Publications by authors named "J F Cerezuela Requena"

Prion diseases, particularly sporadic cases, pose a challenge due to their complex nature and heterogeneity. The underlying mechanism of the spontaneous conversion from PrPC to PrPSc, the hallmark of prion diseases, remains elusive. To shed light on this process and the involvement of cofactors, we have developed an in vitro system that faithfully mimics spontaneous prion misfolding using minimal components.

View Article and Find Full Text PDF

Scrapie is a prion disease of sheep and goats. Prions (PrP) replicate by inducing a natively expressed protein (PrP) to refold into the prion conformation. PrP and PrP contain a disproportionately large number of methionines.

View Article and Find Full Text PDF

Current diagnostic methods for prion diseases only work in late stages of the disease when neurodegeneration is irreversible. Therefore, biomarkers that can detect the disease before the onset of clinical symptoms are necessary. High-throughput discovery proteomics is of great interest in the search for such molecules.

View Article and Find Full Text PDF

The ability of living beings to deal with abrupt environmental changes is paramount for survival, and organisms have evolved a large variety of molecular mechanisms (known globally as stress responses) to buffer the harmful effects of stressors on cellular homeostasis [...

View Article and Find Full Text PDF

The high-throughput proteomics data generated by increasingly more sensible mass spectrometers greatly contribute to our better understanding of molecular and cellular mechanisms operating in live beings. Nevertheless, proteomics analyses are based on accurate genomic and protein annotations, and some information may be lost if these resources are incomplete. Here, we show that most proteomics data may be recovered by interconnecting genomics and proteomics approaches (i.

View Article and Find Full Text PDF