Ras oncogenes: split personalities

Functional rafts in cell membranes

Simons, K., & Ikonen, E. (1997) · Nature · doi:10.1038/42408 · Cited by 9,757

G PROTEINS: TRANSDUCERS OF RECEPTOR-GENERATED SIGNALS

Gilman, A. G. (1987) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.56.070187.003151 · Cited by 6,405

Oncogenic ras provokes premature cell senescence associated with accumulation of p53 and p16INK4a

Serrano, M., Lin, A. W., McCurrach, M. E., Beach, D., & Lowe, S. W. (1997) · Cell · doi:10.1016/s0092-8674(00)81902-9 · Cited by 5,218

Regulation of Renal Organic Anion Transporter 3 (SLC22A8) Expression and Function by the Integrity of Lipid Raft Domains and their Associated Cytoskeleton

Srimaroeng, C., Cecile, J. P., Walden, R., & Pritchard, J. B. (2013) · Cellular Physiology and Biochemistry · doi:10.1159/000350077 · Cited by 2,989

Tumorigenic conversion of primary embryo fibroblasts requires at least two cooperating oncogenes

Land, H., Parada, L. F., & Weinberg, R. A. (1983) · Nature · doi:10.1038/304596a0 · Cited by 2,804

Creation of human tumour cells with defined genetic elements

Hahn, W. C., Counter, C. M., Lundberg, A. S., Beijersbergen, R. L., Brooks, M. W., & Weinberg, R. A. (1999) · Nature · doi:10.1038/22780 · Cited by 2,345

Phosphatidylinositol-3-OH kinase direct target of Ras

Rodriguez-Viciana, P., Warne, P. H., Dhand, R., Vanhaesebroeck, B., Gout, I., Fry, M. J., Waterfield, M. D., & Downward, J. (1994) · Nature · doi:10.1038/370527a0 · Cited by 1,954

Mammalian Ras interacts directly with the serine/threonine kinase raf

Vojtek, A. B., Hollenberg, S. M., & Cooper, J. A. (1993) · Cell · doi:10.1016/0092-8674(93)90307-c · Cited by 1,934

Mutations in PTPN11, encoding the protein tyrosine phosphatase SHP-2, cause Noonan syndrome

Tartaglia, M., Mehler, E. L., Goldberg, R. B., Zampino, G., Brunner, H. G., Kremer, H., van der Burgt, I., Crosby, A. H., Ion, A., Jeffery, S., et al. (2001) · Nature Genetics · doi:10.1038/ng772 · Cited by 1,736

The Ras-RasGAP Complex: Structural Basis for GTPase Activation and Its Loss in Oncogenic Ras Mutants

Scheffzek, K., Ahmadian, M. R., Kabsch, W., Wiesmüller, L., Lautwein, A., Schmitz, F., & Wittinghofer, A. (1997) · Science · doi:10.1126/science.277.5324.333 · Cited by 1,543

The metastasis suppressor Nm23 as a modulator of Ras/ERK signaling

Takács‐Vellai, K. (2014) · Journal of Molecular Signaling · doi:10.1186/1750-2187-9-4 · Cited by 22

Novel RasGRF1-derived Tat-fused peptides inhibiting Ras-dependent proliferation and migration in mouse and human cancer cells

Sacco, E., Metalli, D., Spinelli, M., Manzoni, R., Šamalíková, M., Grandori, R., Morrione, A., Traversa, S., Alberghina, L., & Vanoni, M. (2011) · Biotechnology Advances · doi:10.1016/j.biotechadv.2011.05.011 · Cited by 22

NRAS Mutant Melanoma: An Overview for the Clinician for Melanoma Management

Jenkins, R. W., & Sullivan, R. J. (2016) · Melanoma Management · doi:10.2217/mmt.15.40 · Cited by 24

Downregulation of RASAL2 promotes the proliferation, epithelial-mesenchymal transition and metastasis of colorectal cancer cells

Jia, Z., Liu, W., Gong, L., & Xiao, Z. (2017) · Oncology Letters · doi:10.3892/ol.2017.5581 · Cited by 22

Diet-induced hepatic steatosis activates Ras to promote hepatocarcinogenesis via CPT1α

Xu, A., Wang, B., Fu, J., Qin, W., Yu, T., Yang, Z., Lu, Q., Chen, J., Chen, Y., & Wang, H. (2018) · Cancer Letters · doi:10.1016/j.canlet.2018.10.024 · Cited by 22

KRAS mutations in brown tumor of the jaws in hyperparathyroidism

Guimarães, L. M., Gomes, I. P., Pereira, T. D. S. F., de Andrade, B. A. B., Romañach, M. J., de Lacerda, J. C. T., Pontes, H. A. R., Brennan, P. A., Rahimi, S., Carlos, R., et al. (2020) · Journal of Oral Pathology and Medicine · doi:10.1111/jop.13048 · Cited by 22

Promising Molecular Targets for the Targeted Therapy of Biliary Tract Cancers: An Overview

Yang, W., & Sun, Y. (2021) · OncoTargets and Therapy · doi:10.2147/ott.s297643 · Cited by 22

Bach1 is critical for the transformation of mouse embryonic fibroblasts by RasV12 and maintains ERK signaling

Nakanome, A., Brydun, A., Matsumoto, M., Ota, K., Funayama, R., Nakayama, K., Ono, M., Shiga, K., Kobayashi, T., & Igarashi, K. (2012) · Oncogene · doi:10.1038/onc.2012.336 · Cited by 22

YAP1 Takes Over when Oncogenic K-Ras Slumbers

Greten, F. R. (2014) · Cell · doi:10.1016/j.cell.2014.06.021 · Cited by 21

Elucidating the Mode of Action of a Typical Ras State 1(T) Inhibitor

Rosnizeck, I. C., Filchtinski, D., Lopes, R. P., Kieninger, B., Herrmann, C., Kalbitzer, H. R., & Spoerner, M. (2014) · Biochemistry · doi:10.1021/bi401689w · Cited by 21

Mitochondria as the decision makers for cancer cell fate: from signaling pathways to therapeutic strategies

Genovese, I., Vezzani, B., Danese, A., Modesti, L., Vitto, V. A. M., Corazzi, V., Pelucchi, S., Pinton, P., & Giorgi, C. (2020) · Cell Calcium · doi:10.1016/j.ceca.2020.102308 · Cited by 21

Multidisciplinary Management of Costello Syndrome: Current Perspectives

Leoni, C., Viscogliosi, G., Tartaglia, M., Aoki, Y., & Zampino, G. (2022) · Journal of Multidisciplinary Healthcare · doi:10.2147/jmdh.s291757 · Cited by 21

SOS1 regulates HCC cell epithelial-mesenchymal transition via the PI3K/AKT/mTOR pathway

Li, Y., Yin, Y., He, Y., He, K., & Li, J. (2022) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2022.11.015 · Cited by 21

SLC25A21 downregulation promotes KRAS-mutant colorectal cancer progression by increasing glutamine anaplerosis

Hu, S., Han, Y., Tan, T.-Y., Chen, H., Gao, J.-W., Wang, L., Yang, M., Zhao, L., Wang, Y., Ding, Y., et al. (2023) · JCI Insight · doi:10.1172/jci.insight.167874 · Cited by 22

High Pressure NMR Methods for Characterizing Functional Substates of Proteins

Kalbitzer, H. R. (2015) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-94-017-9918-8_9 · Cited by 21

Selective targeting of KRAS-Mutant cells by miR-126 through repression of multiple genes essential for the survival of KRAS-Mutant cells

Hara, T., Jones, M. F., Subramanian, M., Li, X. L., Ou, O. L., Zhu, Y. J., Yang, Y.-A., Wakefield, L. M., Hussain, S. P., Gaedcke, J., et al. (2014) · Oncotarget · doi:10.18632/oncotarget.2284 · Cited by 21

Ras Effector Mutant Expression Suggest a Negative Regulator Inhibits Lung Tumor Formation

Vandal, G., Geiling, B., & Dankort, D. L. (2014) · PLoS ONE · doi:10.1371/journal.pone.0084745 · Cited by 21

Liver Tumor Models in Transgenic Zebrafish: An Alternative In Vivo Approach to Study Hepatocarcinogenes

Huang, X., Zhou, L. Q., & Gong, Z. (2011) · Future Oncology · doi:10.2217/fon.11.137 · Cited by 21

A rapid and sensitive assay for determining human brain levels of farnesyl-(FPP) and geranylgeranylpyrophosphate (GGPP) and transferase activities using UHPLC–MS/MS

Hooff, G. P., Patel, N., Wood, W. G., Müller, W. E., Eckert, G. P., & Volmer, D. A. (2010) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-010-4088-7 · Cited by 21

Intracellular and intercellular signaling networks in cancer initiation, development and precision anti-cancer therapy

Csermely, P., Korcsmáros, T., & Nussinov, R. (2016) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2016.07.005 · Cited by 22

Enriching Traditional Protein-protein Interaction Networks with Alternative Conformations of Proteins

Halakou, F., Sen-Kilic, E., Cukuroglu, E., Keskin, Ö., & Gürsoy, A. (2017) · Scientific Reports · doi:10.1038/s41598-017-07351-0 · Cited by 21

NRAS and KRAS polymorphisms are not associated with hepatoblastoma susceptibility in Chinese children

Yang, T., Yang, W., Li, J., Tan, T., Yang, J., Pan, J., Hu, C., Yao, Y., Zhang, J., Xin, Y., et al. (2019) · Experimental Hematology and Oncology · doi:10.1186/s40164-019-0135-z · Cited by 21

Oncogenic Ras mutant causes the hyperactivation of NF‐κB via acceleration of its transcriptional activation

Tago, K., Funakoshi‐Tago, M., Ohta, S., Kawata, H., Saitoh, H., Horie, H., Aoki‐Ohmura, C., Yamauchi, J., Tanaka, A., Matsugi, J., et al. (2019) · Molecular Oncology · doi:10.1002/1878-0261.12580 · Cited by 22

Influence of the Lipid Anchor Motif of N-Ras on the Interaction with Lipid Membranes: A Surface Plasmon Resonance Study

Gohlke, A., Triola, G., Waldmann, H., & Winter, R. (2010) · Biophysical Journal · doi:10.1016/j.bpj.2010.02.005 · Cited by 21

Mouse Tissues that Undergo Neoplastic Progression after K-Ras Activation Are Distinguished by Nuclear Translocation of phospho-Erk1/2 and Robust Tumor Suppressor Responses

Parikh, N., Shuck, R. L., Nguyen, T., Herron, A. J., & Donehower, L. A. (2012) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-12-0089 · Cited by 21

α-Lipoic acid suppresses migration and invasion via downregulation of cell surface β1-integrin expression in bladder cancer cells

Yamasaki, M., Iwase, M., Kawano, K., Sakakibara, Y., Suiko, M., Ikeda, M., & Nishiyama, K. (2013) · Journal of Clinical Biochemistry and Nutrition · doi:10.3164/jcbn.13-57 · Cited by 20

Concomitant deletion of HRAS and NRAS leads to pulmonary immaturity, respiratory failure and neonatal death in mice

Fuentes‐Mateos, R., Jimeno, D., Gómez, C., Calzada, N., Fernández‐Medarde, A., & Santos, E. (2019) · Cell Death and Disease · doi:10.1038/s41419-019-2075-2 · Cited by 20

A H-REV107 Peptide Inhibits Tumor Growth and Interacts Directly with Oncogenic KRAS Mutants

Han, C. W., Jeong, M. S., Ha, S. C., & Jang, S. B. (2020) · Cancers · doi:10.3390/cancers12061412 · Cited by 20

ITPR1-AS1 promotes small cell lung cancer metastasis by facilitating P21 splicing and stabilizing DDX3X to activate the cRaf-MEK-ERK cascade

Zhang, Q., Zheng, L., Bai, Y., Su, C., Che, Y., Xu, J., Sun, K., Ni, J., Huang, L., Shen, Y., et al. (2023) · Cancer Letters · doi:10.1016/j.canlet.2023.216426 · Cited by 20

Deformation of a two-domain lipid bilayer due to asymmetric insertion of lipid-modified Ras peptides

Li, Z., & Gorfe, A. A. (2013) · Soft Matter · doi:10.1039/c3sm51388b · Cited by 20

Gα16 activates Ras by forming a complex with tetratricopeptide repeat 1 (TPR1) and Son of Sevenless (SOS)

Liu, A. M. F., Lo, R. K. H., Lee, M. M. K., Wang, Y., Yeung, W. W. S., Ho, M. K. C., Su, Y. L., Ye, R. D., & Wong, Y. H. (2010) · Cellular Signalling · doi:10.1016/j.cellsig.2010.05.013 · Cited by 20

A High-Throughput Assay for Small Molecule Destabilizers of the KRAS Oncoprotein

Carver, J. O., Dexheimer, T. S., Hsu, D. J., Weng, M., Smith, J. L., Guha, R., Jadhav, A., Simeonov, A. M., & Luo, J. (2014) · PLoS ONE · doi:10.1371/journal.pone.0103836 · Cited by 20

RAS and Hedgehog - partners in crime

Lauth, M. (2011) · Frontiers in bioscience · doi:10.2741/3852 · Cited by 21

The role of the NORE1A tumor suppressor in Oncogene-Induced Senescence

Barnoud, T., Schmidt, M., Donninger, H., & Clark, G. J. (2017) · Cancer Letters · doi:10.1016/j.canlet.2017.04.030 · Cited by 20

Structural characterization of 14-3-3ζ in complex with the human Son of sevenless homolog 1 (SOS1)

Ballone, A., Centorrino, F., Wolter, M., & Ottmann, C. (2018) · Journal of Structural Biology · doi:10.1016/j.jsb.2018.01.011 · Cited by 20

Methionine 170 is an Environmentally Sensitive Membrane Anchor in the Disordered HVR of K-Ras4B

Neale, C., & Garcı́a, A. E. (2018) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.8b07919 · Cited by 20

Transcriptomic analysis of differentially expressed genes in the Ras1CA-overexpressed and wildtype posterior silk glands

Ma, L., Ma, Q., Li, X., Cheng, L., Li, K., & Li, S. (2014) · BMC Genomics · doi:10.1186/1471-2164-15-182 · Cited by 20

The inflammatory cytokine TNFα cooperates with Ras in elevating metastasis and turns WT-Ras to a tumor-promoting entity in MCF-7 cells

Leibovich-Rivkin, T., Liubomirski, Y., Meshel, T., Abashidze, A., Brisker, D., Solomon, H., Rotter, V., Weil, M., & Ben‐Baruch, A. (2014) · BMC Cancer · doi:10.1186/1471-2407-14-158 · Cited by 20

Silencing the Expression of Ras Family GTPase Homologues Decreases Inflammation and Joint Destruction in Experimental Arthritis

de Launay, D., Vreijling, J. P., Hartkamp, L. M., Karpus, O. N., Abreu, J. R. F., van Maanen, M. A., Sanders, M. E., Grabiec, A. M., Hamann, J., Ørum, H., et al. (2010) · American Journal Of Pathology · doi:10.2353/ajpath.2010.091053 · Cited by 20

Screening of Focused Compound Library Targeting Liver X Receptors in Pancreatic Cancer Identified Ligands with Inverse Agonist and Degrader Activity

Karaboga, H., Huang, W., Srivastava, S., Widmann, S., Addanki, S., Gamage, K. T., Mazhar, Z., Ebalunode, J. O., Briggs, J. M., Gustafsson, J.-Α., et al. (2020) · ACS Chemical Biology · doi:10.1021/acschembio.0c00546 · Cited by 19

KRAS4A induces metastatic lung adenocarcinomas in vivo in the absence of the KRAS4B isoform

Salmón, M., Paniagua, G., Lechuga, C. G., Fernández-García, F., Zarzuela, E., Álvarez, R., Musteanu, M., Guerra, C. E., Caleiras, E. J., Muñoz, J., et al. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2023112118 · Cited by 19

Narrative review of emerging roles for AKT-mTOR signaling in cancer radioimmunotherapy

Shen, C., He, Y., Chen, Q., Feng, H., Williams, T. M., Lu, Y., & He, Z. (2021) · Annals of Translational Medicine · doi:10.21037/atm-21-4544 · Cited by 20

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

Progression of KRAS mutant pancreatic adenocarcinoma during vemurafenib treatment in a patient with metastatic melanoma

Grey, A., Cooper, A. J., McNeil, C. M., O'Toole, S. A., Thompson, J. F., & Grimison, P. (2014) · Internal Medicine Journal · doi:10.1111/imj.12415 · Cited by 19

Thinking Outside the Box about Ras

Kyriakis, J. M. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.r800085200 · Cited by 19

Low Concentrations of Hydrogen Peroxide or Nitrite Induced of Paracoccidioides brasiliensis Cell Proliferation in a Ras-Dependent Manner

Haniu, A. E. C. J., Maricato, J. T., Mathias, P. P. M., Castilho, D. G., Miguel, R. B., Monteiro, H. P., Puccia, R., & Batista, W. L. (2013) · PLoS ONE · doi:10.1371/journal.pone.0069590 · Cited by 19

Oncogenic Ras influences the expression of multiple lncRNAs

Kotake, Y., Naemura, M., Kitagawa, K., Niida, H., Tsunoda, T., Shirasawa, S., & Kitagawa, M. (2014) · Cytotechnology · doi:10.1007/s10616-014-9834-9 · Cited by 19

Oncogenic Ras Blocks the cAMP Pathway and Dedifferentiates Thyroid Cells Via an Impairment of Pax8 Transcriptional Activity

Baratta, M. G., Porreca, I., & Lauro, R. D. (2009) · Molecular Endocrinology · doi:10.1210/me.2008-0353 · Cited by 19

Bridging the gap: A regulator of NF-κB linking inflammation and cancer

Postler, T. S., & Ghosh, S. (2015) · Journal of Oral Biosciences · doi:10.1016/j.job.2015.05.001 · Cited by 19

Therapeutic Approaches to RAS Mutation

Scott, A. J., Lieu, C. H., & Messersmith, W. A. (2016) · The Cancer Journal · doi:10.1097/ppo.0000000000000187 · Cited by 19

Selectivity of CDC25 Homology Domain-Containing Guanine Nucleotide Exchange Factors

Popovic, M., Rensen, M. G. A., & Rehmann, H. (2013) · Journal of Molecular Biology · doi:10.1016/j.jmb.2013.04.031 · Cited by 19

Addressing the Right Targets in Oncology: Challenges and Alternative Approaches

Stock, J. K., Jones, N. P., Hammonds, T. R., Roffey, J., & Dillon, C. (2015) · SLAS DISCOVERY · doi:10.1177/1087057114564349 · Cited by 19

Allostery

Montserrat‐Canals, M., Cordara, G., & Krengel, U. (2025) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583524000209 · Cited by 19

Current status of KRAS G12C inhibitors in NSCLC and the potential for combination with anti-PD-(L)1 therapy: a systematic review

Zhang, F., Wang, B., Wu, M., Zhang, L., & Ji, M. Q. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1509173 · Cited by 20

Natural Products Attenuating Biosynthesis, Processing, and Activity of Ras Oncoproteins: State of the Art and Future Perspectives

Tisi, R., Gaponenko, V., Vanoni, M., & Sacco, E. (2020) · Biomolecules · doi:10.3390/biom10111535 · Cited by 18

Neurobiological Opportunities in Diabetic Polyneuropathy

Poitras, T. M., Munchrath, E., & Zochodne, D. W. (2021) · Neurotherapeutics · doi:10.1007/s13311-021-01138-y · Cited by 19

Temporally-regulated quick activation and inactivation of Ras is important for olfactory behaviour

Uozumi, T., Hirotsu, T., Yoshida, K., Yamada, R., Suzuki, A., Taniguchi, G., Iino, Y., & Ishihara, T. (2012) · Scientific Reports · doi:10.1038/srep00500 · Cited by 18

Anti-EGFR MoAb treatment in colorectal cancer: limitations, controversies, and contradictories

Cheng, L., Ren, W., Xie, L., Li, M., Liu, J., Hu, J. Y., Liu, B., & Qian, X. (2014) · Cancer Chemotherapy and Pharmacology · doi:10.1007/s00280-014-2489-6 · Cited by 18

Co-amplification at Lower Denaturation-temperature PCR Combined with Unlabled-probe High-resolution Melting to Detect KRAS Codon 12 and 13 Mutations in Plasma-circulating DNA of Pancreatic Adenocarcinoma Cases

Wu, J., Zhou, Y., Zhang, C.-Y., Song, B., Wang, B., Pan, B., Lou, W., & Guo, W. (2015) · Asian Pacific Journal of Cancer Prevention · doi:10.7314/apjcp.2014.15.24.10647 · Cited by 18

Ras1CA-UpregulatedbcpiInhibits Cathepsin Activity to Prevent Tissue Destruction of theBombyxPosterior Silk Gland

Ma, L., Liu, S., Shi, M., Chen, X., & Li, S. (2013) · Journal of Proteome Research · doi:10.1021/pr400005g · Cited by 18

PINTnet: construction of condition-specific pathway interaction network by computing shortest paths on weighted PPI

Moon, J. H., Lim, S., Jo, K., Lee, S., Seo, S., & Kim, S. (2017) · BMC Systems Biology · doi:10.1186/s12918-017-0387-3 · Cited by 18

RUNX3 and p53: How Two Tumor Suppressors Cooperate Against Oncogenic Ras?

Lee, J.-W., van Wijnen, A. J., & Bae, S. (2017) · Advances in experimental medicine and biology · doi:10.1007/978-981-10-3233-2_20 · Cited by 18

Ras-Raf-MAPK signaling promotes nuclear localization of FOXA transcription factor SGF1 via Ser91 phosphorylation

Ma, L., Li, K., Guo, Y., Sun, X., Deng, H., Li, K., Feng, Q., & Li, S. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2018.01.007 · Cited by 18

Wogonoside induces depalmitoylation and translocation of PLSCR 1 and N‐ RAS in primary acute myeloid leukaemia cells

Li, H., Yu, X., Liu, X., Hu, P., Shen, L., Zhou, Y., Zhu, Y., Li, Z., Hui, H., Guo, Q., et al. (2018) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.13481 · Cited by 18

Responses of unicellular predators to cope with the phototoxicity of photosynthetic prey

Uzuka, A., Kobayashi, Y., Onuma, R., Hirooka, S., Kanesaki, Y., Yoshikawa, H., Fujiwara, T., & Miyagishima, S. (2019) · Nature Communications · doi:10.1038/s41467-019-13568-6 · Cited by 18

Oncogenic K-Ras4B Dimerization Enhances Downstream Mitogen-activated Protein Kinase Signaling

Muratcioğlu, S., Aydın, C., Odabasi, E., Özdemir, E. S., Firat‐Karalar, E. N., Jang, H., Tsai, C., Nussinov, R., Kavaklı, İ. H., Gürsoy, A., et al. (2020) · Journal of Molecular Biology · doi:10.1016/j.jmb.2020.01.002 · Cited by 19

A feedforward circuit shaped by ECT2 and USP7 contributes to breast carcinogenesis

Zhang, Q., Cao, C., Gong, W., Bao, K., Wang, Q., Wang, Y., Bi, L., Ma, S., Zhao, J., Liu, L., et al. (2020) · Theranostics · doi:10.7150/thno.46878 · Cited by 18

Mutations of the functional ARH1 allele in tumors from ARH1 heterozygous mice and cells affect ARH1 catalytic activity, cell proliferation and tumorigenesis

Kato, J., Vekhter, D., Heath, J., Zhu, J., Barbieri, J. T., & Moss, J. (2015) · Oncogenesis · doi:10.1038/oncsis.2015.5 · Cited by 20

Discovery of Small-Molecule Ras Inhibitors that Display Antitumor Activity by Interfering with Ras·GTP–Effector Interaction

Shima, F., Yoshikawa, Y., Matsumoto, S., & Kataoka, T. (2013) · The Enzymes · doi:10.1016/b978-0-12-420146-0.00001-9 · Cited by 18

Tnk1/Kos1: a novel tumor suppressor.

May, W. S., Hoare, K., Hoare, S., Reinhard, M. K., Lee, Y. J., & Oh, S.-C. (2010) · PubMed Central · Cited by 18

UBIAD1 suppresses the proliferation of bladder carcinoma cells by regulating H-Ras intracellular trafficking via interaction with the C-terminal domain of H-Ras

Xu, Z., Duan, F., Lu, H., Dragh, M. A. K., Xia, Y., Liang, H., & Hong, L. (2018) · Cell Death and Disease · doi:10.1038/s41419-018-1215-4 · Cited by 19

Serum-dependent transcriptional networks identify distinct functional roles for H-Ras and N-Ras during initial stages of the cell cycle

Castellano, E., Guerrero, C., Núñez, A., Rivas, J. D. L., & Santos, E. (2009) · Genome biology · doi:10.1186/gb-2009-10-11-r123 · Cited by 19

Advancements in gene therapies targeting mutant KRAS in cancers

Wang, Y., Bui, T. A., Yang, X., Hutvágner, G., & Deng, W. (2025) · Cancer and Metastasis Reviews · doi:10.1007/s10555-025-10243-9 · Cited by 20

Glycoprotein non–metastatic melanoma protein B functions with growth factor signaling to induce tumorigenesis through its serine phosphorylation

Wang, C., Okita, Y., Zheng, L., Shinkai, Y., Manevich, L., Chin, J. M., Kimura, T., Suzuki, H., Kumagai, Y., & Kato, M. (2021) · Cancer Science · doi:10.1111/cas.15090 · Cited by 17

Conquering oncogenic KRAS and its bypass mechanisms

Hou, P., & Wang, Y. (2022) · Theranostics · doi:10.7150/thno.71260 · Cited by 18

Targeting Asparagine Synthetase in Tumorgenicity Using Patient-Derived Tumor-Initiating Cells

Nishikawa, G., Kawada, K., Hanada, K., Maekawa, H., Itatani, Y., Miyoshi, H., Taketo, M. M., & Obama, K. (2022) · Cells · doi:10.3390/cells11203273 · Cited by 19

Mitochondrial ribosomal protein S18-2 evokes chromosomal instability and transforms primary rat skin fibroblasts

Darekar, S. D., Mushtaq, M., Gurrapu, S., Kovalevska, L. M., Drummond, C. J., Petruchek, M., Tirinato, L., Fabrizio, E. M. D., Carbone, E., & Kashuba, E. (2015) · Oncotarget · doi:10.18632/oncotarget.4123 · Cited by 18

MEK Inhibitor for Gastric Cancer with MEK1 Gene Mutations

Sogabe, S., Togashi, Y., Kato, H., Kogita, A., Mizukami, T., Sakamoto, Y., Banno, E., Terashima, M., Hayashi, H., Velasco, M. A. D., et al. (2014) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-14-0429 · Cited by 17

From Optimization to Mapping: An Evolutionary Algorithm for Protein Energy Landscapes

Sapin, E., Jong, K. A. D., & Shehu, A. (2016) · IEEE Transactions on Computational Biology and Bioinformatics · doi:10.1109/tcbb.2016.2628745 · Cited by 17

Molecular Basis for Allosteric Inhibition of GTP-Bound H-Ras Protein by a Small-Molecule Compound Carrying a Naphthalene Ring

Matsumoto, S., Hiraga, T., Hayashi, Y., Yoshikawa, Y., Tsuda, C., Araki, M., Neya, M., Shima, F., & Kataoka, T. (2018) · Biochemistry · doi:10.1021/acs.biochem.8b00680 · Cited by 17

Targeting Defects in the Cellular DNA Damage Response for the Treatment of Pancreatic Ductal Adenocarcinoma

Schmitt, A., Feldmann, G., Zander, T., & Reinhardt, H. C. (2018) · Oncology Research and Treatment · doi:10.1159/000493401 · Cited by 18

A novel terpenoid class for prevention and treatment of KRAS‐driven cancers: Comprehensive analysis using in situ, in vitro, and in vivo model systems

Ganaie, A. A., Siddique, H. R., SHEIKH, I. A., Parray, A., Wang, L., Panyam, J., Villalta, P. W., Deng, Y., Konety, B. R., & Saleem, M. (2020) · Molecular Carcinogenesis · doi:10.1002/mc.23200 · Cited by 17

Beyond the Mevalonate Pathway: Control of Post-Prenylation Processing by Mutant p53

Etichetti, C. M. B., Zalazar, E. A., Cocordano, N., & Girardini, J. E. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2020.595034 · Cited by 17

Mutations in the α4-α5 allosteric lobe of RAS do not significantly impair RAS signaling or self-association

Whaby, M., Wallon, L., Mazzei, M., Khan, I., Teng, K. W., Koide, S., & O’Bryan, J. P. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102661 · Cited by 17

Machine learning on normalized protein sequences

Heider, D., Verheyen, J., & Hoffmann, D. E. (2011) · BMC Research Notes · doi:10.1186/1756-0500-4-94 · Cited by 17

Mustard Oil in “Shibori Daikon” a Variety of Japanese Radish, Selectively Inhibits the Proliferation of H-ras-Transformed 3Y1 Cells

Yamasaki, M., Yusuke, O. M. I., FUJII, N., Ozaki, A., Nakama, A., Sakakibara, Y., Suiko, M., & Nishiyama, K. (2009) · Bioscience Biotechnology and Biochemistry · doi:10.1271/bbb.90322 · Cited by 17

The contribution of molecular epidemiology to the identification of human carcinogens: current status and future perspectives

Boffetta, P., & Islami, F. (2012) · Annals of Oncology · doi:10.1093/annonc/mds543 · Cited by 17

State 1(T) Inhibitors of Activated Ras

Kalbitzer, H. R., & Spoerner, M. (2013) · The Enzymes · doi:10.1016/b978-0-12-416749-0.00004-x · Cited by 17

KRAS mutation testing in borderline ovarian tumors and low-grade ovarian carcinomas with a rapid, fully integrated molecular diagnostic system

Sadłecki, P., Antosik, P., Grzanka, D., Grabiec, M., & Walentowicz‐Sadlecka, M. (2017) · Tumor Biology · doi:10.1177/1010428317733984 · Cited by 17

A Computational Approach for the Identification of Small GTPases Based on Preprocessed Amino Acid Sequences

Heider, D., Appelmann, J., Bayro, T., Dreckmann, W., Held, A., Winkler, J., Barnekow, A., & Borschbach, M. (2009) · Technology in Cancer Research & Treatment · doi:10.1177/153303460900800503 · Cited by 17

SRJ09, a promising anticancer drug lead: Elucidation of mechanisms of antiproliferative and apoptogenic effects and assessment of in vivo antitumor efficacy

Wong, C. C., Lim, S. H., Sagineedu, S. R., Lajis, N. H., & Stanslas, J. (2016) · Pharmacological Research · doi:10.1016/j.phrs.2016.02.024 · Cited by 17

Correlation of O2 transport on the micro and macro scale.

Honig, C. R., & Gayeski, T. E. (1982) · PubMed · Cited by 17

Exploring the metabolic signaling network of GFPT in cancer

Sampson, C., Li, P., Wang, Y., Liu, J., Lv, J., Xia, T., Piao, H., & Ma, Y. (2025) · Cell Death Discovery · doi:10.1038/s41420-025-02687-3 · Cited by 16

ERK1/2 inhibitors act as monovalent degraders inducing ubiquitylation and proteasome-dependent turnover of ERK2, but not ERK1

Balmanno, K., Kidger, A. M., Byrne, D. P., Sale, M. J., Nassman, N., Eyers, P. A., & Cook, S. J. (2023) · Biochemical Journal · doi:10.1042/bcj20220598 · Cited by 16

Prediction of anti-TNF therapy failure in ulcerative colitis patients by ensemble machine learning: A prospective study

Nazari, M. H. D., Shahrokh, S., Ghanbari-Maman, L., Maleknia, S., Ghorbaninejad, M., & Meyfour, A. (2023) · Heliyon · doi:10.1016/j.heliyon.2023.e21154 · Cited by 16

Differential age-related transcriptomic analysis of ovarian granulosa cells in Kazakh horses

Ren, W., Wang, J., Zeng, Y., Wang, T., Meng, J., & Yao, X. (2024) · Frontiers in Endocrinology · doi:10.3389/fendo.2024.1346260 · Cited by 16

Interface between normal and transformed epithelial cells: A road to a novel type of cancer prevention and treatment

Fujita, Y. (2011) · Cancer Science · doi:10.1111/j.1349-7006.2011.02011.x · Cited by 16

Screens, maps & networks: from genome sequences to personalized medicine

Sandmann, T., & Boutros, M. (2012) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2012.02.001 · Cited by 17

K-Ras promotes the non-small lung cancer cells survival by cooperating with sirtuin 1 and p27 under ROS stimulation

Cheng, D., Zhao, L., Xu, Y., Ou, R., Li, G., Yang, H., & Li, W. (2015) · Tumor Biology · doi:10.1007/s13277-015-3429-8 · Cited by 17

Exploration of Synthetic Lethal Interactions as Cancer Drug Targets

Kuiken, H. J., & Beijersbergen, R. L. (2010) · Future Oncology · doi:10.2217/fon.10.131 · Cited by 16

Deregulated Ras signaling in developmental disorders: new tricks for an old dog

Schubbert, S., Bollag, G. E., & Shannon, K. (2007) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2006.12.004 · Cited by 117

RESEARCH CHALLENGES IN STAGE III AND IV RAS-ASSOCIATED CANCERS: A Narrative Review of the Complexities and Functions of the Family of RAS Genes and Ras Proteins in Housekeeping and Tumorigenesis

McDonald, R. A., Varela-Ramı́rez, A., & Ashley, A. K. (2025) · Biology · doi:10.3390/biology14080936 · Cited by 2

Abstract IA16: RASopathies: the other face of RAS signaling upregulation

Tartaglia, M. (2023) · Molecular Cancer Research · doi:10.1158/1557-3125.ras23-ia16

Hyperactive Ras in developmental disorders and cancer

Schubbert, S., Shannon, K., & Bollag, G. (2007) · Nature Reviews Cancer · doi:10.1038/nrc2109 · Cited by 1,583

Ras in Cancer and Developmental Diseases

Fernández‐Medarde, A., & Santos, E. (2011) · Genes & Cancer · doi:10.1177/1947601911411084 · Cited by 1,001