Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Science 10 November 2006:
Vol. 314. no. 5801, p. 889
DOI: 10.1126/science.314.5801.889j
Prev | Table of Contents | Next

This Week in Science

The cell's ability to distinguish invading RNA or DNA from the plethora of its own nucleic acid sequences plays a critical role in protecting the genome from potentially harmful damage, and a number of systems have evolved to sniff out unwanted alien genes and trigger cellular responses (see the Perspective by Fujita). Retinoic acid-inducible protein I (RIG-I), part of the cellular alarm system in the cytoplasm, specifically recognizes a number of RNA viruses, but what is RIG-I actually sensing? Hornung et al. (p. 994, published online 12 October) and Pichlmair et al. (p. 997, published online 12 October) show that RIG-I detects and binds to an unusual feature of the 5′ end of the viral RNA, specifically, a 5′-phosphate group.




To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)