Publications

  • Beltman, Rachel, and Mary Kay Pflum. “Kinase-Catalyzed Crosslinking and Immunoprecipitation (K-CLIP) to Explore Kinase-Substrate Pairs”, Curr. protoc. chem. biol., 2022. http://dx.doi.org/10.1002/cpz1.539
  • Zhang, Yuchen, Andrade, Rafael, Hanna, Anthony A, and Mary Kay H. Pflum. “Evidence that HDAC7 acts as an epigenetic “reader” of AR acetylation through NCoR-HDAC3 dissociation”, Cell Chem. Biol., 2022. https://doi.org/10.1016/j.chembiol.2022.05.008
  • Ramanayake-Mudiyanselage, Vinyda, Embogama DM, and Mary Kay H. Pflum. “Kinase-Catalyzed Biotinylation to Map Cell Signaling Pathways: Application to Epidermal Growth Factor Signaling”, J. Proteomics Research, 2021. https://pubs.acs.org/doi/10.1021/acs.jproteome.1c00562
  • Al-Hamashi AA, Koranne R, Dlamini S, Alqahtani A, Karaj E, Rashid MS, Knoff JR, Dunworth M, Pflum MKH, Casero RA Jr, Perera L, Taylor WR, Tillekeratne LMV. “A new class of cytotoxic agents targets tubulin and disrupts  microtubule dynamics”, Bioorganic Chemistry, 2021, 116, 105297, https://doi.org/10.1016/j.bioorg.2021.105297
  • Gomes, Inosha D, Ariyaratne, Udana V, and Mary Kay H. Pflum. “HDAC6 Substrate Discovery Using Proteomics-Based Substrate Trapping: HDAC6 Deacetylates PRMT5 to Influence Methyltransferase Activity” ACS Chemical Biology, 2021, 16, 1435-1444. https://pubs.acs.org/doi/10.1021/acschembio.1c00303
  • Bahl, Sonali, Ling, Hongbo, Acharige, Nuwan PN, Santos-Barriopedro, Irene, Mary Kay H. Pflum, and Edward Seto. “EGFR phosphorylates HDAC1 to regulate its expression and anti-apoptotic function” Cell Death and Disease, 2021, 12, 469. https://www.nature.com/articles/s41419-021-03697-6
  • Zhang, Yuchen, Nalawansha, Dhanusha A, Herath, Kavitha E, Andrade, Rafael, and Mary Kay H. Pflum. “Differential Profiles of HDAC1 substrates and associated proteins in breast cancer cells revealed by trapping” Molecular Omics, 2021, 17, 544-533. https://pubs.rsc.org/en/content/articlelanding/2021/MO/D0MO00047G
  • *Fouda, Ahmed E, *Gamage, Aparni K, Mary Kay H. Pflum. “An Affinity-Based, Cysteine-Specific ATP Analog for Kinase-Catalyzed Crosslinking” Angewante Chem Int Ed, 2021, 60, 9859-9862. *co-first authors, https://onlinelibrary.wiley.com/doi/10.1002/anie.202014047
  • Acharige, Nuwan PN, and Mary Kay H. Pflum. “Identification of L‐lactate Dehydrogenase as a Protein Tyrosine Phosphatase 1B substrate using K‐BIPS.” ChemBioChem, 2021, 22, 186-192.Link
  • Gomes, Inosha D., and Mary Kay H. Pflum. “Optimal Substrate‐Trapping Mutants to Discover Substrates of HDAC1.” ChemBioChem, 2019, 20, 1444-1449.Link
  • Nalawansha, Dhanusha A., Yuchen Zhang, Kavinda Herath, and Mary Kay H. Pflum. “HDAC1 Substrate Profiling Using Proteomics-Based Substrate Trapping.” ACS Chemical Biology, 2018, 13, 3315-3324.Link
  • Anthony, Thilani M., and Mary Kay H. Pflum. “Kinase-catalyzed biotinylation of DNA.” Bioorganic & Medicinal Chemistry, 2018, 26, 2331-2336. Link
  • Dedigama-Arachchige, Pavithra M., Nuwan PN Acharige, and Mary Kay H. Pflum. “Identification of PP1–Gadd34 substrates involved in the unfolded protein response using K-BIPS, a method for phosphatase substrate identification.” Molecular Omics, 2018, 14, 121-133. Link
  • Negmeldin, Ahmed T., Joseph R. Knoff, and Mary Kay H. Pflum. “The structural requirements of histone deacetylase inhibitors: C4-modified SAHA analogs display dual HDAC6/HDAC8 selectivity.” European Journal of Medicinal Chemistry, 2018, 143, 1790-1806. Link
  • Embogama D. Makeeka and Mary Kay H. Pflum. “K-BILDS: A Kinase Substrate Discovery Tool” Chembiochem, 2017, 18, 136-141. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5458359/
  • Nalawansha, Dhanusha A., Inosha D. Gomes, Magdalene K. Wambua, and Mary Kay H. Pflum. “HDAC inhibitor-induced mitotic arrest is mediated by Eg5/Kif11 acetylation.” Cell Chemical Biology, 2017, 24, 481-492. Link
  • Negmeldin, Ahmed T., Geetha Padige, Anton V. Bieliauskas, and Mary Kay H. Pflum. “Structural requirements of HDAC inhibitors: SAHA analogues modified at the C2 position display HDAC6/8 selectivity.” ACS Medicinal Chemistry Letters, 2017, 8, 281-286. Link
  • Nalawansha, Dhanusha A., and Mary Kay H. Pflum. “LSD1 substrate binding and gene expression are affected by HDAC1-mediated deacetylation.” ACS Chemical Biology, 2017, 12, 254-264. Link
  • Dedigama-Arachchige, Pavithra M., and Mary Kay H. Pflum. “K-CLASP: a tool to identify phosphosite specific kinases and interacting proteins.” ACS Chemical Biology, 2016, 11, 3251-3255. Link
  • Bieliauskas, Anton V., Sujith VW Weerasinghe, Ahmed T. Negmeldin, and Mary Kay H. Pflum. “Structural requirements of histone deacetylase inhibitors: SAHA analogs modified on the hydroxamic acid.” Archiv der Pharmazie, 2016, 349, 373-382.Link
  • Senevirathne, Chamara, D. Maheeka Embogama, Thilani A. Anthony, Ahmed E. Fouda, and Mary Kay H. Pflum. “The generality of kinase-catalyzed biotinylation.” Bioorganic & Medicinal Chemistry, 2016, 24, 12-19. Link
  • Anthony, Thilani M., Pavithra M. Dedigama-Arachchige, D. Maheeka Embogama, Todd R. Faner, Ahmed E. Fouda, and Mary Kay H. Pflum. “ATP analogs in protein kinase research.” Kinomics: Approaches and Applications (eds H.-B. Kraatz and S. Martic. Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim, Germany (2015). Link
  • Fouda, Ahmed E., and Mary Kay H. Pflum. “A cell‐permeable ATP analogue for kinase‐catalyzed biotinylation.” Angewandte Chemie International Edition, 2015, 54, 9618-9621. Link
  • Padige, Geetha, Ahmed T. Negmeldin, and Mary Kay H. Pflum. “Development of an ELISA-based HDAC activity assay for characterization of isoform-selective inhibitors.” Journal of Biomolecular Screening, 2015, 20, 1277-1285. Link
  • Garre, Satish, Chamara Senevirathne, and Mary Kay H. Pflum. “A comparative study of ATP analogs for phosphorylation-dependent kinase–substrate crosslinking.” Bioorganic & Medicinal Chemistry, 2014, 22, 1620-1625. Link
  • Wambua, Magdalene K., Dhanusha A. Nalawansha, Ahmed T. Negmeldin, and Mary Kay H. Pflum. “Mutagenesis studies of the 14 Å internal cavity of histone deacetylase 1: insights toward the acetate-escape hypothesis and selective inhibitor design.” Journal of Medicinal Chemistry, 2014, 57, 642-650. Link
  • Senevirathne, Chamara, and Mary Kay H. Pflum. “Biotinylated phosphoproteins from kinase-catalyzed biotinylation are stable to phosphatases: implications for phosphoproteomics.” Chembiochem, 2013, 14, 381. Link
  • Suwal, Sujit, Chamara Senevirathne, Satish Garre, and Mary Kay H. Pflum. “Structural analysis of ATP analogues compatible with kinase-catalyzed labeling.” Bioconjugate Chemistry, 2012, 23, 2386-2391. Link
  • Choi, Sun Ea, and Mary Kay H. Pflum. “The structural requirements of histone deacetylase inhibitors: Suberoylanilide hydroxamic acid analogs modified at the C6 position.” Bioorganic & Medicinal Chemistry Letters, 2012, 22, 7084-7086. Link
  • Senevirathne, Chamara, Keith D. Green, and Mary Kay H. Pflum. “Kinase‐Catalyzed Biotinylation of Peptides, Proteins, and Lysates.” Current Protocols in Chemical Biology, 2012, 4, 83-100. Link
  • Weerasinghe, Sujith VW, Magdalene Wambua, and Mary Kay H. Pflum. “A histone deacetylase-dependent screen in yeast.” Bioorganic & Medicinal Chemistry, 2010, 18, 7586-7592. Link
  • Suwal, Sujit, and Mary Kay H. Pflum. “Phosphorylation‐Dependent Kinase–Substrate Cross‐Linking.” Angewandte Chemie International Edition, 2010, 49, 1627-1630. Link
  • Green, Keith D., and Mary Kay H. Pflum. “Exploring kinase cosubstrate promiscuity: monitoring kinase activity through dansylation.” ChemBioChem, 2009, 10, 234-237. Link
  • Weerasinghe, Sujith VW, Guillermina Estiu, Olaf Wiest, and Mary Kay H. Pflum. “Residues in the 11 Å channel of histone deacetylase 1 promote catalytic activity: Implications for designing isoform-selective histone deacetylase inhibitors.” Journal of Medicinal Chemistry, 2008, 51, 5542-5551. Link
  • Bieliauskas, Anton V., and Mary Kay H. Pflum. “Isoform-selective histone deacetylase inhibitors.” Chemical Society Reviews, 2008, 37, 1402-1413. Link
  • Singh, Erinprit K., Suchitra Ravula, Chung-Mao Pan, Po-Shen Pan, Robert C. Vasko, Stephanie A. Lapera, Sujith VW Weerasinghe, Mary Kay H. Pflum, and Shelli R. McAlpine. “Synthesis and biological evaluation of histone deacetylase inhibitors that are based on FR235222: A cyclic tetrapeptide scaffold.” Bioorganic & Medicinal Chemistry Letters, 2008, 18, 2549-2554. Link
  • Karwowska-Desaulniers, Paulina, Anastasia Ketko, Nayana Kamath, and Mary Kay H. Pflum. “Histone deacetylase 1 phosphorylation at S421 and S423 is constitutive in vivo, but dispensable in vitro.” Biochemical and Biophysical Research Communications, 2007, 361, 349-355. Link
  • Bieliauskas, Anton V., Sujith VW Weerasinghe, and Mary Kay H. Pflum. “Structural requirements of HDAC inhibitors: SAHA analogs functionalized adjacent to the hydroxamic acid.” Bioorganic & Medicinal Chemistry Letters, 2007, 17, 2216-2219. Link
  • Green, Keith D., and Mary Kay H. Pflum. “Kinase-catalyzed biotinylation for phosphoprotein detection.” Journal of the American Chemical Society, 2007, 129, 10-11. Link
  • Warthaka, Mangalika, Paulina Karwowska-Desaulniers, and Mary Kay H. Pflum. “Phosphopeptide Modification and Enrichment by Oxidation–Reduction Condensation.” ACS Chemical Biology, 2006, 1, 697-701. Link
  • Kamath, Nayana, Paulina Karwowska-Desaulniers, and Mary Kay H. Pflum. “Limited proteolysis of human histone deacetylase 1.” BMC Biochemistry, 2006, 7, 1-14. Link
  • Flammer, Jamie R., Katerina N. Popova, and Mary Kay H. Pflum. “Cyclic AMP response element-binding protein (CREB) and CAAT/enhancer-binding protein β (C/EBPβ) bind chimeric DNA sites with high affinity.” Biochemistry, 2006, 45, 9615-9623. Link
  • Mary Kay H. Pflum, “H-NS gives invading DNA the silent treatment.” Nature Chemical Biology, 2006, 2, 400-401. Link
  • Mary Kay H. Pflum, “Grafting miniature DNA binding proteins.” Chemistry & Biology, 2004, 11, 3-4. Link