Alain Schmitt | Searcharxiv

arXiv2026

Phylogeny.fr: the phylogenetic platform designed for non-specialists

Phylogenetic analysis has become a standard approach across many areas of biology, yet the growing complexity of phylogenetic methods and software remains a major obstacle for non-specialists. Since its launch in 2008, Phylogeny.fr has provided an accessible web platform for building phylogenetic trees using widely accepted methods without requiring local software installation. Here, we present a major redesign and modernization of the service. The new version integrates state-of-the-art tools while preserving historical programs for legacy support and relies on modern web architecture and HPC infrastructure. New interactive React-based viewers, ReSeqt and Reactree, provide intuitive exploration and publication-ready visualization of alignments and trees. The Blast-Explorer companion tool has also been updated and now includes clustering options. By combining ease of use, methodological flexibility, and modern phylogenetic tools, the new Phylogeny.fr addresses the needs of researchers, teachers, and students seeking accessible and reliable phylogenetic analyses.

q-bio.QM↗

arXiv2009

In Vivo Localization of Fas-Associated Death Domain Protein in the Nucleus and Cytoplasm of Normal Thyroid and Liver Cells

FADD (Fas-associated death domain) is the main death receptor adaptor molecule that transmits apoptotic signal. Recently, FADD protein was shown to be expressed both in the cytoplasm and nucleus of in vitro cell lines. In contrast to the cytoplasmic FADD, the nuclear FADD was shown to protect cells from apoptosis. However, in vivo subcellular localization of FADD was still unknown. Here, we demonstrated that FADD protein was expressed in both cytoplasmic and nuclear compartment in ex vivo thyroid cells demonstrating that nuclear sublocalization of FADD protein was a relevant phenomenon occurring in vivo. Moreover, we showed that in the nucleus of untransformed thyroid cells FADD localized mainly on euchromatin. We confirmed the nuclear localization of FADD in ex vivo liver and showed that in this organ FADD and MBD4 interact together. These results demonstrate that FADD is physiologically expressed in the nucleus of cells in at least two mouse organs. This particular localization opens new possible role of FADD in vivo either asan inhibitor of cell death, or as a transcription factor, or as a molecular link between apoptosis and genome surveillance.

q-bio.SC↗