Christophe Dhalluin

TL;DR: The solution structure of the bromodomain of the HAT co-activator P/CAF (p300/CBP-associated factor) reveals an unusual left-handed up-and-down four-helix bundle, and it is shown by a combination of structural and site-directed mutagenesis studies that bromidomains can interact specifically with acetylated lysine, making them the first known protein modules to do so.

TL;DR: These findings suggest a novel mechanism by which the EB domain binding to ERK2 is transduced to cause a conformational change of the C-terminal catalytic domain, resulting in the enzymatic activation of MKP-3.

TL;DR: This work shows that the SNT-1 phosphotyrosine binding (PTB) domain utilizes distinct sets of amino acid residues to interact with FGFRs or TRKs in a mutually exclusive manner.

TL;DR: It is demonstrated that minor and major surgeries can be performed safely in PwHA receiving emicizumab prophylaxis, and these trials demonstrate that the data from the HAVEN 1-4 phase 3 clinical trials demonstrate this.

TL;DR: Structural studies of a bromodomain from the human HAT coactivator P/CAF (p300/CBP-associated factor), using heteronuclear multidimensional NMR spectroscopy techniques, report the nearly complete sequencespecific backbone and side-chain 1H, 15N, and 13C resonance assignments of the P/ CAF bromidomain.