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Hydrocarbon Stapled Peptides that Inhibit the Linear Ubiquitin Chain Assembly Complex (LUBAC) for the Therapy of the Activated B Cell-like (ABC) Subtype of Diffuse Large B Bell Lymphoma (A Type of Non-Hodgkin’s Lymphoma)

Researchers at the National Cancer Institute (NCI) have developed an invention consisting of hydrocarbon stapled peptides that disrupt the linear ubiquitin-chain assembly complex (LUBAC), which is involved in NF-κB signaling. These peptides can be used as a therapeutic in the treatment of the activated B cell-like (ABC) subtype of diffuse large B cell lymphoma (DLBCL), a type of non-Hodgkin’s lymphoma, as well as inflammatory diseases. The NCI seeks licensing and/or co-development research collaborations for inhibitors of NF-κB signaling and/or treatment of ABC DLBCL, as well as inflammatory diseases.

Chimeric Antigen Receptors to CD276 for Treating Cancer

This licensing opportunity from the National Cancer Institute concerns the development of CARs comprising an antigen-binding fragment derived from the MGA271 antibody. The resulting CARs can be used in adoptive cell therapy treatment for neuroblastoma and other tumors that express CD276.

T cell tuning molecules that modify the immune response to cancer cells

Researchers at the Eunice Kennedy Shriver National Institute of Child Health and Human Development (NICHD) seek partners to collaborate on in vitro studies to validate these potential immunomodulators and to conduct in vivo studies in a murine cancer model to determine the effects of ligands (e.g., antibodies) to the proteins on the immune response to cancer cells. Preference will be given to responses received by March 31, 2016.

Improved Personalized Cancer Immunotherapy

The National Cancer Institute’s Surgery Branch seeks partners interested in collaborative research to co-develop adoptive transfer of tumor infiltrating leukocytes (TIL) for cancers other than melanoma.

MUC-1 Tumor Antigen Agonist Epitopes for Enhancing T-cell Responses to Human Tumors

Scientists at NIH have identified 7 new agonist epitopes of the MUC-1 tumor associated antigen. Compared to their native epitope counterparts, peptides reflecting these agonist epitopes have been shown to enhance the generation of human tumor cells, which in turn have a greater ability to kill human tumor cells endogenously expressing the native MUC-1 epitope.

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