27 research outputs found
Introducing CEC′ mechanism: Electrochemical oxidation of 4-methylesculetin–boric acid complex in the presence of glutathione
Electrosynthesis of an imidazole derivative and its application as a bifunctional electrocatalyst for simultaneous determination of ascorbic acid, adrenaline, acetaminophen, and tryptophan at a multi-wall carbon nanotubes modified electrode surface
Electrochemical Oxidation of Catechols in the Presence of Phenyl-Meldrum's Acid. Synthesis and Kinetic Evaluation
Electrochemical oxidation of acetaminophen in the presence of diclofenac and piroxicam - Synthesis of new derivatives and kinetic investigation of toxic quinone imine/drugs interactions
Voltammetric determination of ascorbic acid in the presence of acetaminophen and tryptophan using an improved carbon nanotube paste electrode
Selective voltammetric determination of norepinephrine in the presence of acetaminophen and folic acid at a modified carbon nanotube paste electrode
Deletion of low-density lipoprotein-related receptor 5 inhibits liver Cancer cell proliferation via destabilizing Nucleoporin 37
Site-specific ubiquitination affects protein energetics and proteasomal degradation
Changes in the cellular environment modulate protein energy landscapes to drive important biology, with consequences for signaling, allostery, and other vital processes. The effects of ubiquitination are particularly important because of their potential influence on degradation by the 26S proteasome. Moreover, proteasomal engagement requires unstructured initiation regions that many known proteasome substrates lack. To assess the energetic effects of ubiquitination and how these manifest at the proteasome, we developed a generalizable strategy to produce isopeptide-linked ubiquitin within structured regions of a protein. The effects on the energy landscape vary from negligible to dramatic, depending on the protein and site of ubiquitination. Ubiquitination at sensitive sites destabilizes the native structure and increases the rate of proteasomal degradation. Importantly, in well-folded proteins, ubiquitination can even induce the requisite unstructured regions needed for proteasomal engagement. Our results indicate a biophysical role of site-specific ubiquitination as a potential regulatory mechanism for energy-dependent substrate degradation