Meta-Analysis of Risk Factors for Congenital Heart Disease: Part 2, Maternal Medication, Reproductive Technologies, and Familial and Fetal Factors.

Background: The quantitative effects of congenital heart disease (CHD) risk factors are not fully understood. We conducted a meta-analysis of all CHD risk factors. This report explores maternal medication, assisted reproductive technologies (ART), and familial and fetal factors.

Systematic Review and Meta-analysis of Prenatal Risk Factors for Congenital Heart Disease: Part 1, Maternal Chronic Diseases and Parental Exposures.

Background: There is considerable heterogeneity in studies on prenatal risk factors for congenital heart diseases (CHDs). We performed a meta-analysis of all nongenetic factors of CHDs. This report presents results of factors related to maternal chronic diseases and parental exposures.

Patterns of oral anticoagulants use in atrial fibrillation.

Background: Novel oral anticoagulants are available for the management of atrial fibrillation and are considered more convenient to use than warfarin.

Objective: The main objective of this study was to describe patterns of oral anticoagulant use in the 6 months period following the availability of dabigatran at our hospital.

Methods: A cross-sectional study was conducted in a single University hospital in the province of Québec, Canada.

The C-terminal residues in the alpha-interacting domain (AID) helix anchor CaV beta subunit interaction and modulation of CaV2.3 channels.

The alpha-interacting domain (AID) in the I-II linker of high voltage-activated (HVA) Ca(2+) channel alpha1 subunits binds with high affinity to Ca(V)beta auxiliary subunits. The recently solved crystal structures of the AID-Ca(V)beta complex in Ca(V)1.1/1.

Protein motions promote catalysis.

A relationship between molecular dynamics motions of noncatalytic residues and enzyme activity has recently been proposed. We present examples where mutations either near or distal from the active site residues modify internal enzyme motion with resulting modification of catalysis. A better understanding of internal protein motions correlated to catalysis will lead to a greater insight into enzyme function.