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Cas12a System For Combinatorial Transcriptional Repression In Eukaryotic Cells
Brief description not available
Novel therapy for inflammatory disease using fatty acid-bound alpha fetoprotein
α-Fetoprotein (AFP) is a fetal glycoprotein produced by the majority of human hepatocellular carcinoma tumors and other tumor types. Delineating differences between fetal 'normal' AFP (nAFP) and tumor-derived AFP (tAFP), investigators at UCSF and the Parker Institute for Cancer Immunotherapy have uncovered a novel role for tAFP in altering metabolism via lipid-binding partners. They have developed a pharmaceutical composition comprising AFP bound by a fatty acid which, depending on the fatty acid used, can have an immunosuppressive effect allowing for the treatment of inflammatory diseases. AFP bound to other fatty acids can eliminate the immune suppressive impact and have a neutral effect which allows for the development of dendritic cell (DC) vaccines presenting AFP epitopes which could be used to treat and prevent tumor AFP-expressing cancers.
Novel compositions and methods for targeted replacement of endogenous T-cell receptor with a chimeric antigen receptor
Gene Targets For Gamma-Delta T Cell Cytotoxicity Against Tumor Cells
Gene Targets For Manipulating T Cell Behavior
METHOD FOR MANUFACTURING THERAPEUTIC IMMUNE CELLS
Chimeric antigen receptor (CAR) T cells have so far shown limited efficacy on brain and solid tumors. UCSF investigators have developed a method of manufacturing recombinant immune cells by pre-treating them with a combination of small molecules to increase the number of CAR T cells in the tumor microenvironment and improve the survival of animal models bearing glioma in the brain relative to CAR T cells that have not received the pre-treatment. These results may be applicable to other solid tumors.
INTEGRATED OPTICAL PEEL AWAY PLEUROSCOPIC TROCAR FOR USE IN PLEUROSCOPIC AND THORACIC PROCEDURES
New Generation Bitopic Bcr-Abl Inhibitors
Scientists at UCSF have developed a novel class of BCR-ABL inhibitors that engages two binding sites in BCR-ABL simultaneously. This two-site binding (bitopic) mechanism of action is unprecedented against BCR-ABL, one of the most well-validated targets in oncology.