Biology subjects

Torrado, B.

Publications and source records attributed to Torrado, B..

3 recordsLinked to original sources

bioRxiv2025

An open, integrated platform for multiplexed bioluminescence microscopy

We report an imaging package to democratize all-in-one bioluminescence and fluorescence microscopy. The platform comprises three tools: PhasorViewer, a visualization suite to design experiments and identify optimal probe combinations; PhasorScope, an open-source, cost-effective microscopy framework to upgrade conventional microscopes; and PhasorAnalysis, a dedicated, user-friendly analysis pipeline to quantify phasor imaging data. We demonstrate the utility of the platform for multiplexed, simultaneous fluorescence and bioluminescence imaging with readily accessible optical reporters.

bioengineering↗

bioRxiv2025

GSLab: Open-Source Platform for Advanced Phasor Analysis in Fluorescence Microscopy

GSLab addresses the need for effective image analysis tools in fluorescence microscopy by providing an open-source platform that enhances traditional phasor analysis with advanced features. Key capabilities include machine learning-based clustering, real-time monitoring, and quantitative unmixing of fluorescent species. Designed for both commercial and custom systems, GSLab provides researchers with comprehensive lifetime and spectral phasor image analysis tools to tackle complex biological problems.

bioinformatics↗

bioRxiv2021

In vivo macromolecular crowding is differentially modulated by Aquaporin 0 in zebrafish lens: insights from a nano-environment sensor and spectral imaging.

Macromolecular crowding is crucial for cellular homeostasis. In vivo studies of macromolecular crowding and ultimately water-dynamics are needed to understand their role in cellular fates. The macromolecular crowding in the lens is essential for understanding normal optics of the lens, and moreover for understanding and prevention of cataract and presbyopia. Here we combine the use of the water nano-environmentally sensitive sensor (6-acetyl-2-dimethylaminonaphthalene, ACDAN) with in vivo studies of Aquaporin zero zebrafish mutants to understand the lens macromolecular crowding. Spectral phasor analysis of ACDAN fluorescence reveal the extent of water dipolar relaxation and demonstrate that the mutations in the duplicated zebrafish Aquaporin 0s, Aqp0a and Aqp0b, alter the water state and macromolecular crowding in the living zebrafish lens. Our results provide in vivo evidence that Aqp0a promotes fluid influx in the deeper lens cortex, whereas Aqp0b facilitates fluid efflux. This work opens new perspectives for in vivo studies on macromolecular crowding. TeaserIn this study we uncover the roles of Aquaporin 0 in macromolecular crowding required for lens development and vision.

biophysics↗