Ocular Side Effects of Common Systemic Medications and Systemic Side Effects of Ocular Medications.

When prescribing medications, it is important to consider the ocular side effects of common systemic therapy as well as potential systemic side effects of ocular medications. Although not an exhaustive list of medications/classes of medications, this article does include many commonly used drugs and also provides information on some topical therapies commonly used by ophthalmologists. These ocular medications may result in systemic effects and/or alter patients' management of systemic conditions.

Optimal in-hospital defibrillator placement.

Aims: To determine if mathematical optimization of in-hospital defibrillator placements can reduce in-hospital cardiac arrest-to-defibrillator distance compared to existing defibrillators in a single hospital.

Methods: We identified treated IHCAs and defibrillator placements in St. Michael's Hospital in Toronto, Canada from Jan.

Viral Retinopathy in Experimental Models of Zika Infection.

Purpose: Emerging evidence has shown that both congenital and adult Zika virus (ZIKV) infection can cause eye diseases. The goals of the current study were to explore mechanisms and pathophysiology of ZIKV-induced eye defects.

Methods: Wild-type or A129 interferon type I receptor-deficient mice were infected by either FSS13025 or Mex1-7 strain of ZIKV.

Structures of cGMP-Dependent Protein Kinase (PKG) Iα Leucine Zippers Reveal an Interchain Disulfide Bond Important for Dimer Stability.

cGMP-dependent protein kinase (PKG) Iα is a central regulator of smooth muscle tone and vasorelaxation. The N-terminal leucine zipper (LZ) domain dimerizes and targets PKG Iα by interacting with G-kinase-anchoring proteins. The PKG Iα LZ contains C42 that is known to form a disulfide bond upon oxidation and to activate PKG Iα.

Crystal structure of the cGMP-dependent protein kinase II leucine zipper and Rab11b protein complex reveals molecular details of G-kinase-specific interactions.

cGMP-dependent protein kinase (PKG)-interacting proteins (GKIPs) mediate cellular targeting of PKG isoforms by interacting with their leucine zipper (LZ) domains. These interactions prevent aberrant signaling cross-talk between different PKG isotypes. To gain detailed insight into isotype-specific GKIP recognition by PKG, we analyzed the type II PKG leucine zipper domain and found that residues 40-83 dimerized and specifically interacted with Rab11b.