The 'White-eyed' Orbital Blowout Fracture: An Easily Overlooked Injury in Maxillofacial Trauma.

The 'white-eyed' blowout fracture (WEBOF) is an injury that is often overlooked in head trauma patients, as it often has few overt clinical and radiographic features. Although benign in appearance, it can lead to significant patient morbidity. Here, we intend to increase the awareness of WEBOF and provide general principles for its diagnosis. WEBOF should be recognized early to ensure timely management and a successful outcome.

Asystole in Orthognathic Surgery: A Case Report.

A previously healthy 26-year-old man presented for elective Le Fort I osteotomy, bilateral mandibular osteotomy, and genioplasty. During the intraoperative course, the patient developed sudden bradycardia and asystole on placement of a bite block. Asystole is an extremely rare consequence of the trigeminocardiac reflex, and awareness of this potentially life-threatening complication is pivotal in its management.

Wireless Monitoring for Office-Based Anesthesia.

Current research on wireless hemodynamic monitoring during anesthesia is limited as the topic is just beginning to be explored. The aim of this article is to stimulate technological advancements in monitored anesthesia care that will increase safety and efficiency. Here, we introduce this exciting new concept and propose an innovative model for monitoring patients undergoing office-based anesthesia.

Think twice before prescribing certain drugs to children.

Codeine, tramadol, and hydrocodone have been associated with morbidity and death in children, secondary to respiratory depression. The aim of this paper is to increase awareness of this issue and to encourage clinicians to prescribe safer alternatives such as morphine, ibuprofen, or paracetamol.

Stable folding core in the folding transition state of an alpha-helical integral membrane protein.

Defining the structural features of a transition state is important in understanding a folding reaction. Here, we use Φ-value and double mutant analyses to probe the folding transition state of the membrane protein bacteriorhodopsin. We focus on the final C-terminal helix, helix G, of this seven transmembrane helical protein. Φ-values could be derived for 12 amino acid residues in helix G, most of which have low or intermediate values, suggesting that native structure is disrupted at these amino acid positions in the transition state. Notably, a cluster of residues between E204 and M209 all have Φ-values close to zero. Disruption of helix G is further confirmed by a low Φ-value of 0.2 between residues T170 on helix F and S226 on helix G, suggesting the absence of a native hydrogen bond between helices F and G. Φ-values for paired mutations involved in four interhelical hydrogen bonds revealed that all but one of these bonds is absent in the transition state. The unstructured helix G contrasts with Φ-values along helix B that are generally high, implying native structure in helix B in the transition state. Thus helix B seems to constitute part of a stable folding nucleus while the consolidation of helix G is a relatively late folding event. Polarization of secondary structure correlates with sequence position, with a structured helix B near the N terminus contrasting with an unstructured C-terminal helix G.