<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Zhang L</submitter><funding>National Natural Science Foundation of China</funding><pagination>953974</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC9560764</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>9</volume><pubmed_abstract>Mammalian bombesin-like neuropeptides (BLPs) play an important role in regulation of physiological and pathophysiological processes. Frog skin-derived BLPs, of smaller size and diverse lengths and sequences at their N-terminus, have attracted the attention of many researchers. However, these N-terminal variants and the receptors modulating their pharmacological actions are poorly studied and less understood. In this study, two BLPs, namely, [Asn&lt;sup>3&lt;/sup>, Lys&lt;sup>6&lt;/sup>, Thr&lt;sup>10&lt;/sup>, Phe&lt;sup>13&lt;/sup>]3-14-bombesin and [Asn&lt;sup>3&lt;/sup>, Lys&lt;sup>6&lt;/sup>, Phe&lt;sup>13&lt;/sup>]3-14-bombesin with primary structures NLGKQWATGHFM and NLGKQWAVGHFM were isolated from the skin secretion of hybrid &lt;i>Pelophylax&lt;/i> kl. &lt;i>esculentus&lt;/i>. Both BLPs share a similar primary structure with only a si</pubmed_abstract><journal>Frontiers in molecular biosciences</journal><pubmed_title>Two novel bombesin-like neuropeptides from the skin secretion of &lt;i>Pelophylax&lt;/i> kl. &lt;i>esculentus&lt;/i>: &lt;i>Ex vivo&lt;/i> pharmacological characterization on rat smooth muscle types.</pubmed_title><pmcid>PMC9560764</pmcid><funding_grant_id>32002344</funding_grant_id><pubmed_authors>Zhou M</pubmed_authors><pubmed_authors>Xi X</pubmed_authors><pubmed_authors>Ma C</pubmed_authors><pubmed_authors>Liu M</pubmed_authors><pubmed_authors>Shaw C</pubmed_authors><pubmed_authors>Zhang L</pubmed_authors><pubmed_authors>Chen X</pubmed_authors><pubmed_authors>Chen C</pubmed_authors><pubmed_authors>Zou W</pubmed_authors><pubmed_authors>Chen T</pubmed_authors><pubmed_authors>Wang L</pubmed_authors></additional><is_claimable>false</is_claimable><name>Two novel bombesin-like neuropeptides from the skin secretion of &lt;i>Pelophylax&lt;/i> kl. &lt;i>esculentus&lt;/i>: &lt;i>Ex vivo&lt;/i> pharmacological characterization on rat smooth muscle types.</name><description>Mammalian bombesin-like neuropeptides (BLPs) play an important role in regulation of physiological and pathophysiological processes. Frog skin-derived BLPs, of smaller size and diverse lengths and sequences at their N-terminus, have attracted the attention of many researchers. However, these N-terminal variants and the receptors modulating their pharmacological actions are poorly studied and less understood. In this study, two BLPs, namely, [Asn&lt;sup>3&lt;/sup>, Lys&lt;sup>6&lt;/sup>, Thr&lt;sup>10&lt;/sup>, Phe&lt;sup>13&lt;/sup>]3-14-bombesin and [Asn&lt;sup>3&lt;/sup>, Lys&lt;sup>6&lt;/sup>, Phe&lt;sup>13&lt;/sup>]3-14-bombesin with primary structures NLGKQWATGHFM and NLGKQWAVGHFM were isolated from the skin secretion of hybrid &lt;i>Pelophylax&lt;/i> kl. &lt;i>esculentus&lt;/i>. Both BLPs share a similar primary structure with only a si</description><dates><release>2022-01-01T00:00:00Z</release><publication>2022</publication><modification>2026-05-28T07:04:23.114Z</modification><creation>2025-04-06T09:24:20.496Z</creation></dates><accession>S-EPMC9560764</accession><cross_references><pubmed>36250016</pubmed><doi>10.3389/fmolb.2022.953974</doi></cross_references></HashMap>