A.B. Loveland

This study determines cryo-EM structures of GTPBP1 bound to ribosomes and tRNA, revealing its unique architecture and mechanism for slow dissociation and enhanced decoding accuracy.

The paper uses in extracto cryo-EM to study ribosome hibernation factors, finding eEF2 as the most abundant hibernation factor bound to 60S and 80S ribosomes.

This study identifies the ribosome as the activator of angiogenin, revealing how it enhances tRNA cleavage efficiency and ensures substrate specificity through structural rearrangements.

The paper uses time-resolved cryo-EM to visualize GTP-catalyzed ribosomal translocation by EF-G, revealing intermediate structures and mechanisms of tRNA and mRNA movement.

The paper determines the structural basis for +1 ribosomal frameshifting during EF-G-catalyzed translocation using cryo-EM structures.