Pflum Group Laboratory
Bioorganic Chemistry

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Mary Kay H. Pflum
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Newly Renovated Pflum Lab

Open Position: Postdoctoral Research Associate

A.Paul Schaap Chemistry Building Tour

 Latest News

Geetha's paper reporting the ELISA-based HDAC activity assay for Characterization of Isoform-Selective Inhibitors was published at Journal of Biomolecular Screening ...more>>

Fouda's paper was chosen as a VIP at Angewandte Chemie International Edition ...more>>

Ahmed E. Fouda's paper reporting a cell permeable ATP analog was published at Angewandte Chemie International Edition ...more>>

Inosha Gomes joined the lab ...more>>


 
Publications

Dedigama-Arachchige P. M. and Pflum, M. K. H., K-CLASP: A tool to identify phosphosite specific kinases and interacting proteins, ACS Chemical Biology, Articles ASAP.

Bieliauskas A. V., Weerasinghe, S. V. W., Negmeldin, A., and Pflum, M. K. H., The structural requirements of histone deacetylase inhibitors: SAHA analogs modified on the hydroxamic acid, Arch de Pharm, 2016, 349, 373-382.

Senevirathne, C., Embogama D. M., Anthony, T. M., Fouda A. E., and Pflum, M. K. H, The Generality of Kinase-Catalyzed Labeling, Bioorg Med Chem, 2016, 24, 12-19.

Thilani M. Anthony, Pavithra M. Dedigama Arachchige, D. Maheeka Embogama, Todd R. Faner, Ahmed E. Fouda, and Mary Kay H. Pflum (2015). ATP analogs in protein kinase research. Kinomics: Approaches and Applications. Heinz-Bernhard Kraatz, Sanela Martic, Eds. Wiley-VCH Verlag GmbH. ISBN: 978352733765.

Fouda, A. E, and Pflum, M. K. H, A Cell Permeable ATP analog, Angewante Chemie. 2015, 54, 9618-9621.

Padige G., Negmeldin A. T., and Pflum, M. K. H, Development of an ELISA-based HDAC Activity Assay for Characterization of Isoform-Selective Inhibitors, J. Biomolecular Screening, 2015, 20, 1277-1285.

Garre, S., Senevirathne, C., Pflum, M. K. H, A comparative study of ATP analogs for phosphorylation-dependent kinase–substrate crosslinking, Bioorg. Med. Chem. 2014, 22, 1620-1625.

Wambua, M., Nalawansha, D., Negmeldin, A., and Pflum, M. K. H, Mutagenesis Studies of the 14 Å Internal Cavity of Histone Deacetylase 1: Insights towards the Acetate Escape Hypothesis and Selective Inhibitor Design, J. Med. Chem. 2014, 57, 642–650.

Senevirathne, C. and Pflum, M. K. H, Biotinylated phosphoproteins from kinase-catalyzed biotinylation are stable to phosphatases: Implications for phosphoproteomics, ChemBioChem, 2013, 14, 381-387.

Suwal, S, Senevirathne, C., Garre S, and Pflum, M. K. H, Structural Analysis of ATP Analogs Compatible with Kinase-Catalyzed Labeling, Bioconjugate Chem. 2012, 23, 2386-2391.

Choi, S. E., and Pflum, M. K. H, The structural requirements of histone deacetylase inhibitors: Suberoylanilide hydroxamic acid analogs modified at the C6 position, Bioorg. Med. Chem. Lett. 2012, 22, 7084-7086.

Senevirathne, C and Pflum, M. K. H, Kinase-catalyzed biotinylation of peptides, proteins, and lysates, Protocols in Chem. Biol., 2012, 4, 1.

Choi, S. E., Weerasinghe, S. V. W., Pflum, M. K. H, The structural requirements of histone deacetylase inhibitors: Suberoylanilide hydroxamic acid analogs modified at the C3 position display isoform selectivity, 2011, 21, 6139-42.

Weerasinghe S. V., Wambua M., Pflum, M. K. H, A histone deacetylase-dependent screen in yeast, Bioorg. Med. Chem. Lett., 2010, 18 (21), 7586-7592.

Suwal S., and Pflum, M. K. H, Phosphorylation-Dependent Kinase-Substrate Cross-Linking, Angew. Chem. Int. Ed., 2010, 49 (9), 1627-1630. Article highlighted in: Chem & Eng News, 2010, 88, 48.

Green K. D. and Pflum, M. K. H, Exploring Kinase Cosubstrate Promiscuity: Kinase-catalyzed dansylation for monitoring kinase activity, J. Am. Chem. Soc. 2009, 10, 234-237.

Weerasinghe S. V., Estui G., Wiest O., and Pflum, M. K. H, Residues in the 11Å channel of histone deacetylase 1 promote catalytic activity, J. Med. Chem. 2008, 1 (18), 5542-5551.

Bieliauskas A. V. and Pflum, M. K. H, Isoform-selective HDAC inhibitors, Chem. Soc. Rev. 2008, 37, 1402-1413.

Singh E. K., Ravula S., Pan C., Pan P., Vasko R. C., Lapera S. A., Pflum, M. K. H, S. R. McAlpine, Synthesis and biological evaluation of histone deacetylase inhibitors that are based on the FR235222 scaffold, Bioorg. Med Chem Lett.2008, 18, 2549-2554.

Karwowska-Desaulniers P., Ketko A., Kamath N., and Pflum, M. K. H, Histone Deacetylase 1 phosphorylation at S421 and S423 is constitutive in vivo, but dispensable in vitro, Biochem. Biophys. Res. Comm., 2007, 361, 349-355.

Bieliauskas A. V., Weerasinghe S. V., Pflum, M. K. H, Structural Requirements of HDAC Inhibitors: SAHA Analogs Functionalized Adjacent to the Hydroxamic Acid, Bioorg. Med. Chem. Lett. 2007, 17, 2216-2219.

Green K. D. and Pflum, M. K. H., Kinase-Catalyzed Biotinylation for Phosphoprotein Detection, J. Am. Chem. Soc., 2007, 129, 10-11.link Article highlighted in: ACS Chemical Biology, 2007, 2, 85.

Warthaka M., Karwowska-Desaulniers P., and Pflum, M. K. H, Phosphopeptide Modification and Enrichment By Oxidation-Reduction Condensation, ACS Chemical Biology, 2006, 1, 697-701.

Kamath N., Karwowska-Desaulniers P., Pflum, M. K. H, Limited Proteolysis of Histone Deacetylase 1, BMC Biochemistry, 2006, 7, 22.

Flammer J., Popova K., and Pflum, M. K. H Cyclic AMP Response Element-Binding Protein (CREB) and CAAT/Enhancer-Binding Protein beta (C/EBPbeta) Bind Chimeric DNA Sites with High Affinity, Biochemistry, 2006, 45, 9615-23.

Invited Review Articles

Publications while at Wayne State University (2001-present)

A. V. Bieliauskas and M. K. H. Pflum, Isoform-selective HDAC inhibitors, Chem. Soc. Rev. 2008, 37, 1402-1413.

H-NS gives invading DNA the silent treatment M. K. H. Pflum, Nature Chem. Biol., 2006, 2, 400-401.

Miniature DNA Binding Proteins. M. K. H. Pflum, Chemistry and Biology, 2004, 11, 3-4.

 

 

 

 

 

 

 

 

 

 

 

 

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