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

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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

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

The authors provide evidence that the meatiness of Texel sheep may in part be due to a point mutation that downregulates expression of GDF8, a transforming growth factor (TGF)-b family protein that negatively regulates muscle mass.

Paul Garrity
Brandeis University, USA

These papers were selected from multiple disciplines from the Faculty of 1000, a web-based ...

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