Infrared Absorption at 10.6 μ in GaAs

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Observation of mode locking and ultrashort optical pulses induced by antisotropic molecular liquids

Mode locking and ultrashort pulses have been produced in a giant-pulse ruby laser with heated nitrobenzene (T > 110°C) or -chloronaphthalene (T > 62°C) inside the optical resonator. 10^(–11)-sec pulses were observed with the two-photon fluorescence technique

Stable, Chirped, Ultrashort Pulses in Lasers Using the Optical Kerr Effect

A self‐consistent analysis of pulse propagation inside a laser cavity containing, in addition to an amplifying medium, some material displaying the optical Kerr effect, yields ultrashort pulses. These pulses become stable in the limit of high line‐center excess gain with the stabilization provided by an interplay between strong chirping in the Kerr medium and bandlimiting in the laser medium

The O-GlcNAc transferase OGT is a conserved and essential regulator of the cellular and organismal response to hypertonic stress.

The conserved O-GlcNAc transferase OGT O-GlcNAcylates serine and threonine residues of intracellular proteins to regulate their function. OGT is required for viability in mammalian cells, but its specific roles in cellular physiology are poorly understood. Here we describe a conserved requirement for OGT in an essential aspect of cell physiology: the hypertonic stress response. Through a forward genetic screen in Caenorhabditis elegans, we discovered OGT is acutely required for osmoprotective protein expression and adaptation to hypertonic stress. Gene expression analysis shows that ogt-1 functions through a post-transcriptional mechanism. Human OGT partially rescues the C. elegans phenotypes, suggesting that the osmoregulatory functions of OGT are ancient. Intriguingly, expression of O-GlcNAcylation-deficient forms of human or worm OGT rescue the hypertonic stress response phenotype. However, expression of an OGT protein lacking the tetracopeptide repeat (TPR) domain does not rescue. Our findings are among the first to demonstrate a specific physiological role for OGT at the organismal level and demonstrate that OGT engages in important molecular functions outside of its well described roles in post-translational O-GlcNAcylation of intracellular proteins