Defining and Targeting Adaptations to Oncogenic KRASG12C Inhibition Using Quantitative Temporal Proteomics
Open accessPublished version of a preprint
Abstract
ABSTRACT Covalent inhibitors of the KRAS G12C oncoprotein have recently been developed and are being evaluated in clinical trials. Resistance to targeted therapies is common and likely to limit long-term efficacy of KRAS inhibitors (KRASi). To identify pathways of adaptation to KRASi and to predict drug combinations that circumvent resistance, we used a mass spectrometry-based quantitative temporal proteomics and bioinformatics workflow to profile the temporal proteomic response to KRAS G12C inhibition in pancreatic and lung cancer 2D and 3D cellular models. We quantified 10,805 proteins across our datasets, representing the most comprehensive KRASi proteomics effort to date. Our data reveal common mechanisms of acute and long-term response between KRAS G12C -driven tumors. To facilitate discovery in the cancer biology community, we generated an interactive ‘KRASi proteome’ website ( https://manciaslab.shinyapps.io/KRASi/ ). Based on these proteomic data, we identified potent combinations of KRASi with PI3K, HSP90, CDK4/6, and SHP2 inhibitors, in some instances converting a cytostatic response to KRASi monotherapy to a cytotoxic response to combination treatment. Overall, using our quantitative temporal proteomics-bioinformatics platform, we have comprehensively characterized the proteomic adaptations to KRASi and identified combinatorial regimens to induce cytotoxicity with potential therapeutic utility.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Acquired resistance to KRASG12C inhibition may be mediated by activation of multiple RTK regulators, including EGFR, FGFR, IGF1R, HER2, SHP2, and downstream RAS effectors such as MYC and mTOR.
“Recent studies using preclinical models have indicated that acquired resistance to KRASG12C inhibition may be mediated by the activation of multiple receptor tyrosine kinase (RTK) regulators, including epidermal growth factor receptor (EGFR), fibroblast growth factor receptor (FGFR), insulin-like growth factor 1 receptor (IGF1R), human epidermal growth factor 2 (HER2), and Src homology 2 domain-”
From Therapeutic targeting of syndecan-1 axis overcomes acquired resistance to KRAS-targeted therapy in gastrointestinal cancers (2025) · cites this paper as [7]
Inhibition of multiple RTKs through adaptors like SOS and SHP2 has shown promise in preclinical studies for mitigating acquired resistance to KRAS inhibition.
“Previously, inhibition of multiple RTKs through adaptors like SOS and SHP2, which function downstream of RTKs to promote RAS activation, has shown promise in preclinical studies aimed at mitigating acquired resistance to KRAS inhibition.7,22,26”
From Therapeutic targeting of syndecan-1 axis overcomes acquired resistance to KRAS-targeted therapy in gastrointestinal cancers (2025) · cites this paper as [7]
One major route leading to recovery of RAS activity is activation of RTKs through genetic or non-genetic mechanisms.
“One major route leading to such recovery of RAS activity is the activation of RTKs through either genetic (e.g., gene amplification or fusion) or non-genetic mechanisms.2,4,5,6,7,8,22,23,24,25”
From Therapeutic targeting of syndecan-1 axis overcomes acquired resistance to KRAS-targeted therapy in gastrointestinal cancers (2025) · cites this paper as [7]
Cites
Subramanian, A., Tamayo, P., Mootha, V. K., Mukherjee, S., Ebert, B. L., Gillette, M. A., Paulovich, A., Pomeroy, S. L., Golub, T. R., Lander, E. S., et al. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0506580102 · Cited by 53,625 · see citing works
Cytoscape: A software Environment for integrated models of biomolecular interaction networks
Shannon, P., Markiel, A., Ozier, O., Baliga, N. S., Wang, J. T., Ramage, D., Amin, N., Schwikowski, B., & Ideker, T. (2003) · Genome Research · doi:10.1101/gr.1239303 · Cited by 51,888 · see citing works
limma powers differential expression analyses for RNA-sequencing and microarray studies
Ritchie, M. E., Phipson, B., Wu, D., Hu, Y., Law, C. W., Shi, W., & Smyth, G. K. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv007 · Cited by 40,458 · see citing works
Metascape provides a biologist-oriented resource for the analysis of systems-level datasets
Zhou, Y., Zhou, B., Pache, L., Chang, M., Khodabakhshi, A. H., Tanaseichuk, O., Benner, C., & Chanda, S. K. (2019) · Nature Communications · doi:10.1038/s41467-019-09234-6 · Cited by 14,611 · see citing works
DrugBank 5.0: a major update to the DrugBank database for 2018
Wishart, D. S., Feunang, Y. D., Guo, A. C., Lo, E. J., Marcu, A., Grant, J. R., Sajed, T., Johnson, D., Li, C., Sayeeda, Z., et al. (2018) · Nucleic Acids Research · doi:10.1093/nar/gkx1037 · Cited by 8,404 · see citing works
In situ click chemistry generation of cyclooxygenase-2 inhibitors
Bhardwaj, A., Kaur, J., Wuest, M., & Wuest, F. (2017) · Nature Communications · doi:10.1038/s41467-016-0009-6 · Cited by 7,448 · see citing works
An automated method for finding molecular complexes in large protein interaction networks
Bader, G. D., & Hogue, C. W. V. (2003) · BMC Bioinformatics · doi:10.1186/1471-2105-4-2 · Cited by 6,112 · see citing works
A Next Generation Connectivity Map: L1000 Platform and the First 1,000,000 Profiles
Subramanian, A., Narayan, R., Corsello, S. M., Peck, D. D., Natoli, T. E., Lu, X., Gould, J., Davis, J. F., Tubelli, A. A., Asiedu, J. K., et al. (2017) · Cell · doi:10.1016/j.cell.2017.10.049 · Cited by 3,515 · see citing works
Self-citationGOrilla: a tool for discovery and visualization of enriched GO terms in ranked gene lists
Eden, E., Navon, R., Steinfeld, I., Lipson, D., & Yakhini, Z. (2009) · BMC Bioinformatics · doi:10.1186/1471-2105-10-48 · Cited by 3,356 · see citing works
The Clinical KRAS(G12C) Inhibitor AMG 510 Drives Anti-Tumour Immunity
Canon, J., Rex, K., Saiki, A. Y., Mohr, C., Cooke, K., Bagal, D., Gaida, K., Holt, T., Knutson, C. G., Koppada, N., et al. (2019) · Nature · doi:10.1038/s41586-019-1694-1 · Cited by 2,277 · see citing works
Enrichment Map: A Network-Based Method for Gene-Set Enrichment Visualization and Interpretation
Merico, D., Isserlin, R., Stueker, O., Emili, A., & Bader, G. D. (2010) · PLoS ONE · doi:10.1371/journal.pone.0013984 · Cited by 2,235 · see citing works
AZD9291 in EGFR Inhibitor–Resistant Non–Small-Cell Lung Cancer
Jänne, P. A., Yang, J. C.-H., Kim, D.-W., Planchard, D., Ohe, Y., Ramalingam, S. S., Ahn, M.-J., Kim, S.-W., Su, W.-C., Horn, L., et al. (2015) · New England Journal of Medicine · doi:10.1056/nejmoa1411817 · Cited by 2,116 · see citing works
Oncogenic Kras maintains pancreatic tumors through regulation of anabolic glucose metabolism
Ying, H., Kimmelman, A. C., Lyssiotis, C. A., Hua, S., Chu, G. C., Fletcher-Sananikone, E., Locasale, J. W., Son, J., Zhang, H., Coloff, J. L., et al. (2012) · Cell · doi:10.1016/j.cell.2012.01.058 · Cited by 2,043 · see citing works
Drugging the undruggable RAS: Mission Possible?
Cox, A. D., Fesik, S. W., Kimmelman, A. C., Luo, J., & Der, C. J. (2014) · Nature Reviews Drug Discovery · doi:10.1038/nrd4389 · Cited by 1,997 · see citing works
Glutamine supports pancreatic cancer growth through a KRAS-regulated metabolic pathway
Son, J., Lyssiotis, C. A., Ying, H., Wang, X., Hua, S., Ligorio, M., Perera, R. M., Ferrone, C. R., Mullarky, E., Shyh-Chang, N., et al. (2013) · Nature · doi:10.1038/nature12040 · Cited by 1,990 · see citing works
Engelman, J. A., Chen, L., Tan, X., Crosby, K., Guimaraes, A. R., Upadhyay, R., Maira, M., McNamara, K., Perera, S. A., Song, Y., et al. (2008) · Nature Medicine · doi:10.1038/nm.1890 · Cited by 1,330 · see citing works
Hallin, J., Engstrom, L. D., Hargis, L., Calinisan, A., Aranda, R., Briere, D. M., Sudhakar, N., Bowcut, V., Baer, B. R., Ballard, J. A., et al. (2020) · Cancer Discovery · doi:10.1158/2159-8290.cd-19-1167 · Cited by 1,304 · see citing works
McAlister, G. C., Nusinow, D. P., Jedrychowski, M. P., Wühr, M., Huttlin, E. L., Erickson, B. K., Rad, R., Haas, W., & Gygi, S. P. (2014) · Analytical Chemistry · doi:10.1021/ac502040v · Cited by 1,263 · see citing works
Self-citationOncogene ablation-resistant pancreatic cancer cells depend on mitochondrial function
Viale, A., Pettazzoni, P., Lyssiotis, C. A., Ying, H., Sánchez, N., Marchesini, M., Carugo, A., Green, T., Seth, S., Giuliani, V., et al. (2014) · Nature · doi:10.1038/nature13611 · Cited by 1,259 · see citing works
Targeting KRAS mutant cancers with a covalent G12C-specific inhibitor
Janes, M. R., Zhang, J., Li, L.-S., Hansen, R., Peters, U., Guo, X., Chen, Y., Babbar, A., Firdaus, S. J., Darjania, L., et al. (2018) · Cell · doi:10.1016/j.cell.2018.01.006 · Cited by 1,172 · see citing works
Pancreatic stellate cells support tumour metabolism through autophagic alanine secretion
Sousa, C. M., Biancur, D. E., Wang, X., Halbrook, C. J., Sherman, M. H., Zhang, L., Kremer, D., Hwang, R. F., Witkiewicz, A. K., Ying, H., et al. (2016) · Nature · doi:10.1038/nature19084 · Cited by 1,122 · see citing works
Meta- and Orthogonal Integration of Influenza “OMICs” Data Defines a Role for UBR4 in Virus Budding
Tripathi, S., Pohl, M. O., Zhou, Y., Rodríguez-Frandsen, A., Wang, G., Stein, D. A., Moulton, H. M., DeJesus, P., Che, J., Mulder, L. C. F., et al. (2015) · Cell Host & Microbe · doi:10.1016/j.chom.2015.11.002 · Cited by 846 · see citing works
Comparison of 2D- and 3D-culture models as drug-testing platforms in breast cancer
IMAMURA, Y., MUKOHARA, T., SHIMONO, Y., FUNAKOSHI, Y., CHAYAHARA, N., TOYODA, M., KIYOTA, N., TAKAO, S., KONO, S., NAKATSURA, T., et al. (2015) · Oncology Reports · doi:10.3892/or.2015.3767 · Cited by 845 · see citing works
Singh, A., Greninger, P., Rhodes, D., Koopman, L., Violette, S., Bardeesy, N., & Settleman, J. (2009) · Cancer Cell · doi:10.1016/j.ccr.2009.03.022 · Cited by 841 · see citing works
Selective inhibition of oncogenic KRAS output with small molecules targeting the inactive state
Patricelli, M. P., Janes, M. R., Li, L.-S., Hansen, R., Peters, U., Kessler, L. V., Chen, Y., Kucharski, J. M., Feng, J., Ely, T., et al. (2016) · Cancer Discovery · doi:10.1158/2159-8290.cd-15-1105 · Cited by 759 · see citing works
Yap1 Activation Enables Bypass of Oncogenic Kras Addiction in Pancreatic Cancer
Kapoor, A., Yao, W., Ying, H., Hua, S., Liewen, A., Wang, Q., Zhong, Y., Wu, C.-J., Sadanandam, A., Hu, B., et al. (2014) · Cell · doi:10.1016/j.cell.2014.06.003 · Cited by 716 · see citing works
Takezawa, K., Pirazzoli, V., Arcila, M. E., Nebhan, C. A., Song, X., de Stanchina, E., Ohashi, K., Janjigian, Y. Y., Spitzler, P. J., Melnick, M. A., et al. (2012) · Cancer Discovery · doi:10.1158/2159-8290.cd-12-0108 · Cited by 710 · see citing works
Combination of ERK and autophagy inhibition as a treatment approach for pancreatic cancer
Bryant, K. L., Stalnecker, C. A., Zeitouni, D., Klomp, J. E., Peng, S., Tikunov, A. P., Gunda, V., Pierobon, M., Waters, A. M., George, S. D., et al. (2019) · Nature Medicine · doi:10.1038/s41591-019-0368-8 · Cited by 692 · see citing works
Allele-specific inhibitors inactivate mutant KRAS G12C by a trapping mechanism
Lito, P., Solomon, M., Li, L.-S., Hansen, R., & Rosen, N. (2016) · Science · doi:10.1126/science.aad6204 · Cited by 691 · see citing works
KRAS: feeding pancreatic cancer proliferation
Bryant, K. L., Mancias, J. D., Kimmelman, A. C., & Der, C. J. (2014) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2013.12.004 · Cited by 675 · see citing works
Self-citationRapid non-uniform adaptation to conformation-specific KRAS(G12C) inhibition
Xue, J. Y., Zhao, Y., Aronowitz, J., Mai, T. T., Vides, A., Qeriqi, B., Kim, D., Li, C., de Stanchina, E., Mazutis, L., et al. (2020) · Nature · doi:10.1038/s41586-019-1884-x · Cited by 543 · see citing works
Vertical Pathway Inhibition Overcomes Adaptive Feedback Resistance to KRASG12C Inhibition
Ryan, M. B., Fece de la Cruz, F., Phat, S., Myers, D. T., Wong, E., Shahzade, H. A., Hong, C. B., & Corcoran, R. B. (2020) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-19-3523 · Cited by 496 · see citing works
Piotrowska, Z., Niederst, M. J., Karlovich, C., Wakelee, H. A., Neal, J. W., Mino-Kenudson, M. A., Fulton, L. E., Hata, A. N., Lockerman, E. L., Kalsy, A., et al. (2015) · Cancer Discovery · doi:10.1158/2159-8290.cd-15-0399 · Cited by 459 · see citing works
Drugging an undruggable pocket on KRAS
Kessler, D., Gmachl, M., Mantoulidis, A., Martin, L. J., Zoephel, A., Mayer, M., Gollner, A., Covini, D., Fischer, S., Gerstberger, T., et al. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1904529116 · Cited by 449 · see citing works
Nichols, R. J., Haderk, F., Stahlhut, C., Schulze, C. J., Hemmati, G., Wildes, D., Tzitzilonis, C., Mordec, K., Marquez, A., Romero, J., et al. (2018) · Nature Cell Biology · doi:10.1038/s41556-018-0169-1 · Cited by 415 · see citing works
Mertins, P., Yang, F., Liu, T., Mani, D. R., Petyuk, V., Gillette, M. A., Clauser, K. R., Qiao, J., Gritsenko, M. A., Moore, R. J., et al. (2014) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m113.036392 · Cited by 407 · see citing works
Longati, P., Jia, X., Eimer, J., Wagman, A., Witt, M.-R., Rehnmark, S., Verbeke, C., Toftgård, R., Löhr, M., & Heuchel, R. L. (2013) · BMC Cancer · doi:10.1186/1471-2407-13-95 · Cited by 394 · see citing works
Riedl, A., Schlederer, M., Pudelko, K., Stadler, M., Walter, S., Unterleuthner, D., Unger, C., Kramer, N., Hengstschläger, M., Kenner, L., et al. (2016) · Journal of Cell Science · doi:10.1242/jcs.188102 · Cited by 389 · see citing works
Mutant KRAS-driven cancers depend on PTPN11/SHP2 phosphatase
Ruess, D. A., Heynen, G. J., Ciecielski, K. J., Ai, J., Berninger, A., Kabacaoglu, D., Görgülü, K., Dantes, Z., Wörmann, S. M., Diakopoulos, K. N., et al. (2018) · Nature Medicine · doi:10.1038/s41591-018-0024-8 · Cited by 370 · see citing works
Oncogenic KRAS Regulates Tumor Cell Signaling via Stromal Reciprocation
Tape, C. J., Ling, S., Dimitriadi, M., McMahon, K. M., Worboys, J. D., Leong, H. S., Norrie, I. C., Miller, C. J., Poulogiannis, G., Lauffenburger, D. A., et al. (2016) · Cell · doi:10.1016/j.cell.2016.03.029 · Cited by 369 · see citing works
Jänne, P. A., van den Heuvel, M. M., Barlesi, F., Cobo, M., Mazieres, J., Crinò, L., Orlov, S., Blackhall, F., Wolf, J., Garrido, P., et al. (2017) · JAMA · doi:10.1001/jama.2017.3438 · Cited by 335 · see citing works
A Central Role for RAF→MEK→ERK Signaling in the Genesis of Pancreatic Ductal Adenocarcinoma
Collisson, E. A., Trejo, C. L., Silva, J. M., Gu, S., Korkola, J. E., Heiser, L. M., Charles, R., Rabinovich, B. A., Hann, B. C., Dankort, D. L., et al. (2012) · Cancer Discovery · doi:10.1158/2159-8290.cd-11-0347 · Cited by 320 · see citing works
SHP2 is required for growth of KRAS-mutant non-small-cell lung cancer in vivo
Mainardi, S., Mulero-Sánchez, A., Prahallad, A., Germano, G., Bosma, A., Krimpenfort, P., Lieftink, C., Steinberg, J. D., de Wit, N., Gonçalves-Ribeiro, S., et al. (2018) · Nature Medicine · doi:10.1038/s41591-018-0023-9 · Cited by 320 · see citing works
Compensatory metabolic networks in pancreatic cancers upon perturbation of glutamine metabolism
Biancur, D. E., Paulo, J. A., Małachowska, B., Quiles Del Rey, M., Sousa, C. M., Wang, X., Sohn, A. S. W., Chu, G. C., Gygi, S. P., Harper, J. W., et al. (2017) · Nature Communications · doi:10.1038/ncomms15965 · Cited by 315 · see citing works
Self-citationBreslin, S., & O’Driscoll, L. (2016) · Oncotarget · doi:10.18632/oncotarget.9935 · Cited by 312 · see citing works
Targeting wild-type KRAS-amplified gastroesophageal cancer through combined MEK and SHP2 inhibition
Wong, G. S., Zhou, J., Liu, J. B., Wu, Z., Xu, X., Li, T., Xu, D., Schumacher, S. E., Puschhof, J., McFarland, J., et al. (2018) · Nature Medicine · doi:10.1038/s41591-018-0022-x · Cited by 266 · see citing works
KRAS G12C NSCLC Models Are Sensitive to Direct Targeting of KRAS in Combination with PI3K Inhibition
Misale, S., Fatherree, J. P., Cortez, E., Li, C., Bilton, S., Timonina, D., Myers, D. T., Lee, D., Gomez-Caraballo, M., Greenberg, M., et al. (2019) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-18-0368 · Cited by 259 · see citing works
A Convergence-Based Framework for Cancer Drug Resistance
Konieczkowski, D. J., Johannessen, C. M., & Garraway, L. A. (2018) · Cancer Cell · doi:10.1016/j.ccell.2018.03.025 · Cited by 258 · see citing works
Oncogenic KRAS supports pancreatic cancer through regulation of nucleotide synthesis
Santana-Codina, N., Roeth, A. A., Zhang, Y., Yang, A., Mashadova, O., Asara, J. M., Wang, X., Bronson, R. T., Lyssiotis, C. A., Ying, H., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-07472-8 · Cited by 252 · see citing works
Self-citationMetabolic Dependencies in RAS -Driven Cancers
Kimmelman, A. C. (2015) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-14-2425 · Cited by 220 · see citing works
Development of combination therapies to maximize the impact of KRAS-G12C inhibitors in lung cancer
Molina-Arcas, M., Moore, C., Rana, S., van Maldegem, F., Mugarza, E., Romero-Clavijo, P., Herbert, E., Horswell, S., Li, L.-S., Janes, M. R., et al. (2019) · Science Translational Medicine · doi:10.1126/scitranslmed.aaw7999 · Cited by 203 · see citing works
Franco, J., Balaji, U., Freinkman, E., Witkiewicz, A. K., & Knudsen, E. S. (2016) · Cell Reports · doi:10.1016/j.celrep.2015.12.094 · Cited by 199 · see citing works
Will, M., Qin, A. C. R., Toy, W., Yao, Z., Rodrik-Outmezguine, V. S., Schneider, C., Huang, X., Monian, P., Jiang, X., de Stanchina, E., et al. (2014) · Cancer Discovery · doi:10.1158/2159-8290.cd-13-0611 · Cited by 195 · see citing works
KRAS Suppression-Induced Degradation of MYC Is Antagonized by a MEK5-ERK5 Compensatory Mechanism
Vaseva, A. V., Blake, D. R., Gilbert, T. S. K., Ng, S., Hostetter, G. H., Azam, S. H., Ozkan‐Dagliyan, I., Gautam, P., Bryant, K. L., Pearce, K. H., et al. (2018) · Cancer Cell · doi:10.1016/j.ccell.2018.10.001 · Cited by 181 · see citing works
Survival of pancreatic cancer cells lacking KRAS function
Muzumdar, M. D., Chen, P.-Y., Dorans, K. J., Chung, K. M., Bhutkar, A., Hong, E., Noll, E. M., Sprick, M. R., Trumpp, A., & Jacks, T. (2017) · Nature Communications · doi:10.1038/s41467-017-00942-5 · Cited by 177 · see citing works
Vallejo, A., Perurena, N., Guruceaga, E., Mazur, P. K., Martínez-Canarias, S., Zandueta, C., Valencia, K., Arricibita, A., Gwinn, D. M., Sayles, L. C., et al. (2017) · Nature Communications · doi:10.1038/ncomms14294 · Cited by 175 · see citing works
KRAS <sup>G12C</sup> inhibition produces a driver-limited state revealing collateral dependencies
Lou, K., Steri, V., Ge, A. Y., Hwang, Y. C., Yogodzinski, C. H., Shkedi, A. R., Choi, A. L. M., Mitchell, D. C., Swaney, D. L., Hann, B., et al. (2019) · Science Signaling · doi:10.1126/scisignal.aaw9450 · Cited by 175 · see citing works
Fakih, M., O'Neil, B., Price, T. J., Falchook, G. S., Desai, J., Kuo, J., Govindan, R., Rasmussen, E., Morrow, P. K. H., Ngang, J., et al. (2019) · Journal of Clinical Oncology · doi:10.1200/jco.2019.37.15_suppl.3003 · Cited by 172 · see citing works
Erickson, B. K., Jedrychowski, M. P., McAlister, G. C., Everley, R. A., Kunz, R. C., & Gygi, S. P. (2014) · Analytical Chemistry · doi:10.1021/ac503934f · Cited by 159 · see citing works
Self-citationMolina-Arcas, M., Hancock, D. C., Sheridan, C., Kumar, M. S., & Downward, J. (2013) · Cancer Discovery · doi:10.1158/2159-8290.cd-12-0446 · Cited by 157 · see citing works
Combined MEK and PI3K Inhibition in a Mouse Model of Pancreatic Cancer
Alagesan, B., Contino, G., Guimarães, A. R., Corcoran, R. B., Deshpande, V., Wojtkiewicz, G. R., Hezel, A. F., Wong, K., Loda, M. F., Weissleder, R., et al. (2014) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-14-1591 · Cited by 145 · see citing works
Potent and Selective Covalent Quinazoline Inhibitors of KRAS G12C
Zeng, M., Lu, J., Li, L., Feru, F., Quan, C., Gero, T. W., Ficarro, S. B., Xiong, Y., Ambrogio, C., Paranal, R. M., et al. (2017) · Cell Chemical Biology · doi:10.1016/j.chembiol.2017.06.017 · Cited by 136 · see citing works
Self-citationSynthetic vulnerabilities of mesenchymal subpopulations in pancreatic cancer
Genovese, G., Carugo, A., Tepper, J., Robinson, F. S., Li, L., Svelto, M., Nezi, L., Corti, D., Minelli, R., Pettazzoni, P., et al. (2017) · Nature · doi:10.1038/nature21064 · Cited by 131 · see citing works
Yi, T., Zhai, B., Yu, Y., Yoshikawa, K., Raschle, T., Etzkorn, M., Seo, H., Nagiec, M. J., Luna, R. E., Reinherz, E. L., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1404943111 · Cited by 124 · see citing works
GSK3 suppression upregulates β-catenin and c-Myc to abrogate KRas-dependent tumors
Kazi, A., Xiang, S., Yang, H., Delitto, D., Trevino, J. G., Jiang, R. H. Y., Ayaz, M., Lawrence, H. R., Kennedy, P., & Sebti, S. M. (2018) · Nature Communications · doi:10.1038/s41467-018-07644-6 · Cited by 122 · see citing works
Dissection of TBK1 signaling via phosphoproteomics in lung cancer cells
Kim, J., Welsh, E. A., Oguz, U., Fang, B., Bai, Y., Kinose, F., Bronk, C. C., Rix, L. L. R., Beg, A. A., Rix, U., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1220674110 · Cited by 120 · see citing works
Connexin-43-dependent ATP release mediates macrophage activation during sepsis
Dosch, M., Zindel, J., Jebbawi, F., Mélin, N., Sánchez‐Taltavull, D., Stroka, D., Candinas, D., & Beldi, G. (2019) · eLife · doi:10.7554/elife.42670 · Cited by 110 · see citing works
A Phosphoproteomic Comparison of B-RAFV600E and MKK1/2 Inhibitors in Melanoma Cells*
Stuart, S. A., Houel, S., Lee, T., Wang, N., Old, W. M., & Ahn, N. G. (2015) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m114.047233 · Cited by 106 · see citing works
Quantitative phosphoproteomic profiling of human non-small cell lung cancer tumors
Schweppe, D. K., Rigas, J. R., & Gerber, S. A. (2013) · Journal of Proteomics · doi:10.1016/j.jprot.2013.07.023 · Cited by 99 · see citing works
Targeting KRAS-Mutant Non–Small Cell Lung Cancer with the Hsp90 Inhibitor Ganetespib
Acquaviva, J., Smith, D. L., Sang, J., Friedland, J. C., He, S., Sequeira, M., Zhang, C., Wada, Y., & Proia, D. A. (2012) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-12-0615 · Cited by 96 · see citing works
Seth, S., Li, C.-Y., Ho, I.-L., Corti, D., Loponte, S., Sapio, L., Poggetto, E. D., Yen, E.-Y., Robinson, F. S., Peoples, M. D., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.01.048 · Cited by 85 · see citing works
Pettazzoni, P., Viale, A., Shah, P. K., Carugo, A., Ying, H., Wang, H., Genovese, G., Seth, S., Minelli, R., Green, T., et al. (2015) · Cancer Research · doi:10.1158/0008-5472.can-14-1854 · Cited by 80 · see citing works
Kim, J., Welsh, E. A., Fang, B., Bai, Y., Kinose, F., Eschrich, S. A., Koomen, J. M., & Haura, E. B. (2016) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-15-0506 · Cited by 76 · see citing works
Britton, D., Zen, Y., Quaglia, A., Selzer, S., Mitra, V., Lößner, C., Jung, S., Böhm, G., Schmid, P., Prefot, P., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0090948 · Cited by 59 · see citing works
Paulo, J. A., Gaun, A., & Gygi, S. P. (2015) · Journal of Proteome Research · doi:10.1021/acs.jproteome.5b00398 · Cited by 58 · see citing works
Fujita-Sato, S., Galeas, J., Truitt, M., Pitt, C., Urisman, A., Bandyopadhyay, S., Ruggero, D., & McCormick, F. P. (2015) · Cancer Research · doi:10.1158/0008-5472.can-14-1623 · Cited by 54 · see citing works
El‐Jawhari, J. J., El-Sherbiny, Y. M., Scott, G. B., Morgan, R. S. M., Prestwich, R. J. D., Bowles, P. A., Blair, G. E., Tanaka, T. U., Rabbitts, T. H., Meade, J. L., et al. (2013) · Molecular Immunology · doi:10.1016/j.molimm.2013.11.020 · Cited by 54 · see citing works
Dietrich, P., Kuphal, S., Spruß, T., Hellerbrand, C., & Bosserhoff, A. (2017) · Oncogene · doi:10.1038/onc.2017.391 · Cited by 54 · see citing works
Haines, E., Chen, T., Kommajosyula, N., Chen, Z., Herter-Sprie, G. S., Cornell, L., Wong, K., & Shapiro, G. I. (2018) · Oncotarget · doi:10.18632/oncotarget.25803 · Cited by 53 · see citing works
Adaptive and Reversible Resistance to Kras Inhibition in Pancreatic Cancer Cells
Chen, P., Muzumdar, M. D., Dorans, K. J., Robbins, R., Bhutkar, A. J., Rosario, A. M. D., Mertins, P., Qiao, J., Schäfer, C., Gertler, F. B., et al. (2017) · Cancer Research · doi:10.1158/0008-5472.can-17-2129 · Cited by 45 · see citing works
Jacobi, N., Seeboeck, R., Hofmann, E., Schweiger, H., Smolinska, V., Mohr, T., Boyer, A., Sommergruber, W., Lechner, P., Pichler-Huebschmann, C., et al. (2017) · Oncotarget · doi:10.18632/oncotarget.22475 · Cited by 43 · see citing works
A MEK/PI3K/HDAC inhibitor combination therapy for KRAS mutant pancreatic cancer cells
Ischenko, I., Petrenko, O., & Hayman, M. J. (2015) · Oncotarget · doi:10.18632/oncotarget.4538 · Cited by 42 · see citing works
Gagliano, N. (2016) · World Journal of Gastroenterology · doi:10.3748/wjg.v22.i18.4466 · Cited by 37 · see citing works
Rao, G., Kim, I.-K., Conforti, F., Liu, J., Zhang, Y.-W., & Giaccone, G. (2018) · European Journal of Cancer · doi:10.1016/j.ejca.2018.05.013 · Cited by 34 · see citing works
Fritsche‐Guenther, R., Zasada, C., Mastrobuoni, G., Royla, N., Rainer, R. J., Roßner, F., Pietzke, M., Klipp, E., Sers, C., & Kempa, S. (2018) · Scientific Reports · doi:10.1038/s41598-018-27394-1 · Cited by 31 · see citing works
Cotargeting of MEK and PDGFR/STAT3 Pathways to Treat Pancreatic Ductal Adenocarcinoma
Sahu, N., Chan, E., Chu, F., Pham, T. Q., Koeppen, H., Forrest, W. F., Merchant, M. A., & Settleman, J. (2017) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-17-0009 · Cited by 30 · see citing works
Survivin knockdown induces senescence in TTF‑1-expressing, KRAS-mutant lung adenocarcinomas
Sumi, T., Hirai, S., Yamaguchi, M., Tanaka, Y., Tada, M., Yamada, G., Hasegawa, T., Miyagi, Y., Niki, T., Watanabe, A., et al. (2018) · International Journal of Oncology · doi:10.3892/ijo.2018.4365 · Cited by 20 · see citing works
Proteome-Wide Protein Expression Profiling Across Five Pancreatic Cell Lines
Paulo, J. A., Mancias, J. D., & Gygi, S. P. (2017) · Pancreas · doi:10.1097/mpa.0000000000000800 · Cited by 19 · see citing works
Self-citationSimultaneous gene silencing of KRAS and anti-apoptotic genes as a multitarget therapy
Werner, K., Lademann, F., Thepkaysone, M.-L., Jahnke, B., Aust, D. E., Kahlert, C., Weber, G. F., Weitz, J., Grützmann, R., & Pilarsky, C. P. (2015) · Oncotarget · doi:10.18632/oncotarget.6766 · Cited by 15 · see citing works
MEK Inhibition Potentiates the Activity of Hsp90 Inhibitor 17-AAG against Pancreatic Cancer Cells
Zhang, T., Li, Y., Zhu, Z., Gu, M., Newman, B. W., & Sun, D. (2010) · Molecular Pharmaceutics · doi:10.1021/mp900321a · Cited by 13 · see citing works
Flagged first, then by citations
1 of the 91 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Tanaka, N., Lin, J. J., Li, C., Ryan, M. B., Zhang, J., Kiedrowski, L. A., Michel, A. G., Syed, M. U., Fella, K. A., Sakhi, M., et al. (2021) · Cancer Discovery · doi:10.1158/2159-8290.cd-21-0365 · Cited by 527 · see citing works
Copper bioavailability is a KRAS-specific vulnerability in colorectal cancer
Aubert, L., Nandagopal, N., Steinhart, Z., Lavoie, G., Nourreddine, S., Berman, J. M., Saba-El-Leil, M. K., Papadopoli, D. J., Lin, S., Hart, T., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-17549-y · Cited by 288 · see citing works
Chemical remodeling of a cellular chaperone to target the active state of mutant KRAS
Schulze, C. J., Seamon, K. J., Zhao, Y., Yang, Y. C., Cregg, J., Kim, D., Tomlinson, A., Choy, T. J., Wang, Z., Sang, B., et al. (2023) · Science · doi:10.1126/science.adg9652 · Cited by 264 · see citing works
The KRAS-G12C inhibitor: activity and resistance
Liu, J., Kang, R., & Tang, D. (2021) · Cancer Gene Therapy · doi:10.1038/s41417-021-00383-9 · Cited by 222 · see citing works
Targeting de novo lipogenesis and the Lands cycle induces ferroptosis in KRAS-mutant lung cancer
Bartolacci, C., Andreani, C., do Vale, G. D., Berto, S., Melegari, M., Crouch, A. C., Baluya, D. L., Kemble, G. W., Hodges, K. B., Starrett, J. H., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-31963-4 · Cited by 179 · see citing works
Santana-Codina, N., del Rey, M. Q., Kapner, K. S., Zhang, H., Gikandi, A., Malcolm, C., Poupault, C. L., Kuljanin, M., John, K. M., Biancur, D. E., et al. (2022) · Cancer Discovery · doi:10.1158/2159-8290.cd-22-0043 · Cited by 179 · see citing works
Self-citationEpitranscriptomics and epiproteomics in cancer drug resistance: therapeutic implications
Song, H., Liu, D., Dong, S., Zeng, L., Wu, Z., Zhao, P., Zhang, L., Chen, Z., & Zou, C. (2020) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-00300-w · Cited by 138 · see citing works
Ravichandran, M., Hu, J., Cai, C., Ward, N. P., Venida, A., Foakes, C., Kuljanin, M., Yang, A., Hennessey, C. J., Yang, Y., et al. (2022) · Cancer Discovery · doi:10.1158/2159-8290.cd-22-0044 · Cited by 80 · see citing works
Self-citationOncogenic KRAS blockade therapy: renewed enthusiasm and persistent challenges
Tang, D., Kroemer, G., & Kang, R. (2021) · Molecular Cancer · doi:10.1186/s12943-021-01422-7 · Cited by 80 · see citing works
Drugging the Undruggable: Advances on RAS Targeting in Cancer
Molina‐Arcas, M., Samani, A., & Downward, J. (2021) · Genes · doi:10.3390/genes12060899 · Cited by 73 · see citing works
Orsburn, B. C., Yuan, Y., & Bumpus, N. N. (2022) · Nature Communications · doi:10.1038/s41467-022-34919-w · Cited by 71 · see citing works
Mukhopadhyay, S., Encarnación-Rosado, J., Lin, E. Y., Sohn, A. S. W., Zhang, H., Mancias, J. D., & Kimmelman, A. C. (2023) · Science Advances · doi:10.1126/sciadv.adf9284 · Cited by 65 · see citing works
Self-citationResistance looms for KRAS G12C inhibitors and rational tackling strategies
Zhang, J., Zhang, J., Liu, Q., Fan, X., Leung, E. L., Yao, X., & Liu, L. (2021) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2021.108050 · Cited by 56 · see citing works
A neomorphic protein interface catalyzes covalent inhibition of RAS G12D aspartic acid in tumors
Weller, C. E., Burnett, G. L., Jiang, L., Chakraborty, S., Zhang, D., Vita, N. A., Dilly, J., Kim, E., Maldonato, B. J., Seamon, K. J., et al. (2025) · Science · doi:10.1126/science.ads0239 · Cited by 63 · see citing works
Self-citationThinking Differently about Cancer Treatment Regimens
Settleman, J., Neto, J. M. F., & Bernards, R. (2021) · Cancer Discovery · doi:10.1158/2159-8290.cd-20-1187 · Cited by 48 · see citing works
Targeting KRAS in Pancreatic Ductal Adenocarcinoma: The Long Road to Cure
de Jesus, V. H. F., Mathias-Machado, M. C., de Farias, J. P. F., Aruquipa, M. P. S., Jacome, A. A. D. A., & Peixoto, R. D. (2023) · Cancers · doi:10.3390/cancers15205015 · Cited by 47 · see citing works
Lietman, C. D., Johnson, M. L., McCormick, F., & Lindsay, C. R. (2022) · American Society of Clinical Oncology Educational Book · doi:10.1200/edbk_351333 · Cited by 44 · see citing works
Targeting KRAS G12C with Covalent Inhibitors
Ostrem, J. M. L., & Shokat, K. M. (2021) · Annual Review of Cancer Biology · doi:10.1146/annurev-cancerbio-041621-012549 · Cited by 43 · see citing works
Targeting KRASG12C-Mutated Advanced Colorectal Cancer: Research and Clinical Developments
Ji, J., Wang, C., & Fakih, M. (2022) · OncoTargets and Therapy · doi:10.2147/ott.s340392 · Cited by 39 · see citing works
Anastasiou, P., Moore, C., Rana, S., Tomaschko, M., Pillsbury, C. E., de Castro, A., Boumelha, J., Mugarza, E., Trécesson, S. D. C., Mikolajczak, A., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-52324-3 · Cited by 35 · see citing works
Diehl, J. N., Klomp, J. E., Snare, K. R., Hibshman, P. S., Blake, D. R., Kaiser, Z. D., Gilbert, T. S. K., Baldelli, E., Pierobon, M., Papke, B., et al. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.101335 · Cited by 29 · see citing works
McFall, T. B., & Stites, E. C. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.110096 · Cited by 29 · see citing works
Li, H., Qi, W.-L., Wang, Y., & Meng, L. (2021) · Genes & Diseases · doi:10.1016/j.gendis.2021.08.011 · Cited by 25 · see citing works
Tanaka, N., & Ebi, H. (2024) · Cancer Science · doi:10.1111/cas.16441 · Cited by 26 · see citing works
Groendyke, B. J., Nabet, B., Mohardt, M. L., Zhang, H., Peng, K., Koide, E., Coffey, C. R., Che, J., Scott, D. A., Bass, A. J., et al. (2020) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.0c00338 · Cited by 24 · see citing works
Self-citationDirect GDP-KRAS G12C inhibitors and mechanisms of resistance: the tip of the iceberg
Rosen, J. C., Sacher, A. G., & Tsao, M. (2023) · Therapeutic Advances in Medical Oncology · doi:10.1177/17588359231160141 · Cited by 22 · see citing works
Bioinformatic Analysis of Temporal and Spatial Proteome Alternations During Infections
Rahmatbakhsh, M., Gagarinova, A. G., & Babu, M. (2021) · Frontiers in Genetics · doi:10.3389/fgene.2021.667936 · Cited by 21 · see citing works
Yang, F., Xu, X.-L., Hu, T., Liu, J., Zhou, J.-Z., Ma, L., & Liu, H. (2023) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.2c01527 · Cited by 21 · see citing works
Macaya, I., Román, M., Welch, C., Entrialgo‐Cadierno, R., Salmón, M., Santos, A., Feliu, I., Kovalski, J. R., López, I., Rodríguez‐Remírez, M., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-41828-z · Cited by 21 · see citing works
Targeting KRASG12C in Non-Small-Cell Lung Cancer: Current Standards and Developments
Torres-Jiménez, J., Espinar, J. B., Bote, H., Berjaga, M. Z., Esteban-Villarrubia, J., Fraile, J. Z., & Paz-Ares, L. G. (2024) · Drugs · doi:10.1007/s40265-024-02030-7 · Cited by 22 · see citing works
Inhibition of RAS: proven and potential vulnerabilities
Zuberi, M., Khan, I., & O’Bryan, J. P. (2020) · Biochemical Society Transactions · doi:10.1042/bst20190023 · Cited by 20 · see citing works
Orsburn, B. C. (2023) · Journal of Proteome Research · doi:10.1021/acs.jproteome.3c00212 · Cited by 18 · see citing works
De novo pyrimidine biosynthesis inhibition synergizes with BCL-XL targeting in pancreatic cancer
Zhang, H., Santana-Codina, N., Yu, Q., Poupault, C. L., Campos, C., Qin, X., Sindoni, N., Ciscar, M., Padhye, A., Kuljanin, M., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-61242-x · Cited by 19 · see citing works
Self-citationDevelopment and Characterization of Selective FAK Inhibitors and PROTACs with In Vivo Activity
Koide, E., Mohardt, M. L., Doctor, Z. M., Yang, A., Hao, M., Donovan, K. A., Kuismi, C. C., Nelson, A. J., Abell, K., Aguiar, M., et al. (2023) · ChemBioChem · doi:10.1002/cbic.202300141 · Cited by 18 · see citing works
Self-citationConquering oncogenic KRAS and its bypass mechanisms
Hou, P., & Wang, Y. (2022) · Theranostics · doi:10.7150/thno.71260 · Cited by 17 · see citing works
KRASG12C inhibitor: combing for combination
Chakraborty, A. (2020) · Biochemical Society Transactions · doi:10.1042/bst20200473 · Cited by 14 · see citing works
Evaluation of KRAS Concomitant Mutations in Advanced Lung Adenocarcinoma Patients
Aran, V., Zalis, M. G., Montella, T. C., de Sousa, C. A. M., Ferrari, B. L., & Ferreira, C. G. (2021) · Medicina · doi:10.3390/medicina57101039 · Cited by 13 · see citing works
Han, Z., Zhou, D., Wang, J., Jiang, B., & Liu, X. (2022) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2022.188677 · Cited by 13 · see citing works
Single-cell sensor analyses reveal signaling programs enabling Ras-G12C drug resistance
Zhang, J. Z., Ong, S., Baker, D. A., & Maly, D. J. (2024) · Nature Chemical Biology · doi:10.1038/s41589-024-01684-4 · Cited by 12 · see citing works
Kaczmarczyk, J. A., Roberts, R. R., Luke, B. T., Chan, K. C., Wagoner, C. M. V., Felder, R. A., Saul, R. G., Colantonio, S., & Blonder, J. (2021) · Oncotarget · doi:10.18632/oncotarget.28072 · Cited by 11 · see citing works
Unraveling and targeting RAS-driven metabolic signaling for therapeutic gain
DeLiberty, J. M., Robb, R. N., Gates, C. E., & Bryant, K. L. (2022) · Advances in cancer research · doi:10.1016/bs.acr.2021.07.010 · Cited by 9 · see citing works
Ma, T. P., Izrael-Tomasevic, A., Mroue, R. M., Budayeva, H. G., Malhotra, S., Raisner, R. M., Evangelista, M., Rose, C. M., Kirkpatrick, D. S., & Yu, K. (2023) · Journal of Proteome Research · doi:10.1021/acs.jproteome.2c00703 · Cited by 10 · see citing works
Giorgio, E. D., Choudhary, H., Ferino, A., Cortolezzis, Y., Dalla, E., D’Este, F., Comelli, M., Rapozzi, V., & Xodo, L. E. (2023) · iScience · doi:10.1016/j.isci.2023.108566 · Cited by 10 · see citing works
ZBTB11 depletion targets metabolic vulnerabilities in KRAS inhibitor-resistant PDAC
Tran, N. L., Jiang, J., Ma, M., Gadbois, G. E., Gulay, K. C. M., Verano, A. L., Schiavon, C. R., Rebollo, E., Zhou, H., Huang, C., et al. (2025) · Nature Chemical Biology · doi:10.1038/s41589-025-01978-1 · Cited by 12 · see citing works
Self-citationKRAS-targeted therapies in cancer: novel approaches and overcoming resistance
Tang, D., Kroemer, G., & Kang, R. (2025) · BMJ Oncology · doi:10.1136/bmjonc-2025-000946 · Cited by 10 · see citing works
Yu, J. X., Suh, J. M., Popova, K. D., Garcia, K., Joshi, T. V., Culbertson, B., Spinelli, J. B., Subramanyam, V., Lou, K., Charbonneau, T., et al. (2026) · Nature Cancer · doi:10.1038/s43018-026-01130-5 · Cited by 8 · see citing works
Wang, X., Ni, R., Wang, X., & Li, X. (2026) · Molecular Cancer · doi:10.1186/s12943-025-02559-5 · Cited by 9 · see citing works
Cytotoxic activity of KRAS inhibitors in combination with chemotherapeutics
Hamilton, G., & Plangger, A. (2021) · Expert Opinion on Drug Metabolism & Toxicology · doi:10.1080/17425255.2021.1965123 · Cited by 7 · see citing works
Theardy, M. S., Takeda, M., Sorokin, A., Chen, S., Yang, Z., Wang, X., Kanikarla, P., Coker, O., Nguyen, P., Wei, Y., et al. (2025) · Cell Reports Medicine · doi:10.1016/j.xcrm.2025.102253 · Cited by 6 · see citing works
SRC at the Crossroads of KRAS Inhibitor Resistance: Mechanisms and Therapeutic Opportunities
Tian, H., Zhao, D., Zhou, Z., Kim, A., Huang, H., Lee, Y. J., Qu, Z., Kang, R., Zeh, H. J., Westover, K. D., et al. (2026) · Cancer Letters · doi:10.1016/j.canlet.2025.218194 · Cited by 7 · see citing works
Heterogeneous adaptation of cysteine reactivity to a covalent oncometabolite
Perez, M., Bak, D. W., Bergholtz, S. E., Crooks, D. R., Arimilli, B. S., Yang, Y., Weerapana, E., Linehan, W. M., & Meier, J. L. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ac120.014993 · Cited by 6 · see citing works
Combinatorial approaches for mitigating resistance to KRAS-targeted therapies
Warren, H. R., Ross, S. J., Smith, P. D., Coulson, J. M., & Prior, I. A. (2022) · Biochemical Journal · doi:10.1042/bcj20220440 · Cited by 6 · see citing works
Understanding and drugging RAS: 40 years to break the tip of the iceberg
Brady, D. C., Hmeljak, J., & Dar, A. C. (2022) · Disease Models & Mechanisms · doi:10.1242/dmm.049519 · Cited by 5 · see citing works
Miao, J., Guan, W., Wang, J., Gong, H., Xie, Q., & Gao, Y. (2026) · Hereditas · doi:10.1186/s41065-025-00570-w · Cited by 4 · see citing works
KRAS Inhibition Activates an Actionable CD24 “Do Not Eat Me” Signal in Pancreatic Cancer
Wei, Y., Liu, M., Yen, E.-Y., Yao, J., Xun, Z., Nguyen, P. T.-M., Wang, X., Yang, Z., Yousef, A. M. G., Pan, D. N., et al. (2025) · Cancer Research · doi:10.1158/0008-5472.can-25-2024 · Cited by 5 · see citing works
Shen, T., Fei, W., Hu, Z., Pang, M., Ma, J., Zhou, T., & Shang, Y. (2025) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2025.109345 · Cited by 3 · see citing works
ZBTB11 Depletion Targets Metabolic Vulnerabilities in K-Ras Inhibitor Resistant PDACPreprint
Tran, N. L., Jiang, J., Ma, M., Gadbois, G. E., Gulay, K. C. M., Verano, A. L., Zhou, H., Huang, C., Scott, D. A., Bang, A. G., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.05.19.594824 · Cited by 3 · see citing works
Self-citationAguilar‐Valdés, A., González‐Vela, F., Sánchez‐Vidal, H., & Martínez‐Aguilar, J. (2023) · PROTEOMICS · doi:10.1002/pmic.202300041 · Cited by 2 · see citing works
Won, H.-J., Baek, S. M., Lee, M. H., Park, J. H., Shin, J., Yang, Y., Jang, Y. H., Inn, K., & Kim, N. (2026) · European Journal of Organic Chemistry · doi:10.1002/ejoc.202501208 · Cited by 1 · see citing works
On the Diophantine Equation 3 x + b3 y = 6 z
Sándor, J. (2001) · Octogon Mathematical Magazine archive · Cited by 1 · see citing works
Blonder, J., Kaczmarczyk, J. A., Roberts, R. R., Luke, B. T., Chan, K. C., Wagoner, C. M. V., Felder, R. A., Saul, R. G., & Colantonio, S. (2020) · Research Square · doi:10.21203/rs.3.rs-72194/v1 · Cited by 1 · see citing works
Defining the KRAS-regulated kinome in KRAS-mutant pancreatic cancerPreprint
Diehl, J. N., Klomp, J. E., Snare, K. R., Blake, D. R., Hibshman, P. S., Kaiser, Z. D., Gilbert, T. S. K., Baldelli, E., Pierobon, M., Papke, B., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.04.27.441678
Aliquoting of isobaric labeling reagents for low concentration and single cell proteomics samplesPreprint
Yuan, Y., & Orsburn, B. C. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.06.23.449560
Improving cancer therapy through unconventional strategies
Neto, J. M. F. (2021) · doi:10.33540/1009
Recent Developments, Challenges and Opportunities in Targeting the KRAS Pathway
Pothuganti, M. K., Mitra, S., Iyer, P. S., & Gowda, N. M. (2022) · Letters in Drug Design & Discovery · doi:10.2174/1570180819666220704104028
Santana-Codina, N., del Rey, M. Q., Kapner, K. S., Zhang, H., Gikandi, A., Malcolm, C., Poupault, C. L., Kuljanin, M., John, K. M., Biancur, D. E., et al. (2023) · doi:10.1158/2159-8290.22541117.v1
Self-citationSantana-Codina, N., del Rey, M. Q., Kapner, K. S., Zhang, H., Gikandi, A., Malcolm, C., Poupault, C. L., Kuljanin, M., John, K. M., Biancur, D. E., et al. (2023) · doi:10.1158/2159-8290.22541117
Self-citationTakeda, M., Theardy, M. S., Sorokin, A. V., Coker, O., Marie, P. K., Chen, S., Yang, Z., Nguyen, P. T.-M., Wei, Y., Yao, J., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.08.06.606865
Zhang, T., Shin, S., McCrimmon, C., Theocharous, M., Schittenhelm, R. B., Jardé, T., Daly, R. J., & Nguyen, L. K. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.10.27.620536
Vicent, S., Welch, C., Novoa, G., Vasquez-Valencia, C., Macaya, I., Jimenez-Alonso, J. J., Subrizio, A., Lagos, A. F., Llorente, S., Jimenez, M., et al. (2026) · Research Square · doi:10.21203/rs.3.rs-9085811/v1
What Are the Practical Applications of Single-Cell Proteomics?
Orsburn, B. C. (2026) · Proteomes · doi:10.3390/proteomes14020026
Shrivastava, A., Pederson, E. N., Nguyen, T. U., Chuen, J., Mohan, P., Pande, S., Toribio, A. R., Lecomte, N., Melchor, J. P., McAuliffe, J. C., et al. (2026) · Cell Reports · doi:10.1016/j.celrep.2026.117520
GALE-dependent glycoproteome remodelling is a determinant of oncogenic RAS transformationPreprint
Stölting, F., Vesce, R., Rodríguez-Santana, C., Ciscar, M., Delaidelli, A., Lin, Q., Ballmeyer, C., Chan, S., Lesch, R., Li, R., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.06.15.732364
Self-citationHai, N., Dessai, C. V. P., Sun, D., Ao, J., Lyu, P., Zhu, Y., & Cheng, J. (2026) · Science Advances · doi:10.1126/sciadv.aee7678
Suri, P., Daartey, A. B., Khan, D. M. I. O., Rayana, N. P., Chilamakuri, R., Godugu, D., Azad, M. G., Reeb, K. L., & Richardson, D. R. (2026) · Pharmacological Reviews · doi:10.1016/j.pharmr.2026.100158
DeLiberty, J. M., Kong, F. Y., Yu, Q., Sindoni, N., Lin, J., Kang, K., Kim, E. Y., Chen, S., Padhye, A., Coker, O., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.10.01.756025
Self-citation
- Authors
- Santana-Codina, N., Chandhoke, A. S., Yu, Q., Małachowska, B., Kuljanin, M., Gikandi, A., Stańczak, M., Gableske, S., Jedrychowski, M. P., Scott, D. A., Aguirre, A. J., Fendler, W., Gray, N. S., & Mancias, J. D.
- Affiliations
- Dana-Farber Cancer Institute (US)
- Medical University of Lodz (PL)
- Harvard University (US)
- Corresponding author
- Mancias, Joseph D.
- ORCID
- Venue
- Cell Reports
- Publisher
- Elsevier BV
- Published
- 2020-03
- Volume
- 30
- Issue
- 13
- Pages
- 4584-4599.e4
- ISSN
- 2211-1247 (ISSN-L)
- OpenAlex
- W3014191583
- Cited by
- 77
- References
- 91
- Citations by year
- 2026: 11 · 2025: 8 · 2024: 8 · 2023: 13 · 2022: 12 · 2021: 17 · 2020: 7
- FWCI
- 4.06
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Cell Reports (publishedVersion, cc-by-nc-nd)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- Funders
- Sidney Kimmel Foundation
- Dana-Farber Cancer Institute
- Burroughs Wellcome Fund
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Health Sciences › Medicine › Oncology › Pancreatic and Hepatic Oncology Research
- Keywords
- KRAS G12C, KRAS inhibitors, drug resistance, temporal proteomics, pancreatic cancer, lung cancer, PI3K inhibitors, Hsp90 inhibitors, CDK4/6 inhibitors, SHP2 inhibitors, combination therapy
- MeSH terms
- Humans, Models, Biological, Mutation, Neoplasms, Oncogenes, Time Factors, Down-Regulation, Up-Regulation, Proto-Oncogene Proteins p21(ras), Proteome, Proteomics, Cell Line, Tumor, Cell Proliferation
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review