{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["1(8)"],"submitter":["Kaczmarek P"],"pubmed_abstract":["Antiproliferative factor (APF), a sialylated glycopeptide secreted by explanted bladder epithelial cells from interstitial cystitis/painful bladder syndrome (IC/PBS) patients, and its unsialylated analogue (as-APF) significantly decrease proliferation of bladder epithelial cells and/or certain carcinoma cell lines in vitro. We recently reported a structure-activity relationship profile for the peptide portion of as-APF and revealed that truncation of the C-terminal alanine did not significantly affect antiproliferative activity. To better understand the structural basis for the maintenance of activity of this truncated eight amino acid as-APF (as-APF8), we synthesized several amino acid-substituted derivatives and studied their ability to inhibit bladder epithelial cell proliferation in vi"],"journal":["ACS medicinal chemistry letters"],"pagination":["390-4"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4007904"],"repository":["biostudies-literature"],"pubmed_title":["Structure-Activity Studies on Antiproliferative Factor (APF) Glycooctapeptide Derivatives."],"pmcid":["PMC4007904"],"pubmed_authors":["Grkovic D","Tocci GM","Guo L","Zhang CO","Adams KM","Barchi JJ","Kaczmarek P","Michejda CJ","Keay SK","Koch KR"],"additional_accession":[]},"is_claimable":false,"name":"Structure-Activity Studies on Antiproliferative Factor (APF) Glycooctapeptide Derivatives.","description":"Antiproliferative factor (APF), a sialylated glycopeptide secreted by explanted bladder epithelial cells from interstitial cystitis/painful bladder syndrome (IC/PBS) patients, and its unsialylated analogue (as-APF) significantly decrease proliferation of bladder epithelial cells and/or certain carcinoma cell lines in vitro. We recently reported a structure-activity relationship profile for the peptide portion of as-APF and revealed that truncation of the C-terminal alanine did not significantly affect antiproliferative activity. To better understand the structural basis for the maintenance of activity of this truncated eight amino acid as-APF (as-APF8), we synthesized several amino acid-substituted derivatives and studied their ability to inhibit bladder epithelial cell proliferation in vi","dates":{"release":"2010-01-01T00:00:00Z","publication":"2010 Nov","modification":"2025-04-05T10:37:31.922Z","creation":"2019-03-27T01:27:30Z"},"accession":"S-EPMC4007904","cross_references":{"pubmed":["24900223"],"doi":["10.1021/ml100087a"]}}