Wavelet analysis applied to SAR images to detect atmospheric structures

The aim of this work is to evaluate the possibilities offered by the wavelet analysis in the study of the spatial structure of the radar backscatter, which is linked to the spatial structure of the marine atmospheric boundary layer. Continuous wavelet analysis has been applied to a SAR image of the sea surface, previously analysed by the more classical Conditional Sampling technique. The main problem coped with has been to select, among the large number of wavelet maps produced by the analysis (256), those containing the more energetic backscatter structures. Since the phenomenon imaged by SAR was the convective turbulence, a multiscale and quasi-periodic or intermittent process, a selection of wavelet maps according to their mean energy was unsuccessful. On the contrary, a method based on the calculation of the standard deviation of the less probable highest wavelet amplitudes led to a right selection of the wavelet maps and to a convincing reconstruction of the map of backscatter structures, which resulted similar to that provided through the Conditional Sampling

Towards the wind direction determination in RADARSAT-2 polarimetrie images

AbstractThe interpretation of SAR images of the sea surface is difficult, due to the complexity of the geophysics and of the interaction mechanisms between electromagnetic and sea waves. The determination of the wind direction is crucial for the evaluation of the wind speed, but its retrieval is still an open issue. One of the few methods able to extract the sea surface wind from SAR data only has been developed and extensively applied to Envisat ASAR images in the past years, using the two-dimensional wavelet transform to detect the backscatter signature related to locally coherent wind cells. A preliminary analysis on the applicability of this method to RADARSAT-2 fully polarimetric images has been conducted to verify if polarimetry may improve the detection of backscatter imprints related to the wind direction

Expression pattern analysis of odorant-binding proteins in the pea aphid Acyrthosiphon pisum

Odorant-binding proteins (OBPs) are soluble proteins mediating chemoreception in insects. In previous research, we investigated the molecular mechanisms adopted by aphids to detect the alarm pheromone (E)-\u3b2-farnesene and we found that the recognition of this and structurally related molecules is mediated by OBP3 and OBP7. Here, we show the differential expression patterns of 5 selected OBPs (OBP1, OBP3, OBP6, OBP7, OBP8) obtained performing quantitative RT-PCR and immunolocalization experiments in different body parts of adults and in the 5 developmental instars, including winged and unwinged morphs, of the pea aphid Acyrthosiphon pisum. The results provide an overall picture that allows us to speculate on the relationship between the differential expression of OBPs and their putative function. The expression of OBP3, OBP6, and OBP7 in the antennal sensilla suggests a chemosensory function for these proteins, whereas the constant expression level of OBP8 in all instars could suggest a conserved role. Moreover, OBP1 and OBP3 are also expressed in nonsensory organs. A light and scanning electron microscopy study of sensilla on different body parts of aphid, in particular antennae, legs, mouthparts, and cornicles-cauda, completes this research providing a guide to facilitate the mapping of OBP expression profiles

Light--like Wilson loops and gauge invariance of Yang--Mills theory in 1+1 dimensions

A light-like Wilson loop is computed in perturbation theory up to ${\cal O} (g^4)$ for pure Yang--Mills theory in 1+1 dimensions, using Feynman and light--cone gauges to check its gauge invariance. After dimensional regularization in intermediate steps, a finite gauge invariant result is obtained, which however does not exhibit abelian exponentiation. Our result is at variance with the common belief that pure Yang--Mills theory is free in 1+1 dimensions, apart perhaps from topological effects.Comment: 10 pages, plain TeX, DFPD 94/TH/

New Insight on the Bioactivity of Solanum aethiopicum Linn. Growing in Basilicata Region (Italy): Phytochemical Characterization, Liposomal Incorporation, and Antioxidant Effects

Food extract’s biological effect and its improvement using nanotechnologies is one of the challenges of the last and the future decades; for this reason, the antioxidant effect of scarlet eggplant extract liposomal incorporation was investigated. Scarlet eggplant (Solanum aethiopicum L.) is a member of the Solanaceae family, and it is one of the most consumed vegetables in tropical Africa and south of Italy. This study investigated the antioxidant activity and the phytochemical composition of S. aethiopicum grown in the Basilicata Region for the first time. The whole fruit, peel, and pulp were subjected to ethanolic exhaustive maceration extraction, and all extracts were investigated. The HPLC-DAD analysis revealed the presence of ten phenolic compounds, including hydroxycinnamic acids, flavanones, flavanols, and four carotenoids (one xanthophyll and three carotenes). The peel extract was the most promising, active, and the richest in specialized metabolites; hence, it was tested on HepG2 cell lines and incorporated into liposomes. The nanoincorporation enhanced the peel extract’s antioxidant activity, resulting in a reduction of the concentration used. Furthermore, the extract improved the expression of endogenous antioxidants, such as ABCG2, CAT, and NQO1, presumably through the Nrf2 pathway

Crystal structures and binding dynamics of Odorant-Binding Protein 3 from two aphid species Megoura viciae and Nasonovia ribisnigri

Aphids use chemical cues to locate hosts and find mates. The vetch aphid Megoura viciae feeds exclusively on the Fabaceae, whereas the currant-lettuce aphid Nasonovia ribisnigri alternates hosts between the Grossulariaceae and Asteraceae. Both species use alarm pheromones to warn of dangers. For N. ribisnigri this pheromone is a single component (E)-β-farnesene but M. viciae uses a mixture of (E)-β-farnesene, (-)-α- pinene, β-pinene, and limonene. Odorant-binding proteins (OBP) are believed to capture and transport such semiochemicals to their receptors. Here, we report the first aphid OBP crystal structures and examine their molecular interactions with the alarm pheromone components. Our study reveals some unique structural features: 1) the lack of internal ligand binding site; 2) a striking groove in the surface of the proteins as a putative binding site; 3) the N-terminus rather than the C-terminus occupies the site closing off the conventional OBP pocket. The results from fluorescent binding assays, molecular docking and dynamics demonstrate that OBP3 from M. viciae can bind to all four alarm pheromone components and the differential ligand binding between these very similar OBP3s from the two aphid species is determined mainly by the direct π-π interactions between ligands and the aromatic residues of OBP3s in the binding pocket