{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Xue S"],"funding":["NIDA NIH HHS","Seventh Framework Programme","National Institute on Drug Abuse"],"pagination":["1686-1689"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6231713"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["54(14)"],"pubmed_abstract":["A nicotine-degrading enzyme termed NicA2 was altered (NicA2-J1) through fusion of an albumin binding domain to increase its half-life. Examination of NicA2-J1 in vivo demonstrated a complete blockade of brain nicotine access, which in turn blunted nicotine's psychoactive effects. These data further support development of pharmacokinetic nicotine cessation therapeutics."],"journal":["Chemical communications (Cambridge, England)"],"pubmed_title":["An enzymatic advance in nicotine cessation therapy."],"pmcid":["PMC6231713"],"funding_grant_id":["R21 DA041839","R21 DA036691","623155","DA036691","DA041839"],"pubmed_authors":["Miranda PO","Janda KD","Xue S","Kallupi M","Zhou B","George O","Smith LC"],"additional_accession":[]},"is_claimable":false,"name":"An enzymatic advance in nicotine cessation therapy.","description":"A nicotine-degrading enzyme termed NicA2 was altered (NicA2-J1) through fusion of an albumin binding domain to increase its half-life. Examination of NicA2-J1 in vivo demonstrated a complete blockade of brain nicotine access, which in turn blunted nicotine's psychoactive effects. These data further support development of pharmacokinetic nicotine cessation therapeutics.","dates":{"release":"2018-01-01T00:00:00Z","publication":"2018 Feb","modification":"2025-04-04T02:04:46.779Z","creation":"2020-10-29T10:28:04Z"},"accession":"S-EPMC6231713","cross_references":{"pubmed":["29308799"],"doi":["10.1039/c7cc09134f"]}}