A LiNbO3 Active Switch Coupler at 2050 nm for Differential Absorption Lidar and Atmospheric Gas Monitoring

International audienceWe report, for what we believe is the first time, the design and the fabrication of an active optical switch working at 2050 nm. The switch uses a lithium niobate crystal and is fully packaged. It is based on a three-section alternating Delta beta configuration. It is dedicated to differential absorption lidar (DIAL) and atmospheric gas monitoring

Capteurs bio-chimiques Groupe III : capteurs acoustiques et optiques

Etude recouvrant les subventions 91-B-0270 a 91-B-0279 inclusesSIGLEAvailable at INIST (FR), Document Supply Service, under shelf-number : AR 15535 / INIST-CNRS - Institut de l'Information Scientifique et TechniqueFRFranc

Coherent Digital Polarization Diversity Receiver for Real-Time Polarization-Multiplexed QPSK Transmission at 2.8 Gb/s

Pfau T, Peveling R, Hauden Y, et al. Coherent Digital Polarization Diversity Receiver for Real-Time Polarization-Multiplexed QPSK Transmission at 2.8 Gb/s. Photonics Technology Letters, IEEE. 2007;19(24):1988-1990.This letter presents a coherent digital polarization diversity receiver for real-time polarization-multiplexed synchronous quadrature phase-shift keying transmission with distributed feedback lasers at a data rate of 2.8 Gb/s. The tolerance against fast polarization changes and polarization-dependent loss is evaluated for different filter widths in the carrier recovery circuit. The minimum achieved bit-error rate is 3.4 times 10-7

Real-time ultra-wideband spectrum management in critical civil infrastructures : UCELSS project

status: publishe

Ultra-Fast Adaptive Digital Polarization Control in a Realtime Coherent Polarization-Multiplexed QPSK Receiver

Pfau T, Wördehoff C, Peveling R, et al. Ultra-Fast Adaptive Digital Polarization Control in a Realtime Coherent Polarization-Multiplexed QPSK Receiver. In: Proceedings of OFC/NFOEC 2008. 2008.A digital polarization control system integrated in a 2.8 Gbit/s realtime polarization-multiplexed coherent QPSK system compensates for endless polarization changes having a maximum gradient of 3.5 krad/s (12 krad/s) with 1 dB (3.9 dB) loss in receiver sensitivity

Polarization-Multiplexed 2.8 Gbit/s Synchronous QPSK Transmission with Real-Time Digital Polarization Tracking

Pfau T, Peveling R, Samson F, et al. Polarization-Multiplexed 2.8 Gbit/s Synchronous QPSK Transmission with Real-Time Digital Polarization Tracking. In: Proceedings of ECOC. Vol 3. IEE; 2007: 263-264.This paper presents the implementation of an electronic polarization tracking algorithm which enables real-time polarization-multiplexed synchronous QPSK transmission with DFB lasers. The achieved BER at 2.8 Gbit/s is well below the FEC threshold

PDL-Tolerant Real-time Polarization-Multiplexed QPSK Transmission with Digital Coherent Polarization Diversity Receiver

Pfau T, Peveling R, Hoffmann S, et al. PDL-Tolerant Real-time Polarization-Multiplexed QPSK Transmission with Digital Coherent Polarization Diversity Receiver. In: IEEE Lasers and Electro-Optics Society, ed. Proceedings of the 2007 IEEE/LEOS Summer Topical Meetings. Piscataway, NJ: IEEE; 2007: 17-18.This paper presents the implementation of a real-time electronic polarization tracking algorithm which enables robust optical polarization-multiplexed synchronous quadrature phase shift keying transmission with DFB lasers. The achieved BER at a data rate of 2.8 Gbit/s is well below the FEC threshold

A new plant protein interacts with eIF3 and 60S to enhance virus-activated translation re-initiation

The plant viral re-initiation factor transactivator viroplasmin (TAV) activates translation of polycistronic mRNA by a re-initiation mechanism involving translation initiation factor 3 (eIF3) and the 60S ribosomal subunit (60S). QJ; Here, we report a new plant factor-re-initiation supporting protein (RISP)-that enhances TAV function in re-initiation. RISP interacts physically with TAV in vitro and in vivo. Mutants defective in interaction are less active, or inactive, in transactivation and viral amplification. RISP alone can serve as a scaffold protein, which is able to interact with eIF3 subunits a/c and 60S, apparently through the C-terminus of ribosomal protein L24. RISP pre-bound to eIF3 binds 40S, suggesting that RISP enters the translational machinery at the 43S formation step. RISP, TAV and 60S co-localize in epidermal cells of infected plants, and eIF3-TAV-RISP-L24 complex formation can be shown in vitro. These results suggest that RISP and TAV bridge interactions between eIF3-bound 40S and L24 of 60S after translation termination to ensure 60S recruitment during repetitive initiation events on polycistronic mRNA; RISP can thus be considered as a new component of the cell translation machinery