KRAS Dimerization Impacts MEK Inhibitor Sensitivity and Oncogenic Activity of Mutant KRAS

The Genome Analysis Toolkit: A MapReduce framework for analyzing next-generation DNA sequencing data

McKenna, A., Hanna, M., Banks, E., Sivachenko, A., Cibulskis, K., Kernytsky, A., Garimella, K., Altshuler, D., Gabriel, S., Daly, M., et al. (2010) · Genome Research · doi:10.1101/gr.107524.110 · Cited by 27,895

K-Ras(G12C) inhibitors allosterically control GTP affinity and effector interactions

Ostrem, J. M., Peters, U., Sos, M. L., Wells, J. A., & Shokat, K. M. (2013) · Nature · doi:10.1038/nature12796 · Cited by 2,557

Systematic identification of genomic markers of drug sensitivity in cancer cells

Garnett, M. J., Edelman, E. J., Heidorn, S. J., Greenman, C. D., Dastur, A., Lau, K. W., Greninger, P., Thompson, I. R., Luo, X., Soares, J., et al. (2012) · Nature · doi:10.1038/nature11005 · Cited by 2,456

RAS Proteins and Their Regulators in Human Disease

Simanshu, D. K., Nissley, D. V., & McCormick, F. (2017) · Cell · doi:10.1016/j.cell.2017.06.009 · Cited by 1,943

Lentivirus-delivered stable gene silencing by RNAi in primary cells.

Stewart, S. A., Dykxhoorn, D. M., Palliser, D., Mizuno, H., Yu, E. Y., An, D., Sabatini, D., Chen, I. S. Y., Hahn, W., Sharp, P., et al. (2003) · RNA: A publication of the RNA Society · doi:10.1261/rna.2192803 · Cited by 1,619

BRAF mutation predicts sensitivity to MEK inhibition

Solit, D. B., Garraway, L. A., Pratilas, C. A., Sawai, A., Getz, G. A., Basso, A., Ye, Q., Lobo, J. M., She, Y., Osman, I., et al. (2005) · Nature · doi:10.1038/nature04304 · Cited by 1,326

Targeting RAS–ERK signalling in cancer: promises and challenges

Samatar, A. A., & Poulikakos, P. I. (2014) · Nature Reviews Drug Discovery · doi:10.1038/nrd4281 · Cited by 1,163

Synergistic tumor suppressor activity of BRCA2 and p53 in a conditional mouse model for breast cancer

Jonkers, J., Meuwissen, R. L. J., van der Gulden, H. M. L., Peterse, H. L., van der Valk, M., & Berns, A. J. M. (2001) · Nature Genetics · doi:10.1038/ng747 · Cited by 1,044

Biochemical and Structural Analysis of Common Cancer-Associated KRAS Mutations

Hunter, J. C., Manandhar, A., Carrasco, M. A., Gurbani, D., Gondi, S., & Westover, K. D. (2015) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-15-0203 · Cited by 786

Regulation of RAF protein kinases in ERK signalling

Lavoie, H., & Therrien, M. (2015) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3979 · Cited by 702

The KRASG12C Inhibitor MRTX849 Provides Insight toward Therapeutic Susceptibility of KRAS-Mutant Cancers in Mouse Models and Patients

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

RAS-targeted therapies: is the undruggable drugged?

Moore, A. R., Rosenberg, S. C., McCormick, F., & Malek, S. (2020) · Nature Reviews Drug Discovery · doi:10.1038/s41573-020-0068-6 · Cited by 1,103

Molecular Dynamics Simulations in Drug Discovery and Pharmaceutical Development

Salo‐Ahen, O. M. H., Alanko, I., Bhadane, R. N., Bonvin, A. M. J. J., Honorato, R. V., Hossain, S., Juffer, A. H., Kabedev, A., Lahtela-Kakkonen, M. K., Larsen, A. S., et al. (2020) · Processes · doi:10.3390/pr9010071 · Cited by 732

Therapeutic strategies to target RAS-mutant cancers

Ryan, M. B., & Corcoran, R. B. (2018) · Nature Reviews Clinical Oncology · doi:10.1038/s41571-018-0105-0 · Cited by 420

Suppression of the SLC7A11/glutathione axis causes synthetic lethality in KRAS-mutant lung adenocarcinoma

Hu, K., Li, K., Lv, J., Feng, J., Chen, J., Wu, H., Cheng, F., Jiang, W., Wang, J., Pei, H., et al. (2019) · Journal of Clinical Investigation · doi:10.1172/jci124049 · Cited by 409

A model for RAS mutation patterns in cancers: finding the sweet spot

Li, S., Balmain, A., & Counter, C. M. (2018) · Nature Reviews Cancer · doi:10.1038/s41568-018-0076-6 · Cited by 384

Targeting the untargetable KRAS in cancer therapy

Liu, P., Wang, Y., & Li, X. (2019) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2019.03.002 · Cited by 366

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

KRAS interaction with RAF1 RAS-binding domain and cysteine-rich domain provides insights into RAS-mediated RAF activation

Tran, T. H., Chan, A. H., Young, L. C., Bindu, L. K., Neale, C., Messing, S. A. J., Dharmaiah, S., Taylor, T. E., Denson, J.-P., Esposito, D., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-21422-x · Cited by 245

A pan-cancer analysis of synonymous mutations

Sharma, Y., Miladi, M., Dukare, S., Boulay, K., Caudron‐Herger, M., Groß, M., Backofen, R., & Diederichs, S. (2019) · Nature Communications · doi:10.1038/s41467-019-10489-2 · Cited by 229

KRAS-mutant non-small cell lung cancer: Converging small molecules and immune checkpoint inhibition

Adderley, H., Blackhall, F. H., & Lindsay, C. R. (2019) · EBioMedicine · doi:10.1016/j.ebiom.2019.02.049 · Cited by 209

The path to the clinic: a comprehensive review on direct KRASG12C inhibitors

Kwan, A. K., Piazza, G. A., Keeton, A. B., & Leite, C. A. (2022) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-021-02225-w · Cited by 200

RAS: Striking at the Core of the Oncogenic Circuitry

Gimple, R. C., & Wang, X. (2019) · Frontiers in Oncology · doi:10.3389/fonc.2019.00965 · Cited by 174

Pharmacological targeting of RAS: recent success with direct inhibitors

O’Bryan, J. P. (2019) · Pharmacological Research · doi:10.1016/j.phrs.2018.10.021 · Cited by 153

Quantifying single-cell ERK dynamics in colorectal cancer organoids reveals EGFR as an amplifier of oncogenic MAPK pathway signalling

Ponsioen, B., Post, J. B., Amorie, J. R. B. D., Laskaris, D., van Ineveld, R. L., Kersten, S., Bertotti, A., Sassi, F. P., Sipieter, F., Cappe, B., et al. (2021) · Nature Cell Biology · doi:10.1038/s41556-021-00654-5 · Cited by 148

Impact of BRAF Mutation Class on Disease Characteristics and Clinical Outcomes in BRAF-mutant Lung Cancer

Dagogo-Jack, I., Martinez, P., Yeap, B. Y., Ambrogio, C., Ferris, L. A., Lydon, C., Nguyen, T., Jessop, N. A., Iafrate, A. J., Johnson, B. E., et al. (2019) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-18-2062 · Cited by 130

Mechanisms of Resistance to KRASG12C Inhibitors

Dunnett-Kane, V., Nicola, P. A., Blackhall, F. H., & Lindsay, C. R. (2021) · Cancers · doi:10.3390/cancers13010151 · Cited by 122

Distinct Binding Preferences between Ras and Raf Family Members and the Impact on Oncogenic Ras Signaling

Terrell, E. M., Durrant, D., Ritt, D. A., Sealover, N. E., Sheffels, E., Spencer-Smith, R., Esposito, D., Zhou, Y., Hancock, J. F., Kortum, R. L., et al. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.09.004 · Cited by 110

Therapeutic targeting of RAS: New hope for drugging the “undruggable”

Khan, I., Rhett, J. M., & O’Bryan, J. P. (2019) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2019.118570 · Cited by 111

Widespread Selection for Oncogenic Mutant Allele Imbalance in Cancer

Bielski, C. M., Donoghue, M. T. A., Gadiya, M. M., Hanrahan, A. J., Won, H. H., Chang, M. T., Jonsson, P., Penson, A. V., Gorelick, A. N., Harris, C., et al. (2018) · Cancer Cell · doi:10.1016/j.ccell.2018.10.003 · Cited by 108

Clinicogenomic landscape of pancreatic adenocarcinoma identifies KRAS mutant dosage as prognostic of overall survival

Varghese, A. M., Perry, M., Chou, J. F., Nandakumar, S., Muldoon, D. M., Erakky, A., Zucker, A., Fong, C. J., Mehine, M. M., Nguyen, B., et al. (2025) · Nature Medicine · doi:10.1038/s41591-024-03362-3 · Cited by 122

The impact of oncogenic RAS on redox balance and implications for cancer development

Lim, J. K. M., & Leprivier, G. (2019) · Cell Death and Disease · doi:10.1038/s41419-019-2192-y · Cited by 106

Efficient targeted oncogenic KRASG12C degradation via first reversible-covalent PROTAC

Yang, F., Wen, Y., Wang, C., Zhou, Y., Zhou, Y., Zhang, Z.-M., Liu, T., & Lu, X. (2022) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2021.114088 · Cited by 109

KRAS-specific inhibition using a DARPin binding to a site in the allosteric lobe

Bery, N., Legg, S., Debreczeni, J., Breed, J., Embrey, K., Stubbs, C., Kolasinska-Zwierz, P., Barrett, N., Marwood, R., Watson, J., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-10419-2 · Cited by 97

Machine learning–driven multiscale modeling reveals lipid-dependent dynamics of RAS signaling proteins

Ingólfsson, H. I., Neale, C., Carpenter, T. S., Shrestha, R., López, C. A., Tran, T. H., Oppelstrup, T., Bhatia, H., Stanton, L. G., Zhang, X., et al. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2113297119 · Cited by 96

Assessment of mutation probabilities of KRAS G12 missense mutants and their long-timescale dynamics by atomistic molecular simulations and Markov state modeling

Pantsar, T., Rissanen, S., Dauch, D., Laitinen, T., Vattulainen, I., & Poso, A. (2018) · PLOS Computational Biology · doi:10.1371/journal.pcbi.1006458 · Cited by 85

RAS variant signalling

Mo, S. P., Coulson, J. M., & Prior, I. A. (2018) · Biochemical Society Transactions · doi:10.1042/bst20180173 · Cited by 85

KIAA1429 promotes tumorigenesis and gefitinib resistance in lung adenocarcinoma by activating the JNK/ MAPK pathway in an m6A-dependent manner

Lin, X., Ye, R., Li, Z., Zhang, B., Huang, Y., Du, J., Wang, B., Meng, H., Xian, H., Zhang, X., et al. (2022) · Drug Resistance Updates · doi:10.1016/j.drup.2022.100908 · Cited by 84

KRAS G12C Mutations in NSCLC: From Target to Resistance

Addeo, A., Banna, G. L., & Friedlaender, A. (2021) · Cancers · doi:10.3390/cancers13112541 · Cited by 85

ADAM17: An Emerging Therapeutic Target for Lung Cancer

Saad, M. I., Rose‐John, S., & Jenkins, B. J. (2019) · Cancers · doi:10.3390/cancers11091218 · Cited by 81

Two Distinct Structures of Membrane‐Associated Homodimers of GTP‐ and GDP‐Bound KRAS4B Revealed by Paramagnetic Relaxation Enhancement

Lee, K., Fang, Z., Enomoto, M., Gasmi-Seabrook, G. M. C., Zheng, L., Koide, S., Ikura, M., & Marshall, C. B. (2020) · Angewandte Chemie International Edition · doi:10.1002/anie.202001758 · Cited by 78

Extracellular‐signal‐regulated kinase/mitogen‐activated protein kinase signaling as a target for cancer therapy: an updated review

Najafi, M., Ahmadi, A., & Mortezaee, K. (2019) · Cell Biology International · doi:10.1002/cbin.11187 · Cited by 80

Wiskott–Aldrich syndrome protein (WASP) is a tumor suppressor in T cell lymphoma

Menotti, M., Ambrogio, C., Cheong, T.-C., Pighi, C., Mota, I. A., Cassel, S. H., Compagno, M., Wang, Q., Dall’Olio, R., Minero, V. G., et al. (2018) · Nature Medicine · doi:10.1038/s41591-018-0262-9 · Cited by 75

Therapeutics Targeting Mutant KRAS

Thein, K. Z., Biter, A. B., & Hong, D. S. (2020) · Annual Review of Medicine · doi:10.1146/annurev-med-080819-033145 · Cited by 76

Multivalent assembly of KRAS with the RAS-binding and cysteine-rich domains of CRAF on the membrane

Fang, Z., Lee, K., Huo, K.-G., Gasmi-Seabrook, G. M. C., Zheng, L., Moghal, N., Tsao, M., Ikura, M., & Marshall, C. B. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1914076117 · Cited by 74

Current Approaches in NSCLC Targeting K-RAS and EGFR

Aran, V., & Omerović, J. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20225701 · Cited by 74

Precision therapy in RAS mutant colorectal cancer

Dienstmann, R., Connor, K., Byrne, A. T., Fridman, W. H., Lambrechts, D., Sadanandam, A., Trusolino, L., Prehn, J. H. M., Tabernero, J., & Kolch, W. (2020) · Gastroenterology · doi:10.1053/j.gastro.2019.12.051 · Cited by 73

Phosphorylated Rho–GDP directly activates mTORC2 kinase towards AKT through dimerization with Ras–GTP to regulate cell migration

Senoo, H., Kamimura, Y., Kimura, R., Nakajima, A., Sawai, S., Sesaki, H., & Iijima, M. (2019) · Nature Cell Biology · doi:10.1038/s41556-019-0348-8 · Cited by 76

A “Tug of War” Maintains a Dynamic Protein–Membrane Complex: Molecular Dynamics Simulations of C-Raf RBD-CRD Bound to K-Ras4B at an Anionic Membrane

Li, Z., Prakash, P., & Buck, M. (2018) · ACS Central Science · doi:10.1021/acscentsci.7b00593 · Cited by 71

A structural model of a Ras–Raf signalosome

Mysore, V. P., Zhou, Z.-W., Ambrogio, C., Li, L., Kapp, J. N., Lu, C., Wang, Q., Tucker, M. R., Okoro, J. J., Nagy‐Davidescu, G., et al. (2021) · Nature Structural & Molecular Biology · doi:10.1038/s41594-021-00667-6 · Cited by 69

Crystal Structure Reveals the Full Ras–Raf Interface and Advances Mechanistic Understanding of Raf Activation

Cookis, T., & Mattos, C. (2021) · Biomolecules · doi:10.3390/biom11070996 · Cited by 62

DIRAS3 (ARHI) Blocks RAS/MAPK Signaling by Binding Directly to RAS and Disrupting RAS Clusters

Sutton, M. N., Lü, Z., Li, Y.-C., Zhou, Y., Huang, T., Reger, A. S., Hurwitz, A. M., Palzkill, T. G., Logsdon, C. D., Liang, X., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.11.045 · Cited by 68

Assessing Therapeutic Efficacy of MEK Inhibition in a KRASG12C-Driven Mouse Model of Lung Cancer

Li, S., Liu, S., Deng, J., Akbay, E. A., Hai, J., Ambrogio, C., Zhang, L., Zhou, F., Jenkins, R. W., Adeegbe, D. O., et al. (2018) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-17-3438 · Cited by 67

RAS-ON inhibition overcomes clinical resistance to KRAS G12C-OFF covalent blockade

Nokin, M., Mira, A., Patrucco, E., Ricciuti, B., Cousin, S., Soubeyran, I., José, S. S., Peirone, S., Caizzi, L., Michelina, S. V., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-51828-2 · Cited by 70

Direct targeting of oncogenic RAS mutants with a tumor-specific cytosol-penetrating antibody inhibits RAS mutant–driven tumor growth

Shin, S., Kim, J., Park, S.-W., Jun, S.-Y., Kweon, H.-J., Choi, D.-K., Lee, D., Cho, Y. B., & Kim, Y. (2020) · Science Advances · doi:10.1126/sciadv.aay2174 · Cited by 63

K-Ras G-domain binding with signaling lipid phosphatidylinositol (4,5)-phosphate (PIP2): membrane association, protein orientation, and function

Cao, S., Chung, S., Kim, S., Li, Z., Manor, D., & Buck, M. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.004021 · Cited by 63

K-Ras prenylation as a potential anticancer target

Baranyi, M., Buday, L., & Hegedűs, B. (2020) · Cancer and Metastasis Reviews · doi:10.1007/s10555-020-09902-w · Cited by 62

The membrane surface as a platform that organizes cellular and biochemical processes

Leonard, T. A., Loose, M., & Martens, S. (2023) · Developmental Cell · doi:10.1016/j.devcel.2023.06.001 · Cited by 64

ERK1/2: An Integrator of Signals That Alters Cardiac Homeostasis and Growth

Gilbert, C. J., Longenecker, J. Z., & Accornero, F. (2021) · Biology · doi:10.3390/biology10040346 · Cited by 65

ProtCID: a data resource for structural information on protein interactions

Xu, Q., & Dunbrack, R. L. (2020) · Nature Communications · doi:10.1038/s41467-020-14301-4 · Cited by 61

Uncovering a membrane-distal conformation of KRAS available to recruit RAF to the plasma membrane

Van, Q. N., López, C. A., Tonelli, M., Taylor, T. E., Niu, B., Stanley, C. B., Bhowmik, D., Tran, T. H., Frank, P. H., Messing, S. A. J., et al. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2006504117 · Cited by 58

KRASQ61H Preferentially Signals through MAPK in a RAF Dimer-Dependent Manner in Non–Small Cell Lung Cancer

Zhou, Z.-W., Ambrogio, C., Bera, A. K., Li, Q., Li, X.-X., Li, L., Son, J., Gondi, S., Li, J., Campbell, E., et al. (2020) · Cancer Research · doi:10.1158/0008-5472.can-20-0448 · Cited by 60

The Ins and Outs of RAS Effector Complexes

Kiel, C., Matallanas, D., & Kölch, W. (2021) · Biomolecules · doi:10.3390/biom11020236 · Cited by 59

The RAS-ERK pathway: A route for couples

Santos, E., & Crespo, P. (2018) · Science Signaling · doi:10.1126/scisignal.aav0917 · Cited by 57

Impact of RAS mutation subtype on clinical outcome—a cross-entity comparison of patients with advanced non-small cell lung cancer and colorectal cancer

Wiesweg, M., Kasper, S., Worm, K., Herold, T., Reis, H., Sara, L., Metzenmacher, M., Abendroth, A., Darwiche, K., Aigner, C., et al. (2018) · Oncogene · doi:10.1038/s41388-018-0634-0 · Cited by 55

Raf promotes dimerization of the Ras G-domain with increased allosteric connections

Packer, M. R., Parker, J. A., Chung, J. K., Li, Z., Lee, Y. K., Cookis, T., Guterres, H., Alvarez, S. A., Hossain, M. A., Donnelly, D. P., et al. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2015648118 · Cited by 55

Cancer immune evasion through KRAS and PD-L1 and potential therapeutic interventions

Watterson, A., & Coelho, M. A. (2023) · Cell Communication and Signaling · doi:10.1186/s12964-023-01063-x · Cited by 61

Consensus on the RAS dimerization hypothesis: Strong evidence for lipid-mediated clustering but not for G-domain-mediated interactions

Simanshu, D. K., Philips, M. R., & Hancock, J. F. (2023) · Molecular Cell · doi:10.1016/j.molcel.2023.03.008 · Cited by 54

High-throughput, single-particle tracking reveals nested membrane domains that dictate KRasG12D diffusion and trafficking

Lee, Y., Phelps, C. E., Huang, T., Mostofian, B., Wu, L., Zhang, Y., Tao, K. X., Chang, Y. H., Stork, P. A., Gray, J. W., et al. (2019) · eLife · doi:10.7554/elife.46393 · Cited by 56

Targeting the α4–α5 dimerization interface of K-RAS inhibits tumor formation in vivo

Khan, I., Spencer-Smith, R., & O’Bryan, J. P. (2019) · Oncogene · doi:10.1038/s41388-018-0636-y · Cited by 54

40 Years of RAS—A Historic Overview

Fernández‐Medarde, A., Rivas, J. D. L., & Santos, E. (2021) · Genes · doi:10.3390/genes12050681 · Cited by 57

MEK1/2 inhibitor withdrawal reverses acquired resistance driven by BRAFV600E amplification whereas KRASG13D amplification promotes EMT-chemoresistance

Sale, M. J., Balmanno, K., Saxena, J., Ozono, E., Wojdyła, K., McIntyre, R. E., Gilley, R., Woroniuk, A., Howarth, K., Hughes, G. D., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-09438-w · Cited by 53

DIRAS3: An Imprinted Tumor Suppressor Gene that Regulates RAS and PI3K-driven Cancer Growth, Motility, Autophagy, and Tumor Dormancy

Bildik, G., Liang, X., Sutton, M. N., Bast, R. C., & Lü, Z. (2021) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-21-0331 · Cited by 55

Mechanisms of Ras Membrane Organization and Signaling: Ras Rocks Again

Abankwa, D., & Gorfe, A. A. (2020) · Biomolecules · doi:10.3390/biom10111522 · Cited by 46

Targeting KRAS mutant lung cancer: light at the end of the tunnel

Drosten, M., & Barbacid, M. (2021) · Molecular Oncology · doi:10.1002/1878-0261.13168 · Cited by 49

Oligomeric organization of membrane proteins from native membranes at nanoscale spatial and single-molecule resolution

Walker, G., Brown, C., Ge, X., Kumar, S., Muzumdar, M. D., Gupta, K., & Bhattacharyya, M. (2023) · Nature Nanotechnology · doi:10.1038/s41565-023-01547-4 · Cited by 46

Therapeutic gene regulation using pyrrole–imidazole polyamides

Yu, Z., Pandian, G. N., Hidaka, T., & Sugiyama, H. (2019) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2019.02.001 · Cited by 46

Pancreatic cancer: molecular pathogenesis and emerging therapeutic strategies

Rozengurt, E., & Eibl, G. (2026) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-025-02499-y · Cited by 49

KRAS inhibition in non–small cell lung cancer: Past failures, new findings and upcoming challenges

Passiglia, F., Malapelle, U., Re, M. D., Righi, L., Pagni, F., Furlan, D., Danesi, R., Troncone, G., & Novello, S. (2020) · European Journal of Cancer · doi:10.1016/j.ejca.2020.06.023 · Cited by 43

The role of wild-type RAS in oncogenic RAS transformation

Sheffels, E., & Kortum, R. L. (2021) · Genes · doi:10.3390/genes12050662 · Cited by 42

Comparative Analysis and Isoform-Specific Therapeutic Vulnerabilities of KRAS Mutations in Non–Small Cell Lung Cancer

Ricciuti, B., Son, J., Okoro, J. J., Mira, A., Patrucco, E., Eum, Y., Wang, X., Paranal, R., Wang, H., Lin, M., et al. (2022) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-21-2719 · Cited by 42

Not all RAS mutations are equal: A detailed review of the functional diversity of RAS hot spot mutations

Burge, R. A., & Hobbs, G. A. (2022) · Advances in cancer research · doi:10.1016/bs.acr.2021.07.004 · Cited by 44

Conformational resolution of nucleotide cycling and effector interactions for multiple small GTPases determined in parallel

Killoran, R. C., & Smith, M. J. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.008653 · Cited by 41

Oncogenic KRAS G12D mutation promotes dimerization through a second, phosphatidylserine–dependent interface: a model for KRAS oligomerization

Lee, K.-Y., Enomoto, M., Gebregiworgis, T., Gasmi-Seabrook, G. M. C., Ikura, M., & Marshall, C. B. (2021) · Chemical Science · doi:10.1039/d1sc03484g · Cited by 41

BRAF inhibitors promote intermediate BRAF(V600E) conformations and binary interactions with activated RAS

Röck, R., Mayrhofer, J. E., Torres‐Quesada, O., Enzler, F., Raffeiner, A., Raffeiner, P., Feichtner, A., Huber, R. G., Koide, S., Taylor, S. S., et al. (2019) · Science Advances · doi:10.1126/sciadv.aav8463 · Cited by 37

Current smartphone-assisted point-of-care cancer detection: Towards supporting personalized cancer monitoring

Le, L. T. P., Nguyen, A. H. Q., Tu, L. M. T. P. P. L. M., Ngo, H. T. T., Wang, X., Cunningham, B. T., Valera, E., Bashir, R., Taylor-Robinson, A. W., & Do, C. (2024) · TrAC Trends in Analytical Chemistry · doi:10.1016/j.trac.2024.117681 · Cited by 39

KRAS: A Promising Therapeutic Target for Cancer Treatment

Wu, H.-Z., Xiao, J., Xiao, S., & Cheng, Y. (2019) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026619666190905164144 · Cited by 41

Allostery in membrane proteins

Cournia, Z., & Chatzigoulas, A. (2020) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2020.03.006 · Cited by 42

Approaches to inhibiting oncogenic K-Ras

Gorfe, A. A., & Cho, K. (2019) · Small GTPases · doi:10.1080/21541248.2019.1655883 · Cited by 36

Oncogenic context shapes the fitness landscape of tumor suppression

Blair, L. M., Juan, J. M., Sebastian, L., Tran, V. B., Nie, W., Wall, G. D., Gerceker, M., Lai, I. K., Apilado, E. A., Grenot, G., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-42156-y · Cited by 36

TAK1 Phosphorylates RASSF9 and Inhibits Esophageal Squamous Tumor Cell Proliferation by Targeting the RAS/MEK/ERK Axis

Shi, H. M., Ju, Q., Mao, Y., Wang, Y., Ding, J., Liu, X., Tang, X., & Sun, C. (2021) · Advanced Science · doi:10.1002/advs.202001575 · Cited by 35

Targeting KRAS in PDAC: A New Way to Cure It?

He, Q., Liu, Z., & Wang, J. (2022) · Cancers · doi:10.3390/cancers14204982 · Cited by 39

Multiplexed screens identify RAS paralogues HRAS and NRAS as suppressors of KRAS-driven lung cancer growth

Tang, R., Shuldiner, E. G., Kelly, M. R., Murray, C. W., Hebert, J. D., Andrejka, L., Tsai, M. K., Hughes, N. W., Parker, M. I., Cai, H., et al. (2023) · Nature Cell Biology · doi:10.1038/s41556-022-01049-w · Cited by 38

Inhibition of ADAM9 promotes the selective degradation of KRAS and sensitizes pancreatic cancers to chemotherapy

Huang, Y., Cheng, W., Kuo, T.-T., Yang, J., Wu, Y., Wu, H., Lo, C.-C., Hsieh, C.-Y., Wong, S., Lu, C., et al. (2024) · Nature Cancer · doi:10.1038/s43018-023-00720-x · Cited by 34

RAS Nanoclusters: Dynamic Signaling Platforms Amenable to Therapeutic Intervention

Van, Q. N., Prakash, P., Shrestha, R., Balius, T. E., Turbyville, T. J., & Stephen, A. G. (2021) · Biomolecules · doi:10.3390/biom11030377 · Cited by 34

KARATE: PKA-induced KRAS4B-RHOA-mTORC2 supercomplex phosphorylates AKT in insulin signaling and glucose homeostasis

Senoo, H., Murata, D., Wai, M., Arai, K., Iwata, W., Sesaki, H., & Iijima, M. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.09.001 · Cited by 34

Anchorage-independent growth conditions reveal a differential SOS2 dependence for transformation and survival in RAS-mutant cancer cells

Sheffels, E., Sealover, N. E., Theard, P. L., & Kortum, R. L. (2019) · Small GTPases · doi:10.1080/21541248.2019.1611168 · Cited by 31

Natural product manoalide promotes EGFR-TKI sensitivity of lung cancer cells by KRAS-ERK pathway and mitochondrial Ca2+ overload-induced ferroptosis

Ni, Y., Liu, J., Zeng, L., Yang, Y., Liu, L., Yao, M., Chai, L., Zhang, L., Li, Y., Zhang, L., et al. (2023) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.1109822 · Cited by 32

Investigation of GTP-dependent dimerization of G12X K-Ras variants using ultraviolet photodissociation mass spectrometry

Mehaffey, M. R., Schardon, C. L., Novelli, E. T., Cammarata, M. B., Webb, L. J., Fast, W. L., & Brodbelt, J. S. (2019) · Chemical Science · doi:10.1039/c9sc01032g · Cited by 31

An integrative pharmacogenomics analysis identifies therapeutic targets in KRAS-mutant lung cancer

Wang, H., Lv, Q., Xu, Y., Cai, Z., Zheng, J., Cheng, X., Dai, Y., Janne, P. A., Ambrogio, C., & Köhler, J. (2019) · EBioMedicine · doi:10.1016/j.ebiom.2019.10.012 · Cited by 32

RAS Function in cancer cells: translating membrane biology and biochemistry into new therapeutics

Kattan, W. E., & Hancock, J. F. (2020) · Biochemical Journal · doi:10.1042/bcj20190839 · Cited by 33

Signaling pathways downstream to receptor tyrosine kinases: targets for cancer treatment

Cordover, E., & Minden, A. (2020) · Journal of Cancer Metastasis and Treatment · doi:10.20517/2394-4722.2020.101 · Cited by 31

Crosstalk between KRAS, SRC and YAP Signaling in Pancreatic Cancer: Interactions Leading to Aggressive Disease and Drug Resistance

Rozengurt, E., & Eibl, G. (2021) · Cancers · doi:10.3390/cancers13205126 · Cited by 31

Biology, pathology, and therapeutic targeting of RAS

Rhett, J. M., Khan, I., & O’Bryan, J. P. (2020) · Advances in cancer research · doi:10.1016/bs.acr.2020.05.002 · Cited by 29

Limited survival and impaired hepatic fasting metabolism in mice with constitutive Rag GTPase signaling

Arregui, C. D. L. C., Plata-Gómez, A. B., Deleyto-Seldas, N., García, F., Ortega-Molina, A., Abril-Garrido, J., Rodriguez, E., Nemazanyy, I., Tribouillard, L., Martino, A. D., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-23857-8 · Cited by 31

Loss of the wild-type KRAS allele promotes pancreatic cancer progression through functional activation of YAP1

Han, Y., Yu, C.-C., Fine, S. A., Youssof, A. L., Yang, Y., Yan, J., Karg, D. C., Cheung, E. C., Friedman, R. A., Ying, H., et al. (2021) · Oncogene · doi:10.1038/s41388-021-02040-9 · Cited by 28

Down-regulated m6A reader FTO destabilizes PHF1 that triggers enhanced stemness capacity and tumor progression in lung adenocarcinoma

Ning, J., Wang, F., Bu, J., Zhu, K., & Liu, W. (2022) · Cell Death Discovery · doi:10.1038/s41420-022-01125-y · Cited by 28

Small GTPase peripheral binding to membranes: molecular determinants and supramolecular organization

Peurois, F., Peyroche, G., & Cherfils, J. (2018) · Biochemical Society Transactions · doi:10.1042/bst20170525 · Cited by 27

The Ras dimer structure

Rudack, T., Teuber, C., Scherlo, M., Güldenhaupt, J., Schartner, J., Lübben, M., Klare, J. P., Gerwert, K. B., & Kötting, C. (2021) · Chemical Science · doi:10.1039/d1sc00957e · Cited by 27

Exploring CRD mobility during RAS/RAF engagement at the membrane

Nguyen, K., López, C. A., Neale, C., Van, Q. N., Carpenter, T. S., Natale, F. D., Travers, T. S., Tran, T. H., Chan, A. H., Bhatia, H., et al. (2022) · Biophysical Journal · doi:10.1016/j.bpj.2022.06.035 · Cited by 25

P3.02-066 Wild-Type KRAS Mediates Growth Inhibition and Resistance to MEK Inhibitors through Dimerization with Mutant KRAS in Lung Adenocarcinoma

Ambrogio, C., Köhler, J., Zhou, Z., Wang, H., Paranal, R. M., Capelletti, M., Caffarra, C., Li, S., Lv, Q., Gondi, S. R., et al. (2017) · Journal of Thoracic Oncology · doi:10.1016/j.jtho.2017.09.1595 · Cited by 1

Wild-type KRAS mediates growth inhibition and resistance to MEK inhibitors through dimerization with mutant KRAS in lung adenocarcinoma

Ambrogio, C., Köhler, J., Zhou, Z., Wang, H., Paranal, R. M., Capelletti, M., Caffarra, C., Li, S., Lv, Q., Santamarı́a, D., et al. (2017) · Annals of Oncology · doi:10.1093/annonc/mdx361 · Cited by 3

IA02 Insights into KRAS Biology to Identify Potential Therapeutic Strategies

Ambrogio, C. (2020) · Journal of Thoracic Oncology · doi:10.1016/j.jtho.2019.12.003 · Cited by 1

Abstract IA05: Dimerization is critical for the functions of wild-type and mutant KRAS

Ambrogio, C. (2020) · Molecular Cancer Research · doi:10.1158/1557-3125.ras18-ia05

Dimerization Is Critical for the Functions of Wild-type and Mutant KRAS

(2018) · Cancer Discovery · doi:10.1158/2159-8290.cd-rw2018-013 · Cited by 1