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

p53, the cellular gatekeeper for growth and division

Levine, A. J. (1997) · Cell · doi:10.1016/s0092-8674(00)81871-1 · Cited by 7,693

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

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

The mdm-2 oncogene product forms a complex with the p53 protein and inhibits p53-mediated transactivation

Momand, J., Zambetti, G. P., Olson, D. C., George, D., & Levine, A. J. (1992) · Cell · doi:10.1016/0092-8674(92)90644-r · Cited by 3,113

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

The p53-mdm-2 autoregulatory feedback loop.

Wu, X., Bayle, J. H., Olson, D., & Levine, A. J. (1993) · Genes & Development · doi:10.1101/gad.7.7a.1126 · Cited by 1,801

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 1,474

Rescue of early embryonic lethality in mdm2-deficient mice by deletion of p53

de Oca Luna, R. M., Wagner, D. S., & Lozano, G. (1995) · Nature · doi:10.1038/378203a0 · Cited by 1,420

mdm2 expression is induced by wild type p53 activity.

Barak, Y., Juven, T., Haffner, R., & Oren, M. (1993) · The EMBO Journal · doi:10.1002/j.1460-2075.1993.tb05678.x · Cited by 1,290

Rescue of embryonic lethality in Mdm2-deficient mice by absence of p53

Jones, S. N., Roe, A. E., Donehower, L. A., & Bradley, A. (1995) · Nature · doi:10.1038/378206a0 · Cited by 1,280

Key targets for the execution of radiation-induced tumor cell apoptosis: the role of p53 and caspases

Pruschy, M. N., Rocha, S., Zaugg, K., Broggini‐Tenzer, A., Hess, C., Fisher, D. E., Glanzmann, C., & Bodis, S. B. (2001) · International Journal of Radiation Oncology*Biology*Physics · doi:10.1016/s0360-3016(00)01480-2 · Cited by 42

Modulation of p53 binding to MDM2: computational studies reveal important roles of Tyr100

Dastidar, S. G., Lane, D. P., & Verma, C. S. (2009) · BMC Bioinformatics · doi:10.1186/1471-2105-10-s15-s6 · Cited by 40

Exploiting the p53 Pathway for the Diagnosis and Therapy of Human CancerPreprint

Lane, D. P. (2005) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.2005.70.049 · Cited by 40

Targeting Protein–Protein Interfaces with Peptides: The Contribution of Chemical Combinatorial Peptide Library Approaches

Monti, A., Vitagliano, L., Caporale, A., Ruvo, M., & Doti, N. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24097842 · Cited by 43

The Tumor Suppressor Gene TP53: Implications for Cancer Management and Therapy

Seemann, S., Maurici, D., Olivier, M., de Fromentel, C. C., & Hainaut, P. L. (2004) · Critical Reviews in Clinical Laboratory Sciences · doi:10.1080/10408360490504952 · Cited by 39

MDM2 overexpression generates a skin phenotype in both wild type and p53 null mice

Alkhalaf, M., Ganguli, G., Messaddeq, N., LeMeur, M., & Wasylyk, B. (1999) · Oncogene · doi:10.1038/sj.onc.1202448 · Cited by 39

Manipulation of the tumor suppressor p53 for potentiating cancer therapy

Haupt, S. M., & Haupt, Y. (2004) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2004.04.003 · Cited by 38

Dephosphorylation of p53 at Ser20 after cellular exposure to low levels of non-ionizing radiation

Craig, A. L., Blaydes, J. P., Burch, L. R., Thompson, A. M., & Hupp, T. R. (1999) · Oncogene · doi:10.1038/sj.onc.1203085 · Cited by 37

p53 from pathway to therapy

Lane, D. P. (2004) · Carcinogenesis · doi:10.1093/carcin/bgh186 · Cited by 37

Targeting Mouse Double Minute 2: Current Concepts in DNA Damage Repair and Therapeutic Approaches in Cancer

Li, W., Peng, X., Lang, J., & Xu, C. S. (2020) · Frontiers in Pharmacology · doi:10.3389/fphar.2020.00631 · Cited by 36

The p53-Mdm2 Loop: A Critical Juncture of Stress Response

Levav-Cohen, Y., Goldberg, Z., Tan, K. H., Alsheich-Bartok, O., Zuckerman, V., Haupt, S., & Haupt, Y. (2014) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-94-017-9211-0_9 · Cited by 38

Oxidative Stress Induced by MnSOD-p53 Interaction: Pro- or Anti-Tumorigenic?

Robbins, D. F., & Zhao, Y. (2011) · Journal of Signal Transduction · doi:10.1155/2012/101465 · Cited by 34

A Fluorescence Polarization Assay for the Identification of Inhibitors of the p53–DM2 Protein–Protein Interaction

Knight, S. M. G., Umezawa, N., Lee, H., Gellman, S. H., & Kay, B. K. (2002) · Analytical Biochemistry · doi:10.1006/abio.2001.5468 · Cited by 35

The contribution of the RING finger domain of MDM2 to cell cycle progression

Argentini, M., Barboule, N., & Wasylyk, B. (2000) · Oncogene · doi:10.1038/sj.onc.1203737 · Cited by 35

Peptides for Cancer Therapy: a drug-development Opportunity and a drug-delivery Challenge

Bidwell, G. L. (2012) · Therapeutic Delivery · doi:10.4155/tde.12.37 · Cited by 34

p53mRNA and p53 Protein Structures Have Evolved Independently to Interact with MDM2

Karakostis, K., Ponnuswamy, A., Fusée, L. T. S., Bailly, X., Laguerre, L., Worrall, E. G., Vojtesek, B., Nylander, K., & Fåhræus, R. (2016) · Molecular Biology and Evolution · doi:10.1093/molbev/msw012 · Cited by 35

The MDM2 ligand Nutlin-3 differentially alters expression of the immune blockade receptors PD-L1 and CD276

Li, R., Zatloukalová, P., Müller, P., Gil-Mir, M., Kote, S., Wilkinson, S., Kemp, A. J., Hernychová, L., Wang, Y., Ball, K. L., et al. (2020) · Cellular & Molecular Biology Letters · doi:10.1186/s11658-020-00233-w · Cited by 34

mRNA Display Selection of an Optimized MDM2-Binding Peptide That Potently Inhibits MDM2-p53 Interaction

Shiheido, H., Takashima, H., Doi, N., & Yanagawa, H. (2011) · PLoS ONE · doi:10.1371/journal.pone.0017898 · Cited by 33

Exploiting the p53 pathway for cancer diagnosis and therapy.

Lane, D. P. (1999) · PubMed · Cited by 34

Intrinsically Disordered Proteins

Uversky, V. N. (2020) · Wiley eBooks · doi:10.1002/9781118681121.ch25 · Cited by 33

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 34

Protein–protein interactions in transcription: A fertile ground for helix mimetics

Guarracino, D. A., Bullock, B. N., & Arora, P. S. (2010) · Biopolymers · doi:10.1002/bip.21546 · Cited by 32

Baculovirus p33 Binds Human p53 and Enhances p53-Mediated Apoptosis

Prikhod’ko, G. G., Wang, Y., Freulich, E., Prives, C. L., & Miller, L. K. (1999) · Journal of Virology · doi:10.1128/jvi.73.2.1227-1234.1999 · Cited by 31

Suppression of UV-induced apoptosis by the human DNA repair protein XPG

Clément, V., Dunand-Sauthier, I., & Clarkson, S. G. (2005) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401764 · Cited by 31

p53–Mdm2 inhibitors: patent review (2009 – 2010)

Kamal, Ä., Mohammed, A. A., & Shaik, T. B. (2012) · Expert Opinion on Therapeutic Patents · doi:10.1517/13543776.2012.656593 · Cited by 30

Chemical states of the N-terminal “lid” of MDM2 regulate p53 binding: Simulations reveal complexities of modulation

Dastidar, S. G., Raghunathan, D., Nicholson, J., Hupp, T. R., Lane, D. P., & Verma, C. S. (2011) · Cell Cycle · doi:10.4161/cc.10.1.14345 · Cited by 30

Pharmacoproteomic Analysis of a Novel Cell-permeable Peptide Inhibitor of Tumor-induced Angiogenesis

Bang, J., Kim, E., Kang, D., Chang, S., Han, M., Baek, K., & Kang, I. (2011) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m110.005264 · Cited by 29

Identification of a disruptor of the MDM2-p53 protein–protein interaction facilitated by high-throughput in silico docking

Lawrence, H. R., Li, Z., Yip, M. L. R., Sung, S., Lawrence, N. J., McLaughlin, M. L., McManus, G. J., Zaworotko, M. J., Sebti, S. M., Chen, J., et al. (2009) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2009.04.124 · Cited by 29

The Effects of Phosphomimetic Lid Mutation on the Thermostability of the N-terminal Domain of MDM2

Worrall, E. G., Worrall, L. J., Blackburn, E. A., Walkinshaw, M. D., & Hupp, T. R. (2010) · Journal of Molecular Biology · doi:10.1016/j.jmb.2010.03.023 · Cited by 28

The P53 Pathway: Targets for the Development of Novel Cancer Therapeutics

Wang, S., & El‐Deiry, W. S. (2006) · Kluwer Academic Publishers eBooks · doi:10.1007/1-4020-7847-1_9 · Cited by 28

Effect of an hdm-2 antagonist peptide inhibitor on cell cycle progression in p53-deficient H1299 human lung carcinoma cells

VanderBorght, A., Valckx, A., Dun, J. V., Grand‐Perret, T., Schepper, S. D., Vialard, J., Janicot, M., & Arts, J. (2006) · Oncogene · doi:10.1038/sj.onc.1209667 · Cited by 27

UV but not gamma irradiation accelerates p53-induced apoptosis of teratocarcinoma cells by repressing MDM2 transcription.

Zeng, X., Keller, D., Wu, L., & Lu, H. (2000) · PubMed · Cited by 26

C-Terminal Substitution of MDM2 Interacting Peptides Modulates Binding Affinity by Distinctive Mechanisms

Brown, C. J., Dastidar, S. G., Quah, S. T., Lim, A., Chia, B. C. S., & Verma, C. S. (2011) · PLoS ONE · doi:10.1371/journal.pone.0024122 · Cited by 26

Transcription factor TAFII250 promotes Mdm2-dependent turnover of p53

Allende-Vega, N., Saville, M. K., & Meek, D. W. (2007) · Oncogene · doi:10.1038/sj.onc.1210209 · Cited by 26

A systems wide mass spectrometric based linear motif screen to identify dominant in-vivo interacting proteins for the ubiquitin ligase MDM2

Nicholson, J., Scherl, A., Way, L., Blackburn, E. A., Walkinshaw, M. D., Ball, K. L., & Hupp, T. R. (2014) · Cellular Signalling · doi:10.1016/j.cellsig.2014.02.011 · Cited by 25

Rational Design and Biophysical Characterization of Thioredoxin-Based Aptamers: Insights into Peptide Grafting

Brown, C. J., Dastidar, S. G., See, H. Y., Coomber, D., Ortiz-Lombardı́a, M., Verma, C. S., & Lane, D. P. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.10.069 · Cited by 25

Molecular Evolution of the Thermosensitive PAb1620 Epitope of Human p53 by DNA Shuffling

Xirodimas, D. P., & Lane, D. P. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.39.28042 · Cited by 25

E2F activity is essential for survival of Myc-overexpressing human cancer cells

Santoni‐Rugiu, E., Duro, D., Farkas, T., Mathiasen, I. S., Jäättelä, M., Bártek, J., & Lukas, J. (2002) · Oncogene · doi:10.1038/sj.onc.1205828 · Cited by 24

Mdm2 Inhibits the Apoptotic Function of p53 Mainly by Targeting It for Degradation

Yap, D., Hsieh, J.-K., & Lü, X. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m004359200 · Cited by 24

Cytokinesis Failure Leading to Chromosome Instability in v-Src-Induced Oncogenesis

Nakayama, Y., Soeda, S., Ikeuchi, M., Kakae, K., & Yamaguchi, N. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18040811 · Cited by 24

Apoptosis of tumoral and nontumoral lymphoid cells is induced by both mdm2 and p53 antisense oligodeoxynucleotides

Métay, C., Mir, L. M., Carlier, K., Lécluse, Y., Tétaud, C., Mishal, Z., & Wiels, J. (2001) · Blood · doi:10.1182/blood.v97.4.1043 · Cited by 23

Use of p53 for therapy of human cancer

Almazov, V. P., Кочетков, Д. В., & Chumakov, P. M. (2007) · Molecular Biology · doi:10.1134/s0026893307060015 · Cited by 22

Solid-Phase Synthesis of Chlorofusin Analogues

Woon, E. C. Y., Arcieri, M., Wilderspin, A. F., Malkinson, J. P., & Searcey, M. (2007) · The Journal of Organic Chemistry · doi:10.1021/jo070450a · Cited by 22

c-abl is involved in the association of p53 and trk A

Brown, A., Browes, C., Mitchell, M., & Montano, X. (2000) · Oncogene · doi:10.1038/sj.onc.1203619 · Cited by 21

Discovery of novel dihydroimidazothiazole derivatives as p53–MDM2 protein–protein interaction inhibitors: Synthesis, biological evaluation and structure–activity relationships

Miyazaki, M., Kawato, H. C., Naito, H., Ikeda, M., Miyazaki, M., Kitagawa, M., Seki, T., Fukutake, S., Aonuma, M., & Soga, T. (2012) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2012.08.086 · Cited by 20

Pivotal Role of an Aliphatic Side Chain in the Development of an HDM2 Inhibitor

Ma, Y., Lahue, B. R., Gibeau, C. R., Shipps, G. W., Bogen, S. L., Wang, Y., Guo, Z., & Guzi, T. J. (2014) · ACS Medicinal Chemistry Letters · doi:10.1021/ml500019s · Cited by 20

Recent advances in targeting regulators of apoptosis in cancer cells for therapeutic gain

Taylor, K. R., Micha, D., Ranson, M., & Dive, C. (2006) · Expert Opinion on Investigational Drugs · doi:10.1517/13543784.15.6.669 · Cited by 20

Molecular biomarkers in HNSCC: prognostic and therapeutic implications

Hussein, M. R., & Cullen, K. J. (2001) · Expert Review of Anticancer Therapy · doi:10.1586/14737140.1.1.116 · Cited by 20

Molecular neuro-oncology and the development of targeted therapeutic strategies for brain tumors Part 4: p53 signaling pathway

Newton, H. B. (2005) · Expert Review of Anticancer Therapy · doi:10.1586/14737140.5.1.177 · Cited by 20

Regulation of p53-dependent transcription

Jõers, A. (2004) · DSpace repository (University of Tartu) · Cited by 20

Characterizing the conformational landscape of MDM2-binding p53 peptides using Molecular Dynamics simulations

Yadahalli, S., Li, J., Lane, D. P., Gosavi, S., & Verma, C. S. (2017) · Scientific Reports · doi:10.1038/s41598-017-15930-4 · Cited by 19

[The use of p53 as a tool for human cancer therapy].

Almazov, V. P., Кочетков, Д. В., & Chumakov, P. M. (2007) · PubMed · Cited by 20

Altered expression ofBRCA1,BRCA2, and a newly identifiedBRCA2 exon 12 deletion variant in malignant human ovarian, prostate, and breast cancer cell lines

Rauh‐Adelmann, C., Lau, K., Sabeti, N., Long, J. P., Mok, S. C., & Ho, S. (2000) · Molecular Carcinogenesis · doi:10.1002/1098-2744(200008)28:4 · Cited by 48

Chemical Genetics Approach to Identify Peptide Ligands that Selectively Stimulate DAPK-1 Kinase Activity

Fraser, J. A., & Hupp, T. R. (2007) · Biochemistry · doi:10.1021/bi061562j · Cited by 18

The role of alpha-helical structure in p53 peptides as a determinant for their mechanism of cell death: necrosis versus apoptosis

ROSAL, R., Brandt‐Rauf, P. W., Pincus, M. R., WANG, H., Mao, Y., Li, Y., & Fine, R. L. (2005) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2004.10.008 · Cited by 18

Substituted piperidines as HDM2 inhibitors

Ma, Y., Lahue, B. R., Shipps, G. W., Brookes, J., & Wang, Y. (2014) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2014.01.026 · Cited by 17

Forces mediating protein–protein interactions: a computational study of p53 “approaching” MDM2

Dastidar, S. G., Madhumalar, A., Fuentes, G., Lane, D. P., & Verma, C. S. (2009) · Theoretical Chemistry Accounts · doi:10.1007/s00214-009-0682-1 · Cited by 17

Why is F19Ap53 unable to bind MDM2? Simulations suggest crack propagation modulates binding

Dastidar, S. G., Lane, D. P., & Verma, C. S. (2012) · Cell Cycle · doi:10.4161/cc.20333 · Cited by 17

Recognition Dynamics of p53 and MDM2: Implications for Peptide Design

ElSawy, K. M., Lane, D. P., Verma, C. S., & Caves, L. S. D. (2015) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.5b11162 · Cited by 17

Computational Investigation on the p53–MDM2 Interaction Using the Potential of Mean Force Study

Das, P., & Mattaparthi, V. S. K. (2020) · ACS Omega · doi:10.1021/acsomega.9b03372 · Cited by 18

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

Delivery to, and Reactivation of, the p53 Pathway in Cancer Cells Using a Grafted Cyclotide Conjugated with a Cell-Penetrating Peptide

Philippe, G. J.-B., Huang, Y., Mittermeier, A., Brown, C. J., Kaas, Q., Ramlan, S. R., Wang, C. K. L., Lane, D. P., Loewer, A., Henriques, S. T., et al. (2024) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.3c01682 · Cited by 17

Controlled Access of p53 to the Nucleus Regulates Its Proteasomal Degradation by MDM2

Davis, J. R., Mossalam, M., & Lim, C. S. (2013) · Molecular Pharmaceutics · doi:10.1021/mp300543t · 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

Tumor-specific induction of apoptosis by a p53-reactivating compound

Hedström, E., Issaeva, N., Enge, M., & Selivanova, G. (2008) · Experimental Cell Research · doi:10.1016/j.yexcr.2008.11.009 · Cited by 15

Constrained Peptides as Miniature Protein Structures

Yin, H. H. (2012) · ISRN Biochemistry · doi:10.5402/2012/692190 · Cited by 16

Application of Random Peptide Phage Display to the Study of Nuclear Hormone Receptors

Chang, C., Norris, J. D., Jansen, M. S., Huang, H.-J., & McDonnell, D. P. (2003) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(03)64007-3 · Cited by 15

Dissection of the functional interaction between p53 and the embryonic proto‐oncoprotein PAX3

Underwood, T., Amin, J., Lillycrop, K. A., & Blaydes, J. P. (2007) · FEBS Letters · doi:10.1016/j.febslet.2007.11.056 · Cited by 15

Cytotoxic effect of a non-peptidic small molecular inhibitor of the p53-HDM2 interaction on tumor cells

Li, W. (2005) · World Journal of Gastroenterology · doi:10.3748/wjg.v11.i19.2927 · Cited by 15

Disrupting the p53-mdm2 interaction as a potential therapeutic modality

Moll, U. M., & Zaika, A. (2000) · Drug Resistance Updates · doi:10.1054/drup.2000.0160 · Cited by 15

Activation of p53 by scaffold-stabilised expression of Mdm2-binding peptides: visualisation of reporter gene induction at the single-cell level

Karlsson, G. B., Jensen, A., Stevenson, L. F., Woods, Y. L., Lane, D. P., & Sørensen, M. S. (2004) · British Journal of Cancer · doi:10.1038/sj.bjc.6602143 · Cited by 14

Peptide inhibitors expressed in vivo

Kamb, A., & Caponigro, G. (2001) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(00)00160-5 · Cited by 14

Inhibition of cell proliferation, migration and invasion by a glioma‐targeted fusion protein combining the p53 C terminus and MDM2‐binding domain

Yu, J., Guo, M., Wang, T., Li, X., Wang, D., Wang, X., Zhang, Q., Wang, L., Zhang, Y., Zhao, C., et al. (2016) · Cell Proliferation · doi:10.1111/cpr.12238 · Cited by 13

p53: The Challenge of Linking Basic Science and Patient Management

Hall, P. A. (1998) · The Oncologist · doi:10.1634/theoncologist.3-4-218 · Cited by 13

Functional screening of a retroviral peptide library for MHC class I presentation

Tolstrup, A. B., Duch, M., Dalum, I., Pedersen, F. S., & Mouritsen, S. (2001) · Gene · doi:10.1016/s0378-1119(00)00572-2 · Cited by 13

Inhibition of the cell cycle with chemical inhibitors: A targeted approach

Welburn, J. P. I., & Endicott, J. (2005) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2005.02.008 · Cited by 12

Peptide aptamers as new tools to modulate clathrin-mediated internalisation — inhibition of MT1-MMP internalisation

Wickramasinghe, R. D., Ferrigno, P. K., & Roghi, C. H. (2010) · BMC Cell Biology · doi:10.1186/1471-2121-11-58 · Cited by 12

MDM2/MDMX inhibitor peptide: WO2008106507

Macchiarulo, A., & Pellicciari, R. (2009) · Expert Opinion on Therapeutic Patents · doi:10.1517/13543770902755137 · Cited by 12

Drugs Targeting Protein–Protein Interactions

Chêne, P. (2007) · Chemical biology · doi:10.1002/9783527619375.ch15e · Cited by 12

Docking Analysis and Multidimensional Hybrid QSAR Model of 1,4-Benzodiazepine-2,5-Diones as HDM2 Antagonists.

Dai, Y., Chen, N., Wang, Q., Zheng, H., Zhang, X., Jia, S., Dong, L., & Feng, D. (2012) · Europe PMC (PubMed Central) · Cited by 11

PLP2-derived peptide Rb4 triggers PARP-1-mediated necrotic death in murine melanoma cells

Maia, V., Berzaghi, R., Arruda, D. C., Machado, F. C., Loureiro, L. L., Melo, P. M. S., Morais, A. S., Budu, A., & Travassos, L. R. (2022) · Scientific Reports · doi:10.1038/s41598-022-06429-8 · Cited by 11

Molecular Peptide Grafting as a Tool to Create Novel Protein Therapeutics

Komar, A. A. (2023) · Molecules · doi:10.3390/molecules28052383 · 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

Small Scaffolds, Big Potential: Developing Miniature Proteins as Therapeutic Agents

Holub, J. M. (2017) · Drug Development Research · doi:10.1002/ddr.21408 · Cited by 12

(1-Benzimidazolonyl)alanine (Bia): preliminary investigations into a potential tryptophan mimetic

Huber, V. J., Arroll, T. W., Lum, C., Goodman, B. A., & Nakanishi, H. (2002) · Tetrahedron Letters · doi:10.1016/s0040-4039(02)01501-0 · Cited by 11

p53 – ein natürlicher Krebskiller: Einsichten in die Struktur und Therapiekonzepte

Römer, L., Klein, C., Dehner, A., Kessler, H., & Büchner, J. (2006) · Angewandte Chemie · doi:10.1002/ange.200600611 · Cited by 12

The Challenge of p53: Linking Biochemistry, Biology, and Patient Management

Bray, S. E., Schorl, C., & Hall, P. A. (1998) · Stem Cells · doi:10.1002/stem.160248 · Cited by 11

Generation of p53 suppressor peptide from the fragment of p53 protein.

Mittelman, J. M., & Gudkov, A. V. (1999) · Somatic Cell and Molecular Genetics · doi:10.1023/a:1018822121890 · Cited by 11

Why are we Interested in the Unfolded Peptides and Proteins?

Uversky, V. N., & Dunker, A. K. (2012) · Wiley eBooks · doi:10.1002/9781118183373.ch1 · Cited by 11

Antimicrobial sulfonamides clear latent Kaposi sarcoma herpesvirus infection and impair MDM2–p53 complex formation

Angius, F., Piras, E., Uda, S., Madeddu, C., Serpe, R., Bigi, R., Chen, W., Dittmer, D. P., Pompei, R., & Ingianni, A. (2017) · The Journal of Antibiotics · doi:10.1038/ja.2017.67 · Cited by 10

Des agents thérapeutiques ciblant des interactions protéine-protéine

Laudet, B., Prudent, R., Filhol, O., & Cochet, C. (2007) · médecine/sciences · doi:10.1051/medsci/2007233273 · Cited by 10

p53 in the Clinics

Hainaut, P. L., Wiman, K. G., & Olivier, M. (2012) · Springer eBooks · doi:10.1007/978-1-4614-3676-8 · Cited by 10

NMR Screening for Lead Compounds Using Tryptophan-Mutated Proteins

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