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#16. A simple high-throughput approach identifies
​actionable drug responses in
​patient-derived tumor organoids

N. Phan, J. Hong, B. Tofig, M. Mapua, D. Elashoff, N.A. Motamed, J. Huang,  S. Memarzadeh,
​R. Damoiseaux, A. Soragni. 
Paper: Communications Biology, 2019
Preprint: bioRxiv, 2017

#15. Journal clubs in the time of preprints

 P. Avasthi, A. Soragni, J.N. Bembenek
 eLife 2018;7:e38532

#14. A Designed Inhibitor of p53 Aggregation Rescues p53 Tumor Suppression in Ovarian Carcinomas

A. Soragni, D.M. Janzen, L.M. Johnson, A.G. Lindgren, A.T.-Q. Nguyen, E. Tiourin, A.B. Soriaga, J. Lu, L. Jiang, K.F. Faull, M. Pellegrini, S. Memarzadeh* and D.S. Eisenberg*. Cancer Cell, 2016, 29(1): 90-103

#13. Toxicity of Eosinophil MBP Is Repressed by Intracellular Crystallization and Promoted by Extracellular Aggregation

A. Soragni, S. Yousefi, C. Stoeckle, A.B. Soriaga, M.R. Sawaya, E. Kozlowski, I. Schmid, S. Radonjic-Hoesli, S. Boutet, G.J. Williams, M. Messerschmidt, M.M. Seibert, D. Cascio, N.A. Zatsepin, M. Burghammer, C. Riekel, J.-P. Colletier, R. Riek, D. Eisenberg and H.-U. Simon. Molecular Cell, 2015, 57(6):1011-21

#12. Superresolution Imaging of Amyloid Fibrils
​with Binding-Activated Probes

J. Ries, V. Udayar, A. Soragni, S. Hornemann, K.P.R. Nilsson, R. Riek, C. Hock, H. Ewers, A.A. Aguzzi and L. Rajendran.  ACS Chem Neurosci, 2013, 4(7):1057-17

#11. On-Surface Aggregation of α-Synuclein at Nanomolar Concentrations Results in Two Distinct Growth Mechanisms

M. Rabe, A. Soragni, N. Reynolds, D. Verdes, E. Liverani, S.Riek and S. Seeger. ACS Chem Neurosci, 2013, 4(3):408-17

#10. Mechanism of Membrane Interaction
​and Disruption by α-Synuclein

N.P. Reynolds**, A. Soragni**, M. Rabe, D. Verdes, E. Liverani, R. Riek and S. Seeger. ​JACS, 2011, 133(48):19366-75
**Co-first authors 

#9. The Amyloid-Congo Red Interface at Atomic Resolution

A. Schuetz, A. Soragni, S. Hornemann, A. Aguzzi, M. Ernst, A. Böckmann and B.H. Meier. Angewandte Chemie, 2011,  50(26):5956-60 
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#8. In vivo demonstration that α-synuclein oligomers are toxic

B. Winner, R. Jappelli, S.K. Maji, L. Boyer, S. Aigner, C. Hetzer, T. Loher, M. Vilar, S. Campioni, C. Tzitzilonis, A. Soragni, S. Jessberger, H. Mira, A. Consiglio, E.H. Pham, P. Desplants, E. Masliah, F.H. Gage and R. Riek. PNAS, 2011, 108(10):4194-9
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#7. Structural similarity between the prion domain of het-s and a homologue can explain amyloid cross-seeding in spite of limited sequence identity

C. Wasmer, A. Zimmer, R. Sabaté, A. Soragni, S.J. Saupe, C. Ritter and B.H. Meier. J Mol Biol, 2010,  402(2):311-25

#6. The mechanism of prion inhibition by HET-S​

J. Greenwald, C. Buhtz, C. Ritter, W. Kwiatkowski, S. Choe, M.L. Maddelein, F. Ness, S. Cescau, A. Soragni, D. Leitz, S.J. Saupe, and R. Riek. Molecular Cell, 2010, 38(6):889-99

#5. A Combined Solid-State NMR and MD Characterization of the Stability and Dynamics of the HET-s(218-289)
​Prion in its Amyloid Conformation​

A. Lange, Z. Gattin, H. van Melckebeke, C. Wasmer, A. Soragni, W. van Gunsteren and B. Meier. ChemBioChem, 2009, 10(10):1657-65

#4. Structural Characterization of Binding of
​Cu(II) to Tau Protein

A. Soragni, B. Zambelli, M.D. Mukrasch, J. Biernat, S. Jeganathan, C. Griesinger, S. Ciurli, E. Mandelkow and M. Zweckstetter. Biochemistry, 2008, 47(41):10841-51

#3. Infectious and noninfectious amyloids of the HET‐s (218–289) prion have different NMR spectra

C. Wasmer, A. Soragni, R. Sabaté, A. Lange, R. Riek and B.H. Meier. Angewandte Chemie, 2008, 47(31);5839-41

#2. Solution structure of selenoprotein W and NMR analysis of its interaction with 14-3-3 proteins

F.L. Aachmann, D.E. Fomenko, A. Soragni, V.N. Gladyshev, A. Dikiy. Journal of Biological Chemistry, 2007, 282(51):37063-44

#1. In Vitro Analysis of Protein-Operator Interactions of the NikR and Fur Metal-Responsive Regulators
​of Coregulated Genes in Helocobacter pylori

I. Delany, R. Ieva, A. Soragni, M. Hilleringman, R. Rappuoli and V. Scarlato. Journal of Bacteriology, 2005, 187(22):7703-15
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