Closure of tubular patent ductus arteriosus in infants with the Amplatzer Vascular Plug II.

Objectives: We used the Amplatzer Vascular Plug II to close tubular patent ductus arteriosus (DA) in infants.

Background: Despite advancements in device design, catheter-based therapy for the DA of tubular morphology has been problematic. Likewise, the currently available devices are not designed to close DAs in small, often premature infants as the size of the delivery systems can be prohibitive and the devices obstructive to aortic or pulmonary artery flow.

Fiber diffraction as a screen for amyloid inhibitors.

Targeting the initial formation of amyloid assemblies is a preferred approach to therapeutic intervention in amyloidoses, which include such diseases as Alzheimer's, Parkinson's, Huntington's, etc., as the early-stage, oligomers that form before the development of beta-conformation-rich fibers are thought to be toxic. X-ray patterns from amyloid assemblies always show two common intensity maxima: one at 4.

Formation of amyloid fibrils in vitro by human gammaD-crystallin and its isolated domains.

Purpose: Amyloid fibrils are associated with a variety of human protein misfolding and protein deposition diseases. Previous studies have shown that bovine crystallins form amyloid fibers under denaturing conditions and amyloid fibers accumulate in the lens of mice carrying mutations in crystallin genes. Within differentiating lens fiber cells, crystallins may be exposed to low pH lysosome compartments.

Cytoplasmic domain of zebrafish myelin protein zero: adhesive role depends on beta-conformation.

Solution spectroscopy studies on the cytoplasmic domain of human myelin protein zero (P0) (hP0-cyt) suggest that H-bonding between beta-strands from apposed molecules is likely responsible for the tight cytoplasmic apposition in compact myelin. As a follow-up to these findings, in the current study we used circular dichroism and x-ray diffraction to analyze the same type of model membranes previously used for hP0-cyt to investigate the molecular mechanism underlying the zebrafish cytoplasmic apposition. This space is significantly narrower in teleosts compared with that in higher vertebrates, and can be accounted for in part by the much shorter cytoplasmic domain in the zebrafish protein (zP0-cyt).