Jorge Pedro López-Alonso

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

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 uses cryo-EM to show that substrate and cofactor binding in mycobacterial L-GDH180 induces tertiary and quaternary structural remodeling.

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.

The paper uses cryo-electron tomography to study structural changes in mitochondrial protein biogenesis under proteostatic stress, revealing remodeling of cristae and mHsp60 conformation.

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.

The paper presents cryo-EM structures of human mitochondrial Hsp60 chaperonin in different states to elucidate the structural basis of ATP-driven double-ring assembly.

This study determines the high-resolution structure of human RIPK1 homomeric amyloid fibrils, revealing structural differences from RIPK3 fibrils that inform necroptosis mechanisms.

This paper describes a synthetic CRISPR-Cas nuclease with expanded enzymatic activities, capable of targeting various nucleic acids and functioning in human cells and bacteria.