Molecular assemblies of the catalytic domain of SOS with KRas and oncogenic mutants

Targeting RAS signalling pathways in cancer therapy

Downward, J. (2003) · Nature reviews. Cancer · doi:10.1038/nrc969 · Cited by 3,262 · see citing works

A Comprehensive Survey of Ras Mutations in Cancer

Prior, I. A., Lewis, P. D., & Mattos, C. (2012) · Cancer Research · doi:10.1158/0008-5472.can-11-2612 · Cited by 2,063 · see citing works

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 · see citing works

The Guanine Nucleotide-Binding Switch in Three Dimensions

Vetter, I. R., & Wittinghofer, A. (2001) · Science · doi:10.1126/science.1062023 · Cited by 1,875 · see citing works

Ras oncogenes: split personalities

Karnoub, A. E., & Weinberg, R. A. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2438 · Cited by 1,467 · see citing works

Targeting KRAS mutant cancers with a covalent G12C-specific inhibitor

Janes, M. R., Zhang, J., Li, L.-S., Hansen, R., Peters, U., Guo, X., Chen, Y., Babbar, A., Firdaus, S. J., Darjania, L., et al. (2018) · Cell · doi:10.1016/j.cell.2018.01.006 · Cited by 1,172 · cited 11× · see citing works

Molecular Switch for Signal Transduction: Structural Differences Between Active and Inactive Forms of Protooncogenic ras Proteins

Milburn, M. V., Tong, L., deVos, A. M., Brünger, A. T., Yamaizumi, Z., Nishimura, S., & Kim, S. (1990) · Science · doi:10.1126/science.2406906 · Cited by 1,062 · see citing works

Bayesian Deconvolution of Mass and Ion Mobility Spectra: From Binary Interactions to Polydisperse Ensembles

Marty, M. T., Baldwin, A. J., Marklund, E. G., Hochberg, G. K. A., Benesch, J. L. P., & Robinson, C. V. (2015) · Analytical Chemistry · doi:10.1021/acs.analchem.5b00140 · Cited by 1,000 · see citing works

Ras in Cancer and Developmental Diseases

Fernández‐Medarde, A., & Santos, E. (2011) · Genes & Cancer · doi:10.1177/1947601911411084 · Cited by 959 · see citing works

The power of ion mobility-mass spectrometry for structural characterization and the study of conformational dynamics

Lanucara, F., Holman, S. W., Gray, C. J., & Eyers, C. E. (2014) · Nature Chemistry · doi:10.1038/nchem.1889 · Cited by 901 · see citing works

Human RAS Superfamily Proteins and Related GTPases

Colicelli, J. (2004) · Science s STKE · doi:10.1126/stke.2502004re13 · Cited by 828 · see citing works

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

Vigil, D., Cherfils, J., Rossman, K. L., & Der, C. J. (2010) · Nature reviews. Cancer · doi:10.1038/nrc2960 · Cited by 816 · see citing works

Dragging ras back in the ring

Stephen, A. G., Esposito, D., Bagni, R. K., & McCormick, F. (2014) · Cancer Cell · doi:10.1016/j.ccr.2014.02.017 · Cited by 795 · see citing works

Biochemical and Structural Analysis of Common Cancer-Associated KRAS Mutations

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

Direct small-molecule inhibitors of KRAS: from structural insights to mechanism-based design

Ostrem, J. M. L., & Shokat, K. M. (2016) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2016.139 · Cited by 641 · see citing works

Native Mass Spectrometry: What is in the Name?

Leney, A. C., & Heck, A. J. R. (2017) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-016-1545-3 · Cited by 602 · see citing works

Sending Signals Dynamically

Smock, R. G., & Gierasch, L. M. (2009) · Science · doi:10.1126/science.1169377 · Cited by 508 · see citing works

Structural Evidence for Feedback Activation by Ras·GTP of the Ras-Specific Nucleotide Exchange Factor SOS

Margarit, S. M., Sondermann, H., Hall, B. E., Nagar, B., Hoelz, A., Pirruccello, M., Bar‐Sagi, D., & Kuriyan, J. (2003) · Cell · doi:10.1016/s0092-8674(03)00149-1 · Cited by 486 · see citing works

BI-3406, a Potent and Selective SOS1–KRAS Interaction Inhibitor, Is Effective in KRAS-Driven Cancers through Combined MEK Inhibition

Hofmann, M. H., Gmachl, M., Ramharter, J., Savarese, F., Gerlach, D., Marszalek, J. R., Sanderson, M. P., Kessler, D., Trapani, F., Arnhof, H., et al. (2021) · Cancer Discovery · doi:10.1158/2159-8290.cd-20-0142 · Cited by 444 · see citing works

Discovery of potent SOS1 inhibitors that block RAS activation via disruption of the RAS–SOS1 interaction

Hillig, R. C., Sautier, B., Schroeder, J., Moosmayer, D., Hilpmann, A., Stegmann, C. M., Werbeck, N. D., Briem, H., Boemer, U., Weiske, J., et al. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1812963116 · Cited by 388 · see citing works

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

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

A molecular assembly phase transition and kinetic proofreading modulate Ras activation by SOS

Huang, W. Y. C., Alvarez, S. A., Kondo, Y., Lee, Y. K., Chung, J. K., Lam, H. Y. M., Biswas, K. H., Kuriyan, J., & Groves, J. T. (2019) · Science · doi:10.1126/science.aau5721 · Cited by 352 · see citing works

Structural Analysis of Autoinhibition in the Ras Activator Son of Sevenless

Sondermann, H., Soisson, S. M., Boykevisch, S., Yang, S., Bar‐Sagi, D., & Kuriyan, J. (2004) · Cell · doi:10.1016/j.cell.2004.10.005 · Cited by 315 · see citing works

An orthosteric inhibitor of the Ras-Sos interaction

Patgiri, A., Yadav, K. K., Arora, P. S., & Bar‐Sagi, D. (2011) · Nature Chemical Biology · doi:10.1038/nchembio.612 · Cited by 294 · see citing works

<i>In silico</i> discovery of small-molecule Ras inhibitors that display antitumor activity by blocking the Ras–effector interaction

Shima, F., Yoshikawa, Y., Ye, M., Araki, M., Matsumoto, S., Liao, J., Hu, L., Sugimoto, T., Ijiri, Y., Takeda, A., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1217730110 · Cited by 293 · see citing works

NMR-based functional profiling of RASopathies and oncogenic RAS mutations

Smith, M. J., Neel, B. G., & Ikura, M. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1218173110 · Cited by 257 · see citing works

Membrane-dependent signal integration by the Ras activator Son of sevenless

Gureasko, J. M., Galush, W. J., Boykevisch, S., Sondermann, H., Bar‐Sagi, D., Groves, J. T., & Kuriyan, J. (2008) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1418 · Cited by 257 · see citing works

High-resolution mass spectrometry of small molecules bound to membrane proteins

Gault, J., Donlan, J. A. C., Liko, I., Hopper, J. T. S., Gupta, K., Housden, N. G., Struwe, W. B., Marty, M. T., Mize, T. H., Bechara, C., et al. (2016) · Nature Methods · doi:10.1038/nmeth.3771 · Cited by 237 · see citing works

The Structural Basis of Oncogenic Mutations G12, G13 and Q61 in Small GTPase K-Ras4B

Lu, S., Jang, H., Nussinov, R., & Zhang, J. (2016) · Scientific Reports · doi:10.1038/srep21949 · Cited by 219 · see citing works

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 186 · see citing works

Sos-mediated cross-activation of wild-type Ras by oncogenic Ras is essential for tumorigenesis

Jeng, H., Taylor, L. J., & Bar‐Sagi, D. (2012) · Nature Communications · doi:10.1038/ncomms2173 · Cited by 176 · see citing works

Thermal Dissociation of Multimeric Protein Complexes by Using Nanoelectrospray Mass Spectrometry

Benesch, J. L. P., Sobott, F., & Robinson, C. V. (2003) · Analytical Chemistry · doi:10.1021/ac034132x · Cited by 169 · see citing works

Determining Membrane Protein–Lipid Binding Thermodynamics Using Native Mass Spectrometry

Cong, X., Liu, Y., Liu, W., Liang, X., Russell, D. H., & Laganowsky, A. D. (2016) · Journal of the American Chemical Society · doi:10.1021/jacs.6b01771 · Cited by 166 · see citing works

Ras activation by SOS: Allosteric regulation by altered fluctuation dynamics

Iversen, L., Tu, H.-L., Lin, W.-C., Christensen, S. M., Abel, S. M., Iwig, J., Wu, H.-J., Gureasko, J., Rhodes, C., Petit, R. S., et al. (2014) · Science · doi:10.1126/science.1250373 · Cited by 154 · see citing works

Two decades of studying non-covalent biomolecular assemblies by means of electrospray ionization mass spectrometry

Hilton, G. R., & Benesch, J. L. P. (2012) · Journal of The Royal Society Interface · doi:10.1098/rsif.2011.0823 · Cited by 140 · see citing works

Structure-based Mutagenesis Reveals Distinct Functions for Ras Switch 1 and Switch 2 in Sos-catalyzed Guanine Nucleotide Exchange

Hall, B. E., Yang, S. S., Boriack‐Sjodin, P. A., Kuriyan, J., & Bar‐Sagi, D. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m101727200 · Cited by 132 · see citing works

Melting Proteins: Evidence for Multiple Stable Structures upon Thermal Denaturation of Native Ubiquitin from Ion Mobility Spectrometry-Mass Spectrometry Measurements

El‐Baba, T. J., Woodall, D. W., Raab, S. A., Fuller, D. R., Laganowsky, A. D., Russell, D. H., & Clemmer, D. E. (2017) · Journal of the American Chemical Society · doi:10.1021/jacs.7b02774 · Cited by 123 · see citing works

Isoform-Specific Destabilization of the Active Site Reveals a Molecular Mechanism of Intrinsic Activation of KRas G13D

Johnson, C. W., Lin, Y.-J., Reid, D., Parker, J., Pavlopoulos, S., Dischinger, P., Graveel, C., Aguirre, A. J., Steensma, M., Haigis, K. M., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.07.026 · Cited by 89 · see citing works

Mammalian Son of Sevenless Guanine Nucleotide Exchange Factors: Old Concepts and New Perspectives

Rojas, J. M., Oliva, J. L., & Santos, E. (2011) · Genes & Cancer · doi:10.1177/1947601911408078 · Cited by 88 · see citing works

Allosteric modulation of protein-protein interactions by individual lipid binding events

Cong, X., Liu, Y., Liu, W., Liang, X., & Laganowsky, A. D. (2017) · Nature Communications · doi:10.1038/s41467-017-02397-0 · Cited by 82 · see citing works

Surface-Induced Dissociation of Homotetramers with D2 Symmetry Yields their Assembly Pathways and Characterizes the Effect of Ligand Binding

Quintyn, R. S., Yan, J. R., & Wysocki, V. H. (2015) · Chemistry & Biology · doi:10.1016/j.chembiol.2015.03.019 · Cited by 75 · see citing works

Determination of Protein−Ligand Association Thermochemistry Using Variable-Temperature Nanoelectrospray Mass Spectrometry

Daneshfar, R., Kitova, E. N., & Klassen, J. S. (2004) · Journal of the American Chemical Society · doi:10.1021/ja0316972 · Cited by 73 · see citing works

Inhibitors of Ras–SOS Interactions

Lu, S., Jang, H., Zhang, J., & Nussinov, R. (2016) · ChemMedChem · doi:10.1002/cmdc.201500481 · Cited by 72 · see citing works

Comparative effects of oncogenic mutations G12C, G12V, G13D, and Q61H on local conformations and dynamics of K-Ras

Vatansever, S., Erman, B., & Gumus, Z. H. (2020) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2020.04.003 · Cited by 67 · see citing works

Evidence for Many Unique Solution Structures for Chymotrypsin Inhibitor 2: A Thermodynamic Perspective Derived from vT-ESI-IMS-MS Measurements

Raab, S. A., El‐Baba, T. J., Woodall, D. W., Liu, W., Liu, Y., Baird, Z., Hales, D. A., Laganowsky, A. D., Russell, D. H., & Clemmer, D. E. (2020) · Journal of the American Chemical Society · doi:10.1021/jacs.0c05365 · Cited by 53 · see citing works

Monitoring Ras Interactions with the Nucleotide Exchange Factor Son of Sevenless (Sos) Using Site-specific NMR Reporter Signals and Intrinsic Fluorescence

Vo, U., Vajpai, N., Flavell, L., Bobby, R., Breeze, A. L., Embrey, K. J., & Golovanov, A. P. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.691238 · Cited by 43 · see citing works

Structural mass spectrometry comes of age: new insight into protein structure, function and interactions

Allison, T. M., & Bechara, C. (2019) · Biochemical Society Transactions · doi:10.1042/bst20180356 · Cited by 38 · see citing works

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 · see citing works

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 28 · see citing works

Differences in Flexibility Underlie Functional Differences in the Ras Activators Son of Sevenless and Ras Guanine Nucleotide Releasing Factor 1

Freedman, T. S., Sondermann, H., Kuchment, O., Friedland, G. D., Kortemme, T., & Kuriyan, J. (2009) · Structure · doi:10.1016/j.str.2008.11.004 · Cited by 27 · see citing works

Not all RAS mutations created equal: Functional and clinical characterization of 80 different KRAS and NRAS mutations.

Loree, J. M., Miron, B., Holla, V. R., et al. (2017) · Journal of Clinical Oncology · doi:10.1200/jco.2017.35.15_suppl.3589 · Cited by 10 · see citing works

Targeting KRAS mutant cancers: from druggable therapy to drug resistance

Zhu, C., Guan, X., Zhang, X., Luan, X., Song, Z., Cheng, X., Zhang, W., & Qin, J.-J. (2022) · Molecular Cancer · doi:10.1186/s12943-022-01629-2 · Cited by 231 · see citing works

Assessing the significance of KRAS G12C mutation: Clinicopathologic features, treatments, and survival outcomes in a real-world KRAS mutant non-small cell lung cancer cohort.

Cui, W., Franchini, F., Alexander, M., Officer, A., Wong, H., IJzerman, M. J., Desai, J., & Solomon, B. (2020) · Journal of Clinical Oncology · doi:10.1200/jco.2020.38.15_suppl.e19324 · Cited by 3 · see citing works

Lung Cancer and KRAS -Its Molecular Biology/Genetics and Therapeutic Strategy-

Koga, T., & Mitsudomi, T. (2022) · Haigan · doi:10.2482/haigan.62.188 · Cited by 1 · see citing works

Molecular profile of KRAS G12C-mutant colorectal and non-small-cell lung cancer

(2020) · doi:10.21203/rs.3.rs-108171/v1 · Cited by 2 · see citing works

127P RAS, RAF and NF1 oncogenic mutations in KRAS-mutated lung adenocarcinoma

Marinelli, D., Pisegna, S., Chiavassa, A., et al. (2022) · Annals of Oncology · doi:10.1016/j.annonc.2022.09.128

Molecular profile of KRAS G12C-mutant colorectal and non-small-cell lung cancer

Araujo, L. H., Souza, B. M., Leite, L. R., Parma, S. A. F., Lopes, N. P., Malta, F. S. V., & Freire, M. C. M. (2021) · BMC Cancer · doi:10.1186/s12885-021-07884-8 · Cited by 41 · see citing works