Aspergillus terreus Spondylodiscitis in an Immunocompromised Child.

We report the case of a 12-year-old immunocompromised boy with spondylodiscitis of the thoracolumbar spine caused by Aspergillus terreus. Microbiologic diagnosis was confirmed by inoculation of aspiration fluid into blood culture bottles. Because of noncompliance, the patient was treated with extended voriconazole therapy (23 months) with regular serum drug concentration monitoring and intermittent direct observation therapy in an outpatient clinic.

Isoproterenol Enhances Tumor Necrosis Factor-Related Apoptosis-Inducing Ligand-Induced Apoptosis in Human Embryonic Kidney Cells through Death Receptor 5 up-Regulation.

Background And Objectives: Chronic impairment of β-adrenergic receptor signaling increases cardiac apoptosis, hypertrophy and fibrosis. The aim of this study was to investigate whether isoproterenol (ISO), an agonist of the adrenergic receptor, can enhance tumor necrosis factor-related apoptosis-inducing ligand (TRAIL)-induced apoptosis in human embryonic kidney (HEK) 293 cells.

Materials And Methods: HEK 293 cells were treated with ISO and/or TRAIL for 24 hours.

Purification, crystallization and preliminary X-ray diffraction analysis of enoyl-acyl carrier protein reductase (FabK) from Streptococcus mutans strain UA159.

A triclosan-resistant flavoprotein termed FabK is the sole enoyl-acyl carrier protein reductase in Streptococcus pneumoniae and Streptococcus mutans. In this study, FabK from S. mutans strain UA159 was overexpressed in Escherichia coli, purified and crystallized.

Overexpression, crystallization and preliminary X-ray crystallographic analysis of the RNA polymerase domain of primase from Streptococcus mutans strain UA159.

Primase is the enzyme that synthesizes RNA primers on single-stranded DNA during normal DNA replication. In this study, the catalytic core domain of primase from Streptococcus mutans UA159 was overexpressed in Escherichia coli, purified and crystallized. Diffraction data were collected to 1.

Overexpression, purification, crystallization and preliminary X-ray crystallographic analysis of the C-terminal domain of the GyrA subunit of DNA gyrase from Staphylococcus aureus strain Mu50.

DNA gyrase is a type II topoisomerase that is essential for chromosome segregation and cell division owing to its ability to modify the topological form of bacterial DNA. In this study, the C-terminal domain of the GyrA subunit of DNA gyrase from Staphylococcus aureus Mu50 strain was overexpressed in Escherichia coli, purified and crystallized. Diffraction data were collected to 2.

Cloning, purification, crystallization and preliminary X-ray crystallographic analysis of the N-terminal domain of DEAD-box RNA helicase from Staphylococcus aureus strain Mu50.

DEAD-box helicases are enzymes with an ATP-dependent RNA-unwinding function that are involved in a variety of cellular processes including RNA splicing, ribosome biogenesis and RNA degradation. In this study, the N-terminal domain of DEAD-box RNA helicase from Staphylococcus aureus strain Mu50 was overexpressed in Escherichia coli, purified and crystallized. Diffraction data were collected to 2.

Preliminary X-ray crystallographic analysis of the breakage-reunion domain of the GyrA subunit of DNA gyrase from Colwellia psychrerythraea strain 34H.

DNA gyrase is a type II topoisomerase that is essential for chromosome segregation and cell division owing to its ability to modify the topological forms of bacterial DNA. In this study, the N-terminal breakage-reunion domain of the GyrA subunit of DNA gyrase from Colwellia psychrerythraea 34H was overexpressed in Escherichia coli, purified and crystallized. Diffraction data were collected to 2.

Crystallization and preliminary X-ray crystallographic analysis of DNA gyrase GyrB subunit from Xanthomonas oryzae pv. oryzae.

DNA gyrase is a type II topoisomerase that is essential for chromosome segregation and cell division owing to its ability to modify the topological forms of bacterial DNA. In this study, the N-terminal fragment of the GyrB subunit of DNA gyrase from Xanthomonas oryzae pv. oryzae was overexpressed in Escherichia coli, purified and crystallized.

Molecular mechanism for the regulation of human ACC2 through phosphorylation by AMPK.

Acetyl-CoA carboxylases (ACCs) have been highlighted as therapeutic targets for obesity and diabetes, as they play crucial roles in fatty acid metabolism. ACC activity is regulated through the short-term mechanism of inactivation by reversible phosphorylation. Here, we report the crystal structures of the biotin carboxylase (BC) domain of human ACC2 phosphorylated by AMP-activated protein kinase (AMPK).

The pap1(+) gene of fission yeast is transcriptionally regulated by nitrosative and nutritional stress.

In the current work, regulation of the pap1(+) gene was investigated by the use of the pap1(+)-lacZ fusion gene and semi-quantitative reverse transcriptase-PCR. The synthesis of beta-galactosidase from the pap1(+)-lacZ fusion gene was significantly enhanced by nitric oxide (NO)-generating sodium nitroprusside (SNP) and nitrogen starvation. However, the induction by SNP and nitrogen starvation was observed to be much less in the Pap1p-negative cells harboring the fusion gene.