Rational Design and Binding Mode Duality of MDM2–p53 Inhibitors

In Vivo Activation of the p53 Pathway by Small-Molecule Antagonists of MDM2

Vassilev, L. T., Vu, B. T., Graves, B., Carvajal, D., Podlaski, F., Filipovic, Z., Kong, N., Kammlott, U., Lukacs, C., Klein, C., et al. (2004) · Science · doi:10.1126/science.1092472 · Cited by 4,661 · see citing works

Mdm2 promotes the rapid degradation of p53

Haupt, Y., Maya, R., Kazaz, A., & Oren, M. (1997) · Nature · doi:10.1038/387296a0 · Cited by 4,506 · see citing works

Regulation of p53 stability by Mdm2

Kubbutat, M. H. G., Jones, S. N., & Vousden, K. H. (1997) · Nature · doi:10.1038/387299a0 · Cited by 3,312 · see citing works

Structure of the MDM2 Oncoprotein Bound to the p53 Tumor Suppressor Transactivation Domain

Kussie, P. H., Gorina, S., Marechal, V., Elenbaas, B., Moreau, J., Levine, A. J., & Pavletich, N. P. (1996) · Science · doi:10.1126/science.274.5289.948 · Cited by 2,206 · see citing works

Reaching for high-hanging fruit in drug discovery at protein–protein interfaces

Wells, J. A., & McClendon, C. L. (2007) · Nature · doi:10.1038/nature06526 · Cited by 1,963 · see citing works

Amplification of a gene encoding a p53-associated protein in human sarcomas

Oliner, J. D., Kinzler, K. W., Meltzer, P. S., George, D. L., & Vogelstein, B. (1992) · Nature · doi:10.1038/358080a0 · Cited by 1,949 · see citing works

Small-molecule inhibitors of protein–protein interactions: progressing towards the dream

Arkin, M. R., & Wells, J. A. (2004) · Nature Reviews Drug Discovery · doi:10.1038/nrd1343 · Cited by 1,705 · see citing works

Oncoprotein MDM2 conceals the activation domain of tumour suppressor p53

Oliner, J. D., Pietenpol, J. A., Thiagalingam, S., Gyuris, J., Kinzler, K. W., & Vogelstein, B. (1993) · Nature · doi:10.1038/362857a0 · Cited by 1,447 · see citing works

Control of apoptosis by p53

Fridman, J. S., & Lowe, S. W. (2003) · Oncogene · doi:10.1038/sj.onc.1207116 · Cited by 1,401 · see citing works

Inhibiting the p53–MDM2 interaction: an important target for cancer therapy

Chène, P. (2003) · Nature Reviews Cancer · doi:10.1038/nrc991 · Cited by 765 · see citing works

Structure-Based Design of Spiro-oxindoles as Potent, Specific Small-Molecule Inhibitors of the MDM2−p53 Interaction

Ding, K., Lu, Y., Nikolovska-Coleska, Z., Wang, G., Qiu, S., Shangary, S., Gao, W., Qin, D., Stuckey, J., Krajewski, K., et al. (2006) · Journal of Medicinal Chemistry · doi:10.1021/jm051122a · Cited by 702 · see citing works

The genetics of the p53 pathway, apoptosis and cancer therapy

Vázquez, A., Bond, E. E., Levine, A. J., & Bond, G. L. (2008) · Nature Reviews Drug Discovery · doi:10.1038/nrd2656 · Cited by 674 · see citing works

Absolute configuration determination of chiral molecules in the solution state using vibrational circular dichroism

Freedman, T. B., Cao, X., Dukor, R. K., & Nafié, L. A. (2003) · Chirality · doi:10.1002/chir.10287 · Cited by 525 · see citing works

Discovery and Cocrystal Structure of Benzodiazepinedione HDM2 Antagonists That Activate p53 in Cells

Grasberger, B. L., Lu, T., Schubert, C., Parks, D. J., Carver, T. E., Koblish, H. K., Cummings, M. D., LaFrance, L. V., Milkiewicz, K. L., Calvo, R. R., et al. (2005) · Journal of Medicinal Chemistry · doi:10.1021/jm049137g · Cited by 433 · see citing works

The determination of the absolute configurations of chiral molecules using vibrational circular dichroism (VCD) spectroscopy

Stephens, P. J., Devlin, F. J., & Pan, J. (2007) · Chirality · doi:10.1002/chir.20477 · Cited by 365 · see citing works

Design of a synthetic Mdm2-binding mini protein that activates the p53 response in vivo

Böttger, A., Böttger, V., Sparks, A., Liu, W.-L., Howard, S. F., & Lane, D. P. (1997) · Current Biology · doi:10.1016/s0960-9822(06)00374-5 · Cited by 363 · see citing works

p53 protein stability in tumour cells is not determined by mutation but is dependent on Mdm2 binding

MIDGLEY, C. A., & Lane, D. P. (1997) · Oncogene · doi:10.1038/sj.onc.1201459 · Cited by 313 · see citing works

Discovery of Potent Antagonists of the Interaction between Human Double Minute 2 and Tumor Suppressor p53

Garcı́a-Echeverrı́a, C., Chêne, P., Blommers, M. J. J., & Furet, P. (2000) · Journal of Medicinal Chemistry · doi:10.1021/jm990966p · Cited by 246 · see citing works

Potent and orally active small-molecule inhibitors of the MDM2-p53 interaction

Yu, S., Qin, D., Shangary, S., Chen, J., Wang, G., Ding, K., McEachern, D., Qiu, S., Nikolovska-Coleska, Z., Miller, R., et al. (2009) · Journal of Medicinal Chemistry · doi:10.1021/jm901400z · Cited by 180 · see citing works

New antimetabolites in cancer chemotherapy and their clinical impact

Kaye, S. B. (1998) · British Journal of Cancer · doi:10.1038/bjc.1998.747 · Cited by 177 · see citing works

1,4-Benzodiazepine-2,5-diones as small molecule antagonists of the HDM2–p53 interaction: discovery and SAR

Parks, D. J., LaFrance, L. V., Calvo, R. R., Milkiewicz, K. L., Gupta, V., Lattanze, J., Ramachandren, K., Carver, T. E., Petrella, E. C., Cummings, M. D., et al. (2004) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2004.11.009 · Cited by 170 · see citing works

Structure-Based Design of Novel Inhibitors of the MDM2–p53 Interaction

Rew, Y., Sun, D., de Turiso, F. G.-L., Bartberger, M. D., Beck, H. P., Canon, J. R., Chen, A., Chow, D. T., Deignan, J., Fox, B. M., et al. (2012) · Journal of Medicinal Chemistry · doi:10.1021/jm300354j · Cited by 166 · see citing works

The Structure‐Based Design of Mdm2/Mdmx–p53 Inhibitors Gets Serious

Popowicz, G. M., Dömling, A. S. S., & Holak, T. A. (2011) · Angewandte Chemie International Edition · doi:10.1002/anie.201003863 · Cited by 166 · see citing works

Discovery and Optimization of Chromenotriazolopyrimidines as Potent Inhibitors of the Mouse Double Minute 2−Tumor Protein 53 Protein−Protein Interaction

Allen, J. G., Bourbeau, M. P., Wohlhieter, G. E., Bartberger, M. D., Michelsen, K., Hungate, R. W., Gadwood, R. C., Gaston, R. D., Evans, B., Mann, L. W., et al. (2009) · Journal of Medicinal Chemistry · doi:10.1021/jm900681h · Cited by 148 · see citing works

HDM2 protein overexpression, but not gene amplification, is related to tumorigenesis of cutaneous melanoma.

Polsky, D., Bastian, B. C., Hazan, C., Melzer, K., Pack, J., Houghton, A., BUSAM, K. J., Cordon‐Cardo, C., & Osman, I. (2001) · PubMed · Cited by 120 · see citing works

Mdm2 overexpression and p14ARF inactivation are two mutually exclusive events in primary human lung tumors

Eymin, B., Gazzéri, S., Brambilla, C., & Brambilla, E. M. (2002) · Oncogene · doi:10.1038/sj.onc.1205359 · Cited by 104 · see citing works

Small-Molecule Inhibitors of the p53-MDM2 Interaction

Vu, B. T., & Vassilev, L. T. (2010) · Current topics in microbiology and immunology · doi:10.1007/82_2010_110 · Cited by 78 · see citing works

Enhanced pharmacokinetic properties of 1,4-benzodiazepine-2,5-dione antagonists of the HDM2-p53 protein–protein interaction through structure-based drug design

Parks, D. J., LaFrance, L. V., Calvo, R. R., Milkiewicz, K. L., Marugán, J., Raboisson, P., Schubert, C., Koblish, H. K., Zhao, S., Franks, C. F., et al. (2006) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2006.03.055 · Cited by 76 · see citing works

NMR structure of a complex between MDM2 and a small molecule inhibitor

Fry, D. C., Emerson, S. D., Palme, S., Vu, B. T., Liu, C., & Podlaski, F. (2004) · Journal of Biomolecular NMR · doi:10.1023/b:jnmr.0000048856.84603.9b · Cited by 75 · see citing works

The central valine concept provides an entry in a new class of non peptide inhibitors of the p53–MDM2 interaction

Furet, P., Chêne, P., Pover, A. D., Stachyra, T., Lisztwan, J. H., Kallen, J. A., & Masuya, K. (2012) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2012.03.083 · Cited by 73 · see citing works

1,4‐Thienodiazepine‐2,5‐diones via MCR (I): Synthesis, Virtual Space and p53‐Mdm2 Activity

Huang, Y., Wolf, S., Biśta, M., Meireles, L., Camacho, C. J., Holak, T. A., & Dömling, A. S. S. (2010) · Chemical Biology & Drug Design · doi:10.1111/j.1747-0285.2010.00989.x · Cited by 65 · see citing works

Colour-coded switches

Jackson, I. J. (1993) · Nature · doi:10.1038/362587a0 · Cited by 64 · see citing works

Improvement of the synthesis and pharmacokinetic properties of chromenotriazolopyrimidine MDM2-p53 protein-protein inhibitors

Beck, H. P., DeGraffenreid, M. R., Fox, B. M., Allen, J. G., Rew, Y., Schneider, S., Saiki, A. Y., Yu, D., Oliner, J. D., Salyers, K. L., et al. (2010) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2010.11.027 · Cited by 42 · see citing works

123I-labelled vasoactive intestinal peptide receptor scintigraphy in patients with colorectal cancer

Raderer, M., Kurtaran, A., Hejna, M., Vorbeck, F., Angelberger, P., Scheithauer, W., & Virgolini, I. J. (1998) · British Journal of Cancer · doi:10.1038/bjc.1998.433 · Cited by 33 · see citing works

1,2-Diphenyl-2-Aminoethanols. I. Synthesis of some erythro-1,2-Diphenyl-2-Alkylaminoethanols

Wheatley, W. B., Fitzgibbon, W. E., & Cheney, L. C. (1953) · The Journal of Organic Chemistry · doi:10.1021/jo50017a017 · Cited by 21 · see citing works

Drug discovery in the p53 pathway

Lane, D. P., Midgley, C., Sparks, A., Blattner, C., Binden, C., & Laine, S. (2000) · Breast Cancer Research · doi:10.1186/bcr137 · Cited by 1 · see citing works

Drugging the p53 pathway: understanding the route to clinical efficacy

Khoo, K. H., Verma, C. S., & Lane, D. P. (2014) · Nature Reviews Drug Discovery · doi:10.1038/nrd4236 · Cited by 723 · see citing works

Targeting p53–MDM2 interaction by small-molecule inhibitors: learning from MDM2 inhibitors in clinical trials

Zhu, H., Gao, H., Ji, Y., Zhou, Q., Du, Z., Tian, L., Jiang, Y., Yao, K., & Zhou, Z. (2022) · Journal of Hematology & Oncology · doi:10.1186/s13045-022-01314-3 · Cited by 223 · see citing works

Small‐Molecule Control of Intracellular Protein Levels through Modulation of the Ubiquitin Proteasome System

Buckley, D. L., & Crews, C. M. (2014) · Angewandte Chemie International Edition · doi:10.1002/anie.201307761 · Cited by 153 · see citing works

Targeting MDM2-p53 Interaction for Cancer Therapy: Are We There Yet?

Nag, S. A., Zhang, X., Srivenugopal, K. S., Wang, M.-H., Wang, W., & Zhang, R. (2014) · Current Medicinal Chemistry · doi:10.2174/09298673113206660325 · Cited by 151 · see citing works

Discovery of a Small Molecule MDM2 Inhibitor (AMG 232) for Treating Cancer

Rew, Y., & Sun, D. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm500627s · Cited by 125 · see citing works

How To Design a Successful p53–MDM2/X Interaction Inhibitor: A Thorough Overview Based on Crystal Structures

Estrada‐Ortiz, N., Neochoritis, C. G., & Dömling, A. S. S. (2015) · ChemMedChem · doi:10.1002/cmdc.201500487 · Cited by 100 · see citing works

Synthesis, in Vitro, and in Cell Studies of a New Series of [Indoline-3,2′-thiazolidine]-Based p53 Modulators

Bertamino, A., Soprano, M., Musella, S., Rusciano, M. R., Sala, M., Vernieri, E., Sarno, V. D., Limatola, A., Carotenuto, A., Cosconati, S., et al. (2013) · Journal of Medicinal Chemistry · doi:10.1021/jm400311n · Cited by 86 · see citing works

Selective and Potent Morpholinone Inhibitors of the MDM2–p53 Protein–Protein Interaction

González, A. Z., Eksterowicz, J. E., Bartberger, M. D., Beck, H. P., Canon, J. R., Chen, A., Chow, D. T., Duquette, J., Fox, B. M., Fu, J., et al. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm401767k · Cited by 84 · see citing works

Optimization and Evaluation of Site-Identification by Ligand Competitive Saturation (SILCS) as a Tool for Target-Based Ligand Optimization

Ustach, V. D., Lakkaraju, S. K., Jo, S., Yu, W., Jiang, W., & MacKerell, A. D. (2019) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.9b00210 · Cited by 81 · see citing works

Reviving the guardian of the genome: Small molecule activators of p53

Nguyen, D., Liao, W., Zeng, S. X., & Lu, H. (2017) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2017.03.013 · Cited by 80 · see citing works

Design of Chemically Stable, Potent, and Efficacious MDM2 Inhibitors That Exploit the Retro-Mannich Ring-Opening-Cyclization Reaction Mechanism in Spiro-oxindoles

Aguilar, A., Sun, W., Liu, L., Lu, J., McEachern, D., Bernard, D., Deschamps, J. R., & Wang, S. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm501541j · Cited by 79 · see citing works

Synthesis and evaluation of spiroisoxazoline oxindoles as anticancer agents

Ribeiro, C. J. A., Amaral, J. D., Rodrigues, C. M. P., Moreira, R., & Santos, M. M. M. (2013) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2013.10.048 · Cited by 67 · see citing works

Asymmetric Cross-Coupling of Aldehydes with Diverse Carbonyl or Iminyl Compounds by Photoredox-Mediated Cobalt Catalysis

Chi, Z., Liao, J.-B., Cheng, X., Ye, Z., Yuan, W., Lin, Y., & Gong, L. (2024) · Journal of the American Chemical Society · doi:10.1021/jacs.4c01443 · Cited by 64 · see citing works

Apoptosis Therapy in Cancer: The First Single-molecule Co-activating p53 and the Translocator Protein in Glioblastoma

Daniele, S., Taliani, S., Pozzo, E. D., Giacomelli, C., Costa, B., Trincavelli, M. L., Rossi, L., Pietra, V. L., Barresi, E., Carotenuto, A., et al. (2014) · Scientific Reports · doi:10.1038/srep04749 · Cited by 64 · see citing works

The development of piperidinones as potent MDM2-P53 protein-protein interaction inhibitors for cancer therapy

Liao, G., Yang, D., Ma, L., Li, W., Hu, L., Zeng, L., Wu, P., Duan, L., & Liu, Z. (2018) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2018.09.044 · Cited by 63 · see citing works

A Radical Approach for Asymmetric α-C–H Addition of N-Sulfonyl Benzylamines to Aldehydes

Hu, H., Shi, Z., Guo, X., Zhang, F., & Wang, Z. (2024) · Journal of the American Chemical Society · doi:10.1021/jacs.3c12043 · Cited by 59 · see citing works

Copper-catalyzed base-accelerated direct oxidation of C–H bond to synthesize benzils, isatins, and quinoxalines with molecular oxygen as terminal oxidant

Yu, J., Mao, S., & Wang, Y. (2015) · Tetrahedron Letters · doi:10.1016/j.tetlet.2015.02.019 · Cited by 59 · see citing works

Small-Molecule MDM2-p53 Inhibitors: Recent Advances

Zhang, B., Golding, B. T., & Hardcastle, I. R. (2015) · Future Medicinal Chemistry · doi:10.4155/fmc.15.13 · Cited by 58 · see citing works

Novel Inhibitors of the MDM2-p53 Interaction Featuring Hydrogen Bond Acceptors as Carboxylic Acid Isosteres

González, A. Z., Li, Z., Beck, H. P., Canon, J. R., Chen, A., Chow, D. T., Duquette, J., Eksterowicz, J. E., Fox, B. M., Fu, J., et al. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm401911v · Cited by 58 · see citing works

Synthesis and Evaluation of Thiazolidinone–Pyrazole Conjugates as Anticancer and Antimicrobial Agents

Bhat, M., Poojary, B., Kalal, B. S., Matada, G. S. P., Kabilan, S., Kumar, V., Shruthi, N., Anand, S. A. A., & Pai, V. R. (2018) · Future Medicinal Chemistry · doi:10.4155/fmc-2017-0191 · Cited by 55 · see citing works

Cr-Catalyzed Asymmetric Cross Aza-Pinacol Couplings for β-Amino Alcohol Synthesis

Hu, H., & Wang, Z. (2023) · Journal of the American Chemical Society · doi:10.1021/jacs.3c08493 · Cited by 52 · see citing works

Organocatalytic, Diastereo- and Enantioselective Synthesis of Nonsymmetric cis -Stilbene Diamines: A Platform for the Preparation of Single-Enantiomer cis -Imidazolines for Protein–Protein Inhibition

Vara, B., Mayasundari, A., Tellis, J. C., Danneman, M. W., Arredondo, V., Davis, T. A., Min, J., Finch, K. E., Guy, R. K., & Johnston, J. N. (2014) · The Journal of Organic Chemistry · doi:10.1021/jo501003r · Cited by 50 · see citing works

Synthesis of N-Boc-α-amino Acids from Carbon Dioxide by Electrochemical Carboxylation of N-Boc-α-aminosulfones

Senboku, H., Minemura, Y., Suzuki, Y., Matsuno, H., & Takakuwa, M. (2021) · The Journal of Organic Chemistry · doi:10.1021/acs.joc.1c01516 · Cited by 49 · see citing works

Determination of the Absolute Configurations of Chiral Drugs Using Chiroptical Spectroscopy

Polavarapu, P. L. (2016) · Molecules · doi:10.3390/molecules21081056 · Cited by 46 · see citing works

A balancing act: using small molecules for therapeutic intervention of the p53 pathway in cancer

Miller, J. J., Gaiddon, C., & Storr, T. (2020) · Chemical Society Reviews · doi:10.1039/d0cs00163e · Cited by 46 · see citing works

Discovery of AM-7209, a Potent and Selective 4-Amidobenzoic Acid Inhibitor of the MDM2–p53 Interaction

Rew, Y., Sun, D., Yan, X., Beck, H. P., Canon, J. R., Chen, A., Duquette, J., Eksterowicz, J. E., Fox, B. M., Fu, J., et al. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm501550p · Cited by 45 · see citing works

Asymmetric Transfer Hydrogenation: Dynamic Kinetic Resolution of α-Amino Ketones

Gediya, S. K., Clarkson, G. J., & Wills, M. (2020) · The Journal of Organic Chemistry · doi:10.1021/acs.joc.0c01438 · Cited by 45 · see citing works

Computational Modeling as a Tool to Investigate PPI: From Drug Design to Tissue Engineering

Pérez, J. J., Pérez, R. A., & Pérez, A. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.681617 · Cited by 43 · see citing works

The Use of Chlorobenzene as a Probe Molecule in Molecular Dynamics Simulations

Tan, Y. S., Spring, D. R., Abell, C., & Verma, C. S. (2014) · Journal of Chemical Information and Modeling · doi:10.1021/ci500215x · Cited by 40 · see citing works

Disruption of protein–protein interactions: hot spot detection, structure-based virtual screening and in vitro testing for the anti-cancer drug target – survivin

Sarvagalla, S., Cheung, C. H. A., Tsai, J.-Y., Hsieh, H., & Coumar, M. S. (2016) · RSC Advances · doi:10.1039/c5ra22927h · Cited by 38 · see citing works

Tetra-substituted imidazoles as a new class of inhibitors of the p53–MDM2 interaction

Vaupel, A., Bold, G., Pover, A. D., Stachyra, T., Lisztwan, J. H., Kallen, J. A., Masuya, K., & Furet, P. (2014) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2014.03.039 · Cited by 37 · see citing works

Identification of new inhibitors of Mdm2–p53 interaction via pharmacophore and structure-based virtual screening

Atatreh, N., Ghattas, M. A., Bardaweel, S. K., Rawashdah, S. A., & Sorkhy, M. A. (2018) · Drug Design Development and Therapy · doi:10.2147/dddt.s182444 · Cited by 35 · see citing works

Chemical Variations on the p53 Reactivation Theme

Ribeiro, C. J. A., Rodrigues, C. M. P., Moreira, R., & Santos, M. M. M. (2016) · Pharmaceuticals · doi:10.3390/ph9020025 · Cited by 35 · see citing works

Developing structure–activity relationships from an HTS hit for inhibition of the Cks1–Skp2 protein–protein interaction

Singh, R., Sran, A. S., Carroll, D. C., Huang, J., Tsvetkov, L. M., Zhou, X., Sheung, J., McLaughlin, J., Issakani, S. D., Payan, D. G., et al. (2015) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2015.09.067 · Cited by 33 · see citing works

Roles of computational modelling in understanding p53 structure, biology, and its therapeutic targeting

Tan, Y. S., Mhoumadi, Y., & Verma, C. S. (2019) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjz009 · Cited by 32 · see citing works

Practical Approach for Preparation of Unsymmetric Benzils from β-Ketoaldehydes

Ruan, L., Shi, M. J., Li, N., Ding, X., Yang, F., & Tang, J. (2014) · Organic Letters · doi:10.1021/ol403762e · Cited by 31 · see citing works

Resistance acquisition to MDM2 inhibitors

Cinatl, J., Speidel, D., Hardcastle, I., & Michaelis, M. (2014) · Biochemical Society Transactions · doi:10.1042/bst20140035 · Cited by 30 · see citing works

Recent Synthetic Approaches towards Small Molecule Reactivators of p53

Silva, J. L., Lima, C. G. S., Rangel, L. P., Ferretti, G. D. S., Pauli, F. P., Ribeiro, R. C. B., Silva, T. B., da Silva, F. D. C., & Ferreira, V. F. (2020) · Biomolecules · doi:10.3390/biom10040635 · Cited by 28 · see citing works

Impact of electronic polarizability on protein-functional group interactions

Goel, H., Yu, W., Ustach, V. D., Aytenfisu, A. H., Sun, D., & MacKerell, A. D. (2020) · Physical Chemistry Chemical Physics · doi:10.1039/d0cp00088d · Cited by 27 · see citing works

Evolution in non-peptide α-helix mimetics on the road to effective protein-protein interaction modulators

Algar, S., Martín‐Martinez, M., & González‐Muñiz, R. (2020) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2020.113015 · Cited by 26 · see citing works

Microsecond simulations of mdm2 and its complex with p53 yield insight into force field accuracy and conformational dynamics

Pantelopulos, G. A., Mukherjee, S., & Voelz, V. A. (2015) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.24852 · Cited by 26 · see citing works

Transition metal-free oxidation of ynamides for synthesis of α-keto-imides

Chikugo, T., Yauchi, Y., Ide, M., & Iwasawa, T. (2014) · Tetrahedron · doi:10.1016/j.tet.2014.04.080 · Cited by 23 · see citing works

p53: An Attractive Therapeutic Target for Cancer

Patel, K. R., & Patel, H. D. (2019) · Current Medicinal Chemistry · doi:10.2174/1573406415666190621094704 · Cited by 24 · see citing works

Synthesis, characterization, and antiproliferative and apoptosis inducing effects of novel s -triazine derivatives

Shanmugam, M., Narayanan, K., Prasad, K. H., Karthikeyan, D., Loganathan, C., Atchudan, R., & Chidambaranathan, V. (2017) · New Journal of Chemistry · doi:10.1039/c7nj03348f · Cited by 22 · see citing works

Absolute Binding Free Energy Calculations for Highly Flexible Protein MDM2 and Its Inhibitors

Singh, N., & Li, W. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21134765 · Cited by 21 · see citing works

Targeting p53-MDM2 interactions to identify small molecule inhibitors for cancer therapy: beyond “Failure to rescue”

Chukwuemeka, P. O., Umar, H. I., Iwaloye, O., Oretade, O. M., Olowosoke, C. B., Elabiyi, M. O., Igbe, F. O., Oretade, O. J., Eigbe, J. O., & Adeojo, F. J. (2021) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2021.1924267 · Cited by 19 · see citing works

Synthesis and Biological Evaluation of Novel Dispiro-Indolinones with Anticancer Activity

Ivanenkov, Y. A., Kukushkin, M. E., Beloglazkina, A. A., Shafikov, R. R., Barashkin, A. A., Ayginin, A. A., Serebryakova, M. S., Majouga, A. G., Skvortsov, D. A., Тафеенко, В. А., et al. (2023) · Molecules · doi:10.3390/molecules28031325 · Cited by 19 · see citing works

Group-based QSAR and molecular dynamics mechanistic analysis revealing the mode of action of novel piperidinone derived protein–protein inhibitors of p53-MDM2

Goyal, S., Grover, S., Dhanjal, J. K., Tyagi, C., Goyal, M., & Grover, A. (2014) · Journal of Molecular Graphics and Modelling · doi:10.1016/j.jmgm.2014.04.015 · Cited by 19 · see citing works

Discovery of Novel 3,3-Disubstituted Piperidines as Orally Bioavailable, Potent, and Efficacious HDM2-p53 Inhibitors

Bogen, S. L., Pan, W., Gibeau, C. R., Lahue, B. R., Ma, Y., Nair, L. G., Seigel, E., Shipps, G. W., Tian, Y., Wang, Y., et al. (2016) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.5b00472 · Cited by 19 · see citing works

Recent Advancements in the Discovery of MDM2/MDM2-p53 Interaction Inhibitors for the Treatment of Cancer

Bhatia, N., Khator, R., Kulkarni, S., Singh, Y., Kumar, P., & Thareja, S. (2022) · Current Medicinal Chemistry · doi:10.2174/0929867330666221114103924 · Cited by 18 · see citing works

Activity‐Directed Synthesis of Inhibitors of the p53/ h DM2 Protein–Protein Interaction

Green, A. I., Hóbor, F., Tinworth, C. P., Warriner, S. L., Wilson, A. J., & Nelson, A. S. (2020) · Chemistry - A European Journal · doi:10.1002/chem.202002153 · Cited by 17 · see citing works

Synthesis, structure prediction, pharmacokinetic properties, molecular docking and antitumor activities of some novel thiazinone derivatives

Anand, S. A. A., Loganathan, C., Thomas, N. S., Saravanan, K., Alphonsa, A. T., & Kabilan, S. (2015) · New Journal of Chemistry · doi:10.1039/c5nj01369k · Cited by 18 · see citing works

Recent advances in the pharmacological targeting of ubiquitin-regulating enzymes in cancer

Montagut, A. M., Armengol, M., Gorjón-de-Pablo, G., Estrada‐Tejedor, R., Borrell, J. I., & Roué, G. (2022) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2022.02.007 · Cited by 17 · see citing works

p53–MDM2 and MDMX Antagonists

Neochoritis, C. G., Estrada‐Ortiz, N., Khoury, K., & Dömling, A. S. S. (2014) · Annual reports in medicinal chemistry · doi:10.1016/b978-0-12-800167-7.00012-2 · Cited by 16 · see citing works

8-Triazolylpurines: Towards Fluorescent Inhibitors of the MDM2/p53 Interaction

Pettersson, M., Bliman, D., Jacobsson, J., Nilsson, J. R., Min, J., Iconaru, L. I., Guy, R. K., Kriwacki, R. W., Andréasson, J., & Grøtli, M. (2015) · PLoS ONE · doi:10.1371/journal.pone.0124423 · Cited by 15 · see citing works

Core modification of substituted piperidines as Novel inhibitors of HDM2–p53 protein–protein interaction

Pan, W., Lahue, B. R., Ma, Y., Nair, L. G., Shipps, G. W., Wang, Y., Doll, R. J., & Bogen, S. L. (2014) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2014.02.055 · Cited by 15 · see citing works

Intramolecular 6-exo-dig Post-Ugi Cyclization of N-Substituted 2-Alkynamides: Direct Access to Functionalized Morpholinone Glycoconjugates

Kumar, H., Prajapati, G., Dubey, A., Ampapathi⧧, R. S., & Mandal, P. K. (2020) · Organic Letters · doi:10.1021/acs.orglett.0c03486 · Cited by 15 · see citing works

Design, Synthesis and Evaluation of 2,5-Diketopiperazines as Inhibitors of the MDM2-p53 Interaction

Pettersson, M., Quant, M., Min, J., Iconaru, L. I., Kriwacki, R. W., Waddell, M. B., Guy, R. K., Luthman, K., & Grøtli, M. (2015) · PLoS ONE · doi:10.1371/journal.pone.0137867 · Cited by 15 · see citing works

Design, in silico prioritization and biological profiling of apoptosis-inducing lactams amenable by the Castagnoli-Cushman reaction

Krasavin, M., Gureev, M., Dar’in, D. V., Bakulina, O., Chizhova, M., Lepikhina, A., Novikova, D., Grigoreva, T. A., Ivanov, G. S., Zhumagalieva, A., et al. (2018) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2018.04.036 · Cited by 15 · see citing works

Comparison of Molecular Docking and Molecular Dynamics Simulations of 1,3-Thiazin-4-One with MDM2 Protein

Anand, S. A. A., Loganathan, C., Saravanan, K., & Kabilan, S. (2015) · International Letters of Chemistry Physics and Astronomy · doi:10.18052/www.scipress.com/ilcpa.60.161 · Cited by 13 · see citing works

Steuerung der intrazellulären Proteinmenge durch niedermolekulare Modulatoren des Ubiquitin‐Proteasom‐Systems

Buckley, D. L., & Crews, C. M. (2014) · Angewandte Chemie · doi:10.1002/ange.201307761 · Cited by 11 · see citing works

Ni-catalyzed enantioselective synthesis of β-aminoboronates via spin-center shift and proton transfer

Wang, Y., Wu, G., Zhu, W., Qi, X., & Song, Q. (2025) · Science Advances · doi:10.1126/sciadv.aea0777 · Cited by 9 · see citing works

One-pot, two-step desymmetrization of symmetrical benzils catalyzed by the methylsulfinyl (dimsyl) anion

Ragno, D., Bortolini, O., Giovannini, P. P., Massi, A., Pacifico, S., & Zaghi, A. (2014) · Organic & Biomolecular Chemistry · doi:10.1039/c4ob00759j · Cited by 7 · see citing works

Inhibiting mechanism of small molecule toward the p53‐ MDM 2 interaction: A molecular dynamic exploration

Chen, J., Wang, J., Pang, L., & Zhu, W. (2018) · Chemical Biology & Drug Design · doi:10.1111/cbdd.13345 · Cited by 6 · see citing works

Logic-based modeling and drug repurposing for the prediction of novel therapeutic targets and combination regimens against E2F1-driven melanoma progression

Singh, N., Khan, F., Bala, L., Vera, J., Wolkenhauer, O., Pützer, B., Logotheti, S., & Gupta, S. (2023) · BMC Chemistry · doi:10.1186/s13065-023-01082-2 · Cited by 4 · see citing works

1,2-Amino Alcohols via Visible-Light-Mediated Mannich-Type Reaction Enabled by Brook Rearrangement

Wang, A.-L., Yao, Y., Zhang, X.-G., & Xu, P. (2026) · Organic Letters · doi:10.1021/acs.orglett.5c04773 · Cited by 5 · see citing works

FMO Drug Design Consortium

Fukuzawa, K., Tanaka, S., Yagi, Y., Kurita, N., Kawashita, N., Takaba, K., & Honma, T. (2021) · Springer eBooks · doi:10.1007/978-981-15-9235-5_8 · Cited by 5 · see citing works

The p53–Mdm2 regulation relationship under different radiation doses based on the continuous–discrete extended Kalman filter algorithm

Li, Y., Chen, J., Jiang, L., Zeng, N., Jiang, H., & Du, M. (2017) · Neurocomputing · doi:10.1016/j.neucom.2017.08.016 · Cited by 4 · see citing works

Protein–Protein Interaction Inhibitors in Cancer

Hardcastle, I. R. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-409547-2.12392-3 · Cited by 4 · see citing works

Interaction Analysis by Fragment Molecular Orbital Method for Drug Discovery Research

Kawashita, N. (2024) · Chemical and Pharmaceutical Bulletin · doi:10.1248/cpb.c24-00448 · Cited by 3 · see citing works

Discovery of 1,2‐Naphthoquinone Derivatives as Potent p53‐MDM2 Interaction Inhibitors

Jung, M. E., Go, A., Yoo, D., Chae, J., Jeon, M., Lim, B., & Choi, G. (2019) · Bulletin of the Korean Chemical Society · doi:10.1002/bkcs.11897 · Cited by 2 · see citing works

Exploring the binding dynamics of triazolyl-thio-oxazines for MDM2-p53 disruption: Design, synthesis, and p53 upregulation

Narasimhachar, B. C., Nagaraja, O., Ahn, K. S., Yang, M. H., Harish, K. K., Madegowda, M., Bender, A., Basappa, B., & Chandrashekara, P. G. (2026) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2026.151392 · Cited by 1 · see citing works

Benzothiazole–Triphenylphosphonium Conjugates: Synthesis, In Silico Analysis, and Exploratory In Vitro Effects on HT‐29 Colorectal Cancer Cell Viability

Laghchioua, F., Gomes, A. T. P. C., Mendes, A. K., Mendes, R. F., Paz, F. A. A., Videira, P. A., Faustino, M. A. F., Cavaleiro, J. A. S., Rakib, E. M., Neves, M. D. G. P. M. S., et al. (2026) · ChemMedChem · doi:10.1002/cmdc.70382 · Cited by 1 · see citing works

Phe19 modification of HDM2-p53 PPI inhibitors to alleviate CYP3A4 metabolism/mechanism-based inhibition liability

Tian, Y., Lahue, B. R., Ma, Y., Nair, L. G., Pan, W., Doll, R. J., Guzi, T. J., Ma, Y., Wang, Y., & Bogen, S. L. (2022) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2022.128625 · Cited by 1 · see citing works

Discovery of AMG 232, a Small Molecule Disrupting the p53-MDM2 Protein–Protein Interaction and Development of a Validation-Ready Process for Its Manufacture

Caille, S., & Lucas, B. S. (2022) · ACS symposium series · doi:10.1021/bk-2022-1423.ch005 · Cited by 1 · see citing works

Anti-cancer activity elucidation of geissolosimine as an MDM2-p53 interaction inhibitor: An in-silico study

Al-Amin, M., Tanjin, R., Karim, M. R., Etee, J. M., Siddika, A., Akter, N., Uddin, M. H., Mahmud, R., Saffat, T., Hossen, M. F., et al. (2025) · PLoS ONE · doi:10.1371/journal.pone.0323003 · Cited by 1 · see citing works

Targeting dysregulation signatures of p53-MDM2 interactions to identify newer small molecule inhibitors for cancer therapy: Insight from computational directionPreprint

Chukwuemeka, P. O., Umar, H. I., Iwaloye, O., Oretade, O. M., Olowosoke, C. B., Elabiyi, M. O., Igbe, F. O., Oretade, O. J., Eigbe, J. O., & Adeojo, F. J. (2021) · Research Square · doi:10.21203/rs.3.rs-217761/v1 · Cited by 1 · see citing works

Inhibition of the MDM2/p53 Interaction Design, Synthesis and Evaluation of MDM2 Inhibitors

Pettersson, M. (2015) · Gothenburg University Publications Electronic Archive (Gothenburg University) · Cited by 1 · see citing works

Discovery of AMG 232, a Small Molecule MDM2 Inhibitor in Clinical Development and its Back-up Clinical Candidate, AM-7209

Rew, Y., & Eksterowicz, J. E. (2020) · Royal Society of Chemistry eBooks · doi:10.1039/9781788016544-00280

Additional file 3 of Logic-based modeling and drug repurposing for the prediction of novel therapeutic targets and combination regimens against E2F1-driven melanoma progression

Singh, N., Khan, F. M., Bala, L., Vera, J., Olaf Wolkenhauer, A., Pützer, B. M., Logotheti, S., & Gupta, S. K. (2024) · Figshare · doi:10.6084/m9.figshare.26643979

Additional file 1 of Logic-based modeling and drug repurposing for the prediction of novel therapeutic targets and combination regimens against E2F1-driven melanoma progression

Singh, N., Khan, F. M., Bala, L., Vera, J., Olaf Wolkenhauer, A., Pützer, B. M., Logotheti, S., & Gupta, S. K. (2024) · Figshare · doi:10.6084/m9.figshare.26643973

Additional file 2 of Logic-based modeling and drug repurposing for the prediction of novel therapeutic targets and combination regimens against E2F1-driven melanoma progression

Singh, N., Khan, F. M., Bala, L., Vera, J., Olaf Wolkenhauer, A., Pützer, B. M., Logotheti, S., & Gupta, S. K. (2024) · Figshare · doi:10.6084/m9.figshare.26643976

Protein-protein interaction inhibitors in cancer

Hardcastle, I. R., Goujon-Ricci, J., & Thompson, W. I. (2026) · Elsevier eBooks · doi:10.1016/b978-0-443-29808-0.00067-4

Automated pharmacophore hypothesis generator for SILCS-Pharm: ph4gen

Nordquist, E. B., & MacKerell, A. D. (2026) · Journal of Computer-Aided Molecular Design · doi:10.1007/s10822-026-00957-5

BindingDB Entry 50045000: Design of chemically stable, potent, and efficacious MDM2 inhibitors that exploit the retro-mannich ring-opening-cyclization reaction mechanism in spiro-oxindoles.

BindingDB (2016) · UC San Diego · doi:10.7270/q2hh6mqk

BindingDB Entry 50047479: Discovery of Novel 3,3-Disubstituted Piperidines as Orally Bioavailable, Potent, and Efficacious HDM2-p53 Inhibitors.

BindingDB (2017) · UC San Diego · doi:10.7270/q2rj4mcv

BindingDB Entry 50018627: Evolution in non-peptide α-helix mimetics on the road to effective protein-protein interaction modulators.

BindingDB (2024) · UC San Diego · doi:10.7270/q2kp86dp

BindingDB Entry 50003153: The development of piperidinones as potent MDM2-P53 protein-protein interaction inhibitors for cancer therapy.

BindingDB (2020) · UC San Diego · doi:10.7270/q2sb48fv

BindingDB Entry 50045593: Discovery of AM-7209, a potent and selective 4-amidobenzoic acid inhibitor of the MDM2-p53 interaction.

BindingDB (2016) · UC San Diego · doi:10.7270/q2571dpw

BindingDB Entry 50016713: Phe19 modification of HDM2-p53 PPI inhibitors to alleviate CYP3A4 metabolism/mechanism-based inhibition liability.

BindingDB (2023) · UC San Diego · doi:10.7270/q2862mgn

BindingDB Entry 50044097: Core modification of substituted piperidines as novel inhibitors of HDM2-p53 protein-protein interaction.

BindingDB (2015) · UC San Diego · doi:10.7270/q2xd136f

BindingDB Entry 50044171: Selective and potent morpholinone inhibitors of the MDM2-p53 protein-protein interaction.

BindingDB (2015) · UC San Diego · doi:10.7270/q2c24xzz

BindingDB Entry 50044195: Novel inhibitors of the MDM2-p53 interaction featuring hydrogen bond acceptors as carboxylic acid isosteres.

BindingDB (2015) · UC San Diego · doi:10.7270/q2862j0j

BindingDB Entry 50044315: Tetra-substituted imidazoles as a new class of inhibitors of the p53-MDM2 interaction.

BindingDB (2015) · UC San Diego · doi:10.7270/q2rj4m1c

Structure-Based Design of Novel Inhibitors of the MDM2–p53 Interaction

Rew, Y., Sun, D., de Turiso, F. G.-L., Bartberger, M. D., Beck, H. P., Canon, J. R., Chen, A., Chow, D. T., Deignan, J., Fox, B. M., et al. (2012) · Journal of Medicinal Chemistry · doi:10.1021/jm300354j · Cited by 166 · see citing works

Selective and Potent Morpholinone Inhibitors of the MDM2–p53 Protein–Protein Interaction

González, A. Z., Eksterowicz, J. E., Bartberger, M. D., Beck, H. P., Canon, J. R., Chen, A., Chow, D. T., Duquette, J., Fox, B. M., Fu, J., et al. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm401767k · Cited by 84 · see citing works

Structure-Based Design of Potent and Orally Active Isoindolinone Inhibitors of MDM2-p53 Protein–Protein Interaction

Chessari, G., Hardcastle, I. R., Ahn, J. S., Anil, B., Anscombe, E., Bawn, R. H., Bevan, L., Blackburn, T. J., Buck, I. M., Cano, C., et al. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.0c02188 · Cited by 58 · see citing works

Discovery of dihydroisoquinolinone derivatives as novel inhibitors of the p53–MDM2 interaction with a distinct binding mode

Gessier, F., Kallen, J. A., Jacoby, E., Chêne, P., Stachyra, T., Ruetz, S., Jeay, S., Holzer, P., Masuya, K., & Furet, P. (2015) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2015.06.058 · Cited by 59 · see citing works

Novel Inhibitors of the MDM2-p53 Interaction Featuring Hydrogen Bond Acceptors as Carboxylic Acid Isosteres

González, A. Z., Li, Z., Beck, H. P., Canon, J. R., Chen, A., Chow, D. T., Duquette, J., Eksterowicz, J. E., Fox, B. M., Fu, J., et al. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm401911v · Cited by 58 · see citing works