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Research interests
Lab Overview
Protein kinases are a family of ~535 enzymes that, collectively, are termed the kinome. Uncontrolled protein kinase activity has been linked to the development of nearly 25% of all cancers; consequently, protein kinases represent one of the most promising avenues for cancer therapy. Despite the high druggability of the kinome, the majority of the kinome remains untargeted, with many kinases having no established oncogenic function. The vast majority of kinase publications focus on a small group of well-understood kinases, yet synthetic lethal screens repeatedly identify various untargeted kinases as playing functional roles in cancer cell proliferation and survival. Our inability to routinely probe these enzymes has hindered previous attempts to understand how they are regulated and function in cancer. Our lab is interested in applying proteomics approaches including kinome profiling and phosphoproteomics to interrogate what is referred to as “the dark cancer kinome” to identify new therapeutic kinase targets for the treatment of cancer.
Research interests
- Unlocking the therapeutic potential of the dark cancer kinome using proteomics
- Applying kinome profiling technologies to predict combination therapies for cancer
- Exploring kinase-driven therapies to treat K-ras mutant cancers
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Collaborations and top research areas from the last five years
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Rac1 selectively binds a specific lamellipodin isoform via a noncanonical helical interface
Gao, T., Zhang, P., Kurimchak, A. M., Duncan, J. S. & Wu, J., Jan 2026, In: Journal of Biological Chemistry. 302, 1, p. 111023 111023.Research output: Contribution to journal › Article › peer-review
Open Access -
KRAS G12V mutation-selective requirement for ACSS2 in colorectal adenoma formation
Budagyan, K., Cannon, A. C., Chatoff, A., Benton, D., Kurimchak, A. M., Araiza-Olivera, D., Gerasimova, A., Snyder, N. W., Duncan, J. S., Uribe-Alvarez, C. & Chernoff, J., Apr 22 2025, In: Cell Reports. 44, 4, p. 115444 115444.Research output: Contribution to journal › Article › peer-review
Open Access4 Scopus citations -
Rac1 Selectively Binds a Specific Lamellipodin Isoform via a Noncanonical Helical Interface
Gao, T., Zhang, P., Kurimchak, A. M., Duncan, J. S. & Wu, J., Jun 25 2025, (bioRxiv : the preprint server for biology).Research output: Working paper › Preprint
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FAM122A ensures cell cycle interphase progression and checkpoint control by inhibiting B55α/PP2A through helical motifs
Wasserman, J. S., Faezov, B., Patel, K. R., Kurimchak, A. M., Palacio, S. M., Glass, D. J., Fowle, H., McEwan, B. C., Xu, Q., Zhao, Z., Cressey, L., Johnson, N., Duncan, J. S., Kettenbach, A. N., Dunbrack, R. L. & Graña, X., Jul 10 2024, In: Nature Communications. 15, 1, p. 5776 5776.Research output: Contribution to journal › Article › peer-review
Open Access5 Scopus citations -
KRAS mutation-selective requirement for ACSS2 in colorectal adenoma formation
Budyagan, K., Cannon, A. C., Chatoff, A., Snyder, N. W., Kurimchak, A. M., Duncan, J. S. & Chernoff, J., Jan 22 2024, (Research square).Research output: Working paper › Preprint
Press/Media
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Findings on Science Reported by Researchers at Fox Chase Cancer Center (Rac1 Selectively Binds a Specific Lamellipodin Isoform via a Noncanonical Helical Interface)
12/18/25
1 item of Media coverage
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Lapatinib may boost effectiveness of drugs that destroy cancer proteins by blocking resistance
09/5/22
1 item of Media coverage
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Fox Chase Cancer Center: Lapatinib May Boost Effectiveness of Drugs That Destroy Cancer Proteins by Blocking Resistance
08/30/22 → 09/1/22
2 items of Media coverage
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