Laura S. Itzhaki

This paper develops DNA-peptide nanostructures to multivalently inhibit TNKS, showing they effectively downregulate Wnt signaling in cancer cells despite differences in TBP copy number.

This paper identifies DNA aptamers that bind the truncated form of HasA, a hemophore in Pseudomonas aeruginosa, under acidic conditions, showing potential as antimicrobial agents.

This paper describes a method to purify and characterize soluble domains of bacterial membrane receptors, demonstrating its effectiveness with the HasR receptor from Pseudomonas aeruginosa.

This paper designs de novo bifunctional proteins for targeted protein degradation, demonstrating their ability to degrade BCL-xL in cells.

The paper investigates how two small molecule activators of PP2A, ATUX-8385 and DBK-776, affect the structural stability of the PR65 scaffold using biophysical and computational methods.

The paper investigates how SMAPs bind to PR65, showing that S2 is a stable binding site while S1 is not, and that binding promotes an extended PR65 conformation favorable for PP2A holoenzyme assembly.

The paper demonstrates the use of coiled-coil scaffolds to enable targeted protein degradation by integrating target-binding and degradation motifs into single-polypeptide constructs.

This study develops D-box peptides that inhibit APC/C by binding Cdc20, showing they are more potent than Apcin and can drive protein degradation.

The paper demonstrates that stable CTPR proteins can be modified to bind alpha-synuclein fibrils with micromolar affinity, enabling the testing of fibril-binding peptides.

This study designs a synthetic biomolecular condensate platform using CTPR proteins and intrinsically-disordered domains to tune condensate properties and recruit target proteins.

The paper investigates how the CMV 2b protein interacts with AGO1 and 1a protein, finding that residues 56-60 influence these interactions but no single residue is solely responsible.