@article{Hernández-Rojas2026,

title = {Changes in transposable elements expression in male and female mice liver throughout aging},

author = {Bairon Hernández-Rojas and Paola Murgas and Gonzalo Riadi},

doi = {10.1007/s11357-025-02065-y},

year  = {2026},

date = {2026-01-06},

urldate = {2026-01-06},

abstract = {Aging has traditionally been studied through the lens of protein-coding genes, with a strong bias toward data derived from male organisms. As a result, the role of non-coding elements and potential sex-specific differences remains largely unexplored. Transposable elements (TEs), mobile sequences capable of altering genome structure and regulating gene expression, have recently gained attention for their roles in development and aging. However, despite this growing interest, key aspects of TE expression dynamics are still poorly characterized, particularly in female tissues. To address this gap, we analyzed TE expression in RNA-Seq liver tissue from male (8, 26, 60, 78, and 104 weeks) and female (3, 24, 48, and 72 weeks) mice. Our results reveal distinct TE expression trends between sexes. While previous studies report increased TE expression with aging, we identified a subset of TEs with decreasing expression over time, differing between males and females. We also observed inverse expression trends between a few TEs and their nearby genes, supporting a potential regulatory relationship. We identified TEs with changing expression (CE TEs) through age associated with nearby genes showing strong expression correlations (|ρ|≥ 0.6). In males, correlated genes such as Txnrd2, Mthfd1, and Dkk3 are involved in redox regulation, one-carbon metabolism, and Wnt signaling, respectively, while in females, Thrb and Cd55 are linked to metabolic regulation and immune protection. These associations suggest that TE activity may be functionally coupled to transcriptional programs relevant to liver physiology and aging. These findings highlight the importance of examining TE expression in both sexes and suggest their potential regulatory roles in age-related liver physiology.



},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{nokey,

title = {Exploring a peripheral PIP2-binding site and its role in the alternative regulation of the TRP channel superfamily},

author = {L. Gonzalo Espinoza-Arcos and Mariela González-Avendaño and Matias Zuñiga-Bustos and Ricardo A. Zamora and Ariela Vergara-Jaque and Horacio Poblete},

doi = {10.1085/jgp.202413574},

year  = {2025},

date = {2025-11-03},

abstract = {Phosphatidylinositol 4,5-bisphosphate (PIP2) is recognized as an essential modulator of transient receptor potential (TRP) channels. Specifically, it influences the vanilloid receptor I (TRPV1), a pain receptor activated by a wide range of stimuli, including the binding of phospholipids, such as PIP2. The primary PIP2-binding site in TRPV1 has been identified through advanced techniques, revealing that the PIP2 binds to a specific pocket composed of positively charged residues located predominantly within the proximal C-terminus region. Additionally, a conserved segment with positively charged amino acids, K431 and R432, situated at the beginning of TRPV1's S1 transmembrane domain, has attracted considerable attention from the TRP research community. To date, our knowledge of this site's function and the subsequent effects following PIP2 binding is still emerging. In this work, MD simulations were conducted using coarse-grained models to investigate the binding dynamics of PIP2 on both WT and various mutated forms of TRPV1 channels. Our findings indicate that the K431A and R432A mutations significantly reduce the frequency of PIP2 contacts, suggesting that these mutated residues are part of a "peripheral binding pocket." This pocket seems to play a crucial role in facilitating the entry of PIP2 to the TRPV1 channel's primary binding site. Furthermore, our research has shown that these highly conserved residues within the TRPV subfamily are also structurally conserved across other TRP subfamilies, such as TRPM and TRPC, a detail not evident from sequence alignment alone. Consequently, we propose the existence of a structurally conserved peripheral PIP2-binding site shared among the diverse members of the TRP family, which can be categorized into distinct subfamilies.},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{nokey,

title = {Unraveling Lewis base substitution in ansa-type frustrated Lewis pairs: how N → P replacement redefines adduct stability and H2 activation},

author = {César Barrales-Martínez and Javier Rosales-Rojas and Julio Caballero and Rocío Durán },

doi = {10.1039/d5ra06998j },

year  = {2025},

date = {2025-10-21},

urldate = {2025-10-21},

abstract = {This study investigates, through quantum-chemical calculations, how replacing nitrogen with phosphorus in ansa-type frustrated Lewis pairs reshapes both the FLP–CLA equilibrium and H2 activation thermodynamics. Energy decomposition analysis shows that the stabilization of ansa-phosphinoborane adducts arises mainly from steric relief, which compensates for weaker donor–acceptor interactions. For H2 activation, the energetic effect of Lewis base substitution reaches up to 35.9 kcal mol−1 and correlates directly with the proton affinity differences between the corresponding amines and phosphines. This correlation identifies proton affinity as a predictive descriptor of reactivity. By establishing how N → P substitution redefines the steric–electronic balance controlling adduct stability and H2 cleavage, this work provides conceptual design principles for tailoring frustrated Lewis pairs. These insights advance the molecular-level understanding of main-group systems and support the rational development of next-generation metal-free hydrogenation catalysts under sustainable conditions.



},

keywords = {},

pubstate = {published},

tppubtype = {article}

}