Published in Pharma Investments, Ventures and Law Weekly, April 2nd, 2006
"This report examines structural changes in a highly mutated, clinical multidrug-resistant HIV-1 protease, and the crystal structure has been solved to 1.3 angstrom resolution in the absence of any inhibitor. This protease variant contains codon mutations at positions 10, 36, 46, 54, 62, 63, 71, 82, 84, and 90 that confer resistance to protease inhibitors," scientists writing in the journal Structure report.
P. Martin and colleagues from Wayne State University wrote, "Major differences between the wild-type and the variant include a structural change initiated by the M36V...
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