Harmeyer, K., South, P., Bishop, B., Ogas, J., & Briggs, S. (2014). Immediate chromatin immunoprecipitation and on-bead quantitative PCR analysis: a versatile and rapid ChIP procedure. Nucleic Acids Res, pii: gku1347. Retrieved from http://nar.oxfordjournals.org/content/early/2015/01/29/nar.gku1347.full.pdf+html
South, P., Harmeyer, K., Serratore, N., & Briggs, S. (2013). H3K4 methyltransferase Set1 is involved in maintenance of ergosterol homeostasis and resistance to Brefeldin A. Proc. Natl. Acad. Sci. U.S.A, 11, E1016-E1025. Retrieved from http://www.pnas.org/cgi/pmidlookup?view=long&pmid=23382196
Mersman, D., Du, H., Fingerman, I., & South, S. (2012). Charge-based interaction conserved within hisone H3 lysine 4 (H3K4) methyltransferase complexes is needed for protein stability, histone methylation, and gene expression. J. Biol. Chem, 287, 2652-2665. Retrieved from http://www.jbc.org/content/287/4/2652.full.pdf+html
South, P. (2011). ASH2L (ash2 (absent, small, or homeotic)-like (Drosophila)) Atlas of Genetics and Cytogenetics in Oncology and Haematology, N/A. Retrieved from http://atlasgeneticsoncology.org/Genes/ASH2LID44404ch8p11.html
Mersman, D., Du, H., Fingerman, I., & South, P. (2011). Charge-based Interaction Conserved within Histone H3 Lysine 4 (H3K4) Methyltransferase Complexes is needed for Protien Stability, Histone Methylation, and Gene Expression. Journal of Biological Chemistry, 287(4), 2652-2665.
South, P. (2011). Understanding the Structure and Function of ASH2L. Atlas of Genetics and Cytogenetics in Oncology and Haematology, N/A. Retrieved from http://atlasgeneticsoncology.org//Deep/ASH2LFunctionID20097.html
South, P., Fingerman, I., Mersman, D., & Du, H. (2010). A conserved interaction between the SDI domain of Bre2 and the Dpy-3- Domain of Sdc1 is required for histone methylation and gene expression. J. Biol. Chem, 285(1), 595-607. Retrieved from http://www.jbc.org/content/285/1/595.full.pdf+html
Du, H. (2010). A nucleosome surface formed by histone H4, H2A, and H3 residues is needed for proper histone H3 Lys36 methylation, histone acetylation, and repression of cryptic transcription. J. Biol. Chem, 285, 11704-11713. Retrieved from http://www.jbc.org/content/285/15/11704.full.pdf+html
Dhawan, R., Luo, H., Foerster, A., AbuQamar, S., Du, H., Briggs, S., . . . Mengiste, T. (2009). HISTONE MONOUBIQUITINATION 1 interacts with a subunit of the mediator complex and regulates defense responses against necrotrophic fungal pathogens. Plant Cell, 21, 1000-1019.