Ras history: The saga continues

A genetic model for colorectal tumorigenesis

Fearon, E. R., & Vogelstein, B. (1990) · Cell · doi:10.1016/0092-8674(90)90186-i · Cited by 12,132

Mutations of the BRAF gene in human cancer

Davies, H., Bignell, G. R., Cox, C., Stephens, P., Edkins, S., Clegg, S., Teague, J., Woffendin, H., Garnett, M. J., Bottomley, W., et al. (2002) · Nature · doi:10.1038/nature00766 · Cited by 10,674

Cancer statistics, 2009

Jemal, A., Siegel, R., Ward, E., Hao, Y., Xu, J., & Thun, M. J. (2009) · CA: A Cancer Journal for Clinicians · doi:10.3322/caac.20006 · Cited by 9,709

An Integrated Genomic Analysis of Human Glioblastoma Multiforme

Parsons, D. W., Jones, S., Zhang, X., Lin, J. C.-H., Leary, R. J., Angenendt, P., Mankoo, P., Carter, H., Siu, I.-M., Gallia, G. L., et al. (2008) · Science · doi:10.1126/science.1164382 · Cited by 5,857

IDH1 and IDH2 Mutations in Gliomas

Yan, H., Parsons, D. W., Jin, G., McLendon, R., Rasheed, B. A., Yuan, W., Kos, I., Batinic-Haberle, I., Jones, S., Riggins, G. J., et al. (2009) · New England Journal of Medicine · doi:10.1056/nejmoa0808710 · Cited by 5,847

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

Wilhelm, S. M., Carter, C., Tang, L., Wilkie, D. P., McNabola, A., Rong, H., Chen, C., Zhang, X., Vincent, P. W., McHugh, M., et al. (2004) · Cancer Research · doi:10.1158/0008-5472.can-04-1443 · Cited by 4,060

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

Jones, S., Zhang, X., Parsons, D. W., Lin, J. C.-H., Leary, R. J., Angenendt, P., Mankoo, P., Carter, H., Kamiyama, H., Jimeno, A., et al. (2008) · Science · doi:10.1126/science.1164368 · Cited by 3,969

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

Barbie, D. A., Tamayo, P., Boehm, J. S., Kim, S. Y., Moody, S. E., Dunn, I. F., Schinzel, A. C., Sandy, P., Meylan, E., Scholl, C., et al. (2009) · Nature · doi:10.1038/nature08460 · Cited by 3,922

Rab GTPases as coordinators of vesicle traffic

Stenmark, H. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2728 · Cited by 3,413

The Consensus Coding Sequences of Human Breast and Colorectal Cancers

Sjöblom, T., Jones, S., Wood, L. D., Parsons, D. W., Lin, J., Barber, T. D., Mandelker, D. L., Leary, R. J., Ptak, J., Silliman, N., et al. (2006) · Science · doi:10.1126/science.1133427 · Cited by 3,161

Topological and Functional Properties of the Small GTPases Protein Interaction Network

Delprato, A. (2012) · PLoS ONE · doi:10.1371/journal.pone.0044882 · Cited by 40

In Silico Strategies for Designing of Peptide Inhibitors of Oncogenic K-Ras G12V Mutant: Inhibiting Cancer Growth and Proliferation

Ghufran, M., Khan, H. A., Ullah, M., Ghufran, S., Ayaz, M., Siddiq, M., Hassan, S. S. U., & BUNGAU, S. G. (2022) · Cancers · doi:10.3390/cancers14194884 · Cited by 39

In vitro prediction of the efficacy of molecularly targeted cancer therapy by Raman spectral imaging

Yosef, H. K., Mavarani, L., Maghnouj, A., Hahn, S. A., El‐Mashtoly, S. F., & Gerwert, K. B. (2015) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-015-8875-z · Cited by 40

Intrinsic GTPase activity of K-RAS monitored by native mass spectrometry

Moghadamchargari, Z., Huddleston, J., Shirzadeh, M., Zheng, X., Clemmer, D. E., M. Raushel, F., Russell, D. H., & Laganowsky, A. (2019) · Biochemistry · doi:10.1021/acs.biochem.9b00532 · Cited by 38

New structural and functional insight into the regulation of Ras

Kano, Y., Cook, J. D., Lee, J. E., & Ohh, M. (2016) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2016.06.006 · Cited by 38

Behind the Wheel of Epithelial Plasticity in KRAS-Driven Cancers

Arner, E. N., Du, W., & Brekken, R. A. (2019) · Frontiers in Oncology · doi:10.3389/fonc.2019.01049 · Cited by 40

Photosensitizers Based on G-Quadruplex Ligand for Cancer Photodynamic Therapy

Kawauchi, K., Urano, R., Kinoshita, N., Kuwamoto, S., Torii, T., Hashimoto, Y., Taniguchi, S., Tsuruta, M., & Miyoshi, D. (2020) · Genes · doi:10.3390/genes11111340 · Cited by 41

Computationally designed sensors detect endogenous Ras activity and signaling effectors at subcellular resolution

Zhang, J. Z., Nguyen, W. H., Greenwood, N., Rose, J. C., Ong, S.-E., Maly, D. J., & Baker, D. (2024) · Nature Biotechnology · doi:10.1038/s41587-023-02107-w · Cited by 37

Specific Substates of Ras To Interact with GAPs and Effectors: Revealed by Theoretical Simulations and FTIR Experiments

Li, Y., Zhang, Y., Großerueschkamp, F., Stephan, S., Cui, Q., Kötting, C., Xia, F., & Gerwert, K. B. (2018) · The Journal of Physical Chemistry Letters · doi:10.1021/acs.jpclett.8b00342 · Cited by 35

Approaches to inhibiting oncogenic K-Ras

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

κB-Ras and Ral GTPases regulate acinar to ductal metaplasia during pancreatic adenocarcinoma development and pancreatitis

Beel, S., Kolloch, L. J., Apken, L. H., Jürgens, L., Bolle, A., Sudhof, N., Ghosh, S., Wardelmann, E., Meisterernst, M., Steinestel, K., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-17226-0 · Cited by 37

A human model of arteriovenous malformation (AVM)-on-a-chip reproduces key disease hallmarks and enables drug testing in perfused human vessel networks

Soon, K., Li, M., Wu, R., Zhou, A., Khosraviani, N., Turner, W. D., Wythe, J. D., Fish, J. E., & Nunes, S. S. (2022) · Biomaterials · doi:10.1016/j.biomaterials.2022.121729 · Cited by 35

HRAS Mutations Define a Distinct Subgroup in Head and Neck Squamous Cell Carcinoma

Coleman, N., Marcelo, K. L., Hopkins, J. F., Khan, N., Du, R. R., Hong, L., Park, E., Balsara, B., Leoni, M., Pickering, C. R., et al. (2023) · JCO Precision Oncology · doi:10.1200/po.22.00211 · Cited by 36

Time-resolved FTIR spectroscopy for monitoring protein dynamics exemplified by functional studies of Ras protein bound to a lipid bilayer

Kötting, C., Güldenhaupt, J., & Gerwert, K. B. (2011) · Chemical Physics · doi:10.1016/j.chemphys.2011.08.007 · Cited by 36

Absolute Quantification of Endogenous Ras Isoform Abundance

Mageean, C. J., Griffiths, J. R., Smith, D. L., Clague, M. J., & Prior, I. A. (2015) · PLoS ONE · doi:10.1371/journal.pone.0142674 · Cited by 36

Detailed Structure of the H2PO4––Guanosine Diphosphate Intermediate in Ras-GAP Decoded from FTIR Experiments by Biomolecular Simulations

Xia, F., Rudack, T., Cui, Q., Kötting, C., & Gerwert, K. B. (2012) · Journal of the American Chemical Society · doi:10.1021/ja310496e · Cited by 36

Diverse genetic architectures lead to the same cryptic phenotype in a yeast cross

Taylor, M. B., Phan, J. L., Lee, J. T., McCadden, M., & Ehrenreich, I. M. (2016) · Nature Communications · doi:10.1038/ncomms11669 · Cited by 34

The Intrinsic GDP/GTP Exchange Activities of Cdc42 and Rac1 Are Critical Determinants for Their Specific Effects on Mobilization of the Actin Filament System

Aspenström, P. (2019) · Cells · doi:10.3390/cells8070759 · Cited by 39

Oncoprotein-specific molecular interaction maps (SigMaps) for cancer network analyses

Broyde, J., Simpson, D. R., Murray, D., Paull, E., Chu, B., Tagore, S., Jones, S. J., Griffin, A. T., Giorgi, F. M., Lachmann, A., et al. (2020) · Nature Biotechnology · doi:10.1038/s41587-020-0652-7 · Cited by 33

Inside Out: Targeting NHE1 as an Intracellular and Extracellular Regulator of Cancer Progression

Provost, J. J., & Wallert, M. A. (2012) · Chemical Biology & Drug Design · doi:10.1111/cbdd.12035 · Cited by 36

The Allosteric Switch and Conformational States in Ras GTPase Affected by Small Molecules

Johnson, C. W., & Mattos, C. (2013) · The Enzymes · doi:10.1016/b978-0-12-416749-0.00003-8 · Cited by 35

Structure, signaling and the drug discovery of the Ras oncogene protein

Han, C. W., Jeong, M. S., & Jang, S. B. (2017) · BMB Reports · doi:10.5483/bmbrep.2017.50.7.062 · Cited by 38

Coordinating ERK signaling via the molecular scaffold Kinase Suppressor of Ras

Frodyma, D. E., Neilsen, B. K., Costanzo-Garvey, D. L., Fisher, K. W., & Lewis, R. E. (2017) · F1000Research · doi:10.12688/f1000research.11895.1 · Cited by 37

Discovery of Quinazolines That Activate SOS1-Mediated Nucleotide Exchange on RAS

Abbott, J. R., Patel, P. A., Howes, J. E., Akan, D. T., Kennedy, J. P., Burns, M. C., Browning, C. F., Sun, Q., Rossanese, O. W., Phan, J., et al. (2018) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.8b00296 · Cited by 37

Isoform-specific Ras signaling is growth factor dependent

Hood, F. E., Klinger, B., Newlaczyl, A. U., Sieber, A., Dorel, M., Oliver, S. P., Coulson, J. M., Blüthgen, N., & Prior, I. A. (2019) · Molecular Biology of the Cell · doi:10.1091/mbc.e18-10-0676 · Cited by 35

NF1 Regulates Apoptosis in Ovarian Cancer Cells by Targeting MCL1 via miR-142–5p

Su, J., Ruan, S., Dai, S., Mi, J., Chen, W., & Jiang, S. (2018) · Pharmacogenomics · doi:10.2217/pgs-2018-0161 · Cited by 34

pMD-Membrane: A Method for Ligand Binding Site Identification in Membrane-Bound Proteins

Prakash, P., Sayyed–Ahmad, A., & Gorfe, A. A. (2015) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1004469 · Cited by 36

Clinical significance of HRAS and KRAS genes expression in patients with non–small-cell lung cancer - preliminary findings

Pązik, M., Michalska, K., Żebrowska-Nawrocka, M., Zawadzka, I., Łochowski, M. P., & Balcerczak, E. I. (2021) · BMC Cancer · doi:10.1186/s12885-021-07858-w · Cited by 34

Small molecule Son of Sevenless 1 (SOS1) inhibitors: a review of the patent literature

Thompson, S. K., Buckl, A. K., Dossetter, A. G., Griffen, E., & Gill, A. L. (2021) · Expert Opinion on Therapeutic Patents · doi:10.1080/13543776.2021.1952984 · Cited by 35

Discovery of Sulfonamide-Derived Agonists of SOS1-Mediated Nucleotide Exchange on RAS Using Fragment-Based Methods

Sarkar, D., Olejniczak, E. T., Phan, J., Coker, J. A., Sai, J., Arnold, A. L., Beesetty, Y., Waterson, A. G., & Fesik, S. W. (2020) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.0c00511 · Cited by 33

Identification of novel peptide inhibitors for the KRas-G12C variant to prevent oncogenic signaling

Ajmal, A., Ali, Y., Khan, A., Wadood, A., & Rehman, A. U. (2022) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2022.2138550 · Cited by 32

KRAS-Mutant Lung Cancer: Targeting Molecular and Immunologic Pathways, Therapeutic Advantages and Restrictions

Karimi, N., & Moghaddam, S. J. (2023) · Cells · doi:10.3390/cells12050749 · Cited by 37

Overview of simulation studies on the enzymatic activity and conformational dynamics of the GTPase Ras

Prakash, P., & Gorfe, A. A. (2014) · Molecular Simulation · doi:10.1080/08927022.2014.895000 · Cited by 31

KRAS-Mutant Non-Small-Cell Lung Cancer: From Past Efforts to Future Challenges

Ceddia, S., Landi, L. M., & Cappuzzo, F. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23169391 · Cited by 35

Fragment-based drug discovery of triazole inhibitors to block PDEδ-RAS protein-protein interaction

Chen, D., Chen, Y., Lian, F., Chen, L., Li, Y., Cao, D., Wang, X., Chen, L., Li, J., Meng, T., et al. (2019) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2018.12.018 · Cited by 31

Role of the small GTPase Rho1 in cell wall integrity, stress response, and pathogenesis of Aspergillus fumigatus

Zhang, X., Jia, X., Tian, S., Zhang, C., Lu, Z., Chen, Y., Chen, F., Li, Z., Su, X., Han, X., et al. (2018) · Fungal Genetics and Biology · doi:10.1016/j.fgb.2018.09.003 · Cited by 31

Upstream regulators of phosphoinositide 3‐kinase and their role in diseases

Wang, D., Zhou, W., Chen, J., & Wei, W. (2019) · Journal of Cellular Physiology · doi:10.1002/jcp.28215 · Cited by 31

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

Conformational Dynamics Allows Sampling of an “Active-like” State by Oncogenic K-Ras-GDP

Grudzien, P. K., Jang, H., Leschinsky, N., Nussinov, R., & Gaponenko, V. (2022) · Journal of Molecular Biology · doi:10.1016/j.jmb.2022.167695 · Cited by 30

Combined Rational Design and a High Throughput Screening Platform for Identifying Chemical Inhibitors of a Ras-activating Enzyme

Evelyn, C. R., Biesiada, J., Duan, X., Tang, H. M., Shang, X., Papoian, R., Seibel, W. L., Nelson, S. L., Meller, J., & Zheng, Y. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.634493 · Cited by 32

Ubiquitination

de la Vega, M., Burrows, J. F., & Johnston, J. A. (2011) · Small GTPases · doi:10.4161/sgtp.2.4.16707 · Cited by 31

Oncogenic KRAS engages an RSK1/NF1 pathway to inhibit wild-type RAS signaling in pancreatic cancer

Cheng, D. K., Oni, T. E., Thalappillil, J. S., Park, Y., Ting, H.-C., Alagesan, B., Prasad, N. V., Addison, K., Rivera, K. D., Pappin, D. J., et al. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2016904118 · Cited by 30

Molecular Dynamics Simulations and Dynamic Network Analysis Reveal the Allosteric Unbinding of Monobody to H-Ras Triggered by R135K Mutation

Ni, D., Song, K., Zhang, J., & Lu, S. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18112249 · Cited by 30

Characterization With KRAS Mutant Is a Critical Determinant in Immunotherapy and Other Multiple Therapies for Non-Small Cell Lung Cancer

Shen, M., Qi, R., Ren, J., Lv, D., & Yang, H. (2022) · Frontiers in Oncology · doi:10.3389/fonc.2021.780655 · Cited by 31

Development of Son of Sevenless Homologue 1 (SOS1) Modulators To Treat Cancers by Regulating RAS Signaling

Luo, G., Wang, B., Hou, Q., & Wu, X. (2023) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.2c01729 · Cited by 30

Ras Signaling Inhibitors Attenuate Disease in Adjuvant-Induced Arthritis via Targeting Pathogenic Antigen-Specific Th17-Type Cells

Zayoud, M., Marcu‐Malina, V., Vax, E., Jacob‐Hirsch, J., Elad‐Sfadia, G., Barshack, I., Kloog, Y., & Goldstein, I. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.00799 · Cited by 30

The evolution of cancer immunotherapy: a comprehensive review of its history and current perspectives

Ahuja, S., & Zaheer, S. (2024) · Korean Journal of Clinical Oncology · doi:10.14216/kjco.24009 · Cited by 31

The Interaction of CCDC104/BARTL1 with Arl3 and Implications for Ciliary Function

Lokaj, M., Kösling, S. K., Koerner, C., Lange, S. M., van Beersum, S. E. C., van Reeuwijk, J., Roepman, R., Horn, N., Ueffing, M., Boldt, K., et al. (2015) · Structure · doi:10.1016/j.str.2015.08.016 · Cited by 28

Catalysis of GTP Hydrolysis by Small GTPases at Atomic Detail by Integration of X-ray Crystallography, Experimental, and Theoretical IR Spectroscopy

Rudack, T., Jenrich, S., Brucker, S., Vetter, I. R., Gerwert, K. B., & Kötting, C. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.648071 · Cited by 29

IL-17 Exerts Anti-Apoptotic Effect via miR-155-5p Downregulation in Experimental Autoimmune Encephalomyelitis

Ksiazek-Winiarek, D., Szpakowski, P., Turniak, M., Szemraj, J., & Glabinski, A. (2017) · Journal of Molecular Neuroscience · doi:10.1007/s12031-017-0981-2 · Cited by 26

Computationally Empowered Workflow Identifies Novel Covalent Allosteric Binders for KRASG12C

Mortier, J., Friberg, A., Badock, V., Moosmayer, D., Schroeder, J., Steigemann, P., Siegel, F., Gradl, S., Bauser, M., Hillig, R. C., et al. (2020) · ChemMedChem · doi:10.1002/cmdc.201900727 · Cited by 29

Inhibition of Nonfunctional Ras

Nussinov, R., Jang, H., Gürsoy, A., Keskin, Ö., & Gaponenko, V. (2021) · Cell chemical biology · doi:10.1016/j.chembiol.2020.12.012 · Cited by 29

Small-Molecule RAS Inhibitors as Anticancer Agents: Discovery, Development, and Mechanistic Studies

Shetu, S. A., & Bandyopadhyay, D. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23073706 · Cited by 31

Mechanisms of resistance to KRASG12C inhibitors in KRASG12C-mutated non-small cell lung cancer

Chour, A., Toffart, A., Berton, E., & Duruisseaux, M. (2024) · Frontiers in Oncology · doi:10.3389/fonc.2024.1328728 · Cited by 33

What vibrations tell us about GTPases

Kötting, C., & Gerwert, K. B. (2014) · Biological Chemistry · doi:10.1515/hsz-2014-0219 · Cited by 28

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

Computational allosteric ligand binding site identification on Ras proteins

McCarthy, M. J., Prakash, P., & Gorfe, A. A. (2015) · Acta Biochimica et Biophysica Sinica · doi:10.1093/abbs/gmv100 · Cited by 29

miR-331-3p and Aurora Kinase inhibitor II co-treatment suppresses prostate cancer tumorigenesis and progression

Epis, M. R., Giles, K. M., Beveridge, D. J., Richardson, K. L., Candy, P. A., Stuart, L. M., Bentel, J. M., Cohen, R. J., & Leedman, P. J. (2017) · Oncotarget · doi:10.18632/oncotarget.18664 · Cited by 26

A Historic Perspective and Overview of H-Ras Structure, Oncogenicity, and Targeting

Shu, L., Wang, D., Saba, N. F., & Chen, Z. G. (2020) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-19-0660 · Cited by 27

Prognostic value of KRAS mutation status in colorectal cancer patients: a population-based competing risk analysis

Dai, D., Wang, Y., Zhu, L., Jin, H., & Wang, X. (2020) · PeerJ · doi:10.7717/peerj.9149 · 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

Ras and Rheb Signaling in Survival and Cell Death

Ehrkamp, A., Herrmann, C., Stoll, R., & Heumann, R. (2013) · Cancers · doi:10.3390/cancers5020639 · Cited by 27

Therapeutic targeting of protein S-acylation for the treatment of disease

Fraser, N. J., Howie, J., Wypijewski, K. J., & Fuller, W. (2019) · Biochemical Society Transactions · doi:10.1042/bst20190707 · Cited by 29

The role of miR-190a in methylglyoxal-induced insulin resistance in endothelial cells

Mirra, P., Nigro, C., Prevenzano, I., Procopio, T., Leone, A., Raciti, G. A., Andreozzi, F., Longo, M., Fiory, F., Bèguinot, F., et al. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2016.11.018 · Cited by 27

Computational Insights into the Interactions between Calmodulin and the c/nSH2 Domains of p85α Regulatory Subunit of PI3Kα: Implication for PI3Kα Activation by Calmodulin

Ni, D., Liu, D., Zhang, J., & Lu, S. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19010151 · Cited by 26

Development of a High-throughput NanoBRET Screening Platform to Identify Modulators of the RAS/RAF Interaction

Durrant, D., Smith, E. A., Goncharova, E. I., Sharma, N. D., Alexander, P., Stephen, A. G., Henrich, C. J., & Morrison, D. K. (2021) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-21-0175 · Cited by 25

Computational investigation to identify potent inhibitors of the GTPase-Kirsten RAt sarcoma virus (K-Ras) mutants G12C and G12D

Kumar, S. U., & Doss, C. G. P. (2021) · Computers in Biology and Medicine · doi:10.1016/j.compbiomed.2021.104946 · Cited by 26

CRISPR prime editing for unconstrained correction of oncogenic KRAS variants

Jang, G., Kweon, J., & Kim, Y. (2023) · Communications Biology · doi:10.1038/s42003-023-05052-1 · Cited by 30

Ras inhibition boosts galectin-7 at the expense of galectin-1 to sensitize cells to apoptosis

Barkan, B., Cox, A. D., & Kloog, Y. (2013) · Oncotarget · doi:10.18632/oncotarget.844 · Cited by 26

Glycyrrhetinic acid binds to the conserved P-loop region and interferes with the interaction of RAS-effector proteins

Zhang, Y., Wang, Z., Ma, X., Yang, S., Hu, X., Tao, J., Hou, Y., & Bai, G. (2018) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2018.11.002 · Cited by 25

Conformational Fluctuations in GTP-Bound K-Ras: A Metadynamics Perspective with Harmonic Linear Discriminant Analysis

Wang, X. (2021) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.1c00844 · Cited by 23

The glucocorticoid receptor associates with RAS complexes to inhibit cell proliferation and tumor growth

Caratti, B., Fidan, M., Caratti, G., Breitenecker, K., Engler, M., Kazemitash, N., Traut, R., Wittig, R., Casanova, E., Ahmadian, M. R., et al. (2022) · Science Signaling · doi:10.1126/scisignal.abm4452 · Cited by 26

Common mechanisms of catalysis in small and heterotrimeric GTPases and their respective GAPs

Gerwert, K. B., Mann, D., & Kötting, C. (2017) · Biological Chemistry · doi:10.1515/hsz-2016-0314 · Cited by 25

Exploiting RAS Nucleotide Cycling as a Strategy for Drugging RAS-Driven Cancers

Mattox, T. E., Chen, X., Maxuitenko, Y. Y., Keeton, A. B., & Piazza, G. A. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms21010141 · Cited by 25

Numerical Investigation on Dynamical Response of Aluminum Foam Subject to Hypervelocity Impact With Material Point Method

Gong, W., Liu, Y., Zhang, X., & Ma, H. (2012) · Computer Modeling in Engineering & Sciences · doi:10.3970/cmes.2012.083.527 · Cited by 25

Icotinib: activity and clinical application in Chinese patients with lung cancer

Guan, Y., He, Q., & Li, M. (2014) · Expert Opinion on Pharmacotherapy · doi:10.1517/14656566.2014.890183 · Cited by 24

The molecular functions of RIT1 and its contribution to human disease

Van, R., Cuevas-Navarro, A., Castel, P., & McCormick, F. P. (2020) · Biochemical Journal · doi:10.1042/bcj20200442 · Cited by 24

Siah2 integrates mitogenic and extracellular matrix signals linking neuronal progenitor ciliogenesis with germinal zone occupancy

Ong, T., Trivedi, N., Wakefield, R., Frase, S., & Solecki, D. J. (2020) · Nature Communications · doi:10.1038/s41467-020-19063-7 · Cited by 25

Effect of the Up-Regulation of Circular RNA Hsa_circ_0069767 Derived from C-KIT on the Biological Behavior of Multiple Myeloma Cells

Chen, F., Wang, X., Fu, S., Wang, S., Fu, Y., Liu, Z., & Zhang, J. (2020) · Cancer Management and Research · doi:10.2147/cmar.s259393 · Cited by 24

Determinants of Membrane Orientation Dynamics in Lipid-Modified Small GTPases

Prakash, P., & Gorfe, A. A. (2021) · JACS Au · doi:10.1021/jacsau.1c00426 · Cited by 23

Mouse models of Kras activation in gastric cancer

Won, Y., & Choi, E.-Y. K. (2022) · Experimental & Molecular Medicine · doi:10.1038/s12276-022-00882-1 · Cited by 23

RAS‐targeted cancer therapy: Advances in drugging specific mutations

Liu, C., Ye, D., Yang, H., Chen, X., Su, Z., Li, X., Ding, M., & Liu, Y. (2023) · MedComm · doi:10.1002/mco2.285 · Cited by 25

Climbing RAS, the Everest of Oncogenes

Russo, M., Nicolantonio, F. D., & Bardelli, A. (2014) · Cancer Discovery · doi:10.1158/2159-8290.cd-13-0906 · Cited by 25

Higher order signaling: ARL2 as regulator of both mitochondrial fusion and microtubule dynamics allows integration of 2 essential cell functions

Francis, J. W., Turn, R. E., Newman, L. E., Schiavon, C. R., & Kahn, R. (2016) · Small GTPases · doi:10.1080/21541248.2016.1211069 · Cited by 24

Single-molecule fluorescence imaging of RalGDS on cell surfaces during signal transduction from Ras to Ral

Yoshizawa, R., Umeki, N., Yanagawa, M., Murata, M., & Sako, Y. (2017) · Biophysics and Physicobiology · doi:10.2142/biophysico.14.0_75 · Cited by 23

Diversity of mechanisms in Ras–GAP catalysis of guanosine triphosphate hydrolysis revealed by molecular modeling

Grigorenko, B. L., Kots, E. D., & Nemukhin, A. V. (2019) · Organic & Biomolecular Chemistry · doi:10.1039/c9ob00463g · Cited by 24

Origin and Evolution of RAS Membrane Targeting

García‐España, A., & Philips, M. R. (2023) · Oncogene · doi:10.1038/s41388-023-02672-z · Cited by 23

Dimerization Opens New Avenues into Ras Signaling Research

Santos, E. (2014) · Science Signaling · doi:10.1126/scisignal.2005318 · Cited by 23

Targeting RAS in pediatric cancer: is it becoming a reality?

Vaseva, A. V., & Yohe, M. E. (2019) · Current Opinion in Pediatrics · doi:10.1097/mop.0000000000000856 · Cited by 24

How Anionic Lipids Affect Spatiotemporal Properties of KRAS4B on Model Membranes

Ngo, V. A., Sarkar, S., Neale, C., & Garcı́a, A. E. (2020) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.0c02642 · Cited by 22

Targeting RAS in neuroblastoma: Is it possible?

Lin, L., Miao, L., Lin, H., Cheng, J., Li, M., Zhuo, Z., & He, J. (2021) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2021.108054 · Cited by 24

Cross-species analysis of LZTR1 loss-of-function mutants demonstrates dependency to RIT1 orthologs

Cuevas-Navarro, A., Rodríguez-Muñoz, L., Grego‐Bessa, J., Cheng, A., Rauen, K. A., Urisman, A., McCormick, F., Jimenez, G., & Castel, P. (2022) · eLife · doi:10.7554/elife.76495 · Cited by 23

CRISPR-induced RASGAP deficiencies in colorectal cancer organoids reveal that only loss of NF1 promotes resistance to EGFR inhibition

Post, J. B., Hami, N., Mertens, A. E. E., Elfrink, S., Bos, J. L., & Snippert, H. J. G. (2019) · Oncotarget · doi:10.18632/oncotarget.26677 · Cited by 23

Acylpeptide hydrolase is a novel regulator of KRAS plasma membrane localization and function

Tan, L., Cho, K., Kattan, W. E., Garrido, C. M., Zhou, Y., Neupane, P., Capon, R. J., & Hancock, J. F. (2019) · Journal of Cell Science · doi:10.1242/jcs.232132 · Cited by 23

Targeting KRASG12C in Non-Small-Cell Lung Cancer: Current Standards and Developments

Torres-Jiménez, J., Espinar, J. B., Bote, H., Berjaga, M. Z., Esteban-Villarrubia, J., Fraile, J. Z., & Paz-Ares, L. G. (2024) · Drugs · doi:10.1007/s40265-024-02030-7 · Cited by 24

Structural dynamics in the evolution of a bilobed protein scaffold

Gouridis, G., Muthahari, Y. A., de Boer, M., Griffith, D. A., Tsirigotaki, A., Tassis, K., Zijlstra, N., Xu, R., Eleftheriadis, N., Sugijo, Y., et al. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2026165118 · Cited by 25

Direct GDP-KRAS G12C inhibitors and mechanisms of resistance: the tip of the iceberg

Rosen, J. C., Sacher, A. G., & Tsao, M. (2023) · Therapeutic Advances in Medical Oncology · doi:10.1177/17588359231160141 · Cited by 22

A New Strategy to Control and Eradicate “Undruggable” Oncogenic K-RAS-Driven Pancreatic Cancer: Molecular Insights and Core Principles Learned from Developmental and Evolutionary Biology

Sciver, R. E. V., Lee, M., Lee, C. G. L., Lafever, A., Svyatova, E. A., Kanda, K., Collier, A. L., van Reesema, L. L. S., Tang-Tan, A. M., Zheleva, V. P., et al. (2018) · Cancers · doi:10.3390/cancers10050142 · Cited by 21

Functional diversity in the RAS subfamily of small GTPases

Astrain, G. B., Nikolova, M., & Smith, M. J. (2022) · Biochemical Society Transactions · doi:10.1042/bst20211166 · Cited by 21

Genome Editing Approaches with CRISPR/Cas9 for Cancer Treatment: Critical Appraisal of Preclinical and Clinical Utility, Challenges, and Future Research

Chira, S., Nutu, A. M., Isachesku, E., Bica, C., Pop, L., Ciocan, C. A., & Berindan‐Neagoe, I. (2022) · Cells · doi:10.3390/cells11182781 · Cited by 24

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