Abstract: In various aspects and embodiments of the disclosure, the invention provides pharmaceutical compositions and methods for protecting against brain injury associated with Hypoxic-Ischemic Encephalopathy (HIE). The compositions and methods employ omega-3 fatty acid (n-3 FA) diglyceride (DG) and/or triglyceride (TG) emulsions, which may be used alone or in combination with therapeutic Hypothermia (HT).

Abstract: The present invention relates to structural studies of dipeptidyl peptidase I (DPPI) proteins, modified dipeptidyl peptidase I (DPPI) proteins and DPPI co-complexes. Included in the present invention is a crystal of a dipeptidyl peptidase I (DPPI) and corresponding structural information obtained by X-ray crystallography from rat and human DPPI. In addition, this invention relates to methods for using structure co-ordinates of DDPI, mutants hereof and co-complexes, to design compounds that bind to the active site or accessory binding sites of DPPI and to design improved inhibitors of DPPI or homologues of the enzyme.

Abstract: The present invention relates to structural studies of dipeptidyl peptidase I (DPPI) proteins, modified dipeptidyl peptidase I (DPPI) proteins and DPPI co-complexes. Included in the present invention is a crystal of a dipeptidyl peptidase I (DPPI) and corresponding structural information obtained by X-ray crystallography from rat and human DPPI. In addition, this invention relates to methods for using structure co-ordinates of DDPI, mutants hereof and co-complexes, to design compounds that bind to the active site or accessory binding sites of DPPI and to design improved inhibitors of DPPI or homologues of the enzyme.

Abstract: The present invention relates to structural studies of dipeptidyl peptidase I (DPPI) proteins, modified dipeptidyl peptidase I (DPPI) proteins and DPPI co-complexes. Included in the present invention is a crystal of a dipeptidyl peptidase I (DPPI) and corresponding structural information obtained by X-ray crystallography from rat and human DPPI. In addition, this invention relates to methods for using structure co-ordinates of DDPI, mutants hereof andco-complexes, to design compounds that bind to the active site or accessory binding sites of DPPI and to design improved inhibitors of DPPI or homologues of the enzyme.

Abstract: Fluorescence complementation products with intensity levels mimicking the full length intensities are obtained by introduction of improved folding capabilities with a mutation in position 1 preceding the chromophore. This is particularly seen with the yellow variant of Green Fluorescent Protein (GFP). An additive increase is obtained by splitting the GFP between amino acids 172 and 173. Screening for drugs capable of preventing interaction between proteins is performed by selecting the cells with the highest dynamic range through Fluorescence Activated Cell Sorting (FACS), as illustrated with the ability of FK506 to break the rapamycin induced interaction between FRB and FKBP.