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Chk2 is a protein kinase activated in response to DNA double strand breaks. In normal tissues, Chk2 phosphorylates and thereby activates substrates that induce programmed cell death, or apoptosis, via interactions with p53, E2F1, PML proteins. In cancer tissues, where apoptosis is suppressed, Chk2 phosphorylates and inactivates cell cycle checkpoints (via interactions with Cdc25, phosphatases and Brca1 proteins), which allows cancer cells to repair and tolerate DNA damage. Hence, Chk2 inhibitors would be expected to protect normal tissues by reducing apoptosis, and to sensitize cancer cells to DNA-targeted agents. The National Cancer Institute seeks licensees for small molecule inhibitors of Chk2 for the treatment of cancer.

The National Cancer Institute (NCI) seeks research co-development or licensing partners for development of nucleic acid nanoparticles (NANP) and their use for controlled immunomodulation.

Investigators at the National Cancer Institute's Vaccine Branch have identified and enhanced immunogenicity of POTE epitopes to improve their efficacy in cancer vaccines.

The National Eye Institute’s Ophthalmic Genetics and Visual Function Branch seeks partners to co-develop the protocol for iPSC to RPE differentiation and its use in clinical, screening and translational settings.

A human antibody that could be used safely in vitro and in vivo for the detection of CH2 (Fc and IgG as well is available of out-licensing from the National Cancer Institute.

The National Cancer Institute seeks parties to co-develop soluble forms of CD4 as potent HIV-1 therapeutics.

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.

Researchers at the National Cancer Institute (NCI) have developed peptidomimetic inhibitors that disrupt Polo-like kinase 1 (Plk1)-mediated protein interactions by targeting polo-box domain (PBD). These compounds are designed to selectively cause mitotic arrest in cancer cells with abnormal Plk1 expression. Researchers seek licensing and/or co-development research collaborations to further develop the inhibitors.

The National Cancer Institute is seeking parties interested in collaborative research to co-develop or license the in vitro and in vivo removal of targets using light energy.