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ACS Chemical Biology|August 29, 2022
<i>Clostridioides difficile</i> TcdB Toxin Glucosylates Rho GTPase by an S<sub>N</sub><i>i</i> Mechanism and Ion Pair Transition StateAshleigh S Paparella, Sean M Cahill, Briana L Aboulache, et al.
Antibiotics (Basel, Switzerland)|July 28, 2016
Biotin Protein Ligase Is a Target for New AntibacterialsJiage Feng, Ashleigh S Paparella, Grant W Booker, et al.
Nature Communications|November 2, 2021
Inhibition of Clostridium difficile TcdA and TcdB toxins with transition state analoguesAshleigh S Paparella, Briana L Aboulache, Rajesh K Harijan, et al.
Biorxiv : the Preprint Server for Biology|February 6, 2026
First inhibitor of a bacterial two-partner secretion systemAlfred Hartojo, Laurence Don Wai Luu, Lachlan Adamson, et al.
ACS Medicinal Chemistry Letters|December 21, 2016
New Series of BPL Inhibitors To Probe the Ribose-Binding Pocket of <i>Staphylococcus aureus</i> Biotin Protein LigaseJiage Feng, Ashleigh S Paparella, William Tieu, et al.
ACS Infectious Diseases|February 9, 2024
Isofagomine Inhibits Multiple TcdB Variants and Protects Mice from <i>Clostridioides difficile</i>-Induced MortalityAshleigh S Paparella, Isabella Brew, Huynh A Hong, et al.
Biorxiv : the Preprint Server for Biology|October 2, 2023
Isofagomine inhibits multiple TcdB variants and protects mice from <i>Clostridioides difficile</i> induced mortalityAshleigh S Paparella, Isabella Brew, Huynh A Hong, et al.
Current Topics in Medicinal Chemistry|November 19, 2013
Structure guided design of biotin protein ligase inhibitors for antibiotic discoveryAshleigh S Paparella, Tatiana P Soares da Costa, Min Y Yap, et al.
Bioorganic & Medicinal Chemistry Letters|September 7, 2014
Heterocyclic acyl-phosphate bioisostere-based inhibitors of Staphylococcus aureus biotin protein ligaseWilliam Tieu, Angie M Jarrad, Ashleigh S Paparella, et al.
ACS Infectious Diseases|November 14, 2017
Halogenation of Biotin Protein Ligase Inhibitors Improves Whole Cell Activity against Staphylococcus aureusAshleigh S Paparella, Kwang Jun Lee, Andrew J Hayes, et al.
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