Borja Ochoa-Lizarralde

This study identifies CTL1 as a phospholipid-binding protein that deforms membranes, revealing its structural basis and potential role in phospholipid homeostasis.

This study characterizes the interaction between PQLC2 and the WDR41 7CD loop using EPR spectroscopy, revealing structural and dynamic insights into their binding mechanism.

This study identifies a bacterial choline transporter with a structure and mechanism similar to the human CHT1 transporter, revealing conserved choline translocation pathways.

This study determines the cryo-EM structure of human TMEM260, revealing its mechanism for O-mannosylation of key receptors and providing insights into related congenital disorders.

This study identifies the binding site of the antibiotic GE81112 in the ribosomal mRNA channel using cryoEM, showing it acts allosterically to inhibit translation initiation.

This study determines the structure of KBP-7072 bound to the 30S ribosomal subunit, showing it inhibits protein synthesis by binding to the primary tetracycline site and interacting uniquely with the subunit.