PARP1 and CBP lose their footing in cancer.
Department of Physiological Chemistry, Butenandt Institute and Ludwig-Maximilians-University Biomedical Center, Ludwig-Maximilians-University of Munich, Munich, Germany.
Gyula
G
Timinszky
Department of Physiological Chemistry, Butenandt Institute and Ludwig-Maximilians-University Biomedical Center, Ludwig-Maximilians-University of Munich, Munich, Germany.
Andreas G
AG
Ladurner
D015972:Gene Expression Regulation, Neoplastic; D006657:Histones / Q000235:genetics*; D006801:Humans; D010446:Peptide Fragments / Q000235:genetics*; D000071137:Poly (ADP-Ribose) Polymerase-1; D011065:Poly(ADP-ribose) Polymerases / Q000235:genetics*; D012795:Sialoglycoproteins / Q000235:genetics*; D014158:Transcription, Genetic
D006657:Histones; D010446:Peptide Fragments; D012795:Sialoglycoproteins; C571744:bone sialoprotein (35-62), human; C120756:macroH2A histone; C499320:PARP1 protein, human; D000071137:Poly (ADP-Ribose) Polymerase-1; D011065:Poly(ADP-ribose) Polymerases