Protein misfolded oligomers: experimental approaches, mechanism of formation, and structure-toxicity relationships.

Characterizing the amyloidogenic state of the acylphosphatase from Sulfolobus solfataricus

Characterization of the aggregation competent state of the acylphosphatase from Sulfolobus solfataricus

Structural and dynamics characteristics of acylphosphatase from Sulfolobus solfataricus in the monomeric state and in the initial native-like aggregates

Enzymatic activity outside the folded states of proteins

“Native‐like aggregation” of the acylphosphatase from Sulfolobus solfataricus and its biological implications

Assessing the role of aromatic residues in the amyloid aggregation of human muscle acylphosphatase.

A model for the aggregation of the acylphosphatase from Sulfolobus solfataricus in its native-like state.

Biological function in a non-native partially folded state of a protein.

The folding process of acylphosphatase from Escherichia coli is remarkably accelerated by the presence of a disulfide bond