Solution structure of RING finger-like domain of retinoblastoma-binding protein-6 (RBBP6) suggests it functions as a U-box
MA Kappo, AB Eiso, F Hassem, RA Atkinson… - Journal of Biological …, 2012 - ASBMB
Retinoblastoma-binding protein-6 (RBBP6) plays a facilitating role, through its RING finger-
like domain, in the ubiquitination of p53 by Hdm2 that is suggestive of E4-like activity …
like domain, in the ubiquitination of p53 by Hdm2 that is suggestive of E4-like activity …
Retinoblastoma binding protein 6, another p53 monitor
M Ntwasa - Trends in cancer, 2016 - cell.com
The retinoblastoma binding protein 6 (RBBP6), a p53 negative regulator, is essential for
embryonic development. Its loss-of-function phenotype is similar to mouse double minute …
embryonic development. Its loss-of-function phenotype is similar to mouse double minute …
[HTML][HTML] Crystal structure of human retinoblastoma binding protein 9 (RBBP9)
SM Vorobiev, M Su, J Seetharaman, YJ Huang… - Proteins, 2009 - ncbi.nlm.nih.gov
As a step towards better integrating protein three-dimensional (3D) structural information in
cancer systems biology, the Northeast Structural Genomics Consortium (NESG)(www. nesg …
cancer systems biology, the Northeast Structural Genomics Consortium (NESG)(www. nesg …
RBBP6 interacts with multifunctional protein YB-1 through its RING finger domain, leading to ubiquitination and proteosomal degradation of YB-1
RBBP6 (retinoblastoma binding protein 6) is a 250-kDa multifunctional protein that interacts
with both p53 and pRb and has been implicated in mRNA processing. It has also been …
with both p53 and pRb and has been implicated in mRNA processing. It has also been …
Expression and function of retinoblastoma binding protein 6 (RBBP6) in human lung cancer
LR Motadi, KD Bhoola, Z Dlamini - Immunobiology, 2011 - Elsevier
Retinoblastoma binding protein 6 (RBBP6) interacts with both p53 and pRb, and has been
identified as an E3 ubiquitin ligase due to the presence of a RING finger domain. RBBP6 …
identified as an E3 ubiquitin ligase due to the presence of a RING finger domain. RBBP6 …
The Drosophila RetinoblastomaBinding Protein 6 Family Member Has Two Isoformsand Is Potentially Involved in Embryonic Patterning
R Hull, B Oosthuysen, UF Cajee, L Mokgohloa… - International journal of …, 2015 - mdpi.com
The human retinoblastoma binding protein 6 (RBBP6) is implicated in esophageal, lung,
hepatocellular and colon cancers. Furthermore, RBBP6 was identified as a strong marker for …
hepatocellular and colon cancers. Furthermore, RBBP6 was identified as a strong marker for …
Negative regulation of p53 by the long isoform of ErbB3 binding protein Ebp1 in brain tumors
Abstract The ErbB3 binding protein Ebp1 has been implicated in a number of human
cancers. Ebp1 includes 2 isoforms, p48 and p42, that exhibit different cellular activities. Here …
cancers. Ebp1 includes 2 isoforms, p48 and p42, that exhibit different cellular activities. Here …
Solution structure of the Hdm2 C2H2C4 RING, a domain critical for ubiquitination of p53
Regulation of the transcriptional response to the tumor suppressor p53 occurs at many
levels, including control of its transcriptional activity, and of its stability and concentration …
levels, including control of its transcriptional activity, and of its stability and concentration …
De-regulation of the RBBP6 isoform 3/DWNN in human cancers
Abstract Retinoblastoma binding protein 6 (RBBP6) is a nuclear protein, previously
implicated in the regulation of cell cycle and apoptosis. The human RBBP6 gene codes for …
implicated in the regulation of cell cycle and apoptosis. The human RBBP6 gene codes for …
[HTML][HTML] MDM2 promotes proteasome-dependent ubiquitin-independent degradation of retinoblastoma protein
P Sdek, H Ying, DLF Chang, W Qiu, H Zheng… - Molecular cell, 2005 - cell.com
Inactivation of retinoblastoma protein (Rb) plays a critical role in the development of human
malignancies. It has been shown that Rb is degraded through a proteasome-dependent …
malignancies. It has been shown that Rb is degraded through a proteasome-dependent …