Kirill Tsirulnikov, Ph.D

My research interest is to understand how certain protein structures determine function.  I  have been involved in structurally characterizing the enzyme amynoacylase 3 that plays a key role in mediating toxicity of a common industrial contaminant trichloroethylene. The atomic structure of the enzyme complexed with substrates was solved to 2A resolution (PNAS ) and is now used for generation of highly specific inhibitors.  I am using my experience in the crystallography study of the SLC4 transporters and their bacterial homologues.





Recent and Selected Publications

Hsieh JM, Tsirulnikov K, Sawaya MR, Magilnick N, Abuladze N, Kurtz I, Abramson J, Pushkin A. Structures of aminoacylase 3 in complex with acetylated substrates. Proc Natl Acad Sci U S A. 2010 Oct 19;107(42):17962-7.  PMID: 20921362

Tsirulnikov K, Abuladze N, Koag MC, Newman D, Scholz K, Bondar G, Zhu Q, Avliyakulov NK, Dekant W, Faull K, Kurtz I, Pushkin A. Transport of N-acetyl-S-(1,2-dichlorovinyl)-L-cysteine, a metabolite of trichloroethylene, by mouse multidrug resistance associated protein 2 (Mrp2). Toxicol Appl Pharmacol. 2010 Apr 15;244(2):218-25. PMID: 20060011

Tsirulnikov K, Abuladze N, Newman D, Ryazantsev S, Wolak T, Magilnick N, Koag MC, Kurtz I, Pushkin A. Mouse aminoacylase 3: a metalloenzyme activated by cobalt and nickel. Biochim Biophys Acta. 2009 Jul;1794(7):1049-57.  PMID: 19362172