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A 100 W Yb-doped, fiber-based, femtosecond, chirped pulse amplification laser system was developed with a repetition rate of 1 MHz, corresponding to a pulse energy of 100 µJ. Large-scale, fused-silica transmission gratings were used for both the pulse stretcher and compressor, with a compression throughput efficiency of ∼85%. A pulse duration of 270 fs was measured by second harmonic generation frequency-resolved optical gating (SHG-FROG). To the best of our knowledge, this is the shortest pulse duration ever achieved by a 100-W-level fiber chirped pulse amplification laser system at a repetition rate of few megahertz, without any special post-compression manipulation. [ABSTRACT FROM AUTHOR]

Techniques to measure and manipulate the carrier-envelope phase within femtosecond optical parametric oscillators (OPOs) allow their outputs to be stabilized in a way that produces a frequency comb structure, potentially tunable throughout the transparency band of the gain material. In this review we describe the fundamental principles of phase control, on which the development of singly- and doubly-resonant OPO frequency combs is based. We give examples of practical embodiments of such combs, and discuss in detail several applications, including spectroscopy, metrology, quantum computation and astrophotonics. [ABSTRACT FROM AUTHOR]

Toll-like receptor 4 (TLR4) is an indispensable immune receptor for lipopolysaccharide (LPS), a major component of the Gram-negative bacterial cell wall. Following LPS stimulation, TLR4 transmits the signal from the cell surface and becomes internalized in an endosome. However, the spatial regulation of TLR4 signaling is not fully understood. Here, we investigated the mechanisms of LPS-induced TLR4 internalization and clarified the roles of the extracellular LPS-binding molecules, LPS-binding protein (LBP), and glycerophosphatidylinositol-anchored protein (CD14). LPS stimulation of CD14-expressing cells induced TLR4 internalization in the presence of serum, and an inhibitory anti-LBP mAb blocked its internalization. Addition of LBP to serum-free cultures restored LPS-induced TLR4 internalization to comparable levels of serum. The secretory form of the CD14 (sCD14) induced internalization but required a much higher concentration than LBP. An inhibitory anti-sCD14 mAb was ineffective for serum-mediated internalization. LBP lacking the domain for LPS transfer to CD14 and a CD14 mutant with reduced LPS binding both attenuated TLR4 internalization. Accordingly, LBP is an essential serum molecule for TLR4 internalization, and its LPS transfer to membrane-anchored CD14 (mCD14) is a prerequisite. LBP induced the LPS-stimulated phosphorylation of TBK1, IKKϵ, and IRF3, leading to IFN-β expression. However, LPS-stimulated late activation of NF-κB or necroptosis were not affected. Collectively, our results indicate that LBP controls LPS-induced TLR4 internalization, which induces TLR adaptor molecule 1 (TRIF)-dependent activation of the TBK1–IKKϵ–IRF3–IFN-β pathway. In summary, we showed that LBP-mediated LPS transfer to mCD14 is required for serum-dependent TLR4 internalization and activation of the TRIF pathway. [ABSTRACT FROM AUTHOR]