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{"target":"http://pubannotation.org/docs/sourcedb/PMC/sourceid/6172693","sourcedb":"PMC","sourceid":"6172693","source_url":"https://www.ncbi.nlm.nih.gov/pmc/6172693","text":"Figure 5 A Technique to Rapidly Analyze ADP-Ribosylated Peptides\n(A) Schematic representation of the approach to rapidly and easily analyze the modification status of positively charged histone tail peptides.\n(B) Imperial stained gel showing ADPr of H3 (1–21aa) peptides after addition of PARP1/HPF1 during a 6-hr time course. The upward band shift denotes ADPr of the H3 peptide.\n(C) Imperial stained gel showing ADPr of H3 (1–21aa) peptides after addition of PARP1/HPF1 and subsequent addition of ARH3. The upward band shift denotes ADPr of the H3 peptide.\n(D) Imperial stained gel showing H3 (1–21aa) WT, K4me1, K4me2, K4me3, R8me1, R8me2a, K9ac, K9me1, K9me2, K9me3, S10ph, T11ph, and K14ac peptides and subsequent ADPr following addition of PARP1 and HPF1. The upward band shift denotes ADPr of the H3 peptide.\n(E) A schematic showing a map of histone H3 1–20aa with histone marks that interfere with Ser-ADPr on H3 peptide in vitro.","tracks":[]}