The leukemogenic AF4-MLL fusion protein causes P-TEFb kinase activation and altered epigenetic signatures.
Benedikt
A
A
Institute of Pharmaceutical Biology/ZAFES, Goethe-University of Frankfurt, Biocenter, Frankfurt/Main, Germany.
Baltruschat
S
S
Scholz
B
B
Bursen
A
A
Arrey
T N
TN
Meyer
B
B
Varagnolo
L
L
Müller
A M
AM
Karas
M
M
Dingermann
T
T
Marschalek
R
R
D002850:Chromatography, Gel; D004268:DNA-Binding Proteins / Q000302:isolation & purification / Q000502:physiology*; D004789:Enzyme Activation; D044127:Epigenesis, Genetic; D000076983:Histone Methyltransferases; D011495:Histone-Lysine N-Methyltransferase / Q000378:metabolism; D006657:Histones / Q000378:metabolism; D006801:Humans; D007938:Leukemia / Q000209:etiology*; D008745:Methylation; D051788:Myeloid-Lymphoid Leukemia Protein / Q000302:isolation & purification / Q000502:physiology*; D009687:Nuclear Proteins / Q000302:isolation & purification / Q000502:physiology*; D015514:Oncogene Proteins, Fusion / Q000302:isolation & purification / Q000502:physiology*; D010766:Phosphorylation; D042925:Positive Transcriptional Elongation Factor B / Q000378:metabolism*; D035602:Transcriptional Elongation Factors
D004268:DNA-Binding Proteins; D006657:Histones; C497422:KMT2A protein, human; D009687:Nuclear Proteins; D015514:Oncogene Proteins, Fusion; D035602:Transcriptional Elongation Factors; D051788:Myeloid-Lymphoid Leukemia Protein; C081449:AFF1 protein, human; D000076983:Histone Methyltransferases; D011495:Histone-Lysine N-Methyltransferase; D042925:Positive Transcriptional Elongation Factor B