Robert Batey

This paper identifies the MBD-ID module as a unified DNA/RNA binding interface in MECP2, showing it is disrupted in Rett syndrome due to mutations in the intervening domain.

The paper investigates cryptic RNA binding sites in the env8 Cbl riboswitch, showing they are energetically accessible and chemically addressable through base displacement and ligand binding.

This study shows that aliphatic ligands can bind RNA with high affinity and activity, challenging the notion that aromaticity is essential for RNA recognition.

The paper reports crystal structures of dopamine-binding RNA aptamers to show how they recognize ligands while maintaining scaffold integrity through metal-mediated interactions and local remodeling.

This paper introduces epoxide- and aziridine-2-carboxamide electrophiles that covalently target RNA with stereoselectivity, demonstrating their application to RNA targets like r(CUG)exp repeats and FMN riboswitches.

The paper challenges the hypothesis that the yjdF riboswitch is regulated by azaaromatic compounds by showing it binds multiple ligands similarly but requires conserved nucleotides for activation.

This study designs a covalent small molecule targeting unpaired guanines in a riboswitch, showing it modulates riboswitch function in a cellular reporter system.

The paper determines crystal structures of the RhoBAST RNA aptamer complexed with fluorophores to elucidate the mechanism of ring-opening fluorescence.

This study identifies a distinct mechanism of RNA recognition by GATA1, showing competitive DNA/RNA binding through an overlapping surface involving the ARM-like domain.

This paper introduces PNA-based linkers to enhance RNA imaging probes by improving binding affinity and specificity, demonstrating significant improvements in RNA visualization in live cells.

This study shows that the RNA-binding selectivity of hnRNP U's RGG/RG motifs is reduced by the disordered region, leading to broad RNA interactions.

This study identifies and characterizes the extended RNA-binding domain of hnRNP U, revealing two RGG/RG elements that work redundantly to enhance RNA binding.

This study shows Spen binds to endogenous retroviral RNAs and recruits chromatin silencing machinery, linking RNA-mediated retrovirus silencing to X chromosome inactivation.