Spatiotemporal control of subcellular O-GlcNAc signaling using Opto-OGT.

The post-translational modification of intracellular proteins through O-linked β-N-acetylglucosamine (O-GlcNAc) is a conserved regulatory mechanism in multicellular organisms. Catalyzed by O-GlcNAc transferase (OGT), this dynamic modification has an essential role in signal transduction, gene expression, organelle function and systemic physiology. Here, we present Opto-OGT, an optogenetic probe that allows for precise spatiotemporal control of OGT activity through light stimulation.

Toxoplasmosis Frequency Rate in Rheumatoid Arthritis Patients in Northeastern Iran.

Background: Toxoplasmosis is a zoonotic disease caused by the parasite a cosmopolitan intracellular parasite. It can be a risk factor for auto-immune diseases, including rheumatoid arthritis (RA). This study was designed to investigate the possible association between serological history of infection and defined clinical manifestation of RA in Northeast of Iran.

Evaluation of a joint adult and pediatric clinic for cancer survivorship care.

Objectives: The best model of care for long-term follow-up of survivors of childhood cancer is uncertain. We describe the care experience provided by the joint adult/pediatric AfterCare Clinic at the McMaster Children's Hospital. Secondary outcomes include an evaluation of cancer worry, self-management skills, and loss to follow-up rates.

Detection of food additives by voltammetry at the liquid-liquid interface.

Electrochemistry at the liquid-liquid interface enables the detection of nonredoxactive species with electroanalytical techniques. In this work, the electrochemical behavior of two food additives, aspartame and acesulfame K, was investigated. Both ions were found to undergo ion-transfer voltammetry at the liquid-liquid interface.

Fidelity of seryl-tRNA synthetase to binding of natural amino acids from HierDock first principles computations.

Seryl-tRNA synthetase (SerRS) charges serine to tRNA(Ser) following the formation of a seryl adenylate intermediate, but the extent to which other non-cognate amino acids compete with serine to bind to SerRS or for the formation of the activated seryl adenylate intermediate is not known. To examine the mechanism of discrimination against non-cognate amino acids, we calculated the relative binding energies of the 20 natural amino acids to SerRS. Starting with the crystal structure of SerRS from Thermus thermophilus with seryl adenylate bound, we used the HierDock and SCREAM (Side-Chain Rotamer Energy Analysis Method) computational methods to predict the binding conformation and binding energy of each of the 20 natural amino acids in the binding site in the best-binding mode and the activating mode.