A new concept in the field of heart‐failure (HF) research points to a role of misfolded
proteins, forming preamyloid oligomers (PAOs), in cardiac toxicity. This is largely based on …

Deamidation of asparagine and glutamine is the most common nonenzymatic, post-
translational modification. Deamidation can influence the structure, stability, folding, and …

Many neurodegenerative diseases are characterized by misfolding and aggregation of an
expanded polyglutamine tract (polyQ). Huntington's Disease, caused by expansion of the …

The accumulation of cross‐β‐sheet amyloid fibrils is the hallmark of amyloid diseases.
Recently, we reported the discovery of amyloid disaggregase activities in extracts from …

Protein misfolding and aggregation is a pathogenic feature shared among at least ten
polyglutamine (polyQ) neurodegenerative diseases. While solvent-solution interaction is a …

Malfunction and amyloid formation of the Islet Amyloid Polypeptide (IAPP) are factors
contributing to Type 2 diabetes. Unravelling the mechanism of IAPP aggregate formation …

The role of various structural features, namely basic scaffolds and substituents of small
molecule inhibitors of the self-assembly of amyloid-beta (Aβ) peptide, a key process in …

Designing hybrid proteins is a major aspect of protein engineering and covers a very wide
range of applications from basic research to medical applications. This review focuses on …

El impacto de cationes de metales de transicion, especificamente el Cu2+, sobre la
dinámica de la proteina humana β-2-microglobulina (β2m) es explorado a través de …

Ms. Diana Rodriguez Camargo developed during her PhD of a protocol for the recombinant
production of the human hormone Islet Amyloid polypeptide (hIAPP) in E. coli. Furthermore …