Meytal Landau

This paper investigates how environmental conditions influence the structural assembly and cytotoxic function of the Staphylococcus aureus virulence peptide PSM1, revealing condition-dependent polymorphic structures and their role in host-cell interactions.

The paper shows that ERK2 phosphorylation of tau outside the amyloid core directs fibril formation into an Alzheimer's disease-like structure.

The paper shows RNA modulates assembly and activity of two -helical peptides, PSM3 and LL-37, through phase separation and aggregation dynamics, affecting virulence and host defense.

The paper identifies two CLC binding sites on Sla2 and shows Pan1 competes with CLC for a conserved site, revealing divergence in endocytic mechanisms between fungi and metazoa.

This study investigates the structural and functional properties of citropin 1.3, an antimicrobial peptide from the Southern bell frog, revealing its ability to form distinct fibrillar structures and interact with membranes and cells.

This study investigates the resilience and charge-dependent fibrillation of Pseudomonas amyloids FapB and FapC, revealing their complex interactions and implications for biofilm persistence and potential applications.

The paper determines the cryo-EM structures of two amphibian antimicrobial peptides, revealing cross-β amyloid fibrils and their structural polymorphism.

This paper reveals structural similarities between bacterial curli amyloids and human pathological amyloids, leading to the repurposing of anti-amyloid drugs as anti-biofilm agents.