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HIV-1 Rev is highly mutable and glycine substitution of R35 allows mutation of N40 - by Elite Joseph Possik

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dc.contributor.author Possik, Elite Joseph
dc.date.accessioned 2012-06-13T07:14:55Z
dc.date.available 2012-06-13T07:14:55Z
dc.date.issued 2009
dc.identifier.uri http://hdl.handle.net/10938/7980
dc.description Thesis (M.S.)--American University of Beirut, Dept. of Biology, 2009.;"Advisor : Dr. Colin Smith, Assistant Professor, Biology--Member of Committee : Dr. Mike Osta, Assistant Professor, Biology--Member of Committee : Dr. Rabih Talhouk, Professor, Biology.
dc.description Bibliography : leaves 88-98.
dc.description.abstract The arginine-rich domain of the HIV-1 Rev protein binds to a short stem in the R ev Response Element (RRE) RNA and mediates the export of incompletely-spliced vi ral transcripts. Rev-RRE recognition regulates gene expression and is essential for viral rep
dc.format.extent xvii, 98 leaves : ill. (some col.) 30 cm.
dc.language.iso eng
dc.relation.ispartof Theses, Dissertations, and Projects
dc.subject.classification T:005291 AUBNO
dc.subject.lcsh HIV (Viruses)
dc.subject.lcsh Viruses -- Evolution
dc.subject.lcsh RNA-protein interactions
dc.subject.lcsh Glycine
dc.subject.lcsh Biochemistry
dc.subject.lcsh Arginine
dc.title HIV-1 Rev is highly mutable and glycine substitution of R35 allows mutation of N40 - by Elite Joseph Possik
dc.type Thesis
dc.contributor.department American University of Beirut. Faculty of Arts and Sciences. Department of Biology


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