Small molecule inhibition of the KRAS–PDEδ interaction impairs oncogenic KRAS signalling

Targeting RAS signalling pathways in cancer therapy

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

Targeting the Raf-MEK-ERK mitogen-activated protein kinase cascade for the treatment of cancer

Roberts, P. J., & Der, C. J. (2007) · Oncogene · doi:10.1038/sj.onc.1210422 · Cited by 2,788 · 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

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

Targeting protein prenylation for cancer therapy

Berndt, N., Hamilton, A. D., & Sebti, S. M. (2011) · Nature Reviews Cancer · doi:10.1038/nrc3151 · Cited by 614 · see citing works

Chemical screening methods to identify ligands that promote protein stability, protein crystallization, and structure determination

Vedadi, M., Niesen, F., Allali‐Hassani, A., Fedorov, O., Finerty, P. J., Wasney, G. A., Yeung, R., Arrowsmith, C. H., Ball, L., Berglund, H., et al. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0605224103 · Cited by 590 · see citing works

Multidrug Resistance: Retrospect and Prospects in Anti-Cancer Drug Treatment

Pérez‐Tomás, R. (2006) · Current Medicinal Chemistry · doi:10.2174/092986706777585077 · Cited by 509 · 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

Imaging biochemistry inside cells

Wouters, F. S., Verveer, P. J., & Bastiaens, P. I. H. (2001) · Trends in Cell Biology · doi:10.1016/s0962-8924(01)01982-1 · Cited by 455 · see citing works

Galectin-1 binds oncogenic H-Ras to mediate Ras membrane anchorage and cell transformation

Paz, A., Haklai, R., Elad‐Sfadia, G., Ballan, E., & Kloog, Y. (2001) · Oncogene · doi:10.1038/sj.onc.1204950 · Cited by 400 · see citing works

Genetic profile of 22 pancreatic carcinoma cell lines: Analysis of K-ras, p53, p16 and DPC4/Smad4

Moore, P. S., Sipos, B., Orlandini, S., Sorio, C., Real, F. X., Lemoine, N. R., Gress, T., Bassi, C., Klöppel, G., Kalthoff, H., et al. (2001) · Virchows Archiv · doi:10.1007/s004280100474 · Cited by 329 · see citing works

The GDI-like solubilizing factor PDEδ sustains the spatial organization and signalling of Ras family proteins

Chandra, A., Grecco, H. E., Pisupati, V., Perera, D., Cassidy, L., Skoulidis, F., Ismail, S. A., Hedberg, C., Hanzal-Bayer, M., Venkitaraman, A. R., et al. (2012) · Nature Cell Biology · doi:10.1038/ncb2394 · Cited by 325 · see citing works

Galectin-3 Augments K-Ras Activation and Triggers a Ras Signal That Attenuates ERK but Not Phosphoinositide 3-Kinase Activity*

Elad-Sfadia, G., Haklai, R., Balan, E., & Kloog, Y. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m312697200 · Cited by 305 · see citing works

An orthosteric inhibitor of the Ras-Sos interaction

Patgiri, A., Yadav, K. K., Arora, P. S., & Bar‐Sagi, D. (2011) · Nature Chemical Biology · doi:10.1038/nchembio.612 · Cited by 294 · see citing works

Arl2-GTP and Arl3-GTP regulate a GDI-like transport system for farnesylated cargo

Ismail, S. A., Chen, Y.-X., Rusinova, A., Chandra, A., Bierbaum, M., Gremer, L., Triola, G., Waldmann, H., Bastiaens, P. I. H., & Wittinghofer, A. (2011) · Nature Chemical Biology · doi:10.1038/nchembio.686 · Cited by 252 · see citing works

Comparative analysis of mutations in the p53 and K‐ras genes in pancreatic cancer

Berrozpe, G., Schaeffer, J., Peinado, M. A., Real, F. X., & Perucho, M. (1994) · International Journal of Cancer · doi:10.1002/ijc.2910580207 · Cited by 236 · see citing works

An ARL3–UNC119–RP2 GTPase cycle targets myristoylated NPHP3 to the primary ciliumPreprint

Wright, K. J., Baye, L. M., Olivier-Mason, A., Mukhopadhyay, S., Sang, L., Kwong, M., Wang, W., Pretorius, P. R., Sheffield, V. C., Sengupta, P., et al. (2011) · Genes & Development · doi:10.1101/gad.173443.111 · Cited by 229 · see citing works

Therapeutic intervention based on protein prenylation and associated modifications

Gelb, M. H., Brunsveld, L., Hrycyna, C. A., Michaelis, S., Tamanoi, F., A, W. C. V. V., & Waldmann, H. (2006) · Nature Chemical Biology · doi:10.1038/nchembio818 · Cited by 195 · see citing works

UNC119 is required for G protein trafficking in sensory neurons

Zhang, H., Constantine, R., Vorobiev, S. M., Chen, Y., Seetharaman, J., Huang, Y. J., Xiao, R., Montelione, G. T., Gerstner, C. D., Davis, M. W., et al. (2011) · Nature Neuroscience · doi:10.1038/nn.2835 · Cited by 167 · see citing works

Photoreceptor cGMP Phosphodiesterase δ Subunit (PDEδ) Functions as a Prenyl-binding Protein

Zhang, H., Liu, X., Zhang, K., Chen, C.-K., Frederick, J. M., Prestwich, G. D., & Baehr, W. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m306559200 · Cited by 126 · see citing works

A yeast-based screen reveals that sulfasalazine inhibits tetrahydrobiopterin biosynthesis

Chidley, C., Haruki, H., Pedersen, M. G., Muller, E., & Johnsson, K. (2011) · Nature Chemical Biology · doi:10.1038/nchembio.557 · Cited by 122 · see citing works

Global analysis of time correlated single photon counting FRET-FLIM data

Grecco, H. E., Roda‐Navarro, P., & Verveer, P. J. (2009) · Optics Express · doi:10.1364/oe.17.006493 · Cited by 90 · see citing works

In situ analysis of tyrosine phosphorylation networks by FLIM on cell arrays

Grecco, H. E., Roda‐Navarro, P., Girod, A., Hou, J., Frahm, T., Truxius, D. C., Pepperkok, R., Squire, A., & Bastiaens, P. I. H. (2010) · Nature Methods · doi:10.1038/nmeth.1458 · Cited by 77 · see citing works

Synthesis of the Rheb and K‐Ras4B GTPases

Chen, Y., Koch, S., Uhlenbrock, K., Weise, K., Das, D., Gremer, L., Brunsveld, L., Wittinghofer, A., Winter, R., Triola, G., et al. (2010) · Angewandte Chemie International Edition · doi:10.1002/anie.201001884 · Cited by 76 · see citing works

Discovery of Potent, Selective, and Orally Active Carboxylic Acid Based Inhibitors of Matrix Metalloproteinase-13

Monovich, L. G., Tommasi, R., Fujimoto, R. A., Blancuzzi, V., Clark, K., Cornell, W. D., Doti, R. A., Doughty, J., Fang, J. C., FARLEY, D. L., et al. (2009) · Journal of Medicinal Chemistry · doi:10.1021/jm801394m · Cited by 58 · see citing works

Multiple Cellular Proteins Modulate the Dynamics of K-ras Association with the Plasma Membrane

Bhagatji, P., Leventis, R., Rich, R. L., Lin, C., & Silvius, J. R. (2010) · Biophysical Journal · doi:10.1016/j.bpj.2010.10.001 · Cited by 51 · see citing works

The first 30 years

Söldner‐Rembold, S. (2011) · Nature Physics · doi:10.1038/nphys2086 · Cited by 27 · see citing works

Erratum: The GDI-like solubilizing factor PDEδ sustains the spatial organization and signalling of Ras family proteins

Chandra, A., Grecco, H. E., Pisupati, V., Perera, D., Cassidy, L. D., Skoulidis, F., Ismail, S., Hedberg, C., Hanzal‐Bayer, M., Venkitaraman, A. R., et al. (2012) · Nature Cell Biology · doi:10.1038/ncb2462 · Cited by 11 · see citing works

RAS Proteins and Their Regulators in Human Disease

Simanshu, D. K., Nissley, D. V., & McCormick, F. (2017) · Cell · doi:10.1016/j.cell.2017.06.009 · Cited by 1,943 · 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

Targeting RAS–ERK signalling in cancer: promises and challenges

Samatar, A. A., & Poulikakos, P. I. (2014) · Nature Reviews Drug Discovery · doi:10.1038/nrd4281 · Cited by 1,163 · see citing works

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 · see citing works

Small molecules, big targets: drug discovery faces the protein–protein interaction challenge

Scott, D. E., Bayly, A. R., Abell, C., & Skidmore, J. (2016) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2016.29 · Cited by 1,137 · 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

RAS isoforms and mutations in cancer at a glance

Hobbs, G. A., Der, C. J., & Rossman, K. L. (2016) · Journal of Cell Science · doi:10.1242/jcs.182873 · Cited by 973 · see citing works

Recent advances in the development of protein–protein interactions modulators: mechanisms and clinical trials

Lu, H., Zhou, Q., He, J., Jiang, Z., Peng, C., Tong, R., & Shi, J. (2020) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-00315-3 · Cited by 891 · 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

Project DRIVE: a compendium of cancer dependencies and synthetic lethal relationships uncovered by large-scale, deep RNAi screening

McDonald, E. R., de Weck, A., Schlabach, M. R., Billy, E., Mavrakis, K. J., Hoffman, G. R., Belur, D., Castelletti, D., Frias, E., Gampa, K., et al. (2017) · Cell · doi:10.1016/j.cell.2017.07.005 · Cited by 658 · 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

Genetics and biology of pancreatic ductal adenocarcinoma

Ying, H., Dey, P., Yao, W., Kimmelman, A. C., Draetta, G. F., Maitra, A., & DePinho, R. A. (2016) · Genes & Development · doi:10.1101/gad.275776.115 · Cited by 527 · see citing works

Modulators of Protein–Protein Interactions

Milroy, L.-G., Grossmann, T. N., Hennig, S., Brunsveld, L., & Ottmann, C. (2014) · Chemical Reviews · doi:10.1021/cr400698c · Cited by 497 · see citing works

Therapeutic strategies to target RAS-mutant cancers

Ryan, M. B., & Corcoran, R. B. (2018) · Nature Reviews Clinical Oncology · doi:10.1038/s41571-018-0105-0 · Cited by 420 · see citing works

Drugging RAS: know the enemy

Papke, B., & Der, C. J. (2017) · Science · doi:10.1126/science.aam7622 · Cited by 399 · see citing works

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 · see citing works

Targeting the untargetable KRAS in cancer therapy

Liu, P., Wang, Y., & Li, X. (2019) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2019.03.002 · Cited by 366 · 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

Targeting RAS Membrane Association: Back to the Future for Anti-RAS Drug Discovery?

Cox, A. D., Der, C. J., & Philips, M. R. (2015) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-14-3214 · Cited by 351 · see citing works

KRAS as a Therapeutic Target

McCormick, F. (2015) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-14-2662 · Cited by 320 · see citing works

Autopalmitoylation of TEAD proteins regulates transcriptional output of the Hippo pathway

Chan, P., Han, X., Zheng, B., DeRan, M., Yu, J., Jarugumilli, G. K., Deng, H., Pan, D., Luo, X., & Wu, X. (2016) · Nature Chemical Biology · doi:10.1038/nchembio.2036 · Cited by 313 · see citing works

Oncogenic protein interfaces: small molecules, big challenges

Nero, T. L., Morton, C. J., Holien, J. K., Wielens, J., & Parker, M. W. (2014) · Nature Reviews Cancer · doi:10.1038/nrc3690 · Cited by 312 · see citing works

Therapeutic Targeting of Oncogenic K‐Ras by a Covalent Catalytic Site Inhibitor

Lim, S. M., Westover, K. D., Ficarro, S. B., Harrison, R. A., Choi, H. G., Pacold, M. E., Carrasco, M., Hunter, J., Kim, N. D., Xie, T., et al. (2014) · Angewandte Chemie International Edition · doi:10.1002/anie.201307387 · Cited by 300 · see citing works

Mutant KRAS is a druggable target for pancreatic cancer

Zorde Khvalevsky, E., Gabai, R., Rachmut, I. H., Horwitz, E., Brunschwig, Z., Orbach, A., Shemi, A., Golan, T., Domb, A. J., Yavin, E., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1314307110 · Cited by 295 · see citing works

PROTACs: great opportunities for academia and industry (an update from 2020 to 2021)

He, M., Cao, C., Ni, Z., Liu, Y., Song, P., Hao, S., He, Y., Sun, X., & Rao, Y. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-00999-9 · Cited by 283 · see citing works

KRas Localizes to the Plasma Membrane by Spatial Cycles of Solubilization, Trapping and Vesicular Transport

Schmick, M., Vartak, N., Papke, B., Kovacevic, M., Truxius, D. C., Rossmannek, L., & Bastiaens, P. I. H. (2014) · Cell · doi:10.1016/j.cell.2014.02.051 · Cited by 243 · see citing works

In situ selectivity profiling and crystal structure of SML-8-73-1, an active site inhibitor of oncogenic K-Ras G12C

Hunter, J. C., Gurbani, D., Ficarro, S. B., Carrasco, M. A., Lim, S. M., Choi, H. G., Xie, T., Marto, J. A., Chen, Z., Gray, N. S., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1404639111 · Cited by 242 · see citing works

Molecular pathways and therapeutic targets in lung cancer

Shtivelman, E., Hensing, T., Simon, G. R., Dennis, P. A., Otterson, G. A., Bueno, R., & Salgia, R. (2014) · Oncotarget · doi:10.18632/oncotarget.1891 · Cited by 220 · see citing works

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 · see citing works

Survival of pancreatic cancer cells lacking KRAS function

Muzumdar, M. D., Chen, P.-Y., Dorans, K. J., Chung, K. M., Bhutkar, A., Hong, E., Noll, E. M., Sprick, M. R., Trumpp, A., & Jacks, T. (2017) · Nature Communications · doi:10.1038/s41467-017-00942-5 · Cited by 177 · see citing works

KRAS G12C Game of Thrones, which direct KRAS inhibitor will claim the iron throne?

Nagasaka, M., Li, Y., Sukari, A., Ou, S.-H. I., Al-Hallak, M. N., & Azmi, A. S. (2020) · Cancer Treatment Reviews · doi:10.1016/j.ctrv.2020.101974 · Cited by 185 · see citing works

RAS: Striking at the Core of the Oncogenic Circuitry

Gimple, R. C., & Wang, X. (2019) · Frontiers in Oncology · doi:10.3389/fonc.2019.00965 · Cited by 174 · see citing works

State-of-the-art strategies for targeting protein–protein interactions by small-molecule inhibitors

Sheng, C., Dong, G., Miao, Z., Zhang, W., & Wang, W. (2015) · Chemical Society Reviews · doi:10.1039/c5cs00252d · Cited by 165 · 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

Potent and Selective Covalent Quinazoline Inhibitors of KRAS G12C

Zeng, M., Lu, J., Li, L., Feru, F., Quan, C., Gero, T. W., Ficarro, S. B., Xiong, Y., Ambrogio, C., Paranal, R. M., et al. (2017) · Cell Chemical Biology · doi:10.1016/j.chembiol.2017.06.017 · Cited by 136 · see citing works

K-Ras protein as a drug target

McCormick, F. (2016) · Journal of Molecular Medicine · doi:10.1007/s00109-016-1382-7 · Cited by 105 · see citing works

A RAS Renaissance: Emerging Targeted Therapies for KRAS-Mutated Non–Small Cell Lung Cancer

Vasan, N., Boyer, J. L., & Herbst, R. S. (2014) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-13-1762 · Cited by 102 · see citing works

Focal Adhesion Kinase Regulates the DNA Damage Response and Its Inhibition Radiosensitizes Mutant <i>KRAS</i> Lung Cancer

Tang, K.-J., Constanzo, J. D., Venkateswaran, N., Melegari, M., Ilcheva, M., Morales, J. C., Skoulidis, F., Heymach, J. V., Boothman, D. A., & Scaglioni, P. P. (2016) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-15-2603 · Cited by 91 · see citing works

Discovery of High-Affinity Noncovalent Allosteric KRAS Inhibitors That Disrupt Effector Binding

McCarthy, M. J., Pagba, C. V., Prakash, P., Naji, A. K., van der Hoeven, D., Liang, H., Gupta, A. K., Zhou, Y., Cho, K.-J., Hancock, J. F., et al. (2019) · ACS Omega · doi:10.1021/acsomega.8b03308 · Cited by 90 · see citing works

Activation of protein phosphatase 2A tumor suppressor as potential treatment of pancreatic cancer

Chien, W., Sun, Q.-Y., Lee, K. L., Ding, L.-W., Wuensche, P., Torres-Fernandez, L. A., Tan, S. Z., Tokatly, I., Zaiden, N., Poellinger, L., et al. (2015) · Molecular Oncology · doi:10.1016/j.molonc.2015.01.002 · Cited by 80 · see citing works

Drugging K-RasG12C through covalent inhibitors: Mission possible?

Ni, D., Li, X., He, X., Zhang, H., Zhang, J., & Lu, S. (2019) · Pharmacology &amp; Therapeutics · doi:10.1016/j.pharmthera.2019.06.007 · Cited by 73 · see citing works

Inhibitors of Ras–SOS Interactions

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

Protein–Protein Interactions: Emerging Oncotargets in the RAS-ERK Pathway

García-Gómez, R., Bustelo, X. R., & Crespo, P. (2018) · Trends in Cancer · doi:10.1016/j.trecan.2018.07.002 · Cited by 72 · 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

Development of PDE6D and CK1α Degraders through Chemical Derivatization of FPFT-2216

Teng, M., Lu, W., Donovan, K. A., Sun, J., Krupnick, N. M., Nowak, R. P., Li, Y.-D., Sperling, A. S., Zhang, T., Ebert, B. L., et al. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c01832 · Cited by 63 · see citing works

Development of covalent inhibitors: Principle, design, and application in cancer

Zheng, L., Li, Y., Wu, D., Xiao, H., Zheng, S., Wang, G., & Sun, Q. (2023) · MedComm – Oncology · doi:10.1002/mog2.56 · Cited by 71 · see citing works

miR-1298 Inhibits Mutant KRAS-Driven Tumor Growth by Repressing FAK and LAMB3

Zhou, Y., Dang, J., Chang, K.-Y., Yau, E., Aza-Blanc, P., Moscat, J., & Rana, T. M. (2016) · Cancer Research · doi:10.1158/0008-5472.can-15-2936 · Cited by 54 · see citing works

PDE6D Inhibitors with a New Design Principle Selectively Block K-Ras Activity

Siddiqui, F. A., Alam, C., Rosenqvist, P., Ora, M., Sabt, A., Manoharan, G. B., Bindu, L., Okutachi, S., Catillon, M., Taylor, T., et al. (2020) · ACS Omega · doi:10.1021/acsomega.9b03639 · Cited by 46 · see citing works

Efforts to Develop KRAS Inhibitors

Holderfield, M. (2018) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a031864 · Cited by 43 · see citing works

Identification of a new inhibitor of KRAS‐PDEδ interaction targeting KRAS mutant nonsmall cell lung cancer

Leung, E. L., Luo, L. X., Li, Y., Liu, Z., Li, L. L., Shi, D. F., Xie, Y., Huang, M., Lu, L. L., Duan, F. G., et al. (2019) · International Journal of Cancer · doi:10.1002/ijc.32222 · Cited by 39 · see citing works

Identification of a New Potent Inhibitor Targeting KRAS in Non-small Cell Lung Cancer Cells

Xie, C., Li, Y., Li, L.-L., Fan, X.-X., Wang, Y.-W., Wei, C.-L., Liu, L., Leung, E. L.-H., & Yao, X.-J. (2017) · Frontiers in Pharmacology · doi:10.3389/fphar.2017.00823 · Cited by 40 · see citing works

Discovery of Novel KRAS-PDEδ Inhibitors by Fragment-Based Drug Design

Chen, L., Zhuang, C., Lu, J., Jiang, Y., & Sheng, C. (2018) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.8b00057 · Cited by 33 · see citing works

Structural Biology-Inspired Discovery of Novel KRAS–PDEδ Inhibitors

Jiang, Y., Zhuang, C., Chen, L., Lu, J., Dong, G., Miao, Z., Zhang, W., Li, J., & Sheng, C. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.7b01243 · Cited by 34 · see citing works

Fragment-based drug discovery of triazole inhibitors to block PDEδ-RAS protein-protein interaction

Chen, D., Chen, Y., Lian, F., Chen, L., Li, Y., Cao, D., Wang, X., Chen, L., Li, J., Meng, T., et al. (2019) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2018.12.018 · Cited by 31 · see citing works

Inducing Oncoprotein Degradation to Improve Targeted Cancer Therapy

Ray, D., Cuneo, K. C., Rehemtulla, A., Lawrence, T. S., & Nyati, M. K. (2015) · Neoplasia · doi:10.1016/j.neo.2015.08.008 · Cited by 22 · see citing works

Discovery of novel KRAS‒PDEδ inhibitors with potent activity in patient-derived human pancreatic tumor xenograft models

Chen, L., Zhang, J., Wang, X., Li, Y., Zhou, L., Lu, X., Dong, G., & Sheng, C. (2022) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2021.07.009 · Cited by 20 · see citing works

Assessing the significance of KRAS G12C mutation: Clinicopathologic features, treatments, and survival outcomes in a real-world KRAS mutant non-small cell lung cancer cohort.

Cui, W., Franchini, F., Alexander, M., Officer, A., Wong, H., IJzerman, M. J., Desai, J., & Solomon, B. (2020) · Journal of Clinical Oncology · doi:10.1200/jco.2020.38.15_suppl.e19324 · Cited by 3 · see citing works

127P RAS, RAF and NF1 oncogenic mutations in KRAS-mutated lung adenocarcinoma

Marinelli, D., Pisegna, S., Chiavassa, A., et al. (2022) · Annals of Oncology · doi:10.1016/j.annonc.2022.09.128

Antibody-enabled small-molecule drug discovery

Lawson, A. D. G. (2012) · Nature Reviews Drug Discovery · doi:10.1038/nrd3756 · Cited by 80 · see citing works

Structure Guided Design and Kinetic Analysis of Highly Potent Benzimidazole Inhibitors Targeting the PDEδ Prenyl Binding Site

Zimmermann, G., Schultz‐Fademrecht, C., Küchler, P., Murarka, S., Ismail, S., Triola, G., Nußbaumer, P., Wittinghofer, A., & Waldmann, H. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm500632s · Cited by 63 · see citing works

RNA‐Selective Small‐Molecule Ligands: Recent Advances in Live‐Cell Imaging and Drug Discovery

Chan, K. H., Wang, Y., Zheng, B., et al. (2023) · ChemMedChem · doi:10.1002/cmdc.202300271 · Cited by 10 · see citing works