Nanobodies

Nanobody production and applications

Structural basis for ion selectivity in TMEM175 K channels.

Brunner, J. D., R. P. Jakob, T. Schulze, Y. Neldner, A. Moroni, G. Thiel, T. Maier, and S. Schenck, "Structural basis for ion selectivity in TMEM175 K channels.", Elife, vol. 9, 2020 Apr 08.

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Structural basis for phospholipid scrambling in the TMEM16 family.

Brunner, J. D., S. Schenck, and R. Dutzler, "Structural basis for phospholipid scrambling in the TMEM16 family.", Curr Opin Struct Biol, vol. 39, pp. 61-70, 2016 08.

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Structural basis for anion conduction in the calcium-activated chloride channel TMEM16A.

Paulino, C., Y. Neldner, A. Km Lam, V. Kalienkova, J. D. Brunner, S. Schenck, and R. Dutzler, "Structural basis for anion conduction in the calcium-activated chloride channel TMEM16A.", Elife, vol. 6, 2017 05 31.

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Preparation of Proteoliposomes with Purified TMEM16 Protein for Accurate Measures of Lipid Scramblase Activity.

Brunner, J. D., and S. Schenck, "Preparation of Proteoliposomes with Purified TMEM16 Protein for Accurate Measures of Lipid Scramblase Activity.", Methods Mol Biol, vol. 1949, pp. 181-199, 2019.

Production and Application of Nanobodies for Membrane Protein Structural Biology.

Brunner, J. D., and S. Schenck, "Production and Application of Nanobodies for Membrane Protein Structural Biology.", Methods Mol Biol, vol. 2127, pp. 167-184, 2020.

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X-ray structure of a calcium-activated TMEM16 lipid scramblase.

Brunner, J. D., N. K. Lim, S. Schenck, A. Duerst, and R. Dutzler, "X-ray structure of a calcium-activated TMEM16 lipid scramblase.", Nature, vol. 516, issue 7530, pp. 207-12, 2014 Dec 11.

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A lipid site shapes the agonist response of a pentameric ligand-gated ion channel.

Hénault, C. M., C. Govaerts, R. Spurny, M. Brams, A. Estrada-Mondragon, J. Lynch, D. Bertrand, E. Pardon, G. L. Evans, K. Woods, et al., "A lipid site shapes the agonist response of a pentameric ligand-gated ion channel.", Nat Chem Biol, vol. 15, issue 12, pp. 1156-1164, 2019 Dec.

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Structure of an endosomal signaling GPCR-G protein-β-arrestin megacomplex.

Nguyen, A. H., A. R. B. Thomsen, T. J. Cahill, R. Huang, L-Y. Huang, T. Marcink, O. B. Clarke, S. Heissel, A. Masoudi, D. Ben-Hail, et al., "Structure of an endosomal signaling GPCR-G protein-β-arrestin megacomplex.", Nat Struct Mol Biol, vol. 26, issue 12, pp. 1123-1131, 2019 Dec.

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Structural evidence for the critical role of the prion protein hydrophobic region in forming an infectious prion.

Abskharon, R., F. Wang, A. Wohlkonig, J. Ruan, S. Soror, G. Giachin, E. Pardon, W. Zou, G. Legname, J. Ma, et al., "Structural evidence for the critical role of the prion protein hydrophobic region in forming an infectious prion.", PLoS Pathog, vol. 15, issue 12, pp. e1008139, 2019 Dec.

Structure of PINK1 in complex with its substrate ubiquitin.

Schubert, A. F., C. Gladkova, E. Pardon, J. L. Wagstaff, S. M. V. Freund, J. Steyaert, S. L. Maslen, and D. Komander, "Structure of PINK1 in complex with its substrate ubiquitin.", Nature, vol. 552, issue 7683, pp. 51-56, 2017 12 07.

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