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Spain-GR-GR Azienda Directories
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Azienda News:
- Specific interaction of Tat with the human but not rodent P . . .
Together, our data indicated that the specific interaction of human P-TEFb with Tat TAR, mostly through cyclin T1, is crucial for P-TEFb to mediate a Tat-specific and species-restricted activation of HIV-1 transcription
- P-TEFb: The master regulator of transcription elongation - PMC
What roles do different P-TEFb components (such as CycT2a and CycT2b as well as CDK9-55) play in development and tissues? How many transcription factors interact with P-TEFb directly or via the SEC? What roles do interactions between BRD4 and P-TEFb play in transcription elongation? Indeed, how well does chromatin bound BRD4 interact with P-TEFb?
- Requirement for a Kinase-specific Chaperone Pathway in the . . .
Our recent data indicate that the specific interaction of human but not rodent P-TEFb with HIV-1 Tat protein and TAR RNA to form a multicomponent ribonucleoprotein complex is crucial for P-TEFb to mediate a Tat-specific and species-restricted activation of HIV-1 transcription (5)
- The AFF4 scaffold binds human P-TEFb adjacent to HIV Tat
AFF4 is positioned to make unexpected direct contacts with HIV Tat, and Tat enhances P-TEFb affinity for AFF4 These studies define the mechanism of scaffold recognition by P-TEFb and reveal an unanticipated intersubunit pocket on the AFF4 SEC that potentially represents a target for therapeutic intervention against HIV AIDS
- HIV Tat P-TEFb Interaction: A Potential Target for Novel Anti . . .
In this review, we describe the molecular mechanism underlying how Tat activates viral transcription through interaction with P-TEFb We propose a novel therapeutic strategy against HIV replication through blocking Tat action
- The Control of HIV Transcription: Keeping RNA Polymerase II . . .
Here, we review advances in HIV transcription research with a focus on the growing family of cellular P-TEFb complexes, structural insights into the interactions between Tat, P-TEFb, and TAR RNA, and the multifaceted regulation of these interactions by posttranscriptional modifications of Tat
- Crystal structure of HIV-1 Tat complexed with human P-TEFb
Tat•P-TEFb interactions Interactions between Tat and P-TEFb can be divided into four areas (Figures 3a and 3b) The first area involves a U-shaped, acidic proline-rich region of Tat and a wide depression between the two cyclin repeats of Cyclin T1 The second area involves a β-turn in the acidic proline-rich region of Tat and the T-loop of
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