메뉴 건너뛰기




Volumn , Issue , 2013, Pages 7-22

The biophysics and engineering of signaling photoreceptors

Author keywords

[No Author keywords available]

Indexed keywords


EID: 85029314987     PISSN: None     EISSN: None     Source Type: Book    
DOI: None     Document Type: Chapter
Times cited : (3)

References (57)
  • 3
    • 53749101663 scopus 로고    scopus 로고
    • Cyanobacteriochromes: a new superfamily of tetrapyrrole-binding photoreceptors in cyanobacteria
    • Ikeuchi M, Ishizuka T. Cyanobacteriochromes: a new superfamily of tetrapyrrole-binding photoreceptors in cyanobacteria. Photochem. Photobiol. Sci. 2008; 7: 1159-67.
    • (2008) Photochem. Photobiol. Sci. , vol.7 , pp. 1159-1167
    • Ikeuchi, M.1    Ishizuka, T.2
  • 4
    • 77951166118 scopus 로고    scopus 로고
    • A brief history of phytochromes
    • Rockwell NC, Lagarias JC. A brief history of phytochromes. ChemPhysChem 2010; 11: 1172-80.
    • (2010) ChemPhysChem , vol.11 , pp. 1172-1180
    • Rockwell, N.C.1    Lagarias, J.C.2
  • 5
    • 0032990441 scopus 로고    scopus 로고
    • PAS domains: internal sensors of oxygen, redox potential, and light
    • Taylor BL, Zhulin IB. PAS domains: internal sensors of oxygen, redox potential, and light. Microbiol. Mol. Biol. Rev. 1999; 63: 479-506.
    • (1999) Microbiol. Mol. Biol. Rev. , vol.63 , pp. 479-506
    • Taylor, B.L.1    Zhulin, I.B.2
  • 6
    • 70349777587 scopus 로고    scopus 로고
    • Structure and Signaling Mechanism of Per-ARNT-Sim Domains
    • Möglich A, Ayers RA, Moffat K. Structure and Signaling Mechanism of Per-ARNT-Sim Domains. Structure 2009; 17: 1282-94.
    • (2009) Structure , vol.17 , pp. 1282-1294
    • Möglich, A.1    Ayers, R.A.2    Moffat, K.3
  • 8
    • 0043125483 scopus 로고    scopus 로고
    • Anticipatory active-site motions and chromophore distortion prime photoreceptor PYP for light activation
    • Getzoff ED, Gutwin KN, Genick UK. Anticipatory active-site motions and chromophore distortion prime photoreceptor PYP for light activation. Nat. Struct. Biol. 2003; 10: 663-8.
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 663-668
    • Getzoff, E.D.1    Gutwin, K.N.2    Genick, U.K.3
  • 9
    • 37049002915 scopus 로고    scopus 로고
    • N-and C-terminal flanking regions modulate light-induced signal transduction in the LOV2 domain of the blue light sensor phototropin 1 from Avena sativa
    • Halavaty AS, Moffat K. N-and C-terminal flanking regions modulate light-induced signal transduction in the LOV2 domain of the blue light sensor phototropin 1 from Avena sativa. Biochemistry 2007; 46: 14001-9.
    • (2007) Biochemistry , vol.46 , pp. 14001-14009
    • Halavaty, A.S.1    Moffat, K.2
  • 13
    • 0036971196 scopus 로고    scopus 로고
    • Crystallographic structure of the K intermediate of bacteriorhodopsin: conservation of free energy after photoisomerization of the retinal
    • Schobert B, Cupp-Vickery J, Hornak V, Smith S, Lanyi J. Crystallographic structure of the K intermediate of bacteriorhodopsin: conservation of free energy after photoisomerization of the retinal. J. Mol. Biol. 2002; 321: 715-26.
    • (2002) J. Mol. Biol. , vol.321 , pp. 715-726
    • Schobert, B.1    Cupp-Vickery, J.2    Hornak, V.3    Smith, S.4    Lanyi, J.5
  • 14
    • 55749108880 scopus 로고    scopus 로고
    • Crystal structure of Pseudomonas aeruginosa bacteriophytochrome: Photoconversion and signal transduction
    • Yang X, Kuk J, Moffat K. Crystal structure of Pseudomonas aeruginosa bacteriophytochrome: Photoconversion and signal transduction. Proc. Natl. Acad. Sci. USA 2008; 105: 14715-20.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 14715-14720
    • Yang, X.1    Kuk, J.2    Moffat, K.3
  • 15
    • 78650647900 scopus 로고    scopus 로고
    • Natural and engineered photoactivated nucleotidyl cyclases for optogenetic applications
    • Ryu M-H, Moskvin OV, Siltberg-Liberles J, Gomelsky M. Natural and engineered photoactivated nucleotidyl cyclases for optogenetic applications. J. Biol. Chem. 2010; 285: 41501-8.
    • (2010) J. Biol. Chem. , vol.285 , pp. 41501-41508
    • Ryu, M-H.1    Moskvin, O.V.2    Siltberg-Liberles, J.3    Gomelsky, M.4
  • 19
    • 65649113981 scopus 로고    scopus 로고
    • Mammalian expression of infrared fluorescent proteins engineered from a bacterial phytochrome
    • Shu X, Royant A, Lin MZ, Aguilera TA, Lev-Ram V, Steinbach PA, Tsien RY. Mammalian expression of infrared fluorescent proteins engineered from a bacterial phytochrome. Science 2009; 324: 804-7.
    • (2009) Science , vol.324 , pp. 804-807
    • Shu, X.1    Royant, A.2    Lin, M.Z.3    Aguilera, T.A.4    Lev-Ram, V.5    Steinbach, P.A.6    Tsien, R.Y.7
  • 21
    • 84857715916 scopus 로고    scopus 로고
    • Structure-guided Engineering Enhances a Phytochrome-based Infrared Fluorescent Protein
    • Auldridge ME, Satyshur KA, Anstrom DM, Forest KT. Structure-guided Engineering Enhances a Phytochrome-based Infrared Fluorescent Protein. J. Biol. Chem. 2012; 287: 7000-9.
    • (2012) J. Biol. Chem. , vol.287 , pp. 7000-7009
    • Auldridge, M.E.1    Satyshur, K.A.2    Anstrom, D.M.3    Forest, K.T.4
  • 22
    • 84868556564 scopus 로고    scopus 로고
    • Optical Control of Protein Activity by Fluorescent Protein Domains
    • Zhou XX, Chung HK, Lam AJ, Lin MZ. Optical Control of Protein Activity by Fluorescent Protein Domains. Science 2012; 338: 810-4.
    • (2012) Science , vol.338 , pp. 810-814
    • Zhou, X.X.1    Chung, H.K.2    Lam, A.J.3    Lin, M.Z.4
  • 24
    • 0344443180 scopus 로고    scopus 로고
    • FKF1 is essential for photoperiodic-specific light signalling in Arabidopsis
    • Imaizumi T, Tran HG, Swartz TE, Briggs WR, Kay SA. FKF1 is essential for photoperiodic-specific light signalling in Arabidopsis. Nature 2003; 426: 302-6.
    • (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
  • 25
    • 78650901467 scopus 로고    scopus 로고
    • Tripping the Light Fantastic: Blue-Light Photoreceptors as Examples of Environmentally Modulated Protein-Protein Interactions
    • Zoltowski BD, Gardner KH. Tripping the Light Fantastic: Blue-Light Photoreceptors as Examples of Environmentally Modulated Protein-Protein Interactions. Biochemistry 2011; 50: 4-16.
    • (2011) Biochemistry , vol.50 , pp. 4-16
    • Zoltowski, B.D.1    Gardner, K.H.2
  • 26
    • 49449118042 scopus 로고    scopus 로고
    • Light-activated DNA binding in a designed allosteric protein
    • Strickland D, Moffat K, Sosnick TR. Light-activated DNA binding in a designed allosteric protein. Proc. Natl. Acad. Sci. USA 2008; 105: 10709-14.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 10709-10714
    • Strickland, D.1    Moffat, K.2    Sosnick, T.R.3
  • 27
    • 78650885619 scopus 로고    scopus 로고
    • Engineered photoreceptors as novel optogenetic tools
    • Möglich A, Moffat K. Engineered photoreceptors as novel optogenetic tools. Photochem. Photobiol. Sci. 2010; 9: 1286-1300.
    • (2010) Photochem. Photobiol. Sci. , vol.9 , pp. 1286-1300
    • Möglich, A.1    Moffat, K.2
  • 28
    • 78650868371 scopus 로고    scopus 로고
    • Method of the Year 2010
    • Baker M. Method of the Year 2010. Nat. Methods 2011; 8: 1.
    • (2011) Nat. Methods , vol.8 , pp. 1
    • Baker, M.1
  • 29
  • 31
    • 79958003499 scopus 로고    scopus 로고
    • Computational protein design: engineering molecular diversity, nonnatural enzymes, nonbiological cofactor complexes, and membrane proteins
    • Saven JG. Computational protein design: engineering molecular diversity, nonnatural enzymes, nonbiological cofactor complexes, and membrane proteins. Curr. Opin. Chem. Biol. 2011; 15: 452-7.
    • (2011) Curr. Opin. Chem. Biol. , vol.15 , pp. 452-457
    • Saven, J.G.1
  • 32
    • 58549105950 scopus 로고    scopus 로고
    • Design and Signaling Mechanism of Light-regulated Histidine Kinases
    • Möglich A, Ayers RA, Moffat K. Design and Signaling Mechanism of Light-regulated Histidine Kinases. J. Mol. Biol. 2009; 385: 1433-44.
    • (2009) J. Mol. Biol. , vol.385 , pp. 1433-1444
    • Möglich, A.1    Ayers, R.A.2    Moffat, K.3
  • 34
    • 0033575370 scopus 로고    scopus 로고
    • Bacterial Photoreceptor with Similarity to Photoactive Yellow Protein and Plant Phytochromes
    • Jiang Z, Swem LR, Rushing BG, Devanathan S, Tollin G, Bauer CE. Bacterial Photoreceptor with Similarity to Photoactive Yellow Protein and Plant Phytochromes. Science 1999; 285: 406-9.
    • (1999) Science , vol.285 , pp. 406-409
    • Jiang, Z.1    Swem, L.R.2    Rushing, B.G.3    Devanathan, S.4    Tollin, G.5    Bauer, C.E.6
  • 35
    • 34250183058 scopus 로고    scopus 로고
    • Phototropin blue-light receptors
    • Christie JM. Phototropin blue-light receptors. Annu. Rev. Plant Biol. 2007; 58: 21-45.
    • (2007) Annu. Rev. Plant Biol. , vol.58 , pp. 21-45
    • Christie, J.M.1
  • 36
    • 77954383214 scopus 로고    scopus 로고
    • Addition at the molecular level: signal integration in designed Per-ARNT-Sim receptor proteins
    • Möglich A, Ayers RA, Moffat K. Addition at the molecular level: signal integration in designed Per-ARNT-Sim receptor proteins. J. Mol. Biol. 2010; 400: 477-86.
    • (2010) J. Mol. Biol. , vol.400 , pp. 477-486
    • Möglich, A.1    Ayers, R.A.2    Moffat, K.3
  • 37
    • 34248371291 scopus 로고    scopus 로고
    • The signaling helix: a common functional theme in diverse signaling proteins
    • Anantharaman V, Balaji S, Aravind L. The signaling helix: a common functional theme in diverse signaling proteins. Biol. Direct 2006; 1: 25.
    • (2006) Biol. Direct , vol.1 , pp. 25
    • Anantharaman, V.1    Balaji, S.2    Aravind, L.3
  • 38
    • 0037453510 scopus 로고    scopus 로고
    • Assembly of cell regulatory systems through protein interaction domains
    • Pawson T, Nash P. Assembly of cell regulatory systems through protein interaction domains. Science 2003; 300: 445-52.
    • (2003) Science , vol.300 , pp. 445-452
    • Pawson, T.1    Nash, P.2
  • 39
    • 33845542919 scopus 로고    scopus 로고
    • Elasticity of alpha-helical coiled coils
    • Wolgemuth CW, Sun SX. Elasticity of alpha-helical coiled coils. Phys. Rev. Lett. 2006; 97: 248101.
    • (2006) Phys. Rev. Lett. , vol.97 , pp. 248101
    • Wolgemuth, C.W.1    Sun, S.X.2
  • 40
    • 0037435618 scopus 로고    scopus 로고
    • The LOV domain family: photoresponsive signaling modules coupled to diverse output domains
    • Crosson S, Rajagopal S, Moffat K. The LOV domain family: photoresponsive signaling modules coupled to diverse output domains. Biochemistry 2003; 42: 2-10.
    • (2003) Biochemistry , vol.42 , pp. 2-10
    • Crosson, S.1    Rajagopal, S.2    Moffat, K.3
  • 43
  • 44
    • 70350070364 scopus 로고    scopus 로고
    • Spatiotemporal control of cell signalling using a lightswitchable protein interaction
    • Levskaya A, Weiner OD, Lim WA, Voigt CA. Spatiotemporal control of cell signalling using a lightswitchable protein interaction. Nature 2009; 461: 997-1001.
    • (2009) Nature , vol.461 , pp. 997-1001
    • Levskaya, A.1    Weiner, O.D.2    Lim, W.A.3    Voigt, C.A.4
  • 48
    • 85040557017 scopus 로고    scopus 로고
    • Unpublished results
    • Hahn K. Unpublished results.
    • Hahn, K.1
  • 50
    • 70350340730 scopus 로고    scopus 로고
    • Mechanism-based tuning of a LOV domain photoreceptor
    • Zoltowski BD, Vaccaro B, Crane BR. Mechanism-based tuning of a LOV domain photoreceptor. Nat. Chem. Biol. 2009; 5: 827-34.
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 827-834
    • Zoltowski, B.D.1    Vaccaro, B.2    Crane, B.R.3
  • 51
    • 57349088665 scopus 로고    scopus 로고
    • Photoexcited CRY2 interacts with CIB1 to regulate transcription and floral initiation in Arabidopsis
    • Liu H, Yu X, Li K, Klejnot J, Yang H, Lisiero D, Lin C. Photoexcited CRY2 interacts with CIB1 to regulate transcription and floral initiation in Arabidopsis. Science 2008; 322: 1535-9.
    • (2008) Science , vol.322 , pp. 1535-1539
    • Liu, H.1    Yu, X.2    Li, K.3    Klejnot, J.4    Yang, H.5    Lisiero, D.6    Lin, C.7
  • 52
    • 0032437591 scopus 로고    scopus 로고
    • Toward controlling gene expression at will: specific regulation of the erbB-2/HER-2 promoter by using polydactyl zinc finger proteins constructed from modular building blocks
    • Beerli RR, Segal DJ, Dreier B, Barbas CF 3rd. Toward controlling gene expression at will: specific regulation of the erbB-2/HER-2 promoter by using polydactyl zinc finger proteins constructed from modular building blocks. Proc. Natl. Acad. Sci. USA 1998; 95: 14628-33.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 14628-14633
    • Beerli, R.R.1    Segal, D.J.2    Dreier, B.3    Barbas, C.F.4
  • 53
    • 84864856835 scopus 로고    scopus 로고
    • Comprehensive interrogation of natural TALE DNA-binding modules and transcriptional repressor domains
    • Cong L, Zhou R, Kuo Y-C, Cunniff M, Zhang F. Comprehensive interrogation of natural TALE DNA-binding modules and transcriptional repressor domains. Nat. Commun. 2012; 3: 968.
    • (2012) Nat. Commun. , vol.3 , pp. 968
    • Cong, L.1    Zhou, R.2    Kuo, Y-C.3    Cunniff, M.4    Zhang, F.5
  • 54
    • 77952280117 scopus 로고    scopus 로고
    • The discovery of zinc fingers and their development for practical applications in gene regulation and genome manipulation
    • Klug A. The discovery of zinc fingers and their development for practical applications in gene regulation and genome manipulation. Q. Rev. Biophys. 2010; 43: 1-21.
    • (2010) Q. Rev. Biophys. , vol.43 , pp. 1-21
    • Klug, A.1
  • 56
    • 72149090954 scopus 로고    scopus 로고
    • A simple cipher governs DNA recognition by TAL effectors
    • Moscou MJ, Bogdanove AJ. A simple cipher governs DNA recognition by TAL effectors. Science 2009; 326: 1501.
    • (2009) Science , vol.326 , pp. 1501
    • Moscou, M.J.1    Bogdanove, A.J.2
  • 57
    • 85040611493 scopus 로고    scopus 로고
    • Unpublished results
    • Zhang F. Unpublished results.
    • Zhang, F.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.