Global ETD Search
Search theses and dissertations gathered from participating repositories worldwide. Every result links back to the library that holds it. No account is needed.
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Showing 1 to 4 of 4 for “"Retinoblastoma binding protein 6"”.
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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 interacts with both tumour suppressors p53 and pRb, suggesting that it is …
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Biophysical investigations of the interaction between substrate binding domain of Hsp40 and the RING finger domain of Retinoblastoma Binding Protein 6
… side effects of current chemotherapy treatments. Protein-protein interactions have recently come onto the scene as potential targets for novel treatment and management options for the disease. Through a yeast-two hybrid study, the RING finger domain of the Retinoblastoma binding protein 6 (RBBP6) …
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Analysis of the biophysical and in silico exploration of the interaction between small ribonucleoprotein G and the RING finger domain of retinoblastoma binding protein 6 for the identification of protein anti-cancer compounds
… and develop cancer treatment methods using protein-protein interactions (PPIs) have become promising targets for therapeutic discovery. Suggestive evidence has proposed putative interactions between Small nuclear ribonucleoprotein polypeptide G (SNRPG) (also referred to as SmG in this study) …
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Recombinant expression, purification and structural characterization of aspergillus niger ring finger domain using nuclear magnetic resonance spectroscopy
e retinoblastoma binding protein 6 (RBBP6) is a 250 kDa nuclear protein which contains an N-terminal DWNN domain and a conserved RING finger domain. Previous studies determined the solution structure of the human RING finger domain using heteronuclear NMR spectroscopy. A bioinformatics analysis …