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Details on Person Tat associates with the Cyclin T1 subunit of P-TEFb (Cyclin ...

Class:IdSummation:167896
_displayNameTat associates with the Cyclin T1 subunit of P-TEFb (Cyclin ...
_timestamp2006-01-15 13:13:57
created[InstanceEdit:167897] Matthews, L, 2005-11-10 09:49:07
literatureReference[LiteratureReference:167873] A novel CDK9-associated C-type cyclin interacts directly with HIV-1 Tat and mediates its high-affinity, loop-specific binding to TAR RNA
[LiteratureReference:170692] Lentivirus Tat proteins specifically associate with a cellular protein kinase, TAK, that hyperphosphorylates the carboxyl-terminal domain of the large subunit of RNA polymerase II: candidate for a Tat cofactor
[LiteratureReference:170731] Recruitment of a protein complex containing Tat and cyclin T1 to TAR governs the species specificity of HIV-1 Tat
[LiteratureReference:170751] The interaction between HIV-1 Tat and human cyclin T1 requires zinc and a critical cysteine residue that is not conserved in the murine CycT1 protein
modified[InstanceEdit:169255] Matthews, L, 2005-11-24 23:42:49
[InstanceEdit:170260] Matthews, L, 2006-01-03 21:42:30
[InstanceEdit:170768] Matthews, L, 2006-01-15 13:04:15
textTat associates with the Cyclin T1 subunit of P-TEFb (Cyclin T1:Cdk9) through a region of cysteine-rich and core sequences referred to as the ARM domain within Tat (Wei et al., 1998; see also Herrmann 1995). This interaction is believed to involve metal ions stabilized by cysteine residues in both proteins (Bieniasz et al., 1998; Garber et al., 1998).
(summation)[Reaction:167234] Association of Tat with P-TEFb(Cyclin T1:Cdk9) [Homo sapiens]
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