BackgroundEffective communication is critical for patient safety. One potential threat to communication in the operating room is incivility. Although examined in other industries, little has been done to examine how incivility impacts the ability to deliver safe care in a crisis. We therefore sought to determine how incivility influenced anaesthesiology resident performance during a standardised simulation scenario of occult haemorrhage.MethodsThis is a multicentre, prospective, randomised control trial from three academic centres. Anaesthesiology residents were randomly assigned to either a normal or ‘rude’ environment and subjected to a validated simulated operating room crisis. Technical and non-technical performance domains including vigilance, diagnosis, communication and patient management were graded on survey with Likert scales by blinded raters and compared between groups.Results76 participants underwent randomisation with 67 encounters included for analysis (34 control, 33 intervention). Those exposed to incivility scored lower on every performance metric, including a binary measurement of overall performance with 91.2% (control) versus 63.6% (rude) obtaining a passing score (p=0.009). Binary logistic regression to predict this outcome was performed to assess impact of confounders. Only the presence of incivility reached statistical significance (OR 0.110, 95% CI 0.022 to 0.544, p=0.007). 65% of the rude group believed the surgical environment negatively impacted performance; however, self-reported performance assessment on a Likert scale was similar between groups (p=0.112).ConclusionAlthough self-assessment scores were similar, incivility had a negative impact on performance. Multiple areas were impacted including vigilance, diagnosis, communication and patient management even though participants were not aware of these effects. It is imperative that these behaviours be eliminated from operating room culture and that interpersonal communication in high-stress environments be incorporated into medical training.

We report the first synthesis of taxadiene-4(5)-epoxide, which rearranges upon acid treatment to produce products of relevance to taxol biosynthesis.

BASIC AND TRANSLATIONAL ATcapabilities. Thus, colonic SELENOP is the most informative means to assess selenium levels and activity in IBD patients and may serve as a novel biomarker for UC disease severity and identify patients most predisposed to CAC development.

Ezrin is a key regulator of cancer metastasis that links the extracellular matrix to the actin cytoskeleton and regulates cell morphology and motility. We discovered a small-molecule inhibitor, NSC305787, that directly binds to ezrin and inhibits its function. In this study, we used a nano-liquid chromatography-tandem mass spectrometry (nano-LC-MS-MS)-based proteomic approach to identify ezrin-interacting proteins that are competed away by NSC305787. A large number of the proteins that interact with ezrin were implicated in protein translation and stress granule dynamics. We validated direct interaction between ezrin and the RNA helicase DDX3, and NSC305787 blocked this interaction. Downregulation or long-term pharmacological inhibition of ezrin led to reduced DDX3 protein levels without changes in DDX3 mRNA. Ectopic overexpression of ezrin in low-ezrin-expressing osteosarcoma cells caused a notable increase in DDX3 protein levels. Ezrin inhibited the RNA helicase activity of DDX3 but increased its ATPase activity. Our data suggest that ezrin controls the translation of mRNAs preferentially with a structured 5= untranslated region, at least in part, by sustaining the protein level of DDX3 and/or regulating its function. Therefore, our findings suggest a novel function for ezrin in regulation of gene translation that is distinct from its canonical role as a cytoskeletal scaffold at the cell membrane. Ezrin is a prototype member of the ERM (ezrin-radixin-moesin) family of proteins that functions as a scaffold between the plasma membrane and the underlying cortical actin cytoskeleton (1, 2). Ezrin regulates cytoskeletal dynamics in response to both internal and external stimuli through its intracellular localization and protein binding activities; thus, it plays an important role in the maintenance of cell shape, cell polarity, adhesion, and movement (3). All members of the ERM family are characterized by the presence of a shared FERM domain at the amino terminus, which can bind to transmembrane proteins, including CD43, CD44, CD95, ICAMs, syndecan 2, EBP50/NHERF1, and E3KARP/NHERF2. The carboxy termini of ERM proteins contain an F-actin binding domain, which both regulates intramolecular interactions with amino-terminal FERM domains and promotes F-actin organization. The pleiotropic functions of ezrin in a wide range of cellular processes can be explained through its association with numerous proteins with diverse functions (4). Several lines of evidence have indicated that ezrin can oscillate between various "open/active" and "closed/dormant" states, which are regulated by self-association of N-terminal and Cterminal regions. Head-to-tail folding of the molecule likely masks the respective protein binding sites and leads to the localization of ezrin in the cytoplasm in its monomeric form. The conformational switch to an open state requires direct interaction with the plasma membrane phospholipid phosphatidylinositol 4,5-bisphosphate [PI(4,5)P 2 ] and phosphorylation of a conserved threonine (T567) located in the ...