Resonance energy transfer in a novel two-component system: two-photon fluorophore and a photo-chromic acceptor molecule

2005 ◽  
Author(s):  
Raz Gvishi ◽  
Zvi Kotler ◽  
Garry Berkovic ◽  
Pnina Krief ◽  
Mark Sigalov ◽  
...  
Keyword(s):  
Energy Transfer ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Acceptor Molecule ◽  
Two Component System ◽  
Component System ◽  
Two Photon ◽  
Two Component

scholarly journals Chromenes involving a two-photon absorbing moiety: photochromism via intramolecular resonance energy transfer

2016 ◽  
Vol 40 (2) ◽  
pp. 1143-1148 ◽  
Author(s):  
Laura Bekere ◽  
Vladimir Lokshin ◽  
Mark Sigalov ◽  
Raz Gvishi ◽  
Peng Zhao ◽  
...  
Keyword(s):  
Energy Transfer ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Two Photon ◽  
Molecular Dyads

A general approach toward the synthesis of molecular dyads involving the photoactive moieties connected by a non-conjugative link is described.

scholarly journals Spatial Distribution and Function of Sterol Regulatory Element-Binding Protein 1a and 2 Homo- and Heterodimers by In Vivo Two-Photon Imaging and Spectroscopy Fluorescence Resonance Energy Transfer

2005 ◽  
Vol 25 (8) ◽  
pp. 2946-2956 ◽  
Author(s):  
Aikaterini Zoumi ◽  
Shrimati Datta ◽  
Lih-Huei L. Liaw ◽  
Cristen J. Wu ◽  
Gopi Manthripragada ◽  
...  
Keyword(s):  
Energy Transfer ◽  
Fluorescence Resonance Energy Transfer ◽  
Regulatory Element ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Two Photon ◽  
Sterol Regulatory Element ◽  
Photon Imaging ◽  
Imaging And Spectroscopy

ABSTRACT Sterol regulatory element-binding proteins (SREBPs) are a subfamily of basic helix-loop-helix-leucine zipper proteins that regulate lipid metabolism. We show novel evidence of the in vivo occurrence and subnuclear spatial localization of both exogenously expressed SREBP-1a and -2 homodimers and heterodimers obtained by two-photon imaging and spectroscopy fluorescence resonance energy transfer. SREBP-1a homodimers localize diffusely in the nucleus, whereas SREBP-2 homodimers and the SREBP-1a/SREBP-2 heterodimer localize predominantly to nuclear speckles or foci, with some cells showing a diffuse pattern. We also used tethered SREBP dimers to demonstrate that both homo- and heterodimeric SREBPs activate transcription in vivo. Ultrastructural analysis revealed that the punctate foci containing SREBP-2 are electron-dense nuclear bodies, similar or identical to structures containing the promyelocyte (PML) protein. Immunofluorescence studies suggest that a dynamic interplay exists between PML, as well as another component of the PML-containing nuclear body, SUMO-1, and SREBP-2 within these nuclear structures. These findings provide new insight into the overall process of transcriptional activation mediated by the SREBP family.

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