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

The emerging hallmarks of cancer metabolism

Pavlova, N. N., & Thompson, C. B. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2015.12.006 · Cited by 5,926 · see citing works

The Activated Complex in Chemical Reactions

Eyring, H. (1935) · The Journal of Chemical Physics · doi:10.1063/1.1749604 · Cited by 5,236 · see citing works

The GTPase superfamily: conserved structure and molecular mechanism

Bourne, H. R., Sanders, D. A., & McCormick, F. (1991) · Nature · doi:10.1038/349117a0 · Cited by 3,392 · see citing works

Targeting RAS signalling pathways in cancer therapy

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

COSMIC: mining complete cancer genomes in the Catalogue of Somatic Mutations in Cancer

Forbes, S. A., Bindal, N., Bamford, S., Cole, C., Kok, C. Y., Beare, D., Jia, M., Shepherd, R., Leung, K., Menzies, A., et al. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkq929 · Cited by 2,278 · see citing works

An improved assay for nanomole amounts of inorganic phosphate

Lanzetta, P. A., Alvarez, L. J., Reinach, P. S., & Candia, O. A. (1979) · Analytical Biochemistry · doi:10.1016/0003-2697(79)90115-5 · Cited by 2,150 · 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

RAS oncogenes: the first 30 years

Malumbres, M., & Barbacid, M. (2003) · Nature Reviews Cancer · doi:10.1038/nrc1097 · Cited by 1,902 · 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: weaving a tumorigenic web

Pylayeva-Gupta, Y., Grabocka, E., & Bar-Sagi, D. (2011) · Nature Reviews Cancer · doi:10.1038/nrc3106 · Cited by 1,789 · see citing works

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 · see citing works

The Ras superfamily at a glance

Wennerberg, K., Rossman, K. L., & Der, C. J. (2005) · Journal of Cell Science · doi:10.1242/jcs.01660 · Cited by 1,549 · 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

Regulation of Small GTPases by GEFs, GAPs, and GDIs

Cherfils, J., & Zeghouf, M. (2013) · Physiological Reviews · doi:10.1152/physrev.00003.2012 · Cited by 1,245 · see citing works

Refined crystal structure of the triphosphate conformation of H‐ras p21 at 1.35 A resolution: implications for the mechanism of GTP hydrolysis.

PAI, E. F., Krengel, U., Petsko, G. A., Goody, R. S., Kabsch, W., & Wittinghofer, A. (1990) · The EMBO Journal · doi:10.1002/j.1460-2075.1990.tb07409.x · Cited by 1,074 · 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

Ras history: The saga continues

Cox, A. D., & Der, C. J. (2010) · Small GTPases · doi:10.4161/sgtp.1.1.12178 · Cited by 706 · see citing works

Electrostatic Origin of the Catalytic Power of Enzymes and the Role of Preorganized Active Sites

Warshel, A. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.42.27035 · Cited by 613 · see citing works

Evidence for Macromolecular Protein Rings in the Absence of Bulk Water

Ruotolo, B. T., Giles, K., Campuzano, I. D. G., Sandercock, A. M., Bateman, R. H., & Robinson, C. V. (2005) · Science · doi:10.1126/science.1120177 · Cited by 597 · see citing works

Global Kinetic Explorer: A new computer program for dynamic simulation and fitting of kinetic data

Johnson, K. A., Simpson, Z. B., & Blom, T. (2008) · Analytical Biochemistry · doi:10.1016/j.ab.2008.12.024 · Cited by 596 · see citing works

Investigation of intact protein complexes by mass spectrometry

Heck, A. J. R., & van den Heuvel, R. H. H. (2004) · Mass Spectrometry Reviews · doi:10.1002/mas.10081 · Cited by 584 · see citing works

An Interlaboratory Evaluation of Drift Tube Ion Mobility–Mass Spectrometry Collision Cross Section Measurements

Stow, S. M., Causon, T. J., Zheng, X., Kurulugama, R. T., Mairinger, T., May, J. C., Rennie, E. E., Baker, E. S., Smith, R. D., MCLEAN, J. A. J., et al. (2017) · Analytical Chemistry · doi:10.1021/acs.analchem.7b01729 · Cited by 535 · see citing works

Mass spectrometry of intact membrane protein complexes

Laganowsky, A., Reading, E., Hopper, J. T. S., & Robinson, C. V. (2013) · Nature Protocols · doi:10.1038/nprot.2013.024 · Cited by 409 · see citing works

Protein Complexes in the Gas Phase: Technology for Structural Genomics and Proteomics

Benesch, J. L. P., Ruotolo, B. T., Simmons, D. A., & Robinson, C. V. (2007) · Chemical Reviews · doi:10.1021/cr068289b · Cited by 408 · see citing works

Conformational Ordering of Biomolecules in the Gas Phase: Nitrogen Collision Cross Sections Measured on a Prototype High Resolution Drift Tube Ion Mobility-Mass Spectrometer

May, J. C., Goodwin, C. R., Lareau, N. M., Leaptrot, K. L., Morris, C. B., Kurulugama, R. T., Mordehai, A. V., Klein, C., Barry, W., Darland, E. J., et al. (2014) · Analytical Chemistry · doi:10.1021/ac4038448 · Cited by 404 · see citing works

High-sensitivity Orbitrap mass analysis of intact macromolecular assemblies

Rose, R. J., Damoc, E., Denisov, E., Makarov, A., & Heck, A. J. R. (2012) · Nature Methods · doi:10.1038/nmeth.2208 · Cited by 392 · see citing works

Characterization of Nucleotide Pools as a Function of Physiological State in <i>Escherichia coli</i>

Buckstein, M. H., He, J., & Rubin, H. (2008) · Journal of Bacteriology · doi:10.1128/jb.01020-07 · Cited by 370 · see citing works

Ras Conformational Ensembles, Allostery, and Signaling

Lu, S., Jang, H., Muratcioglu, S., Gursoy, A., Keskin, O., Nussinov, R., & Zhang, J. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00542 · Cited by 355 · see citing works

Genetic analysis of Ras signalling pathways in cell proliferation, migration and survival

Drosten, M., Dhawahir, A., Sum, E. Y. M., Urosevic, J., Lechuga, C. G., Esteban, L. M., Castellano, E., Guerra, C., Santos, E., & Barbacid, M. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.7 · Cited by 347 · see citing works

FitSpace Explorer: An algorithm to evaluate multidimensional parameter space in fitting kinetic data

Johnson, K. A., Simpson, Z. B., & Blom, T. (2008) · Analytical Biochemistry · doi:10.1016/j.ab.2008.12.025 · Cited by 344 · see citing works

Mutational and Kinetic Analyses of the GTPase-Activating Protein (GAP)-p21 Interaction: The C-Terminal Domain of GAP Is Not Sufficient for Full Activity

Gideon, P., John, J., Frech, M., Lautwein, A., Clark, R., Scheffler, J. E., & Wittinghofer, A. (1992) · Molecular and Cellular Biology · doi:10.1128/mcb.12.5.2050 · Cited by 287 · see citing works

Collision Cross Sections for Structural Proteomics

Marklund, E. G., Degiacomi, M. T., Robinson, C. V., Baldwin, A. J., & Benesch, J. L. P. (2015) · Structure · doi:10.1016/j.str.2015.02.010 · Cited by 270 · 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

K-ras codon 12 mutation induces higher level of resistance to apoptosis and predisposition to anchorage-independent growth than codon 13 mutation or proto-oncogene overexpression.

Guerrero, S., Casanova, I., Farré, L., Mazo, A., Capellá, G., & Mangues, R. (2000) · PubMed · Cited by 243 · 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

How important are entropic contributions to enzyme catalysis?

Villà­-Freixa, J., Štrajbl, M., Glennon, T. M., Sham, Y. Y., Chu, Z. T., & Warshel, A. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.22.11899 · Cited by 187 · 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

The ras superfamily of small GTP-binding proteins

Downward, J. (1990) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(90)90300-z · Cited by 175 · see citing works

Solvation, Reorganization Energy, and Biological Catalysis

Cannon, W. R., & Benkovic, S. J. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.41.26257 · Cited by 168 · 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

Structural Basis for Conformational Dynamics of GTP-bound Ras Protein

Shima, F., Ijiri, Y., Muraoka, S., Liao, J., Ye, M., Araki, M., Matsumoto, K., Yamamoto, N., Sugimoto, T., Yoshikawa, Y., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.125161 · Cited by 148 · 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

Mass spectrometry based tools to investigate protein–ligand interactions for drug discovery

Pacholarz, K. J., Garlish, R. A., Taylor, R. J., & Barran, P. E. (2012) · Chemical Society Reviews · doi:10.1039/c2cs35035a · Cited by 140 · see citing works

Kinetic analysis of the hydrolysis of GTP by p21N-ras. The basal GTPase mechanism.

Neal, S. E., Eccleston, J. F., Hall, A., & Webb, M. R. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)77694-7 · Cited by 130 · see citing works

[8] Measurement of intrinsic nucleotide exchange and GTP hydrolysis rates

Self, A. J., & Hall, A. (1995) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(95)56010-6 · Cited by 125 · see citing works

Transformation Efficiency of RasQ61 Mutants Linked to Structural Features of the Switch Regions in the Presence of Raf

Buhrman, G., Wink, G., & Mattos, C. (2007) · Structure · doi:10.1016/j.str.2007.10.011 · Cited by 116 · see citing works

Solution Structure of the State 1 Conformer of GTP-bound H-Ras Protein and Distinct Dynamic Properties between the State 1 and State 2 Conformers

Araki, M., Shima, F., Yoshikawa, Y., Muraoka, S., Ijiri, Y., Nagahara, Y., Shirono, T., Kataoka, T., & Tamura, A. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.227074 · Cited by 105 · see citing works

Allostery revealed within lipid binding events to membrane proteins

Patrick, J. W., Boone, C. D., Liu, W., Conover, G. M., Liu, Y., Cong, X., & Laganowsky, A. D. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1719813115 · Cited by 104 · see citing works

Fourier Transform-Ion Mobility-Orbitrap Mass Spectrometer: A Next-Generation Instrument for Native Mass Spectrometry

Poltash, M. L., McCabe, J. W., Shirzadeh, M., Laganowsky, A. D., Clowers, B. H., & Russell, D. H. (2018) · Analytical Chemistry · doi:10.1021/acs.analchem.8b02463 · Cited by 79 · see citing works

RAS Mutations and Oncogenesis: Not all RAS Mutations are Created Equally

Miller, M. S., & Miller, L. D. (2012) · Frontiers in Genetics · doi:10.3389/fgene.2011.00100 · Cited by 76 · see citing works

Deoxyribonucleotide Triphosphate Metabolism in Cancer and Metabolic Disease

Buj, R., & Aird, K. M. (2018) · Frontiers in Endocrinology · doi:10.3389/fendo.2018.00177 · Cited by 74 · 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

Two conformational states of Ras GTPase exhibit differential GTP-binding kinetics

Liao, J., Shima, F., Araki, M., Ye, M., Muraoka, S., Sugimoto, T., Kawamura, M., Yamamoto, N., Tamura, A., & Kataoka, T. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.01.169 · Cited by 68 · see citing works

Time-resolved FTIR studies provide activation free energy, activation enthalpy and activation entropy for GTPase reactions

Kötting, C., & Gerwert, K. B. (2004) · Chemical Physics · doi:10.1016/j.chemphys.2004.06.051 · Cited by 66 · see citing works

Ion mobility-mass spectrometry applied to cyclic peptide analysis: Conformational preferences of gramicidin S and linear analogs in the gas phase

Ruotolo, B. T., Tate, C. C., & Russell, D. H. (2004) · Journal of the American Society for Mass Spectrometry · doi:10.1016/j.jasms.2004.02.006 · Cited by 66 · see citing works

Signal transduction pathways involving RAS

Wiesmüller, L., & Wittinghofer, F. (1994) · Cellular Signalling · doi:10.1016/0898-6568(94)90030-2 · Cited by 63 · see citing works

Rapid Purification of Native Dynamin I and Colorimetric GTPase Assay

Quan, A., & Robinson, P. J. (2005) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(05)04049-8 · Cited by 59 · see citing works

Kinetic Mechanisms of Mutation-Dependent Harvey Ras Activation and Their Relevance for the Development of Costello Syndrome

Wey, M., Lee, J., Jeong, S. S., Kim, J., & Heo, J. (2013) · Biochemistry · doi:10.1021/bi400679q · Cited by 53 · see citing works

A Scanning Frequency Mode for Ion Cyclotron Mobility Spectrometry

Glaskin, R. S., Valentine, S. J., & Clemmer, D. E. (2010) · Analytical Chemistry · doi:10.1021/ac1017474 · Cited by 44 · see citing works

Interaction of GTPase-activating protein with p21ras, measured using a continuous assay for inorganic phosphate release

Webb, M. R., & Hunter, J. L. (1992) · Biochemical Journal · doi:10.1042/bj2870555 · Cited by 33 · see citing works

Quantitative Measurement of Intrinsic GTP Hydrolysis for Carcinogenic Glutamine 61 Mutants in H-Ras

Novelli, E. T., First, J. T., & Webb, L. J. (2018) · Biochemistry · doi:10.1021/acs.biochem.8b00878 · Cited by 33 · see citing works

Application of the Exactive Plus EMR for automated protein–ligand screening by non‐covalent mass spectrometry

Maple, H. J., Scheibner, O., Baumert, M., Allen, M. H., Taylor, R. J., Garlish, R. A., Bromirski, M., & Burnley, R. J. (2014) · Rapid Communications in Mass Spectrometry · doi:10.1002/rcm.6925 · Cited by 29 · see citing works

Topological Analysis of Transthyretin Disassembly Mechanism: Surface-Induced Dissociation Reveals Hidden Reaction Pathways

Shirzadeh, M., Boone, C. D., Laganowsky, A. D., & Russell, D. H. (2019) · Analytical Chemistry · doi:10.1021/acs.analchem.8b05066 · Cited by 29 · see citing works

Hurdles and Complexities of Codon 13KRASMutations

Morelli, M. P., & Kopetz, S. (2012) · Journal of Clinical Oncology · doi:10.1200/jco.2012.43.6535 · Cited by 28 · see citing works

Effects of ions on the intrinsic activities of c‐H‐ras protein p21

Mistou, M., Cool, R. H., & Parmeggiani, A. (1992) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1992.tb16621.x · Cited by 26 · see citing works

Conserved Motifs in Different Classes of GTPases Dictate their Specific Modes of Catalysis

Åqvist, J., & Kamerlin, S. C. L. (2016) · ACS Catalysis · doi:10.1021/acscatal.5b02491 · Cited by 25 · see citing works

New insights into the metal-induced oxidative degradation pathways of transthyretin

Poltash, M. L., Shirzadeh, M., McCabe, J. W., Moghadamchargari, Z., Laganowsky, A. D., & Russell, D. H. (2019) · Chemical Communications · doi:10.1039/c9cc00682f · Cited by 24 · see citing works

Intrinsic GTPase activity of a bacterial twin‐arginine translocation proofreading chaperone induced by domain swapping

Guymer, D., Maillard, J., Agacan, M. F., Brearley, C. A., & Sargent, F. (2010) · FEBS Journal · doi:10.1111/j.1742-4658.2009.07507.x · Cited by 18 · see citing works

The balanced induction of K-ras codon 12 and 13 mutations in mucosa differs from their ratio in neoplastic tissues

Kraus, M., Seelig, M. H., Linnemann, U., & Berger, M. R. (2006) · International Journal of Oncology · doi:10.3892/ijo.29.4.957 · Cited by 17 · see citing works

High-Resolution Native Mass Spectrometry

Tamara, S., den Boer, M. A., & Heck, A. J. R. (2022) · Chemical Reviews · doi:10.1021/acs.chemrev.1c00212 · Cited by 511 · see citing works

Protein–Small Molecule Interactions in Native Mass Spectrometry

Bennett, J. L., Nguyen, G. T. H., & Donald, W. A. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.1c00293 · Cited by 159 · see citing works

Approaches to Heterogeneity in Native Mass Spectrometry

Rolland, A. D., & Prell, J. S. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.1c00696 · Cited by 71 · see citing works

Targeted therapies for KRAS-mutant non-small cell lung cancer: from preclinical studies to clinical development—a narrative review

Santarpia, M., Ciappina, G., Spagnolo, C. C., Squeri, A., Passalacqua, M. I., Aguilar, A., Gonzalez-Cao, M., Giovannetti, E., Silvestris, N., & Rosell, R. (2023) · Translational Lung Cancer Research · doi:10.21037/tlcr-22-639 · Cited by 65 · see citing works

K-Ras prenylation as a potential anticancer target

Baranyi, M., Buday, L., & Hegedűs, B. (2020) · Cancer and Metastasis Reviews · doi:10.1007/s10555-020-09902-w · Cited by 62 · see citing works

Overcoming Resistance to Drugs Targeting KRAS Mutation

Jiao, D., & Yang, S. (2020) · The Innovation · doi:10.1016/j.xinn.2020.100035 · Cited by 61 · see citing works

THE IMS PARADOX: A PERSPECTIVE ON STRUCTURAL ION MOBILITY‐MASS SPECTROMETRY

McCabe, J. W., Hebert, M. J., Shirzadeh, M., Mallis, C. S., Denton, J. K., Walker, T. E., & Russell, D. H. (2020) · Mass Spectrometry Reviews · doi:10.1002/mas.21642 · Cited by 51 · see citing works

Variable-Temperature Native Mass Spectrometry for Studies of Protein Folding, Stabilities, Assembly, and Molecular Interactions

Laganowsky, A. D., Clemmer, D. E., & Russell, D. H. (2021) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-102221-101121 · Cited by 50 · see citing works

Intrinsically disordered proteins: Ensembles at the limits of Anfinsen's dogma

Kulkarni, P., Leite, V. B. P., Roy, S., Bhattacharyya, S., Mohanty, A. R., Achuthan, S., Singh, D., Appadurai, R., Govindan Rangarajan, C., Weninger, K., et al. (2022) · Biophysics Reviews · doi:10.1063/5.0080512 · Cited by 50 · see citing works

Not all RAS mutations are equal: A detailed review of the functional diversity of RAS hot spot mutations

Burge, R. A., & Hobbs, G. A. (2022) · Advances in cancer research · doi:10.1016/bs.acr.2021.07.004 · Cited by 44 · see citing works

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

Moghadamchargari, Z., Shirzadeh, M., Liu, C., Schrecke, S., Packianathan, C., Russell, D. H., Zhao, M., & Laganowsky, A. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2022403118 · Cited by 38 · see citing works

Discovery of a Bicyclic Peptidyl Pan-Ras Inhibitor

Buyanova, M. Y., Cai, S., Cooper, J. K., Rhodes, C. A., Salim, H., Sahni, A., Upadhyaya, P., Yang, R., Sarkar, A., Li, N., et al. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c01130 · Cited by 38 · see citing works

Farnesyl-transferase inhibitors show synergistic anticancer effects in combination with novel KRAS-G12C inhibitors

Baranyi, M., Molnár, E., Hegedüs, L., Gábriel, Z., Petenyi, F. G., Bordás, F., Lener, V., Ranđelović, I., Cserepes, M., Tóvári, J., et al. (2024) · British Journal of Cancer · doi:10.1038/s41416-024-02586-x · Cited by 35 · see citing works

Excited-state observation of active K-Ras reveals differential structural dynamics of wild-type versus oncogenic G12D and G12C mutants

Hansen, A. L., Xiang, X., Yuan, C., Bruschweiler‐Li, L., & Brüschweiler, R. (2023) · Nature Structural & Molecular Biology · doi:10.1038/s41594-023-01070-z · Cited by 27 · see citing works

Scratching the surface: native mass spectrometry of peripheral membrane protein complexes

Sahin, C., Reid, D. J., Marty, M. T., & Landreh, M. (2020) · Biochemical Society Transactions · doi:10.1042/bst20190787 · Cited by 27 · see citing works

Dynamic Multilevel Regulation of EGFR, KRAS, and MYC Oncogenes: Driving Cancer Cell Proliferation Through (Epi)Genetic and Post-Transcriptional/Translational Pathways

Šereš, M., Spacayova, K., Sulová, Z., Špaldová, J., Breier, A., & Pavlíková, L. (2025) · Cancers · doi:10.3390/cancers17020248 · Cited by 26 · see citing works

Recent advances in computational and experimental protein-ligand affinity determination techniques

Kairys, V., Baranauskienė, L., Kazlauskiene, M., Zubrienė, A., Petrauskas, V., Matulis, D., & Kazlauskas, E. (2024) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2024.2349169 · Cited by 27 · see citing works

Revealing the mechanism of action of a first-in-class covalent inhibitor of KRASG12C (ON) and other functional properties of oncogenic KRAS by 31P NMR

Sharma, A. K., Pei, J., Yang, Y., Dyba, M. D., Smith, B. D., Rabara, D., Larsen, E. K., Lightstone, F. C., Esposito, D., Stephen, A. G., et al. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.105650 · Cited by 24 · see citing works

Advances in mass spectrometry to unravel the structure and function of protein condensates

Sahin, C., Leppert, A., & Landreh, M. (2023) · Nature Protocols · doi:10.1038/s41596-023-00900-0 · Cited by 17 · see citing works

Native mass spectrometry and structural studies reveal modulation of MsbA–nucleotide interactions by lipids

Zhang, T., Lyu, J., Yang, B., Yun, S. D., Scott, E., Zhao, M., & Laganowsky, A. D. (2024) · Nature Communications · doi:10.1038/s41467-024-50350-9 · Cited by 12 · see citing works

GLOBAL AND TARGETED PROFILING OF GTP‐BINDING PROTEINS IN BIOLOGICAL SAMPLES BY MASS SPECTROMETRY

Huang, M., & Wang, Y. (2020) · Mass Spectrometry Reviews · doi:10.1002/mas.21637 · Cited by 12 · see citing works

Capturing RAS oligomerization on a membrane

Yun, S. D., Scott, E., Chang, J., Bahramimoghaddam, H., Lynn, M., Lantz, C., Russell, D. H., & Laganowsky, A. D. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2405986121 · Cited by 11 · see citing works

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

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

Deciphering allosteric mechanisms in KRAS activation: insights from GTP-induced conformational dynamics and interaction network reorganization

Zhao, D.-R., Yang, J.-T., Liu, M.-T., Yang, L.-Q., & Sang, P. (2025) · RSC Advances · doi:10.1039/d4ra07924h · Cited by 8 · see citing works

Progress in Targeting KRAS Directly

Nissley, D. V., Stephen, A. G., Yi, M., & McCormick, F. P. (2024) · Methods in molecular biology · doi:10.1007/978-1-0716-3822-4_1 · Cited by 6 · see citing works

GAP positions catalytic H-Ras residue Q61 for GTP hydrolysis in molecular dynamics simulations, complicating chemical rescue of Ras deactivation

Patel, L. A., Waybright, T. J., Stephen, A. G., & Neale, C. (2023) · Computational Biology and Chemistry · doi:10.1016/j.compbiolchem.2023.107835 · Cited by 6 · see citing works

Characterization of adenine phosphoribosyltransferase (APRT) activity in Trypanosoma brucei brucei: Only one of the two isoforms is kinetically active

Glockzin, K., Meek, T. D., & Katzfuss, A. (2022) · PLoS neglected tropical diseases · doi:10.1371/journal.pntd.0009926 · Cited by 6 · see citing works

Discovering Targetable Conformation of RhoA Mutant by Integrating Native Mass Spectrometry, Ultraviolet Photodissociation, and X-ray Diffraction

Wu, H., Liu, Z., Jiang, H., Zhao, H., Dong, C., Lu, Y., Zu, S., Guo, Y., Lai, C., Luo, P., et al. (2026) · Journal of the American Chemical Society · doi:10.1021/jacs.5c20067 · Cited by 5 · see citing works

SOS1: tracking the evolving path from promising to actionable therapeutic target in RAS-dependent cancers

Luna-Ramírez, L., García‐Navas, R., Santos, E., & Baltanás, F. C. (2026) · Molecular Cancer · doi:10.1186/s12943-026-02632-7 · Cited by 3 · see citing works

Prognostic Implications of Codon-Specific KRAS Mutations in Localized and Advanced Stages of Pancreatic Cancer

Raji, S., Zaribafzadeh, H., Jones, T., Kanu, E. N., Tong, K., Fletcher, A. A., Howell, T. C., McCall, S. J., Marks, J., Rogers, B., et al. (2026) · JCO Precision Oncology · doi:10.1200/po-25-00115 · Cited by 3 · see citing works

Proteogenomic Approaches to Understand Gene Mutations and Protein Structural Alterations in Colon Cancer

Sarkar, S. (2023) · Physiologia · doi:10.3390/physiologia3010002 · Cited by 3 · see citing works

Time-Resolved Crystallography Reveals the Mechanisms of GTP hydrolysis for N-RAS and the Oncogenic Mutants G12C, G12V and Q61LPreprint

Lin, G., Peniche, P. Z., Zhou, X., Santiago, U., Kurnikov, I. V., Russi, S., Chagas, B. C. A., Sharpe, M. E., Stegmann, D. P., Heinig, S. A., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.08.21.670574 · Cited by 3 · see citing works

Brønsted-basic small molecules activate GTP hydrolysis in KRAS-Q61 mutants

Wang, Y., Chen, S., Cao, Y., Wu, Y., Shi, Z., Wang, C. D., Norinskiy, M. A., Celik, H., & Zhang, Z. (2026) · Nature Chemical Biology · doi:10.1038/s41589-026-02291-1 · Cited by 2 · see citing works

Native top-down mass spectrometry for monitoring the rapid chymotrypsin catalyzed hydrolysis reaction

Ying, Y., & Li, H. (2023) · Analytica Chimica Acta · doi:10.1016/j.aca.2023.341971 · Cited by 2 · see citing works

Ras S89D mutation induced allosteric changes that promoted its nucleotide exchange and signaling activation

Li, Y., Huang, W., Guo, L., & Sun, Q. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.139538 · Cited by 1 · see citing works

Time-Resolved Native Mass Spectrometry for Direct Measurement of Biomolecular Kinetics

James, V. K., Stover, L., Bahramimoghaddam, H., Khandelwal, T., Chang, J., Downing, J., Scott, E., Bailey, K. O., Russell, D. H., Baker, L. A., et al. (2026) · Journal of the American Chemical Society · doi:10.1021/jacs.5c21842 · Cited by 1 · see citing works

Designing Graphics

Biegel, C. M., & Kamat, P. V. (2020) · American Chemical Society eBooks · doi:10.1021/acsguide.40103

Real time characterization of the MAPK pathway using native mass spectrometry

Scott, E., Yun, S. D., Moghadamchargari, Z., Bahramimoghaddam, H., Chang, J., Zhang, T., Zhu, Y. K., Lyu, J., & Laganowsky, A. D. (2025) · Communications Biology · doi:10.1038/s42003-025-08028-5

BindingDB Entry 50014692: Discovery of a Bicyclic Peptidyl Pan-Ras Inhibitor.

BindingDB (2022) · UC San Diego · doi:10.7270/q22v2kz6

Interrogating the interactions of oncogenic KRAS mutants with SOS and BRAF

Moghadamchargari, Z. (2021) · OakTrust (Texas A&M University Libraries)

GTP hydrolysis in RAS

Knihtila, R. (2016) · doi:10.17760/d20211606

GTP hydrolysis in RAS: how mutations affect hydrogen bonding and catalysis.

(n.d.) · Digital Repository Service (Northeastern University)

How KRAS Mutations Impair Intrinsic GTP Hydrolysis: Experimental and Computational Investigations

Song, L. F., Rabara, D., Bali, S. K., Pei, J., Lau, E. Y., Kirshner, D. A., Lightstone, F. C., McCormick, F., Stephen, A. G., & Yang, Y. (2025) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.5c02061 · Cited by 5 · see citing works

Abstract 1366: Structural basis of impaired GTP hydrolysis in oncogenic mutants of KRAS

Tran, T. H., Dharmaiah, S., Chertov, O., Waybright, T. J., Gillette, W., Esposito, D., Nissley, D. V., McCormick, F., Stephen, A. G., & Simanshu, D. K. (2017) · Cancer Research · doi:10.1158/1538-7445.am2017-1366