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. | [PubMed]

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. | [PubMed]

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 in the myostatin gene affects muscularity in sheep," Nat Genet , 38:813-818, July 2006. | [PubMed]

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 literature awareness tool (www.f1000biology.com).



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