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Recent findings from X.H. Hou and co-authors highlight research in life sciences

Published in Hepatitis Weekly, March 23rd, 2009

"Despite being the focus of intensive investigation for its enzymatic activities and its roles in HCV virus replication, little is known about the internal processing of NS3. Here we show that single mutations at P1 position of the NS3/4A junction lead to alternative cleavages," investigators in the United States report.

"Among the multiple novel cleavage products observed. there were two predominant species of about 12 kDa (p12) and 67 kDa (p67). This p12 species consists of the NS4A and about a 6 kDa long C-terminal region of NS3 and forms a complex with NS3. The remaining NS3 corresponds to the p67 species. This alternative cleavage is an N53 protease-mediated...

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