of LOV-domain containing polypeptides from Arabidopsis phototropin 1 and 2 studied by small-angle X-ray scattering
    • M. Nakasako, T. Iwata, D. Matsuoka, and S. Tokutomi Light-induced structural changes of LOV-domain containing polypeptides from Arabidopsis phototropin 1 and 2 studied by small-angle X-ray scattering Biochemistry 43 2004 14881 14890
    • (2004) Biochemistry , vol.43 , pp. 14881-14890
    • Nakasako, M.1    Iwata, T.2    Matsuoka, D.3    Tokutomi, S.4
  • 12
    • 0026910457 scopus 로고
    • Determination of the regularization parameter in indirect-transform methods using perceptual criteria
    • D.I. Svergun Determination of the regularization parameter in indirect-transform methods using perceptual criteria J. Appl. Crystallogr. 25 1992 495 503
    • (1992) J. Appl. Crystallogr. , vol.25 , pp. 495-503
    • Svergun, D.I.1
  • 13
    • 0035010533 scopus 로고    scopus 로고
    • Determination of domain structure of proteins from X-ray solution scattering
    • D.I. Svergun, M.V. Petoukhov, and M.H.J. Koch Determination of domain structure of proteins from X-ray solution scattering Biophys. J. 80 2001 2946 2953
    • (2001) Biophys. J. , vol.80 , pp. 2946-2953
    • Svergun, D.I.1    Petoukhov, M.V.2    Koch, M.H.J.3
  • 14
    • 0034724518 scopus 로고    scopus 로고
    • ZEITLUPE encodes a novel clock-associated PAS protein from Arabidopsis
    • D.E. Somers, T.F. Schultz, M. Milnamow, and S.A. Kay ZEITLUPE encodes a novel clock-associated PAS protein from Arabidopsis Cell 101 2000 319 329
    • (2000) Cell , vol.101 , pp. 319-329
    • Somers, D.E.1    Schultz, T.F.2    Milnamow, M.3    Kay, S.A.4
  • 16
    • 0029017976 scopus 로고
    • Protein-protein interaction via PAS domains: Role of the PAS domain in positive and negative regulation of the bHLH/PAS dioxin receptor-Arnt
    • M.C. Lindebro, L. Poellinger, and M.L. Whitelaw Protein-protein interaction via PAS domains: role of the PAS domain in positive and negative regulation of the bHLH/PAS dioxin receptor-Arnt EMBO J. 14 1995 3528 3539
    • (1995) EMBO J. , vol.14 , pp. 3528-3539
    • Lindebro, M.C.1    Poellinger, L.2    Whitelaw, M.L.3
  • 17
    • 0036016438 scopus 로고    scopus 로고
    • Photoexcited structure of a plant photoreceptor domain reveals a light-driven molecular switch
    • S. Crosson, and K. Moffat Photoexcited structure of a plant photoreceptor domain reveals a light-driven molecular switch Plant Cell 14 2002 1067 1075
    • (2002) Plant Cell , vol.14 , pp. 1067-1075
    • Crosson, S.1    Moffat, K.2
  • 18
    • 0037380836 scopus 로고    scopus 로고
    • Crystal structures and molecular mechanism of a light-induced signaling switch: The Phot-LOV1 domain from Chlamydomonas reinhardtii
    • R. Fedorov, I. Schlichting, E. Hartmann, T. Domratcheva, M. Fuhrmann, and P. Hegemann Crystal structures and molecular mechanism of a light-induced signaling switch: the Phot-LOV1 domain from Chlamydomonas reinhardtii Biophys. J. 84 2003 2474 2482
    • (2003) Biophys. J. , vol.84 , pp. 2474-2482
    • Fedorov, R.1    Schlichting, I.2    Hartmann, E.3    Domratcheva, T.4    Fuhrmann, M.5    Hegemann, P.6
  • 19
    • 0141707094 scopus 로고    scopus 로고
    • Structural basis of a phototropin light switch
    • S.M. Harper, L.C. Neil, and K.H. Gardner Structural basis of a phototropin light switch Science 301 2003 1541 1544
    • (2003) Science , vol.301 , pp. 1541-1544
    • Harper, S.M.1    Neil, L.C.2    Gardner, K.H.3
  • 20
    • 0035853139 scopus 로고    scopus 로고
    • Structure of a flavin-binding plant photoreceptor domain: Insights into ligand-mediated signal transduction
    • S. Crosson, and K. Moffat Structure of a flavin-binding plant photoreceptor domain: insights into ligand-mediated signal transduction Proc. Natl. Acad. Sci. USA 98 2001 2995 3000
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 2995-3000
    • Crosson, S.1    Moffat, K.2
  • 21
    • 0000107715 scopus 로고    scopus 로고
    • ASSA - A program for three-dimensional rendering in solution scattering from biopolymers
    • M.B. Kozin, and D.I. Svergun ASSA - a program for three-dimensional rendering in solution scattering from biopolymers J. Appl. Crystallogr. 34 1997 33 41
    • (1997) J. Appl. Crystallogr. , vol.34 , pp. 33-41
    • Kozin, M.B.1    Svergun, D.I.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.