Ian M. Fingerman, Ph.D.

Affiliations: 
2003 Rutgers University, New Brunswick, New Brunswick, NJ, United States 
Area:
Molecular Biology
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"Ian Fingerman"
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Parents

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Andrew K. Vershon grad student 2003 Rutgers, New Brunswick
 (The role of SFP1 in ribosome biogenesis in the yeast Saccharomyces cerevisiae.)
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Publications

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Mersman DP, Du HN, Fingerman IM, et al. (2012) Charge-based interaction conserved within histone H3 lysine 4 (H3K4) methyltransferase complexes is needed for protein stability, histone methylation, and gene expression. The Journal of Biological Chemistry. 287: 2652-65
Fingerman IM, McDaniel L, Zhang X, et al. (2011) NCBI Epigenomics: a new public resource for exploring epigenomic data sets. Nucleic Acids Research. 39: D908-12
South PF, Fingerman IM, Mersman DP, et al. (2010) A conserved interaction between the SDI domain of Bre2 and the Dpy-30 domain of Sdc1 is required for histone methylation and gene expression. The Journal of Biological Chemistry. 285: 595-607
Plazas-Mayorca MD, Zee BM, Young NL, et al. (2009) One-pot shotgun quantitative mass spectrometry characterization of histones. Journal of Proteome Research. 8: 5367-74
Mersman DP, Du HN, Fingerman IM, et al. (2009) Polyubiquitination of the demethylase Jhd2 controls histone methylation and gene expression. Genes & Development. 23: 951-62
Fingerman IM, Du HN, Briggs SD. (2008) In vitro histone methyltransferase assay. Csh Protocols. 2008: pdb.prot4939
Du HN, Fingerman IM, Briggs SD. (2008) Histone H3 K36 methylation is mediated by a trans-histone methylation pathway involving an interaction between Set2 and histone H4. Genes & Development. 22: 2786-98
Fingerman IM, Du HN, Briggs SD. (2008) Controlling histone methylation via trans-histone pathways. Epigenetics. 3: 237-42
Fingerman IM, Li HC, Briggs SD. (2007) A charge-based interaction between histone H4 and Dot1 is required for H3K79 methylation and telomere silencing: identification of a new trans-histone pathway. Genes & Development. 21: 2018-29
Shi X, Kachirskaia I, Walter KL, et al. (2007) Proteome-wide analysis in Saccharomyces cerevisiae identifies several PHD fingers as novel direct and selective binding modules of histone H3 methylated at either lysine 4 or lysine 36. The Journal of Biological Chemistry. 282: 2450-5
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