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Robert and Renée Belfer Office for Dana-Farber Innovations

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    In this section

    Contact the Innovation Office

    Belfer Office for Dana-Farber Innovations
    10 Brookline Place, 3rd Floor
    Brookline, MA 02445

    General Inquiry: innovation@dfci.harvard.edu
    Academic and/or Corporate MTAs: contractsteam@dfci.harvard.edu

    Belfer Office for Dana-Farber Innovations
    10 Brookline Place, 3rd Floor
    Brookline, MA 02445

    General Inquiry: innovation@dfci.harvard.edu

    Academic and/or Corporate MTAs: contractsteam@dfci.harvard.edu

    Innovations

    Our Mission

    To actively accelerate innovations to benefit patients, society, and the Dana-Farber Cancer Institute. We team with investigators to identify new discoveries and generate alliances to move science from bench to clinic for maximum impact.

    Our Vision

    To spark and fuel a spirit of innovation across the organization by providing effective tools to continuously question, create, and imagine what else might be possible.

    Collaboration Opportunities

    In collaborating with Dana-Farber, your organization will have access to the Institute's specialized expertise, and to the unique array of core facilities needed to explore new areas of research. Learn more about Dana-Farber Centers that are interested in partnering with industry. Explore Dana-Farber's extensive Core Facilities. And discover more opportunities to collaborate.

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    In partnership with the Innovation Office, Dana-Farber makes publicly available a list of FDA-approved therapeutics and diagnostics in which the Institute has a financial interest.
    View the list

    Technology News

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    Extracellular Domain Shedding of the ALK Receptor Mediates Neuroblastoma Cell Migration (Cell)

    Although activating mutations of the anaplastic lymphoma kinase (ALK) membrane receptor occur in ∼10% of neuroblastoma (NB) tumors, the role of the wild-type (WT) receptor, which is aberrantly expressed in most non-mutated cases, is unclear. Both WT and mutant proteins undergo ECD cleavage. In a recent study published in Cell, first author, Hao Huang, PhD, and senior author, Rani George, MD, PhD, show that extracellular domain (ECD) cleavage of the ALK cell surface tyrosine kinase receptor mediates neuroblastoma cell migration through induction of an epithelial-to-mesenchymal transition (EMT) gene signature. They also show that ECD cleavage is caused by matrix metalloproteinase 9 (MMP-9), whose inhibition leads to decreased NB cell migration. Proteolytic cleavage of the ECD of WT ALK, which is expressed in most NB cases, promotes metastasis. By targeting that process, these adverse cancer-associated features of ALK cleavage can be circumvented, raising the possibility of MMP-9 inhibition, either singly or in combination with that of ALK in patients with NB ...

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    Structure-Guided Design of a “Bump-and-Hole” Bromodomain-Based Degradation Tag (Journal of Medicinal Chemistry)

    Targeted protein degradation offers the potential for rapid and dose-dependent protein depletion through the use of protein fusion tags toward which protein degraders have been established. In a recent article published in the Journal of Medicinal Chemistry, first author Radoslaw Nowak, PhD, and senior author Eric Fischer, PhD, present a newly developed protein degradation tag BRD4BD1L94V along with the corresponding cereblon (CRBN)-based heterobifunctional degrader based on a “bump-and-hole” approach. The resulting compound XY-06-007 binds to BRD4BD1L94V with increased selectivity over the wild-type bromodomain, which translates into potent and preferential degradation of the degron tag. Nowak, Fisher, et al. anticipate that the BRD4BD1L94V degradation system can be used in tandem with other ligand-induced degradation tags to assess the synergistic effect of degrading multiple targets in a chemically controlled manner, enabling investigation into the consequences resulting from rapid degradation of previously undruggable disease codependencies ...

    Recent Research at Dana-Farber