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Protein real-time monitoring

Gales, C., Rebois, R. V., Hogue, M., Trieu, P., Breit, A., Hebert, T. E., and Bouvier, M. (2005). Real-time monitoring of receptor and G-protein interactions in living cells. Nat. Methods 2, 177-184. [Pg.186]

N.C. Yu, J.M. Atienza, J. Bernard, S. Blanc, J. Zhu, X.B. Wang, X. Xu and Y. A. Abassi, Real-time monitoring of morphological changes in living cells by electronic cell sensor arrays An approach to study g protein-coupled receptors. Analytical Chemistry, 78(1), 35-43 (2006). [Pg.423]

EPL, a FRET pair, tetramethylrhodamine and fluorescein, was incorporated in c-Crk-II. By judicious placement of the fluorophores within the c-Crk-II molecule, it was possible to monitor the phosphorylation state of the protein using FRET measurements (Fig. 10.1-6). In a subsequent study, an extremely sensitive dual labeled c-Crk-II analog was developed that enabled real-time monitoring of c-Abl kinase activity, and provided a nonradioactive assay for the screening of potential inhibitors of the kinase [69). [Pg.550]

Painter, A.J., Jaya, N., Basha, E., Vierling, E., Robinson, C.V., Benesch, L.P. (2008) Real-time Monitoring of Protein Complexes Reveals Their Quaternary Organization and Dynamics. Chem. Biol. 15 246-253. [Pg.149]

Ko PJ, Ishikawa R, Takamura T, Sohn H, Sandhu A (2012) Porous silicon based protocol for the rapid and real-time monitoring of biorecognition between human IgG and protein A using functionalized superparamagnetic beads. IEEE Trans Magn 48 2846... [Pg.404]

EAPs have proved to be effective at detection of small quantities of biomolecules, specifically in cancer detection and real-time monitoring of blood-borne analytes such as glucose and nucleic acids (383-389). These sensors employ EAPs containing natural biomolecular recognition units sometimes referred to as biosensors. These biosensor moieties can be ligands, single strands of DNA, enzymes, antibodies, or synthetic proteins that can detect whole cells or individual proteins (390-392). [Pg.2406]

Bonomi, F. lametti, S. Real-time monitoring of the surface hydrophobicity changes associated with isothermal treatment of milk and milk protein fractions. Milchwissenschaft 1991, 46, 71—74. [Pg.42]


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See also in sourсe #XX -- [ Pg.161 , Pg.162 ]




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