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1.
Mohamad, M.* ; Goricanec, D.* ; Wagner, G.* & Hagn, F.: NMR sample optimization and backbone assignment of a stabilized neurotensin receptor. J. Struct. Biol. 215:107970 (2023)
2.
Sundaria, A. et al.: SAA fibrils involved in AA amyloidosis are similar in bulk and by single particle reconstitution: A MAS solid-state NMR study. J. Struct. Biol. 6:100069 (2022)
3.
Fuenzalida Werner, J.P. et al.: Crystal structure of a biliverdin-bound phycobiliprotein: Interdependence of oligomerization and chromophorylation. J. Struct. Biol. 204, 519-522 (2018)
4.
Stolt-Bergner, P.* et al.: Baculovirus-driven protein expression in insect cells: A benchmarking study. J. Struct. Biol. 203, 71-80 (2018)
5.
Honigschmid, P.* & Frishman, D.: Accurate prediction of helix interactions and residue contacts in membrane proteins. J. Struct. Biol. 194, 112-123 (2016)
6.
Karabulut, N.P.* & Frishman, D.: Tissue-specific sequence and structural environments of lysine acetylation sites. J. Struct. Biol. 191, 39-48 (2015)
7.
Collinet, B.* et al.: Strategies for the structural analysis of multi-protein complexes: Lessons from the 3D-Repertoire project. J. Struct. Biol. 175, 147-158 (2011)
8.
Madl, T. ; Gabel, F.* & Sattler, M.: NMR and small-angle scattering-based structural analysis of protein complexes in solution. J. Struct. Biol. 173, 472-482 (2011)
9.
Alphonse, S.* et al.: Structure of the Pseudomonas aeruginosa XcpT pseudopilin, a major component of the type II secretion system. J. Struct. Biol. 169, 75-80 (2010)
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