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Kinetic and mechanistic studies on the hydrolysis of ubiquitin C-terminal 7-amido-4-methylcoumarin by deubiquitinating enzymes.
The results suggest that deubiquitinating enzymes are able to utilize the free energy that is released from remote interactions with Ub-containing substrates for stabilization of catalytic transition states, and UCHs are more efficient at utilizing the energy from these interactions, presumably because they do not possess a binding domain for a Ub "leaving group". Expand
MEKK1 activates both IkappaB kinase alpha and IkappaB kinase beta.
- F. Lee, R. Peters, L. C. Dang, T. Maniatis
- Chemistry, Biology
- Proceedings of the National Academy of Sciences…
- 4 August 1998
It is shown that recombinant IKK-alpha and Ikk-beta can directly phosphorylate IkappaB alpha at Ser-32 and Ser-36, as well as homologous residues in Ikappa b beta in vitro, and thus are bona fide Ikappa B kinases. Expand
Crystal structure of the cysteine protease interleukin-1β-converting enzyme: A (p20/p10)2 homodimer
Conservation among members of the ICE/CED-3 family of the amino acids that form the active site region of ICE supports the hypothesis that they share functional similarities. Expand
Novel IKK inhibitors: beta-carbolines.
- Alfredo C. Castro, L. C. Dang, +7 authors J. Adams
- Bioorganic & medicinal chemistry letters
Optimization of this beta-carboline natural product derivative resulted in a novel class of selective IKK inhibitors with IC(50)s in the nanomolar range and it is shown that one of these beta- carboline analogues inhibits the phosphorylation of IkappaBalpha and subsequent activation of NF-kappaB in whole cells, as well as blocking TNF-alpha release in LPS-challenged mice. Expand
Novel IKK inhibitors: β-carbolines
Abstract Inhibitors of IκB kinase (IKK) have long been sought as specific regulators of NF-κB. A screening effort of the endogenous IKK complex allowed us to identify 5-bromo-6-methoxy-β-carboline as… Expand
MEKK1 activates both IκB kinase α and IκB kinase β
It is shown that recombinant IKK-α and Ikk-β can, in fact, directly phosphorylate IκBα at Ser-32 and Ser-36, as well as homologous residues in IKKBβ in vitro, and thus are bona fide IkkB kinases. Expand
Stability and Oligomeric Equilibria of Refolded Interleukin-1β Converting Enzyme*
- R. Talanian, L. C. Dang, +5 authors K. Brady
- Chemistry, Medicine
- The Journal of Biological Chemistry
- 6 September 1996
The observation of a reversible equilibrium between ICE (p20p10) and ( p20p 10)2 suggests that analogous associations, possibly between ICE and ICE homologs, can occur in vivo, resulting in novel oligomeric protease species. Expand
Novel IKK Inhibitors: β‐Carbolines.
Preparation of an autolysis-resistant interleukin-1 beta converting enzyme mutant.
The point mutation Asp381 to Glu was added to eliminate the major site of autolytic degradation while maintaining catalytic activity, and an N-terminal polyhistidine tag was added in place of the ICE pro-region to facilitate purification. Expand