No data available.
Please log in to see this content.
You have no subscription access to this content.
No metrics data to plot.
The attempt to load metrics for this article has failed.
The attempt to plot a graph for these metrics has failed.
The full text of this article is not currently available.
Bioresistive identification of heat shock protein 90
1.J. Fritz, M. K. Baller, H. P. Lang, H. Rothuizen, P. Vettiger, E. Meyer, H. J. Güntherodt, C. Gerber, and J. K. Gimzewski, Science 288, 316 (2000).
2.V. M. Jakob, Columbia Sci. Rev. 3, 20 (2006).
4.R. Bagatell and L. Whitesell, Mol. Cancer Ther. 3, 1021 (2004).
9.A. Chandrasekaran, A. Acharya, J. L. You, K. Y. Soo, M. Packirisamy, I. Stiharu, and A. Darveau, Sensors 7, 1901 (2007).
10.Y. C. Lo, C. S. Huang, W. Hsu, and C. Wang, in Proceedings of the International Conference on MEMS, NANO and Smart Systems (ICMENS’04) (IEEE Computer Society, Washington, D.C., 2004), pp. 671–674.
Article metrics loading...
90 kDa heat shock protein (HSP90) is a ubiquitous molecular chaperone and is one of the abundant proteins present in a cell under normal and stressed conditions. The adenosine triphosphate (ATP) binding region of HSP90 is currently under a great degree of study because of the interest of its role in cancer and protein maintenance; the binding of ATP to HSP90 induces a large conformational change in the protein as a result of the activity of different types of stressors within the cells. In the present paper, a simple microfluidicbiosensor is proposed for the characterization of ATP-HSP90 interactions through the principle of bioresistive variation. The experimental results prove that the present biosensor system is highly suitable for the detection of heat shock proteins present in a real-time biological sample, which is very useful for in-situ biomedical applications and rapid pathogenic detections.
Full text loading...
Most read this month