Abstract: Magnetic resonance (MR) spins are inverted by applying an inversion recovery (IR) radio frequency pulse (50). MR signals are acquired at an inversion time (TI) after the IR radio frequency pulse. TI is selected such that a first tissue of interest (e.g., blood) exhibits negative magnetism excited by the IR radio frequency pulse and a second tissue (e.g., intraplaque hemorrhage tissue) exhibits positive magnetism excited by the IR radio frequency pulse. The acquired magnetic resonance signals are reconstructed to generate spatial pixels or voxels wherein positive pixel or voxel values indicate spatial locations of positive magnetism and negative pixel or voxel values indicates spatial locations of negative magnetism. A first image (28) representative of the first tissue is generated from spatial pixels or voxels having negative signal intensities, and a second image (26) representative of the second tissue is generated from spatial pixels or voxels having positive signal intensities.

Abstract: Magnetic resonance (MR) spins are inverted by applying an inversion recovery (IR) radio frequency pulse (50). MR signals are acquired at an inversion time (TI) after the IR radio frequency pulse. TI is selected such that a first tissue of interest (e.g., blood) exhibits negative magnetism excited by the IR radio frequency pulse and a second tissue (e.g., intraplaque hemorrhage tissue) exhibits positive magnetism excited by the IR radio frequency pulse. The acquired magnetic resonance signals are reconstructed to generate spatial pixels or voxels wherein positive pixel or voxel values indicate spatial locations of positive magnetism and negative pixel or voxel values indicates spatial locations of negative magnetism. A first image (28) representative of the first tissue is generated from spatial pixels or voxels having negative signal intensities, and a second image (26) representative of the second tissue is generated from spatial pixels or voxels having positive signal intensities.

Abstract: The present invention includes a number of structural analogues of UK-1. A comparision of the anticancer activity of the UK-1 analogues with their ability to inhibit the growth of methicillin-sensitive and methicillin-resistant Staphylococcus aureus demonstrates that a structurally simplified analogue of UK-1 retains the natural product's selective activity against cancer cells. Structurally conservative changes to UK-1 that diminish Mg2+-binding ability may result in a dramatic decrease in cancer cell cytotoxicity. The results may establish a minimum structural pharmacophore as well as a functional role for Mg2+-binding in the selective cytotoxicity of UK-1.

Abstract: Ricin A-chain is an N-glycosidase that attacks ribosomal RNA at a highly conserved adenine residue. Crystallographic studies show that not only adenine and formycin, but also pterin-based rings can bind in the ricin active site. For a better understanding of the recognition mode between ricin, and adenine-like rings, the interaction energies and geometries were calculated for a number of complexes. Shiga toxin, a compound essentially identical to the protein originally isolated from Shigella dysenteniae, has an active protein chain that is a homologue of the ricin active chain, and catalyzes the same depurination reaction. The present invention is drawn to identifying inhibitors of ricin and Shiga toxin, using methods molecular mechanics and ab initio methods and using the identified inhibitors as antidotes to ricin or Shiga toxin, or to facilitate immunotoxin treatment by controlling non-specific cytotoxicity.

Abstract: Ricin A-chain is an N-glycosidase that attacks ribosomal RNA at a highly conserved adenine residue. Crystallographic studies show that not only adenine and formycin, but also pterin-based rings can bind in the ricin active site. For a better understanding of the recognition mode between ricin, and adenine-like rings, the interaction energies and geometries were calculated for a number of complexes. Shiga toxin, a compound essentially identical to the protein originally isolated from Shigella dysenteriae, has an active protein chain that is a homologue of the ricin active chain, and catalyzes the same depurination reaction. The present invention is drawn to identifying inhibitors of ricin and Shiga toxin, using methods molecular mechanics and ab initio methods and using the identified inhibitors as antidotes to ricin or Shiga toxin, or to facilitate immunotoxin treatment by controlling non-specific cytotoxicity.