SEARCH

SEARCH BY CITATION

  • 1
    “In vitro attachment of bilins to apophycocyanin. I. Specific covalent adduct formation at cysteinyl residues involved in phycocyanobilin binding in C-phycocyanin”: D. M. Arciero, D. A. Bryant, A. N. Glazer, J. Biol. Chem. 1988, 263, 1834318349.
  • 2
    “In vitro attachment of bilins to apophycocyanin. II. Determination of the structures of tryptic bilin peptides derived from the phycocyanobilin adduct”: D. M. Arciero, J. L. Dallas, A. N. Glazer, J. Biol. Chem. 1988, 263, 1835018357.
  • 3
    “In vitro attachment of bilins to apophycocyanin. III. Properties of the phycoerythrobilin adduct”: D. M. Arciero, J. L. Dallas, A. N. Glazer, J. Biol. Chem. 1988, 263, 1835818363.
  • 4
    “Oligomeric structure, enzyme kinetics, and substrate specificity of the phycocyanin α subunit phycocyanobilin lyase”: C. D. Fairchild, A. N. Glazer, J. Biol. Chem. 1994, 269, 86868694.
  • 5
    “A cyclic-3′,5′-adenosine monophosphate dependent protein kinase from the adrenal cortex: comparison with a cyclic AMP binding protein”: G. N. Gill, L. D. Garren, Biochem. Biophys. Res. Commun. 1970, 39, 335343.
  • 6
    “A cyclic 3′,5′-AMP-stimulated protein kinase from cardiac muscle”: M. A. Brostrom, E. M. Reimann, D. A. Walsh, E. G. Krebs, Adv. Enzyme Regul. 1970, 8, 191203.
  • 7
    “Mechanism of activation by adenosine 3′:5′-cyclic monophosphate of a protein phosphokinase from rabbit reticulocytes”: M. Tao, M. L. Salas, F. Lipmann, Proc. Natl. Acad. Sci. USA 1970, 67, 408414.
  • 8
    “Expression of the type I regulatory subunit of cAMP-dependent protein kinase in Escherichia coli”: L. D. Saraswat, M. Filutowicz, S. S. Taylor, J. Biol. Chem. 1986, 261, 1109111096.
  • 9
    “Expression of the catalytic subunit of cAMP-dependent protein kinase in Escherichia coli”: L. W. Slice, S. S. Taylor, J. Biol. Chem. 1989, 264, 2094020946.
  • 10
    “Fluorescence ratio imaging of cyclic AMP in single cells”: S. R. Adams, A. T. Harootunian, Y. J. Buechler, S. S. Taylor, R. Y. Tsien, Nature 1991, 349, 694697.
  • 11
    S. R. Adams, B. J. Bacskai, S. S. Taylor, R. Y. Tsien, Fluorescent Probes for Biological Activity of Living Cells—A Practical Guide (Ed.: W. T. Mason), Academic Press, New York, 1993, pp. 133149.
  • 12
    “Single-cell analysis of cyclic AMP response to parathyroid hormone in osteoblastic cells”: R. Civitelli, B. J. Bacskai, M. P. Mahaut-Smith, S. R. Adams, L. V. Avioli, R. Y. Tsien, J. Bone Miner. Res. 1994, 9, 14071417.
  • 13
    “Spatio-temporal dynamics of cAMP signals in an intact neural circuit”: C. M. Hempel, P. Vincent, S. R. Adams, R. Y. Tsien, A. I. Selverston, Nature 1996, 384, 166169.
  • 14
    “Intracellular cyclic AMP not Ca2+ determines the direction of vesicle movement in melanophores: direct measurements by fluorescence ratio imaging”: P. J. Sammak, S. R. Adams, A. T. Harootunian, M. Schliwa, R. Y. Tsien, J. Cell Biol. 1992, 117, 5772.
  • 15
    “Spatially resolved dynamics of cAMP and protein kinase A subunits in Aplysia sensory neurons”: B. J. Bacskai, B. Hochner, M. Mahaut-Smith, S. R. Adams, B. K. Kaang, E. R. Kandel, R. Y. Tsien, Science 1993, 260, 222226.
  • 16
    “Measurement of Ca2+ concentrations in living cells”: J. R. Blinks, W. G. Wier, P. Hess, F. G. Prendergast, Prog. Biophys. Mol. Biol. 1982, 40, 1114.
  • 17
    “Primary structure of the Aequorea victoria green-fluorescent protein”: D. C. Prasher, V. K. Eckenrode, W. W. Ward, F. G. Prendergast, M. J. Cormier, Gene 1992, 111, 229233.
  • 18
    “Expression, purification, and properties of the plasma membrane Ca2+ pump and of its N-terminally truncated 105 kDa fragment”: R. Heim, T. Iwata, E. Zvaritch, H. P. Adamo, B. Rutishauser, E. E. Strehler, D. Guerini, E. Carafoli, J. Biol. Chem. 1992, 267, 2447624484.
  • 19
    “Microdiversity of human-plasma-membrane calcium-pump isoform 2 generated by alternative RNA splicing in the N-terminal coding region”: R. Heim, M. Hug, T. Iwata, E. E. Strehler, E. Carafoli, Eur. J. Biochem. 1992, 205, 333340.
  • 20
    “Wavelength mutations and post-translational autooxidation of green fluorescent protein”: R. Heim, D. C. Prasher, R. Y. Tsien, Proc. Natl. Acad. Sci. USA 1994, 91, 1250112504.
  • 21
    “Engineering green fluorescent protein for improved brightness, longer wavelengths and fluorescence energy transfer”: R. Heim, R. Y. Tsien, Curr. Biol. 1996, 6, 178182.
  • 22
    “Chemical structure of the hexapeptide chromophore of the Aequorea green-fluorescent protein”: C. W. Cody, D. C. Prasher, W. M. Westler, F. G. Prendergast, W. W. Ward, Biochemistry 1993, 32, 12121218.
  • 23
    “Reaction progress of chromophore biogenesis in green fluorescent protein”: L. Zhang, H. N. Patel, J. W. Lappe, R. M. Wachter, J. Am. Chem. Soc. 2006, 128, 47664772.
  • 24
    “Structure of the chromophore of Aequorea green fluorescent protein”: O. Shimomura, FEBS Lett. 1979, 104, 220222.
  • 25
    “Improved green fluorescence”: R. Heim, A. B. Cubitt, R. Y. Tsien, Nature 1995, 373, 663664.
  • 26
    “Heterologous HIS3 marker and GFP reporter modules for PCR-targeting in Saccharomyces cerevisiae”: A. Wach, A. Brachat, C. Alberti-Segui, C. Rebischung, P. Philippsen, Yeast 1997, 13, 10651075.
  • 27
    “Red-shifted excitation mutants of the green fluorescent protein”: S. Delagrave, R. E. Hawtin, C. M. Silva, M. M. Yang, D. C. Youvan, Bio/Technology 1995, 13, 151154.
  • 28
    “Fluorescence resonance energy transfer between blue-emitting and red-shifted excitation derivatives of the green fluorescent protein”: R. D. Mitra, C. M. Silva, D. C. Youvan, Gene 1996, 173, 1317.
  • 29
    “FACS-optimized mutants of the green fluorescent protein (GFP)”: B. P. Cormack, R. H. Valdivia, S. Falkow, Gene 1996, 173, 3338.
  • 30
    “X-ray diffraction and time-resolved fluorescence analyses of Aequorea green fluorescent protein crystals”: M. A. Perozzo, K. B. Ward, R. B. Thompson, W. W. Ward, J. Biol. Chem. 1988, 263, 77137716.
  • 31
    “Crystal structure of the Aequorea victoria green fluorescent protein”: M. Ormö, A. B. Cubitt, K. Kallio, L. A. Gross, R. Y. Tsien, S. J. Remington, Science 1996, 273, 13921395.
  • 32
    “The molecular structure of green fluorescent protein”: F. Yang, L. G. Moss, G. N. Phillips, Jr., Nat. Biotechnol. 1996, 14, 12461251.
  • 33
    “Structural basis for dual excitation and photoisomerization of the Aequorea victoria green fluorescent protein”: K. Brejc, T. K. Sixma, P. A. Kitts, S. R. Kain, R. Y. Tsien, M. Ormö, S. J. Remington, Proc. Natl. Acad. Sci. USA 1997, 94, 23062311.
  • 34
    “Primary structure and functional expression of the inositol 1,4,5-trisphosphate-binding protein P400”: T. Furuichi, S. Yoshikawa, A. Miyawaki, K. Wada, N. Maeda, K. Mikoshiba, Nature 1989, 342, 3238.
  • 35
    “Structure-function relationships of the mouse inositol 1,4,5-trisphosphate receptor”: A. Miyawaki, T. Furuichi, Y. Ryou, S. Yoshikawa, T. Nakagawa, T. Saitoh, K. Mikoshiba, Proc. Natl. Acad. Sci. USA 1991, 88, 49114915.
  • 36
    “A calmodulin-target peptide hybrid molecule with unique calcium-binding properties”: T. Porumb, P. Yau, T. S. Harvey, M. Ikura, Protein Eng. 1994, 7, 109115.
  • 37
    “Fluorescent indicators for Ca2+ based on green fluorescent proteins and calmodulin”: A. Miyawaki, J. Llopis, R. Heim, J. M. McCaffery, J. A. Adams, M. Ikura, R. Y. Tsien, Nature 1997, 388, 882887.
  • 38
    “Dynamic and quantitative Ca2+ measurements using improved cameleons”: A. Miyawaki, O. Griesbeck, R. Heim, R. Y. Tsien, Proc. Natl. Acad. Sci. USA 1999, 96, 21352140.
  • 39
    “A genetically encoded, fluorescent indicator for cyclic AMP in living cells”: M. Zaccolo, F. De Giorgi, C. Y. Cho, L. Feng, T. Knapp, P. A. Negulescu, S. S. Taylor, R. Y. Tsien, T. Pozzan, Nat. Cell Biol. 2000, 2, 2529.
  • 40
    “Discrete microdomains with high concentration of cAMP in stimulated rat neonatal cardiac myocytes”: M. Zaccolo, T. Pozzan, Science 2002, 295, 17111715.
  • 41
    “Genetically encoded reporters of protein kinase A activity reveal impact of substrate tethering”: J. Zhang, Y. Ma, S. S. Taylor, R. Y. Tsien, Proc. Natl. Acad. Sci. USA 2001, 98, 1499715002.
  • 42
    “FRET-based biosensors for protein kinases: illuminating the kinome”: J. Zhang, M. D. Allen, Mol. Biosyst. 2007, 3, 759765.
  • 43
    “A genetically encoded fluorescent reporter reveals oscillatory phosphorylation”: J. D. Violin, J. Zhang, R. Y. Tsien, A. C. Newton, J. Cell Biol. 2003, 161, 899909.
  • 44
    “Targeting protein kinase C activity reporter to discrete intracellular regions reveals spatiotemporal differences in agonist-dependent signaling”: L. L. Gallegos, M. T. Kunkel, A. C. Newton, J. Biol. Chem. 2006, 281, 3094730956.
  • 45
    “Spatio-temporal dynamics of protein kinase B/Akt signaling revealed by a genetically encoded fluorescent reporter”: M. T. Kunkel, Q. Ni, R. Y. Tsien, J. Zhang, A. C. Newton, J. Biol. Chem. 2005, 280, 55815587.
  • 46
    “Calcium-dependent regulation of protein kinase D revealed by a genetically encoded kinase activity reporter”: M. T. Kunkel, A. Toker, R. Y. Tsien, A. C. Newton, J. Biol. Chem. 2007, 282, 67336742.
  • 47
    “Genetically encoded fluorescent reporters of protein tyrosine kinase activities in living cells”: A. Y. Ting, K. H. Kain, R. L. Klemke, R. Y. Tsien, Proc. Natl. Acad. Sci. USA 2001, 98, 1500315008.
  • 48
    “A pair of FRET-based probes for tyrosine phosphorylation of the CrkII adaptor protein in vivo”: K. Kurokawa, N. Mochizuki, Y. Ohba, H. Mizuno, A. Miyawaki, M. Matsuda, J. Biol. Chem. 2001, 276, 3130531310.
  • 49
    “Visualizing the mechanical activation of Src”: Y. Wang, E. L. Botvinick, Y. Zhao, M. W. Berns, S. Usami, R. Y. Tsien, S. Chien, Nature 2005, 434, 10401045.
  • 50
    “Fluorescent proteins from nonbioluminescent Anthozoa species”: M. V. Matz, A. F. Fradkov, Yu. A. Labas, A. P. Savitsky, A. G. Zaraisky, M. L. Markelov, S. A. Lukyanov, Nat. Biotechnol. 1999, 17, 969973.
  • 51
    “Biochemistry mutagenesis, and oligomerization of dsRed, a red fluorescent protein from coral”: G. S. Baird, D. A. Zacharias, R. Y. Tsien, Proc. Natl. Acad. Sci. USA 2000, 97, 1198411989.
  • 52
    “The structure of the chromophore within DsRed, a red fluorescent protein from coral”: L. A. Gross, G. S. Baird, R. C. Hoffman, K. K. Baldridge, R. Y. Tsien, Proc. Natl. Acad. Sci. USA 2000, 97, 1199011995.
  • 53
    “Refined crystal structure of DsRed, a red fluorescent protein from coral, at 2.0-Å resolution”: D. Yarbrough, R. M. Wachter, K. Kallio, M. V. Matz, S. J. Remington, Proc. Natl. Acad. Sci. USA 2001, 98, 462467.
  • 54
    “The structural basis for red fluorescence in the tetrameric GFP homolog DsRed”: M. A. Wall, M. Socolich, R. Ranganathan, Nat. Struct. Biol. 2000, 7, 11331138.
  • 55
    “A monomeric red fluorescent protein”: R. E. Campbell, O. Tour, A. E. Palmer, P. A. Steinbach, G. S. Baird, D. A. Zacharias, R. Y. Tsien, Proc. Natl. Acad. Sci. USA 2002, 99, 78777882.
  • 56
    “Improved monomeric red, orange and yellow fluorescent proteins derived from Discosoma sp. red fluorescent protein”: N. C. Shaner, R. E. Campbell, P. A. Steinbach, B. N. G. Giepmans, A. E. Palmer, R. Y. Tsien, Nat. Biotechnol. 2004, 22, 15671572.
  • 57
    “Evolution of new nonantibody proteins via iterative somatic hypermutation”: L. Wang, W. C. Jackson, P. A. Steinbach, R. Y. Tsien, Proc. Natl. Acad. Sci. USA 2004, 101, 1674516749.
  • 58
    “Advances in fluorescent protein technology”: N. C. Shaner, G. H. Patterson, M. W. Davidson, J. Cell Sci. 2007, 120, 42474260.
  • 59
    “Alzheimer’s disease—Fresh evidence points to an old suspect: Calcium”: J. Marx, Science 2007, 318, 384385.
  • 60
    “A beta plaques lead to aberrant regulation of calcium homeostasis in vivo resulting in structural and functional disruption of neuronal networks”: K. V. Kuchibhotla, S. T. Goldman, C. R. Lattarulo, H.-Y. Wu, B. T. Hyman, B. J. Bacskai, Neuron 2008, 59, 214225.
  • 61
    “A high-throughput screen for compounds that inhibit aggregation of the Alzheimer’s peptide”: W. Kim, Y. Kim, J. Min, D. J. Kim, Y.-T. Chang, M. H. Hecht, Chem. Biol. 2006, 1, 461469.
  • 62
    “Visualizing spatiotemporal dynamics of multicellular cell-cycle progression”: A. Sakaue-Sawano, H. Kurokawa, T. Morimura, A. Hanyu, H. Hama, H. Osawa, S. Kashiwagi, K. Fukami, T. Miyata, H. Miyoshi, T. Imamura, M. Ogawa, H. Masai, A. Miyawaki, Cell 2008, 132, 487498.
  • 63
    “Short tetracysteine tags to beta-tubulin demonstrate the significance of small labels for live cell imaging”: M. Andresen, R. Schmitz-Salue, S. Jakobs, Mol. Biol. Cell 2004, 15, 56165622.
  • 64
    “A FlAsH-based FRET approach to determine G protein-coupled receptor activation in living cells”: C. Hoffmann, G. Gaietta, M. Bünemann, S. R. Adams, S. Oberdorff-Maass, B. Behr, J.-P. Vilardaga, R. Y. Tsien, M. H. Ellisman, M. J. Lohse, Nat. Methods 2005, 2, 171176.
  • 65
    “Secretion of type III effectors into host cells in real time”: J. Enninga, J. Mounier, P. Sansonetti, G. T. Van Nhieu, Nat. Methods 2005, 2, 959965.
  • 66
    “The potential of nucleic acid repair in functional genomics”: M. C. Rice, K. Czymmek, E. B. Kmiec, Nat. Biotechnol. 2001, 19, 321326.
  • 67
    “Visualization of mRNA translation in living cells”: A. J. Rodriguez, S. M. Shenoy, R. H. Singer, J. Condeelis, J. Cell Biol. 2006, 175, 6776.
  • 68
    “Mammalian cell-based optimization of the biarsenical-binding tetracysteine motif for improved fluorescence and affinity”: B. R. Martin, B. N. Giepmans, S. R. Adams, R. Y. Tsien, Nat. Biotechnol. 2005, 23, 13081314.
  • 69
    “Hairpin structure of a biarsenical-tetracysteine motif determined by NMR”: F. Madani, J. Lind, P. Damberg, S. R. Adams, R. Y. Tsien, A. O. Gräslund, J. Am. Chem. Soc. 2009, 131, 46134615.
  • 70
    “Reporter proteins for in vivo fluorescence without oxygen”: T. Drepper, T. Eggert, F. Circolone, A. Heck, U. Krauß, J.-K. Guterl, M. Wendorff, A. Losi, W. Gärtner, K.-E. Jaeger, Nat. Biotechnol. 2007, 25, 443445.
  • 71
    “Harnessing phytochrome’s glowing potential”: A. J. Fischer, J. C. Lagarias, Proc. Natl. Acad. Sci. USA 2004, 101, 1733417339.
  • 72
    “The phytofluors: a new class of fluorescent protein probes”: J. T. Murphy, J. C. Lagarias, Curr. Biol. 1997, 7, 870876.
  • 73
    “Mammalian expression of infrared fluorescent proteins engineered from a bacterial phytochrome”: X. Shu, A. Royant, M. Z. Lin, T. A. Aguilera, V. Lev-Ram, P. A. Steinbach, R. Y. Tsien, Science 2009, 324, 804807.
  • 74
    “Tumor imaging by means of proteolytic activation of cell-penetrating peptides”: T. Jiang, E. S. Olson, Q. T. Nguyen, M. Roy, P. A. Jennings, R. Y. Tsien, Proc. Natl. Acad. Sci. USA 2004, 101, 1786717872.
  • 75
    “Understanding, using and improving green fluorescent protein”: A. B. Cubitt, R. Heim, S. R. Adams, A. E. Boyd, L. A. Gross, R. Y. Tsien, Trends Biochem. Sci. 1995, 20, 448455.
  • 76
    “Nonenzymatic deamidation of asparaginyl and glutaminyl residues in proteins”: H. T. Wright, Crit. Rev. Biochem. Mol. Biol. 1991, 26, 152.
  • 77
    “Expanded dynamic range of fluorescent indicators for Ca2+, by circularly permuted yellow fluorescent proteins”: T. Nagai, S. Yamada, T. Tominaga, M. Ichikawa, A. Miyawaki, Proc. Natl. Acad. Sci. USA 2004, 101, 1055410559.
  • 78
    “Predominant mode of human immunodeficiency virus transfer between T cells is mediated by sustained Env-dependent neutralization-resistant virological synapses”: P. Chen, W. Hubner, M. A. Spinelli, B. K. Chen, J. Virol. 2007, 81, 1258212595.
  • 79
    “A light-sensing knot revealed by the structure of the chromophore-binding domain of phytochrome”: J. R. Wagner, J. S. Brunzelle, K. T. Forest, R. D. Vierstra, Nature 2005, 438, 325331.
  • 80
    “Bright far-red fluorescent protein for whole-body imaging”: D. Shcherbo, E. M. Merzlyak, T. V. Chepurnykh, A. F. Fradkov, G. V. Ermakova, E. A. Solovieva, K. A. Lukyanov, E. A. Bogdanova, A. G. Zaraisky, S. Lukyanov, D. M. Chudakov, Nat. Methods 2007, 4, 741746.