Correlating Thermodynamics with Cognitive Outcomes in Magnetic Resonance-guided Laser Interstitial Thermal Therapy (MRgLITT) of a Pediatric Hypothalamic Hamartoma.

Objective: Magnetic resonance-guided laser interstitial thermal therapy (MRgLITT) is a commonly used clinical method of destroying intracranial brain foci. Our objective was to correlate the thermal damage estimate transition zone with cognitive outcomes in MRgLITT of a pediatric hypothalamic hamartoma.

Methods: Uncomplicated MRgLITT was used to disconnect an 8-mm left Delalande grade II hypothalamic hamartoma (HH) revealed on neuroimaging of a 17-year-old male patient with drug-resistant epilepsy and a "gelastic +" semiology including both gelastic and tonic-clonic seizures.

Profound Hypotonia and Respiratory Failure due to Suspected Nemaline Myopathy in a Preterm Infant.

Congenital myopathies, such as nemaline myopathy, may present with hypotonia and respiratory failure in the neonatal period. Respiratory function can be further compromised in affected infants by the development of chylous effusions. We present the case of a preterm male infant born at 32 weeks' gestation, who was profoundly hypotonic and required intubation at birth.

Structural and topographical studies of the type IV bundle-forming pilus assembly complex of enteropathogenic Escherichia coli.

The type IV bundle-forming pili (BFP) of enteropathogenic Escherichia coli (EPEC) are required for virulence in orally challenged human volunteers and for the localized adherence and autoaggregation in vitro phenotypes. BFP filament biogenesis and function are encoded by the 14-gene bfp operon. The BFP assembly complex, containing a BfpB-His6 fusion protein, was chemically cross-linked in situ, and the complex was then purified from BFP-expressing EPEC by a combination of nickel- and BfpB antibody-based affinity chromatography.

The type IV pilus assembly complex: biogenic interactions among the bundle-forming pilus proteins of enteropathogenic Escherichia coli.

Production of type IV bundle-forming pili (BFP) by enteropathogenic Escherichia coli (EPEC) requires the protein products of 12 genes of the 14-gene bfp operon. Antisera against each of these proteins were used to demonstrate that in-frame deletion of individual genes within the operon reduces the abundance of other bfp operon-encoded proteins. This result was demonstrated not to be due to downstream polar effects of the mutations but rather was taken as evidence for protein-protein interactions and their role in the stabilization of the BFP assembly complex.