J. Santiago

The paper identifies RALF22 as a peptide that functions both structurally and signaling in plant cell wall assembly, forming complexes with LRX1 and LLG1-FER to regulate cell expansion.

This study identifies CEPs as immune-modulatory peptides in Arabidopsis that coordinate immunity with nitrogen status through receptor-dependent mechanisms.

This study identifies three Arabidopsis RLKs with LRR and MAL domains that recognize cellulose and MLG-derived oligosaccharides, triggering PTI, distinct from chitin recognition.

The paper identifies CTNIPs as a conserved family of plant signaling peptides and shows that HSL3 is their receptor, revealing an ancient signaling module involved in stress responses.

The paper identifies CB002 analogues that restore p53 signaling and target an S-phase checkpoint in p53-mutated tumors, inducing apoptosis and reducing proliferation without harming normal cells.

The paper reports the crystal structure of the LRX-RALF complex and shows RALF peptides function as folded, disulfide-stabilized proteins that bind LRXs with nanomolar affinity.

The paper presents crystal structures of two CrRLK1L receptor kinases involved in plant reproduction and identifies a novel protein-protein interaction interface.