Susanna Navarro

Surface-exposed amino acids of eosinophil cationic protein play a critical role in the inhibition of mammalian cell proliferation.

Topography studies on the membrane interaction mechanism of the eosinophil cationic protein.

Eosinophil cationic protein high-affinity binding to bacteria-wall lipopolysaccharides and peptidoglycans.

Eosinophil-induced neurotoxicity: the role of eosinophil cationic protein/RNase 3.

A human ribonuclease induces apoptosis associated with p21WAF1/CIP1 induction and JNK inactivation.

Selection against toxic aggregation-prone protein sequences in bacteria.

Fluorescent dye ProteoStat to detect and discriminate intracellular amyloid-like aggregates in Escherichia coli.

Characterization of amyloid-like properties in bacterial intracellular aggregates.

The prion-like RNA-processing protein HNRPDL forms inherently toxic amyloid-like inclusion bodies in bacteria.

Mammalian prion protein (PrP) forms conformationally different amyloid intracellular aggregates in bacteria.

A fast and specific method to screen for intracellular amyloid inhibitors using bacterial model systems.

Amyloid properties of the leader peptide of variant B cystatin C: implications for Alzheimer and macular degeneration.

Exploring the mechanisms of action of human secretory RNase 3 and RNase 7 against Candida albicans.

Benzbromarone, Quercetin, and Folic Acid Inhibit Amylin Aggregation.

Staphylococcal Bap Proteins Build Amyloid Scaffold Biofilm Matrices in Response to Environmental Signals.

Data on correlation between Aβ42 structural aggregation propensity and toxicity in bacteria.

Characterization of Amyloid Cores in Prion Domains.

Dissecting the contribution of Staphylococcus aureus α-phenol-soluble modulins to biofilm amyloid structure.

The effects of the novel A53E alpha-synuclein mutation on its oligomerization and aggregation.

Aggregation propensity of neuronal receptors: potential implications in neurodegenerative disorders.

Prion-like proteins and their computational identification in proteomes.

Protein aggregation into insoluble deposits protects from oxidative stress.

Characterization of Soft Amyloid Cores in Human Prion-Like Proteins.

A single cysteine post-translational oxidation suffices to compromise globular proteins kinetic stability and promote amyloid formation.

Minimalist Prion-Inspired Polar Self-Assembling Peptides.