<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Kmet, P.</style></author><author><style face="normal" font="default" size="100%">Kucerova, L.</style></author><author><style face="normal" font="default" size="100%">Sehadova, H.</style></author><author><style face="normal" font="default" size="100%">Wu, B.C.-H.</style></author><author><style face="normal" font="default" size="100%">Wu, Y.-L.</style></author><author><style face="normal" font="default" size="100%">Zurovec, M.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Identification of silk components in the bombycoid moth Andraca theae (Endromidae) reveals three fibroin subunits resembling those of Bombycidae and SphingidaeKmet, </style></title><secondary-title><style face="normal" font="default" size="100%">Journal of Insect Physiology</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">ANDRACA</style></keyword><keyword><style  face="normal" font="default" size="100%">BOMBYCIDAE</style></keyword><keyword><style  face="normal" font="default" size="100%">BOMBYX</style></keyword><keyword><style  face="normal" font="default" size="100%">COCOON</style></keyword><keyword><style  face="normal" font="default" size="100%">ENDROMIDAE</style></keyword><keyword><style  face="normal" font="default" size="100%">EVOLUTION</style></keyword><keyword><style  face="normal" font="default" size="100%">FIBROIN</style></keyword><keyword><style  face="normal" font="default" size="100%">MANDUCA</style></keyword><keyword><style  face="normal" font="default" size="100%">PROTEIN</style></keyword><keyword><style  face="normal" font="default" size="100%">SILK</style></keyword><keyword><style  face="normal" font="default" size="100%">SPHINGIDAE</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2023</style></year><pub-dates><date><style  face="normal" font="default" size="100%">06/2023</style></date></pub-dates></dates><urls><web-urls><url><style face="normal" font="default" size="100%">https://doi.org/10.1016/j.jinsphys.2023.104523</style></url></web-urls></urls><volume><style face="normal" font="default" size="100%">147</style></volume><pages><style face="normal" font="default" size="100%">104523</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;&amp;quot;The silk produced by Lepidoptera caterpillars is a mixture of proteins secreted by the transformed labial glands, the silk glands (SG). The silk fiber consists of insoluble filamentous proteins that form a silk core and are produced in the posterior part of the SG and soluble coat proteins consisting of sericins and various other polypeptides secreted in the middle part of the SG. We constructed a silk gland specific transcriptome of &lt;em&gt;Andraca theae&lt;/em&gt;&lt;span&gt; and created a protein database required for peptide mass fingerprinting. We identified major silk components by proteomic analysis of cocoon silk and by searching for homologies with known silk protein sequences from other species. We identified 30 proteins including a heavy chain &lt;span style=&quot;&quot;&gt;fibroin&lt;/span&gt;&lt;span&gt;, a light chain &lt;span style=&quot;&quot;&gt;fibroin&lt;/span&gt; and fibrohexamerin (P25) that form the silk core, as well as members of several structural families that form the silk coating. To uncover the evolutionary relationships among silk proteins, we included orthologs of silk genes from several recent genome projects and performed phylogenetic analyses. Our results confirm the recent molecular classification that the family Endromidae appears to be slightly more distant from the family Bombycidae. Our study provides important information on the evolution of silk proteins in the Bombycoidea, which is needed for proper annotation of the proteins and future functional studies.&amp;quot;&lt;/span&gt;&lt;/span&gt;&lt;/p&gt;
</style></abstract><section><style face="normal" font="default" size="100%">104523</style></section></record></records></xml>