The DOI matches its Crossref record; 51 of the 53 references it cites were found in a registry or an index.
Structural basis for high-affinity peptide inhibition of p53 interactions with MDM2 and MDMX
Open accessAbstract
The oncoproteins MDM2 and MDMX negatively regulate the activity and stability of the tumor suppressor protein p53—a cellular process initiated by MDM2 and/or MDMX binding to the N-terminal transactivation domain of p53. MDM2 and MDMX in many tumors confer p53 inactivation and tumor survival, and are important molecular targets for anticancer therapy. We screened a duodecimal peptide phage library against site-specifically biotinylated p53-binding domains of human MDM2 and MDMX chemically synthesized via native chemical ligation, and identified several peptide inhibitors of the p53-MDM2/MDMX interactions. The most potent inhibitor (TSFAEYWNLLSP), termed PMI, bound to MDM2 and MDMX at low nanomolar affinities—approximately 2 orders of magnitude stronger than the wild-type p53 peptide of the same length (ETFSDLWKLLPE). We solved the crystal structures of synthetic MDM2 and MDMX, both in complex with PMI, at 1.6 Å resolution. Comparative structural analysis identified an extensive, tightened intramolecular H-bonding network in bound PMI that contributed to its conformational stability, thus enhanced binding to the 2 oncogenic proteins. Importantly, the C-terminal residue Pro of PMI induced formation of a hydrophobic cleft in MDMX previously unseen in the structures of p53-bound MDM2 or MDMX. Our findings deciphered the structural basis for high-affinity peptide inhibition of p53 interactions with MDM2 and MDMX, shedding new light on structure-based rational design of different classes of p53 activators for potential therapeutic use.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“MDM2 amplification is frequently observed in several cancer types, especially in tumors that still retain wild-type p53.”
From Recent advances in targeting the “undruggable” proteins: from drug discovery to clinical trials (2023) · cites this paper as [216]
In the citing paper
“Therefore, disrupting the MDM2-p53 interaction, presents a potential approach for treating cancer by restoring the impaired function of p53.216,217”
From Recent advances in targeting the “undruggable” proteins: from drug discovery to clinical trials (2023) · cites this paper as [216]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Coot : model-building tools for molecular graphics
Emsley, P., & Cowtan, K. (2004) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444904019158 · Cited by 30,571
Kabsch, W., & Sander, C. (1983) · Biopolymers · doi:10.1002/bip.360221211 · Cited by 15,320
Refinement of Macromolecular Structures by the Maximum-Likelihood Method
Murshudov, G. N., Vagin, A. A., & Dodson, E. J. (1997) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444996012255 · Cited by 14,796
Vogelstein, B., Lane, D., & Levine, A. J. (2000) · Nature · doi:10.1038/35042675 · Cited by 6,607
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
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
Synthesis of Proteins by Native Chemical Ligation
Dawson, P. E., Muir, T. W., Clark‐Lewis, I., & Kent, S. B. H. (1994) · Science · doi:10.1126/science.7973629 · Cited by 4,190
How to measure and predict the molar absorption coefficient of a protein
Pace, C., Vajdos, F., Fee, L. R., Grimsley, G., & Gray, T. (1995) · Protein Science · doi:10.1002/pro.5560041120 · Cited by 3,924
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 · cited 1×
“Growing evidence supports that in unstressed cells MDM2 primarily controls p53 stability through ubiquitylation to target the tumor suppressor protein for constitutive degradation by the proteasome (13, 14), whereas MDMX mainly functions as a significant p53 transcriptional antagonist independently of MDM2 (15, 16).”
BackgroundLive or let die: the cell's response to p53
Vousden, K. H., & Lü, X. (2002) · Nature reviews. Cancer · doi:10.1038/nrc864 · Cited by 3,231
Cited by
Sorted by citations
Items 201–300 of 403
Avoiding drug resistance through extended drug target interfaces: a case for stapled peptides
Wei, S. J., Chee, S. M. Q., Yurlova, L., Lane, D. P., Verma, C. S., Brown, C. J., & Ghadessy, F. J. (2016) · Oncotarget · doi:10.18632/oncotarget.8572 · Cited by 16
Xu, D. D., Si, Y., & Meroueh, S. O. (2017) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.7b00181 · Cited by 16
Fortuna, P., Twarda‐Clapa, A., Skalniak, Ł., Ożga, K., Holak, T. A., & Berlicki, Ł. (2020) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2020.112814 · Cited by 16
Apamin as a Template for Structure‐Based Rational Design of Potent Peptide Activators of p53
Li, C., Pazgier, M., Liu, M., Lu, W., & Lu, W. (2009) · Angewandte Chemie · doi:10.1002/ange.200904550 · Cited by 16
Self-citationLi, H., Xie, H., Huang, Y., Bo, B., Zhu, X., Shu, Y., & Li, G. (2013) · Chemical Communications · doi:10.1039/c3cc45529g · Cited by 15
Markov State Models to Elucidate Ligand Binding Mechanism
Ge, Y., & Voelz, V. A. (2021) · Methods in molecular biology · doi:10.1007/978-1-0716-1209-5_14 · Cited by 14
Kapun, M., Pérez-Areales, F. J., Ashman, N., Rowling, P. J. E., Schober, T., Fowler, E., Itzhaki, L. S., & Spring, D. R. (2023) · RSC Chemical Biology · doi:10.1039/d3cb00176h · Cited by 15
MDMX in Cancer: A Partner of p53 and a p53-Independent Effector
Wu, L., Yan, Y., Huang, Q., & Zheng, D. (2024) · Biologics · doi:10.2147/btt.s436629 · Cited by 17
Guanidinium‐Stapled Helical Peptides for Targeting Protein‐Protein Interactions
Perdriau, C., Luton, A., Zimmeter, K., Neuville, M., Saragaglia, C., Peluso‐Iltis, C., Ősz, J., Kauffmann, B., Collie, G. W., Rochel, N., et al. (2024) · Angewandte Chemie International Edition · doi:10.1002/anie.202416348 · Cited by 15
Joshi, M. R., Yao, N., Myers, K. A., & Li, Z. (2013) · PLoS ONE · doi:10.1371/journal.pone.0080926 · Cited by 15
Pattern enrichment analysis for phage selection of stapled peptide ligands
Miki, T., Namii, K., Seko, K., Kakehi, S., Moro, G., & Mihara, H. (2022) · Chemical Science · doi:10.1039/d2sc04058a · Cited by 15
A mix-and-read drop-based in vitro two-hybrid method for screening high-affinity peptide binders
Cui, N., Zhang, H., Schneider, N., Tao, Y., Asahara, H., Sun, Z., Cai, Y., Koehler, S. A., de Greef, T. F. A., Abbaspourrad, A., et al. (2016) · Scientific Reports · doi:10.1038/srep22575 · Cited by 15
Subbanna, M. S., Winters, M. J., Örd, M., Davey, N. E., & Pryciak, P. M. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.108225 · Cited by 16
Bacterial Systems as a Precision Delivery Platform of Therapeutic Peptides for Cancer Therapy
Liu, J., Shen, G., & Yan, X. (2025) · Polymer science & technology. · doi:10.1021/polymscitech.4c00026 · Cited by 14
Disulfide trapping of protein complexes on the yeast surface
Lim, K. H., Madabhushi, S. R., Mann, J. K., Neelamegham, S., & Park, S. (2009) · Biotechnology and Bioengineering · doi:10.1002/bit.22651 · Cited by 14
Ge, Y., Zhang, S., Erdélyi, M., & Voelz, V. A. (2021) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.1c00029 · Cited by 13
MDM4 binds ligands via a mechanism in which disordered regions become structured
Sanchez, M. C., Renshaw, J., Davies, G. M., Barlow, P. N., & Vogtherr, M. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.05.058 · Cited by 14
FRETting about the affinity of bimolecular protein–protein interactions
Lin, T., Scott, B. L., Hoppe, A. D., & Chakravarty, S. (2018) · Protein Science · doi:10.1002/pro.3482 · Cited by 16
Synthesis by native chemical ligation and crystal structure of human CCL2
Grygiel, T. L. R., Teplyakov, A., Obmolova, G., Stowell, N. C., Holland, R., Nemeth, J. F., Pomerantz, S. C., Kruszynski, M., & Gilliland, G. L. (2010) · Biopolymers · doi:10.1002/bip.21390 · Cited by 15
Chakravarty, D., McElfresh, G., Kundrotas, P. J., & Vakser, I. A. (2020) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.25875 · Cited by 13
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
Liu, M., Chen, J., Li, H., Ma, Y., Xiao, Q., Ding, J., Li, J., & Chen, X. (2026) · Chemical Society Reviews · doi:10.1039/d5cs01504a · Cited by 15
Self-citationDurojaye, O. A., Yekeen, A. A., Idris, M. O., Okoro, N. O., Odiba, A. S., & Nwanguma, B. C. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.131840 · Cited by 15
Li, T., Jiang, S., Li, T., Xu, H., Zhang, X., Yan, R., Wu, X., Jin, Y., & Wang, Z. (2024) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.4c00393 · Cited by 13
Therapeutic peptides and their delivery using lipid-based nanoparticles
Yen, J.-H., Chang, C., Wu, T., Yang, C.-H., Hsu, H., & Liou, J.-W. (2025) · Tzu Chi Medical Journal · doi:10.4103/tcmj.tcmj_321_24 · Cited by 13
Carotti, A., Macchiarulo, A., Giacchè, N., & Pellicciari, R. (2009) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.22464 · Cited by 13
Chan, K. P., Chao, S., & Kah, J. C. Y. (2019) · Bioconjugate Chemistry · doi:10.1021/acs.bioconjchem.9b00032 · Cited by 11
Wu, L., He, Y., Hu, Y., Lu, H., Cao, Z. Y., Yi, X., & Wang, J. (2019) · The Analyst · doi:10.1039/c9an01121h · Cited by 13
Cheng, W.-Y., Chen, J., Liang, Z.-Q., Li, G., Yi, C., Wang, W., & Wang, K.-Y. (2012) · Computational and Theoretical Chemistry · doi:10.1016/j.comptc.2012.01.010 · Cited by 13
Kashima, D., Kageoka, M., Kimura, Y., Horikawa, M., Miura, M., Nakakido, M., Tsumoto, K., Nagamune, T., & Kawahara, M. (2021) · ACS Synthetic Biology · doi:10.1021/acssynbio.0c00483 · Cited by 12
Zhang, X., Li, T., Zhao, L., Xu, H., Chang, Y., Jin, Y., & Wang, Z. (2023) · Journal of Molecular Structure · doi:10.1016/j.molstruc.2023.134903 · Cited by 12
Dezi, C., Carotti, A., Magnani, M., Baroni, M., Padova, A., Cruciani, G., Macchiarulo, A., & Pellicciari, R. (2010) · Journal of Chemical Information and Modeling · doi:10.1021/ci100113p · Cited by 12
Analysis and Design of Piezoelectric Braille Display
Smithmaitrie, P. (2009) · InTech eBooks · doi:10.5772/7391 · Cited by 12
Iera, J. A., Jenkins, L. M. M., Kajiyama, H., Kopp, J. B., & Appella, D. H. (2010) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2010.09.054 · Cited by 12
Yoon, H. K., & Yoo, T. H. (2013) · The Analyst · doi:10.1039/c3an01336g · Cited by 12
Topoisomeric Membrane-Active Peptides: A Review of the Last Two Decades
Carrera-Aubesart, A., Gallo, M., Defaus, S., Todorovski, T., & Andreu, D. (2023) · Pharmaceutics · doi:10.3390/pharmaceutics15102451 · Cited by 11
Protein grafting of p53TAD onto a leucine zipper scaffold generates a potent HDM dual inhibitor
Lee, J., Kang, E., Lee, J., Kim, J., Lee, K. H., Han, J., Kang, H. Y., Ahn, S.-S., Oh, Y., Shin, D., et al. (2014) · Nature Communications · doi:10.1038/ncomms4814 · Cited by 13
Structure-activity studies of Mdm2/Mdm4-binding stapled peptides comprising non-natural amino acids
Chee, S. M. Q., Wongsantichon, J., Siau, J. W., Thean, D., Ferrer, F. J., Robinson, R. C., Lane, D. P., Brown, C. J., & Ghadessy, F. J. (2017) · PLoS ONE · doi:10.1371/journal.pone.0189379 · Cited by 11
Synthetic 10FN3-based mono- and bivalent inhibitors of MDM2/X function
Lau, S. Y., Siau, J. W., Sobota, R. M., Wang, C. I., Zhong, P., Lane, D. P., & Ghadessy, F. J. (2018) · Protein Engineering Design and Selection · doi:10.1093/protein/gzy018 · Cited by 11
Torner, J. M., Yang, Y., Rooklin, D. W., Zhang, Y., & Arora, P. S. (2021) · ACS Chemical Biology · doi:10.1021/acschembio.1c00418 · Cited by 11
Shi, S., Zhang, S., & Zhang, Q. (2015) · PLoS ONE · doi:10.1371/journal.pone.0141409 · Cited by 10
Identification of a Structural Determinant for Selective Targeting of HDMX
Ben‐Nun, Y., Seo, H., Harvey, E. P., Hauseman, Z. J., Wales, T. E., Newman, C. E., Cathcart, A. M., Engen, J. R., Dhe‐Paganon, S., & Walensky, L. D. (2020) · Structure · doi:10.1016/j.str.2020.04.011 · Cited by 10
Nuclear delivery of dual anti-cancer drugs by molecular self-assembly
Wu, J., Ding, W., Han, G., You, W., Gao, W., Shen, H., Tang, J., Tang, Q., & Wang, X. (2020) · Biomaterials Science · doi:10.1039/d0bm00971g · Cited by 10
Li, H., Chen, X., Wu, M., Song, P., & Zhao, X. (2021) · Chinese Chemical Letters · doi:10.1016/j.cclet.2021.08.130 · Cited by 11
Affinity Selection from Synthetic Peptide Libraries Enabled by De Novo MS/MS Sequencing
Koh, L. Q., Lim, Y. W., & Gates, Z. P. (2022) · International Journal of Peptide Research and Therapeutics · doi:10.1007/s10989-022-10370-9 · Cited by 11
Rapid screening of protein–protein interaction inhibitors using the protease exclusion assay
Nirantar, S., Li, X. O., Siau, J. W., & Ghadessy, F. J. (2014) · Biosensors and Bioelectronics · doi:10.1016/j.bios.2013.12.060 · Cited by 10
D ‐Peptide‐Based Drug Discovery Aided by Chemical Protein Synthesis
Zhao, L., & Lu, W. (2011) · Israel Journal of Chemistry · doi:10.1002/ijch.201100085 · Cited by 10
Self-citationAnananuchatkul, T., Tsutsumi, H., Miki, T., & Mihara, H. (2020) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2020.127605 · Cited by 9
Bridged Analogues for p53-Dependent Cancer Therapy Obtained by S-Alkylation
Micewicz, E. D., Sharma, S. K., Waring, A. J., Luong, H. T., McBride, W. H., & Ruchala, P. P. (2015) · International Journal of Peptide Research and Therapeutics · doi:10.1007/s10989-015-9487-3 · Cited by 11
-Amino acid mutation of PMI as potent dual peptide inhibitors of p53-MDM2/MDMX interactions
Li, X., Liu, C., Chen, S., Hu, H., Su, J., & Zou, Y. (2017) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2017.09.014 · Cited by 10
Neuville, M., Bourgeais, M., Li, B., Varajao, L., Hallé, F., Goudreau, S. R., Thinon, E., Pasco, M., Khatib, A., & Guichard, G. (2024) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.4c01762 · Cited by 10
Han, J. Y., Choi, T. S., Heo, C. E., Son, M. K., & Kim, H. I. (2019) · Mass Spectrometry Reviews · doi:10.1002/mas.21596 · Cited by 9
Shin, J., Ha, J., & Chi, S. (2013) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2013.12.054 · Cited by 9
Designing dual inhibitors of Mdm2/MdmX: Unexpected coupling of water with gatekeeper Y100/99
Lee, X. A., Verma, C. S., & Sim, A. Y. L. (2017) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.25310 · Cited by 9
Functional profiling of p53-binding sites in Hdm2 and Hdmx using a genetic selection system
Datta, S., Bucks, M. E., Koley, D., Lim, P. X., & Savinov, S. N. (2010) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2010.06.053 · Cited by 9
Rapid alchemical free energy calculation employing a generalized born implicit solvent model.
Ostermeir, K., & Zacharias, M. (2015) · Journal of Physical Chemistry B · doi:10.1021/jp506367y · Cited by 8
Chen, S., Li, X., Yuan, W., Zou, Y., Guo, Z., Chai, Y., & Lu, W. (2017) · RSC Advances · doi:10.1039/c7ra00473g · Cited by 9
Self-citationGarton, M., Corbi‐Verge, C., Hu, Y., Nim, S., Tarasova, N. I., Sherborne, B. S., & Kim, P. M. (2018) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.25644 · Cited by 9
Fan, S., Li, J., Zhuang, J., Zhou, Q., Mai, Y., Lin, B., Wang, M., & Wu, C. (2024) · Journal of the American Chemical Society · doi:10.1021/jacs.4c12808 · Cited by 8
Self-citationChoudhury, A. R., Gaikwad, V., Maity, A., & Chakrabarti, R. (2025) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.26793 · Cited by 9
Engineering Optogenetic Control of Endogenous p53 Protein Levels
Wehler, P., & Ventura, B. D. (2019) · Applied Sciences · doi:10.3390/app9102095 · Cited by 8
A Left‐Handed Solution to Peptide Inhibition of the p53–MDM2 Interaction
Liu, M., Pazgier, M., Li, C., Yuan, W., Li, C., & Lu, W. (2010) · Angewandte Chemie · doi:10.1002/ange.201000329 · Cited by 10
Self-citationZhao, L., Li, T., Xu, H., Zhang, X., Lin, H., Liu, N., Jin, Y., & Wang, Z. (2023) · New Journal of Chemistry · doi:10.1039/d3nj01202f · Cited by 9
Benzyl stapled modification and anticancer activity of antimicrobial peptide A4K14-Citropin 1.1
Shen, H., Zhang, N., Kong, X., Wang, N., Hu, H., Cong, W., & Liu, C. (2023) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2023.129499 · Cited by 8
Shi, S., Zhang, S., & Zhang, Q. (2014) · Computational and Theoretical Chemistry · doi:10.1016/j.comptc.2014.07.002 · Cited by 8
Jalali‐Yazdi, F., Corbin, J. M., Takahashi, T. T., & Roberts, R. W. (2014) · Analytical Chemistry · doi:10.1021/ac500084d · Cited by 8
Huang, A., Zhou, L. Y., Zhang, D., Yao, J., & Zhang, Y. (2016) · Journal of Molecular Graphics and Modelling · doi:10.1016/j.jmgm.2016.09.007 · Cited by 8
Chen, R., Zhou, J., Qin, L., Chen, Y., Huang, Y., Liu, H., & Su, Z. (2017) · Biochemistry · doi:10.1021/acs.biochem.7b00085 · Cited by 8
Wang, Y.-T., & Cheng, T. (2020) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2020.1773317 · Cited by 8
Lee, M.-K., & Lim, Y. (2014) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2014.05.041 · Cited by 7
Mechanistic insights into RNase L through use of an MDMX-derived multi-functional protein domain
Garvie, C. W., Vasanthavada, K., & Xiang, Q. (2013) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2013.04.010 · Cited by 7
Structure and dynamics of the retro-form of the bacteriophage T5 endolysin
Kutyshenko, V. P., Mikoulinskaia, G. V., Molochkov, N. V., Prokhorov, D. A., Таран, С. А., & Uversky, V. N. (2016) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2016.06.018 · Cited by 7
Diller, D., Swanson, J., Bayden, A. S., Brown, C. J., Thean, D., Lane, D. P., Partridge, A. W., Sawyer, T. K., & Audie, J. (2019) · Molecules · doi:10.3390/molecules24244586 · Cited by 7
Construction of Peptide Library in Mammalian Cells by dsDNA-Based Strategy
Su, W., Wang, Y., Zou, S., Zhao, Y., Li, Y., Zhang, C., Guo, X., & Li, S. (2022) · ACS Omega · doi:10.1021/acsomega.2c06402 · Cited by 7
Identification of Small Molecules Affecting p53-MDM2/MDMX Interaction by Fluorescence Polarization
Zhang, Q., & Lu, H. (2012) · Methods in molecular biology · doi:10.1007/978-1-62703-236-0_8 · Cited by 7
Jetzt wird es ernst: strukturbasiertes Design von Mdm2/Mdmx‐p53‐Inhibitoren
Popowicz, G. M., Dömling, A. S. S., & Holak, T. A. (2011) · Angewandte Chemie · doi:10.1002/ange.201003863 · Cited by 7
Natural Functions and Structure–Activity Relationships of Cyclotides
Oguis, G. K., Kan, M., & Craik, D. J. (2015) · Advances in botanical research · doi:10.1016/bs.abr.2015.10.001 · Cited by 7
Macrocyclization and labeling of helix–loop–helix peptide with intramolecular bis‐thioether linkage
Nishihara, T., Kitada, H., Fujiwara, D., & Fujii, I. (2016) · Biopolymers · doi:10.1002/bip.22826 · Cited by 8
Li, Y., Yu, X., Lou, Y., & Wang, T. (2016) · Australian Journal of Chemistry · doi:10.1071/ch16096 · Cited by 7
Kashima, D., Kawade, R., Nagamune, T., & Kawahara, M. (2017) · Analytical Chemistry · doi:10.1021/acs.analchem.6b04063 · Cited by 7
Sana, B., Chee, S. M. Q., Wongsantichon, J., Raghavan, S. S., Robinson, R. C., & Ghadessy, F. J. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.007141 · Cited by 7
Fujiwara, D., Kitada, H., Oguri, M., Nishihara, T., Michigami, M., Shiraishi, K., Yuba, E., Nakase, I., Im, H., Cho, S., et al. (2016) · Angewandte Chemie · doi:10.1002/ange.201603230 · Cited by 7
Inhibition of protein-protein interactions using biodegradable depsipeptide nanoassemblies
Choi, S.-H., Hwang, H.-S., Han, S., Eom, H., Choi, J. S., Han, S., Lee, D., Lee, S. Y., Koo, H., Kwon, H. J., et al. (2023) · Journal of Controlled Release · doi:10.1016/j.jconrel.2023.12.028 · Cited by 6
Chen, J., Wang, J., Pang, L., & Zhu, W. (2018) · Chemical Biology & Drug Design · doi:10.1111/cbdd.13345 · Cited by 7
Shi, S., Sui, K., Liu, W., Lei, Y., Zhang, S., & Zhang, Q. (2019) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2019.1695671 · Cited by 6
Vaas, S., Zimmermann, M. O., Klett, T., & Boeckler, F. M. (2023) · Drug Design Development and Therapy · doi:10.2147/dddt.s406703 · Cited by 6
Chemical Strategies towards the Development of Effective Anticancer Peptides
Li, C., & Jin, K. (2023) · Current Medicinal Chemistry · doi:10.2174/0929867330666230426111157 · Cited by 6
Self-citationQin, L., Liu, H., Chen, R., Zhou, J., Cheng, X., Chen, Y., Huang, Y., & Su, Z. (2017) · Biochemistry · doi:10.1021/acs.biochem.7b00903 · Cited by 7
Molecular and Biochemical Techniques for Deciphering p53-MDM2 Regulatory Mechanisms
Karakostis, K., López, I., Peña-Balderas, A. M., Fåhareus, R., & Olivares‐Illana, V. (2020) · Biomolecules · doi:10.3390/biom11010036 · Cited by 7
Editorial of Special Column “Novel Peptides and Peptidomimetics in Drug Discovery”
Cai, J., & Wei, L. (2021) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2021.08.023 · Cited by 6
Chen, Z., Lim, Y. W., Neo, J. Y., Chan, R. S. T., Koh, L. Q., Yuen, T. Y., Lim, Y. H., Johannes, C. W., & Gates, Z. P. (2023) · Analytical Chemistry · doi:10.1021/acs.analchem.3c01742 · Cited by 6
Zhang, X., Li, T., Xu, H., Wang, Q., Wu, X., Yan, R., Jin, Y., & Wang, Z. (2024) · Journal of Molecular Liquids · doi:10.1016/j.molliq.2024.125682 · Cited by 5
Zhang, X., Zhou, C., Yang, Y., Liu, H., Wang, S., Ding, X., & Hu, W. (2021) · ChemMedChem · doi:10.1002/cmdc.202100517 · Cited by 5
Virtual Screening for DNA Repair Inhibitors
Barakat, K., & Tuszyński, J. A. (2011) · InTech eBooks · doi:10.5772/24436 · Cited by 5
Protein Chemical Synthesis in Drug Discovery
Liu, F., & Mayer, J. P. (2014) · Topics in current chemistry · doi:10.1007/128_2014_598 · Cited by 6
In SituHybridization of Superparamagnetic Iron-Biomolecule Nanoparticles
Moghimi, N., Donkor, A. D., Mohapatra, M., Thomas, J. P., Su, Z., Tang, X. S., & Leung, K. T. (2014) · Journal of the American Chemical Society · doi:10.1021/ja505242c · Cited by 5
Functional Interrogation of the N-Terminal Lid of MDMX in p53 Binding via Native Chemical Ligation
Chen, X., & Lu, W. (2016) · Chemical and Pharmaceutical Bulletin · doi:10.1248/cpb.c15-00975 · Cited by 5
Self-citationSi, Y., Xu, D. D., Bum‐Erdene, K., Ghozayel, M. K., Yang, B., Clemons, P. A., & Meroueh, S. O. (2018) · ChemMedChem · doi:10.1002/cmdc.201800537 · Cited by 5
A dimethylbromobenzene-cysteine stapled peptide dual inhibitor of the p53-MDM2/MDMX interactions
Jiang, W., Jin, L., Liu, M., Hou, P., & He, W. (2019) · Hepatoma Research · doi:10.20517/2394-5079.2018.97 · Cited by 5
Self-citationDiscovery of SCY45, a Natural Small‐Molecule MDM2‐p53 Interaction Inhibitor
Gong, H., An, J., Dong, Q., Li, J., Yang, W., Sun, W., Su, Z., & Zhang, S. (2019) · Chemistry & Biodiversity · doi:10.1002/cbdv.201900081 · Cited by 5
Self-citation
Metadata
- Authors
- Pazgier, M., Liu, M., Zou, G., Yuan, W., Li, C., Li, C., Li, J., Monbo, J., Zella, D., Tarasov, S. G., & Lu, W.
- Affiliations
- University of Maryland, Baltimore (US)
- National Cancer Institute (US)
- ORCID
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2009-03-24
- Volume
- 106
- Issue
- 12
- Pages
- 4665-4670
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC2660734
- OpenAlex
- W2076060796
- Cited by
- 391
- References
- 53
- Citations by year
- 2026: 10 · 2025: 28 · 2024: 27 · 2023: 23 · 2022: 18 · 2021: 29 · 2020: 25 · 2019: 24 · 2018: 18 · 2017: 31 · 2016: 18 · 2015: 20 · 2014: 24 · 2013: 21 · 2012: 19
- FWCI
- 12.67
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (AI056264)
- National Institute of Allergy and Infectious Diseases (AI 061482, AI 056264, R21AI056264, R01AI061482)
- Topics
- Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Physical Sciences › Chemistry › Organic Chemistry › Chemical Synthesis and Analysis
- Keywords
- p53, MDM2, MDMX, peptide inhibitors, transactivation domain, crystal structure, hydrogen bond network, hydrophobic cleft, p53 activators, anticancer drug design, phage display peptide library, native chemical ligation
- MeSH terms
- Amino Acid Sequence, Humans, Models, Molecular, Molecular Sequence Data, Nuclear Proteins, Oligopeptides, Peptides, Protein Binding, Proto-Oncogene Proteins, Structure-Activity Relationship, Tumor Suppressor Protein p53, Protein Structure, Secondary, Cell Cycle Proteins, Peptide Library, Proto-Oncogene Proteins c-mdm2
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review