K-Ras(G12D)-selective inhibitory peptides generated by random peptide T7 phage display technology

K-Ras(G12C) inhibitors allosterically control GTP affinity and effector interactions

Ostrem, J. M., Peters, U., Sos, M. L., Wells, J. A., & Shokat, K. M. (2013) · Nature · doi:10.1038/nature12796 · Cited by 2,557 · 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

Ras oncogenes: split personalities

Karnoub, A. E., & Weinberg, R. A. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2438 · Cited by 1,467 · 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

Inhibition of Ras for Cancer Treatment: The Search Continues

Baines, A. T., Xu, D., & Der, C. J. (2011) · Future Medicinal Chemistry · doi:10.4155/fmc.11.121 · Cited by 385 · 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

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 · see citing works

Inhibition of Ras Signaling by Blocking Ras–Effector Interactions with Cyclic Peptides

Upadhyaya, P., Qian, Z., Selner, N. G., Clippinger, S. R., Wu, Z., Briesewitz, R., & Pei, D. (2015) · Angewandte Chemie International Edition · doi:10.1002/anie.201502763 · Cited by 149 · see citing works

Cancer: The Ras renaissance

Ledford, H. K. (2015) · Nature · doi:10.1038/520278a · Cited by 126 · see citing works

Discovery of a Direct Ras Inhibitor by Screening a Combinatorial Library of Cell-Permeable Bicyclic Peptides

Trinh, T. B., Upadhyaya, P., Qian, Z., & Pei, D. (2015) · ACS Combinatorial Science · doi:10.1021/acscombsci.5b00164 · Cited by 119 · see citing works

Fragment-Based Screening Using Surface Plasmon Resonance Technology

Perspicace, S., Banner, D. W., Benz, J., Müller, F., Schlatter, D., & Huber, W. (2009) · SLAS DISCOVERY · doi:10.1177/1087057109332595 · Cited by 105 · see citing works

Structure and Activity of (2,8)-Dicarba-(3,12)-cystino α-ImI, an α-Conotoxin Containing a Nonreducible Cystine Analogue

MacRaild, C. A., Illesinghe, J., van Lierop, B. J., Townsend, A. L., Chebib, M., Livett, B. G., Robinson, A. J., & Norton, R. S. (2009) · Journal of Medicinal Chemistry · doi:10.1021/jm8011504 · Cited by 82 · see citing works

Inhibition of Ras–effector interactions by cyclic peptides

Wú, X., Upadhyaya, P., Villalona-Calero, M. A., Briesewitz, R., & Pei, D. (2012) · MedChemComm · doi:10.1039/c2md20329d · Cited by 69 · see citing works

Enhancing Membrane Permeability by Fatty Acylation of Oligoarginine Peptides

Pham, W. N., Kircher, M. F., Weissleder, R., & Tung, C. (2004) · ChemBioChem · doi:10.1002/cbic.200400063 · Cited by 66 · see citing works

Identification of mutant K-Ras-dependent phenotypes using a panel of isogenic cell lines

Vartanian, S., Bentley, C., Brauer, M. J., Li, L., Shirasawa, S., Sasazuki, T., Kim, J.-S., Haverty, P., Stawiski, E., Modrusan, Z., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.394130 · Cited by 65 · see citing works

Chemical Syntheses and Biological Activities of Lactam Analogues of α-Conotoxin SI,,

Hargittai, B., Solé, N. A., Groebe, D. R., Abramson, S. N., & Bárány, G. (2000) · Journal of Medicinal Chemistry · doi:10.1021/jm990635c · Cited by 61 · see citing works

Interaction of Human Lactoferrin with Cell Adhesion Molecules through RGD Motif Elucidated by Lactoferrin-binding Epitopes

Sakamoto, K., Ito, Y., Mori, T., & Sugimura, K. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m604974200 · Cited by 48 · see citing works

Characterization of a Ras Mutant with Identical GDP- and GTP-Bound Structures,

Ford, B. A., Boykevisch, S., Zhao, C., Kunzelmann, S., Bar‐Sagi, D., Herrmann, C., & Nassar, N. N. (2009) · Biochemistry · doi:10.1021/bi901479b · Cited by 36 · see citing works

Discovery and Characterization of a Peptide Motif That Specifically Recognizes a Non-native Conformation of Human IgG Induced by Acidic pH Conditions

Sakamoto, K., Ito, Y., Hatanaka, T., Soni, P., Mori, T., & Sugimura, K. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m807618200 · Cited by 34 · see citing works

Novel DOCK2-selective inhibitory peptide that suppresses B-cell line migration

Sakamoto, K., Adachi, Y., Komoike, Y., Kamada, Y., Koyama, R., Fukuda, Y., Kadotani, A., Asami, T., & Sakamoto, J. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.12.170 · Cited by 28 · 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

Identification of MRTX1133, a Noncovalent, Potent, and Selective KRAS ^G12D Inhibitor

Wang, X., Allen, S., Blake, J. F., Bowcut, V., Briere, D. M., Calinisan, A., Dahlke, J. R., Fell, J. B., Fischer, J. P., Gunn, R. J., et al. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c01688 · Cited by 769 · 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

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 · see citing works

Progress on Ras/MAPK Signaling Research and Targeting in Blood and Solid Cancers

Dillon, M., Lopez, A. R., Lin, E., Sales, D., Perets, R., & Jain, P. (2021) · Cancers · doi:10.3390/cancers13205059 · Cited by 160 · see citing works

Chemical acylation of an acquired serine suppresses oncogenic signaling of K-Ras(G12S)

Zhang, Z., Guiley, K. Z., & Shokat, K. M. (2022) · Nature Chemical Biology · doi:10.1038/s41589-022-01065-9 · Cited by 153 · see citing works

Targeting the Small GTPase Superfamily through Their Regulatory Proteins

Gray, J. L., von Delft, F., & Brennan, P. E. (2019) · Angewandte Chemie International Edition · doi:10.1002/anie.201900585 · Cited by 142 · see citing works

Mutation-Induced Impacts on the Switch Transformations of the GDP- and GTP-Bound K-Ras: Insights from Multiple Replica Gaussian Accelerated Molecular Dynamics and Free Energy Analysis

Chen, J., Zhang, S., Wang, W., Pang, L., Zhang, Q., & Liu, X. (2021) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.0c01470 · Cited by 140 · see citing works

GTP-State-Selective Cyclic Peptide Ligands of K-Ras(G12D) Block Its Interaction with Raf

Zhang, Z., Gao, R., Hu, Q., Peacock, H., Peacock, D. M., Dai, S., Shokat, K. M., & Suga, H. (2020) · ACS Central Science · doi:10.1021/acscentsci.0c00514 · Cited by 124 · see citing works

KRAS is vulnerable to reversible switch-II pocket engagement in cells

Vasta, J. D., Peacock, D. M., Zheng, Q., Walker, J. A., Zhang, Z., Zimprich, C. A., Thomas, M. R., Beck, M. T., Binkowski, B. F., Corona, C. R., et al. (2022) · Nature Chemical Biology · doi:10.1038/s41589-022-00985-w · Cited by 115 · see citing works

Crystal Structures of Protein-Bound Cyclic Peptides

Malde, A. K., Hill, T. A., Iyer, A., & Fairlie, D. P. (2019) · Chemical Reviews · doi:10.1021/acs.chemrev.8b00807 · Cited by 113 · see citing works

Peptide-Based Agents for Cancer Treatment: Current Applications and Future Directions

Nhàn, N. T. T., Yamada, T., & Yamada, K. H. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241612931 · Cited by 109 · see citing works

Cyclic Peptide Screening Methods for Preclinical Drug Discovery

Li, X., Craven, T. W., & Levine, P. M. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.2c01077 · Cited by 95 · see citing works

Direct inhibition of RAS: Quest for the Holy Grail?

Spencer-Smith, R., & O’Bryan, J. P. (2017) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2017.12.005 · Cited by 89 · see citing works

Selective and noncovalent targeting of RAS mutants for inhibition and degradation

Teng, K. W., Tsai, S. T., Hattori, T., Fedele, C., Koide, A., Yang, C., Hou, X., Zhang, Y., Neel, B. G., O’Bryan, J. P., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-22969-5 · Cited by 88 · see citing works

Generation of KS-58 as the first K-Ras(G12D)-inhibitory peptide presenting anti-cancer activity in vivo

Sakamoto, K., Masutani, T., & Hirokawa, T. (2020) · Scientific Reports · doi:10.1038/s41598-020-78712-5 · Cited by 85 · see citing works

Crystal Structure of a Human K-Ras G12D Mutant in Complex with GDP and the Cyclic Inhibitory Peptide KRpep-2d

Sogabe, S., Kamada, Y., Miwa, M., Niida, A., Sameshima, T., Kamaura, M., Yonemori, K., Sasaki, S., Sakamoto, J.-I., & Sakamoto, K. (2017) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.7b00128 · Cited by 83 · 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

Selection of Nucleotide-Encoded Mass Libraries of Macrocyclic Peptides for Inaccessible Drug Targets

Colas, K., Bindl, D., & Suga, H. (2024) · Chemical Reviews · doi:10.1021/acs.chemrev.4c00422 · Cited by 77 · see citing works

Advances in the T7 phage display system (Review)

Deng, X., Wang, L., You, X., Dai, P., & Zeng, Y. (2017) · Molecular Medicine Reports · doi:10.3892/mmr.2017.7994 · Cited by 63 · see citing works

Overcoming Resistance to Drugs Targeting KRAS Mutation

Jiao, D., & Yang, S. (2020) · The Innovation · doi:10.1016/j.xinn.2020.100035 · Cited by 61 · see citing works

T7 Phage as an Emerging Nanobiomaterial with Genetically Tunable Target Specificity

Hui, Y., Li, Y., Yang, M., & Mao, C. (2021) · Advanced Science · doi:10.1002/advs.202103645 · Cited by 59 · see citing works

Targeting KRAS-Mutant Non–Small-Cell Lung Cancer: One Mutation at a Time, With a Focus on KRAS G12C Mutations

Burns, T. F., Borghaei, H., Ramalingam, S. S., Mok, T. S. K., & Peters, S. (2020) · Journal of Clinical Oncology · doi:10.1200/jco.20.00744 · Cited by 56 · see citing works

Conformational transformation of switch domains in GDP/K-Ras induced by G13 mutants: An investigation through Gaussian accelerated molecular dynamics simulations and principal component analysis

Chen, J., Wang, L., Wang, W., Sun, H., Pang, L., & Bao, H. (2021) · Computers in Biology and Medicine · doi:10.1016/j.compbiomed.2021.104639 · Cited by 49 · see citing works

Annual review of KRAS inhibitors in 2022

Wang, H., Chi, L., Yu, F., Dai, H., Gao, C., Si, X., Wang, Z., Liu, L., Zheng, J., Shan, L., et al. (2023) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2023.115124 · Cited by 48 · see citing works

Blocking Ras inhibition as an antitumor strategy

Marín‐Ramos, N. I., Ortega‐Gutiérrez, S., & López-Rodríguez, M. L. (2018) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2018.01.017 · Cited by 46 · see citing works

Tackling Undruggable Targets with Designer Peptidomimetics and Synthetic Biologics

Swenson, C., Mandava, G., Thomas, D. M., & Moellering, R. E. (2024) · Chemical Reviews · doi:10.1021/acs.chemrev.4c00423 · Cited by 48 · see citing works

High-Throughput Kinetic Characterization of Irreversible Covalent Inhibitors of KRAS G12C by Intact Protein MS and Targeted MRM

Li, K. S., Quinn, J. G., Saabye, M. J., Guerrero, J. F. S., Nonomiya, J., Lian, Q., Phung, W., Izrayelit, Y., Walters, B. T., Gustafson, A. E., et al. (2022) · Analytical Chemistry · doi:10.1021/acs.analchem.1c04463 · Cited by 45 · see citing works

Investigation of the structural requirements of K-Ras(G12D) selective inhibitory peptide KRpep-2d using alanine scans and cysteine bridging

Niida, A., Sasaki, S., Yonemori, K., Sameshima, T., Yaguchi, M., Asami, T., Sakamoto, K., & Kamaura, M. (2017) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2017.04.063 · Cited by 41 · see citing works

Insights into microfabrication and implementation of microfluidics in pharmaceutical drug delivery and analysis

Al-wdan, O. A., Sharallah, O. A., Abdelwahab, N. A., Mohammed, A. O., Elmowafy, E. M., & Soliman, M. E. (2023) · OpenNano · doi:10.1016/j.onano.2023.100156 · Cited by 39 · see citing works

Discovery of cell active macrocyclic peptides with on-target inhibition of KRAS signaling

Lim, S., Boyer, N. C., Boo, N., Huang, C., Venkatachalam, G., Juang, Y.-C. A., Garrigou, M., Kaan, H. Y. K., Duggal, R., Peh, K. M., et al. (2021) · Chemical Science · doi:10.1039/d1sc05187c · Cited by 38 · see citing works

Bacteriophage-Mediated Cancer Gene Therapy

Petrov, G., Dymova, M., & Richter, V. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232214245 · Cited by 38 · see citing works

Discovery of a Bicyclic Peptidyl Pan-Ras Inhibitor

Buyanova, M. Y., Cai, S., Cooper, J. K., Rhodes, C. A., Salim, H., Sahni, A., Upadhyaya, P., Yang, R., Sarkar, A., Li, N., et al. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c01130 · Cited by 38 · see citing works

Expanding the Chemical Diversity of Genetically Encoded Libraries

Iskandar, S. E., Haberman, V. A., & Bowers, A. A. (2020) · ACS Combinatorial Science · doi:10.1021/acscombsci.0c00179 · Cited by 35 · see citing works

Molecular Mechanism of Phosphorylation-Mediated Impacts on the Conformation Dynamics of GTP-Bound KRAS Probed by GaMD Trajectory-Based Deep Learning

Chen, J., Wang, J., Yang, W., Zhao, L., Zhao, J., & Hu, G. (2024) · Molecules · doi:10.3390/molecules29102317 · Cited by 34 · see citing works

De-risking Drug Discovery of Intracellular Targeting Peptides: Screening Strategies to Eliminate False-Positive Hits

Ng, S., Juang, Y.-C. A., Chandramohan, A., Kaan, H. Y. K., Sadruddin, A., Yuen, T. Y., Ferrer‐Gago, F. J., Lee, X. C., Liew, X., Johannes, C. W., et al. (2020) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.0c00022 · Cited by 34 · see citing works

Accelerated Identification of Cell Active KRAS Inhibitory Macrocyclic Peptides using Mixture Libraries and Automated Ligand Identification System (ALIS) Technology

Garrigou, M., Sauvagnat, B., Duggal, R., Boo, N., Gopal, P., Johnston, J. M., Partridge, A. W., Sawyer, T. K., Biswas, K., & Boyer, N. C. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.2c00154 · Cited by 33 · see citing works

Protein-Based Degraders: From Chemical Biology Tools to Neo-Therapeutics

Ou, L., Setegne, M. T., Elliot, J., Shen, F., & Dassama, L. M. K. (2025) · Chemical Reviews · doi:10.1021/acs.chemrev.4c00595 · Cited by 30 · see citing works

Mechanism of activation and the rewired network: New drug design concepts

Nussinov, R., Zhang, M., Maloney, R., Tsai, C., Yavuz, B. R., Tunçbağ, N., & Jang, H. (2021) · Medicinal Research Reviews · doi:10.1002/med.21863 · Cited by 30 · see citing works

Cyclic Peptide Keap1–Nrf2 Protein–Protein Interaction Inhibitors: Design, Synthesis, and In Vivo Treatment of Acute Lung Injury

Zou, J., Yan, J., Lu, Y., Zhou, Y., Zhang, K., Han, Q., Han, D., Gai, C., Chai, X., Zhao, Q., et al. (2024) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.4c00065 · Cited by 29 · see citing works

Inhibition of Nonfunctional Ras

Nussinov, R., Jang, H., Gürsoy, A., Keskin, Ö., & Gaponenko, V. (2021) · Cell chemical biology · doi:10.1016/j.chembiol.2020.12.012 · Cited by 29 · see citing works

Advances in Targeted Therapy and Immunotherapy for Pancreatic Cancer

Liu, X., Li, Z., & Wang, Y. (2021) · Advanced Biology · doi:10.1002/adbi.201900236 · Cited by 29 · see citing works

Current Advances and Trends in KRAS Targeted Therapies for Colorectal Cancer

Teo, M. Y. M., Fong, J. Y., Lim, W. M., & In, L. L. A. (2021) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-21-0248 · Cited by 28 · see citing works

Small molecule inhibitors of RAS proteins with oncogenic mutations

Orgován, Z., & Keserű, G. M. (2020) · Cancer and Metastasis Reviews · doi:10.1007/s10555-020-09911-9 · Cited by 25 · see citing works

Exploiting RAS Nucleotide Cycling as a Strategy for Drugging RAS-Driven Cancers

Mattox, T. E., Chen, X., Maxuitenko, Y. Y., Keeton, A. B., & Piazza, G. A. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms21010141 · Cited by 25 · 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

Targeting RAS in neuroblastoma: Is it possible?

Lin, L., Miao, L., Lin, H., Cheng, J., Li, M., Zhuo, Z., & He, J. (2021) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2021.108054 · Cited by 24 · see citing works

Utilization of macrocyclic peptides to target protein-protein interactions in cancer

Yang, J., Zhu, Q., Wu, Y., Xiao-juan, Q., Liu, H., Jiang, B., Ge, D., & Song, X. (2022) · Frontiers in Oncology · doi:10.3389/fonc.2022.992171 · Cited by 23 · see citing works

Evolution of direct RAS inhibitors: from undruggable target to clinical breakthroughs

Wang, X., Wu, J., Xiao, A., Wang, J., & Tian, J. (2025) · Molecular Cancer · doi:10.1186/s12943-025-02364-0 · Cited by 24 · see citing works

The K-Ras(G12D)-inhibitory peptide KS-58 suppresses growth of murine CT26 colorectal cancer cell-derived tumors

Sakamoto, K., Lin, B., Nunomura, K., Izawa, T., & Nakagawa, S. (2022) · Scientific Reports · doi:10.1038/s41598-022-12401-3 · Cited by 21 · see citing works

Recent advances in the biology and therapy of medullary thyroid carcinoma

Nelkin, B. D. (2017) · F1000Research · doi:10.12688/f1000research.12645.1 · Cited by 21 · see citing works

Targeting the “undruggable” RAS with biologics

Whaby, M., Khan, I., & O’Bryan, J. P. (2022) · Advances in cancer research · doi:10.1016/bs.acr.2021.07.006 · Cited by 19 · see citing works

Targeting the ‘Undruggable’ Driver Protein, KRAS, in Epithelial Cancers: Current Perspective

Lam, K. K., Wong, S. H., & Cheah, P. Y. (2023) · Cells · doi:10.3390/cells12040631 · Cited by 19 · see citing works

Structure-based designing efficient peptides based on p53 binding site residues to disrupt p53-MDM2/X interaction

Rasafar, N., Barzegar, A., & Aghdam, E. M. (2020) · Scientific Reports · doi:10.1038/s41598-020-67510-8 · Cited by 15 · see citing works

Solid-phase peptide synthesis on disulfide-linker resin followed by reductive release affords pure thiol-functionalized peptides

Bognár, Z., Kumar, M. G., Nielsen, A. L., Merz, M. L., Pânzar, P. M. F., & Heinis, C. (2022) · Organic & Biomolecular Chemistry · doi:10.1039/d2ob00910b · Cited by 16 · see citing works

Allosteric Binding-Mediated Suppression on Activity of G12D KRAS Recognized via Markov State Model and Communication Pathway.

Chen, J.-Z., Wang, J., Wang, W., Zhao, L., Jin, H., & Hu, G.-D. (2026) · Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.5c07583 · Cited by 16 · see citing works

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 17 · see citing works

Targeting Ras with MacromoleculesPreprint

Pei, D., Chen, K., & Liao, H. (2017) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a031476 · Cited by 15 · see citing works

Nanoformulation of the K-Ras(G12D)-inhibitory peptide KS-58 suppresses colorectal and pancreatic cancer-derived tumors

Sakamoto, K., Qi, Y., & Miyako, E. (2023) · Scientific Reports · doi:10.1038/s41598-023-27825-8 · Cited by 14 · see citing works

Daily Practice Assessment of KRAS Status in NSCLC Patients: A New Challenge for the Thoracic Pathologist Is Right around the Corner

Bontoux, C., Hofman, V., Brest, P., Ilié, M., Mograbi, B., & Hofman, P. M. (2022) · Cancers · doi:10.3390/cancers14071628 · Cited by 14 · see citing works

Peptide inhibitors: Breaking cancer code

Coburn, F., Nsereko, Y., Armstrong, A. J., & Musaimi, O. A. (2025) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2025.117961 · Cited by 13 · see citing works

A Covalent Self-Reporting Peptide Degrader Enables Real-Time Monitoring of Targeted Protein Degradation In Vivo

Zhang, W., Yuan, L., Liu, R., Jing, Y., Lin, S., Fang, H., Li, Y., Zhang, X., Dai, J. Y., Liu, T., et al. (2025) · Journal of the American Chemical Society · doi:10.1021/jacs.5c07041 · Cited by 13 · see citing works

Phage-based peptides for pancreatic cancer diagnosis and treatment: alternative approach

Li, Y., Yang, K., Duan, H.-Y., Du, Y., & Ye, J. (2023) · Frontiers in Microbiology · doi:10.3389/fmicb.2023.1231503 · Cited by 13 · see citing works

Structural diversity inde novocyclic peptide ligands from genetically encoded library technologies

McAllister, T. E., Coleman, O. D., Roper, G., & Kawamura, A. (2020) · Peptide Science · doi:10.1002/pep2.24204 · Cited by 13 · see citing works

Overcoming Cellular and Systemic Barriers to Design the Next Wave of Peptide Therapeutics

Hochman, J. H., Sawyer, T. K., & Duggal, R. (2021) · Methods in pharmacology and toxicology · doi:10.1007/978-1-0716-1250-7_10 · Cited by 12 · see citing works

First-line treatments for KRAS-mutant non-small cell lung cancer: current state and future perspectives

He, Q., Liu, X., Jiang, L., Liu, P., Xuan, W., Wang, Y., Meng, R., Feng, H., Lv, S., Miao, Q., et al. (2024) · Cancer Biology & Therapy · doi:10.1080/15384047.2024.2441499 · Cited by 13 · see citing works

Recent trends in T7 phage application in diagnosis and treatment of various diseases

Yu, T., Sun, Z., Xiangyu, C., Pang, Q., & Deng, H. (2022) · International Immunopharmacology · doi:10.1016/j.intimp.2022.109071 · Cited by 12 · see citing works

The Use of Genetically Engineered Mouse Models for Studying the Function of Mutated Driver Genes in Pancreatic Cancer

Weng, C., Lin, Y., & Cheng, K. (2019) · Journal of Clinical Medicine · doi:10.3390/jcm8091369 · Cited by 12 · see citing works

Targeting a Novel KRAS Binding Site: Application of One-Component Stapling of Small (5–6-mer) Peptides

Fumagalli, G., Carbajo, R. J., Nissink, J. W. M., Tart, J., Dou, R., Thomas, A. P., & Spring, D. R. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c01334 · Cited by 11 · see citing works

Therapeutic peptides targeting the Ras superfamily

Hurd, C. A., Mott, H. R., & Owen, D. (2020) · Peptide Science · doi:10.1002/pep2.24165 · Cited by 10 · 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

Allosteric Inhibitor of KRas Identified Using a Barcoded Assay Microchip Platform

McCarthy, A., Kim, J.-W., Museth, A. K., Henning, R. K., Heath, J. E., Winson, E., Oh, J., Liang, J., Hong, S., & Heath, J. R. (2018) · Analytical Chemistry · doi:10.1021/acs.analchem.8b00706 · Cited by 10 · see citing works

The switch states of the GDP-bound HRAS affected by point mutations: a study from Gaussian accelerated molecular dynamics simulations and free energy landscapes

Bao, H., Wang, W., Sun, H., & Chen, J. (2023) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2023.2213355 · Cited by 10 · see citing works

Recent Anti-KRASG12D Therapies: A “Possible Impossibility” for Pancreatic Ductal Adenocarcinoma

Sobhani, N., Pittacolo, M., D’Angelo, A., & Marchegiani, G. (2025) · Cancers · doi:10.3390/cancers17040704 · Cited by 10 · see citing works

Pathogen biosensors for food safety and public healthcare based on specific biological probes biopanned by phage display: A critical review

Wang, M., Yang, Z., Liu, X., Jiang, Y., Zhang, H., & Liu, A. (2025) · Food Chemistry · doi:10.1016/j.foodchem.2025.145290 · Cited by 9 · see citing works

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 · see citing works

Peptide inhibitors targeting Ras and Ras-associated protein–protein interactions

Han, D., Li, A., Zhu, L., Zhuang, C., Zhao, Q., & Zou, Y. (2024) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2024.116878 · Cited by 7 · see citing works

NGS and the design of an optimized phage display workflow for peptide discovery

Bakhshinejad, B., & Kjær, A. (2025) · Amino Acids · doi:10.1007/s00726-025-03492-z · Cited by 6 · see citing works

Moving Towards Dawn: KRas Signaling and Treatment in Pancreatic Ductal Adenocarcinoma

Bhattacharya, S., & Rajpurohit, T. (2022) · Current Molecular Pharmacology · doi:10.2174/1874467215666220128161647 · Cited by 6 · see citing works

Ras Isoforms from Lab Benches to Lives—What Are We Missing and How Far Are We?

Nair, A., Kubatzky, K. F., & Saha, B. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22126508 · Cited by 6 · see citing works

Mycoplasma genitalium Protein of Adhesion Promotes the Early Proliferation of Human Urothelial Cells by Interacting with RPL35

Dai, P., Deng, X., Liu, P., Li, L., Luo, D., Liao, Y., & Zeng, Y. (2021) · Pathogens · doi:10.3390/pathogens10111449 · Cited by 6 · see citing works

Peptide Drug DiscoveryRaison d’Etre: Engineering Mindset, Design Rules and Screening Tools

Sawyer, T. K., & Biswas, K. (2022) · ACS symposium series · doi:10.1021/bk-2022-1417.ch001 · Cited by 6 · see citing works

Vaccination and Microbiota Manipulation Approaches for Colon Cancer Prevention in Rodent Models

Tosti, E., Srivastava, N., & Edelmann, W. (2023) · Cancer Prevention Research · doi:10.1158/1940-6207.capr-23-0015 · Cited by 6 · see citing works

Bioblockades join the assault on small G protein signalling

Mott, H. R., & Owen, D. (2018) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2018.01.001 · Cited by 6 · see citing works

Somatic Mutations in Surgically Treated Colorectal Liver Metastases: An Overview

Wang, J., Botvinov, J., Bhatt, A. J., Beyer, K., Kreis, M. E., Adam, M. A., Alseidi, A. A., & Margonis, G. A. (2024) · Cells · doi:10.3390/cells13080679 · Cited by 5 · see citing works

Design, synthesis, and biological evaluation of JNK1 peptide inhibitors for alleviating insulin resistance in type 2 diabetes

Heng, C., Wang, Y., Jiang, H., Gu, H., Li, Z., Niu, M.-M., Zhang, M., & Li, J. (2025) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2025.117892 · Cited by 5 · see citing works

Integrated Decision-Making in the Treatment of Colon-Rectal Cancer: The Case of KRAS-Mutated Tumors

Cherri, S., Melocchi, L., Gandolfi, L., Rossi, G., & Zaniboni, A. (2023) · Life · doi:10.3390/life13020395 · Cited by 5 · see citing works

Phage Display - A Promising Tool for the Recovery of Valuable Metals from Primary and Secondary Resources

Matys, S., Lederer, F., Schönberger, N., Braun, R., Lehmann, F., Flemming, K., Bachmann, S., Curtis, S. B., MacGillivray, R. T. A., & Pollmann, K. (2017) · Diffusion and defect data, solid state data. Part B, Solid state phenomena/Solid state phenomena · doi:10.4028/www.scientific.net/ssp.262.443 · Cited by 5 · see citing works

Design, synthesis, and antitumor activity of stapled peptide inhibitors targeting the RAS–RAF interactions

Han, D., Zhou, Y., Zhang, K., Gai, C., Zhang, P., Chai, X., Zhuo, X., Zhao, Q., Zou, Y., & Zhu, L. (2025) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2025.117568 · Cited by 4 · see citing works

Ligand-induced conformational changes in protein molecules detected by sum-frequency generation

Salafsky, J., Johansson, P. K., Abdelkader, E. H., & Otting, G. (2024) · Biophysical Journal · doi:10.1016/j.bpj.2024.09.017 · Cited by 4 · see citing works

A novel Imidazo[1,2-a]pyridine derivative modulates active KRASG12D through off-like conformational shifts in switch-I and switch-II regions, mimicking inactive KRASG12D

Ali, Y., Khan, A. A., Alanazi, A. M., Fatima, S., & Kozmon, S. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.132477 · Cited by 3 · see citing works

Suite of Biochemical and Cell-Based Assays for the Characterization of Kirsten Rat Sarcoma (KRAS) Inhibitors and Degraders

Kidane, M., Hoffman, R. M., Wolfe-Demarco, J. K., Huang, T.-Y., Teng, C.-L., Samanta, S., Lira, L. M. G., Lin‐Jones, J., Pallares, G., Lamerdin, J. E., et al. (2024) · ACS Pharmacology & Translational Science · doi:10.1021/acsptsci.4c00450 · Cited by 3 · see citing works

Identification and characterization of oncogenic KRAS G12V inhibitory peptides by phage display, molecular docking and molecular dynamic simulation

Saetang, J., Yamabhai, M., Rangnoi, K., Prompat, N., Haewphet, T., Sangkhathat, S., Tipmanee, V., & Benjakul, S. (2025) · Computers in Biology and Medicine · doi:10.1016/j.compbiomed.2025.110272 · Cited by 3 · see citing works

Simplified Expression and Production of Small Metal Binding Peptides

Braun, R., Matys, S., Schönberger, N., Lederer, F., & Pollmann, K. (2017) · Diffusion and defect data, solid state data. Part B, Solid state phenomena/Solid state phenomena · doi:10.4028/www.scientific.net/ssp.262.447 · Cited by 3 · see citing works

Lipid bilayer membrane permeability mechanism of the K-Ras(G12D)-inhibitory bicyclic peptide KS-58 elucidated by molecular dynamics simulations

Sakamoto, K., & Hirokawa, T. (2024) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2024.129649 · Cited by 3 · see citing works

Kirsten rat sarcoma inhibitors in clinical development against nonsmall cell lung cancer

Li, Y., Hu, L., & Xu, C. S. (2021) · Current Opinion in Oncology · doi:10.1097/cco.0000000000000808 · Cited by 3 · see citing works

A PDX model combined with CD-DST assay to evaluate the antitumor properties of KRpep-2d and oxaliplatin in KRAS (G12D) mutant colorectal cancer

Li, W., Chen, W., Wang, J., Zhao, G., Chen, L., Wan, Y., Luo, Q., Li, W., Huang, H., Li, W., et al. (2022) · Heliyon · doi:10.1016/j.heliyon.2022.e12518 · Cited by 2 · see citing works

The AUTACE That Degrades KRAS and Engages CD8 + T Cells for the Treatment of KRAS/TP53 Co‐Mutant Tumors

Li, L., Li, B., Hao, Y., Pang, B., Li, P., Li, C., & Tang, Y. (2026) · Advanced Science · doi:10.1002/advs.202518455 · Cited by 1 · see citing works

Macrocyclic peptides and peptidomimetics as modulators of protein–protein interactions

Parmar, R., Shrivastava, V., Kaur, G., Goyal, B., & Jain, R. (2026) · RSC Medicinal Chemistry · doi:10.1039/d6md00640j · Cited by 1 · see citing works

Discovery and development of MRTX1133, a potent, selective, noncovalent inhibitor of KRASG12D

Gill, A. L., & Wang, X. (2024) · Elsevier eBooks · doi:10.1016/b978-0-443-21861-3.00016-4 · Cited by 1 · see citing works

Abstract B35: Discovery of K-Ras(G12D)-targeting peptide KRpep-2d and its optimization strategy

Sakamoto, K. (2020) · Molecular Cancer Research · doi:10.1158/1557-3125.ras18-b35

Generation of KS-58 as the first K-Ras(G12D)-inhibitory peptide presenting anti-cancer activity in vivo

Sakamoto, K., Masutani, T., & Hirokawa, T. (2020) · Scientific Reports · doi:10.1038/s41598-020-78712-5 · Cited by 85 · see citing works

Identification of novel peptide inhibitors for oncogenic KRAS G12D as therapeutic options using mutagenesis-based remodeling and MD simulations

Samad, A., Khurshid, B., Mahmood, A., Rehman, A. U., Khalid, A., Abdalla, A. N., Algarni, A. S., & Wadood, A. (2023) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2023.2192298 · Cited by 14 · see citing works

Identification and characterization of oncogenic KRAS G12V inhibitory peptides by phage display, molecular docking and molecular dynamic simulation

Saetang, J., Yamabhai, M., Rangnoi, K., Prompat, N., Haewphet, T., Sangkhathat, S., Tipmanee, V., & Benjakul, S. (2025) · Computers in Biology and Medicine · doi:10.1016/j.compbiomed.2025.110272 · Cited by 3 · see citing works

In-silico design of peptide inhibitors of K-Ras target in cancer disease

Ghufran, M., Rehman, A. U., Shah, M., Ayaz, M., Ng, H. L., & Wadood, A. (2019) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2019.1704880 · Cited by 42 · see citing works