Hepatitis C Virus Therapy
Studies from Uppsala University update current data on hepatitis C virus therapy
Published in Hepatitis Weekly, December 24th, 2007
Researchers detail in 'Effects on protease inhibition by modifying of helicase residues in hepatitis C virus nonstructural protein 3,' new data in hepatitis C virus. "This study of the full-length bifunctional nonstructural protein 3 from hepatitis C virus (HCV) has revealed that residues in the helicase domain affect the inhibition of the protease. Two residues (Q526 and H528), apparently located in the interface between the S2 and S4 binding pockets of the substrate binding site of the protease, were selected for modification, and three enzyme variants (Q526A, H528A and H528S) were expressed, purified and characterized," investigators in Sweden report.
"The...
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Source: Hepatitis Weekly (2007-12-24)
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