Publications

2018

Stabilization of a membrane-associated amyloid-β oligomer for its validation in Alzheimer’s disease
Serra-Batiste, M.; Giusti, F.; Zoonens M., Carulla N.  Research Topic “Structural and Molecular Biology of Alzheimer’s Disease”, Front. Mol. Biosci. (in press).
Preparation of well-defined and stable β-barrel pore-forming Aβ42 oligomers.
Serra-Batiste, M.; Ninot-Pedrosa, M.; Puig. E.; Ciudad, S.; Gairí M.; Carulla, N. Third edition of the volume on Amyloid Proteins in Meth. Mol. Biol. (in press)
Direct evidence of the presence of cross-linked Aβ dimers in the brains of Alzheimer’s disease patients
Vázquez de la Torre, A.#; Gay. M.#; Vilaprinyó-Pascual, S.; Mazzucato, R.; Serra-Batiste, M.; Vilaseca, M.; Carulla, N. (#both authors contributed equally to this work) Anal. Chem. 90, 4552-4560. doi: 10.1021/acs.analchem.7b04936.

2017

Alzheimer’s disease-associated Aβ42 peptide: expression and purification for NMR structural studies

Serra-Batiste, M.; Garcia-Castellanos R.; Ninot-Pedrosa, M.; Serra-Vidal B., Berrow, N.S.; Carulla, N. Curr. Chem. Biol. 11, 50-62 (2017). doi: 10.2174/2212796811666170206113722.

2016

Aβ42 assembles into specific β-barrel pore-forming oligomers in membrane-mimicking environments

Serra-Batiste, M.; Bayoumi, M.; Gairí, M.; Ninot-Pedrosa, M.; Maglia, G., Carulla, N. Proc. Natl. Acad. Sci. USA 113, 10866-10871 (2016). doi: 10.1073/pnas.1605104113.

2015

SDS-PAGE analysis of Aβ oligomers is disserving research into Alzheimer´s disease: appealing for ESI-IM-MS
Pujol-Pina, R.#; Vilaprinyó-Pascual, S.#; Mazzucato, R.; Arcella, A.; Vilaseca, M.; Orozco, M.; Carulla, N. (#both authors contributed equally to this work)
Sci. Rep. 5, 14809 (2015). doi: 10.1038/srep14809.

2014

Hydrogen/deuterium exchange-protected oligomers populated during Aβ fibril formation correlate with neuronal cell death
Serra-Vidal B.; Pujadas, Ll.; Rossi, D.; Soriano, E.; Madurga, S.; Carulla N. ACS Chem. Biol. 9, 2678-2685 (2014). doi: 10.1021/cb500621x.
Reelin delays amyloid-β fibril formation and rescues cognitive deficits in a mouse model of Alzheimer´s disease
Pujadas, Ll.; Rossi, D.; Andrés, R.; Teixeira, C.M.; Serra-Vidal, B.; Parcerisas, A.; Maldonado, R.; Giralt, E.; Carulla N.; Soriano E.
Nat. Commun. 5, 1-11 (2014). doi: 10.1038/ncomms4443.

Pre – 2013

Template-assisted lateral growth of amyloid- β42 fibrils studied by differential labeling with gold nanoparticles
Arimon, M., Sanz, F., Giralt, E., Carulla, N.Bioconjug. Chem. 23, 27-32 (2012). doi: 10.1021/bc200077s.
Aβ40 and Aβ42 amyloid fibrils exhibit distinct molecular recycling properties.
Sánchez, L., Madurga, S., Pukala, T., Vilaseca, M., López-Iglesias, C., Robinson, C.V., Giralt, E., Carulla N.J. Am. Chem. Soc. 133, 6505-6508 (2011). doi: 10.1021/ja1117123.
Structure and intermolecular dynamics of aggregates populated during amyloid fibril formation studied by hydrogen/deuterium exchange.
Carulla, N., Zhou, M., Giralt, E., Robinson, C.V, Dobson, C.M.
Acc. Chem. Res. 43, 1072-1079 (2010). doi: 10.1021/ar9002784.
Experimental characterization of disordered and ordered aggregates populated during the process of amyloid fibril formation.
Carulla, N., Zhou, M., Arimon M., Gairí, M., Giralt, E., Robinson, C.V, Dobson, C.M.
Proc. Natl. Acad. Sci. USA 106, 7828-7833 (2009). doi: 10.1073/pnas.0812227106.
Retro-Enantio N-Methylated Peptides as β-Amyloid Aggregation Inhibitors
Grillo-Bosch, D., Carulla, N., Cruz, M., Sánchez, L., Pujol, R., Madurga, S., Rabanal, F., Giralt, E.
ChemMedChem 4, 1488-1494 (2009). doi: 10.1002/cmdc.200900191.
Redesign of protein domains using one-bead-one-compound combinatorial chemistry
Pastor, J.J., Granados G., Carulla, N., Rabanal, F., Giralt, E.
J. Am. Chem. Soc. 129, 14922-14932 (2007).
Molecular recycling within amyloid fibrils
Carulla, N., Caddy, G.L., Hall D.R., Zurdo, J., Gairí, M., Feliz, M., Giralt, E., Robinson, C.V., Dobson, C.M.
Nature 436, 554-558 (2005).
Native exchange hydrogen exchange analysis of protein folding and protein motional domains.
Woodward, C., Carulla, N., Barany, G.
Methods Enzymol. “Energetics of Biological Macromolecules, Part E” (Johnson, M.L.; Acke, G.K.; Holt, J.M. Eds.), Academic Press, 380, 379-400 (2004). 
Hydrogen exchange, core modules and new designed proteins.
Carulla, N., Barany, G., Woodward, C.
Biophys. Chem., 101-102, 67-79 (2002).
BetaCore, a Designed Water Soluble Four-Stranded Antiparallel β-Sheet Protein.
Carulla, N., Woodward, C., Barany, G.
Protein Sci., 11, 1539-1551 (2002).
Experimental Approaches to Protein Folding Based on the Concept of a Slow Exchange
Woodward, C., Barbar, E., Carulla, N., Battiste, J., Barany G.
Core. J. Mol. Graph. Model., 19, 94-101 (2001).
Simple Methods for the Preparation of Protected Derivatives of D-Allo- and L-Allo-Threonine.
Lloyd-Williams, P., Carulla, N., Giralt, E.
Tetrahedron Letters, 38, 299-302 (1997).
Synthetic Studies on Threonines. The Preparation of Protected Derivatives of D-Allo- and L-Allo-Threonine for Peptide Synthesis.
Lloyd-Williams, P., Sánchez, A., Ochoa, T., Carulla, N., Giralt, E.
Tetrahedron, 35, 3369-3382 (1997).