@article {69773,
	title = {Live imaging of the extracellular matrix with a glycan-binding fluorophore.},
	journal = {Nat Methods},
	year = {2025},
	month = {2025 Feb 06},
	abstract = {<p>All multicellular systems produce and dynamically regulate extracellular matrices (ECMs) that play essential roles in both biochemical and mechanical signaling. Though the spatial arrangement of these extracellular assemblies is critical to their biological functions, visualization of ECM structure is challenging, in part because the biomolecules that compose the ECM are difficult to fluorescently label individually and collectively. Here, we present a cell-impermeable small-molecule fluorophore, termed Rhobo6, that turns on and red shifts upon reversible binding to glycans. Given that most ECM components are densely glycosylated, the dye enables wash-free visualization of ECM, in systems ranging from in vitro substrates to in vivo mouse mammary tumors. Relative to existing techniques, Rhobo6 provides a broad substrate profile, superior tissue penetration, non-perturbative labeling, and negligible photobleaching. This work establishes a straightforward method for imaging the distribution of ECM in live tissues and organisms, lowering barriers for investigation of extracellular biology.</p>
},
	issn = {1548-7105},
	doi = {10.1038/s41592-024-02590-2},
	url = {https://doi.org/10.1038/s41592-024-02590-2},
	author = {Fiore, Antonio and Yu, Guoqiang and Northey, Jason J and Patel, Ronak and Ravenscroft, Thomas A. and Ikegami, Richard and Kolkman, W and Pratik Kumar and Dilan, Tanya L and Ruetten, Virginia M.S. and Ahrens, Misha B and Shroff, Hari and Wang, Shaohe and Weaver, Valarie M and Pedram, Kayvon}
}
@article {69144,
	title = {Transforming chemigenetic bimolecular fluorescence complementation systems into chemical dimerizers using chemistry.},
	journal = {bioRxiv},
	year = {2024},
	month = {2024 Jan 01},
	abstract = {<p>Chemigenetic tags are versatile labels for fluorescence microscopy that combine some of the advantages of genetically encoded tags with small molecule fluorophores. The Fluorescence Activating and absorbance Shifting Tags (FASTs) bind a series of highly fluorogenic and cell-permeable chromophores. Furthermore, FASTs can be used in complementation-based systems for detecting or inducing protein-protein interactions, depending on the exact FAST protein variant chosen. In this study, we systematically explore substitution patterns on FAST fluorogens and generate a series of fluorogens that bind to FAST variants, thereby activating their fluorescence. This effort led to the discovery of a novel fluorogen with superior properties, as well as a fluorogen that transforms splitFAST systems into a fluorogenic dimerizer, eliminating the need for additional protein engineering.</p>
},
	doi = {10.1101/2023.12.30.573644},
	url = {https://doi.org/10.1101/2023.12.30.573644},
	author = {Pratik Kumar and Alina Gutu and Amelia Waring and Timothy A. Brown and Luke D. Lavis and Alison G. Tebo}
}
