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4. Tat modifies the activity of CDK9 to phosphorylate serine 5 of the RNA polymerase II carboxyl-terminal domain during human immunodeficiency virus type 1 transcription. Zhou M; Halanski MA; Radonovich MF; Kashanchi F; Peng J; Price DH; Brady JN Mol Cell Biol; 2000 Jul; 20(14):5077-86. PubMed ID: 10866664 [TBL] [Abstract][Full Text] [Related]
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16. Direct evidence that HIV-1 Tat stimulates RNA polymerase II carboxyl-terminal domain hyperphosphorylation during transcriptional elongation. Isel C; Karn J J Mol Biol; 1999 Jul; 290(5):929-41. PubMed ID: 10438593 [TBL] [Abstract][Full Text] [Related]
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18. Phase-separation mechanism for C-terminal hyperphosphorylation of RNA polymerase II. Lu H; Yu D; Hansen AS; Ganguly S; Liu R; Heckert A; Darzacq X; Zhou Q Nature; 2018 Jun; 558(7709):318-323. PubMed ID: 29849146 [TBL] [Abstract][Full Text] [Related]
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20. Human cytomegalovirus infection induces specific hyperphosphorylation of the carboxyl-terminal domain of the large subunit of RNA polymerase II that is associated with changes in the abundance, activity, and localization of cdk9 and cdk7. Tamrakar S; Kapasi AJ; Spector DH J Virol; 2005 Dec; 79(24):15477-93. PubMed ID: 16306619 [TBL] [Abstract][Full Text] [Related] [Next] [New Search]