Our research program is at the interface of chemistry and biology. Our current efforts are directed toward understanding protein posttranslational modification (PTM) by ubiquitin (Ub) and ...

Solution structure of ThiS. The solution structure of ThiS reveals a compact ubiquitin fold. With excellent dispersion in the 2D 15 N-1 H chemical shift correlation spectrum (Fig. 2a), standard ...

Although the highly conserved small polypeptide ubiquitin is the best-studied post-translational modifier, there is a growing family of ubiquitin-like proteins (UBLs) that modify cellular targets ...

Modifications in proteins after they are synthesized (post-translational) are changes that play a fundamental role in cell ...

Ubiquitin-like proteins (Ubls) are conjugated to target proteins or lipids to regulate their activity, stability, subcellular localization, or macromolecular interactions. Conjugation is achieved ...

It showed that another chemical group called ubiquitin, which is attached on the tail of a completely different histone, H2B, affected methylation of lysine at this K4 position on the H3 tail.

A team of international scientists has recently characterized the structure of tumor necrosis factor receptor associated factor 6 (TRAF6) N-terminal domain for therapeutic purposes.

Chemical Biology and Biochemistry of the Ubiquitin System. ... Such modifications include ubiquitination and covalent attachment of ubiquitin-like molecules (e.g., SUMO or small ubiquitin-like ...

Click synthesis of ubiquitin dimer analogs to interrogate linkage-specific UBA domain binding, Chem Commun 48, 296-298. Sommer, S., Ritterhoff, T., Melchior, F., and Mootz, H. D. (2015) A stable ...

Ubiquitin can be thought of as a “tag” that bonds to substrate proteins that should be degraded by the proteasome. It acts as a signal and, once bound, the protein is usually directed towards ...