- About
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The Global ETD Search service is a free service for researchers
to find electronic theses and dissertations. This service is
provided by the
Networked Digital Library of Theses and Dissertations.
Our metadata is collected from universities around the world. If you manage a university/consortium/country archive and want to be added, details can be found on the NDLTD website.
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An investigation of the zinc binding characteristics of the RING finger domain from the human RBBP6 protein using heteronuclear NMR spectroscopy.Mulaudzi, Takalani. January 2007 (has links)
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<p align="left">Retinoblastoma binding protein 6 (RBBP6) is a 250 kDa human splicing-associated protein that is also known to interact with tumour suppressor proteins p53 and pRb and to mediate ubiquitination of p53 via its interaction with Hdm2. RBBP6 is highly up regulated in oesophageal cancer, and has been shown to be a promising target for immunotherapy against the disease. RBBP6 is also known to play a role in mRNA splicing, cell cycle control and apoptosis.</p>
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An investigation of the zinc binding characteristics of the RING finger domain from the human RBBP6 protein using heteronuclear NMR spectroscopy.Mulaudzi, Takalani. January 2007 (has links)
<p>
<p>  / </p>
</p>
<p align="left">Retinoblastoma binding protein 6 (RBBP6) is a 250 kDa human splicing-associated protein that is also known to interact with tumour suppressor proteins p53 and pRb and to mediate ubiquitination of p53 via its interaction with Hdm2. RBBP6 is highly up regulated in oesophageal cancer, and has been shown to be a promising target for immunotherapy against the disease. RBBP6 is also known to play a role in mRNA splicing, cell cycle control and apoptosis.</p>
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An investigation of the zinc binding characteristics of the RING finger domain from the human RBBP6 protein using heteronuclear NMR spectroscopy.Mulaudzi, Takalani January 2007 (has links)
Magister Scientiae - MSc / Retinoblastoma binding prot
ein 6 (RBBP6) is a 250 kDa human splicing-associated
protein that is also known to
interact with tumour suppresso
r proteins p53 and pRb and to
mediate ubiquitination of p53 via its intera
ction with Hdm2. RBBP6 is highly up
regulated in oesophageal cancer, and has been shown to be a promising target for immunotherapy against the disease. RBBP6 is also known to play a role in mRNA splicing, cell cycle control and apoptosis. / South Africa
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