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  1. Self-assembly of repeat proteins: Concepts and design of new interfaces. Sanchez-deAlcazar D, Mejias SH, Erazo K, Sot B, Cortajarena AL. J Struct Biol. 2017 pii: S1047-8477(17)30142-9. doi: 10.1016/j.jsb.2017.09.002.

  2. Domain topology of human Rasal. Cuellar J, Valpuesta JM, Wittinghofer A, Sot B. Biol Chem. 2017 pii: /j/bchm.just-accepted/hsz-2017-0159/hsz-2017-0159.xml. doi: 10.1515/hsz-2017-0159.

  3. The chaperonin CCT inhibits assembly of α-synuclein amyloid fibrils by a specific, conformation-dependent interaction. Sot B, Rubio-Muñoz A, Leal-Quintero A, Martínez-Sabando J, Marcilla M, Roodveldt C, Valpuesta JM. Sci Rep. 2017;7:40859. doi: 10.1038/srep40859.

  4. Molecular chaperones: functional mechanisms and nanotechnological applications. Fernández-Fernández MR, Sot B, Valpuesta JM. Nanotechnology. 2016;27(32):324004. doi: 10.1088/0957-4484/27/32/324004. Epub 2016 Jul 1. PMID: 27363314

  5. Designed modular proteins as scaffolds to stabilize fluorescent nanoclusters. Pierre Couleaud, Sergio Adan-Bermudez, Antonio Aires, Sara H Mejías, Begoña Sot, Alvaro Somoza, Aitziber L Cortajarena. Biomacromolecules 2015, 16, 3836-3844.

  6. Controlled nanometric fibers of self-assembled designed protein scaffolds. Mejías SH, Sot B, Guantes R, Cortajarena AL. Nanoscale. 2014; 6(19):10982-8. doi: 10.1039/c4nr01210k.

  7. Ras GTPase activating (RasGAP) activity of the dual specificity GAP protein Rasal requires colocalization and C2 domain binding to lipid membranes. Sot B, Behrmann E, Raunser S, Wittinghofer A. Proc Natl Acad Sci U S A. 2013; 110(1):111-6. doi: 10.1073/pnas.1201658110.