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Immuno- and Constitutive Proteasome Crystal Structures Reveal Differences in Substrate and Inhibitor Specificity
A unified mechanism for proteolysis and autocatalytic activation in the 20S proteasome
- E. M. Huber, W. Heinemeyer, Xia Li, C. S. Arendt, M. Hochstrasser, M. Groll
- Biology, ChemistryNature communications
- 11 March 2016
Insight is provided into the basic mechanism of proteolysis and propeptide autolysis, as well as the evolutionary pressures that drove the proteasome to become a threonine protease.
The Mammalian Proteasome Activator PA28 Forms an Asymmetric α4β3 Complex.
Structure-based design of beta 1i or beta 5i specific inhibitors of human immunoproteasomes
DNA minor groove sensing and widening by the CCAAT-binding complex.
Inhibitors for the Immuno‐ and Constitutive Proteasome: Current and Future Trends in Drug Development
Inhibitors for the immuno- and constitutive proteasome: current and future trends in drug development.
The recently determined crystal structure of the iCP will further promote the development and optimization of iCP-selective compounds, and appears to be a promising therapeutic rationale for the treatment of autoimmune disorders.
Structure-based design of β1i or β5i specific inhibitors of human immunoproteasomes.
- Gerjan de Bruin, E. M. Huber, H. Overkleeft
- Biology, ChemistryJournal of medicinal chemistry
- 15 July 2014
The development of cell-permeable β1i and β5i selective inhibitors that outperform existing leads in terms of selectivity and/or potency are reported.
Flavoenzyme-catalyzed formation of disulfide bonds in natural products.
Despite their differently sized substrate binding clefts and hence, their diverse substrate preferences, a unifying reaction mechanism is proposed based on the obtained crystal structures and further supported by mutagenesis experiments.