{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,1]],"date-time":"2026-09-01T09:18:27Z","timestamp":1788254307735,"version":"build-2803163510"},"reference-count":85,"publisher":"American Chemical Society (ACS)","issue":"33","license":[{"start":{"date-parts":[[2026,8,14]],"date-time":"2026-08-14T00:00:00Z","timestamp":1786665600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000054","name":"National Cancer Institute","doi-asserted-by":"publisher","award":["1R01CA303154"],"award-info":[{"award-number":["1R01CA303154"]}],"id":[{"id":"10.13039\/100000054","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/na","name":"National Science Foundation","doi-asserted-by":"publisher","award":["MCB-2103637"],"award-info":[{"award-number":["MCB-2103637"]}],"id":[{"id":"10.13039\/na","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/na","name":"National Science Foundation","doi-asserted-by":"publisher","award":["MCB-2531447"],"award-info":[{"award-number":["MCB-2531447"]}],"id":[{"id":"10.13039\/na","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2026,8,26]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>The Ras-Raf protein association initiates the downstream mitogen-activated protein kinase (MAPK) signaling cascade. This interaction depends on the Ras-nucleotide ligand, whereby Raf preferentially binds to the active guanosine triphosphate (GTP)-loaded state over the guanosine diphosphate (GDP)-loaded state of Ras. Whether GDP-bound Ras can also form specific protein\u2013protein interactions with Raf, however, remains unclear. Here, we characterize the interaction between human K-Ras in both nucleotide states and the Ras-binding domain (RBD) of B-Raf by solution NMR. Active K-Ras\u00b7GTP forms a tight, conformationally restricted complex with RBD, causing pronounced chemical shift perturbations at the binding interface consistent with existing cryo-EM and X-ray crystallography structures. Surprisingly, we detect specific binding between \u201cinactive\u201d wild-type K-Ras\u00b7GDP with RBD in the millimolar affinity range, whereby the oncogenic G12D mutant of K-Ras further strengthens this interaction. NMR relaxation dispersion and chemical exchange saturation transfer (CEST) experiments allow the detailed structural characterization of the transient K-Ras\u00b7GDP\u00b7RBD complex, along with the determination of the interaction affinity and kinetics. The results demonstrate that the transient K-Ras\u00b7GDP\u00b7RBD bound state closely resembles the active K-Ras\u00b7GTP\u00b7RBD complex, providing a quantitative understanding at the backbone 15N-level of the nucleotide-specific K-Ras-Raf interaction. These findings underscore the prospect of the highly adaptable GDP-bound state of K-Ras for both signaling and as a drug target.<\/jats:p>","DOI":"10.1021\/jacs.6c09870","type":"journal-article","created":{"date-parts":[[2026,8,14]],"date-time":"2026-08-14T13:02:51Z","timestamp":1786712571000},"page":"35961-35972","source":"Crossref","is-referenced-by-count":0,"title":["GDP-Loaded K-Ras\nTransiently Binds to Effector\nB-Raf RBD, Mirroring the Structure of the Active GTP-Loaded\nComplex"],"prefix":"10.1021","volume":"148","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-8584-3642","authenticated-orcid":true,"given":"Xinyao","family":"Xiang","sequence":"first","affiliation":[{"name":"The Ohio State University , , , ,","place":["Columbus, Ohio, United States, 43210"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mamata","family":"Basnet","sequence":"additional","affiliation":[{"name":"The Ohio State University , , , ,","place":["Columbus, Ohio, United States, 43210"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Chunhua","family":"Yuan","sequence":"additional","affiliation":[{"name":"The Ohio State University , , , ,","place":["Columbus, Ohio, United States, 43210"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lei","family":"Bruschweiler-Li","sequence":"additional","affiliation":[{"name":"The Ohio State University , , , ,","place":["Columbus, Ohio, United States, 43210"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3649-4543","authenticated-orcid":true,"given":"Rafael","family":"Bru\u0308schweiler","sequence":"additional","affiliation":[{"name":"The Ohio State University , , , ,","place":["Columbus, Ohio, United States, 43210"]},{"name":"The Ohio State University , , , ,","place":["Columbus, Ohio, United States, 43210"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2026,8,14]]},"reference":[{"issue":"7","key":"2026090104492072200_cit1","doi-asserted-by":"publisher","first-page":"425","DOI":"10.1016\/S0898-6568(00)00084-X","article-title":"The Importance of Being K-Ras","volume":"12","author":"Ellis","year":"2000","journal-title":"Cell. Signalling"},{"key":"2026090104492072200_cit2","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/bs.acr.2021.07.003","article-title":"A Brief History\nof RAS and the RAS Initiative","volume":"153","author":"McCormick","year":"2022","journal-title":"Adv. Cancer Res."},{"key":"2026090104492072200_cit3","doi-asserted-by":"publisher","first-page":"103183","DOI":"10.1016\/j.sbi.2025.103183","article-title":"Recent Breakthroughs\nin Understanding the Allosteric Features of\nRas GTPases and Their Effector and Regulatory Protein Interactions,\nEnabling Drug Design","volume":"96","author":"Bhattarai","year":"2026","journal-title":"Curr. Opin. Struct. Biol."},{"issue":"5","key":"2026090104492072200_cit4","doi-asserted-by":"publisher","first-page":"865","DOI":"10.1016\/j.cell.2007.05.018","article-title":"GEFs and GAPs:\nCritical Elements\nin the Control of Small G Proteins","volume":"129","author":"Bos","year":"2007","journal-title":"Cell"},{"issue":"8","key":"2026090104492072200_cit5","doi-asserted-by":"publisher","first-page":"831","DOI":"10.1515\/hsz-2014-0257","article-title":"Ras Activation\nRevisited: Role of GEF and GAP Systems","volume":"396","author":"Hennig","year":"2015","journal-title":"Biol.\nChem."},{"issue":"14","key":"2026090104492072200_cit6","doi-asserted-by":"publisher","first-page":"2969","DOI":"10.1158\/0008-5472.CAN-19-3682","article-title":"The Frequency of Ras Mutations in\nCancer","volume":"80","author":"Prior","year":"2020","journal-title":"Cancer Res."},{"key":"2026090104492072200_cit7","doi-asserted-by":"publisher","first-page":"189","DOI":"10.1016\/j.csbj.2019.12.004","article-title":"The Current\nUnderstanding of KRAS Protein Structure and Dynamics","volume":"18","author":"Pantsar","year":"2020","journal-title":"Comput. Struct. Biotechnol. J."},{"issue":"10","key":"2026090104492072200_cit8","doi-asserted-by":"publisher","first-page":"1446","DOI":"10.1038\/s41594-023-01070-z","article-title":"Excited-State Observation of Active\nK-Ras Reveals Differential\nStructural Dynamics of Wild-Type versus Oncogenic G12D and G12C Mutants","volume":"30","author":"Hansen","year":"2023","journal-title":"Nat. Struct. Mol. Biol."},{"issue":"7","key":"2026090104492072200_cit9","doi-asserted-by":"publisher","first-page":"2551","DOI":"10.1073\/pnas.1812963116","article-title":"Discovery of Potent SOS1 Inhibitors\nThat Block RAS Activation via Disruption of the RAS\u2013SOS1 Interaction","volume":"116","author":"Hillig","year":"2019","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"44","key":"2026090104492072200_cit10","doi-asserted-by":"publisher","first-page":"22122","DOI":"10.1073\/pnas.1908353116","article-title":"KRAS G13D\nSensitivity to Neurofibromin-Mediated\nGTP Hydrolysis","volume":"116","author":"Rabara","year":"2019","journal-title":"Proc. Natl. Acad. Sci. U. S.\nA."},{"issue":"3","key":"2026090104492072200_cit11","doi-asserted-by":"publisher","first-page":"107909","DOI":"10.1016\/j.celrep.2020.107909","article-title":"Structural Insights into the SPRED1-Neurofibromin-KRAS\nComplex and Disruption of SPRED1-Neurofibromin Interaction by Oncogenic\nEGFR","volume":"32","author":"Yan","year":"2020","journal-title":"Cell Rep."},{"issue":"33","key":"2026090104492072200_cit12","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.2103261118","article-title":"RAS Interaction\nwith Sin1 Is Dispensable for mTORC2 Assembly and Activity","volume":"118","author":"Castel","year":"2021","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"12","key":"2026090104492072200_cit13","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.2022403118","article-title":"Molecular\nAssemblies of the Catalytic Domain of SOS with KRas and Oncogenic\nMutants","volume":"118","author":"Moghadamchargari","year":"2021","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"1","key":"2026090104492072200_cit14","doi-asserted-by":"publisher","first-page":"1176","DOI":"10.1038\/s41467-021-21422-x","article-title":"KRAS Interaction with RAF1 RAS-Binding Domain and Cysteine-Rich\nDomain Provides Insights into RAS-Mediated RAF Activation","volume":"12","author":"Tran","year":"2021","journal-title":"Nat. Commun."},{"issue":"9","key":"2026090104492072200_cit15","doi-asserted-by":"publisher","first-page":"167527","DOI":"10.1016\/j.jmb.2022.167527","article-title":"Structures of RGL1\nRAS-Association Domain in Complex with KRAS and the Oncogenic G12V\nMutant","volume":"434","author":"Eves","year":"2022","journal-title":"J. Mol. Biol."},{"issue":"1","key":"2026090104492072200_cit16","doi-asserted-by":"publisher","first-page":"4580","DOI":"10.1038\/s41467-023-40299-6","article-title":"Cryo-EM Structure\nof a RAS\/RAF Recruitment Complex","volume":"14","author":"Park","year":"2023","journal-title":"Nat. Commun."},{"issue":"1","key":"2026090104492072200_cit17","doi-asserted-by":"publisher","first-page":"1","DOI":"10.52396\/JUSTC-2024-0132","article-title":"Dynamic Binding\nof HRas\u00b7GTP to the Allosteric Site of Sos Investigated by Solution\nNMR","volume":"55","author":"Li","year":"2025","journal-title":"JUSTC"},{"issue":"1","key":"2026090104492072200_cit18","doi-asserted-by":"publisher","first-page":"7","DOI":"10.1007\/s12104-023-10162-2","article-title":"NMR 1H, 13C, 15N Backbone\nResonance Assignments\nof Wild-Type Human K-Ras and Its Oncogenic Mutants G12D and G12C Bound\nto GTP","volume":"18","author":"Yuan","year":"2024","journal-title":"Biomol. NMR Assign."},{"issue":"12","key":"2026090104492072200_cit19","doi-asserted-by":"publisher","first-page":"970","DOI":"10.1107\/S2059798317015418","article-title":"Structural Insight\ninto the Rearrangement of the Switch\nI Region in GTP-Bound G12A K-Ras","volume":"73","author":"Xu","year":"2017","journal-title":"Acta Crystallogr.:\nD Struct Biol."},{"issue":"34","key":"2026090104492072200_cit20","doi-asserted-by":"publisher","first-page":"9272","DOI":"10.1039\/D0SC03441J","article-title":"Structural Impact of GTP Binding on Downstream KRAS\nSignaling","volume":"11","author":"Menyha\u0301rd","year":"2020","journal-title":"Chem. Sci."},{"issue":"32","key":"2026090104492072200_cit21","doi-asserted-by":"publisher","first-page":"10308","DOI":"10.1021\/bi952858k","article-title":"Conformational\nTransitions in p21ras and in Its Complexes\nwith the Effector Protein Raf-RBD\nand the GTPase Activating Protein GAP","volume":"35","author":"Geyer","year":"1996","journal-title":"Biochemistry"},{"issue":"9","key":"2026090104492072200_cit22","doi-asserted-by":"publisher","first-page":"4944","DOI":"10.1073\/pnas.081441398","article-title":"Dynamic Properties of the Ras Switch\nI Region and Its\nImportance for Binding to Effectors","volume":"98","author":"Spoerner","year":"2001","journal-title":"Proc. Natl.\nAcad. Sci. U. S. A."},{"issue":"6","key":"2026090104492072200_cit23","doi-asserted-by":"publisher","first-page":"810","DOI":"10.1016\/j.str.2018.03.018","article-title":"K-Ras Populates Conformational\nStates Differently from Its Isoform H-Ras and Oncogenic Mutant K-RasG12D","volume":"26","author":"Parker","year":"2018","journal-title":"Structure"},{"issue":"1","key":"2026090104492072200_cit24","doi-asserted-by":"publisher","first-page":"11","DOI":"10.1038\/nrc969","article-title":"Targeting\nRAS Signalling Pathways in Cancer Therapy","volume":"3","author":"Downward","year":"2003","journal-title":"Nat.\nRev. Cancer"},{"issue":"15","key":"2026090104492072200_cit25","doi-asserted-by":"publisher","first-page":"2807","DOI":"10.1016\/j.molcel.2024.06.027","article-title":"Functional and Structural Insights\ninto RAS Effector Proteins","volume":"84","author":"Mozzarelli","year":"2024","journal-title":"Mol. Cell"},{"issue":"11","key":"2026090104492072200_cit26","doi-asserted-by":"publisher","first-page":"875","DOI":"10.1038\/nrm1498","article-title":"The RAF Proteins Take Centre Stage","volume":"5","author":"Wellbrock","year":"2004","journal-title":"Nat. Rev. Mol. Cell Biol."},{"issue":"1","key":"2026090104492072200_cit27","doi-asserted-by":"publisher","first-page":"2593","DOI":"10.1038\/s41467-026-69437-6","article-title":"Positive Cooperativity between RAS-Binding\nand Cysteine-Rich Domains Regulates RAF Membrane Binding Kinetics\nvia Lateral Rebinding","volume":"17","author":"Jimenez Salinas","year":"2026","journal-title":"Nat. Commun."},{"issue":"1","key":"2026090104492072200_cit28","doi-asserted-by":"publisher","first-page":"a033746","DOI":"10.1101\/cshperspect.a033746","article-title":"Ras-Mediated Activation\nof the Raf Family Kinases","volume":"9","author":"Terrell","year":"2019","journal-title":"Cold Spring Harbor\nPerspect. Med."},{"issue":"7783","key":"2026090104492072200_cit29","doi-asserted-by":"publisher","first-page":"545","DOI":"10.1038\/s41586-019-1660-y","article-title":"Architecture of Autoinhibited and Active BRAF\u2013MEK1\u201314-3-3\nComplexes","volume":"575","author":"Park","year":"2019","journal-title":"Nature"},{"key":"2026090104492072200_cit30","doi-asserted-by":"publisher","first-page":"195","DOI":"10.1007\/978-1-0716-3822-4_14","article-title":"Profiling Complex\nRAS-Effector Interactions Using NMR Spectroscopy","volume-title":"KRAS: Methods and Protocols","author":"Strakhova","year":"2024"},{"issue":"1","key":"2026090104492072200_cit31","doi-asserted-by":"publisher","first-page":"106","DOI":"10.1039\/D4CB00233D","article-title":"Dynamic Conformational Equilibria in the Active States\nof KRAS and NRAS","volume":"6","author":"Rennella","year":"2025","journal-title":"RSC Chem. Biol."},{"issue":"14","key":"2026090104492072200_cit32","doi-asserted-by":"publisher","first-page":"169162","DOI":"10.1016\/j.jmb.2025.169162","article-title":"Switch II\nPocket Inhibitor Allosterically\nFreezes KRASG12D Nucleotide-Binding Site and Arrests the\nGTPase Cycle","volume":"437","author":"Kim","year":"2025","journal-title":"J. Mol. Biol."},{"issue":"20","key":"2026090104492072200_cit33","doi-asserted-by":"publisher","first-page":"6472","DOI":"10.1021\/ja800201j","article-title":"Quantitative\nLid Dynamics of MDM2 Reveals Differential Ligand Binding Modes of\nthe p53-Binding Cleft","volume":"130","author":"Showalter","year":"2008","journal-title":"J. Am. Chem. Soc."},{"issue":"2","key":"2026090104492072200_cit34","doi-asserted-by":"publisher","first-page":"93","DOI":"10.1016\/S0079-6565(98)00025-9","article-title":"Heteronuclear Multidimensional NMR\nExperiments for the Structure Determination of Proteins in Solution\nEmploying Pulsed Field Gradients","volume":"34","author":"Sattler","year":"1999","journal-title":"Prog. Nucl.\nMagn. Reson. Spectrosc."},{"issue":"1","key":"2026090104492072200_cit35","doi-asserted-by":"publisher","first-page":"151","DOI":"10.1016\/0022-2364(91)90036-S","article-title":"Sensitivity Improvement\nin Proton-Detected Two-Dimensional Heteronuclear Correlation NMR Spectroscopy","volume":"93","author":"Palmer","year":"1991","journal-title":"J. Magn. Reson."},{"issue":"2","key":"2026090104492072200_cit36","doi-asserted-by":"publisher","first-page":"301","DOI":"10.1007\/BF00175254","article-title":"A General\nEnhancement Scheme in Heteronuclear Multidimensional NMR Employing\nPulsed Field Gradients","volume":"4","author":"Schleucher","year":"1994","journal-title":"J. Biomol. NMR"},{"issue":"2","key":"2026090104492072200_cit37","doi-asserted-by":"publisher","first-page":"185","DOI":"10.1007\/BF00178261","article-title":"Amino Acid Type Determination\nin the Sequential Assignment Procedure\nof Uniformly 13C\/15N-Enriched Proteins","volume":"3","author":"Grzesiek","year":"1993","journal-title":"J. Biomol. NMR"},{"issue":"7","key":"2026090104492072200_cit38","doi-asserted-by":"publisher","first-page":"2145","DOI":"10.1021\/ja908004w","article-title":"Poisson-Gap\nSampling and Forward\nMaximum Entropy Reconstruction for Enhancing the Resolution and Sensitivity\nof Protein NMR Data","volume":"132","author":"Hyberts","year":"2010","journal-title":"J. Am. Chem. Soc."},{"key":"2026090104492072200_cit39","doi-asserted-by":"publisher","first-page":"177","DOI":"10.1023\/A:1008367912535","article-title":"An Efficient\nStrategy for Assignment\nof Cross-Peaks in 3D Heteronuclear NOESY Experiments","volume":"15","author":"Diercks","year":"1999","journal-title":"J. Biomol. NMR"},{"issue":"3","key":"2026090104492072200_cit40","doi-asserted-by":"publisher","first-page":"277","DOI":"10.1007\/BF00197809","article-title":"NMRPipe: A Multidimensional Spectral Processing System Based on UNIX\nPipes","volume":"6","author":"Delaglio","year":"1995","journal-title":"J. Biomol. NMR"},{"issue":"2","key":"2026090104492072200_cit41","doi-asserted-by":"publisher","first-page":"101","DOI":"10.1007\/s10858-016-0072-7","article-title":"Sparse Multidimensional\nIterative Lineshape-Enhanced (SMILE) Reconstruction of Both Non-Uniformly\nSampled and Conventional NMR Data","volume":"68","author":"Ying","year":"2017","journal-title":"J. Biomol.\nNMR"},{"issue":"5","key":"2026090104492072200_cit42","doi-asserted-by":"publisher","first-page":"603","DOI":"10.1007\/BF00404272","article-title":"NMR View: A Computer Program for\nthe Visualization\nand Analysis of NMR Data","volume":"4","author":"Johnson","year":"1994","journal-title":"J. Biomol. NMR"},{"issue":"8","key":"2026090104492072200_cit43","doi-asserted-by":"publisher","first-page":"1529","DOI":"10.1016\/j.bpj.2017.03.011","article-title":"NMRbox:\nA Resource for Biomolecular NMR Computation","volume":"112","author":"Maciejewski","year":"2017","journal-title":"Biophys. J."},{"key":"2026090104492072200_cit44","doi-asserted-by":"publisher","first-page":"D402","DOI":"10.1093\/nar\/gkm957","article-title":"BioMagResBank","volume":"36","author":"Ulrich","year":"2008","journal-title":"Nucleic Acids Res."},{"key":"2026090104492072200_cit45","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/j.jmr.2015.05.003","article-title":"A 15N CPMG\nRelaxation Dispersion Experiment More Resistant to Resonance Offset\nand Pulse Imperfection","volume":"257","author":"Jiang","year":"2015","journal-title":"J. Magn. Reson."},{"issue":"19","key":"2026090104492072200_cit46","doi-asserted-by":"publisher","first-page":"8148","DOI":"10.1021\/ja3001419","article-title":"Studying \u201cInvisible\u201d\nExcited Protein States in Slow Exchange with a Major State Conformation","volume":"134","author":"Vallurupalli","year":"2012","journal-title":"J. Am. Chem. Soc."},{"issue":"41","key":"2026090104492072200_cit47","doi-asserted-by":"publisher","first-page":"12352","DOI":"10.1021\/ja0207089","article-title":"Reconstructing NMR Spectra of \u201cInvisible\u201d\nExcited Protein States Using HSQC and HMQC Experiments","volume":"124","author":"Skrynnikov","year":"2002","journal-title":"J. Am. Chem. Soc."},{"issue":"1","key":"2026090104492072200_cit48","doi-asserted-by":"publisher","first-page":"118","DOI":"10.1006\/jmre.1998.1590","article-title":"A Method for Determining B1 Field Inhomogeneity.\nAre the Biases Assumed in Heteronuclear Relaxation\nExperiments Usually Underestimated?","volume":"136","author":"Guenneugues","year":"1999","journal-title":"J. Magn.\nReson."},{"issue":"8","key":"2026090104492072200_cit49","doi-asserted-by":"publisher","first-page":"1325","DOI":"10.1093\/bioinformatics\/btu830","article-title":"NMRFAM-SPARKY: Enhanced Software\nfor Biomolecular NMR Spectroscopy","volume":"31","author":"Lee","year":"2015","journal-title":"Bioinformatics"},{"issue":"18","key":"2026090104492072200_cit50","doi-asserted-by":"publisher","first-page":"3041","DOI":"10.1093\/bioinformatics\/btab180","article-title":"POKY: A Software Suite\nfor Multidimensional NMR and 3D Structure Calculation of Biomolecules","volume":"37","author":"Lee","year":"2021","journal-title":"Bioinformatics"},{"issue":"24","key":"2026090104492072200_cit51","doi-asserted-by":"publisher","first-page":"8674","DOI":"10.1021\/acs.analchem.2c00891","article-title":"COLMARq: A\nWeb Server for 2D NMR Peak Picking and Quantitative Comparative Analysis\nof Cohorts of Metabolomics Samples","volume":"94","author":"Li","year":"2022","journal-title":"Anal. Chem."},{"issue":"2","key":"2026090104492072200_cit52","doi-asserted-by":"publisher","first-page":"160","DOI":"10.1071\/CH21149","article-title":"Determination\nof Sample Concentrations by PULCON NMR Spectroscopy","volume":"75","author":"Mak","year":"2022","journal-title":"Aust. J. Chem."},{"issue":"36","key":"2026090104492072200_cit53","doi-asserted-by":"publisher","first-page":"26503","DOI":"10.1074\/jbc.M607458200","article-title":"B- and C-RAF Display\nEssential Differences in Their\nBinding to Ras","volume":"282","author":"Fischer","year":"2007","journal-title":"J. Biol. Chem."},{"issue":"3","key":"2026090104492072200_cit54","doi-asserted-by":"publisher","first-page":"643","DOI":"10.1016\/j.cell.2016.03.045","article-title":"A Small Molecule\nRAS-Mimetic Disrupts RAS Association with Effector Proteins to Block\nSignaling","volume":"165","author":"Athuluri-Divakar","year":"2016","journal-title":"Cell"},{"key":"2026090104492072200_cit55","doi-asserted-by":"publisher","first-page":"204","DOI":"10.1016\/S0076-6879(01)39315-1","article-title":"Nuclear Magnetic Resonance Methods\nfor Quantifying Microsecond-to-Millisecond Motions in Biological Macromolecules","volume":"339","author":"Palmer","year":"2001","journal-title":"Methods Enzymol."},{"issue":"21","key":"2026090104492072200_cit56","doi-asserted-by":"publisher","first-page":"6911","DOI":"10.1021\/bi00021a001","article-title":"Solution\nStructure of the Ras-Binding Domain of c-Raf-1 and Identification\nof Its Ras Interaction Surface","volume":"34","author":"Emerson","year":"1995","journal-title":"Biochemistry"},{"issue":"9","key":"2026090104492072200_cit57","doi-asserted-by":"publisher","first-page":"4196","DOI":"10.1021\/jacs.2c00007","article-title":"Insights into\nthe Cross Talk between Effector and Allosteric Lobes of KRAS from\nMethyl Conformational Dynamics","volume":"144","author":"Chao","year":"2022","journal-title":"J. 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