SteyaertGroup

Probing the N-terminal β-sheet conversion in the crystal structure of the human prion protein bound to a nanobody.

Abskharon, R. N. N., G. Giachin, A. Wohlkonig, S. H. Soror, E. Pardon, G. Legname, and J. Steyaert, "Probing the N-terminal β-sheet conversion in the crystal structure of the human prion protein bound to a nanobody.", J Am Chem Soc, vol. 136, issue 3, pp. 937-44, 2014 Jan 22.

Regulation of β2-adrenergic receptor function by conformationally selective single-domain intrabodies.

Staus, D. P., L. M. Wingler, R. T. Strachan, S. G. F. Rasmussen, E. Pardon, S. Ahn, J. Steyaert, B. K. Kobilka, and R. J. Lefkowitz, "Regulation of β2-adrenergic receptor function by conformationally selective single-domain intrabodies.", Mol Pharmacol, vol. 85, issue 3, pp. 472-81, 2014 Mar.

Mechanistic analysis of allosteric and non-allosteric effects arising from nanobody binding to two epitopes of the dihydrofolate reductase of Escherichia coli.

Oyen, D., R. Wechselberger, V. Srinivasan, J. Steyaert, and J. N. Barlow, "Mechanistic analysis of allosteric and non-allosteric effects arising from nanobody binding to two epitopes of the dihydrofolate reductase of Escherichia coli.", Biochim Biophys Acta, vol. 1834, issue 10, pp. 2147-57, 2013 Oct.

Structural flexibility of the G alpha s alpha-helical domain in the beta2-adrenoceptor Gs complex.

Westfield, G. H., S. G. F. Rasmussen, M. Su, S. Dutta, B. T. Devree, K. Young Chung, D. Calinski, G. Velez-Ruiz, A. N. Oleskie, E. Pardon, et al., "Structural flexibility of the G alpha s alpha-helical domain in the beta2-adrenoceptor Gs complex.", Proc Natl Acad Sci U S A, vol. 108, issue 38, pp. 16086-91, 2011 Sep 20.

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