Now showing items 1-4 of 4
Solution structure of the RING finger domain from the human splicing-associated protein RBBP6 using heteronuclear Nuclear Magnetic Resonance (NMR) spectroscopy
Retinoblastoma-binding protein 6 (RBBP6) is a multi-domain human protein known to play a role in mRNA splicing, cell cycle control and apoptosis. The protein interacts with tumour suppressor proteins p53 and pRb and recent ...
A yeast 2-hybrid screen to identify and characterize interaction partners of the cancer associated protein retinoblastoma binding protein 6
Retinoblastoma binding protein 6 (RBBP6) is a 250 kDa protein that is implicated in mRNA processing and ubiquitination functions and has been shown to be highly up-regulated in a number of cancers. In humans and mice,RBBP6 ...
Investigation of the interactions of retinoblastoma binding protein-6 with transcription factors p53 and Y-Box Binding Protein-1
Retinoblastoma Binding Protein 6 (RBBP6) is a 250 kDa multi-domain protein that has been implicated in diverse cellular processes including apoptosis, mRNA processing and cell cycle regulation. Many of these functions are ...
Structural characterisation of the interaction between RBBP6 and the multifunctional protein YB-1
(University of the Western Cape, 2010)
As a means of further localising the interaction, truncated fragments derived from the C-terminal region of YB-1, were tested for their interaction with the RING finger domain of RBBP6 using three different assays: a ...