Inhibition of K-RAS4B by a Unique Mechanism of Action: Stabilizing Membrane-Dependent Occlusion of the Effector-Binding Site

NMRPipe: A multidimensional spectral processing system based on UNIX pipes

Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., & Bax, A. (1995) · Journal of Biomolecular NMR · doi:10.1007/bf00197809 · Cited by 15,994 · see citing works

PRODRG: a tool for high-throughput crystallography of protein–ligand complexes

Schüttelkopf, A. W., & van Aalten, D. M. F. (2004) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444904011679 · Cited by 4,815 · see citing works

The HADDOCK2.2 Web Server: User-Friendly Integrative Modeling of Biomolecular Complexes

van Zundert, G. C. P., Rodrigues, J. P. G. L. M., Trellet, M., Schmitz, C., Kastritis, P. L., Karaca, E., Melquiond, A. S. J., van Dijk, M., de Vries, S. J., & Bonvin, A. M. J. J. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2015.09.014 · Cited by 2,785 · see citing works

NMRFAM-SPARKY: enhanced software for biomolecular NMR spectroscopy

Lee, W., Tonelli, M., & Markley, J. L. (2014) · Bioinformatics · doi:10.1093/bioinformatics/btu830 · Cited by 2,076 · 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

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

Directed Self-Assembly of Monodisperse Phospholipid Bilayer Nanodiscs with Controlled Size

Denisov, I. G., Grinkova, Y. V., Lazarides, A. A., & Sligar, S. G. (2004) · Journal of the American Chemical Society · doi:10.1021/ja0393574 · Cited by 1,066 · 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

Regulation of RAF protein kinases in ERK signalling

Lavoie, H., & Therrien, M. (2015) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3979 · Cited by 683 · 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

Small-molecule ligands bind to a distinct pocket in Ras and inhibit SOS-mediated nucleotide exchange activity

Maurer, T., Garrenton, L. S., Oh, A., Pitts, K., Anderson, D. J., Skelton, N. J., Fauber, B. P., Pan, B., Malek, S., Stokoe, D., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1116510109 · Cited by 618 · see citing works

Methods for Measurement of Intermolecular NOEs by Multinuclear NMR Spectroscopy: Application to a Bacteriophage λ N-Peptide/boxB RNA Complex

Zwahlen, C., Legault, P., Vincent, S. J. F., Greenblatt, J., Konrat, R., & Kay, L. E. (1997) · Journal of the American Chemical Society · doi:10.1021/ja970224q · Cited by 606 · see citing works

A robust and cost-effective method for the production of Val, Leu, Ile (δ1) methyl-protonated 15N-, 13C-, 2H-labeled proteins

Goto, N. K., Gardner, K. H., Mueller, G. A., Willis, R. C., & Kay, L. E. (1999) · Journal of Biomolecular NMR · doi:10.1023/a:1008393201236 · Cited by 512 · see citing works

Discovery of Small Molecules that Bind to K‐Ras and Inhibit Sos‐Mediated Activation

Sun, Q., Burke, J. P., Phan, J., Burns, M. C., Olejniczak, E. T., Waterson, A. G., Lee, T., Rossanese, O. W., & Fesik, S. W. (2012) · Angewandte Chemie International Edition · doi:10.1002/anie.201201358 · Cited by 490 · see citing works

X-ray structures of general anaesthetics bound to a pentameric ligand-gated ion channel

Nury, H., Van Renterghem, C., Weng, Y., Tran, A., Baaden, M., Dufresne, V., Changeux, J.-P., Sonner, J. M., Delarue, M., & Corringer, P.-J. (2011) · Nature · doi:10.1038/nature09647 · Cited by 412 · see citing works

Inhibition of RAS function through targeting an allosteric regulatory site

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

Effective rotational correlation times of proteins from NMR relaxation interference

Lee, D., Hilty, C., Wider, G., & Kurt Wüthrich, A. (2005) · Journal of Magnetic Resonance · doi:10.1016/j.jmr.2005.08.014 · Cited by 269 · see citing works

Oncogenic and RASopathy-associated K-RAS mutations relieve membrane-dependent occlusion of the effector-binding site

Mazhab-Jafari, M. T., Marshall, C. B., Smith, M. J., Gasmi-Seabrook, G. M. C., Stathopulos, P. B., Inagaki, F., Kay, L. E., Neel, B. G., & Ikura, M. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1419895112 · Cited by 220 · see citing works

Small-molecule modulation of Ras signaling

Spiegel, J., Cromm, P. M., Zimmermann, G., Grossmann, T. N., & Waldmann, H. (2014) · Nature Chemical Biology · doi:10.1038/nchembio.1560 · Cited by 215 · see citing works

Isotope-filtered NMR methods for the study of biomolecular structure and interactions

Breeze, A. L. (2000) · Progress in Nuclear Magnetic Resonance Spectroscopy · doi:10.1016/s0079-6565(00)00020-0 · Cited by 202 · see citing works

Nanodiscs as a New Tool to Examine Lipid–Protein Interactions

Schuler, M. A., Denisov, I. G., & Sligar, S. G. (2012) · Methods in molecular biology · doi:10.1007/978-1-62703-275-9_18 · Cited by 153 · see citing works

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

Prakash, P., Zhou, Y., Hong, L., Hancock, J. F., & Gorfe, A. A. (2016) · Biophysical Journal · doi:10.1016/j.bpj.2016.01.019 · Cited by 135 · see citing works

Integrated RAS signaling defined by parallel NMR detection of effectors and regulators

Smith, M. J., & Ikura, M. (2014) · Nature Chemical Biology · doi:10.1038/nchembio.1435 · Cited by 87 · see citing works

Crystal structures of the state 1 conformations of the GTP‐bound H‐Ras protein and its oncogenic G12V and Q61L mutants

Muraoka, S., Shima, F., Araki, M., Inoue, T., Yoshimoto, A., Ijiri, Y., Seki, N., Tamura, A., Kumasaka, T., Yamamoto, M., et al. (2012) · FEBS Letters · doi:10.1016/j.febslet.2012.04.058 · Cited by 81 · see citing works

The cellular membrane as a mediator for small molecule interaction with membrane proteins

Mayne, C. G., Arcario, M. J., Mahinthichaichan, P., Baylon, J. L., Vermaas, J. V., Navidpour, L., Wen, P., Thangapandian, S., & Tajkhorshid, E. (2016) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2016.04.016 · Cited by 47 · see citing works

Requirements on Paramagnetic Relaxation Enhancement Data for Membrane Protein Structure Determination by NMR

Gottstein, D., Reckel, S., Dötsch, V., & Güntert, P. (2012) · Structure · doi:10.1016/j.str.2012.03.010 · Cited by 40 · see citing works

Phosphoinositide-incorporated lipid–protein nanodiscs: A tool for studying protein–lipid interactions

Kobashigawa, Y., Harada, K., Yoshida, N., Ogura, K., & Inagaki, F. (2010) · Analytical Biochemistry · doi:10.1016/j.ab.2010.11.021 · Cited by 31 · see citing works

Inhibition of prenylated KRAS in a lipid environment

Jansen, J. M., Wartchow, C. A., Jahnke, W., Fong, S. K., Tsang, T., Pfister, K. B., Zavorotinskaya, T., Bussiere, D. E., Cheng, J. M., Crawford, K. R., et al. (2017) · PLoS ONE · doi:10.1371/journal.pone.0174706 · Cited by 29 · see citing works

Automated NMR Resonance Assignment of Large Proteins for Protein−Ligand Interaction Studies

Gossert, A. D., Hiller, S., & Fernández, C. F. (2010) · Journal of the American Chemical Society · doi:10.1021/ja108383x · Cited by 27 · see citing works

RAS-targeted therapies: is the undruggable drugged?

Moore, A. R., Rosenberg, S. C., McCormick, F., & Malek, S. (2020) · Nature Reviews Drug Discovery · doi:10.1038/s41573-020-0068-6 · Cited by 1,103 · see citing works

Phase separation of FSP1 promotes ferroptosis

Nakamura, T., Hipp, C., Mourão, A., Borggräfe, J., Aldrovandi, M., Henkelmann, B., Wanninger, J., Mishima, E., Lytton, E., Emler, D., et al. (2023) · Nature · doi:10.1038/s41586-023-06255-6 · Cited by 365 · see citing works

The current understanding of KRAS protein structure and dynamics

Pantsar, T. (2019) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2019.12.004 · Cited by 288 · see citing works

KRAS interaction with RAF1 RAS-binding domain and cysteine-rich domain provides insights into RAS-mediated RAF activation

Tran, T. H., Chan, A. H., Young, L. C., Bindu, L. K., Neale, C., Messing, S. A. J., Dharmaiah, S., Taylor, T. E., Denson, J.-P., Esposito, D., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-21422-x · Cited by 245 · 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

Pharmacological targeting of RAS: recent success with direct inhibitors

O’Bryan, J. P. (2019) · Pharmacological Research · doi:10.1016/j.phrs.2018.10.021 · Cited by 153 · see citing works

RAS signaling in carcinogenesis, cancer therapy and resistance mechanisms

Yang, X., & Wu, H. K. (2024) · Journal of Hematology & Oncology · doi:10.1186/s13045-024-01631-9 · Cited by 123 · see citing works

Therapeutic targeting of RAS: New hope for drugging the “undruggable”

Khan, I., Rhett, J. M., & O’Bryan, J. P. (2019) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2019.118570 · Cited by 109 · see citing works

Machine learning–driven multiscale modeling reveals lipid-dependent dynamics of RAS signaling proteins

Ingólfsson, H. I., Neale, C., Carpenter, T. S., Shrestha, R., López, C. A., Tran, T. H., Oppelstrup, T., Bhatia, H., Stanton, L. G., Zhang, X., et al. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2113297119 · Cited by 92 · see citing works

Integrative Modelling of Biomolecular Complexes

Koukos, P. I., & Bonvin, A. M. J. J. (2019) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.11.009 · Cited by 89 · see citing works

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

Yin, G., Huang, J., Petela, J., Jiang, H., Zhang, Y., Gong, S., Wu, J., Liu, B., Shi, J., & Gao, Y. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01441-4 · Cited by 87 · see citing works

Multivalent assembly of KRAS with the RAS-binding and cysteine-rich domains of CRAF on the membrane

Fang, Z., Lee, K., Huo, K.-G., Gasmi-Seabrook, G. M. C., Zheng, L., Moghal, N., Tsao, M., Ikura, M., & Marshall, C. B. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1914076117 · Cited by 74 · see citing works

Intrinsically disordered proteins and membranes: a marriage of convenience for cell signalling?

Cornish, J., Chamberlain, S. G., Owen, D., & Mott, H. R. (2020) · Biochemical Society Transactions · doi:10.1042/bst20200467 · Cited by 69 · see citing works

Cryo-EM and MD infer water-mediated proton transport and autoinhibition mechanisms of V o complex

Roh, S., Shekhar, M., Pintilie, G. D., Chipot, C. J., Wilkens, S., Singharoy, A., & Chiu, W. (2020) · Science Advances · doi:10.1126/sciadv.abb9605 · Cited by 71 · see citing works

Progress in targeting RAS with small molecule drugs

McCormick, F. P. (2019) · Biochemical Journal · doi:10.1042/bcj20170441 · Cited by 63 · see citing works

Stopping the beating heart of cancer: KRAS reviewed

Herdeis, L., Gerlach, D., McConnell, D. B., & Kessler, D. (2021) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2021.06.013 · Cited by 63 · see citing works

Lipid Nanodiscs for High-Resolution NMR Studies of Membrane Proteins

Günsel, U., & Hagn, F. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.1c00702 · Cited by 62 · see citing works

K-Ras G-domain binding with signaling lipid phosphatidylinositol (4,5)-phosphate (PIP2): membrane association, protein orientation, and function

Cao, S., Chung, S., Kim, S., Li, Z., Manor, D., & Buck, M. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.004021 · Cited by 62 · see citing works

Uncovering a membrane-distal conformation of KRAS available to recruit RAF to the plasma membrane

Van, Q. N., López, C. A., Tonelli, M., Taylor, T. E., Niu, B., Stanley, C. B., Bhowmik, D., Tran, T. H., Frank, P. H., Messing, S. A. J., et al. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2006504117 · Cited by 58 · see citing works

The Plasma Membrane as a Competitive Inhibitor and Positive Allosteric Modulator of KRas4B Signaling

Neale, C., & García, A. E. (2020) · Biophysical Journal · doi:10.1016/j.bpj.2019.12.039 · Cited by 56 · see citing works

KRAS: A Druggable Target in Colon Cancer Patients

Negri, F., Bottarelli, L., de’Angelis, G. L., & Gnetti, L. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23084120 · Cited by 55 · see citing works

Integrative modeling of membrane-associated protein assemblies

Roel‐Touris, J., Jiménez‐García, B., & Bonvin, A. M. J. J. (2020) · Nature Communications · doi:10.1038/s41467-020-20076-5 · Cited by 53 · see citing works

Probing the Conformational and Energy Landscapes of KRAS Membrane Orientation

Prakash, P., & Gorfe, A. A. (2019) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.9b05796 · Cited by 51 · see citing works

Mechanisms of Ras Membrane Organization and Signaling: Ras Rocks Again

Abankwa, D., & Gorfe, A. A. (2020) · Biomolecules · doi:10.3390/biom10111522 · Cited by 48 · see citing works

1H, 15N backbone assignment and comparative analysis of the wild type and G12C, G12D, G12V mutants of K-Ras bound to GDP at physiological pH

Pálfy, G., Vida, I., & Perczel, A. (2019) · Biomolecular NMR Assignments · doi:10.1007/s12104-019-09909-7 · Cited by 39 · see citing works

Approaches to inhibiting oncogenic K-Ras

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

Real-Time In-Cell NMR Reveals the Intracellular Modulation of GTP-Bound Levels of RAS

Zhao, Q., Fujimiya, R., Kubo, S., Marshall, C. B., Ikura, M., Shimada, I., & Nishida, N. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.108074 · Cited by 35 · see citing works

Pioneer in Molecular Biology: Conformational Ensembles in Molecular Recognition, Allostery, and Cell Function

Nussinov, R. (2025) · Journal of Molecular Biology · doi:10.1016/j.jmb.2025.169044 · Cited by 33 · see citing works

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 31 · see citing works

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 · 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

Molecular dynamics simulations for the structure-based drug design: targeting small-GTPases proteins

Parise, A., Cresca, S., & Magistrato, A. (2024) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2024.2387856 · Cited by 27 · see citing works

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 · see citing works

Calmodulin disrupts plasma membrane localization of farnesylated KRAS4b by sequestering its lipid moiety

Grant, B., Enomoto, M., Back, S.-I., Lee, K., Gebregiworgis, T., Ishiyama, N., Ikura, M., & Marshall, C. B. (2020) · Science Signaling · doi:10.1126/scisignal.aaz0344 · Cited by 26 · see citing works

Exploring CRD mobility during RAS/RAF engagement at the membrane

Nguyen, K., López, C. A., Neale, C., Van, Q. N., Carpenter, T. S., Natale, F. D., Travers, T. S., Tran, T. H., Chan, A. H., Bhatia, H., et al. (2022) · Biophysical Journal · doi:10.1016/j.bpj.2022.06.035 · Cited by 27 · see citing works

Direct Modulators of K-Ras–Membrane Interactions

Morstein, J., Shrestha, R., Van, Q. N., López, C. A., Arora, N., Tonelli, M., Hong, L., Chen, D., Zhou, Y., Hancock, J. F., et al. (2023) · ACS Chemical Biology · doi:10.1021/acschembio.3c00413 · Cited by 26 · see citing works

Dynamic conformational equilibria in the active states of KRAS and NRAS

Rennella, E., Henry, C., Dickson, C. J., Georgescauld, F., Wales, T. E., Erdmann, D., Cotesta, S., Maira, S.-M., Sedrani, R. C., Brachmann, S. M., et al. (2024) · RSC Chemical Biology · doi:10.1039/d4cb00233d · Cited by 24 · see citing works

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 · see citing works

Eliminating oncogenic RAS: back to the future at the drawing board

Steffen, C. L., Kaya, P., Schaffner‐Reckinger, E., & Abankwa, D. (2023) · Biochemical Society Transactions · doi:10.1042/bst20221343 · Cited by 23 · see citing works

How Anionic Lipids Affect Spatiotemporal Properties of KRAS4B on Model Membranes.

Ngo, V. A., Sarkar, S., Neale, C., & Garcia, A. (2020) · Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.0c02642 · Cited by 23 · see citing works

Organization of Farnesylated, Carboxymethylated KRAS4B on Membranes

Barklis, E., Stephen, A. G., Staubus, A. O., Barklis, R. L., & Alfadhli, A. (2019) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.07.025 · Cited by 20 · see citing works

Lipid nanodiscs as a template for high-resolution cryo-EM structures of peripheral membrane proteins

Cannon, K. S., Sarsam, R. D., Tedamrongwanish, T., Zhang, K., & Baker, R. W. (2023) · Journal of Structural Biology · doi:10.1016/j.jsb.2023.107989 · Cited by 19 · see citing works

Computational Design of Myristoylated Cell-Penetrating Peptides Targeting Oncogenic K-Ras.G12D at the Effector-Binding Membrane Interface

Li, Z., & Buck, M. (2019) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.9b00690 · Cited by 19 · see citing works

Correlation of O2 transport on the micro and macro scale.

Honig, C. R., & Gayeski, T. E. (1982) · PubMed · Cited by 17 · see citing works

Methylation of KRAS by SETD7 promotes KRAS degradation in non-small cell lung cancer

Chiang, C.-Y., Fan, S., Zheng, H., Guo, W., Zheng, Z., Sun, Y., Zhong, C., Zeng, J., Li, S., Zhang, M., et al. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.113003 · Cited by 16 · see citing works

Mutations in the α4-α5 allosteric lobe of RAS do not significantly impair RAS signaling or self-association

Whaby, M., Wallon, L., Mazzei, M., Khan, I., Teng, K. W., Koide, S., & O’Bryan, J. P. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102661 · Cited by 17 · see citing works

Direct Observation of Membrane-Associated H-Ras in the Native Cellular Environment by In-Cell 19F-NMR Spectroscopy

Ikari, M., Yagi, H., Kasai, T., Inomata, K., Ito, M., Higuchi, K., Matsuda, N., Ito, Y., & Kigawa, T. (2023) · JACS Au · doi:10.1021/jacsau.3c00108 · Cited by 15 · see citing works

Nanodiscs for Structural Biology in a Membranous Environment

Yokogawa, M., Fukuda, M., & Osawa, M. (2019) · Chemical and Pharmaceutical Bulletin · doi:10.1248/cpb.c18-00941 · Cited by 15 · see citing works

The role of NMR in leveraging dynamics and entropy in drug design

Dubey, A., Takeuchi, K., Reibarkh, M., & Arthanari, H. (2020) · Journal of Biomolecular NMR · doi:10.1007/s10858-020-00335-9 · Cited by 15 · see citing works

NMR in integrated biophysical drug discovery for RAS: past, present, and future

Marshall, C. B., KleinJan, F., Gebregiworgis, T., Lee, K., Fang, Z., Eves, B. J., Liu, N. F., Gasmi-Seabrook, G. M. C., Enomoto, M., & Ikura, M. (2020) · Journal of Biomolecular NMR · doi:10.1007/s10858-020-00338-6 · Cited by 15 · see citing works

Unveiling the Dynamics of KRAS4b on Lipid Model Membranes

López, C., Agarwal, A., Van, Q. N., Stephen, A., & Gnanakaran, S. (2021) · Journal of Membrane Biology · doi:10.1007/s00232-021-00176-z · Cited by 13 · see citing works

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 · see citing works

Early-stage structure-based drug discovery for small GTPases by NMR spectroscopy

Yin, G., Lv, G., Zhang, J., Jiang, H., Lai, T., Yang, Y., Ren, Y., Wang, J., Yi, C., Chen, H., et al. (2022) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2022.108110 · Cited by 10 · see citing works

A Top-Down Proteomic Assay to Evaluate KRAS4B-Compound Engagement

D'Ippolito, R., Rabara, D., Blanco, M. A., Alberico, E. O., Drew, M. R., Ramakrishnan, N., Sontan, D., Widmeyer, S. R. T., Scheidemantle, G. M., Messing, S., et al. (2024) · Analytical Chemistry · doi:10.1021/acs.analchem.3c05626 · Cited by 7 · see citing works

How to make an undruggable enzyme druggable: lessons from ras proteins

Sayyed–Ahmad, A., & Gorfe, A. A. (2020) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2020.05.003 · Cited by 10 · see citing works

Quantitative Paramagnetic NMR-Based Analysis of Protein Orientational Dynamics on Membranes: Dissecting the KRas4B-Membrane Interactions

Gu, X., Liu, D., Yu, Y., Wang, H., & Long, D. (2023) · Journal of the American Chemical Society · doi:10.1021/jacs.3c01597 · Cited by 10 · see citing works

Monoubiquitination of KRAS at Lysine104 and Lysine147 Modulates Its Dynamics and Interaction with Partner Proteins

Nair, V. V., Yin, G., Zhang, J., Hancock, J. F., Campbell, S. L., & Gorfe, A. A. (2021) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.1c01062 · Cited by 9 · see citing works

Membrane-bound KRAS approximates an entropic ensemble of configurations

Heinrich, F., Van, Q. N., Jean-Francois, F. L., Stephen, A. G., & Lösche, M. (2021) · Biophysical Journal · doi:10.1016/j.bpj.2021.08.008 · Cited by 9 · see citing works

Target Genetic Abnormalities for the Treatment of Colon Cancer and Its Progression to Metastasis

Baviskar, T., Momin, M. M., Liu, J., Guo, B., & Bhatt, L. K. (2020) · Current Drug Targets · doi:10.2174/1389450121666201119141015 · Cited by 11 · see citing works

Membrane Composition and Raf[CRD]-Membrane Attachment Are Driving Forces for K-Ras4B Dimer Stability

Andreadelis, I., Kiriakidi, S., Lamprakis, C., Theodoropoulou, A., Doerr, S., Chatzigoulas, A., Manchester, J. I., Velez‐Vega, C., Duca, J. S., & Cournia, Z. (2022) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.1c01184 · Cited by 9 · see citing works

Membrane-Driven Dimerization of the Peripheral Membrane Protein KRAS: Implications for Downstream Signaling

Lee, K. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25052530 · Cited by 8 · see citing works

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 · see citing works

Unraveling the Genetic Web: H-Ras Expression and Mutation in Oral Squamous Cell Carcinoma—A Systematic Review

Devi, P., Dwivedi, R., Sankar, R., Jain, A., Gupta, S., & Gupta, S. (2024) · Head and Neck Pathology · doi:10.1007/s12105-024-01623-8 · Cited by 8 · see citing works

Spotlight on the Ballet of Proteins: The Structural Dynamic Properties of Proteins Illuminated by Solution NMR

Tokunaga, Y., Viennet, T., Arthanari, H., & Takeuchi, K. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21051829 · Cited by 8 · see citing works

RLIP76: A Structural and Functional Triumvirate

Cornish, J., Owen, D., & Mott, H. R. (2021) · Cancers · doi:10.3390/cancers13092206 · Cited by 8 · see citing works

Conserved allosteric perturbation of the GTPase domains by region 1 of Ras hypervariable regions

Gu, X. Q., Zhang, Y., & Long, D. (2024) · Biophysical Journal · doi:10.1016/j.bpj.2024.02.022 · Cited by 6 · see citing works

From disorder comes function: Regulation of small GTPase function by intrinsically disordered lipidated membrane anchor

Hutchins, C. M., & Gorfe, A. A. (2024) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2024.102869 · Cited by 5 · see citing works

Natural Product Graveoline Modulates Kirsten Rat Sarcoma Viral Oncogene Homologue (KRAS) Membrane Association: Insights from Advanced Spectroscopic Studies

Cornilescu, G., Bindu, L. K., Sternicki, L. M., Chao, F.-A., Gillette, W., Fer, N. D., Colombus, J., Castillo, J., Bonilla, P. A., Van, Q. N., et al. (2024) · ACS Pharmacology & Translational Science · doi:10.1021/acsptsci.4c00075 · Cited by 5 · see citing works

A regulatory role of membrane by direct modulation of the catalytic kinase domain

Prakash, P. (2020) · Small GTPases · doi:10.1080/21541248.2020.1788886 · Cited by 5 · see citing works

Water in Ras Superfamily Evolution

Marcus, K., & Mattos, C. (2019) · Journal of Computational Chemistry · doi:10.1002/jcc.26060 · Cited by 5 · see citing works

An Integrative Framework for Mapping Orientational Landscapes of Peripheral Membrane Proteins by Paramagnetic NMR and Atomistic Simulation

Liu, D., Ni, Y., Shui, L., & Long, D. (2025) · JACS Au · doi:10.1021/jacsau.5c00331 · Cited by 4 · see citing works

RAS–membrane interaction and oligomerization: there is more than meets the eye

Sianoya, A. C., Bhardwaj, V. K., & Gorfe, A. A. (2025) · Biochemical Society Transactions · doi:10.1042/bst20253030 · Cited by 4 · see citing works

Antipsychotic phenothiazine drugs bind to KRAS in vitro

Wang, X., Gorfe, A. A., & Putkey, J. A. (2021) · Journal of Biomolecular NMR · doi:10.1007/s10858-021-00371-z · Cited by 4 · see citing works

Comprehensive classification of proteins based on structures that engage lipids by COMPOSEL

Overduin, M., Kervin, T. A., Klarenbach, Z., Adra, T. R. C., & Bhat, R. K. (2023) · Biophysical Chemistry · doi:10.1016/j.bpc.2023.106971 · Cited by 4 · see citing works

The hanging heart: How KRAS lures its prey to the membrane

Kessler, D., & McConnell, D. B. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2017730117 · Cited by 2 · see citing works

1 H, 15 N and 13 C resonance assignments of the Q61H mutant of human KRAS bound to GDP

Huang, Q., Ng, E. Y., Li, Q., & Kang, C. (2021) · Biomolecular NMR Assignments · doi:10.1007/s12104-021-10058-z · Cited by 2 · see citing works

Biophysical and Biochemical Characterization of Structurally Diverse Small Molecule Hits for KRAS Inhibition

Pagba, C. V., Gupta, A. K., Dilsha, K. M., Sadrpour, P., Jakubec, J. L., Prakash, P., van der Hoeven, D., Cho, K., Gilbertson, S. R., & Gorfe, A. A. (2024) · ChemBioChem · doi:10.1002/cbic.202300827 · Cited by 1 · see citing works

Membrane Proteins in Nanodiscs: Methods and Applications

Guo, J., Hou, Q., Tan, Y., Fu, R., Huang, X., & Cao, C. (2025) · ChemMedChem · doi:10.1002/cmdc.202400775 · Cited by 1 · see citing works

The evolution of RAS structural biology

Simanshu, D. K., & Knox, J. E. (2024) · Elsevier eBooks · doi:10.1016/b978-0-443-21861-3.00012-7 · Cited by 1 · see citing works

Methylation of KRAS at lysine 182 and 184 by SETD7 promotes KRAS degradationPreprint

Chiang, C., Xiao, T., Fan, S., Zheng, H., Li, S., Guo, W., Zhang, M., Zhong, C., Zeng, J., & Zheng, D. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.02.10.429309 · Cited by 1 · see citing works

Membrane Composition and Raf[CRD]-Membrane Attachment Are Driving Forces for K-Ras4B Dimer StabilityPreprint

Cournia, Z., Andreadelis, I., Kiriakidi, S., Lamprakis, C., Theodoropoulou, A., Doerr, S., Chatzigoulas, A., Manchester, J. I., Velez‐Vega, C., & Duca, J. S. (2021) · doi:10.33774/chemrxiv-2021-4pdzb · Cited by 1 · see citing works

Membrane Composition and Raf[CRD]-Membrane Attachment Are Driving Forces for K-Ras4B Dimer StabilityPreprint

Cournia, Z., Andreadelis, I., Kiriakidi, S., Lamprakis, C., Theodoropoulou, A., Doerr, S., Chatzigoulas, A., Manchester, J. I., Velez‐Vega, C., & Duca, J. S. (2021) · ChemRxiv · doi:10.26434/chemrxiv-2021-4pdzb

Quantitative Membrane Paramagnetic Relaxation Enhancement (mPRE) Measurements on Lipid-Anchored Proteins: Insight into Orientational Dynamics

Wu, J., Yu, Y., Wang, L., Ji, L., Liu, D., Fang, M., Zheng, J., & Long, D. (2026) · Journal of the American Chemical Society · doi:10.1021/jacs.5c18374

Activation des petites GTPases à la périphérie des membranes

Peurois, F. (2018) · doi:10.70675/17a7d716zcb19z4e3cz9dbfz49690c621294

The Nanodisc System for Investigating Protein–Lipid Interactions

Denisov, I. G., & Sligar, S. G. (2026) · Methods in molecular biology · doi:10.1007/978-1-0716-5054-7_26

Allostery in the Ras-Raf-PI3K-PTEN signaling network at the membrane: Implications for drug discovery

Nussinov, R., & Jang, H. (2026) · The Journal of Chemical Physics · doi:10.1063/5.0354338

Interaction of KRas4B protein with C6-ceramide containing lipid model membranes

Li, L., Dwivedi, M., Erwin, N., Möbitz, S., Nußbaumer, P., & Winter, R. (2018) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2018.01.016 · Cited by 3 · see citing works

Inhibition of K-Ras4B-plasma membrane association with a membrane microdomain-targeting peptide

Li, F.-Y., Zhang, Z., Voß, S., Wu, Y., Zhao, Y., Li, Y., & Chen, Y. (2019) · Chemical Science · doi:10.1039/c9sc04726c · Cited by 8 · see citing works

Dissociation of the Signaling Protein K‐Ras4B from Lipid Membranes Induced by a Molecular Tweezer

Li, L., Erwin, N., Möbitz, S., Niemeyer, F. C., Schrader, T. H., & Winter, R. (2019) · Chemistry - A European Journal · doi:10.1002/chem.201901861 · Cited by 6 · see citing works

The Plasma Membrane as a Competitive Inhibitor and Positive Allosteric Modulator of KRas4B Signaling

Neale, C., & García, A. E. (2020) · Biophysical Journal · doi:10.1016/j.bpj.2019.12.039 · Cited by 56 · see citing works

Quantitative biophysical analysis defines key components modulating recruitment of the GTPase KRAS to the plasma membrane

Lakshman, B., Messing, S. A. J., Schmid, E. M., Clogston, J. D., Gillette, W., Esposito, D., Kessing, B. D., Fletcher, D. A., Nissley, D. V., McCormick, F. P., et al. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.005669 · Cited by 43 · see citing works