Dragging Ras Back in the Ring

Hallmarks of Cancer: The Next Generation

Hanahan, D., & Weinberg, R. A. (2011) · Cell · doi:10.1016/j.cell.2011.02.013 · Cited by 66,590

ras GENES

Barbacid, M. (1987) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.56.070187.004023 · Cited by 3,885

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

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Evidence of RNAi in humans from systemically administered siRNA via targeted nanoparticles

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A Comprehensive Survey of Ras Mutations in Cancer

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Oncogenic Kras maintains pancreatic tumors through regulation of anabolic glucose metabolism

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GEFs and GAPs: Critical Elements in the Control of Small G Proteins

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Ras oncogenes: split personalities

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A Cytoplasmic Protein Stimulates Normal N- ras p21 GTPase, But Does Not Affect Oncogenic Mutants

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Phase II Study of Sorafenib in Patients With Advanced Hepatocellular Carcinoma

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RASAL1 Attenuates Gastric Carcinogenesis in Nude Mice by Blocking RAS/ERK Signaling

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Novel virtual lead identification in the discovery of hematopoietic cell kinase (HCK) inhibitors: application of 3D QSAR and molecular dynamics simulation

Bavi, R., Kumar, R., Rampogu, S. D., Kim, Y., Kwon, Y. J., Park, S. J., & Lee, K. W. (2016) · Journal of Receptors and Signal Transduction · doi:10.1080/10799893.2016.1212376 · Cited by 13

Identification of lysine methylation in the core GTPase domain by GoMADScan

Yoshino, H., Yin, G., Kawaguchi, R. K., Popov, K. I., Temple, B. R. S., Sasaki, M., Kofuji, S., Wolfe, K., Kofuji, K., Okumura, K., et al. (2019) · PLoS ONE · doi:10.1371/journal.pone.0219436 · Cited by 13

Proximal Protein Interaction Landscape of RAS Paralogs

Béganton, B., Coyaud, É., Laurent, E. M. N., Mangé, A., Jacquemetton, J., Romancer, M. L., Raught, B., & Solassol, J. (2020) · Cancers · doi:10.3390/cancers12113326 · Cited by 13

Emerging targets in sarcoma: Rising to the challenge of RAS signaling in undifferentiated pleomorphic sarcoma

Dodd, R. D. (2015) · Cancer · doi:10.1002/cncr.29730 · Cited by 13

Inhibition mechanism of MRTX1133 on KRASG12D: a molecular dynamics simulation and Markov state model study

Liang, F., Kang, Z., Sun, X., Chen, J., Duan, X., He, H., & Cheng, J. (2023) · Journal of Computer-Aided Molecular Design · doi:10.1007/s10822-023-00498-1 · Cited by 12

High sensitivity isoelectric focusing to establish a signaling biomarker for the diagnosis of human colorectal cancer

Padhan, N., Nordling, T. E. M., Sundström, M., Åkerud, P., Birgisson, H., Nygren, P., Nelander, S., & Claesson, L. (2016) · BMC Cancer · doi:10.1186/s12885-016-2725-z · Cited by 12

IQGAP1 Maintains Pancreatic Ductal Adenocarcinoma Clonogenic Growth and Metastasis

Li, J. H., McMillan, R. H., Begum, A., Gocke, C. B., & Matsui, W. H. (2018) · Pancreas · doi:10.1097/mpa.0000000000001198 · Cited by 12

A multitargeted probe-based strategy to identify signaling vulnerabilities in cancers

Rao, S., Du, G., Hafner, M. A., Subramanian, K., Sorger, P. K., & Gray, N. S. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.006805 · Cited by 12

Effects of NRAS Mutations on Leukemogenesis and Targeting of Children With Acute Lymphoblastic Leukemia

Qian, J., Li, Z., Pei, K., Li, Z., Li, C., Yan, M., Qian, M., Song, Y., Zhang, H., & He, Y. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.712484 · Cited by 14

New lead compounds identification against KRas mediated cancers through pharmacophore-based virtual screening and in vitro assays

Ghufran, M., Rehman, A. U., Ayaz, M., Ul‐Haq, Z., Uddin, R., Azam, S. S., & Wadood, A. (2022) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2022.2128878 · Cited by 12

Defining bone fide effectors of RAS GTPases

Smith, M. J. (2023) · BioEssays · doi:10.1002/bies.202300088 · Cited by 11

Clinicopathological and prognostic significance of Ras association and pleckstrin homology domains 1 (RAPH1) in breast cancer

Kurozumi, S., Joseph, C., Sonbul, S. N., Aleskandarany, M. A., Pigera, M., Alsaleem, M. A., Alsaeed, S. A., Kariri, Y. A., Nolan, C. C., Diez, M., et al. (2018) · Breast Cancer Research and Treatment · doi:10.1007/s10549-018-4891-y · Cited by 12

Modeling and subtleties of K-Ras and Calmodulin interaction

Garrido, E., Lázaro, J., Jaumot, M., Agell, N., & Rubio, J. (2018) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1006552 · Cited by 12

Ras functional proximity proteomics establishes mTORC2 as new direct ras effector

Kovalski, J. R., Shanderson, R. L., & Khavari, P. A. (2019) · Oncotarget · doi:10.18632/oncotarget.27025 · Cited by 13

KRAS phosphorylation regulates cell polarization and tumorigenic properties in colorectal cancer

Cabot, D., Brun, S., Paco, N., Morell, M., Gendrau‐Sanclemente, N., Abuasaker, B., Ruiz-Fariña, T., Barceló, C., Cuatrecasas, M., Bosch, M., et al. (2021) · Oncogene · doi:10.1038/s41388-021-01967-3 · Cited by 12

MDM2 induces EMT via the B‑Raf signaling pathway through 14‑3‑3

Ou, M., Xu, X., Chen, Y., Li, L., Zhang, L., Liao, Y., Sun, W., Quach, C., Feng, J., & Tang, L. (2021) · Oncology Reports · doi:10.3892/or.2021.8071 · Cited by 11

Akt-mediated Ephexin1–Ras interaction promotes oncogenic Ras signaling and colorectal and lung cancer cell proliferation

Kim, J., Jeon, Y. J., Lim, S., Ryu, J., Lee, J.-H., Chang, I. Y., & You, H. J. (2021) · Cell Death and Disease · doi:10.1038/s41419-021-04332-0 · Cited by 11

A First-Class Degrader Candidate Targeting Both KRAS G12D and G12V Mediated by CANDDY Technology Independent of Ubiquitination

Miyamoto‐Sato, E., Imanishi, S., Huang, L., Itakura, S., Iwasaki, Y., & Ishizaka, M. (2023) · Molecules · doi:10.3390/molecules28145600 · Cited by 13

Transgenic mouse model expressing P53R172H, luciferase, EGFP and KRASG12D in a single open reading frame for live imaging of tumor

Ju, H.-L., Calvisi, D. F., Moon, H., Baek, S., Ribback, S., Dombrowski, F., Cho, K. J., Chung, S. I., Han, K., & Ro, S. W. (2015) · Scientific Reports · doi:10.1038/srep08053 · Cited by 11

Ras oncogene-independent activation of RALB signaling is a targetable mechanism of escape from NRAS(V12) oncogene addiction in acute myeloid leukemia

Pomeroy, E. J., Lee, L. A., Lee, R. D. W., Schirm, D. K., Temiz, N. A., Ma, J., Gruber, T. A., Díaz-Flores, E., Moriarity, B. S., Downing, J. R., et al. (2016) · Oncogene · doi:10.1038/onc.2016.471 · Cited by 11

IKKβ targeting reduces KRAS-induced lung cancer angiogenesis in vitro and in vivo: A potential anti-angiogenic therapeutic target

Carneiro-Lobo, T., Scalabrini, L. C., Magalhães, L. D. S., Cardeal, L. B. D. S., Rodrigues, F. S., dos Santos, E. O., Baldwin, A. S., Levantini, E., Giordano, R. J., & Bassères, D. S. D. S. (2019) · Lung Cancer · doi:10.1016/j.lungcan.2019.02.027 · Cited by 11

Ras inhibition by zoledronic acid effectively sensitizes cervical cancer to chemotherapy

Xu, J., Pan, Q., & Ju, W. (2019) · Anti-Cancer Drugs · doi:10.1097/cad.0000000000000779 · Cited by 11

Expression and clinical significance of FOS-like antigen 1 in gastric adenocarcinoma

Zhu, X., Liu, H., Zhen-xing, X., & Zhang, Y. (2019) · Pathology - Research and Practice · doi:10.1016/j.prp.2019.03.022 · Cited by 11

Production of Farnesylated and Methylated Proteins in an Engineered Insect Cell System

Gillette, W., Frank, P. H., Perkins, S. C., Drew, M. R., Grose, C., & Esposito, D. (2019) · Methods in molecular biology · doi:10.1007/978-1-4939-9532-5_20 · Cited by 11

Targeting a Novel KRAS Binding Site: Application of One-Component Stapling of Small (5–6-mer) Peptides

Fumagalli, G., Carbajo, R. J., Nissink, J. W. M., Tart, J., Dou, R., Thomas, A. P., & Spring, D. R. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c01334 · Cited by 12

Recapitulation of cell-like KRAS4b membrane dynamics on complex biomimetic membranes

Shrestha, R., Chen, D., Frank, P. H., Nissley, D. V., & Turbyville, T. J. (2021) · iScience · doi:10.1016/j.isci.2021.103608 · Cited by 11

Med23 deficiency reprograms the tumor microenvironment to promote lung tumorigenesis

Fu, X., Liu, S., Cao, D., Li, C., Ji, H., & Wang, G. (2024) · British Journal of Cancer · doi:10.1038/s41416-023-02556-9 · Cited by 11

Gluing GAP to RAS Mutants: A New Approach to an Old Problem in Cancer Drug Development

Ranđelović, I., Nyíri, K., Koppány, G., Baranyi, M., Tóvári, J., Kigyós, A., Tímár, J., Vértessy, B. G., & Grolmusz, V. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25052572 · Cited by 10

Enrichment technique to allow early detection and monitor emergence of KRAS mutation in response to treatment

Kitagawa, Y., Okumura, K., Watanabe, T., Tsukamoto, K., Kitano, S., Nankinzan, R., Suzuki, T., Hara, T., Soda, H., Denda, T., et al. (2019) · Scientific Reports · doi:10.1038/s41598-019-47700-9 · Cited by 10

How to make an undruggable enzyme druggable: lessons from ras proteins

Sayyed–Ahmad, A., & Gorfe, A. A. (2020) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2020.05.003 · Cited by 11

Mega-High-Throughput Screening Platform for the Discovery of Biologically Relevant Sequence-Defined Non-Natural Polymers

Avital‐Shmilovici, M., Liu, X., Shaler, T. A., Lowenthal, A. C., Bourbon, P., Snider, J., Tambo-ong, A., Repellin, C. E., Yniguez, K., Sambucetti, L. C., et al. (2022) · ACS Central Science · doi:10.1021/acscentsci.1c01041 · Cited by 11

Isoprenylcysteine carboxyl methyltransferase is critical for glioblastoma growth and survival by activating Ras/Raf/Mek/Erk

Wan, W., Xiao, W., Pan, W., Chen, L., Liu, Z., & Xu, J. (2022) · Cancer Chemotherapy and Pharmacology · doi:10.1007/s00280-022-04401-x · Cited by 10

Non-coding RNAs in leukemia drug resistance: new perspectives on molecular mechanisms and signaling pathways

Rahmati, A., Mafi, A., Vakili, O., Soleymani, F., Alishahi, Z., Yahyazadeh, S., Gholinezhad, Y., Rezaee, M., Johnston, T. P., & Sahebkar, A. (2023) · Annals of Hematology · doi:10.1007/s00277-023-05383-3 · Cited by 10

Pharmacological treats for SUMO addicts

Licciardello, M. P., & Kubicek, S. (2016) · Pharmacological Research · doi:10.1016/j.phrs.2016.01.004 · Cited by 12

STK38L kinase ablation promotes loss of cell viability in a subset of KRAS-dependent pancreatic cancer cell lines

Grant, T. J., Mehta, A. K., Gupta, A., Sharif, A. A. D., Arora, K. S., Deshpande, V., Ting, D. T., Bardeesy, N. M., Ganem, N. J., Hergovich, A., et al. (2017) · Oncotarget · doi:10.18632/oncotarget.20833 · Cited by 10

Drug Combinatorial Therapies for the Treatment of KRAS Mutated Lung Cancers

He, H., Xu, C., Cheng, Z., Qian, X., & Zheng, L. (2019) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026619666190902150555 · Cited by 10

Dynamic density functional theory of multicomponent cellular membranes

Stanton, L. G., Oppelstrup, T., Carpenter, T. S., Ingólfsson, H. I., Surh, M. P., Lightstone, F. C., & Glosli, J. N. (2023) · Physical Review Research · doi:10.1103/physrevresearch.5.013080 · Cited by 12

Characterisation of HRas local signal transduction networks using engineered site-specific exchange factors

Herrero, A., Reis-Cardoso, M., Jiménez-Gómez, I., Doherty, C., Agudo‐Ibáñez, L., Pinto-Fernández, A., Calvo, F., Kölch, W., Crespo, P., & Matallanas, D. (2017) · Small GTPases · doi:10.1080/21541248.2017.1406434 · Cited by 10

ST2 gene products critically contribute to cellular transformation caused by an oncogenic Ras mutant

Tago, K., Ohta, S., Kashiwada, M., Funakoshi‐Tago, M., Matsugi, J., Tominaga, S., & Yanagisawa, K. (2017) · Heliyon · doi:10.1016/j.heliyon.2017.e00436 · Cited by 10

How often is each gene mutated within the cancer patient population?

Mendiratta, G., Jones, M. K., & Stites, E. C. (2022) · Molecular & Cellular Oncology · doi:10.1080/23723556.2022.2065176 · Cited by 10

Identification of Ras-degrading small molecules that inhibit the transformation of colorectal cancer cells independent of β-catenin signaling

Shin, W., Lee, S.-K., Hwang, J.-H., Park, J.-C., Cho, Y.-H., Ro, E. J., Song, Y., Seo, H. R., & Choi, K.-Y. (2018) · Experimental & Molecular Medicine · doi:10.1038/s12276-018-0102-5 · Cited by 10

Triple Blockade of Oncogenic RAS Signaling Using KRAS and MEK Inhibitors in Combination with Irradiation in Pancreatic Cancer

Wang, X., Breuer, J., Garbe, S., Giordano, F. A., Brossart, P., Feldmann, G., & Bisht, S. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25116249 · Cited by 10

Direkte Modulation von Aktivität und Funktion kleiner GTPasen

Cromm, P. M., Spiegel, J., Grossmann, T. N., & Waldmann, H. (2015) · Angewandte Chemie · doi:10.1002/ange.201504357 · Cited by 9

Monoubiquitination of KRAS at Lysine104 and Lysine147 Modulates Its Dynamics and Interaction with Partner Proteins

Nair, V. V., Yin, G., Zhang, J., Hancock, J. F., Campbell, S. L., & Gorfe, A. A. (2021) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.1c01062 · Cited by 9

Membrane-bound KRAS approximates an entropic ensemble of configurations

Heinrich, F., Van, Q. N., Jean-Francois, F. L., Stephen, A. G., & Lösche, M. (2021) · Biophysical Journal · doi:10.1016/j.bpj.2021.08.008 · Cited by 9

A PDE6δ‐KRas Inhibitor Chemotype with up to Seven H‐Bonds and Picomolar Affinity that Prevents Efficient Inhibitor Release by Arl2

Martín‐Gago, P., Fansa, E. K., Klein, C. H., Murarka, S., Janning, P., Schürmann, M., Metz, M., Ismail, S., Schultz‐Fademrecht, C., Baumann, M., et al. (2017) · Angewandte Chemie · doi:10.1002/ange.201610957 · Cited by 8

The value of genomics in dissecting the RAS-network and in guiding therapeutics for RAS-driven cancers

Shrestha, G., MacNeil, S. M., McQuerry, J. A., Jenkins, D. F., Sharma, S., & Bild, A. H. (2016) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2016.06.012 · Cited by 10

RALB provides critical survival signals downstream of Ras in acute myeloid leukemia

Eckfeldt, C. E., Pomeroy, E. J., Lee, R. D., Hazen, K. S., Lee, L. A., Moriarity, B. S., & Largaespada, D. A. (2016) · Oncotarget · doi:10.18632/oncotarget.11431 · Cited by 9

A peptide-based synthetic transcription factor selectively down-regulates the proto-oncogene CFOS in tumour cells and inhibits proliferation

Chakraborty, M., & Roy, S. (2016) · Chemical Communications · doi:10.1039/c6cc08086c · Cited by 9

“Examining RAS pathway rewiring with a chemically inducible activator of RAS”

Rose, J. C., Dieter, E. M., Cunningham‐Bryant, D., & Maly, D. J. (2018) · Small GTPases · doi:10.1080/21541248.2018.1446697 · Cited by 8

Let K-Ras activate its own inhibitor

Statsyuk, A. V. (2018) · Nature Structural & Molecular Biology · doi:10.1038/s41594-018-0066-0 · Cited by 9

Multiple mechanisms involved in a low concentration of FL118 enhancement of AMR-MeOAc to induce pancreatic cancer cell apoptosis and growth inhibition.

Rabi, T., & Li, F. (2018) · Europe PMC (PubMed Central) · Cited by 9

KRAS codon 12 and 13 mutations may guide the selection of irinotecan or oxaliplatin in first-line treatment of metastatic colorectal cancer

Ergün, Y., Açıkgöz, Y., Bal, Ö., Uçar, G., Dirikoç, M., Yıldırım, E. Ç., Akdeniz, N., & Uncu, D. (2019) · Expert Review of Molecular Diagnostics · doi:10.1080/14737159.2019.1693266 · Cited by 9

K-ras peptide mimotope induces a humoral immune response against G12V K-ras antigen in BALB/c mice

Hoo, W. P. Y., Siak, P. Y., Alias, N. A. R., Wong, J. J., Tan, E. W., Song, A. A., Rahim, R. A., & In, L. L. A. (2020) · Asia-Pacific Journal of Molecular Biology and Biotechnology · doi:10.35118/apjmbb.2020.028.3.03 · Cited by 9

A Gene Expression High-Throughput Screen (GE-HTS) for Coordinated Detection of Functionally Similar Effectors in Cancer

Rao, C., Huisman, D. H., Vieira, H. M., Frodyma, D. E., Neilsen, B. K., Chakraborty, B., Hight, S. K., White, M. A., Fisher, K. W., & Lewis, R. E. (2020) · Cancers · doi:10.3390/cancers12113143 · Cited by 8

HPLC Method to Resolve, Identify and Quantify Guanine Nucleotides Bound to the GTPase Ras

Hannan, J. P., Swisher, G. H., Martyr, J. G., Cordaro, N. J., Erbse, A. H., & Falke, J. J. (2021) · Analytical Biochemistry · doi:10.1016/j.ab.2021.114338 · Cited by 8

Differences in sensitivity to EGFR inhibitors could be explained by described biochemical differences between oncogenic Ras mutantsPreprint

Stites, E. C. (2014) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/005397 · Cited by 10

KRAS protein expression becomes progressively restricted during embryogenesis and in adulthood

Minati, M.-A., Assi, M., Libert, M., Cordi, S., Lemaigre, F. P., & Jacquemin, P. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.995013 · Cited by 8

Differential functions of the KRAS splice variants

Rossi, J. A. K., Nuevo‐Tapioles, C., & Philips, M. R. (2023) · Biochemical Society Transactions · doi:10.1042/bst20221347 · Cited by 8

Revolutionizing Senescence Detection: Advancements from Traditional Methods to Cutting-Edge Techniques

Xiao, R., Hu, S., Du, X., Wang, Y., Fang, K., Zhu, Y., Lou, N., Yuan, C., & Yang, J. (2024) · Aging and Disease · doi:10.14336/ad.202.0565 · Cited by 8

From bench to bedside: murine models of inherited and sporadic brain arteriovenous malformations

Ricciardelli, A., Genet, G., Genet, N., McClugage, S. T., Kan, P., Hirschi, K. K., Fish, J. E., & Wythe, J. D. (2025) · Angiogenesis · doi:10.1007/s10456-024-09953-5 · Cited by 8

Antitumor activity of sorafenib plus CDK4/6 inhibitor in pancreatic patient derived cell with KRAS mutation

Lee, T., Kim, K., Lee, J., Park, S. H., Park, Y. S., Lim, H. Y., Kang, W. K., Park, J. O., & Kim, S. T. (2018) · Journal of Cancer · doi:10.7150/jca.26068 · Cited by 8

2′-Deoxy Guanosine Nucleotides Alter the Biochemical Properties of Ras

Yun, S. D., Scott, E., Moghadamchargari, Z., & Laganowsky, A. D. (2023) · Biochemistry · doi:10.1021/acs.biochem.3c00258 · Cited by 9

Disease pathways at the Rat Genome Database Pathway Portal: genes in context-a network approach to understanding the molecular mechanisms of disease

Petri, V., Hayman, G. T., Tutaj, M., Smith, J. R., Laulederkind, S. J. F., Wang, S., Nigam, R., Pons, J. D., Shimoyama, M. E., Dwinell, M. R., et al. (2014) · Human Genomics · doi:10.1186/preaccept-2344511051385730 · Cited by 8

KRAS as Potential Target in Colorectal Cancer Therapy

Eng, S.-K., Loh, T. H. T., Goh, B. H., & Lee, W.-L. (2019) · Springer eBooks · doi:10.1007/978-981-13-7154-7_12 · Cited by 8

Sensitivity and Resistance of Oncogenic RAS-Driven Tumors to Dual MEK and ERK Inhibition

Catalano, A., Adlesic, M., Kaltenbacher, T., Klar, R. F. U., Albers, J., Seidel, P., Brandt, L. P., Hejhal, T., Busenhart, P., Röhner, N., et al. (2021) · Cancers · doi:10.3390/cancers13081852 · Cited by 9

Covalent Fragment Screening Identifies Rgl2 RalGEF Cysteine for Targeted Covalent Inhibition of Ral GTPase Activation

Bum‐Erdene, K., Ghozayel, M. K., Xu, D. D., & Meroueh, S. O. (2022) · ChemMedChem · doi:10.1002/cmdc.202100750 · Cited by 8

Combination of RSK inhibitor LJH-685 and FLT3 inhibitor FF-10101 promoted apoptosis and proliferation inhibition of AML cell lines

Zhang, S., Liu, J., Lu, Z.-Y., Xue, Y.-T., Mu, X.-R., Liu, Y., Cao, J., Li, Z., Li, F., Xu, K.-L., et al. (2022) · Cellular Oncology · doi:10.1007/s13402-022-00703-7 · Cited by 8

SFPQ promotes RAS-mutant cancer cell growth by modulating 5′-UTR mediated translational control of CK1α

Kok, V. J. T., Tang, J. Y., Eng, G. W. L., Tan, S. Y., Chin, J. T. F., Quek, C. H., Lai, W. X., Lim, T. K., Lin, Q., Chua, J. J. E., et al. (2022) · NAR Cancer · doi:10.1093/narcan/zcac027 · Cited by 8

Inhibition of mutant RAS-RAF interaction by mimicking structural and dynamic properties of phosphorylated RAS

Ilter, M., Kaşmer, R., Jalalypour, F., Atılgan, C., Topcu, O., Karakaş, N., & Şensoy, Ö. (2022) · eLife · doi:10.7554/elife.79747 · Cited by 7

KRAS Allelic Imbalance: Strengths and Weaknesses in Numbers

Doherty, G. J., Kerr, E. M., & Martins, C. P. (2017) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2017.03.005 · Cited by 8

Effectors and potential targets selectively upregulated in human KRAS-mutant lung adenocarcinomas

Li, J., Sordella, R., & Powers, S. (2016) · Scientific Reports · doi:10.1038/srep27891 · Cited by 8

SUMO wrestling with Ras

Zhang, H., & Luo, J. (2016) · Small GTPases · doi:10.1080/21541248.2016.1161698 · Cited by 8

Misshapen Disruption Cooperates with RasV12 to Drive Tumorigenesis

Kong, D., Lu, J., Li, X., Zhao, S., Xu, W., Fang, J., Wang, X., & Ma, X. (2021) · Cells · doi:10.3390/cells10040894 · Cited by 7

A conformation-selective protein binder for a KRAS mutant inhibits the interaction between RAS and RAF

Jung, Y. H., Choi, Y., Seo, H., Seo, M., & Kim, H. (2023) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2023.01.019 · Cited by 7

Nucleotide Exchange on RAS Proteins Using Hydrolysable and Non-hydrolysable Nucleotides

Waybright, T. J., & Stephen, A. G. (2024) · Methods in molecular biology · doi:10.1007/978-1-0716-3822-4_4 · Cited by 7

Modulation of the cytoskeleton for cancer therapy

Matov, A. (2026) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2025.1681065 · Cited by 7

Microtubule regulation in cancer cells

Matov, A. (2026) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2025.1677302 · Cited by 7

Identification of a fragmented small GTPase capable of conditional effector binding

Zhao, J., & Stains, C. I. (2017) · RSC Advances · doi:10.1039/c6ra25575b · Cited by 7

A Raf-Competitive K-Ras Binder Can Fail to Functionally Antagonize Signaling

Kauke, M. J., Tisdale, A. W., Kelly, R. L., Braun, C. J., Hemann, M. T., & Wittrup, K. D. (2018) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-17-0645 · Cited by 8

Transcriptome analysis to identify the Ras and Rap1 signal pathway genes involved in the response of TM3 Leydig cells exposed to zearalenone

Wang, M., Wang, N., Tong, J., Pan, J., Long, M., & Li, P. (2018) · Environmental Science and Pollution Research · doi:10.1007/s11356-018-3129-1 · Cited by 7

Comparative MD simulations and advanced analytics based studies on wild-type and hot-spot mutant A59G HRas

Sharma, N., Sonavane, U., & Joshi, R. (2020) · PLOS ONE · doi:10.1371/journal.pone.0234836 · Cited by 7

Context Matters—Why We Need to Change From a One Size Fits all Approach to Made-to-Measure Therapies for Individual Patients With Pancreatic Cancer

Sankarasubramanian, S., Pfohl, U., Regenbrecht, C. R. A., Reinhard, C., & Wedeken, L. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.760705 · Cited by 7

An In Vivo Inflammatory Loop Potentiates KRAS Blockade

Arendt, K. A. M., Ntaliarda, G., Armenis, V., Kati, D., Henning, C., Giotopoulou, G. A., Pepe, M. A. A., Klotz, L. V., Lamort, A., Hatz, R. A., et al. (2022) · Biomedicines · doi:10.3390/biomedicines10030592 · Cited by 7

Activated K-RAS and its effect on morphological appearance

Kiyokawa, E., & Minato, H. (2014) · The Journal of Biochemistry · doi:10.1093/jb/mvu041 · Cited by 7

Spiclomazine displays a preferential anti-tumor activity in mutant KRas-driven pancreatic cancer

Guo, X., Zhao, W., Liu, Z., & Wang, J. (2018) · Oncotarget · doi:10.18632/oncotarget.24025 · Cited by 7

Molecular Orientation Determination in Nanodiscs at the Single-Molecule Level

Camp, T., Mehta, K., Sligar, S. G., & Zhang, K. (2019) · Analytical Chemistry · doi:10.1021/acs.analchem.9b04950 · Cited by 7

Peptidomimetics designed to bind to RAS effector domain are promising cancer therapeutic compounds

Pallara, C., Cabot, D., Rivas, J., Brun, S., Seco, J., Abuasaker, B., Tarragó, T., Jaumot, M., Prades, R., & Agell, N. (2022) · Scientific Reports · doi:10.1038/s41598-022-19703-6 · Cited by 7

Metabolic vulnerability of KRAS-driven cancer cells

Foster, D. A. (2014) · Molecular & Cellular Oncology · doi:10.4161/23723548.2014.963445 · Cited by 7

Structural insights, regulation, and recent advances of RAS inhibitors in the MAPK signaling cascade: a medicinal chemistry perspective

Prajapati, V., Singh, A. K., Kumar, A. M., Singh, H., Pathak, P., Grishina, M., Kumar, V., Khalilullah, H., Verma, A., & Kumar, P. (2025) · RSC Medicinal Chemistry · doi:10.1039/d4md00923a · Cited by 6

Navigating the complexities of pancreatic ductal adenocarcinoma: A review on therapeutic models and RAS inhibitors

Barrambana, S., Zamorano-Domínguez, E., Liaki, V., & Guerra, C. E. (2025) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2025.115652 · Cited by 8

Moving Towards Dawn: KRas Signaling and Treatment in Pancreatic Ductal Adenocarcinoma

Bhattacharya, S., & Rajpurohit, T. (2022) · Current Molecular Pharmacology · doi:10.2174/1874467215666220128161647 · Cited by 6

Production and Membrane Binding of N-Terminally Acetylated, C-Terminally Farnesylated and Carboxymethylated KRAS4b

Messing, S. A. J., Agamasu, C., Drew, M. R., DeHart, C. J., Stephen, A. G., & Gillette, W. (2021) · Methods in molecular biology · doi:10.1007/978-1-0716-1190-6_6 · Cited by 6

Non-Oncogene Addiction of KRAS-Mutant Cancers to IL-1β via Versican and Mononuclear IKKβ

Σπέλλα, Μ., Ntaliarda, G., Skiadas, G., Lamort, A., Vreka, M., Marazioti, A., Lilis, I., Bouloukou, E., Giotopoulou, G. A., Pepe, M. A. A., et al. (2023) · Cancers · doi:10.3390/cancers15061866 · Cited by 6

Structure-based prediction of Ras-effector binding affinities and design of “branchegetic” interface mutations

(2023) · doi:10.1016/j.str.2023.04.007 · Cited by 6

Classical prescription Floris Sophorae Powder treat colorectal cancer by regulating KRAS/MEK-ERK signaling pathway

Han, L., Hao, Y., Wang, S., Bao, Y., Li, T., Zheng, Y., Luo, X., Jia, M., Zhang, Q., & Meng, X. (2024) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2024.117805 · Cited by 6

Growth factor transduction pathways: paradigm of anti-neoplastic targeted therapy

Carlomagno, F., & Chiariello, M. (2014) · Journal of Molecular Medicine · doi:10.1007/s00109-014-1177-7 · Cited by 6

NMR 1H,13C, 15N backbone and 13C side chain resonance assignment of the G12C mutant of human K-Ras bound to GDP

Sharma, A. K., Lee, S., Rigby, A. C., & Townson, S. A. (2018) · Biomolecular NMR Assignments · doi:10.1007/s12104-018-9821-8 · Cited by 6

KRAS Q61H Mutation Confers Cancer Cells with Acquired Resistance to SHP2 Inhibition

Song, Y., Yang, X., & Yu, B. (2022) · Pharmaceutical Fronts · doi:10.1055/s-0042-1743411 · Cited by 6

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

Ras and Ras Signaling as a Therapeutic Target in Cancer

Sliker, B. H., & Campbell, P. M. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-820472-6.00006-2

Targeting the “undruggable” RAS with biologics

Whaby, M., Khan, I., & O’Bryan, J. P. (2022) · Advances in cancer research · doi:10.1016/bs.acr.2021.07.006 · Cited by 19

Targeting the Undruggable: Small Molecule Modulation of Ras Proteins

Kim, J. (2025) · International journal of high school research · doi:10.36838/v7i9.103

RASpecting the oncogene: New pathways to therapeutic advances

Stout, M. C., & Campbell, P. M. (2018) · Biochemical Pharmacology · doi:10.1016/j.bcp.2018.10.022 · Cited by 7