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Synthesis/biological evaluation of hydroxamic acids and their prodrugs as inhibitors for Botulinum neurotoxin A light chain.
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Synthesis and structure-activity relationships of second-generation hydroxamate botulinum neurotoxin A protease inhibitors.
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Strategies to Counteract Botulinum Neurotoxin A: Nature's Deadliest Biomolecule.
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Examination of α-exosite inhibitors against Botulinum neurotoxin A protease through structure-activity relationship studies of chicoric acid.
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Metal Ions Effectively Ablate the Action of Botulinum Neurotoxin A.
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Newly Designed Quinolinol Inhibitors Mitigate the Effects of Botulinum Neurotoxin A in Enzymatic, Cell-Based, and ex Vivo Assays.
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Picolinic acids as β-exosite inhibitors of botulinum neurotoxin A light chain.
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Probing BoNT/A protease exosites: implications for inhibitor design and light chain longevity.
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Benzoquinones as inhibitors of botulinum neurotoxin serotype A.
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Quinolinol and peptide inhibitors of zinc protease in botulinum neurotoxin A: effects of zinc ion and peptides on inhibition.
Arch Biochem Biophys. 2009 Nov;491(1-2):75-84. doi: 10.1016/j.abb.2009.09.008. Epub 2009 Sep 20.
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The strange case of the botulinum neurotoxin: using chemistry and biology to modulate the most deadly poison.
Angew Chem Int Ed Engl. 2008;47(44):8360-79. doi: 10.1002/anie.200705531.
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Exosites in the substrate specificity of blood coagulation reactions.
J Thromb Haemost. 2007 Jul;5 Suppl 1(Suppl 1):81-94. doi: 10.1111/j.1538-7836.2007.02496.x.
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Unique substrate recognition by botulinum neurotoxins serotypes A and E.
J Biol Chem. 2006 Apr 21;281(16):10906-11. doi: 10.1074/jbc.M513032200. Epub 2006 Feb 14.
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The evolving field of biodefence: therapeutic developments and diagnostics.
Nat Rev Drug Discov. 2005 Apr;4(4):281-97. doi: 10.1038/nrd1694.

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