Papers to watch

I.C. Lorenz et al., "Structure of the catalytic domain of the hepatitis C virus NS2-3 protease," Nature, 442:831-5, Aug. 17, 2006. This paper reports that the NS2-3 protease of hepatitis C virus is a cysteine protease with a novel fold, and that the active site is located at the interface of a dimer. The results suggest that dimerization (or NS2 concentration) may be a regulatory mechanism in the auto-processing of the viral polyprotein. Liang Tong

The Scientist Staff
Oct 1, 2006
I.C. Lorenz et al., "Structure of the catalytic domain of the hepatitis C virus NS2-3 protease," Nature, 442:831-5, Aug. 17, 2006.

This paper reports that the NS2-3 protease of hepatitis C virus is a cysteine protease with a novel fold, and that the active site is located at the interface of a dimer. The results suggest that dimerization (or NS2 concentration) may be a regulatory mechanism in the auto-processing of the viral polyprotein.

Liang Tong
Columbia University, USA

J. Hollien, J.S. Weissman, "Decay of endoplasmic reticulum-localized mRNAs during the unfolded protein response," Science, 313:104-7, July 7, 2006.

This fascinating study identifies selective degradation of mRNAs encoding proteins targeted to the endoplasmic reticulum (ER) as a novel, fast component of the unfolded protein response (UPR).

Peter Van Endert
National Institute of Health and Medical Rresearch, France

A. Clop et al., "A mutation creating a potential illegitimate microRNA target site...

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