Research on the chemistry of phenoxazines

Afanas'eva, G. B.; Viktorova, T. S.; Pashkevich, K. I.; Postovskii, I. Ya.

doi:10.1007/bf00472415

Cited by 3 publications

(1 citation statement)

References 5 publications

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“…General Synthesis of Biarsenical Derivatives of Dyes. 3,6-Dihydroxyxanthone, 2,7-dichloro-3,6-dihydroxyxanthone, 2‘-bromofluorescein (prepared by fusion of 4-bromoresorcinol and phthalic anhydride at 190 °C; purified as the diacetate), 2‘,7‘-dibromofluorescein, thiofluorescein (3‘,6‘-dihydroxyspiro[isobenzofuran-1(3H),9‘-[9H]thioxanthene]-3-one), thionol (7-hydroxy-3H-phenothiazin-3-one), and 2,7-dibromoresorufin (2,8-dibromo-7-hydroxy-3H-phenoxazin-3-one) were synthesized according to literature methods. 5,(6)-Sulfofluorescein was purchased from Molecular Probes.…”

Section: Methodsmentioning

confidence: 99%

New Biarsenical Ligands and Tetracysteine Motifs for Protein Labeling in Vitro and in Vivo: Synthesis and Biological Applications

et al. 2002

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We recently introduced a method (Griffin, B. A.; Adams, S. R.; Tsien, R. Y. Science 1998, 281, 269-272 and Griffin, B. A.; Adams, S. R.; Jones, J.; Tsien, R. Y. Methods Enzymol. 2000, 327, 565-578) for site-specific fluorescent labeling of recombinant proteins in living cells. The sequence Cys-Cys-Xaa-Xaa-Cys-Cys, where Xaa is an noncysteine amino acid, is genetically fused to or inserted within the protein, where it can be specifically recognized by a membrane-permeant fluorescein derivative with two As(III) substituents, FlAsH, which fluoresces only after the arsenics bind to the cysteine thiols. We now report kinetics and dissociation constants ( approximately 10(-11) M) for FlAsH binding to model tetracysteine peptides. Affinities in vitro and detection limits in living cells are optimized with Xaa-Xaa = Pro-Gly, suggesting that the preferred peptide conformation is a hairpin rather than the previously proposed alpha-helix. Many analogues of FlAsH have been synthesized, including ReAsH, a resorufin derivative excitable at 590 nm and fluorescing in the red. Analogous biarsenicals enable affinity chromatography, fluorescence anisotropy measurements, and electron-microscopic localization of tetracysteine-tagged proteins.

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Section: Methodsmentioning

confidence: 99%

New Biarsenical Ligands and Tetracysteine Motifs for Protein Labeling in Vitro and in Vivo: Synthesis and Biological Applications

et al. 2002

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[4] Caged fluorescent probes

Mitchison¹,

Sawin²,

Theriot³

et al. 1998

Methods in Enzymology

137

116

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Drosophila Mitotic Domain Boundaries as Cell Fate Boundaries

Cambridge

Davis

Minden

1997

Science

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Fate determination in Drosophila embryos is evidenced by the appearance of mitotic domains. To identify fate or fates of cells, individual cells in mitotic domains 2, 8, and 15 were marked and monitored through development. Comparison of the different fates indicated that domain boundaries are cell fate boundaries. Cells were marked by expression of GAL4-dependent transgenes after photoactivation of a caged GAL4VP16 analog that had its DNA binding activity inhibited with a photolabile blocking reagent. Caged GAL4VP16 was also used to induce gene expression in Xenopus embryos. Thus, photoactivated gene expression is a versatile tool for spatiotemporal control of gene expression.

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Research on the chemistry of phenoxazines

Cited by 3 publications

References 5 publications

New Biarsenical Ligands and Tetracysteine Motifs for Protein Labeling in Vitro and in Vivo: Synthesis and Biological Applications

New Biarsenical Ligands and Tetracysteine Motifs for Protein Labeling in Vitro and in Vivo: Synthesis and Biological Applications

[4] Caged fluorescent probes

Drosophila Mitotic Domain Boundaries as Cell Fate Boundaries

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