anti-Transcription Elongation Factor B (SIII), Polypeptide 2 (18kDa, Elongin B) (TCEB2) Antibodies

Mouse (Murine) Transcription Elongation Factor B (SIII), Polypeptide 2 (18kDa, Elongin B) (TCEB2) interaction partners

1. EPOP (E130012A19Rik) functionally links elongin B, elongin C, and polycomb in pluripotent stem cells.

2. EPOP (E130012A19Rik) interacts with elongin B, elongin C, and USP7 to modulate the chromatin landscape.

3. Crystal structure shows interaction between SOCS2-elongin BC and Cullin-5.

4. both P-TEFb activity and H1 phosphorylation are necessary for the full differentiation of C2C12 myoblasts into myotubes.

5. Elongin B/C recruitment regulates substrate binding by CIS

6. SOCS box acts as an independent binding domain capable of recruiting elonginBC and cullin5 to promote E3 ligase formation.

Human Transcription Elongation Factor B (SIII), Polypeptide 2 (18kDa, Elongin B) (TCEB2) interaction partners

1. Study shows that TCEB2 is involved in the development of acquired resistance to bevacizumab in ovarian cancer cells via the mechanisms of suppression of VEGF-A expression by promoting HIF-1alpha degradation and induction of interleukin-8 (IL-8) expression.

2. crystals of SOCS2 in complex with its adaptor proteins, Elongin C and Elongin B, underwent a change in crystallographic parameters when treated with dimethyl sulfoxide during soaking experiments.

3. The crystal structure of VHL bound to a Cul2 N-terminal domain, Elongin B, and Elongin C.

4. Vif interaction with EloB-EloC may contribute to recruitment of CBF-beta to Vif, demonstrating that the EloB C-teminus may play a role in improving Vif function and that the over-expression of EloB results in Vif stabilization.

5. ASB9 is unstable alone but forms a stable ternary complex with EloBC that binds with high affinity to the Cullin 5 N-terminal domain.

6. Elongin B also enhances gene expression from the double-stranded DNA genome of human cytomegalovirus.

7. Recombinant full-length Vif interacted with the Elongin BC complex in vitro with a K(d) of 1.9 muM and resulted in observable changes in deuterium uptake in both Elongin C and B.

8. findings report that HIV-1 Vif interacts with cellular proteins Cul5, elongins B and C, and Rbx1 to form an Skp1-cullin-F-box (SCF)-like complex

9. show that ASB2, by interacting with the Elongin BC complex, can assemble with Cullin5.Rbx1 to form an E3 ubiquitin ligase complex that stimulates polyubiquitination by the E2 ubiquitin-conjugating enzyme Ubc5

10. the E3 ubiquitin ligase activity of the Vif-BC-Cul5 complex is essential for Vif function against APOBEC3G

11. Results describe the 1.9-A crystal structure of the ternary complex of SOCS2 with elongin C and elongin B.

12. nuclear level of active P-TEFb is controlled by dynamic and reversible remodelling of 7SK snRNP

13. Elongin B/C recruitment regulates substrate binding by CIS