Publications by authors named "D Salom"

Arrestins halt signal transduction by binding to the phosphorylated C-termini of activated G protein-coupled receptors. Arrestin-1, the first subtype discovered, binds to rhodopsin in rod cells. Mutations in , the gene encoding Arrestin-1, are linked to Oguchi disease, characterized by delayed dark adaptation.

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The groundwater at the Sardas landfill in Huesca, Spain, is contaminated with benzene, chlorobenzenes, and hexachlorocyclohexane (HCH) isomers due to illegal waste dumping from a former lindane factory. In this study, microcosms using field-derived groundwater to evaluate in situ bioremediation were constructed. Anaerobic biostimulation with lactate successfully transformed α-, β-, δ-, and γ-HCH within two weeks, but failed to degrade benzene and less chlorinated benzenes, even with nutrient addition.

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Delivering ribonucleoproteins (RNPs) for in vivo genome editing is safer than using viruses encoding for Cas9 and its respective guide RNA. However, transient RNP activity does not typically lead to optimal editing outcomes. Here we show that the efficiency of delivering RNPs can be enhanced by cell-penetrating peptides (covalently fused to the protein or as excipients) and that lipid nanoparticles (LNPs) encapsulating RNPs can be optimized for enhanced RNP stability, delivery efficiency and editing potency.

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Rhodopsin, the prototypical class-A G-protein coupled receptor, is a highly sensitive receptor for light that enables phototransduction in rod photoreceptors. Rhodopsin plays not only a sensory role but also a structural role as a major component of the rod outer segment disc, comprising over 90% of the protein content of the disc membrane. Mutations in which lead to structural or functional abnormalities, including the autosomal recessive E150K mutation, result in rod dysfunction and death.

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Article Synopsis
  • Visual arrestin 1 (Arr1) is crucial for stopping the light response in photoreceptors, and while its dimer and tetramer formations have been studied in mammals, similar research in amphibians is lacking.
  • In this study, the dimerization of Arr1 from two amphibian species, Xenopus laevis and Ambystoma tigrinum, revealed that both proteins primarily form dimers with similar dissociation constants (K) to mammalian Arr1.
  • Crystallography and other techniques identified two potential dimer structures for amphibian Arr1, suggesting that the interaction between dimer forms may influence their stability and that the distribution of Arr1 in dark-adapted photoreceptors is impacted by
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