Douglas B. Kell

To what extent are the terminal stages of sepsis, septic shock, SIRS, and multiple organ dysfunction syndrome actually driven by a prion/amyloid form of fibrin? bioRxiv preprint.

The paper argues that fibrin in sepsis-related conditions forms amyloid-like structures, contributing to disease severity and proposes therapeutic inhibition as a potential intervention.

Substoichiometric molecular control and amplification of the initiation and nature of amyloid fibril formation: lessons from and for blood clotting. BioRXiv preprint.

The paper explores how fibrinogen can form amyloid-like structures under certain conditions and links this to disease, suggesting new therapeutic strategies.

Acute induction of anomalous blood clotting by molecular amplification of highly substoichiometric levels of bacterial lipopolysaccharide (LPS)

This paper shows that extremely low concentrations of bacterial LPS alter fibrin structure and coagulation properties, suggesting a direct role for LPS in inflammatory diseases.