BUSCADOR RECOLECTA

Figure S1. Photographs of different fractions obtained during pectin isolation; Figure S2. Representative GC-FID chromatograms of acid-soluble (CAP, a) and Ca-bound (AOPP, b) pectin-rich fractions monosaccharide composition obtained after complete hydrolysis. Table S1. Results of a two-tailed Student’s t-test of acid-soluble (CAP) and Ca-bound (AOPP) pectin-rich fractions influence on S. epidermidis strains growth compared to control sample without supplementation. Table S2. Results of a two-tailed Student’s t-test of acid-soluble (CAP) and Ca-bound (AOPP) pectin-rich fractions influence on S. aureus strains growth compared to control sample without supplementation., Peer reviewed

Individual penetration vs angle plots for each metal atom in (LMX)2 dimers and L2M–X covalent or incipient bonds, and table with fitting parameters and size of the data sets (PDF)., All of the data used, including CSD refcode, fragment number when there is more than one hit in a particular structure, crystallographic labels for the interacting atoms M and X, bond angle, covalent, and van der Waals radii of the M and X atoms, the calculated penetration index, and a label to indicate whether the M–X atom pair was retrieved as an M–X bond or an M···X contact (XLSX)., Peer reviewed

Peer reviewed

Experimental details, characterization data, DFT calculations, and NMR spectra., Peer reviewed

A—Protein sequence alignment comparing Vfr from A. baumannii AB5075 and its orthologue from P. aeruginosa PAO1. Residues involved in the interaction with cAMP, according to Beatson et al. [76], are framed in red. The strong conservation between these residues in both orthologues suggests that both proteins will interact with cAMP with the same specificity. The DNA binding domain of both proteins, as predicted by an InterPro sequence scan (PF00325), appears framed in green. The conservation in this region suggests a similar target promoter sequence for both orthologues. (*): identical residues; (:): highly similar residues; (.): somewhat similar residues. The sequence alignment was performed using Clustal Omega. B-D–Structural alignment of VfrAB5075 and VfrPAO1 in PyMOL. Overall alignment of the two proteins (VfrAB5075 in magenta and VfrPAO1 in cyan) indicates root mean square deviation (RMSD) of 1.938811 over 208 residues (B). Highlighted are the DNA binding domains (C) and cAMP binding sites (D) in VfrAB5075 (magenta) and VfrPAO1 (blue). E–Two residues (threonine 138 and threonine 139) from the VfrAB5075 cAMP binding site (magenta) were modified to alanine and tryptophan respectively resulting in VfrT138A,T139W variant which was subsequently used to demonstrate the necessity of cAMP binding for proper Vfr function in A. baumannii. Protein structure visualised using PyMOL., Peer reviewed

Images of nests were taken in a saltpan and rice fields in southern Spain, considering whether the nests were on natural or on substrates of anthropogenic origin. The images were analysed using specific software and the camouflage of eggs in relation to both nests and the microhabitats surrounding nests was estimated. The camouflage was considered as the differences in textures among such categories. Nest survival according to substrate type was estimated using a logistic exposure model. Further details on field, laboratory and statistical methods can be obtained from: Liñán-Cembrano, G., Castro, M., Ramo, C., Rendón, M. A., Amat, J. A., and Pérez-Hurtado, A. 2025. Effects of the anthropogenic introduction of substrates on egg camouflage and nest success in a ground-nesting bird. Animal Conservation. https://doi.org/10.1111/acv.70008, This dataset corresponds to information employed for analysis in Liñán-Cembrano, G., Castro, M., Ramo, C., Rendón, M. A., Amat, J, A., Pérez-Hurtado, A. 2025. Effects of the anthropogenic introduction of substrates on egg camouflage and nest success in a ground-nesting bird. Animal Conservation https://doi.org/10.1111/acv.70008, The dataset includes three files. One with information relative to egg characteristics (i). A second file contains data on egg camouflage according to the visual systems of the main predators in the study area (ii). Lastly, the third file presents information on the fate of nests (iii). (i) File: Characteristics of nests according to total area of eggshell covered by spots, fractal dimension of spottieness, and eggshell coloration. (ii) File: Nests according to habitat type, substrate type, and camouflage of eggs relative to both nests and microhabitats. Camouflage according to the visual systems of predators. (iii) File: Fate of nests according to substrate type, habitat type, and egg camouflage according to the visual systems of predators., No

Document S1. Tables S1–S3. Table S4. Peak-to-gene annotations, related to Figure 6., Peer reviewed

Materials contain R codes with analyses (*.R), phylogenetic trees (*.tre) and dataset (SupplementaryDataset1.xlsx). Dataset contains variables expressing visual system architecture and exposure to environmental light across birds: -eye axial length. -cornreal diameter. -optic tectum volume. -visual wulst volume. -nocturnal habits. -prefered habitat. These variables were extracted from literature and open sources for 760 avian species., Peer reviewed

Additional file 1: Supplementary figures S1 to S11 and Supplementary Tables S1 to S10., Ministerio de Ciencia e Innovación Fundación CajaCanarias Agència de Gestió d'Ajuts Universitaris i de Recerca Ministerio de Ciencia, Innovación y Universidades., Peer reviewed

Additional file 2. Excel file with the posterior values of the accepted models in the ABC-DL analysis. Factor 2, Kullback Leiber, and Spearman correlation tables for the accepted models in both ABC-DL analysis., Ministerio de Ciencia e Innovación Fundación CajaCanarias Agència de Gestió d'Ajuts Universitaris i de Recerca Ministerio de Ciencia, Innovación y Universidades., Peer reviewed