Publications by authors named "Anna Zaloudikova"

Article Synopsis
  • This study investigates the complete sequences of major silk proteins from two moth species within the Pyralidae family and compares their characteristics.
  • It utilizes proteomic analysis alongside genomic and transcriptomic data to identify and analyze silk genes, focusing on their structure, expression, and evolutionary relationships.
  • Key findings reveal significant differences in silk properties, such as hydrophobicity and hygroscopicity, and document a higher number of sericin genes in one species, along with the duplication of sericin gene regions in both species, which sets the stage for further research on silk evolution.
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Insect adipokinetic hormones (AKHs) are short peptides produced in the corpora cardiaca and are responsible for mobilizing energy stores from the fat body to the hemolymph. Three related peptides, AKH1, AKH2, and AKH/corazonin-related peptide (ACP) as well as three AKH receptors have been reported in . AKH1 and AKH2 are specific for the AKHR1 receptor, whereas ACP interacts with the other two AKHRs.

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Lepidopteran silk is a complex assembly of proteins produced by a pair of highly specialized labial glands called silk glands. Silk composition has been examined only in a handful of species. Here we report on the analysis of silk gland-specific transcriptomes from three developmental stages of the greater wax moth, Galleria mellonella, combined with proteomics, Edman microsequencing and northern blot analysis.

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Adipokinetic hormones (Akhs) are small peptides (8-10 amino acid [aa] residues long) found in insects that regulate metabolic responses to stress by stimulating catabolic reactions and mobilizing energy stores. We employed Transcription activator-like effector nuclease (TALEN) mutagenesis and isolated an Akh(1) mutant carrying a small deletion in the gene that resulted in a truncated peptide; the second aa (Leu) was missing from the functional octapeptide. This null Dmel/Akh mutant is suitable to study Akh function without any effect on the C-terminal associated peptide encoded by the same gene.

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