• Publications
  • Influence
DNA Converts Cellular Prion Protein into the β-Sheet Conformation and Inhibits Prion Peptide Aggregation*
It is suggested that a macromolecular complex of prion-DNA may act as an intermediate for the formation of the growing fiber, and host nucleic acid may modulate the delicate balance between the cellular and the misfolded conformations by reducing the protein mobility and by making the protein-protein interactions more likely. Expand
Snake venomics and venom gland transcriptomic analysis of Brazilian coral snakes, Micrurus altirostris and M. corallinus.
The venom proteomes of Micrurus altirostris and M. corallinus supports the view of a recruitment event predating the divergence of Elapidae and Viperidae more than 60 Mya, and points to 3FTxs and PLA(2) molecules as the major players of the envenoming process. Expand
Amyloid-β oligomers link depressive-like behavior and cognitive deficits in mice
The results indicate that AβOs have an acute impact on memory, learning and mood in mice, and that fluoxetine treatment prevented both cognitive impairment and depressive-like behavior induced by A βOs. Expand
Intriguing nucleic-acid-binding features of mammalian prion protein.
The participation of NAs in prion propagation opens new avenues for developing new diagnostic tools and therapeutics to target prion diseases, as well as for understanding the function of PrP(C), probably as a NA chaperone. Expand
A Metabolic Shift toward Pentose Phosphate Pathway Is Necessary for Amyloid Fibril- and Phorbol 12-Myristate 13-Acetate-induced Neutrophil Extracellular Trap (NET) Formation*
It is demonstrated that a metabolic shift toward the pentose phosphate pathway (PPP) is necessary for NET release because glucose-6-phosphate dehydrogenase (G6PD), an important enzyme from PPP, fuels NADPH oxidase with NADPH to produce superoxide and thus induce NETs. Expand
Structural insights into the interaction between prion protein and nucleic acid.
The infectious agent of transmissible spongiform encephalopathies (TSE) is believed to comprise, at least in part, the prion protein (PrP). Other molecules can modulate the conversion of the normalExpand
Pressure provides new insights into protein folding, dynamics and structure.
Kinetic studies under pressure enable dissection of the roles of packing and cavities in folding, and in assembly of multimolecular structures such as protein-DNA complexes and viruses. Expand
Controlling {beta}-amyloid oligomerization by the use of naphthalene sulfonates: trapping low molecular weight oligomeric species.
The stabilization of small oligomers of Abeta by the use of sulfonated hydrophobic molecules such as AMNS, 1-amino-5-naphthalene sulfonate; 1,8-ANS; 1-anilinonaphthalenes-8-sulfonate) and bis-ANS are described. Expand
Tetramerization of the LexA repressor in solution: implications for gene regulation of the E.coli SOS system at acidic pH.
The results are discussed in relation to the activation of the Escherichia coli SOS regulon in response to environmental conditions resulting in acidic intracellular pH, which is proposed to be a possible regulation mechanism of this regulon. Expand
LexA Repressor Forms Stable Dimers in Solution
In contrast to the previous model, a tight dimer rather than a monomer is the functional repressor, and the LexA dimer only loses its ability to recognize a specific DNA sequence by RecA-induced autoproteolysis. Expand