{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Zhang L"],"funding":["National Natural Science Foundation of China"],"pagination":["953974"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9560764"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["9"],"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<sup>3</sup>, Lys<sup>6</sup>, Thr<sup>10</sup>, Phe<sup>13</sup>]3-14-bombesin and [Asn<sup>3</sup>, Lys<sup>6</sup>, Phe<sup>13</sup>]3-14-bombesin with primary structures NLGKQWATGHFM and NLGKQWAVGHFM were isolated from the skin secretion of hybrid <i>Pelophylax</i> kl. <i>esculentus</i>. Both BLPs share a similar primary structure with only a si"],"journal":["Frontiers in molecular biosciences"],"pubmed_title":["Two novel bombesin-like neuropeptides from the skin secretion of <i>Pelophylax</i> kl. <i>esculentus</i>: <i>Ex vivo</i> pharmacological characterization on rat smooth muscle types."],"pmcid":["PMC9560764"],"funding_grant_id":["32002344"],"pubmed_authors":["Zhou M","Xi X","Ma C","Liu M","Shaw C","Zhang L","Chen X","Chen C","Zou W","Chen T","Wang L"],"additional_accession":[]},"is_claimable":false,"name":"Two novel bombesin-like neuropeptides from the skin secretion of <i>Pelophylax</i> kl. <i>esculentus</i>: <i>Ex vivo</i> pharmacological characterization on rat smooth muscle types.","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<sup>3</sup>, Lys<sup>6</sup>, Thr<sup>10</sup>, Phe<sup>13</sup>]3-14-bombesin and [Asn<sup>3</sup>, Lys<sup>6</sup>, Phe<sup>13</sup>]3-14-bombesin with primary structures NLGKQWATGHFM and NLGKQWAVGHFM were isolated from the skin secretion of hybrid <i>Pelophylax</i> kl. <i>esculentus</i>. Both BLPs share a similar primary structure with only a si","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022","modification":"2026-05-28T07:04:23.114Z","creation":"2025-04-06T09:24:20.496Z"},"accession":"S-EPMC9560764","cross_references":{"pubmed":["36250016"],"doi":["10.3389/fmolb.2022.953974"]}}