Implementation of Partnered Pharmacist Medication Charting in haematology and oncology inpatients.

Aim: Partnered Pharmacist Medication Charting (PPMC) in patients admitted under general medical units has been shown to reduce medication errors. The aim of this study is to evaluate the impact of the PPMC model on medication errors in patients admitted under cancer units in Victorian hospitals.

Methods: A prospective cohort study comparing cohorts before and after the introduction of PPMC was conducted.

Monoterpenoid aryl hydrocarbon receptor allosteric antagonists protect against ultraviolet skin damage in female mice.

The human aryl hydrocarbon receptor (AhR) is a ligand-activated transcription factor that is a pivotal regulator of human physiology and pathophysiology. Allosteric inhibition of AhR was previously thought to be untenable. Here, we identify carvones as noncompetitive, insurmountable antagonists of AhR and characterize the structural and functional consequences of their binding.

Partnered pharmacist medication charting (PPMC) in regional and rural general medical patients.

Objective: Errors in hospital medication charts are commonly encountered and have been associated with morbidity and mortality. This study evaluates the impact of the Partnered Pharmacist Medication Charting (PPMC) model on medication errors in general medical patients admitted to rural and regional hospitals.

Design/method: A prospective cohort study, comparing before and after the introduction of PPMC was conducted in 13 rural and regional health services.

Liquid-Liquid Phase Transition Drives Intra-chloroplast Cargo Sorting.

In eukaryotic cells, organelle biogenesis is pivotal for cellular function and cell survival. Chloroplasts are unique organelles with a complex internal membrane network. The mechanisms of the migration of imported nuclear-encoded chloroplast proteins across the crowded stroma to thylakoid membranes are less understood.

Nucleus-Encoded Protein BFA1 Promotes Efficient Assembly of the Chloroplast ATP Synthase Coupling Factor 1.

F-type ATP synthases produce nearly all of the ATP found in cells. The catalytic module F commonly comprises an αβ hexamer surrounding a γ/ε stalk. However, it is unclear how these subunits assemble to form a catalytic motor.

The crystal structure of Deg9 reveals a novel octameric-type HtrA protease.

The high temperature requirement A (HtrA) proteases (also termed Deg proteases) play important roles in diverse organisms by regulating protein quality and quantity. One of the 16 Arabidopsis homologs, Deg9, is located in the nucleus where it modulates cytokinin- and light-mediated signalling via degrading the ARABIDOPSIS RESPONSE REGULATOR 4 (ARR4). To uncover the structural features underlying the proteolytic activity of Deg9, we determined its crystal structure.

Crystal structure of glutamate-1-semialdehyde-2,1-aminomutase from Arabidopsis thaliana.

Glutamate-1-semialdehyde-2,1-aminomutase (GSAM) catalyzes the isomerization of glutamate-1-semialdehyde (GSA) to 5-aminolevulinate (ALA) and is distributed in archaea, most bacteria and plants. Although structures of GSAM from archaea and bacteria have been resolved, a GSAM structure from a higher plant is not available, preventing further structure-function analysis. Here, the structure of GSAM from Arabidopsis thaliana (AtGSA1) obtained by X-ray crystallography is reported at 1.

Crystal structure of methylesterase family member 16 (MES16) from Arabidopsis thaliana.

Methylesterase family member 16 (MES16) is an integral component of chlorophyll breakdown. It catalyzes the demethylation of fluorescent chlorophyll catabolite (FCC) and pheophorbide in vitro, and specifically demethylates FCC in vivo. Here we report the crystal structure of MES16 from Arabidopsis thaliana at 2.

Crystal structure of the catalytic subunit of magnesium chelatase.

Tetrapyrroles, including haem and chlorophyll, play vital roles for various biological processes, such as respiration and photosynthesis, and their biosynthesis is critical for virtually all organisms. In photosynthetic organisms, magnesium chelatase (MgCh) catalyses insertion of magnesium into the centre of protoporphyrin IX, the branch-point precursor for both haem and chlorophyll, leading tetrapyrrole biosynthesis into the magnesium branch(1,2). This reaction needs a cooperated action of the three subunits of MgCh: the catalytic subunit ChlH and two AAA(+) subunits, ChlI and ChlD (refs 3-5).