The PHENIX Experiment at RHIC

The physics emphases of the PHENIX collaboration and the design and current status of the PHENIX detector are discussed. The plan of the collaboration for making the most effective use of the available luminosity in the first years of RHIC operation is also presented.Comment: 5 pages, 1 figure. Further details of the PHENIX physics program available at http://www.rhic.bnl.gov/phenix

The upgrade of the ALICE TPC with GEMs and continuous readout

The upgrade of the ALICE TPC will allow the experiment to cope with the high interaction rates foreseen for the forthcoming Run 3 and Run 4 at the CERN LHC. In this article, we describe the design of new readout chambers and front-end electronics, which are driven by the goals of the experiment. Gas Electron Multiplier (GEM) detectors arranged in stacks containing four GEMs each, and continuous readout electronics based on the SAMPA chip, an ALICE development, are replacing the previous elements. The construction of these new elements, together with their associated quality control procedures, is explained in detail. Finally, the readout chamber and front-end electronics cards replacement, together with the commissioning of the detector prior to installation in the experimental cavern, are presented. After a nine-year period of R&D, construction, and assembly, the upgrade of the TPC was completed in 2020.publishedVersio

Structural biology of NAD metabolism in bacteria

FASEB RESEARCH CONFERENCE – NAD METABOLISM AND SIGNALING; Lucca (Italy) - Abstract autho

Ammonia is the Physiological Substrate of ‘GAT-less’ Prokaryotic NAD Synthetase

FASEB RESEARCH CONFERENCE – NAD METABOLISM AND SIGNALING; Carefree, AZ (USA) - Autho

NAD biosynthesis under attack

FASEB RESEARCH CONFERENCE – NAD METABOLISM AND SIGNALING; Lucca, Italy - Speaker and Poster Presente

Nucleotide sequence of a novel δ-endotoxin gene cryIg of Bacillus thuringiensis ssp. galleriae

AbstractA gene cryIg coding for entomocidal protein δ-endotoxin of Bacillus thuringiensis ssp. galleriae str. 11-67 named CryIG has been cloned and sequenced (EMBL accession number X58120). The deduced amino acid sequence that contains 1156 amino acid residues shows only 28% of identical residues, when compared with other δ-endotoxins of the CryI family. The extent of identity is substantially higher for some regions of the sequence (‘conserved blocks’), that presumably bear important structural or functional properties. This implies that CryIG δ-endotoxin follows the same type of polypeptide chain folding as other Cryl proteins, whereas peculiarities of primary structure help to explain its unique specificity