메뉴 건너뛰기




Volumn 1, Issue 1, 2008, Pages 178-194

In4

Author keywords

[No Author keywords available]

Indexed keywords

ARABIDOPSIS;

EID: 47849128479     PISSN: 16742052     EISSN: 17529867     Source Type: Journal    
DOI: 10.1093/mp/ssm017     Document Type: Article
Times cited : (83)

References (64)
  • 1
    • 0033197801 scopus 로고    scopus 로고
    • Molecular genetic analysis of the drought-inducible linker histone variant in Arabidopsis thaliana
    • Ascenzi, R., and Gantt, J.S. (1999). Molecular genetic analysis of the drought-inducible linker histone variant in Arabidopsis thaliana. Plant Mol. Biol. 41, 159-169.
    • (1999) Plant Mol. Biol. , vol.41 , pp. 159-169
    • Ascenzi, R.1    Gantt, J.S.2
  • 2
    • 84889366079 scopus 로고    scopus 로고
    • Plant cryptochromes: Their genes, biochemistry, and physiological roles
    • W.R. Briggs and J.L. Spudich, eds (Weinheim: Wiley-VCH)
    • Batschauer, A. (2005). Plant cryptochromes: their genes, biochemistry, and physiological roles. In Handbook of Photosensory Receptors, W.R. Briggs and J.L. Spudich, eds (Weinheim: Wiley-VCH), pp. 2112-2146.
    • (2005) Handbook of Photosensory Receptors , pp. 2112-2146
    • Batschauer, A.1
  • 3
    • 0034752569 scopus 로고    scopus 로고
    • The PINOID protein kinase regulates organ development in Arabidopsis by enhancing polar auxin transport
    • Benjamins, R., Quint, A., Weijers, D., Hooykaas, P., and Offringa, R. (2001). The PINOID protein kinase regulates organ development in Arabidopsis by enhancing polar auxin transport. Development 128, 4057-4067.
    • (2001) Development , vol.128 , pp. 4057-4067
    • Benjamins, R.1    Quint, A.2    Weijers, D.3    Hooykaas, P.4    Offringa, R.5
  • 4
    • 0141503468 scopus 로고    scopus 로고
    • Growth signalling pathways in Arabidopsis and the AGC protein kinases
    • Bogre, L., Okresz, L., Henriques, R., and Anthony, R.G. (2003). Growth signalling pathways in Arabidopsis and the AGC protein kinases. Trends Plant Sci. 8, 424-431.
    • (2003) Trends Plant Sci. , vol.8 , pp. 424-431
    • Bogre, L.1    Okresz, L.2    Henriques, R.3    Anthony, R.G.4
  • 5
    • 34547911296 scopus 로고    scopus 로고
    • Flavin-based photoreceptors in plants
    • Silvia, E., and Edwards, A.M., eds (Cambridge: RCS Publishing)
    • Briggs, W.R. (2006). Flavin-based photoreceptors in plants. In Flavins: Photochemistry and Photobiology, Silvia, E., and Edwards, A.M., eds (Cambridge: RCS Publishing), pp. 183-216.
    • (2006) Flavins: Photochemistry and Photobiology , pp. 183-216
    • Briggs, W.R.1
  • 6
    • 0034980776 scopus 로고    scopus 로고
    • The phototropin family of photoreceptors
    • Briggs, W.R., et al. (2001). The phototropin family of photoreceptors. Plant Cell 13, 993-997.
    • (2001) Plant Cell , vol.13 , pp. 993-997
    • Briggs, W.R.1
  • 7
    • 33846377245 scopus 로고    scopus 로고
    • Physiological roles of the light, oxygen, or voltage domains of phototropin 1 and phototropin 2 in Arabidopsis
    • Cho, H.Y., Tseng, T.S., Kaiserli, E., Sullivan, S., Christie, J.M., and Briggs, W.R. (2007). Physiological roles of the light, oxygen, or voltage domains of phototropin 1 and phototropin 2 in Arabidopsis. Plant Physiol 143, 517-529.
    • (2007) Plant Physiol , vol.143 , pp. 517-529
    • Cho, H.Y.1    Tseng, T.S.2    Kaiserli, E.3    Sullivan, S.4    Christie, J.M.5    Briggs, W.R.6
  • 8
    • 0034681263 scopus 로고    scopus 로고
    • Regulation of auxin response by the protein kinase PINOID
    • Christensen, S.K., Dagenais, N., Chory, J., and Weigel, D. (2000). Regulation of auxin response by the protein kinase PINOID. Cell 100, 469-478.
    • (2000) Cell , vol.100 , pp. 469-478
    • Christensen, S.K.1    Dagenais, N.2    Chory, J.3    Weigel, D.4
  • 9
    • 34250183058 scopus 로고    scopus 로고
    • Phototropin blue-light receptors
    • Christie, J.M. (2007). Phototropin blue-light receptors. Annu. Rev. Plant Biol. 58, 21-45.
    • (2007) Annu. Rev. Plant Biol. , vol.58 , pp. 21-45
    • Christie, J.M.1
  • 10
    • 0036776294 scopus 로고    scopus 로고
    • Phototropin LOV domains exhibit distinct roles in regulating photoreceptor function
    • Christie, J.M., Swartz, T.E., Bogomolni, R.A., and Briggs, W.R. (2002). Phototropin LOV domains exhibit distinct roles in regulating photoreceptor function. Plant J 32, 205-219.
    • (2002) Plant J , vol.32 , pp. 205-219
    • Christie, J.M.1    Swartz, T.E.2    Bogomolni, R.A.3    Briggs, W.R.4
  • 11
    • 0033587744 scopus 로고    scopus 로고
    • LOV (light, oxygen, or voltage) domains of the blue-light photoreceptor phototropin (nph1): Binding sites for the chromophore flavin mononucleotide
    • Christie, J.M., Salomon, M., Nozue, K., Wada, M., and Briggs, W.R. (1999). LOV (light, oxygen, or voltage) domains of the blue-light photoreceptor phototropin (nph1): binding sites for the chromophore flavin mononucleotide. Proc. Natl Acad. Sci. U S A 96, 8779-8783.
    • (1999) Proc. Natl Acad. Sci. U S A , vol.96 , pp. 8779-8783
    • Christie, J.M.1    Salomon, M.2    Nozue, K.3    Wada, M.4    Briggs, W.R.5
  • 14
    • 0034724178 scopus 로고    scopus 로고
    • Random GFP:cDNA fusions enable visualization of subcellular structures in cells of Arabidopsis at a high frequency
    • Cutler, S.R., Ehrhardt, D.W., Griffitts, J.S., and Somerville, C.R. (2000). Random GFP:cDNA fusions enable visualization of subcellular structures in cells of Arabidopsis at a high frequency. Proc. Natl Acad. Sci. USA. 97, 3718-3723.
    • (2000) Proc. Natl Acad. Sci. USA. , vol.97 , pp. 3718-3723
    • Cutler, S.R.1    Ehrhardt, D.W.2    Griffitts, J.S.3    Somerville, C.R.4
  • 15
    • 0037008528 scopus 로고    scopus 로고
    • White Collar-1, a circadian blue light photoreceptor, binding to the frequency promoter
    • Froehlich, A.C., Liu, Y., Loros, J.J., and Dunlap, J.C. (2002). White Collar-1, a circadian blue light photoreceptor, binding to the frequency promoter. Science 297, 815-819.
    • (2002) Science , vol.297 , pp. 815-819
    • Froehlich, A.C.1    Liu, Y.2    Loros, J.J.3    Dunlap, J.C.4
  • 16
    • 0141707094 scopus 로고    scopus 로고
    • Structural basis of a phototropin light switch
    • Harper, S.M., Neil, L.C., and Gardner, K.H. (2003). Structural basis of a phototropin light switch. Science 301, 1541-1544.
    • (2003) Science , vol.301 , pp. 1541-1544
    • Harper, S.M.1    Neil, L.C.2    Gardner, K.H.3
  • 17
    • 11144344967 scopus 로고    scopus 로고
    • Disruption of the LOV-J alpha helix interaction activates phototropin kinase activity
    • Harper, S.M., Christie, J.M., and Gardner, K.H. (2004). Disruption of the LOV-J alpha helix interaction activates phototropin kinase activity. Biochemistry 43, 16184-16192.
    • (2004) Biochemistry , vol.43 , pp. 16184-16192
    • Harper, S.M.1    Christie, J.M.2    Gardner, K.H.3
  • 18
    • 0037008508 scopus 로고    scopus 로고
    • White collar-1, a DNA binding transcription factor and a light sensor
    • He, Q., Cheng, P., Yang, Y., Wang, L., Gardner, K.H., and Liu, Y. (2002). White collar-1, a DNA binding transcription factor and a light sensor. Science 297, 840-843.
    • (2002) Science , vol.297 , pp. 840-843
    • He, Q.1    Cheng, P.2    Yang, Y.3    Wang, L.4    Gardner, K.H.5    Liu, Y.6
  • 19
    • 0031470701 scopus 로고    scopus 로고
    • Arabidopsis NPH1: A protein kinase with a putative redox-sensing domain
    • Huala, E., Oeller, P.W., Liscum, E., Han, I.S., Larsen, E., and Briggs, W.R. (1997). Arabidopsis NPH1: a protein kinase with a putative redox-sensing domain. Science 278, 2120-2123.
    • (1997) Science , vol.278 , pp. 2120-2123
    • Huala, E.1    Oeller, P.W.2    Liscum, E.3    Han, I.S.4    Larsen, E.5    Briggs, W.R.6
  • 20
    • 1842712611 scopus 로고    scopus 로고
    • RPT2 is a signal transducer involved in phototropic response and stomatal opening by association with phototropin 1 in Arabidopsis thaliana
    • Inada, S., Ohgishi, M., Mayama, T., Okada, K., and Sakai, T. (2004). RPT2 is a signal transducer involved in phototropic response and stomatal opening by association with phototropin 1 in Arabidopsis thaliana. Plant Cell 16, 887-896.
    • (2004) Plant Cell , vol.16 , pp. 887-896
    • Inada, S.1    Ohgishi, M.2    Mayama, T.3    Okada, K.4    Sakai, T.5
  • 22
    • 34250345266 scopus 로고    scopus 로고
    • Mutational analysis of phototropin 1 provides insights into the mechanism underlying LOV2 signal transmission
    • Jones, M.A., Feeney, K.A., Kelly, S.M., and Christie, J.M. (2007). Mutational analysis of phototropin 1 provides insights into the mechanism underlying LOV2 signal transmission. J. Biol. Chem. 282, 6405-6414.
    • (2007) J. Biol. Chem. , vol.282 , pp. 6405-6414
    • Jones, M.A.1    Feeney, K.A.2    Kelly, S.M.3    Christie, J.M.4
  • 23
    • 0033953240 scopus 로고    scopus 로고
    • Blue light-induced chloroplast relocation in Arabidopsis thaliana as analyzed by microbeam irradiation
    • Kagawa, T., and Wada, M. (2000). Blue light-induced chloroplast relocation in Arabidopsis thaliana as analyzed by microbeam irradiation. Plant Cell Physiol. 41, 84-93.
    • (2000) Plant Cell Physiol. , vol.41 , pp. 84-93
    • Kagawa, T.1    Wada, M.2
  • 24
    • 2342541694 scopus 로고    scopus 로고
    • Function analysis of phototropin2 using fern mutants deficient in blue light-induced chloroplast avoidance movement
    • Kagawa, T., Kasahara, M., Abe, T., Yoshida, S., andWada, M. (2004). Function analysis of phototropin2 using fern mutants deficient in blue light-induced chloroplast avoidance movement. Plant Cell Physiol. 45, 416-426.
    • (2004) Plant Cell Physiol. , vol.45 , pp. 416-426
    • Kagawa, T.1    Kasahara, M.2    Abe, T.3    Yoshida, S.4    Wada, M.5
  • 25
    • 0035896393 scopus 로고    scopus 로고
    • Arabidopsis NPL1: A phototropin homolog controlling the chloroplast high-light avoidance response
    • Kagawa, T., Sakai, T., Suetsugu, N., Oikawa, K., Ishiguro, S., Kato, T., Tabata, S., Okada, K., and Wada, M. (2001). Arabidopsis NPL1: a phototropin homolog controlling the chloroplast high-light avoidance response. Science 291, 2138-2141.
    • (2001) Science , vol.291 , pp. 2138-2141
    • Kagawa, T.1    Sakai, T.2    Suetsugu, N.3    Oikawa, K.4    Ishiguro, S.5    Kato, T.6    Tabata, S.7    Okada, K.8    Wada, M.9
  • 26
    • 35348841586 scopus 로고    scopus 로고
    • UV-B promotes rapid nuclear translocation of the Arabidopsis UV-B specific signaling component UVR8 and activates its function in the nucleus
    • Kaiserli, E., and Jenkins, G.I. (2007). UV-B promotes rapid nuclear translocation of the Arabidopsis UV-B specific signaling component UVR8 and activates its function in the nucleus. Plant Cell 19, 2662-2673.
    • (2007) Plant Cell , vol.19 , pp. 2662-2673
    • Kaiserli, E.1    Jenkins, G.I.2
  • 27
    • 0035983657 scopus 로고    scopus 로고
    • Photochemical properties of the flavin mononucleotide-binding domains of the phototropins from Arabidopsis, rice, and Chlamydomonas reinhardtii
    • Kasahara, M., et al. (2002). Photochemical properties of the flavin mononucleotide-binding domains of the phototropins from Arabidopsis, rice, and Chlamydomonas reinhardtii. Plant Physiol. 129, 762-773.
    • (2002) Plant Physiol. , vol.129 , pp. 762-773
    • Kasahara, M.1
  • 28
    • 35348856969 scopus 로고    scopus 로고
    • Targeted degradation of PSEUDO-RESPONSE REGULATOR5 by an SCFZTL complex regulates clock function and photomorphogenesis in Arabidopsis thaliana
    • Kiba, T., Henriques, R., Sakakibara, H., and Chua, N.H. (2007). Targeted degradation of PSEUDO-RESPONSE REGULATOR5 by an SCFZTL complex regulates clock function and photomorphogenesis in Arabidopsis thaliana. Plant Cell 19, 2516-2530.
    • (2007) Plant Cell , vol.19 , pp. 2516-2530
    • Kiba, T.1    Henriques, R.2    Sakakibara, H.3    Chua, N.H.4
  • 29
    • 34548813657 scopus 로고    scopus 로고
    • ZEITLUPE is a circadian photoreceptor stabilized by GIGANTEA in blue light
    • Kim, W.Y., et al. (2007). ZEITLUPE is a circadian photoreceptor stabilized by GIGANTEA in blue light. Nature 449, 356-360.
    • (2007) Nature , vol.449 , pp. 356-360
    • Kim, W.Y.1
  • 30
    • 0036859483 scopus 로고    scopus 로고
    • Biochemical evidence for the requirement of 14-3-3 protein binding in activation of the guard-cell plasma membrane H+-ATPase by blue light
    • Kinoshita, T., and Shimazaki, K. (2002). Biochemical evidence for the requirement of 14-3-3 protein binding in activation of the guard-cell plasma membrane H+-ATPase by blue light. Plant Cell Physiol. 43, 1359-1365.
    • (2002) Plant Cell Physiol. , vol.43 , pp. 1359-1365
    • Kinoshita, T.1    Shimazaki, K.2
  • 31
    • 0035818967 scopus 로고    scopus 로고
    • Phot1 and phot2 mediate blue light regulation of stomatal opening
    • Kinoshita, T., Doi, M., Suetsugu, N., Kagawa, T., Wada, M., and Shimazaki, K. (2001). Phot1 and phot2 mediate blue light regulation of stomatal opening. Nature 414, 656-660.
    • (2001) Nature , vol.414 , pp. 656-660
    • Kinoshita, T.1    Doi, M.2    Suetsugu, N.3    Kagawa, T.4    Wada, M.5    Shimazaki, K.6
  • 32
    • 0345791404 scopus 로고    scopus 로고
    • Blue-light-and phosphorylation-dependent binding of a 14-3-3 protein to phototropins in stomatal guard cells of broad bean
    • Kinoshita, T., Emi, T., Tominaga, M., Sakamoto, K., Shigenaga, A., Doi, M., and Shimazaki, K. (2003). Blue-light-and phosphorylation-dependent binding of a 14-3-3 protein to phototropins in stomatal guard cells of broad bean. Plant Physiol. 133, 1453-1463.
    • (2003) Plant Physiol. , vol.133 , pp. 1453-1463
    • Kinoshita, T.1    Emi, T.2    Tominaga, M.3    Sakamoto, K.4    Shigenaga, A.5    Doi, M.6    Shimazaki, K.7
  • 33
    • 1642380220 scopus 로고    scopus 로고
    • Tissue-specific and subcellular localization of phototropin determined by immunoblotting
    • Knieb, E., Salomon, M., and Rudiger, W. (2004). Tissue-specific and subcellular localization of phototropin determined by immunoblotting. Planta 218, 843-851.
    • (2004) Planta , vol.218 , pp. 843-851
    • Knieb, E.1    Salomon, M.2    Rudiger, W.3
  • 34
    • 14744270377 scopus 로고    scopus 로고
    • Autophosphorylation, electrophoretic mobility and immunoreaction of oat phototropin 1 under UV and blue light
    • Knieb, E., Salomon, M., and Rudiger, W. (2005). Autophosphorylation, electrophoretic mobility and immunoreaction of oat phototropin 1 under UV and blue light. Photochem. Photobiol. 81, 177-182.
    • (2005) Photochem. Photobiol. , vol.81 , pp. 177-182
    • Knieb, E.1    Salomon, M.2    Rudiger, W.3
  • 36
    • 34548118780 scopus 로고    scopus 로고
    • The C-terminal kinase fragment of Arabidopsis phototropin 2 triggers constitutive phototropin responses
    • Kong, S.G., Kinoshita, T., Shimazaki, K., Mochizuki, N., Suzuki, T., and Nagatani, A. (2007). The C-terminal kinase fragment of Arabidopsis phototropin 2 triggers constitutive phototropin responses. Plant J. 51, 862-873.
    • (2007) Plant J. , vol.51 , pp. 862-873
    • Kong, S.G.1    Kinoshita, T.2    Shimazaki, K.3    Mochizuki, N.4    Suzuki, T.5    Nagatani, A.6
  • 38
    • 13444263450 scopus 로고    scopus 로고
    • Deciphering the plant phosphoproteome: Tools and strategies for a challenging task
    • Laugesen, S., Bergoin, A., and Rossignol, M. (2004). Deciphering the plant phosphoproteome: tools and strategies for a challenging task. Plant Physiol. Biochem. 42, 929-936.
    • (2004) Plant Physiol. Biochem. , vol.42 , pp. 929-936
    • Laugesen, S.1    Bergoin, A.2    Rossignol, M.3
  • 39
    • 0029278701 scopus 로고
    • Mutations in the NPH1 locus of Arabidopsis disrupt the perception of phototropic stimuli
    • Liscum, E., and Briggs, W.R. (1995). Mutations in the NPH1 locus of Arabidopsis disrupt the perception of phototropic stimuli. Plant Cell 7, 473-485.
    • (1995) Plant Cell , vol.7 , pp. 473-485
    • Liscum, E.1    Briggs, W.R.2
  • 40
    • 24744445152 scopus 로고    scopus 로고
    • A role for Arabidopsis cryptochromes and COP1 in the regulation of stomatal opening
    • Mao, J., Zhang, Y.C., Sang, Y., Li, Q.H., and Yang, H.Q. (2005). A role for Arabidopsis cryptochromes and COP1 in the regulation of stomatal opening. Proc. Natl Acad. Sci. U S A 102, 12270-12275.
    • (2005) Proc. Natl Acad. Sci. U S A , vol.102 , pp. 12270-12275
    • Mao, J.1    Zhang, Y.C.2    Sang, Y.3    Li, Q.H.4    Yang, H.Q.5
  • 41
    • 24944553332 scopus 로고    scopus 로고
    • Blue light-regulated molecular switch of Ser/Thr kinase in phototropin
    • Matsuoka, D., and Tokutomi, S. (2005). Blue light-regulated molecular switch of Ser/Thr kinase in phototropin. Proc. Natl Acad. Sci. U S A 102, 13337-13342.
    • (2005) Proc. Natl Acad. Sci. U S A , vol.102 , pp. 13337-13342
    • Matsuoka, D.1    Tokutomi, S.2
  • 43
    • 1442281536 scopus 로고    scopus 로고
    • Functional analysis of each blue light receptor, cry1, cry2, phot1, and phot2, by using combinatorial multiple mutants in Arabidopsis
    • Ohgishi, M., Saji, K., Okada, K., and Sakai, T. (2004). Functional analysis of each blue light receptor, cry1, cry2, phot1, and phot2, by using combinatorial multiple mutants in Arabidopsis. Proc. Natl Acad. Sci. U S A 101, 2223-2228.
    • (2004) Proc. Natl Acad. Sci. U S A , vol.101 , pp. 2223-2228
    • Ohgishi, M.1    Saji, K.2    Okada, K.3    Sakai, T.4
  • 45
    • 0000032477 scopus 로고
    • Blue light-induced phosphorylation of a plasma membrane-associated protein in Zea mays L
    • Palmer, J.M., Short, T.W., Gallagher, S., and Briggs, W.R. (1993). Blue light-induced phosphorylation of a plasma membrane-associated protein in Zea mays L. Plant Physiol. 102, 1211-1218.
    • (1993) Plant Physiol. , vol.102 , pp. 1211-1218
    • Palmer, J.M.1    Short, T.W.2    Gallagher, S.3    Briggs, W.R.4
  • 47
    • 0036671887 scopus 로고    scopus 로고
    • Cellular and subcellular localization of phototropin 1
    • Sakamoto, K., and Briggs, W.R. (2002). Cellular and subcellular localization of phototropin 1. Plant Cell 14, 1723-1735.
    • (2002) Plant Cell , vol.14 , pp. 1723-1735
    • Sakamoto, K.1    Briggs, W.R.2
  • 48
    • 4143081643 scopus 로고    scopus 로고
    • Dimerization of the plant photoreceptor phototropin is probably mediated by the LOV1 domain
    • Salomon, M., Lempert, U., and Rudiger, W. (2004). Dimerization of the plant photoreceptor phototropin is probably mediated by the LOV1 domain. FEBS Lett. 572, 8-10.
    • (2004) FEBS Lett. , vol.572 , pp. 8-10
    • Salomon, M.1    Lempert, U.2    Rudiger, W.3
  • 49
    • 0037446727 scopus 로고    scopus 로고
    • Mapping of low-and high-fluence autophosphorylation sites in phototropin 1
    • Salomon, M., Knieb, E., von Zeppelin, T., and Rudiger, W. (2003). Mapping of low-and high-fluence autophosphorylation sites in phototropin 1. Biochemistry 42, 4217-4225.
    • (2003) Biochemistry , vol.42 , pp. 4217-4225
    • Salomon, M.1    Knieb, E.2    Von Zeppelin, T.3    Rudiger, W.4
  • 50
    • 0034622586 scopus 로고    scopus 로고
    • Photochemical and mutational analysis of the FMNbinding domains of the plant blue light receptor, phototropin
    • Salomon, M., Christie, J.M., Knieb, E., Lempert, U., and Briggs, W.R. (2000). Photochemical and mutational analysis of the FMNbinding domains of the plant blue light receptor, phototropin. Biochemistry 39, 9401-9410.
    • (2000) Biochemistry , vol.39 , pp. 9401-9410
    • Salomon, M.1    Christie, J.M.2    Knieb, E.3    Lempert, U.4    Briggs, W.R.5
  • 51
    • 35348910170 scopus 로고    scopus 로고
    • FKF1 and GIGANTEA complex formation is required for day-length measurement in Arabidopsis
    • Sawa, M., Nusinow, D.A., Kay, S.A., and Imaizumi, T. (2007). FKF1 and GIGANTEA complex formation is required for day-length measurement in Arabidopsis. Science 318, 261-265.
    • (2007) Science , vol.318 , pp. 261-265
    • Sawa, M.1    Nusinow, D.A.2    Kay, S.A.3    Imaizumi, T.4
  • 53
    • 0028117990 scopus 로고
    • Blue light induces phosphorylation at seryl residues on a pea (Pisum sativum L.) plasma membrane protein
    • Short, T.W., Porst, M., Palmer, J., Fernbach, E., and Briggs, W.R. (1994). Blue light induces phosphorylation at seryl residues on a pea (Pisum sativum L.) plasma membrane protein. Plant Physiol. 104, 1317-1324.
    • (1994) Plant Physiol. , vol.104 , pp. 1317-1324
    • Short, T.W.1    Porst, M.2    Palmer, J.3    Fernbach, E.4    Briggs, W.R.5
  • 54
    • 31644439146 scopus 로고    scopus 로고
    • Phosphorylation analysis by mass spectrometry: Myths, facts, and the consequences for qualitative and quantitative measurements
    • Steen, H., Jebanathirajah, J.A., Rush, J., Morrice, N., and Kirschner, M.W. (2006). Phosphorylation analysis by mass spectrometry: myths, facts, and the consequences for qualitative and quantitative measurements. Mol. Cell Proteomics 5, 172-181.
    • (2006) Mol. Cell Proteomics , vol.5 , pp. 172-181
    • Steen, H.1    Jebanathirajah, J.A.2    Rush, J.3    Morrice, N.4    Kirschner, M.W.5
  • 55
    • 33644746720 scopus 로고    scopus 로고
    • An auxilinlike J-domain protein, JAC1, regulates phototropin-mediated chloroplast movement in Arabidopsis
    • Suetsugu, N., Kagawa, T., and Wada, M. (2005). An auxilinlike J-domain protein, JAC1, regulates phototropin-mediated chloroplast movement in Arabidopsis. Plant Physiol. 139, 151-162.
    • (2005) Plant Physiol. , vol.139 , pp. 151-162
    • Suetsugu, N.1    Kagawa, T.2    Wada, M.3
  • 56
    • 23944471774 scopus 로고    scopus 로고
    • Phototropins promote plant growth in response to blue light in low light environments
    • Takemiya, A., Inoue, S., Doi, M., Kinoshita, T., and Shimazaki, K. (2005). Phototropins promote plant growth in response to blue light in low light environments. Plant Cell 17, 1120-1127.
    • (2005) Plant Cell , vol.17 , pp. 1120-1127
    • Takemiya, A.1    Inoue, S.2    Doi, M.3    Kinoshita, T.4    Shimazaki, K.5
  • 57
    • 0032990441 scopus 로고    scopus 로고
    • PAS domains: Internal sensors of oxygen, redox potential, and light
    • Taylor, B.L., and Zhulin, I.B. (1999). PAS domains: internal sensors of oxygen, redox potential, and light. Microbiol. Mol. Biol. Rev. 63, 479-506.
    • (1999) Microbiol. Mol. Biol. Rev. , vol.63 , pp. 479-506
    • Taylor, B.L.1    Zhulin, I.B.2
  • 58
    • 34547915890 scopus 로고    scopus 로고
    • Phototropins and Neochrome1 mediate nuclear movement in the fern Adiantum capillus-veneris
    • Tsuboi, H., Suetsugu, N., Kawai-Toyooka, H., and Wada, M. (2007). Phototropins and Neochrome1 mediate nuclear movement in the fern Adiantum capillus-veneris. Plant Cell Physiol. 48, 892-896.
    • (2007) Plant Cell Physiol. , vol.48 , pp. 892-896
    • Tsuboi, H.1    Suetsugu, N.2    Kawai-Toyooka, H.3    Wada, M.4
  • 59
    • 34250878954 scopus 로고    scopus 로고
    • Mechanisms of specificity in protein phosphorylation
    • Ubersax, J.A., and Ferrell, J.E., Jr (2007). Mechanisms of specificity in protein phosphorylation. Nat. Rev. Mol. Cell Biol. 8, 530-541.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 530-541
    • Ubersax, J.A.1    Ferrell Jr., J.E.2
  • 60
    • 0035051907 scopus 로고    scopus 로고
    • Interactions within a network of phytochrome, cryptochrome and UV-B phototransduction pathways regulate chalcone synthase gene expression in Arabidopsis leaf tissue
    • Wade, H.K., Bibikova, T.N., Valentine, W.J., and Jenkins, G.I. (2001). Interactions within a network of phytochrome, cryptochrome and UV-B phototransduction pathways regulate chalcone synthase gene expression in Arabidopsis leaf tissue. Plant J. 25, 675-685.
    • (2001) Plant J. , vol.25 , pp. 675-685
    • Wade, H.K.1    Bibikova, T.N.2    Valentine, W.J.3    Jenkins, G.I.4
  • 61
    • 33644674733 scopus 로고    scopus 로고
    • Automated identification and quantification of protein phosphorylation sites by LC/MS on a hybrid triple quadrupole linear ion trap mass spectrometer
    • Williamson, B.L., Marchese, J., and Morrice, N.A. (2006). Automated identification and quantification of protein phosphorylation sites by LC/MS on a hybrid triple quadrupole linear ion trap mass spectrometer. Mol. Cell Proteomics 5, 337-346.
    • (2006) Mol. Cell Proteomics , vol.5 , pp. 337-346
    • Williamson, B.L.1    Marchese, J.2    Morrice, N.A.3
  • 62
    • 33646580103 scopus 로고    scopus 로고
    • Phosphorylation and activation of PINOID by the phospholipid signaling kinase 3-phosphoinositide-dependent protein kinase 1 (PDK1) in Arabidopsis
    • Zegzouti, H., Anthony, R.G., Jahchan, N., Bogre, L., and Christensen, S.K. (2006a). Phosphorylation and activation of PINOID by the phospholipid signaling kinase 3-phosphoinositide-dependent protein kinase 1 (PDK1) in Arabidopsis. Proc. Natl Acad. Sci. U S A 103, 6404-6409.
    • (2006) Proc. Natl Acad. Sci. U S A , vol.103 , pp. 6404-6409
    • Zegzouti, H.1    Anthony, R.G.2    Jahchan, N.3    Bogre, L.4    Christensen, S.K.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.