A pilot study on an electromagnetic tracking system using tunneling magnetoresistance (TMR) sensors applicable to a 4F catheter (1.4 mm in diameter).

PURPOSE: Tracking the position and orientation of a 4F catheter ([Formula: see text] 1.4 mm) is required in superselective intra-arterial chemotherapy (SSIAC). Tunneling magnetoresistance (TMR) sensors, which measure magnetic fields, are promising candidates because the size of the TMR sensor can be less than a few tenths of a millimeter. The purpose of this paper is to prove the feasibility of an EMT system utilizing TMR sensors as magnetometers. METHODS: Three 1-axis TMR sensors (0.3 mm × 0.3 mm) were packaged on a flexible printed circuit board (PCB) together with an amplifier chip. The PCB was integrated into a 4F catheter. Six field generator coils driven by alternating current (AC) at different frequencies were used. Magnetic field measurement errors were evaluated to assess the effect of electromotive force (EMF) on TMR-based sensing by changing the coils' driving frequencies. The tracking error was also evaluated. As a result, the feasibility of catheter navigation utilizing the EMT system was demonstrated. RESULTS: There was a positive correlation between the frequency and the magnetic field measurement error using the TMR sensor (R2 = 0.999). With magnetic field frequencies less than 603 Hz, the average position and orientation estimation error were 10.1 mm and 2.3 degree, respectively. Under ideal conditions, the average estimation error values were 0.9 mm and 0.3 degree, respectively. CONCLUSION: The position and orientation errors varied with frequency owing to the induced electromotive force. We should consider the effect of electromotive force on TMR sensor assemblies caused by alternating magnetic fields. An EMT system using TMR sensors was validated, although room for further improvement was identified.

Catalytic properties and crystal structure of UDP-galactose 4-epimerase-like l-threonine 3-dehydrogenase from Phytophthora infestans.

We report, for the first time, the three-dimensional structure and biochemical properties of a UDP-galactose 4-epimerase-like l-threonine 3-dehydrogenase (GalE-like L-ThrDH) from Phytophthora infestans, a plant disease-causing fungus. We identified GalE-like L-ThrDH using Kyoto Encyclopedia of Genes and Genomes (KEGG) database as a candidate target for the development of a new fungicide. The GalE-like L-ThrDH gene was expressed in Escherichia coli, and its product was purified and characterized. N-Acetylglycine was found to act as a competitive inhibitor of the enzyme (Ki =0.18 mM). The crystal structure of the unique hexameric GalE-like L-ThrDH was determined using the molecular replacement method at a resolution of 2.3 Å, in the presence of NAD+ and citrate, an analogue of the substrate. Based on the molecular docking simulation, N-acetylglycine molecule was modeled into the active site and the binding mode and inhibition mechanism of N-acetylglycine were elucidated.

Influenza A virus nucleoprotein is acetylated by histone acetyltransferases PCAF and GCN5.

Histone acetylation plays crucial roles in transcriptional regulation and chromatin organization. Viral RNA of the influenza virus interacts with its nucleoprotein (NP), whose function corresponds to that of eukaryotic histones. NP regulates viral replication and has been shown to undergo acetylation by the cAMP-response element (CRE)-binding protein (CBP) from the host. However, whether NP is the target of other host acetyltransferases is unknown. Here, we show that influenza virus NP undergoes acetylation by the two host acetyltransferases GCN5 and P300/CBP-associated factor (PCAF) and that this modification affects viral polymerase activities. Western blot analysis with anti-acetyl-lysine antibody on cultured A549 human lung adenocarcinoma epithelial cells infected with different influenza virus strains indicated acetylation of the viral NP. A series of biochemical analyses disclosed that the host lysine acetyltransferases GCN5 and PCAF acetylate NP in vitro MS experiments identified three lysine residues as acetylation targets in the host cells and suggested that Lys-31 and Lys-90 are acetylated by PCAF and GCN5, respectively. RNAi-mediated silencing of GCN5 and PCAF did not change acetylation levels of NP. However, interestingly, viral polymerase activities were increased by the PCAF silencing and were decreased by the GCN5 silencing, suggesting that acetylation of the Lys-31 and Lys-90 residues has opposing effects on viral replication. Our findings suggest that epigenetic control of NP via acetylation by host acetyltransferases contributes to regulation of polymerase activity in the influenza A virus.