A study on a common sequence motif in membrane proteins, called a …

• Abstract
• Methods
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• Acknowledgements
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Biology Articles » Biophysics » Medical Biophysics » Transmembrane glycine zippers: Physiological and pathological roles in membrane proteins » Acknowledgements

Acknowledgements

- Transmembrane glycine zippers: Physiological and pathological roles in membrane proteins

We thank Alessandro Senes for helpful discussions and members of J.U.B.'s laboratory for discussions and comments on the manuscript. This work was supported by National Institutes of Health Grant GM3919 and a National Science Foundation Integrative Graduate Education and Research Traineeship predoctoral award (to A.O.). J.U.B. is a Leukemia and Lymphoma Society Scholar.

Footnotes 
 
Author contributions: S.K., T.-J.J., A.O., D.Y., J.J.S., and J.U.B. designed research; S.K., T.-J.J., A.O., and D.Y. performed research; T.-J.J., A.O., and D.Y. contributed new reagents/analytic tools; S.K., T.-J.J., A.O., D.Y., J.J.S., and J.U.B. analyzed data; and S.K., T.-J.J., J.J.S., and J.U.B. wrote the paper.

This paper was submitted directly (Track II) to the PNAS office.

Abbreviations: TM, transmembrane; A, amyloid-; RCS, relative conservation score; PrP, prion protein; MscS, mechanosensitive channel of small conductance; VacA, vacuolating toxin A; TJ, tight junction.

Present address: Department of Life Science, POSTECH, Pohang University of Science and Technology, Pohang, Kyung-Buk 790-784, Korea.

To whom correspondence should be addressed. E-mail: bowie@mbi.ucla.edu .

© 2005 by The National Academy of Sciences of the USA