Ras history: The saga continues

A genetic model for colorectal tumorigenesis

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Mutations of the BRAF gene in human cancer

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Cancer statistics, 2009

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An Integrated Genomic Analysis of Human Glioblastoma Multiforme

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IDH1 and IDH2 Mutations in Gliomas

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BAY 43-9006 Exhibits Broad Spectrum Oral Antitumor Activity and Targets the RAF/MEK/ERK Pathway and Receptor Tyrosine Kinases Involved in Tumor Progression and Angiogenesis

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Core Signaling Pathways in Human Pancreatic Cancers Revealed by Global Genomic Analyses

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Systematic RNA interference reveals that oncogenic KRAS-driven cancers require TBK1

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Rab GTPases as coordinators of vesicle traffic

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The Consensus Coding Sequences of Human Breast and Colorectal Cancers

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A Comprehensive Survey of Ras Mutations in Cancer

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Drugging the undruggable RAS: Mission Possible?

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Regulation of Small GTPases by GEFs, GAPs, and GDIs

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RAS isoforms and mutations in cancer at a glance

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Prostate Cancer Review: Genetics, Diagnosis, Treatment Options, and Alternative Approaches

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Targeting the RAS/RAF/MAPK pathway for cancer therapy: from mechanism to clinical studies

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KRAS: The Critical Driver and Therapeutic Target for Pancreatic Cancer

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Ras superfamily GEFs and GAPs: validated and tractable targets for cancer therapy?

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Immunogenicity of somatic mutations in human gastrointestinal cancers

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KRAS: feeding pancreatic cancer proliferation

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Regulating the regulator: post-translational modification of RAS

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The current state of the art and future trends in RAS-targeted cancer therapies

Punekar, S. R., Velcheti, V., Neel, B. G., & Wong, K.-K. (2022) · Nature Reviews Clinical Oncology · doi:10.1038/s41571-022-00671-9 · Cited by 549

Targeting Aberrant RAS/RAF/MEK/ERK Signaling for Cancer Therapy

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Proteomic Analysis of Exosomes from Mutant KRAS Colon Cancer Cells Identifies Intercellular Transfer of Mutant KRAS

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The MAPK and AMPK signalings: interplay and implication in targeted cancer therapy

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A RASopathy gene commonly mutated in cancer: the neurofibromatosis type 1 tumour suppressor

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Differential association of STK11 and TP53 with KRAS mutation-associated gene expression, proliferation and immune surveillance in lung adenocarcinoma

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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

Drugging RAS: know the enemy

Papke, B., & Der, C. J. (2017) · Science · doi:10.1126/science.aam7622 · Cited by 399

Inhibition of Ras for Cancer Treatment: The Search Continues

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Rho guanine nucleotide exchange factors: regulators of Rho GTPase activity in development and disease

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KRAS Alleles: The Devil Is in the Detail

Haigis, K. M. (2017) · Trends in Cancer · doi:10.1016/j.trecan.2017.08.006 · Cited by 373

Ras Conformational Ensembles, Allostery, and Signaling

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Targeting RAS Membrane Association: Back to the Future for Anti-RAS Drug Discovery?

Cox, A. D., Der, C. J., & Philips, M. R. (2015) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-14-3214 · Cited by 351

Myeloid cells are required for PD-1/PD-L1 checkpoint activation and the establishment of an immunosuppressive environment in pancreatic cancer

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MEK inhibition exhibits efficacy in human and mouse neurofibromatosis tumors

Jessen, W. J., Miller, S. J., Jousma, E., Wu, J., Rizvi, T. A., Brundage, M. E., Eaves, D. W., Widemann, B. C., Kim, M., Dombi, E., et al. (2012) · Journal of Clinical Investigation · doi:10.1172/jci60578 · Cited by 345

Molecular epidemiology and diagnostics of KRAS mutations in human cancer

Timar, J., & Kashofer, K. (2020) · Cancer and Metastasis Reviews · doi:10.1007/s10555-020-09915-5 · Cited by 334

KRAS-Mutant non-small cell lung cancer: From biology to therapy

Ferrer, I., Zugazagoitia, J., Herbertz, S., John, W. J., Paz-Ares, L. G., & Schmid‐Bindert, G. (2018) · Lung Cancer · doi:10.1016/j.lungcan.2018.07.013 · Cited by 315

The current understanding of KRAS protein structure and dynamics

Pantsar, T. (2019) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2019.12.004 · Cited by 304

Inhibition of RAS function through targeting an allosteric regulatory site

Spencer-Smith, R., Koide, A., Zhou, Y., Eguchi, R. R., Sha, F., Gajwani, P., Santana, D., Gupta, A., Jacobs, M., Herrero-Garcia, E., et al. (2017) · Nature Chemical Biology · doi:10.1038/nchembio.2231 · Cited by 283

The Ras/ MAPK pathway and hepatocarcinoma: pathogenesis and therapeutic implications

Delire, B., & Stärkel, P. (2015) · European Journal of Clinical Investigation · doi:10.1111/eci.12441 · Cited by 277

Ras-GTP dimers activate the Mitogen-Activated Protein Kinase (MAPK) pathway

Nan, X., Tamgüney, T. M., Collisson, E. A., Lin, L.-J., Pitt, C., Galeas, J., Lewis, S., Gray, J. W., McCormick, F., & Chu, S. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1509123112 · Cited by 273

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

Inhibition of SHP2-mediated dephosphorylation of Ras suppresses oncogenesis

Bunda, S., Burrell, K., Heir, P., Zeng, L., Alamsahebpour, A., Kano, Y., Raught, B., Zhang, Z.-Y., Zadeh, G., & Ohh, M. (2015) · Nature Communications · doi:10.1038/ncomms9859 · Cited by 249

Enhancing CRISPR/Cas gene editing through modulating cellular mechanical properties for cancer therapy

Zhang, D., Wang, G., Yu, X., Wei, T., Farbiak, L., Johnson, L. T., Taylor, A. M., Xu, J., Hong, Y., Zhu, H., et al. (2022) · Nature Nanotechnology · doi:10.1038/s41565-022-01122-3 · Cited by 243

Allosteric Effects of the Oncogenic RasQ61L Mutant on Raf-RBD

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Tipifarnib in Head and Neck Squamous Cell Carcinoma With HRAS Mutations

Ho, A. L., Brana, I., Haddad, R., Bauman, J., Bible, K., Oosting, S., Wong, D. J., Ahn, M.-J., Boni, V., Even, C., et al. (2021) · Journal of Clinical Oncology · doi:10.1200/jco.20.02903 · Cited by 208

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

Drugging Ras GTPase: a comprehensive mechanistic and signaling structural view

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The Ras Superfamily of Small GTPases: The Unlocked Secrets

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KRAS Mutant Pancreatic Cancer: No Lone Path to an Effective Treatment

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Structural basis of recognition of farnesylated and methylated KRAS4b by PDEδ

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The RASopathies: from pathogenetics to therapeutics

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H-Ras forms dimers on membrane surfaces via a protein–protein interface

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Biology of colorectal cancer

Arvelo, F. A. (2015) · ecancermedicalscience · doi:10.3332/ecancer.2015.520 · Cited by 163

Extracellular-Signal Regulated Kinase: A Central Molecule Driving Epithelial–Mesenchymal Transition in Cancer

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Targeting the Small GTPase Superfamily through Their Regulatory Proteins

Gray, J. L., von Delft, F., & Brennan, P. E. (2019) · Angewandte Chemie International Edition · doi:10.1002/anie.201900585 · Cited by 148

Oncogenic K-Ras Binds to an Anionic Membrane in Two Distinct Orientations: A Molecular Dynamics Analysis

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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

Targeting KRAS Mutant Non-Small-Cell Lung Cancer: Past, Present and Future

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The small GTPases K-Ras, N-Ras, and H-Ras have distinct biochemical properties determined by allosteric effects

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Targeting RAS -mutant Cancers: Is ERK the Key?

Ryan, M. B., Der, C. J., Wang‐Gillam, A., & Cox, A. D. (2015) · Trends in cancer · doi:10.1016/j.trecan.2015.10.001 · Cited by 133

Transforming mutations of RAC guanosine triphosphatases in human cancers

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The role of wild type RAS isoforms in cancer

Zhou, B., Der, C. J., & Cox, A. D. (2016) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2016.07.012 · Cited by 130

The RalGEF-Ral Effector Signaling Network: The Road Less Traveled for Anti-Ras Drug Discovery

Neel, N. F., Martin, T. D., Stratford, J. K., Zand, T. P., Reiner, D. J., & Der, C. J. (2011) · Genes & Cancer · doi:10.1177/1947601911407329 · Cited by 134

Structural insights into the BRAF monomer-to-dimer transition mediated by RAS binding

Fiesco, J. A. M., Durrant, D., Morrison, D. K., & Zhang, P. (2022) · Nature Communications · doi:10.1038/s41467-022-28084-3 · Cited by 120

Molecular Mechanisms of Conidial Germination in Aspergillus spp

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Malignant peripheral nerve sheath tumor: models, biology, and translation

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Membrane curvature enables N-Ras lipid anchor sorting to liquid-ordered membrane phases

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Racial and Ethnic Differences in the Epidemiology and Genomics of Lung Cancer

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The Importance of Being PI3K in the RAS Signaling Network

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The complex landscape of pancreatic cancer metabolism

Sousa, C. M., & Kimmelman, A. C. (2014) · Carcinogenesis · doi:10.1093/carcin/bgu097 · Cited by 125

Emerging roles of allosteric modulators in the regulation of protein‐protein interactions (PPIs): A new paradigm for PPI drug discovery

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

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Ral small GTPase signaling and oncogenesis: More than just 15minutes of fame

Gentry, L. R., Martin, T. D., Reiner, D. J., & Der, C. J. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.09.004 · Cited by 116

Vascular smooth muscle cell proliferation as a therapeutic target. Part 1: molecular targets and pathways

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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

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

RAF suppression synergizes with MEK inhibition in KRAS mutant cancer cells

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Ras and autophagy in cancer development and therapy

Schmukler, E., Kloog, Y., & Pinkas‐Kramarski, R. (2014) · Oncotarget · doi:10.18632/oncotarget.1775 · Cited by 110

Ras signaling through RASSF proteins

Donninger, H., Schmidt, M., Mezzanotte-Sharpe, J., Barnoud, T., & Clark, G. J. (2016) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2016.06.007 · Cited by 110

RAL GTPases: Biology and Potential as Therapeutic Targets in Cancer

Yan, C., & Theodorescu, D. (2018) · Pharmacological Reviews · doi:10.1124/pr.117.014415 · Cited by 119

Predictive in vivo animal models and translation to clinical trials

Cook, N., Jodrell, D. I., & Tuveson, D. A. (2012) · Drug Discovery Today · doi:10.1016/j.drudis.2012.02.003 · Cited by 105

Crucial Role of Oncogenic KRAS Mutations in Apoptosis and Autophagy Regulation: Therapeutic Implications

Ferreira, A. I., Pereira, F. D. S., Reis, C. A., Oliveira, M. J., Sousa, M. J., & Preto, A. (2022) · Cells · doi:10.3390/cells11142183 · Cited by 111

Small-Molecule Inhibitors Directly Targeting KRAS as Anticancer Therapeutics

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Src promotes GTPase activity of Ras via tyrosine 32 phosphorylation

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Vascular mimicry: Triggers, molecular interactions and in vivo models

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Structural analysis of the Ras‐like G protein MglA and its cognate GAP MglB and implications for bacterial polarity

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Targeting mutant KRAS with CRISPR-Cas9 controls tumor growth

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Computational and biochemical characterization of two partially overlapping interfaces and multiple weak-affinity K-Ras dimers

Prakash, P., Sayyed–Ahmad, A., Cho, K.-J., Dolino, D. M., Chen, W., Li, H., Grant, B. J., Hancock, J. F., & Gorfe, A. A. (2017) · Scientific Reports · doi:10.1038/srep40109 · Cited by 93

A New View of Ras Isoforms in Cancers

Nussinov, R., Tsai, C., Chakrabarti, M., & Jang, H. (2015) · Cancer Research · doi:10.1158/0008-5472.can-15-1536 · Cited by 92

The discovery of modular binding domains: building blocks of cell signalling

Mayer, B. J. (2015) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm4068 · Cited by 89

Discovery of High-Affinity Noncovalent Allosteric KRAS Inhibitors That Disrupt Effector Binding

McCarthy, M. J., Pagba, C. V., Prakash, P., Naji, A. K., van der Hoeven, D., Liang, H., Gupta, A. K., Zhou, Y., Cho, K.-J., Hancock, J. F., et al. (2019) · ACS Omega · doi:10.1021/acsomega.8b03308 · Cited by 90

Nrf2, but not β‐catenin, mutation represents an early event in rat hepatocarcinogenesis

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Crosstalk of Ras and Rho: activation of RhoA abates Kras-induced liver tumorigenesis in transgenic zebrafish models

Chew, T. W., Liu, X. J., Liu, L., Spitsbergen, J. M., Gong, Z., & Low, B. C. (2013) · Oncogene · doi:10.1038/onc.2013.240 · Cited by 91

Reconstructing targetable pathways in lung cancer by integrating diverse omics data

Balbin, O. A., Prensner, J. R., Sahu, A., Yocum, A. K., Shankar, S., Malik, R., Fermin, D., Dhanasekaran, S. M., Chandler, B. C., Thomas, D. G., et al. (2013) · Nature Communications · doi:10.1038/ncomms3617 · Cited by 90

The Ras switch in structural and historical perspective

Gasper, R., & Wittinghofer, F. (2019) · Biological Chemistry · doi:10.1515/hsz-2019-0330 · Cited by 92

Posttranslational Modifications of RAS ProteinsPreprint

Ahearn, I. M., Zhou, M., & Philips, M. R. (2018) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a031484 · Cited by 89

Targeting small GTPases: emerging grasps on previously untamable targets, pioneered by KRAS

Yin, G., Huang, J., Petela, J., Jiang, H., Zhang, Y., Gong, S., Wu, J., Liu, B., Shi, J., & Gao, Y. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01441-4 · Cited by 98

Oncogene-Driven Metabolic Alterations in Cancer

Min, H., & Lee, H. (2017) · Biomolecules & Therapeutics · doi:10.4062/biomolther.2017.211 · Cited by 88

Rho GTPases—Emerging Regulators of Glucose Homeostasis and Metabolic Health

Møller, L. L. V., Klip, A., & Sylow, L. (2019) · Cells · doi:10.3390/cells8050434 · Cited by 82

Computational Modeling Reveals that Signaling Lipids Modulate the Orientation of K-Ras4A at the Membrane Reflecting Protein Topology

Li, Z., & Buck, M. (2017) · Structure · doi:10.1016/j.str.2017.02.007 · Cited by 80

Spatiotemporal Analysis of K-Ras Plasma Membrane Interactions Reveals Multiple High Order Homo-oligomeric Complexes

Sarkar‐Banerjee, S., Sayyed–Ahmad, A., Prakash, P., Cho, K., Waxham, M. N., Hancock, J. F., & Gorfe, A. A. (2017) · Journal of the American Chemical Society · doi:10.1021/jacs.7b06292 · Cited by 78

K-Ras Populates Conformational States Differently from Its Isoform H-Ras and Oncogenic Mutant K-RasG12D

Parker, J. A., Volmar, A. Y., Pavlopoulos, S., & Mattos, C. (2018) · Structure · doi:10.1016/j.str.2018.03.018 · Cited by 81

A Landscape of Therapeutic Cooperativity in KRAS Mutant Cancers Reveals Principles for Controlling Tumor Evolution

Anderson, G. R., Winter, P. S., Lin, K. H., Nussbaum, D. P., Cakir, M., Stein, E. M., Soderquist, R. S., Crawford, L., Leeds, J. C., Newcomb, R., et al. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.07.006 · Cited by 80

The Ras Superfamily of Small GTPases in Non-neoplastic Cerebral Diseases

Qu, L., Pan, C., He, S., Lang, B., Gao, G.-D., Wang, X., & Wang, Y. (2019) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2019.00121 · Cited by 84

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

The Key Role of Calmodulin in KRAS-Driven Adenocarcinomas

Nussinov, R., Muratcioğlu, S., Tsai, C., Jang, H., Gürsoy, A., & Keskin, Ö. (2015) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-15-0165 · Cited by 78

Direct Modulation of Small GTPase Activity and Function

Cromm, P. M., Spiegel, J., Grossmann, T. N., & Waldmann, H. (2015) · Angewandte Chemie International Edition · doi:10.1002/anie.201504357 · Cited by 80

YAP/TAZ Activation Drives Uveal Melanoma Initiation and Progression

Li, H., Li, Q., Dang, K., Ma, S., Cotton, J. L., Yang, S., Zhu, L. J., DENG, A. C., Ip, Y. T., Johnson, R. L., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.03.021 · Cited by 77

Flashback in the history of Ras research

Chaldaiopoulou, G., Γουλιελμάκη, Μ., Khoury, N., Ζουμπουρλής, Β., & Zoumpourlis (2017) · National Hellenic Research Foundation Helios Repository (National Hellenic Research Foundation)

Ras Stories: The State of the Art

Roberts, P. J., & Der, C. J. (2006) · Springer eBooks · doi:10.1007/1-4020-4708-8_1

The Ras Superfamily of Small GTPases: The Unlocked Secrets

Goitre, L., Trapani, E., Trabalzini, L., & Retta, S. F. (2013) · Methods in molecular biology · doi:10.1007/978-1-62703-791-4_1 · Cited by 195

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

Ras Proteins☆

George, S., & Der, C. J. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-801238-3.98756-7