A5034512228- RNA Research and Splicing
- RNA modifications and cancer
- RNA and protein synthesis mechanisms
- Pancreatic function and diabetes
- Ubiquitin and proteasome pathways
- Protein Structure and Dynamics
- Porphyrin Metabolism and Disorders
- Genomics and Chromatin Dynamics
- Nuclear Structure and Function
- Hydrology and Watershed Management Studies
- Water Quality and Resources Studies
- Enzyme Structure and Function
- Lipid metabolism and biosynthesis
- Hyperglycemia and glycemic control in critically ill and hospitalized patients
- Metabolism and Genetic Disorders
- Neuroscience and Neural Engineering
- Additive Manufacturing and 3D Printing Technologies
- Biochemical and Molecular Research
- Diet, Metabolism, and Disease
- 3D Printing in Biomedical Research
- Diabetes and associated disorders
Howard Hughes Medical Institute
2015-2021
The University of Texas Southwestern Medical Center
2015-2021
Marine Biological Laboratory
2018
Southwestern Medical Center
2015
University of Georgia
2015
St. Matthew's University
1969
Nielsen Engineering & Research (United States)
1969
United States Geological Survey
1969
Maryland Geological Survey
1969
Maryland Department of Health
1969
Significance Many eukaryotic proteins are composed of tandem arrays modular domains, which bind peptide ligands that also often appear in arrays. The interdomain linkers such systems considered merely passive elements flexibly connect the functional domains. Collective interactions among multivalent molecules lead to micron-sized phase-separated states thought be important cellular organization. Here, we show signaling adaptor protein Nck, weak involving an linker play a significant role...
Abstract Biomolecular condensates concentrate macromolecules into discrete cellular foci without an encapsulating membrane. Condensates are often presumed to increase enzymatic reaction rates through increased concentrations of enzymes and substrates (mass action), although this idea has not been widely tested other mechanisms modulation possible. Here we describe a synthetic system where the SUMOylation enzyme cascade is recruited engineered generated by liquid-liquid phase separation...
Human UDP-α-D-xylose synthase (hUXS) is a member of the short-chain dehydrogenase/reductase family nucleotide-sugar modifying enzymes. hUXS contains bound NAD(+) cofactor that it recycles by first oxidizing UDP-α-D-glucuronic acid (UGA), and then reducing UDP-α-D-4-keto-xylose (UX4O) to produce (UDX). Despite observation purified cofactor, has been reported exogenous will stimulate enzyme activity. Here we show small fraction releases NADH UX4O intermediates as products during turnover. The...
Ketopantoate reductase (KPR) catalyzes the NADPH-dependent production of pantoate, an essential precursor in biosynthesis coenzyme A. Previous structural studies have been limited to Escherichia coli KPR, a monomeric enzyme that follows sequential ordered mechanism. Here we report crystal structure Staphylococcus aureus at 1.8 Å resolution, first description dimeric KPR. Using sedimentation velocity analysis, show S. KPR dimer is stable solution. In fact, our analysis shows assembly identify...