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Optical Highlighter Fluorescent Protein Literature Sources

The ability to selectively initiate or alter fluorescence emission profiles in photoconversion optical highlighter proteins renders these probes as excellent tools for exploring protein behavior in living cells. As the fluorescence intensity (or color spectrum) of highlighters occurs only after photon-mediated conversion, newly synthesized non-photoactivated protein pools remain unobserved and do not complicate experimental results. This section lists sources for review articles and original research reports on optical highlighter fluorescent proteins.

Ando, R., Hama, H., Yamamoto-Hino, M., Mizuno, H., and Miyawaki, A., An optical marker based on the UV-induced green-to-red-photoconversion of a fluorescent protein., Proceedings of the National Academy of Sciences (USA) 99: 12651-12656 (2002).
| PubMed |

Ando, R., Mizuno, H., and Miyawaki, A., Regulated fast nucleocytoplasmic shuttling observed by reversible protein highlighting., Science 306: 1370-1373 (2004).
| PubMed |

Andresen, M., Wahl, M. C., Stiel, A. C., Gräter, F., Schäfer, L. V., Trowitzsch, S., Weber, G., Eggeling, C., Grubmüller, H., Hell, S. W., and Jakobs, S., Structure and mechanism of the reversible photoswitch of a fluorescent protein., Proceedings of the National Academy of Sciences (USA) 102: 13070-13074 (2005). | PubMed |

Arimura, S., Yamamoto, J., Aida, G. P., Nakazono, M., and Tsutsumi, N., Frequent fusion and fission of plant mitochondria with unequal nucleoid distribution., Proceedings of the National Academy of Sciences (USA) 101: 7805-7808 (2002). | PubMed |

Bates, M., Blosser, T. R., and Zhuang, X., Short-range spectroscopic ruler based on a single-molecule optical switch., Physical Review Letters 94: 108101 (2005). | PRL |

Bell, A. F., Stoner-Ma, D., Wachter, R. M., and Tonge, P. J., Light-driven decarboxylation of wild-type green fluorescent protein., Journal of the American Chemical Society 125: 6919-6926 (2003). | PubMed |

Chattoraj, M., King, B. A., Bublitz, G. U., and Boxer, S. G., Ultra-fast excited state dynamics in green fluorescent protein: Multiple states and proton transfer., Proceedings of the National Academy of Sciences (USA) 93: 8362-8367 (1996). | PubMed |

Chen, Y., Macdonald, P. J., Skinner, J. P., Patterson, G. H., and Müller, J. D., Probing nucleocytoplasmic transport by two-photon activation of PA-GFP., Microscopy Research and Technique 69: 220-226 (2006). | PubMed |

Chudakov, D. M., Belousov, V. V., Zaraisky, A. G., Novoselov, V. V., Staroverov, D. B., Zorov, D. B., Lukyanov, S., and Lukyanov, K. A., Kindling fluorescent proteins for precise in vivo photolabeling., Nature Biotechnology 21: 191-194 (2003). | PubMed |

Chudakov, D. M., Feofanov, A. V., Mudrik, N. N., Lukyanov, S., and Lukyanov, K. A., Chromophore environment provides clues to "kindling fluorescent protein" riddle., Journal of Biological Chemistry 278: 7215-7219 (2003). | PubMed |

Chudakov, D. M. and Lukyanov, K. A., Use of green fluorescent protin (GFP) and its homologs for in vivo protein motility studies., Biochemistry (Moscow) 68: 952-957 (2003). | PubMed |

Chudakov, D. M., Verkhusha, V. V., Staroverov, D. B., Souslova, E. A., Lukyanov, S., and Lukyanov, K. A., Photoswitchable cyan fluorescent protein for protein tracking., Nature Biotechnology 22: 1435-1439 (2004). | PubMed |

Cinelli, R. A. G., Pellegrini, V., Ferrari, A., Faraci, P., Nifosi, R., Tyagi, M., Giacca, M., and Beltram, F., Green fluorescent proteins as optically controllable elements in bioelectronics., Applied Physics Letters 79: 3353-3355 (2001). | APL |

Cotlet, M., Habuchi, S., De Schryver, F. C., and Hofkens, J., Spectroscopy and microscopy of the autofluorescent protein DsRed from Discosoma genus coral., Proceedings of the International Society for Optical Engineering (SPIE) 5329: 88-98 (2004). | SPIE |

Cotlet, M., Hofkens, J., Köhn, F., Michiels, J., Dirix, G., Van Guyse, M., Vanderleyden, J., and De Schryver, F. C., Collective effects in individual oligomers of the red fluorescent coral protein DsRed., Chemical Physics Letters 336: 415-423 (2001). | CPL |

Cotlet, M., Hofkens, J., Maus, M., Gensch, T., Van der Auweraer, M., Michiels, J., Dirix, G., Van Guyse, M., Vanderleyden, J., Visser, A. J. W. G., and De Scheyver, F. C., Excited-state dynamics in the enhanced green fluorescent protein mutant probed by picosecond time-resolved single photon counting spectroscopy., Journal of Physical Chemistry B 105: 4999-5006 (2001). | JPCB |

Creemers, T. M. H., Lock, A. J., Subramanium, V., Jovin, T. M., and Volker, S., Three photoconvertible forms of green fluorescent protein identified by spectral hole-burning., Nature Structural Biology 6: 557-560 (1999). | PubMed |

Deryusheva, S. and Gall, J. G., Dynamics of coilin in Cajal bodies of the Xenopus germinal vesicle., Proceedings of the National Academy of Sciences (USA) 101: 4810-4814 (2004). | PubMed |

Dickson, R. M., Cubitt, A. B., Tsien, R. Y., and Moerner, W. E., On/off blinking and switching behavior of single molecules of green fluorescent protein., Nature 388: 355-358 (1997). | PubMed |

Dittrich, P. S., Schäfer, S. P., and Schwille, P., Characterization of the photoconversion on reaction of the fluorescent protein Kaede on the single-molecule level., Biophysical Journal 89: 3446-3455 (2005). | PubMed |

Dunn, G. A., Dobbie, I. M., Monypenny, J., Holt, M. R., and Zicha, D., Fluorescence localization after photobleaching (FLAP): A new method for studying protein dynamics in living cells., Journal of Microscopy 205: 109-112 (2002). | PubMed |

Eisenstein, M., New fluorescent protein includes handy on-off switch., Nature Methods 2: 8-9 (2005). | Nature Methods |

Elowitz, M. B., Surette, M. G., Wolf, P. E., Stock, J. B., and Leibler, S., Photoactivation turns green fluorescent protein red., Current Biology 7: 809-812 (1997). | PubMed |

Elowitz, M. B., Surette, M. G., Wolf, P. E., Stock, J. B., and Liebler, S., Protein mobility in the cytoplasm of Escherichia coli., Journal of Bacteriology 181: 197-203 (1999). | PubMed |

Evanko, D., Highlighting protein movement in living cells., Nature Methods 1: 96-97 (2004). | Nature Methods |

Fischer, A. J., Coleman, W. J., Yang, M. M., and Lagarias, J. C., Engineering phytochromes: Biliproteins that switch and glow., Proceedings of the International Society for Optical Engineering (SPIE) 5329: 33-43 (2004). | SPIE |

Gurskaya, N. G., Fradkov, A. F., Pounkova, N. I., Staroverov, D. B., Bulina, M. E., Yanushevich, Y. G., Labas, Y. A., Lukyanov, S., and Lukyanov, K. A., A colourless green fluorescent protein homologue from the non-fluorescent hydromedusa Aequorea coerulescens and its fluorescent mutants., Biochemical Journal 373: 403-408 (2003). | PubMed |

Gurskaya, N. G., Verkhusha, V. V., Shcheglov, A. S., Staroverov, D. B., Chepurnykh, T. V., Fradkov, A. F., Lukyanov, S., and Lukyanov, K. A., Engineering of a monomeric green-to-red photoactivatable fluorescent protein induced by blue light., Nature Biotechnology 24: 461-465 (2006). | PubMed |

Habuchi, S., Ando, R., Dedecker, P., Verheijen, W., Mizuno, H., Miyawaki, A., and Hofkens, J., Reversible single-molecule photoswitching in the GFP-like fluorescent protein Dronpa., Proceedings of the National Academy of Sciences (USA) 102: 9511-9516 (2005).
| PubMed |

Habuchi, S., Cotlet, M., Gensch, T., Bednarz, T., Haber-Pohlmeier, S., Rozenski, J., Dirix, G., Michiels, J., Vanderleyden, J., Herberle, J., De Schryver, F. C., and Hofkens, J., Evidence for the isomerization and decarboxylation in the photoconversion of the red fluorescent protein DsRed., Journal of the American Chemical Society 127: 8977-8984 (2005).
| PubMed |

Hell, S. W., Strategy for far-field optical imaging and writing without diffraction limit., Physics Letters A 326: 140-145 (2004). | PLA |

Henderson, J. N. and Remington, S. J., The kindling fluorescent protein: A transient photoswitchable marker., Physiology 21: 162-170 (2006). | Physiology |

Hofmann, M., Eggeling, C., Jakobs, S., and Hell, S. W., Breaking the diffraction barrier in fluorescence microscopy at low light intensities by using reversibly photoswitchable proteins., Proceedings of the National Academy of Sciences (USA) 102: 17565-17569 (2005). | PubMed |

Hogan, H., Fluorescence at the flip of a molecular switch., Biophotonics International 12: 34-38 (2005). | BioPhotonics |

Irie, M., Diarylethenes for memories and switches., Chemical Reviews 100: 1685-1716 (2000). | PubMed |

Irie, M., Fukaminato, T., Sasaki, T., Tamai, N., and Kawai, T., Organic Chemistry: A digital fluorescent molecular photoswitch., Nature 420: 759-760 (2002). | PubMed |

Ivanchenko, S., Roecker, C., Oswald, F., Wiedenmann, J., and Nienhaus, G. U., Targeted green-red photoconversion of EosFP, a fluorescent marker protein., Journal of Biological Physics 31: 249-259 (2005). | JBP |

Izquierdo, M. A., Bell, T. D. M., Habuchi, S., Fron, E., Pilot, R., Vosch, T., De Feyter, S., Verhoeven, J., Jacob, J., Mullen, K., Hofkens, J., and De Schryver, F. C., Switching of the fluorescence emission of single molecules between the locally excited and charge transfer states., Chemical Physics Letters 401: 503-508 (2005). | CPL |

Jakobs, S., Schauss, A. C., and Hell, S. W., Photoconversion of matrix targeted GFP enables analysis of continuity and intermixing of the mitochondrial lumen., FEBS Letters 554: 194-200 (2003). | PubMed |

Jung, G., Wiehler, J., and Zumbusch, A., The photophysics of green fluorescent protein: Influence of the key amino acids at positions 65, 203, and 222., Biophysical Journal 88: 1932-1947 (2005). | PubMed |

Karbowski, M., Arnoult, D., Chen, H., Chan, D. C., Smith, C. L., and Youle, R. J., Quantitation of mitochondrial dynamics by photolabeling of individual organelles shows that mitochondrial fusion is blocked during the Bax activation phase of apoptosis., Journal of Cell Biology 164: 493-499 (2004). | PubMed |

Kennis, J. T. M., Larsen, D. S., van Stokkum, I. H. M., Vengris, M., van Thor, J. J., and van Grondelle, R., Uncovering the hidden ground state of green fluorescent protein., Proceedings of the National Academy of Sciences (USA) 101: 17988-17993 (2004).
| PubMed |

Labas, Y. A., Gurskaya, N. G., Yanushevich, Y. G., Fradkov, A. F., Lukyanov, K. A., Lukyanov, S. A., and Matz, M. V., Diversity and evolution of the green fluorescent protein family., Proceedings of the National Academy of Sciences (USA) 99: 4256-4261 (2002). | PubMed |

Lee, W. L., Kim, M. K., Schreiber, A. D., and Grinstein, S., Role of ubiquitin and proteasomes in phagosome maturation., Molecular Biology of the Cell 16: 2077-2090 (2005). | PubMed |

Liang, Y. C., Dvornikov, A. S., and Rentzepis, P. M., Nonvolatile read-out molecular memory., Proceedings of the National Academy of Sciences (USA) 100: 8109-8112 (2003). | PubMed |

Lippincott-Schwartz, J., Altan-Bonnet, N., and Patterson, G. H., Photobleaching and photoactivation: Following protein dynamics in living cells., Nature Cell Biology 5: S7-S14 (2003). | PubMed |

Lippincott-Schwartz, J. and Patterson, G. H., Development and use of fluorescent protein markers in living cells., Science 300: 87-91 (2003). | PubMed |

Lukyanov, K. A., Chudakov, D. M., Lukyanov, S., and Verkhusha, V. V., Innovation: Photoactivatable fluorescent proteins., Nature Reviews Molecular Cell Biology 6: 885-891 (2005). | PubMed |

Lukyanov, K. A., Fradkov, A. F., Gurskaya, N. G., Matz, M. V., Labas, Y. A., Savitsky, A. P., Markelov, M. L., Zaraisky, A. G., Zhao, X., Fang, Y., Tan, W., and Lukyanov, S. A., Natural animal coloration can be determined by a nonfluorescent green fluorescent protein homolog., Journal of Biological Chemistry 275: 25879-25882 (2000). | PubMed |

Malvezzi-Campeggi, F., Jahnz, M., Heinze, K. G., Dittrich, P., and Schwille, P., Light-induced flickering of DsRed provides evidence for distinct and interconvertible fluorescent states., Biophysical Journal 81: 1776-1785 (2001). | PubMed |

Marchant, J. S., Stutzmann, G. E., Leissring, M. A., LaFerla, F. M., and Parker, I., Multiphoton-evoked color change of DsRed as an optical highlighter for cellular and subcellular labeling., Nature Biotechnology 19: 645-649 (2001). | PubMed |

Martynov, V. I., Savitsky, A. P., Martynova, N. Y., Savitsky, P. A., Lukyanov, K. A., and Lukyanov, S. A., Alternative cyclization in GFP-like proteins family., Journal of Biological Chemistry 276: 21012-21016 (2001). | PubMed |

McAnaney, T. B., Zeng, W., Doe, C. F. E., Bhanji, N., Wakelin, S., Pearson, D. S., Abbyad, P., Shi, X., Boxer, S. G., and Bagshaw, C. R., Protonation, photobleaching, and photoactivation of yellow fluorescent protein (YFP 10C): A unifying mechanism., Biochemistry 44: 510-524 (2005). | PubMed |

Mirabella, R., Franken, C., van der Krogt, G. N. M., Bisseling, T., and Geurts, R., Use of the fluorescent timer DsRed-E5 as reporter to monitor dynamics of gene activity in plants., Plant Physiology 135: 1879-1887 (2004). | PubMed |

Mitchison, T. J., Polewards microtubule flux in the mitotic spindle: Evidence from photoactivation of fluorescence., Journal of Cell Biology 109: 637-652 (1989).
| PubMed |

Miyawaki, A., Fluorescent proteins in a new light., Nature Biotechnology 22: 1374-1376 (2004). | PubMed |

Miyawaki, A., Innovations in the imaging of brain functions using fluorescent proteins., Neuron 48: 189-199 (2005). | PubMed |

Mizuno, H., Mal, T. K., Tong, K. I., Ando, R., Furuta, T., Ikura, M., and Miyawaki, A., Photo-induced peptide cleavage in the green-to-red conversion of a fluorescent protein., Molecular Cell 12: 1051-1058 (2003). | PubMed |

Nienhaus, G. U., Nienhaus, K., Hölze, A., Ivanchenko, S., Renzi, F., Oswald, F., Wolff, M., Schmitt, F., Röcker, C., Vallone, B., Wiedenmann, W., Heilker, R., Nar, H., and Wiedenmann, J., Photoconvertible fluorescent protein EosFP - Biophysical properties and cell biology applications., Photochemistry and Photobiology 82: 351-358 (2006). | PubMed |

Nienhaus, K., Nienhaus, G. U., Wiedenmann, J., and Nar, H., Structural basis for photo-induced protein cleavage and green-to-red conversion of fluorescent protein EosFP., Proceedings of the National Academy of Sciences (USA) 102: 9156-9159 (2005).
| PubMed |

O'Connell, K. M. and Tamkun, M. M., Targeting of voltage-gated potassium channel isoforms to distinct cell surface microdomains., Journal of Cell Science 118: 2155-2166 (2005). | PubMed |

Pakhomov, A. A., Martynova, N. Y., Gurskaya, N. G., Balashova, T. A., and Martynov, V., Photoconversion of the chromophore of a fluorescent protein from Dendronephthya sp., Biochemistry (Moscow) 69: 901-908 (2004). | PubMed |

Patterson, G. H. and Lippincott-Schwartz, J., A photoactivatable GFP for selective photolabeling of proteins and cells., Science 297: 1873-1877 (2002). | PubMed |

Patterson, G. H. and Lippincott-Schwartz, J., Development of a photoactivatable fluorescent protein from Aequorea victoria GFP., Proceedings of the International Society for Optical Engineering (SPIE) 5329: 13-22 (2004). | SPIE |

Patterson, G. H. and Lippincott-Schwartz, J., Selective photolabeling of proteins using photoactivatable GFP., Methods 32: 445-450 (2004). | PubMed |

Politz, J. C., Use of caged fluorochromes to track macromolecular movement in living cells., Trends in Cell Biology 9: 284-287 (1999). | PubMed |

Post, J. N., Lidke, K. A., Rieger, B., and Anrndt-Jovin, D. J., One- and two-photon photoactivation of a pa-GFP fusion protein in live Drosophila embryos., Federation of European Biochemical Societies Letters 579: 325-330 (2005). | PubMed |

Quillin, M. L., Anstrom, D. M., Shu, X., O'Leary, S., Kallio, K., Chudakov, D. M., and Remington, S. J., Kindling fluorescent protein from Anemonia sulcata: Dark-state structure at 1.38 Angstrom resolution., Biochemistry 44: 5774-5787 (2005). | PubMed |

Rasse, T. M., Fouquet, W., Schmid, A., Kittel, R. J., Mertel, S., Sigrist, C. B., Schmidt, M., Guzman, A., Merino, C., Qin, G., Quentin, C., Madeo, F. F., Heckmann, M., and Sigrist, S. J., Glutamate receptor dynamics organizing synapse formation in vivo., Nature Neuroscience 8: 898-905 (2005). | PubMed |

Rizzo, M. A. and Piston, D. W., Fluorescent protein tracking and detection., in Live Cell Imaging: A Laboratory Manual, Goldman, R. D. and Spector, D. L. (eds.), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York, pages 3-23 (2005). | Amazon |

Robinson, L. C. and Marchant, J. S., Improved "optical highlighter" probes derived from Discosoma red fluorescent protein., Biophysical Journal 88: 1444-1457 (2005).
| PubMed |

Runions, J., Brach, T., Kühner, S., and Hawes, C., Photoactivation of GFP reveals protein dynamics within the endoplasmic reticulum membrane., Journal of Experimental Botany 57: 43-50 (2006). | PubMed |

Sacchetti, A., Cappetti, V., Crescenzi, C., Celli, N., Rotilio, D., and Alberti, S., Red GFP and endogenous porphyrins., Current Biology 9: R391-R393 (1999). | PubMed |

Salih, A., Larkum, A., Cronin, T., Wiedenmann, J., Szymczak, R., and Cox, G., Biological properties of coral GFP-type proteins provide clues for engineering novel optical probes and biosensors., Proceedings of the International Society for Optical Engineering (SPIE) 5329: 61-72 (2004). | SPIE |

Sato, T., Takahoko, M., and Okamoto, H., HuC:Kaede, a useful tool to label neural morphologies in networks in vivo., Genesis 44: 136-142 (2006). | PubMed |

Sauer, M., Reversible molecular photoswitches: A key technology for nanoscience and fluorescence imaging., Proceedings of the National Academy of Sciences (USA) 102: 9433-9434 (2005). | PubMed |

Sawin, K. E. and Nurse, P., Photoactivation of green fluorescent protein., Current Biology 7: 606-607 (1997). | PubMed |

Schäfer, S. P., Dittrich, P. S., Petrov, E. P., and Schwille, P., Single molecule fluorescence imaging of photoinduced conversion and bleaching behavior of the fluorescent protein Kaede., Microscopy Research and Technique 69: 210-219 (2006). | PubMed |

Schermelleh, L., Spada, F., Easwaran, H. P., Zolghadr, K., Margot, J. B., Cardoso, M. C., and Leonhardt, H., Trapped in action: Direct visualization of DNA methyltransferase activity in living cells., Nature Methods 2: 751-756 (2005). | PubMed |

Schneider, M., Barozzi, S., Testa, I., Faretta, M., and Diaspro, A., Two-photon activation and excitation properties of PA-GFP in the 720-920 nm region., Biophysical Journal 89: 1346-1352 (2005). | PubMed |

Shagin, D. A., Barsova, E. V., Yanushevich, Y. G., Fradkov, A. F., Lukyanov, K. A., Labas, Y. A., Semenova, T. N., Ugalde, J. A., Meyers, A., Nunez, J. M., Widder, E. A., Lukyanov, S. A., and Matz, M. V., GFP-like proteins as ubiquitous metazoan superfamily: Evolution of functional features and structural complexity., Molecular Biology and Evolution 21: 841-850 (2004). | PubMed |

Shav-Tal, Y., Darzacq, X., Shenoy, S. M., Fusco, D., Janicki, S. M., Spector, D. L., and Singer, R. H., Dynamics of single mRNPs in nuclei of living cells., Science 304: 1797-1800 (2004). | PubMed |

Souslova, E. A. and Chudakov, D. M., Photoswitchable cyan fluorescent protein as a FRET donor., Microscopy Research and Technique 69: 207-209 (2006). | PubMed |

Stark, D. A and Kulesa, P. M., Photoactivatable green fluorescent protein as a single-cell marker in living embryos., Developmental Dynamics 233: 983-992 (2005). | PubMed |

Terskikh, A., Fradkov, A., Ermakova, G., Zaraisky, A., Tan, P., Kajava, A., Zhao, X., Lukyanov, S., Matz, M., Kim, S., Weissman, I., and Siebert, P., "Fluorescent timer": Protein that changes color with time., Science 290: 1585-1588 (2000). | PubMed |

Tinnefield, P. and Sauer, M., Branching out of single-molecule fluorescence spectroscopy: Challenges for chemistry and influence on biology., Angewandte Chemie International Edition 44: 2642-2671 (2005). | PubMed |

Tsutsui, H., Karasawa, S., Shimizu, H., Nukina, N., and Miyawaki, A., Semi-rational engineering of a coral fluorescent protein into an efficient highlighter., EMBO Reports 6: 233-238 (2005). | PubMed |

van Thor, J. J., Gensch, T., Hellingwerf, K. J., and Johnson, L. N., Phototransformation of green fluorescent protein with UV and visible light leads to decarboxylation of glutamate 222., Nature Structural Biology 9: 37-41 (2002). | PubMed |

van Thor, J. J., Pierik, A. J., Nugteren-Roodzant, I., Xie, A., and Hellingwerf, K. J., Characterization of the photoconversion of green fluorescent protein with FTIR spectroscopy., Biochemistry 37: 16915-16921 (1998). | PubMed |

Verkhusha, V. V. and Lukyanov, K. A., The molecular properties and applications of Anthozoa fluorescent proteins and chromoproteins., Nature Biotechnology 22: 289-296 (2004). | PubMed |

Verkhusha, V. V., Otsuna, H., Awasaki, T., Oda, H., Tsukita, S., and Ito, K., An enhanced mutant of red fluorescent protein DsRed for double labeling and developmental timer of neural fiber bundle formation., Journal of Biological Chemistry 276: 29621-29624 (2001). | PubMed |

Verkhusha, V. V. and Sorkin, A., Conversion of the monomeric red fluorescent protein into a photoactivatable probe., Chemistry and Biology 12: 279-285 (2005). | PubMed |

Wiedenmann, J., Ivanchenko, S., Oswald, F., Schmitt, F., Rocker, C., Salih, A., Spindler, K., and Nienhaus, G. U., EosFP, a fluorescent marker protein with UV-inducible green-to-red fluorescence conversion., Proceedings of the National Academy of Sciences (USA) 101: 15905-15910 (2004). | PubMed |

Wiedenmann, J. and Nienhaus, G. U., Live-cell imaging with EosFP and other photoactivatable marker proteins of the GFP family., Expert Review of Proteomics 3: 361-374 (2006). | ERP |

Wiegand, U. K., Duncan, R. R., Greaves, J., Chow, R. H., Shipston, M. J., and Apps, D. K., Red, yellow, green go! A novel tool for microscopic segregation of secretory vesicle pools according to their age., Biochemistry Society Transactions 31: 851-856 (2003).
| PubMed |

Wilmann, P. G., Petersen, J., Devenish, R. J., Prescott, M., and Rossjohn, J., Variations on the GFP chromophore., Journal of Biological Chemistry 280: 2401-2404 (2005).
| PubMed |

Yampolsky, I. V., Remington, S. J., Martynov, V. I., Potapov, V. K., Lukyanov, S., and Lukyanov, K. A., Synthesis and properties of the chromophore of the asFP595 chromoprotein from Anemonia sulcata., Biochemistry 44: 5788-5793 (2005). | PubMed |

Yokoe, H. and Meyer, T., Spatial dynamics of GFP-tagged proteins investigated by local fluorescence enhancement., Nature Biotechnology 14: 1252-1256 (1996). | PubMed |

Zagranichny, V. E., Rudenko, N. V., Gorokhovatsky, A. Y., Zakharov, M. V., Balashova, T. A., and Arseniev, A. S., Traditional GFP-type cyclization and unexpected fragmentation from Anemonia sulcata, asFP595., Biochemistry 43: 13598-13603 (2004). | PubMed |

Zagranichny, V. E., Rudenko, N. V., Gorokhovatsky, A. Y., Zakharov, M. V., Shenkarev, Z. O., Balashova, T. A., and Arseniev, A. S., zFP538, a yellow fluorescent protein from coral, belongs to the DsRed subfamily of GFP-like proteins but possesses the unexpected site of fragmentation., Biochemistry 43: 4764-4772 (2004). | PubMed |


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