Virtual postoperative visits following robotic gynecologic surgery: a study of patient satisfaction, safety, and feasibility.

Since the onset of the COVID-19 pandemic the use of telehealth has burgeoned. Numerous surgical specialties have already adopted the use of virtual postoperative visits, but there is data lacking in both robotics and gynecology. In this single-institution prospective cohort study we sought to evaluate the patient satisfaction, feasibility and safety of postoperative telehealth visits following robotic gynecologic surgery. Thirty-three patients undergoing robotic gynecologic procedures participated in a postoperative telehealth visit approximately 2 weeks following surgery, of which 27 completed a survey which assessed participant satisfaction with the telehealth visit, overall health-related quality of life following surgery, exposure to telehealth visits, and social determinants of health. The mean satisfaction score was just below 'excellent'. Only 2 participants (6.3%) required an in-person visit. Postoperative telehealth visit satisfaction score was significantly associated only with BMI (Pearson r = 0.45, p = 0.018). These data suggest that telehealth visits following robotic gynecologic procedures appear to be safe and feasible, and are associated with a high level of patient satisfaction.

Heteromerization of ligand binding domains of N-methyl-D-aspartate receptor requires both coagonists, L-glutamate and glycine.

NMDA receptors (NMDAR) are voltage- and glutamate-gated heteromeric ion channels found at excitatory neuronal synapses, the functions of which are to mediate the mechanisms of brain plasticity and, thereby, its higher order functions. In addition to Glu, the activation of these heteromeric receptors requires Gly or d-Ser as a coagonist. However, it is not fully known as to why coagonism is required for the opening of NMDAR ion channels. We show herein that the ligand binding domains (LBD) of the GluN1 and GluN2A subunits of the NMDAR heterodimerize only when both coagonists, Glu and Gly/d-Ser, bind to their respective sites on GluN2 and GluN1. In the agonist-free state, these domains form homomeric interactions, which are disrupted by binding of their respective agonists. Also, in a heteromer formed by the LBDs, GluN2A is more sensitized to bind Glu, while the affinity of Gly for GluN1 remains unchanged. We thus provide direct evidence to show that coagonism is necessary for heteromeric pairing of LBDs, which is an essential step in forming functional ion channels in NMDARs.