Byung Hak Ha

Cryo-EM structure and biochemical characterization of a BRAF/CRAF heterodimer: Negative charge in the NtA motif is not required for RAF activation

RAF isoform selectivity of MEK inhibitors and rational design of a covalent ARAF-MEK inhibitor

The paper investigates MEK inhibitor selectivity across RAF isoforms and develops a covalent ARAF-MEK inhibitor with improved potency.

In vitro reconstitutions suggest a general model for paradoxical activation of ARAF, BRAF, and CRAF by diverse RAF inhibitor types that does not rely on negative allostery.

This study shows that RAF inhibitors paradoxically activate ARAF, BRAF, and CRAF through dimerization, not negative allostery, by using biochemical assays and mass photometry.

Nickel binding to c-Src SH3 domain facilitates crystallization

This paper reports a unique crystal structure of the c-Src SH3 domain mediated by nickel ions, revealing a 2:2 stoichiometry and dimerization mechanism.

Characterization and inhibitor sensitivity of ARAF, BRAF, and CRAF complexes

This study compares the potency of thirteen RAF inhibitors against ARAF, BRAF, and CRAF isoforms, revealing differences in inhibitor selectivity and mechanism.