Associated Papers
Systematic cysteine scanning identifies a druggable pocket in oncogenic KRAS.
van Tienen LM et al.
Cell Chemical Biology, 2026
Mechanistic insights into KRASG12D inhibitor binding revealed by molecular dynamics simulations of multiple crystal structures.
Kim D et al.
Physical Chemistry Chemical Physics : Pccp, 2026
Distal Covalent Targeting Suppresses Signaling of Oncogenic K-Ras(G13C) in Cancer Cells.
Zheng Q et al.
Acs Chemical Biology, 2025
Denitrogenative Alkylation of K-Ras(G12D) Inhibits Oncogenic Signaling in Cancer Cells.
Zheng Q et al.
Journal of the American Chemical Society, 2025
Switch II Pocket Inhibitor Allosterically Freezes KRASG12D Nucleotide-binding Site and Arrests the GTPase Cycle.
Kim HN et al.
Journal of Molecular Biology, 2025
Biophysical and structural analysis of KRAS switch-II pocket inhibitors reveals allele-specific binding constraints.
Alexander P et al.
The Journal of Biological Chemistry, 2025
Reversible Small Molecule Multivariant Ras Inhibitors Display Tunable Affinity for the Active and Inactive Forms of Ras.
Parry CW et al.
Journal of Medicinal Chemistry, 2025
Single-cell DNA and surface protein characterization of high hyperdiploid acute lymphoblastic leukemia at diagnosis and during treatment.
Aertgeerts M et al.
Hemasphere, 2025
The structure of KRASG12C bound to divarasib highlights features of potent switch-II pocket engagement.
Fernando MC et al.
Small Gtpases, 2024
Comprehensive structure-function analysis reveals gain- and loss-of-function mechanisms impacting oncogenic KRAS activity.
Kwon JJ et al.
Biorxiv : the Preprint Server for Biology, 2024
Strain-release alkylation of Asp12 enables mutant selective targeting of K-Ras-G12D.
Zheng Q et al.
Nature Chemical Biology, 2024
Discovery of MK-1084: An Orally Bioavailable and Low-Dose KRASG12C Inhibitor.
Ma X et al.
Journal of Medicinal Chemistry, 2024
K128 ubiquitination constrains RAS activity by expanding its binding interface with GAP proteins.
Magits W et al.
The Embo Journal, 2024
Translational and Therapeutic Evaluation of RAS-GTP Inhibition by RMC-6236 in RAS-Driven Cancers.
Jiang J et al.
Cancer Discovery, 2024
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 AK et al.
The Journal of Biological Chemistry, 2024
Crystal Packing Reveals a Potential Autoinhibited KRAS Dimer Interface and a Strategy for Small-Molecule Inhibition of RAS Signaling.
Brenner RJ et al.
Biochemistry, 2023
Excited-state observation of active K-Ras reveals differential structural dynamics of wild-type versus oncogenic G12D and G12C mutants.
Hansen AL et al.
Nature Structural & Molecular Biology, 2023
Exploring switch II pocket conformation of KRAS(G12D) with mutant-selective monobody inhibitors.
Akkapeddi P et al.
Proceedings of the National Academy of Sciences of the United States of America, 2023
Targeting oncogenic KRasG13C with nucleotide-based covalent inhibitors.
Goebel L et al.
Elife, 2023
Chemical acylation of an acquired serine suppresses oncogenic signaling of K-Ras(G12S).
Zhang Z et al.
Nature Chemical Biology, 2022
Inhibition of RAS-driven signaling and tumorigenesis with a pan-RAS monobody targeting the Switch I/II pocket.
Wallon L et al.
Proceedings of the National Academy of Sciences of the United States of America, 2022
Chemoselective Covalent Modification of K-Ras(G12R) with a Small Molecule Electrophile.
Zhang Z et al.
Journal of the American Chemical Society, 2022
Oncogenic KRAS G12C: Kinetic and redox characterization of covalent inhibition.
Huynh MV et al.
The Journal of Biological Chemistry, 2022
Delineating the RAS Conformational Landscape.
Parker MI et al.
Cancer Research, 2022
Discovery, Preclinical Characterization, and Early Clinical Activity of JDQ443, a Structurally Novel, Potent, and Selective Covalent Oral Inhibitor of KRASG12C.
Weiss A et al.
Cancer Discovery, 2022
Massively parallel phenotyping of coding variants in cancer with Perturb-seq.
Ursu O et al.
Nature Biotechnology, 2022
Structures of RGL1 RAS-Association Domain in Complex with KRAS and the Oncogenic G12V Mutant.
Eves BJ et al.
Journal of Molecular Biology, 2022
NMR 1H, 13C, 15N backbone resonance assignments of the T35S and oncogenic T35S/Q61L mutants of human KRAS4b in the active, GppNHp-bound conformation.
Sharma AK et al.
Biomolecular Nmr Assignments, 2022
Regulation of GTPase function by autophosphorylation.
Johnson CW et al.
Molecular Cell, 2022
The Q61H mutation decouples KRAS from upstream regulation and renders cancer cells resistant to SHP2 inhibitors.
Gebregiworgis T et al.
Nature Communications, 2021
Oncogenic KRAS G12D mutation promotes dimerization through a second, phosphatidylserine-dependent interface: a model for KRAS oligomerization.
Lee KY et al.
Chemical Science, 2021
Blockade of mutant RAS oncogenic signaling with a special emphasis on KRAS.
Roskoski R
Pharmacological Research, 2021
Structural bioinformatics enhances mechanistic interpretation of genomic variation, demonstrated through the analyses of 935 distinct RAS family mutations.
Tripathi S et al.
Bioinformatics (oxford, England), 2021
Monoubiquitination of KRAS at Lysine104 and Lysine147 Modulates Its Dynamics and Interaction with Partner Proteins.
Nair VV et al.
The Journal of Physical Chemistry. B, 2021
Spatially interacting phosphorylation sites and mutations in cancer.
Huang KL et al.
Nature Communications, 2021
Biophysical and Structural Characterization of Novel RAS-Binding Domains (RBDs) of PI3Kα and PI3Kγ.
Martinez NG et al.
Journal of Molecular Biology, 2021
KRAS interaction with RAF1 RAS-binding domain and cysteine-rich domain provides insights into RAS-mediated RAF activation.
Tran TH et al.
Nature Communications, 2021
KRAS Ubiquitination at Lysine 104 Retains Exchange Factor Regulation by Dynamically Modulating the Conformation of the Interface.
Yin G et al.
Iscience, 2020
The molecular basis for immune dysregulation by the hyperactivated E62K mutant of the GTPase RAC2.
Arrington ME et al.
The Journal of Biological Chemistry, 2020
Computationally Empowered Workflow Identifies Novel Covalent Allosteric Binders for KRASG12C.
Mortier J et al.
Chemmedchem, 2020
RAS ubiquitylation modulates effector interactions.
Thurman R et al.
Small Gtpases, 2020
Biology, pathology, and therapeutic targeting of RAS.
Rhett JM et al.
Advances in Cancer Research, 2020
Bifunctional Small-Molecule Ligands of K-Ras Induce Its Association with Immunophilin Proteins.
Zhang Z et al.
Angewandte Chemie (international Ed. in English), 2019
Cysteine-based regulation of redox-sensitive Ras small GTPases.
Messina S et al.
Redox Biology, 2019
Drugging an undruggable pocket on KRAS.
Kessler D et al.
Proceedings of the National Academy of Sciences of the United States of America, 2019