Highly integrated direct conversion receiver for GSM/GPRS/EDGE with on-chip 84-dB dynamic range continuous-time /spl Sigma//spl Delta/ ADC

This paper describes a highly digitized direct conversion receiver of a single-chip quadruple-band RF transceiver that meets GSM/GPRS and EDGE requirements. The chip uses an advanced 0.25-/spl mu/m BiCMOS technology. The I and Q on-chip fifth-order single-bit continuous-time sigma-delta (/spl Sigma//spl Delta/) ADC has 84-dB dynamic range over a total bandwidth of /spl plusmn/135 kHz for an active area of 0.4 mm/sup 2/. Hence, most of the channel filtering is realized in a CMOS IC where digital processing is achieved at a lower cost. The systematic analysis of dc offset at each stage of the design enables to perform the dc offset cancellation loop in the digital domain as well. The receiver operates at 2.7 V with a current consumption of 75 mA. A first-order substrate coupling analysis enables to optimize the floor plan strategy. As a result, the receiver has an area of 1.8 mm/sup 2/.     

Requirement of cysteine-rich repeats of the Fas receptor for binding by the Fas ligand

The Fas receptor is a member of a family of cell death receptors, including tumor necrosis factor receptor I (TNFR I), death receptor 3 and 4 (DR3 and DR4), and cytopathic avian receptor 1 (CAR1). The Fas receptor is composed of several discrete domains, including three cysteine-rich domains (CRDs), a transmembrane domain, and an intracellular domain responsible for transmitting an apoptotic signal. While the mechanism of Fas-mediated cell death has become elucidated, the requirements for Fas ligand binding to the receptor have not been fully defined. Using a series of chimeric Fc-receptor fusion proteins between the human Fas receptor and TNFR I, each cysteine-rich domain of Fas was found to be required for interaction with the Fas ligand. Interestingly, TNFR I CRD1 could partially substitute for the Fas CRD1. The importance of this domain was underscored by the analysis of a Fas extracellular mutation (C66R), which resulted in a complete loss of ligand binding. This mutation was cloned from a human patient suffering from Canale-Smith syndrome, which is characterized by autoimmunity resembling that observed in the lpr and lprcg mice. The localization of essential ligand binding domains in the Fas receptor correlated exactly with the ability of the Fas receptor fusion proteins to prevent cell death mediated by the Fas ligand.     

Low-voltage 32 Msample/s parallel pipelined switched-current ADC

A parallel switched-current A/D converter is presented. Eight time-interleaved switched-current ADCs operating at 4 Msample/s are used to increase the sampling rate. With channel compensation, the measured SFDR is >50 dB at 32 Msample/s with f_m=1.13 MHz. The performance of this experimental design is limited by noise and a fixed-pattern timing error that is not removed by the compensation algorithm     

Cell signaling by the type IV pili of pathogenic Neisseria

Neisseria gonorrhoeae and Neisseria meningitidis are Gram-negative bacterial pathogens that infect human mucosal epithelia. Type IV pilus-mediated adherence of these bacteria is a crucial early event for establishment of infection. In this work, we show that the type IV pili transduce a signal into the eucaryotic host cell. Purified adherent pili, but not pili from a low binding mutant, trigger an increase in the cytosolic free calcium ([Ca2+]i) in target epithelial cells, a signal known to control many cellular responses. The [Ca2+]i increase was blocked by antibodies against CD46, a putative pilus receptor, suggesting a role for this protein in signal transduction. Pilus-mediated attachment was inhibited by depletion of host cell intracellular Ca2+ stores but not by removal of extracellular Ca2+. Further, kinase inhibition studies showed that pilus-mediated adherence is dependent on casein kinase II. In summary, these data reveal a novel function of the type IV pili, namely induction of signal transduction pathways in host cells.     

A Study of Surface Deformation during Wire‐Rod Rolling of High Speed Steels using Experimental and Computational Techniques

The evolution of surface defects during shape rolling of high‐speed steel billets is studied using longitudinal surface defects prepared by machining and welding. The reduction of the defects during rolling in a production mill is compared to the total area reduction of the billets. Samples are collected after pass 4, 6, 8, 14, 19 and the final pass, 28, representing the finished 5.5mm wire. By inspecting the cross sections, the rotation of the billets from pass to pass is evaluated. Results from FE simulations on solid billets are compared to the experimental results. Generally, simulations predict less reduction than observed experimentally. In most cases cracks reduce most effectively followed by carbon steel welds and stainless steel welds.