Ras activation by SOS: Allosteric regulation by altered fluctuation dynamics

A general method for numerically simulating the stochastic time evolution of coupled chemical reactions

Gillespie, D. T. (1976) · Journal of Computational Physics · doi:10.1016/0021-9991(76)90041-3 · Cited by 6,029

Dynamic personalities of proteins

Henzler-Wildman, K., & Kern, D. (2007) · Nature · doi:10.1038/nature06522 · Cited by 2,545

The role of dynamic conformational ensembles in biomolecular recognition

Boehr, D. D., Nussinov, R., & Wright, P. E. (2009) · Nature Chemical Biology · doi:10.1038/nchembio.232 · Cited by 2,008

GEFs and GAPs: Critical Elements in the Control of Small G Proteins

Bos, J. L., Rehmann, H., & Wittinghofer, A. (2007) · Cell · doi:10.1016/j.cell.2007.05.018 · Cited by 1,903

Single-Molecule Enzymatic Dynamics

Lu, H. P. (1998) · Science · doi:10.1126/science.282.5395.1877 · Cited by 1,470

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

Paradigm Shift of the Plasma Membrane Concept from the Two-Dimensional Continuum Fluid to the Partitioned Fluid: High-Speed Single-Molecule Tracking of Membrane Molecules

Kusumi, A., Nakada, C., Ritchie, K. P., Murase, K., Suzuki, K. G. N., Murakoshi, H., Kasai, R. S., Kondo, J., & Fujiwara, T. K. (2005) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.34.040204.144637 · Cited by 1,122

A hierarchy of timescales in protein dynamics is linked to enzyme catalysis

Henzler‐Wildman, K. A., Lei, M., Thai, V., Kerns, S. J., Karplus, M., & Kern, D. (2007) · Nature · doi:10.1038/nature06407 · Cited by 1,067

Direct observation of ligand recognition by T cells

Irvine, D. J., Purbhoo, M. A., Krogsgaard, M., & Davis, M. M. (2002) · Nature · doi:10.1038/nature01076 · Cited by 824

Induced fit, conformational selection and independent dynamic segments: an extended view of binding events

Csermely, P., Palotai, R., & Nussinov, R. (2010) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2010.04.009 · Cited by 821

KRAS Mutation: From Undruggable to Druggable in Cancer

Huang, L., Guo, Z., Wang, F., & Fu, L. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00780-4 · Cited by 1,127

Protein Ensembles: How Does Nature Harness Thermodynamic Fluctuations for Life? The Diverse Functional Roles of Conformational Ensembles in the Cell

Wei, G., Xi, W., Nussinov, R., & Ma, B. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00562 · Cited by 436

Recent advances in targeting the “undruggable” proteins: from drug discovery to clinical trials

Xie, X., Yu, T., Li, X., Zhang, N., Foster, L. J., Peng, C., Huang, W., & He, G. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01589-z · Cited by 396

The Control Centers of Biomolecular Phase Separation: How Membrane Surfaces, PTMs, and Active Processes Regulate Condensation

Snead, W. T., & Gladfelter, A. S. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.09.016 · Cited by 356

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

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

Single‐Molecule Sensors: Challenges and Opportunities for Quantitative Analysis

Gooding, J. J., & Gaus, K. (2016) · Angewandte Chemie International Edition · doi:10.1002/anie.201600495 · Cited by 343

Regulation of Transmembrane Signaling by Phase Separation

Case, L. B., Ditlev, J. A., & Rosen, M. K. (2019) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-052118-115534 · Cited by 304

KRAS: From undruggable to a druggable Cancer Target

Uprety, D., & Adjei, A. A. (2020) · Cancer Treatment Reviews · doi:10.1016/j.ctrv.2020.102070 · Cited by 271

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

Allostery without a conformational change? Revisiting the paradigm

Nussinov, R., & Tsai, C.-J. (2015) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2014.11.005 · Cited by 202

Drugging Ras GTPase: a comprehensive mechanistic and signaling structural view

Lu, S., Jang, H., Gu, S., Zhang, J., & Nussinov, R. (2016) · Chemical Society Reviews · doi:10.1039/c5cs00911a · Cited by 188

The Dynamical Nature of Enzymatic Catalysis

Callender, R. H., & Dyer, R. B. (2014) · Accounts of Chemical Research · doi:10.1021/ar5002928 · Cited by 155

Phosphotyrosine-mediated LAT assembly on membranes drives kinetic bifurcation in recruitment dynamics of the Ras activator SOS

Huang, W. Y. C., Yan, Q., Lin, W., Chung, J. K., Hansen, S. D., Christensen, S. M., Tu, H., Kuriyan, J., & Groves, J. T. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1602602113 · Cited by 138

Deconstruction of the Ras switching cycle through saturation mutagenesis

Bandaru, P., Shah, N. H., Bhattacharyya, M., Barton, J. P., Kondo, Y., Cofsky, J. C., Gee, C. L., Chakraborty, A. K., Kortemme, T., Ranganathan, R., et al. (2017) · eLife · doi:10.7554/elife.27810 · Cited by 117

Compartmentalization of the Cell Membrane

Honigmann, A., & Pralle, A. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.09.022 · Cited by 113

Direct observation of proton pumping by a eukaryotic P-type ATPase

Veshaguri, S., Christensen, S. M., Kemmer, G. C., Ghale, G., Møller, M. P., Lohr, C., Christensen, A. L., Justesen, B. H., Jørgensen, I. L., Schiller, J., et al. (2016) · Science · doi:10.1126/science.aad6429 · Cited by 97

Supported Lipid Bilayers for the Generation of Dynamic Cell–Material Interfaces

van Weerd, J., Karperien, M., & Jonkheijm, P. (2015) · Advanced Healthcare Materials · doi:10.1002/adhm.201500398 · Cited by 93

Keep on Moving: Discovering and Perturbing the Conformational Dynamics of Enzymes

Bhabha, G., Biel, J. T., & Fraser, J. S. (2014) · Accounts of Chemical Research · doi:10.1021/ar5003158 · Cited by 94

A two-component protein condensate of the EGFR cytoplasmic tail and Grb2 regulates Ras activation by SOS at the membrane

Lin, C., Nocka, L. M., Stinger, B. L., DeGrandchamp, J. B., Lew, L. J. N., Alvarez, S. A., Phan, H. T., Kondo, Y., Kuriyan, J., & Groves, J. T. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2122531119 · Cited by 84

The Interdependent Activation of Son-of-Sevenless and RasPreprint

Bandaru, P., Kondo, Y., & Kuriyan, J. (2018) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a031534 · Cited by 81

Stochastic geometry sensing and polarization in a lipid kinase–phosphatase competitive reaction

Hansen, S. D., Huang, W. Y. C., Lee, Y. K., Bieling, P., Christensen, S. M., & Groves, J. T. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1901744116 · Cited by 72

Biased cytochrome P450-mediated metabolism via small-molecule ligands binding P450 oxidoreductase

Jensen, S. B., Thodberg, S., Parween, S., Moses, M. E., Hansen, C. C., Thomsen, J., Sletfjerding, M. B., Knudsen, C., Del Giudice, R., Lund, P. M., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-22562-w · Cited by 64

Inhibitors of Ras–SOS Interactions

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

K-Ras4B Remains Monomeric on Membranes over a Wide Range of Surface Densities and Lipid Compositions

Chung, J. K., Lee, Y. K., Denson, J.-P., Gillette, W., Alvarez, S. A., Stephen, A. G., & Groves, J. T. (2018) · Biophysical Journal · doi:10.1016/j.bpj.2017.10.042 · Cited by 72

microRNA‐148a‐3p inhibited the proliferation and epithelial–mesenchymal transition progression of non‐small‐cell lung cancer via modulating Ras/MAPK/Erk signaling

Xie, Q., Yu, Z., Lu, Y., Fan, J., Ni, Y., & Ma, L. (2018) · Journal of Cellular Physiology · doi:10.1002/jcp.27899 · Cited by 66

Switch-like activation of Bruton’s tyrosine kinase by membrane-mediated dimerization

Chung, J. K., Nocka, L. M., Decker, A., Wang, Q., Kadlecek, T. A., Weiss, A., Kuriyan, J., & Groves, J. T. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1819309116 · Cited by 67

One-way membrane trafficking of SOS in receptor-triggered Ras activation

Christensen, S. M., Tu, H., Jun, J. E., Alvarez, S. A., Triplet, M. G., Iwig, J. S., Yadav, K. K., Bar‐Sagi, D., Roose, J. P., & Groves, J. T. (2016) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3275 · Cited by 62

Discovery and Structure-Based Optimization of Benzimidazole-Derived Activators of SOS1-Mediated Nucleotide Exchange on RAS

Hodges, T. R., Abbott, J. R., Little, A. J., Sarkar, D., Salovich, J. M., Howes, J. E., Akan, D. T., Sai, J., Arnold, A. L., Browning, C. F., et al. (2018) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.8b01108 · Cited by 62

The membrane surface as a platform that organizes cellular and biochemical processes

Leonard, T. A., Loose, M., & Martens, S. (2023) · Developmental Cell · doi:10.1016/j.devcel.2023.06.001 · Cited by 64

Mechanism of SOS PR-domain autoinhibition revealed by single-molecule assays on native protein from lysate

Lee, Y. K., Low-Nam, S. T., Chung, J. K., Hansen, S. D., Lam, H. Y. M., Alvarez, S. A., & Groves, J. T. (2017) · Nature Communications · doi:10.1038/ncomms15061 · Cited by 60

Raf promotes dimerization of the Ras G-domain with increased allosteric connections

Packer, M. R., Parker, J. A., Chung, J. K., Li, Z., Lee, Y. K., Cookis, T., Guterres, H., Alvarez, S. A., Hossain, M. A., Donnelly, D. P., et al. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2015648118 · Cited by 55

How the T cell signaling network processes information to discriminate between self and agonist ligands

Ganti, R., Lo, W., McAffee, D. B., Groves, J. T., Weiss, A., & Chakraborty, A. K. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2008303117 · Cited by 54

Membrane orientation dynamics of lipid-modified small GTPases

Prakash, P., & Gorfe, A. A. (2016) · Small GTPases · doi:10.1080/21541248.2016.1211067 · Cited by 48

Direct observation of Thermomyces lanuginosus lipase diffusional states by Single Particle Tracking and their remodeling by mutations and inhibition

Bohr, S. S.-R., Lund, P. M., Kallenbach, A. S., Pinholt, H. D., Thomsen, J., Iversen, L., Svendsen, A., Christensen, S. M., & Hatzakis, N. S. (2019) · Scientific Reports · doi:10.1038/s41598-019-52539-1 · Cited by 48

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

Plasma membrane regulates Ras signaling networks

Chavan, T., Muratcioğlu, S., Marszalek, R. J., Jang, H., Keskin, Ö., Gürsoy, A., Nussinov, R., & Gaponenko, V. (2015) · Cellular Logistics · doi:10.1080/21592799.2015.1136374 · Cited by 43

The role of wild-type RAS in oncogenic RAS transformation

Sheffels, E., & Kortum, R. L. (2021) · Genes · doi:10.3390/genes12050662 · Cited by 42

KRAS Mutations in Cancer: Understanding Signaling Pathways to Immune Regulation and the Potential of Immunotherapy

Uniyal, P., Kashyap, V. K., Behl, T., Parashar, D., & Rawat, R. (2025) · Cancers · doi:10.3390/cancers17050785 · Cited by 48

Covalent Ras Dimerization on Membrane Surfaces through Photosensitized Oxidation

Chung, J. K., Lee, Y. K., Lam, H. Y. M., & Groves, J. T. (2016) · Journal of the American Chemical Society · doi:10.1021/jacs.5b12648 · Cited by 38

Insights into K-Ras 4B regulation by post-translational lysine acetylation

Knyphausen, P., Lang, F., Baldus, L., Extra, A., & Lammers, M. (2016) · Biological Chemistry · doi:10.1515/hsz-2016-0118 · Cited by 39

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

Allosteric KRas4B Can Modulate SOS1 Fast and Slow Ras Activation Cycles

Liao, T.-J., Jang, H., Fushman, D., & Nussinov, R. (2018) · Biophysical Journal · doi:10.1016/j.bpj.2018.07.016 · 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

Rhythmicity and waves in the cortex of single cells

Yang, Y., & Wu, M. (2018) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2017.0116 · Cited by 37

Novel regulation of Ras proteins by direct tyrosine phosphorylation and dephosphorylation

Buday, L., & Vas, V. (2020) · Cancer and Metastasis Reviews · doi:10.1007/s10555-020-09918-2 · Cited by 30

Allosteric Modulation of Grb2 Recruitment to the Intrinsically Disordered Scaffold Protein, LAT, by Remote Site Phosphorylation

Huang, W. Y. C., Ditlev, J. A., Chiang, H.-K., Rosen, M. K., & Groves, J. T. (2017) · Journal of the American Chemical Society · doi:10.1021/jacs.7b09387 · Cited by 30

Oncogenic KRAS effector USP13 promotes metastasis in non-small cell lung cancer through deubiquitinating β-catenin

Guo, Y., Tian, J., Guo, Y., Wang, C., Chen, C., Cai, S., Yu, W., Sun, B., Yan, J., Li, Z., et al. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.113511 · Cited by 28

Molecular clustering in the cell: from weak interactions to optimized functional architectures

Recouvreux, P., & Lenne, P. (2016) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2016.01.002 · Cited by 28

Small GTPase peripheral binding to membranes: molecular determinants and supramolecular organization

Peurois, F., Peyroche, G., & Cherfils, J. (2018) · Biochemical Society Transactions · doi:10.1042/bst20170525 · Cited by 27

Understand KRAS and the Quest for Anti-Cancer Drugs

Han, C. W., Jeong, M. S., & Jang, S. B. (2021) · Cells · doi:10.3390/cells10040842 · Cited by 27

Monitoring the Waiting Time Sequence of Single Ras GTPase Activation Events Using Liposome Functionalized Zero-Mode Waveguides

Christensen, S. M., Triplet, M. G., Rhodes, C., Iwig, J. S., Tu, H., Stamou, D. G., & Groves, J. T. (2016) · Nano Letters · doi:10.1021/acs.nanolett.6b00969 · Cited by 25

The intramolecular allostery of GRB2 governing its interaction with SOS1 is modulated by phosphotyrosine ligands

Jasemi, N. S. K., Herrmann, C., Estirado, E. M., Gremer, L., Willbold, D., Brunsveld, L., Dvorský, R., & Ahmadian, M. R. (2021) · Biochemical Journal · doi:10.1042/bcj20210105 · Cited by 26

A review on tyrosine kinase inhibitors for targeted breast cancer therapy

Sankarapandian, V., Rajendran, R. L., Miruka, C. O., Poornima, S., Maran, B. A. V., Krishnamoorthy, R., Gangadaran, P., & Ahn, B. (2024) · Pathology - Research and Practice · doi:10.1016/j.prp.2024.155607 · Cited by 29

Current approaches to studying membrane organization

van Zanten, T. S., & Mayor, S. (2015) · F1000Research · doi:10.12688/f1000research.6868.1 · Cited by 24

Minute-scale persistence of a GPCR conformation state triggered by non-cognate G protein interactions primes signaling

Gupte, T. M., Ritt, M., Dysthe, M., Malik, R. U., & Sivaramakrishnan, S. (2019) · Nature Communications · doi:10.1038/s41467-019-12755-9 · Cited by 24

Stochasticity and positive feedback enable enzyme kinetics at the membrane to sense reaction size

Lee, A. A., Huang, W. Y. C., Hansen, S. D., Kim, N. H., Alvarez, S., & Groves, J. (2021) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.2103626118 · Cited by 21

Relating cellular signaling timescales to single-molecule kinetics: A first-passage time analysis of Ras activation by SOS

Huang, W. Y. C., Alvarez, S. A., Kondo, Y., Kuriyan, J., & Groves, J. T. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2103598118 · Cited by 23

Membrane localization accelerates association under conditions relevant to cellular signaling

Huang, W. Y. C., Boxer, S. G., & Ferrell, J. E. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2319491121 · Cited by 22

Past, Present, and Future of Targeting Ras for Cancer Therapies

Tan, Z., & Zhang, S. (2015) · Mini-Reviews in Medicinal Chemistry · doi:10.2174/1389557515666151001154111 · Cited by 21

Shedding Light on Protein Folding, Structural and Functional Dynamics by Single Molecule Studies

Bavishi, K., & Hatzakis, N. S. (2014) · Molecules · doi:10.3390/molecules191219407 · Cited by 21

Single-Molecule Study of Thermomyces lanuginosus Lipase in a Detergency Application System Reveals Diffusion Pattern Remodeling by Surfactants and Calcium

Moses, M. E., Lund, P. M., Bohr, S. S.-R., Iversen, J. F., Kæstel‐Hansen, J., Kallenbach, A. S., Iversen, L., Christensen, S. M., & Hatzakis, N. S. (2021) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.1c08809 · Cited by 20

PHLDA1 promotes glioblastoma cell growth via sustaining the activation state of Ras

Wang, J., Yao, N., Hu, Y., Lei, M., Wang, M., Yang, L., Patel, S., Li, X., Liu, K., & Dong, Z. (2022) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-022-04538-1 · Cited by 20

New insights into RAS biology reinvigorate interest in mathematical modeling of RAS signaling

Erickson, K. E., Rukhlenko, O. S., Posner, R. G., Hlavacek, W. S., & Kholodenko, B. Ν. (2018) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2018.02.008 · Cited by 21

Allostery in Disease: Anticancer Drugs, Pockets, and the Tumor Heterogeneity Challenge

Nussinov, R., Yavuz, B. R., & Jang, H. (2025) · Journal of Molecular Biology · doi:10.1016/j.jmb.2025.169050 · Cited by 19

PPDPF Promotes the Development of Mutant KRAS‐Driven Pancreatic Ductal Adenocarcinoma by Regulating the GEF Activity of SOS1

Ni, Q., Zhu, B., Ji, Y., Zheng, Q., Liang, X., Ma, N., Jiang, H., Zhang, F., Shang, Y., Wang, Y., et al. (2022) · Advanced Science · doi:10.1002/advs.202202448 · Cited by 17

Supported lipid bilayers as dynamic platforms for tethered particles

Hartman, K. L., Kim, S., Kim, K., & Nam, J. (2014) · Nanoscale · doi:10.1039/c4nr05591h · Cited by 18

Fluctuation relations, effective temperature, and ageing of enzymes: The case of protein electron transfer

Matyushov, D. V. (2018) · Journal of Molecular Liquids · doi:10.1016/j.molliq.2018.06.087 · Cited by 18

Timing Correlations in Proteins Predict Functional Modules and Dynamic Allostery

Lin, M. M. (2016) · Journal of the American Chemical Society · doi:10.1021/jacs.5b08814 · Cited by 18

Multiple sources of signal amplification within the B-cell Ras/MAPK pathway

Mclaurin, J. D., & Weiner, O. D. (2019) · Molecular Biology of the Cell · doi:10.1091/mbc.e18-09-0560 · Cited by 16

On the relationship between cell cycle analysis with ergodic principles and age-structured cell population models

Kuritz, K., Stöhr, D., Pollak, N., & Allgöwer, F. (2016) · Journal of Theoretical Biology · doi:10.1016/j.jtbi.2016.11.024 · Cited by 15

Polarizability of the Active Site in Enzymatic Catalysis: Cytochrome c

Martin, D. R., Dinpajooh, M., & Matyushov, D. V. (2019) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.9b09236 · Cited by 16

Single-molecule phospholipase A2 becomes processive on melittin-induced membrane deformations

Jepson, T. A., Hall, S. C., & Chung, J. K. (2022) · Biophysical Journal · doi:10.1016/j.bpj.2022.03.019 · Cited by 15

Visualizing enzyme catalytic process using single-molecule techniques

Wang, H., Zhu, C., & Li, D. (2023) · TrAC Trends in Analytical Chemistry · doi:10.1016/j.trac.2023.117083 · Cited by 15

Advancements in gene therapies targeting mutant KRAS in cancers

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

Multicomponent Supported Membrane Microarray for Monitoring Spatially Resolved Cellular Signaling Reactions

Biswas, K. H., Zhongwen, C., Dubey, A. K., Oh, D., & Groves, J. T. (2018) · Advanced Biosystems · doi:10.1002/adbi.201800015 · Cited by 15

Graphene-Templated Supported Lipid Bilayer Nanochannels

Li, W., Chung, J. K., Lee, Y. K., & Groves, J. T. (2016) · Nano Letters · doi:10.1021/acs.nanolett.6b01798 · Cited by 14

Switching of the positive feedback for RAS activation by a concerted function of SOS membrane association domains

Nakamura, Y., Hibino, K., Yanagida, T., & Sako, Y. (2016) · Biophysics and Physicobiology · doi:10.2142/biophysico.13.0_1 · Cited by 15

Bridging intracellular scales by mechanistic computational models

Widmer, L. A., & Stelling, J. (2018) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2018.02.005 · Cited by 14

Nras Q61R/+ and Kras −/− cooperate to downregulate Rasgrp1 and promote lympho-myeloid leukemia in early T-cell precursors

Wen, Z. H., Yun, G., Hebert, A. S., Kong, G., Ranheim, E. A., Finn, R., Rajagoplan, A., Li, S., Zhou, Y., Yu, M., et al. (2021) · Blood · doi:10.1182/blood.2020009082 · Cited by 14

Anomalously Small Reorganization Energy of the Half Redox Reaction of Azurin

Sarhangi, S. M., & Matyushov, D. V. (2022) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.2c00338 · Cited by 14

Stochastic focusing coupled with negative feedback enables robust regulation in biochemical reaction networks

Milias‐Argeitis, A., Engblom, S., Bauer, P., & Khammash, M. (2015) · Journal of The Royal Society Interface · doi:10.1098/rsif.2015.0831 · Cited by 14

Understanding T cell signaling using membrane reconstitution

Hui, E. (2019) · Immunological Reviews · doi:10.1111/imr.12767 · Cited by 14

Immunotherapy in advanced, KRAS G12C-mutant non-small-cell lung cancer: current strategies and future directions

Ghazali, N., Garassino, M. C., Leighl, N. B., & Bestvina, C. M. (2025) · Therapeutic Advances in Medical Oncology · doi:10.1177/17588359251323985 · Cited by 13

Kinetics of PTEN-mediated PI(3,4,5)P3 hydrolysis on solid supported membranes

Liu, C., Deb, S., Ferreira, V. S., Xu, H. E., & Baumgart, T. (2018) · PLoS ONE · doi:10.1371/journal.pone.0192667 · Cited by 13

Bimodality in Ras signaling originates from processivity of the Ras activator SOS without deterministic bistability

Lee, A. A., Kim, N. H., Alvarez, S. A., Ren, H., DeGrandchamp, J. B., Lew, L. J. N., & Groves, J. T. (2024) · Science Advances · doi:10.1126/sciadv.adi0707 · Cited by 11

Lipid raft protein flotillin‐1 is important for the interaction between SOS1 and H‐Ras / K‐Ras , leading to Ras activation

Jin, H., Koh, M., Lim, H., Yong, H., Kim, E., Kim, S. Y., Kim, K., Jung, J., Ryu, W., Choi, K., et al. (2023) · International Journal of Cancer · doi:10.1002/ijc.34443 · Cited by 12

Dynamic disorder in simple enzymatic reactions induces stochastic amplification of substrate

Gupta, A., Milias‐Argeitis, A., & Khammash, M. (2017) · Journal of The Royal Society Interface · doi:10.1098/rsif.2017.0311 · Cited by 13

Allosteric autoactivation of SOS and its kinetic mechanism

Hoang, H. M., Umutesi, H. G., & Heo, J. (2019) · Small GTPases · doi:10.1080/21541248.2019.1601954 · Cited by 11

Recapitulation of cell-like KRAS4b membrane dynamics on complex biomimetic membranes

Shrestha, R., Chen, D., Frank, P. H., Nissley, D. V., & Turbyville, T. J. (2021) · iScience · doi:10.1016/j.isci.2021.103608 · Cited by 11

Fabrication of Multicomponent, Spatially Segregated DNA and Protein-Functionalized Supported Membrane Microarray

Biswas, K. H., Cho, N., & Groves, J. T. (2018) · Langmuir · doi:10.1021/acs.langmuir.8b01364 · Cited by 11

The invariances of power law size distributions

Frank, S. A. (2016) · F1000Research · doi:10.12688/f1000research.9452.1 · Cited by 10

A Membrane‐Associated Light‐Harvesting Model is Enabled by Functionalized Assemblies of Gene‐Doubled TMV Proteins

Dai, J., Wilhelm, K. B., Bischoff, A. J., Pereira, J. H., Dedeo, M. T., García-Almedina, D. M., Adams, P. D., Groves, J. T., & Francis, M. B. (2023) · Small · doi:10.1002/smll.202207805 · Cited by 9

Competition for shared downstream signaling molecules establishes indirect negative feedback between EGFR and EphA2

Oh, D., Chen, Z., Biswas, K. H., Bai, F., Ong, H. T., Sheetz, M. P., & Groves, J. T. (2022) · Biophysical Journal · doi:10.1016/j.bpj.2022.04.015 · Cited by 10

Nano-bio interfaces for electrical and biochemical signal transduction

Yang, X., Tsai, C., Yang, Y., Zhang, W., You, H., Forró, C., Pașca, S. P., & Cui, B. (2025) · Nature Reviews Bioengineering · doi:10.1038/s44222-025-00374-7 · Cited by 14

The invariances of power law size distributions

Frank, S. A. (2016) · F1000Research · doi:10.12688/f1000research.9452.3 · Cited by 9

Studying early structural changes in SOS1 mediated KRAS activation mechanism

Bhadhadhara, K., Jani, V., Koulgi, S., Sonavane, U., & Joshi, R. (2023) · Current Research in Structural Biology · doi:10.1016/j.crstbi.2023.100115 · Cited by 8

Einzelmolekül‐Sensoren: Herausforderungen und Möglichkeiten für die quantitative Analyse

Gooding, J. J., & Gaus, K. (2016) · Angewandte Chemie · doi:10.1002/ange.201600495 · Cited by 8

Positive cooperativity between RAS-binding and cysteine-rich domains regulates RAF membrane binding kinetics via lateral rebinding

Salinas, A. J., Tevdorashvili, K., Grim, J., Morales, A., Chakhrakia, A., & Lee, Y. K. (2026) · Nature Communications · doi:10.1038/s41467-026-69437-6 · Cited by 7

Discovery and Characterization of Divarasib (GDC-6036), a Potent Covalent Inhibitor of KRAS G12C

Endres, N., Do, S., Mroue, R. M., Terrett, J. A., Saabye, M., Oh, A., Hunsaker, T., Chan, E., (1471192), J. C. T., Nguyen, L. K., et al. (2026) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5c02272 · Cited by 8

Functional Dynamics and Allosteric Regulation of Ras Activation by SOS

Iversen, L., Tu, H., Lin, W., Christensen, S. M., Iwig, J. S., Gureasko, J. M., Kuriyan, J., & Groves, J. T. (2013) · Biophysical Journal · doi:10.1016/j.bpj.2012.11.689

Total Reconstitution of Receptor-Mediated Ras Activation by SOS in Vitro Reveals Kinetic and Conformational Layers of Regulation in MAPK Signaling

Alvarez, S. A., Huang, W. Y. C., Lam, H. Y. M., Low-Nam, S. T., Lee, Y. K., Chung, J. K., Hansen, S. D., Kondo, Y., Biswas, K. H., Kuriyan, J., et al. (2019) · Biophysical Journal · doi:10.1016/j.bpj.2018.11.2861

New Insights into the Mechanisms of SOS Activation

Quilliam, L. A. (2007) · Science s STKE · doi:10.1126/stke.4142007pe67 · Cited by 14

Allosteric autoactivation of SOS and its kinetic mechanism

Hoang, H. M., Umutesi, H. G., & Heo, J. (2019) · Small GTPases · doi:10.1080/21541248.2019.1601954 · Cited by 11

A SOS in regulation of the SOS/ RAS positive feedback loop as identified by using single-molecule analysis in living cells

中村, 由. (2016) · OUKA (Osaka University Knowledge Archive) (Osaka University) · doi:10.18910/56116