Gustavo Glowacki

TL;DR: These results delineate an alternative mechanism for inducing T cell death and set an interesting precedent for immunoregulation via crosstalk between NAD-dependent ADP-ribosyltransferases and purinoceptors.

TL;DR: The position‐sensitive iterative database search program PSI‐BLAST connected the mammalian ARTs with most known bacterial ADP‐ribosylating toxins, suggesting that the two enzyme families that catalyze reversible mono‐ADP‐ ribosylation either were lost from the genomes of these nonchordata eucaryotes or were subject to horizontal gene transfer between kingdoms.

TL;DR: The structure, chromosomal localization, and expression profile of the gene for mouse ecto-ADP-ribosyltransferase ART5 was determined and the secreted epitope-tagged ART5 protein resembled rat ART2 in exhibiting potent NAD-glycohydrolase activity.

TL;DR: Using genetic immunization, monoclonal antibodies that recognize the native human ARTs on the surface of living cells are raised and these mAbs recognize an epitope shared with the mouse ART orthologue but not with more distant ART paralogues.

TL;DR: Staining of Do/art4-transfected cells by these mAbs was reduced following treatment of cells with PI-PLC, confirming that Do/ART4 is anchored in the cell membrane by linkage to glycosylphosphatidylinositol as predicted from its amino acid sequence.