• Machtens DA, Willerding JM, Eschenburg S & Reubold T.F. (2020). Crystal structure of the metaeffector MesI (Lpg2505) from Legionella pneumophila. Biochem Biophys Res Commun 527, 696-701.

• Tossidou I, Teng B, Worthmann K, Muller-Deile J, Jobst-Schwan T, Kardinal C, Schroder P, Bolanos-Palmieri P, Haller H, Willerding J, Drost DM, de Jonge L, Reubold T.F., Eschenburg S, Johnson RI & Schiffer M. (2019). Tyrosine Phosphorylation of CD2AP Affects Stability of the Slit Diaphragm Complex. J Am Soc Nephrol 30, 1220-1237.

• Eschenburg, S., Reubold, T.F. (2018) Modulation of dynamin function by small molecules. Biol. Chem. 399, 1421-1432.

• Duong, M., Yu, X., Teng, B., Schroder, P., Haller, H., Eschenburg, S., Schiffer, M. (2017) Protein kinase C ϵ stabilizes β-catenin and regulates its subcellular localization in podocytes. J. Biol. Chem. 292, 12100-12110.

• Zumbrägel, F.K., Machtens, D.A., Curth, U., Lüder, C.G., Reubold, T.F., Eschenburg S. (2017) Survivin does not influence the anti-apoptotic action of XIAP on caspase-9. Biochem. Biophys. Res. Commun.  482, 530-535.

• Anand, R., Eschenburg, S. ,Reubold, T.F. (2016) Crystal structure of the GTPase domain and the bundle signalling element of dynamin in the GDP state. Biochem. Biophys. Res. Commun. 469, 76-80.
   
• Reubold, T.F., Faelber, K., Plattner, N., Posor, Y., Ketel, K., Curth, U., Schlegel, J., Anand, R., Manstein, D.J., Noé, F., Haucke, V., Daumke, O., Eschenburg, S. (2015) Crystal Structure of the dynamin tetramer. Nature 525, 404-408.
   
• Graumann, K., Schaumburg, F., Reubold, T.F., Hippe, D., Eschenburg, S., Lüder, C.G.K (2015)
  Toxoplasma gondii inhibits cytochrome c-induced caspase activation in its host cell by interference with holo-apoptosome assembly. Microbial Cell 2, 150 – 162.
   
• Reubold, T.F., Hahne, G., Wohlgemuth, S., Eschenburg, S. (2014) Crystal structure of the leucine-rich repeat domain of the NOD-like receptor NLRP1: implications for binding of muramyl dipeptide. FEBS Lett. 588, 3327-3332.
   
• Yuan, S., Topf, M., Reubold, T.F., Eschenburg, S., Akey, C.W. (2013) Changes in Apaf-1 conformation that drive apoptosome assembly. Biochemistry 52, 2319-2327.
   
• Reubold, T.F., Eschenburg, S. (2012) A molecular view on signal transduction by the apoptosome. Cell. Signal. 24, 1420-1425.
   
• Reubold, T.F., Wohlgemuth, S., Eschenburg, S. (2011) Crystal structure of full-length Apaf-1: how the death signal is relayed in the mitochondrial pathway of apoptosis. Structure 19, 1074-1083.
   
• Knoth, T., Warburg, K., Katzka, C., Rai, A., Wolf, A., Brockmeyer, A., Janning, P., Reubold, T.F., Eschenburg, S., Manstein, D.J., Hübel, K., Kaiser, M., Waldmann, H. (2009) The Ras pathway modulator melophlin A targets dynamins. Angew. Chem. Int. Ed. Engl. 48, 7240-7245.
   
• Reubold, T.F., Wohlgemuth, S., Eschenburg, S. (2009) A new model for the transition of APAF-1 from inactive monomer to caspase-activating apoptosome. J. Biol. Chem. 284, 32717-32724.
   
• Reubold, F.T., Eschenburg, S., Becker, A., Leonard, M., Schmid, S.L., Vallee, R.B., Kull, F.J., Manstein, D.J. (2005). Crystal structure of the GTPase domain of rat dynamin 1. Proc. Natl. Acad. Sci. USA 102, 13093-13098.
   
• Eschenburg, S., Priestman, M.A., Abdul-Latif, F.A., Delachaume, C., Florence Fassy, F., Schönbrunn, E. (2005). A novel inhibitor that suspends the induced-fit mechanism of UDP-N-acetylglucosamin enolpyruvyl transferase (MurA). J. Biol. Chem. 280, 14070-14075.
   
• Eschenburg, S., Priestman, M.A., Schönbrunn, E. (2005). Evidence that the fosfomycin target Cys115 in UDP-N-acetylglucosamine enolpyruvyl transferase (MurA) is essential for product release. J. Biol. Chem. 280, 3757-3763.
   
• Eschenburg, S., Kabsch, W., Healy, M.L., Schönbrunn, E. (2003). A new view on the mechanism of MurA and AroA derived from X-ray structures of their tetrahedral reaction intermediate states. J. Biol. Chem. 49, 49215-49222.
   
• Reubold, T.F., Eschenburg, S., Becker, A., Kull, F.J., Manstein, D.J. (2003). A structural model for actin-induced nucleotide release in myosin. Nat. Struct. Biol. 10, 826-830.
   
• Eschenburg, S., Healy, M.L., Priestman, M.A., Lushington, G.H., Schönbrunn, E. (2002). How the mutation glycine96 to alanine confers glyphosate insensitivity to 5-enolpyruvyl shikimate-3-phosphate synthase (EPSP synthase) from Escherichia coli. Planta 216, 129-135.
   
• Rajashankar, K., Bufe, A., Weber, W., Eschenburg, S., Lindner, B., Betzel, Ch. (2002). Structure of the functional domain of the major pollen allergen Phl p 5b. Acta Cryst. D58, 1175-1181.
   
• Eschenburg, S., Schönbrunn, E. Shuttleworth, W.A., Evans, J.N.S., Schloss, J.V., Amrhein, N., Kabsch, W. (2001). Interaction of the herbicide glyphosate with its target enzyme EPSP synthase in atomic detail. Proc. Natl. Acad. Sci. USA 98, 1376-1380.
   
• Konareva, N.V., Gabulkhakov, A.G., Eschenburg, S., Stoeva, S., Popov, A.N., Krauspenhaar, R., Andrianova, M.E., Savochkina, Y., Agapov, I.I., Tonevitski, A.G., Kornev, A.N., Kornilov, V.V., Zaitsev, V.N., Voelter, W., Betzel, Ch., Nikonov, S.V., Vainshtein, B.K., Mikhailov, A.M. (2001). Topology of the polypeptide chain in the complex of agglutinin from castor bean seeds with D-galactose in the crystalline state. Crystallography Reports 46, 792-800.
   
• Gourinath, S., Degenhardt, M., Eschenburg, S., Moore, K., Delucas, L.J., Betzel, C., Singh, T.P. (2001). Mercury induced modifications in the stereochemistry of the active site through Cys-73 in a serine protease--crystal structure of the complex of a partially modified proteinase K with mercury at 1.8 A resolution. Indian J. Biochem. Biophys. 38, 298-302.
   
• Betzel, C., Gourinath, S., Kumar, P., Kaur, P., Perbandt, M., Eschenburg, S., Singh, T.P. (2001).
  Structure of a serine protease proteinase K from Tritirachium album limber at 0.98 A resolution. Biochemistry 40, 3080-3088.
   
• Eschenburg, S., Schönbrunn, E., Luger, K., Kabsch, W., Amrhein, N. (2000).
  Structural basis for the interaction of the fluorescence probe 8-anilino-1-naphthalene sulfonate (ANS) with the antibiotic target MurA. Proc. Natl. Acad. Sci. USA 97, 6345-6349

• Eschenburg, S., Schönbrunn, E. (2000). Comparative X-ray analysis of the unliganded fosfomycin-target MurA. Proteins 40, 290-298.

• Schönbrunn, E., Eschenburg, S., Krekel, F., Luger, K., Amrhein, N. (2000). Role of the loop containing residue 115 in the induced-fit mechanism of the bacterial cell wall biosynthetic enzyme MurA. Biochemistry 39, 2164-2173.

• Eschenburg, S., Degenhardt, M., Moore, K., DeLucas, L.J., Peters, K., Fittkau, S., Weber, W., Betzel, Ch. (2000). Crystallization of Proteinase K complexed with substrate analogue peptides on US space missions STS-91 and STS-95. J. Crystal Growth 208, 657-664.

• Schönbrunn, E., Phlippen, W., Trinczek, B., Sack, S., Eschenburg, S., Mandelkow, E.-M., Mandelkow, E. (1999). Crystallization of a macromolecular ring assembly of Tubulin liganded with the anti-mitotic drug podophyllotoxin. J. Struct. Biol. 128, 211-215.

• Krauspenhaar, R., Eschenburg, S., Perbandt, M., Kornilov, V., Konareva, N., Mikhailova, I., Stoeva, S., Wacker, R., Maier, T., Singh, T.P., Mikhailov, A., Voelter, W., Betzel, Ch. (1999). Crystal structure of Misteltoe Lectin I from Viscum album. Biochem. Biophys. Res. Commun. 257, 418-424.

• Eschenburg, S., Krauspenhaar, K., Mikhailov, A., Stoeva, S., Betzel, Ch., Voelter., W. (1998). Primary structure and molecular modeling of Misteltoe Lectin I from viscum album. Biochem. Biophys. Res. Commun. 247, 367-372.

• Degenhardt, M., Weber, W., Eschenburg, S., Dierks, K., Funari, S.S., Rapp, G., Betzel, Ch. (1998). Crystallization and preliminary X-ray crystallographic analysis of the EGF receptor ectodomain. Acta Crystallogr. D Biol. Crystallogr. 54, 999-1001.

• Eschenburg, S., Genov, N., Peters, K., Fittkau, S., Stoeva, S., Wilson, K.S., Betzel, Ch. (1998). Crystal structure of subtilisin DY, a random mutant of subtilisin Carlsberg. Eur. J. Biochem. 257, 309-318.

• Perbandt, M., Wilson, J.C., Eschenburg, S., Mancheva, I., Aleksiev, B., Genov, N., Willingmann, P., Weber, W., Singh, T.P., Betzel, Ch. (1997). Crystal structure of vipoxin at 2.0 Å: an example of regulation of a toxic function generated by molecular evolution. FEBS Letters 412, 573-577.

• Schönbrunn, E., Sack, S., Eschenburg, S., Perrakis, A., Krekel, F., Amrhein, N., Mandelkow, E. (1996). Crystal structure of UDP-N-acetylglucosamine enolpyruvyl transferase, the target of the antibiotic fosfomycin. Structure 4, 1065-1075.

• Prassl, R., Chapman, J.M., Nigon, F., Sara, M., Eschenburg, S., Betzel, Ch., Saxena, A., Laggner, P. (1996). Crystallization and preliminary X-ray analysis of a low density lipoprotein from human plasma. J. Biol. Chem. 271, 28731-28733.

• Pedersen, J.T., Olsen, O.H., Betzel, Ch., Eschenburg, S., Branner, S., Hastrup, S. (1994). Cavity mutants of Savinase. Crystal structures and differential scanning calorimetry experiments give hints of the function of buried water molecules in subtilisins. J. Mol. Biol. 242, 193-202.

• Betzel, Ch., Visanji, M., Eschenburg, S., Wilson, K.S., Peters, K., Fittkau, S., Singh, T.P., Genov, N. (1993). Crystallization and preliminary X-ray analysis of subtilisin DY, a natural mutant of subtilisin Carlsberg. Arch. Biochem. Biophys. 302, 499-502.

• Olsen, O.H., Pedersen, J.T., Betzel, Ch., Eschenburg, S., Branner, S., Hastrup, S. (1996). An investigation of the Savinase water channel: implications of cavity mutations. Adv. Exp. Med. Biol. 379, 235-241.