{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Checco JW"],"funding":["NIDA NIH HHS","HHS | NIH | National Institute of Neurological Disorders and Stroke","HHS | NIH | National Institute on Drug Abuse","National Natural Science Foundation of China","NINDS NIH HHS","NIH HHS"],"pagination":["16862-16873"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6204918"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["293(43)"],"pubmed_abstract":["l- to d-residue isomerization is a post-translational modification (PTM) present in neuropeptides, peptide hormones, and peptide toxins from several animals. In most cases, the d-residue is critical for the biological function of the resulting d-amino acid-containing peptide (DAACP). Here, we provide an example in native neuropeptides in which the DAACP and its all-l-amino acid epimer are both active at their newly identified receptor <i>in vitro</i> and at a neuronal target associated with feeding behavior. On the basis of sequence similarity to a known DAACP from cone snail venom, we hypothesized that allatotropin-related peptide (ATRP), a neuropeptide from the neuroscience model organism <i>Aplysia californica</i>, may form multiple diastereomers in the <i>Aplysia</i> central nervous sy"],"journal":["The Journal of biological chemistry"],"pubmed_title":["Aplysia allatotropin-related peptide and its newly identified d-amino acid-containing epimer both activate a receptor and a neuronal target."],"pmcid":["PMC6204918"],"funding_grant_id":["P40 OD010952","R01 NS031609","P30 DA018310","31671097 and 31371104"],"pubmed_authors":["Checco JW","Zhang G","Jing J","Le ZW","Sweedler JV","Yuan WD"],"additional_accession":[]},"is_claimable":false,"name":"Aplysia allatotropin-related peptide and its newly identified d-amino acid-containing epimer both activate a receptor and a neuronal target.","description":"l- to d-residue isomerization is a post-translational modification (PTM) present in neuropeptides, peptide hormones, and peptide toxins from several animals. In most cases, the d-residue is critical for the biological function of the resulting d-amino acid-containing peptide (DAACP). Here, we provide an example in native neuropeptides in which the DAACP and its all-l-amino acid epimer are both active at their newly identified receptor <i>in vitro</i> and at a neuronal target associated with feeding behavior. On the basis of sequence similarity to a known DAACP from cone snail venom, we hypothesized that allatotropin-related peptide (ATRP), a neuropeptide from the neuroscience model organism <i>Aplysia californica</i>, may form multiple diastereomers in the <i>Aplysia</i> central nervous sy","dates":{"release":"2018-01-01T00:00:00Z","publication":"2018 Oct","modification":"2026-04-15T17:04:59.441Z","creation":"2019-11-05T08:04:18Z"},"accession":"S-EPMC6204918","cross_references":{"pubmed":["30194283"],"doi":["10.1074/jbc.RA118.004367","10.1074/jbc.ra118.004367"]}}