An investigation of the zinc binding characteristics of the RING finger domain from the human RBBP6 protein using heteronuclear NMR spectroscopy.

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dc.contributor.advisorPugh, David J.R.
dc.contributor.authorMulaudzi, Takalani
dc.contributor.otherMagister Scientiae - MSc
dc.contributor.otherFaculty of Science
dc.date.accessioned2014-02-10T12:26:45Z
dc.date.accessioned2024-05-09T07:45:00Z
dc.date.available2007/12/07 10:13
dc.date.available2007/12/07
dc.date.available2014-02-10T12:26:45Z
dc.date.available2024-05-09T07:45:00Z
dc.date.issued2007
dc.descriptionMagister Scientiae - MSc
dc.description.abstractRetinoblastoma 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.
dc.description.countrySouth Africa
dc.identifier.urihttps://hdl.handle.net/10566/13265
dc.language.isoen
dc.publisherUniversity of the Western Cape
dc.rights.holderUniversity of the Western Cape
dc.subject15N-HSQC
dc.subject1H-113Cd-HSQC
dc.subjectCadmium ion
dc.subjectCoordination
dc.subjectExpression
dc.subjectRING
dc.subjectSpectroscopy
dc.subjectZinc ion
dc.titleAn investigation of the zinc binding characteristics of the RING finger domain from the human RBBP6 protein using heteronuclear NMR spectroscopy.
dc.typeThesis

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