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

Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino-terminal Neh2 domain

Itoh, K., Wakabayashi, N., Katoh, Y., Ishii, T., Igarashi, K., Engel, J. D., & Yamamoto, M. (1999) · Genes & Development · doi:10.1101/gad.13.1.76 · Cited by 3,634 · see citing works

An inhibitor of Bcl-2 family proteins induces regression of solid tumours

Oltersdorf, T., Elmore, S. W., Shoemaker, A. R., Armstrong, R. C., Augeri, D. J., Belli, B., Bruncko, M., Deckwerth, T. L., Dinges, J., Hajduk, P. J., et al. (2005) · Nature · doi:10.1038/nature03579 · Cited by 3,407 · see citing works

Principles of protein-protein interactions

Jones, S., & Thornton, J. M. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.1.13 · Cited by 2,684 · 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

Discovering High-Affinity Ligands for Proteins: SAR by NMR

Shuker, S. B., Hajduk, P. J., Meadows, R. P., & Fesik, S. W. (1996) · Science · doi:10.1126/science.274.5292.1531 · Cited by 2,045 · see citing works

Anatomy of hot spots in protein interfaces

Bogan, A. A., & Thorn, K. S. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.1843 · Cited by 1,988 · see citing works

A Hot Spot of Binding Energy in a Hormone-Receptor Interface

Clackson, T., & Wells, J. A. (1995) · Science · doi:10.1126/science.7529940 · Cited by 1,987 · see citing works

The atomic structure of protein-protein recognition sites 1 1Edited by A. R. Fersht

Conte, L. L., Chothia, C., & Janin, J. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.2439 · Cited by 1,967 · 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

Untitled work

Leaver-Fay (2011) · doi:10.1016/b978-0-12-381270-4.00019-6 · Cited by 1,904 · see citing works

Identifying and Characterizing Binding Sites and Assessing Druggability

Halgren, T. A. (2009) · Journal of Chemical Information and Modeling · doi:10.1021/ci800324m · Cited by 1,771 · 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

A ‘Rule of Three’ for fragment-based lead discovery?

Congreve, M., Carr, R. A. E., Murray, C. W., & Jhoti, H. (2003) · Drug Discovery Today · doi:10.1016/s1359-6446(03)02831-9 · Cited by 1,365 · see citing works

High-Resolution Epitope Mapping of hGH-Receptor Interactions by Alanine-Scanning Mutagenesis

Cunningham, B. C., & Wells, J. A. (1989) · Science · doi:10.1126/science.2471267 · Cited by 1,361 · see citing works

Multicomponent Reaction Design in the Quest for Molecular Complexity and Diversity

Ruijter, E., Scheffelaar, R., & Orrù, R. V. A. (2011) · Angewandte Chemie International Edition · doi:10.1002/anie.201006515 · Cited by 1,332 · see citing works

A decade of fragment-based drug design: strategic advances and lessons learned

Hajduk, P. J., & Greer, J. (2007) · Nature Reviews Drug Discovery · doi:10.1038/nrd2220 · Cited by 1,068 · see citing works

Small-Molecule Inhibitors of Protein-Protein Interactions: Progressing toward the Reality

Arkin, M. R., Tang, Y., & Wells, J. A. (2014) · Chemistry & Biology · doi:10.1016/j.chembiol.2014.09.001 · Cited by 1,065 · see citing works

Targeting the Hedgehog pathway in cancer

Rubin, L. L., & de Sauvage, F. J. (2006) · Nature Reviews Drug Discovery · doi:10.1038/nrd2086 · Cited by 951 · see citing works

An empirical framework for binary interactome mapping

Venkatesan, K., Rual, J.-F. M., Vázquez, A., Stelzl, U., Lemmens, I. H., Hirozane-Kishikawa, T., Hao, T., Zenkner, M., Xin, X., Goh, K. I., et al. (2008) · Nature Methods · doi:10.1038/nmeth.1280 · Cited by 907 · see citing works

Diversity-oriented synthesis as a tool for the discovery of novel biologically active small molecules

Galloway, W. R. J. D., Isidro‐Llobet, A., & Spring, D. R. (2010) · Nature Communications · doi:10.1038/ncomms1081 · Cited by 895 · see citing works

A small molecule inhibitor of β-catenin/cyclic AMP response element-binding protein transcription

Emami, K. H., Nguyen, C., Ma, H., Kim, D. H., Jeong, K. W., Eguchi, M., Moon, R. T., Teo, J.-L., Oh, S. W., Kim, H. Y., et al. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0404875101 · Cited by 879 · see citing works

Macrocycles Are Great Cycles: Applications, Opportunities, and Challenges of Synthetic Macrocycles in Drug Discovery

Marsault, É., & Peterson, M. L. (2011) · Journal of Medicinal Chemistry · doi:10.1021/jm1012374 · Cited by 862 · see citing works

Estimating the size of the human interactome

Stumpf, M. P. H., Thorne, T., de Silva, E., Stewart, R., An, H. J., Lappé, M., & Wiuf, C. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0708078105 · Cited by 827 · see citing works

The rise of fragment-based drug discovery

Murray, C. W., & Rees, D. C. (2009) · Nature Chemistry · doi:10.1038/nchem.217 · Cited by 802 · see citing works

Fragment-based lead discovery

Rees, D. C., Congreve, M., Murray, C. W., & Carr, R. A. E. (2004) · Nature Reviews Drug Discovery · doi:10.1038/nrd1467 · Cited by 797 · see citing works

Structure of an HIF-1α-pVHL Complex: Hydroxyproline Recognition in Signaling

Min, J.-H., Yang, H., Ivan, M., Gertler, F., Kaelin, W. G., & Pavletich, N. P. (2002) · Science · doi:10.1126/science.1073440 · Cited by 765 · see citing works

Small Molecule Modulators of <scp>K</scp> eap1‐ <scp>N</scp> rf2‐ <scp>ARE</scp> Pathway as Potential Preventive and Therapeutic Agents

Magesh, S., Chen, Y., & Hu, L. (2012) · Medicinal Research Reviews · doi:10.1002/med.21257 · Cited by 760 · see citing works

Hot spots—A review of the protein–protein interface determinant amino‐acid residues

Moreira, I. S., Fernandes, P. A., & Ramos, M. J. (2007) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.21396 · Cited by 760 · see citing works

Long-timescale molecular dynamics simulations of protein structure and function

Klepeis, J. L., Lindorff‐Larsen, K., Dror, R. O., & Shaw, D. E. (2009) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2009.03.004 · Cited by 750 · see citing works

Structural basis for defects of Keap1 activity provoked by its point mutations in lung cancer

Padmanabhan, B., Tong, K. I., Ohta, T., Nakamura, Y., Scharlock, M., Ohtsuji, M., Kang, M.-I., Kobayashi, A., Yokoyama, S., & Yamamoto, M. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.01.013 · Cited by 735 · see citing works

Inhibition of α-helix-mediated protein–protein interactions using designed molecules

Azzarito, V., Long, K., Murphy, N. S., & Wilson, A. J. (2013) · Nature Chemistry · doi:10.1038/nchem.1568 · Cited by 727 · 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

Principles of Protein−Protein Interactions: What are the Preferred Ways For Proteins To Interact?

Keskin, O., Gursoy, A., Ma, B., & Nussinov, R. (2008) · Chemical Reviews · doi:10.1021/cr040409x · Cited by 697 · see citing works

Structure-based maximal affinity model predicts small-molecule druggability

Cheng, A. C., Coleman, R. G., Smyth, K. T., Cao, Q., Soulard, P., Caffrey, D. R., Salzberg, A. C., & Huang, E. S. (2007) · Nature Biotechnology · doi:10.1038/nbt1273 · Cited by 694 · see citing works

Convergent Solutions to Binding at a Protein-Protein Interface

DeLano, W. L., Ultsch, M. H., de, A. M., Vos, & Wells, J. A. (2000) · Science · doi:10.1126/science.287.5456.1279 · Cited by 673 · see citing works

Structure-based design of potent non-peptide MDM2 inhibitors

Ding, K., Lu, Y., Nikolovska-Coleska, Z., Qiu, S., Ding, Y., Gao, W., Stuckey, J., Krajewski, K., Roller, P. P., Tomita, Y., et al. (2005) · Journal of the American Chemical Society · doi:10.1021/ja051147z · Cited by 657 · see citing works

Efficient Drug Lead Discovery and Optimization

Jorgensen, W. L. (2009) · Accounts of Chemical Research · doi:10.1021/ar800236t · Cited by 651 · see citing works

Small-molecule ligands bind to a distinct pocket in Ras and inhibit SOS-mediated nucleotide exchange activity

Maurer, T., Garrenton, L. S., Oh, A., Pitts, K., Anderson, D. J., Skelton, N. J., Fauber, B. P., Pan, B., Malek, S., Stokoe, D., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1116510109 · Cited by 618 · see citing works

Recent Developments in Fragment-Based Drug Discovery

Congreve, M., Chessari, G., Tisi, D., & Woodhead, A. (2008) · Journal of Medicinal Chemistry · doi:10.1021/jm8000373 · Cited by 613 · see citing works

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

Zimmermann, G., Papke, B., Ismail, S., Vartak, N., Chandra, A., Hoffmann, M., Hahn, S. A., Triola, G., Wittinghofer, A., Bastiaens, P. I. H., et al. (2013) · Nature · doi:10.1038/nature12205 · Cited by 596 · see citing works

Structure-Based Virtual Screening for Drug Discovery: a Problem-Centric Review

Cheng, T., Li, Q., Zhou, Z., Wang, Y., & Bryant, S. H. (2012) · The AAPS Journal · doi:10.1208/s12248-012-9322-0 · Cited by 575 · see citing works

Effect of the MDM2 antagonist RG7112 on the P53 pathway in patients with MDM2-amplified, well-differentiated or dedifferentiated liposarcoma: an exploratory proof-of-mechanism study

Ray-Coquard, I., Blay, J.-Y., Italiano, A., Le Cesne, A., Penel, N., Zhi, J., Heil, F., Rueger, R., Graves, B., Ding, M., et al. (2012) · The Lancet Oncology · doi:10.1016/s1470-2045(12)70474-6 · Cited by 571 · see citing works

Highly enantioselective synthesis and cellular evaluation of spirooxindoles inspired by natural products

Antonchick, A. P., Gerding‐Reimers, C., Catarinella, M., Schürmann, M., Preut, H., Ziegler, S., Rauh, D., & Waldmann, H. (2010) · Nature Chemistry · doi:10.1038/nchem.730 · Cited by 570 · see citing works

Targeting the von Hippel-Lindau E3 ubiquitin ligase using small molecules to disrupt the VHL/HIF-1α interaction

Buckley, D. L., Van Molle, I., Gareiss, P. C., Tae, H. S., Michel, J., Noblin, D. J., Jorgensen, W. L., Ciulli, A., & Crews, C. M. (2012) · Journal of the American Chemical Society · doi:10.1021/ja209924v · Cited by 569 · see citing works

Phase II Study of Single-Agent Navitoclax (ABT-263) and Biomarker Correlates in Patients with Relapsed Small Cell Lung Cancer

Rudin, C. M., Hann, C. L., Garon, E. B., de Oliveira, M. R., Bonomi, P., Camidge, D. R., Chu, Q. S.-C., Giaccone, G., Khaira, D. K., Ramalingam, S. S., et al. (2012) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-11-3090 · Cited by 563 · see citing works

Towards the Optimal Screening Collection: A Synthesis Strategy

Nielsen, T. E., & Schreiber, S. L. (2007) · Angewandte Chemie International Edition · doi:10.1002/anie.200703073 · Cited by 552 · see citing works

Druggability Indices for Protein Targets Derived from NMR-Based Screening Data

Hajduk, P. J., Huth, J. R., & Fesik, S. W. (2005) · Journal of Medicinal Chemistry · doi:10.1021/jm049131r · Cited by 525 · see citing works

Biology‐Oriented Synthesis

Wetzel, S., Bon, R. S., Kumar, K., & Waldmann, H. (2011) · Angewandte Chemie International Edition · doi:10.1002/anie.201007004 · Cited by 507 · see citing works

Modulators of Protein–Protein Interactions

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

Menin-MLL inhibitors reverse oncogenic activity of MLL fusion proteins in leukemia

Grembecka, J. E., He, S., Shi, A., Purohit, T., Muntean, A. G., Sorenson, R. J., Showalter, H. D., Murai, M. J., Belcher, A. M., Hartley, T., et al. (2012) · Nature Chemical Biology · doi:10.1038/nchembio.773 · Cited by 468 · see citing works

Small-Molecule Inhibitors of the MDM2–p53 Protein–Protein Interaction (MDM2 Inhibitors) in Clinical Trials for Cancer Treatment

Zhao, Y., Aguilar, A., Bernard, D., & Wang, S. (2015) · Journal of Medicinal Chemistry · doi:10.1021/jm501092z · Cited by 462 · see citing works

Diversity-oriented synthesis: producing chemical tools for dissecting biology

Connor, C. J. O., Beckmann, H. S. G., & Spring, D. R. (2012) · Chemical Society Reviews · doi:10.1039/c2cs35023h · Cited by 434 · 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

Fragment-Based Lead Discovery Using X-ray Crystallography

Hartshorn, M. J., Murray, C. W., Cleasby, A., Frederickson, M., Tickle, I. J., & Jhoti, H. (2004) · Journal of Medicinal Chemistry · doi:10.1021/jm0495778 · Cited by 425 · see citing works

Targeting protein–protein interactions as an anticancer strategy

Ivanov, A. A., Khuri, F. R., & Fu, H. (2013) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2013.04.007 · Cited by 401 · see citing works

Discovery of RG7112: a small-molecule MDM2 inhibitor in clinical development

Vu, B., Wovkulich, P., Pizzolato, G., Lovey, A., Ding, Q., Jiang, N., Liu, J.-J., Zhao, C., Glenn, K., Wen, Y., et al. (2013) · ACS Medicinal Chemistry Letters · doi:10.1021/ml4000657 · Cited by 395 · see citing works

Tethering: Fragment-Based Drug Discovery

Erlanson, D. A., Wells, J. A., & Braisted, A. C. (2004) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.33.110502.140409 · Cited by 385 · see citing works

Binding of small molecules to an adaptive protein–protein interface

Arkin, M. R., Randal, M., DeLano, W. L., Hyde, J., Luong, T. N., Oslob, J. D., Raphael, D. R., Taylor, L., Wang, J., McDowell, R. S., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.252756299 · Cited by 376 · see citing works

Theory and Applications of NMR-Based Screening in Pharmaceutical Research

Lepre, C. A., Moore, J. M., & Peng, J. W. (2004) · Chemical Reviews · doi:10.1021/cr030409h · Cited by 323 · see citing works

Oncogenic protein interfaces: small molecules, big challenges

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

Predicting druggable binding sites at the protein–protein interface

Fuller, J. C., Burgoyne, N. J., & Jackson, R. M. (2008) · Drug Discovery Today · doi:10.1016/j.drudis.2008.10.009 · Cited by 311 · see citing works

Privileged Structures: Efficient Chemical “Navigators” toward Unexplored Biologically Relevant Chemical Spaces

Kim, J., Kim, H., & Park, S. B. (2014) · Journal of the American Chemical Society · doi:10.1021/ja508343a · Cited by 308 · see citing works

Discovery of Potent Myeloid Cell Leukemia 1 (Mcl-1) Inhibitors Using Fragment-Based Methods and Structure-Based Design

Friberg, A., Vigil, D., Zhao, B., Daniels, R. N., Burke, J. P., García-Barrantes, P. M., Camper, D. V., Chauder, B. A., Lee, T., Olejniczak, E. T., et al. (2012) · Journal of Medicinal Chemistry · doi:10.1021/jm301448p · Cited by 306 · see citing works

Studies Leading to Potent, Dual Inhibitors of Bcl-2 and Bcl-xL

Bruncko, M., Oost, T. K., Belli, B., Ding, H., Joseph, M. K., Kunzer, A. R., Martineau, D., McClellan, W. J., Mitten, M. J., Ng, S., et al. (2007) · Journal of Medicinal Chemistry · doi:10.1021/jm061152t · Cited by 306 · see citing works

Small‐Molecule Inhibitors of the Interaction between the E3 Ligase VHL and HIF1α

Buckley, D. L., Gustafson, J. L., Van Molle, I., Roth, A. G., Tae, H. S., Gareiss, P. C., Jorgensen, W. L., Ciulli, A., & Crews, C. M. (2012) · Angewandte Chemie International Edition · doi:10.1002/anie.201206231 · Cited by 302 · see citing works

Discovery of an Orally Bioavailable Small Molecule Inhibitor of Prosurvival B-Cell Lymphoma 2 Proteins

Park, C., Bruncko, M., Adickes, J., Bauch, J. L., Ding, H., Kunzer, A. R., Marsh, K. C., Nimmer, P. M., Shoemaker, A. R., Song, X., et al. (2008) · Journal of Medicinal Chemistry · doi:10.1021/jm800669s · Cited by 301 · see citing works

Assessing Helical Protein Interfaces for Inhibitor Design

Bullock, B. N., Jochim, A. L., & Arora, P. S. (2011) · Journal of the American Chemical Society · doi:10.1021/ja206074j · Cited by 298 · see citing works

A small molecule that binds Hedgehog and blocks its signaling in human cells

Stanton, B. Z., Peng, L. F., Maloof, N., Nakai, K., Wang, X., Duffner, J. L., Taveras, K. M., Hyman, J. M., Lee, S. W., Koehler, A. N., et al. (2009) · Nature Chemical Biology · doi:10.1038/nchembio.142 · Cited by 297 · see citing works

Discovery of a Potent Inhibitor of the Antiapoptotic Protein Bcl-x L from NMR and Parallel Synthesis

Petros, A. M., Dinges, J., Augeri, D. J., Baumeister, S. A., Betebenner, D. A., Bures, M. G., Elmore, S. W., Hajduk, P. J., Joseph, M. K., Landis, S. K., et al. (2005) · Journal of Medicinal Chemistry · doi:10.1021/jm0507532 · Cited by 295 · see citing works

Molecular diversity by design

Schreiber, S. L. (2009) · Nature · doi:10.1038/457153a · Cited by 292 · see citing works

Features of protein–protein interactions that translate into potent inhibitors: topology, surface area and affinity

Smith, M. C. P., & Gestwicki, J. E. (2012) · Expert Reviews in Molecular Medicine · doi:10.1017/erm.2012.10 · Cited by 285 · see citing works

MDM2 small-molecule antagonist RG7112 activates p53 signaling and regresses human tumors in preclinical cancer models

Tovar, C., Graves, B., Packman, K., Filipovic, Z., Xia, B. H. M., Tardell, C., Garrido, R., Lee, E., Kolinsky, K., To, K.-H., et al. (2013) · Cancer Research · doi:10.1158/0008-5472.can-12-2807 · Cited by 283 · see citing works

Route to three-dimensional fragments using diversity-oriented synthesis

Hung, A. W., Ramek, A., Wang, Y., Kaya, T., Wilson, J. A., Clemons, P. A., & Young, D. W. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1015271108 · Cited by 272 · see citing works

Discovery of Potent Keap1–Nrf2 Protein–Protein Interaction Inhibitor Based on Molecular Binding Determinants Analysis

Jiang, Z., Lu, M., Xu, L., Yang, T., Xi, M., Xu, X., Guo, X., Zhang, X., You, Q., & Sun, H.-P. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm5000529 · Cited by 263 · see citing works

Inhibition of protein–protein interactions using designed molecules

Wilson, A. J. (2009) · Chemical Society Reviews · doi:10.1039/b807197g · Cited by 262 · see citing works

Targeting Protein–Protein Interactions for Therapeutic Intervention: A Challenge for the Future

Zinzalla, G., & Thurston, D. E. (2009) · Future Medicinal Chemistry · doi:10.4155/fmc.09.12 · Cited by 257 · see citing works

Locating and characterizing binding sites on proteins

Mattos, C., & Ringe, D. (1996) · Nature Biotechnology · doi:10.1038/nbt0596-595 · Cited by 256 · see citing works

Terphenyl‐Based Helical Mimetics That Disrupt the p53/HDM2 Interaction

Yin, H. H., Lee, G., Park, H. S., Payne, G. A., Rodriguez, J. M., Sebti, S. M., & Hamilton, A. D. (2005) · Angewandte Chemie International Edition · doi:10.1002/anie.200462316 · Cited by 254 · see citing works

Bioactivity-Guided Navigation of Chemical Space

Bon, R. S., & Waldmann, H. (2010) · Accounts of Chemical Research · doi:10.1021/ar100014h · Cited by 246 · see citing works

Protein–protein interaction inhibitors get into the groove

Mullard, A. (2012) · Nature Reviews Drug Discovery · doi:10.1038/nrd3680 · Cited by 246 · see citing works

Structural conservation of druggable hot spots in protein–protein interfaces

Kozakov, D., Hall, D. R., Chuang, G., Cencic, R., Brenke, R., Grove, L. E., Beglov, D., Pelletier, J., Whitty, A., & Vajda, S. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1101835108 · Cited by 245 · see citing works

Small molecules inhibit the interaction of Nrf2 and the Keap1 Kelch domain through a non-covalent mechanism

Marcotte, D. J., Zeng, W., Hus, J., McKenzie, A., Hession, C., Jin, P., Bergeron, C., Lugovskoy, A. A., Enyedy, I. J., Cuervo, H., et al. (2013) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2013.04.019 · Cited by 245 · see citing works

State-of-the-art in ligand-based virtual screening

Ripphausen, P., Nisius, B., & Bajorath, J. (2011) · Drug Discovery Today · doi:10.1016/j.drudis.2011.02.011 · Cited by 240 · see citing works

Synthetic non-peptide mimetics of α-helices

Davis, J. M., Tsou, L. K., & Hamilton, A. D. (2007) · Chemical Society Reviews · doi:10.1039/b608043j · Cited by 238 · see citing works

Multiple Independent Binding Sites for Small-Molecule Inhibitors on the Oncoprotein c-Myc

Hammoudeh, D. I., Follis, A. V., Prochownik, E. V., & Metallo, S. J. (2009) · Journal of the American Chemical Society · doi:10.1021/ja900616b · Cited by 232 · see citing works

Druggable protein–protein interactions – from hot spots to hot segments

London, N., Raveh, B., & Schueler‐Furman, O. (2013) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2013.10.011 · Cited by 224 · see citing works

Study of the insulin dimerization: Binding free energy calculations and per‐residue free energy decomposition

Zoete, V., Meuwly, M., & Karplus, M. (2005) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.20528 · Cited by 212 · see citing works

Transient Pockets on Protein Surfaces Involved in Protein−Protein Interaction

Eyrisch, S., & Helms, V. (2007) · Journal of Medicinal Chemistry · doi:10.1021/jm070095g · Cited by 212 · see citing works

Discovery of a small-molecule inhibitor and cellular probe of Keap1–Nrf2 protein–protein interaction

Hu, L., Magesh, S., Chen, L., Wang, L., Lewis, T. A., Chen, Y., Khodier, C., Inoyama, D., Beamer, L. J., Emge, T. J., et al. (2013) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2013.03.013 · Cited by 206 · see citing works

Library Design for Fragment Based Screening

Schuffenhauer, A., Rüdisser, S., Marzinzik, A. L., Jahnke, W., Selzer, P. M., & Jacoby, E. (2005) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026054637700 · Cited by 203 · see citing works

Terphenyl-Based Bak BH3 α-Helical Proteomimetics as Low-Molecular-Weight Antagonists of Bcl-x L

Yin, H. H., Lee, G.-I., Sedey, K. A., Kutzki, O., Park, H. S., Orner, B. P., Ernst, J. T., Wang, H., Sebti, S. M., & Hamilton, A. D. (2005) · Journal of the American Chemical Society · doi:10.1021/ja050122x · Cited by 199 · see citing works

Dissecting Fragment-Based Lead Discovery at the von Hippel-Lindau Protein:Hypoxia Inducible Factor 1α Protein-Protein Interface

Molle, I. V., Thomann, A., Buckley, D. L., So, E. C., Lang, S., Crews, C. M., & Ciulli, A. (2012) · Chemistry & Biology · doi:10.1016/j.chembiol.2012.08.015 · Cited by 198 · see citing works

Place your BETs: the therapeutic potential of bromodomains

Prinjha, R. K., Witherington, J., & Lee, K. (2012) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2011.12.002 · Cited by 197 · see citing works

Ligand efficiency and fragment-based drug discovery

Bembenek, S. D., Tounge, B. A., & Reynolds, C. H. (2009) · Drug Discovery Today · doi:10.1016/j.drudis.2008.11.007 · Cited by 196 · see citing works

Targeting Protein-Protein Interaction by Small Molecules

Jin, L., Wang, W., & Fang, G. (2014) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-011613-140028 · Cited by 195 · see citing works

SPR-based Fragment Screening: Advantages and Applications

Neumann, T., Junker, H.-D., Schmidt, K., & Sekul, R. (2007) · Current Topics in Medicinal Chemistry · doi:10.2174/156802607782341073 · Cited by 190 · see citing works

Fragment-Based Discovery of Bromodomain Inhibitors Part 1: Inhibitor Binding Modes and Implications for Lead Discovery

Chung, C., Dean, A. W., Woolven, J. M., & Bamborough, P. (2011) · Journal of Medicinal Chemistry · doi:10.1021/jm201320w · Cited by 188 · see citing works

Identification of a new JNK inhibitor targeting the JNK-JIP interaction site

Stebbins, J. L., De, S. K., Machleidt, T., Becattini, B., Vazquez, J., Kuntzen, C., Chen, L.-H., Cellitti, J. F., Riel-Mehan, M., Emdadi, A., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0805677105 · Cited by 186 · see citing works

Progress in the Development and Application of Small Molecule Inhibitors of Bromodomain–Acetyl-lysine Interactions

Hewings, D. S., Rooney, T. P. C., Jennings, L. E., Hay, D. A., Schofield, C. J., Brennan, P. E., Knapp, S., & Conway, S. J. (2012) · Journal of Medicinal Chemistry · doi:10.1021/jm300915b · Cited by 182 · see citing works

Structural biology and drug discovery for protein–protein interactions

Jubb, H. C., Higueruelo, A. P., Winter, A., & Blundell, T. L. (2012) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2012.03.006 · Cited by 182 · 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

Structural Plasticity in a Remodeled Protein-Protein Interface

Atwell, S., Ultsch, M. H., de Vos, A. M., & Wells, J. A. (1997) · Science · doi:10.1126/science.278.5340.1125 · Cited by 180 · see citing works

Fragment-Based Discovery of Bromodomain Inhibitors Part 2: Optimization of Phenylisoxazole Sulfonamides

Bamborough, P., Diallo, H., Goodacre, J. D., Gordon, L. J., Lewis, A. J., Seal, J. T., Wilson, D. M., Woodrow, M. D., & Chung, C. (2011) · Journal of Medicinal Chemistry · doi:10.1021/jm201283q · Cited by 175 · see citing works

Between a rock and a hard place?

Whitty, A., & Kumaravel, G. (2006) · Nature Chemical Biology · doi:10.1038/nchembio0306-112 · Cited by 170 · see citing works

Deconstructing fragment-based inhibitor discovery

Babaoglu, K., & Shoichet, B. K. (2006) · Nature Chemical Biology · doi:10.1038/nchembio831 · Cited by 166 · see citing works

Selective Small Molecules Blocking HIV-1 Tat and Coactivator PCAF Association

Zeng, L., Li, J., Müller, M., Yan, S. X., Mujtaba, S., Pan, C., Wang, Z., & Zhou, M. (2005) · Journal of the American Chemical Society · doi:10.1021/ja044885g · Cited by 164 · see citing works

Rapid Identification of Keap1–Nrf2 Small-Molecule Inhibitors through Structure-Based Virtual Screening and Hit-Based Substructure Search

Zhuang, C., Narayanapillai, S. C., Zhang, W., Sham, Y. Y., & Xing, C. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm4017174 · Cited by 156 · see citing works

Drug design targeting protein-protein interactions (PPIs) using multiple ligand simultaneous docking (MLSD) and drug repositioning: discovery of raloxifene and bazedoxifene as novel inhibitors of IL-6/GP130 interface.

Li, H., Xiao, H., Lin, L., Jou, D., Kumari, V., Lin, J., & Li, C.-L. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm401144z · Cited by 155 · see citing works

Discovery of Small‐Molecule Inhibitors of the TLR1/TLR2 Complex

Cheng, K., Wang, X., Zhang, S., & Yin, H. H. (2012) · Angewandte Chemie International Edition · doi:10.1002/anie.201204910 · Cited by 155 · see citing works

SAR by MS: A Ligand Based Technique for Drug Lead Discovery Against Structured RNA Targets

Swayze, E. E., Jefferson, E. A., Sannes, K. A., Blyn, L. B., Risen, L. M., Arakawa, S., Osgood, S. A., Hofstadler, S. A., & Griffey, R. H. (2002) · Journal of Medicinal Chemistry · doi:10.1021/jm0255466 · Cited by 145 · see citing works

Design, Synthesis, and Evaluation of an α-Helix Mimetic Library Targeting Protein−Protein Interactions

Shaginian, A., Whitby, L. R., Hong, S., Hwang, I., Farooqi, B., Searcey, M., Chen, J., Vogt, P. K., & Boger, D. L. (2009) · Journal of the American Chemical Society · doi:10.1021/ja810025g · Cited by 144 · see citing works

Hot spot-based design of small-molecule inhibitors for protein–protein interactions

Guo, W., Wisniewski, J. A., & Ji, H. (2014) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2014.03.095 · Cited by 142 · see citing works

Integration of fragment screening and library design

Siegal, G., Eiso, A. B., & Schultz, J. (2007) · Drug Discovery Today · doi:10.1016/j.drudis.2007.08.005 · Cited by 142 · see citing works

Oligobenzamide proteomimetic inhibitors of the p53–hDM2 protein–protein interaction

Plante, J. P., Burnley, T., Malkova, B., Webb, M. E., Warriner, S. L., Edwards, T. A., & Wilson, A. J. (2009) · Chemical Communications · doi:10.1039/b908207g · Cited by 141 · see citing works

Target Structure-Based Discovery of Small Molecules that Block Human p53 and CREB Binding Protein Association

Sachchidanand, Resnick‐Silverman, L., Yan, S. X., Mutjaba, S., Liu, W., Zeng, L., Manfredi, J. J., & Zhou, M. (2006) · Chemistry & Biology · doi:10.1016/j.chembiol.2005.10.014 · Cited by 141 · see citing works

Terephthalamide Derivatives as Mimetics of Helical Peptides: Disruption of the Bcl-xL/Bak Interaction

Yin, H. H., Lee, G.-I., Sedey, K. A., Rodriguez, J. M., Wang, H., Sebti, S. M., & Hamilton, A. D. (2005) · Journal of the American Chemical Society · doi:10.1021/ja0446404 · Cited by 138 · see citing works

A strategy for the diversity-oriented synthesis of macrocyclic scaffolds using multidimensional coupling

Beckmann, H. S. G., Nie, F., Hagerman, C. E., Johansson, H., Tan, Y. S., Wilcke, D., & Spring, D. R. (2013) · Nature Chemistry · doi:10.1038/nchem.1729 · Cited by 137 · see citing works

A Small Molecule Binding to the Coactivator CREB-Binding Protein Blocks Apoptosis in Cardiomyocytes

Borah, J. C., Mujtaba, S., Karakikes, I., Zeng, L., Müller, M., Patel, J. A., Moshkina, N., Morohashi, K., Zhang, W., Gerona‐Navarro, G., et al. (2011) · Chemistry & Biology · doi:10.1016/j.chembiol.2010.12.021 · Cited by 136 · see citing works

Robust Generation of Lead Compounds for Protein–Protein Interactions by Computational and MCR Chemistry: p53/Hdm2 Antagonists

Czarna, A., Beck, B., Srivastava, S., Popowicz, G. M., Wolf, S., Huang, Y., Biśta, M., Holak, T. A., & Dömling, A. S. S. (2010) · Angewandte Chemie International Edition · doi:10.1002/anie.201001343 · Cited by 134 · see citing works

Small‐molecule protein–protein interaction inhibitors: Therapeutic potential in light of molecular size, chemical space, and ligand binding efficiency considerations

Buchwald, P. (2010) · IUBMB Life · doi:10.1002/iub.383 · Cited by 133 · see citing works

Discovery, Synthesis, and Biological Evaluation of Orally Active Pyrrolidone Derivatives as Novel Inhibitors of p53–MDM2 Protein–Protein Interaction

Zhuang, C., Miao, Z., Zhu, L., Dong, G., Guo, Z., Wang, S., Zhang, Y., Wu, Y., Yao, J., Sheng, C., et al. (2012) · Journal of Medicinal Chemistry · doi:10.1021/jm300969t · Cited by 131 · see citing works

Discovery of Novel Small-Molecule Inhibitors of BRD4 Using Structure-Based Virtual Screening

Vidler, L. R., Filippakopoulos, P., Fedorov, O., Picaud, S., Martin, S., Tomsett, M., Woodward, H. L., Brown, N., Knapp, S., & Hoelder, S. (2013) · Journal of Medicinal Chemistry · doi:10.1021/jm4011302 · Cited by 129 · see citing works

Drugs Targeting Protein–Protein Interactions

Chêne, P. (2006) · ChemMedChem · doi:10.1002/cmdc.200600004 · Cited by 129 · see citing works

Protein–protein interactions as druggable targets: recent technological advances

Higueruelo, A. P., Jubb, H. C., & Blundell, T. L. (2013) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2013.05.009 · Cited by 126 · see citing works

Novel Pyrrolopyrimidine-Based α-Helix Mimetics: Cell-Permeable Inhibitors of Protein−Protein Interactions

Lee, J. H., Zhang, Q., Jo, S., Chai, S. C., Oh, M., Im, W., Lu, H., & Lim, H. (2010) · Journal of the American Chemical Society · doi:10.1021/ja108230s · Cited by 126 · see citing works

Protein–protein interaction inhibition (2P2I) combining high throughput and virtual screening: Application to the HIV-1 Nef protein

Betzi, S., Restouin, A., Opi, S., Arold, S. T., Parrot, I., Guerlesquin, F., Morelli, X., & Collette, Y. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0707130104 · Cited by 125 · see citing works

Rational Design of Topographical Helix Mimics as Potent Inhibitors of Protein–Protein Interactions

Lao, B. B., Drew, K., Guarracino, D. A., Brewer, T. F., Heindel, D. W., Bonneau, R., & Arora, P. S. (2014) · Journal of the American Chemical Society · doi:10.1021/ja502310r · Cited by 124 · see citing works

Hot Spots and Transient Pockets: Predicting the Determinants of Small-Molecule Binding to a Protein–Protein Interface

Metz, A., Pfleger, C., Kopitz, H., Pfeiffer‐Marek, S., Baringhaus, K. H., & Gohlke, H. (2011) · Journal of Chemical Information and Modeling · doi:10.1021/ci200322s · Cited by 123 · see citing works

Relationship between Hot Spot Residues and Ligand Binding Hot Spots in Protein–Protein Interfaces

Zerbe, B. S., Hall, D. R., Vajda, S., Whitty, A., & Kozakov, D. (2012) · Journal of Chemical Information and Modeling · doi:10.1021/ci300175u · Cited by 122 · see citing works

Designing Focused Chemical Libraries Enriched in Protein-Protein Interaction Inhibitors using Machine-Learning Methods

Reynès, C., Host, H., Camproux, A., Laconde, G., Leroux, F., Mazars, A., Deprez, B. P., Fåhræus, R., Villoutreix, B. O., & Spérandio, O. (2010) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1000695 · Cited by 120 · see citing works

Fragment-Based Drug Discovery of 2-Thiazolidinones as Inhibitors of the Histone Reader BRD4 Bromodomain

Zhao, L., Cao, D., Chen, T., Wang, Y.-Q., Miao, Z., Xu, Y., Chen, W., Wang, X., Li, Y., Du, Z., et al. (2013) · Journal of Medicinal Chemistry · doi:10.1021/jm301793a · Cited by 119 · see citing works

A Small Nonrule of 3 Compatible Fragment Library Provides High Hit Rate of Endothiapepsin Crystal Structures with Various Fragment Chemotypes

Köster, H., Craan, T., Brass, S., Herhaus, C., Zentgraf, M., Neumann, L., Heine, A., & Klebe, G. (2011) · Journal of Medicinal Chemistry · doi:10.1021/jm200642w · Cited by 117 · see citing works

In vivo modulation of hypoxia-inducible signaling by topographical helix mimetics

Lao, B. B., Grishagin, I. V., Mesallati, H., Brewer, T. F., Olenyuk, B. Z., & Arora, P. S. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1402393111 · Cited by 115 · see citing works

Discovery of a Nanomolar Inhibitor of the Human Murine Double Minute 2 (MDM2)−p53 Interaction through an Integrated, Virtual Database Screening Strategy

Lu, Y., Nikolovska‐Coleska, Z., Fang, X., Gao, W., Shangary, S. K., Qiu, S., Qin, D., & Wang, S. (2006) · Journal of Medicinal Chemistry · doi:10.1021/jm060023+ · Cited by 115 · see citing works

Biophysical and computational fragment-based approaches to targeting protein–protein interactions: applications in structure-guided drug discovery

Winter, A., Higueruelo, A. P., Marsh, M., Sigurdardottir, A., Pitt, W. R., & Blundell, T. L. (2012) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583512000108 · Cited by 115 · see citing works

Natural product–inspired cascade synthesis yields modulators of centrosome integrity

Dückert, H., Pries, V., Khedkar, V., Menninger, S., Bruss, H., Bird, A. W., Maliga, Z., Brockmeyer, A., Janning, P., Hyman, A. A., et al. (2011) · Nature Chemical Biology · doi:10.1038/nchembio.758 · Cited by 115 · see citing works

Drug‐Like ProteinProtein Interaction Modulators: Challenges and Opportunities for Drug Discovery and Chemical Biology

Villoutreix, B. O., Kuenemann, M. A., Poyet, J., Bruzzoni‐Giovanelli, H., Labbé, C. M., Lagorce, D., Spérandio, O., & Miteva, M. A. (2014) · Molecular Informatics · doi:10.1002/minf.201400040 · Cited by 114 · see citing works

NMR-Based Approaches for the Identification and Optimization of Inhibitors of Protein–Protein Interactions

Barile, E., & Pellecchia, M. (2014) · Chemical Reviews · doi:10.1021/cr500043b · Cited by 109 · see citing works

Targeting Protein–Protein Interactions and Fragment-Based Drug Discovery

Valkov, E., Sharpe, T., Marsh, M., Greive, S., & Hyvönen, M. (2011) · Topics in Current Chemistry · doi:10.1007/128_2011_265 · Cited by 107 · see citing works

Structure, function, and dynamics of the dimerization and DNA-binding domain of oncogenic transcription factor v-Myc11Edited by P. E. Wright

Fieber, W., Schneider, M. L., Dunzendorfer-Matt, T., Kräutler, B., Konrat, R., & Bister, K. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.4537 · Cited by 107 · see citing works

Fragonomics: fragment-based drug discovery

Zartler, E. R., & Shapiro, M. J. (2005) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2005.05.002 · Cited by 104 · see citing works

Enabling Large-Scale Design, Synthesis and Validation of Small Molecule Protein-Protein Antagonists

Koes, D. R., Khoury, K., Huang, Y., Wang, W., Biśta, M., Popowicz, G. M., Wolf, S., Holak, T. A., Dömling, A. S. S., & Camacho, C. J. (2012) · PLoS ONE · doi:10.1371/journal.pone.0032839 · Cited by 104 · see citing works

Discovery of Small Molecule Inhibitors of the Interaction of the Thyroid Hormone Receptor with Transcriptional Coregulators

Arnold, L. A., Estébanez‐Perpiñá, E., Togashi, M., Jouravel, N., Shelat, A. A., McReynolds, A. C., Mar, E., Nguyen, P., Baxter, J. D., Fletterick, R. J., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m506693200 · Cited by 102 · see citing works

Minimal Pharmacophoric Elements and Fragment Hopping, an Approach Directed at Molecular Diversity and Isozyme Selectivity. Design of Selective Neuronal Nitric Oxide Synthase Inhibitors

Ji, H., Stanton, B. Z., Igarashi, J., Li, H., Pavel Martasek, E., Roman, L. J., Poulos, T. L., & Silverman, R. B. (2008) · Journal of the American Chemical Society · doi:10.1021/ja0772041 · Cited by 99 · see citing works

Comprehensive Peptidomimetic Libraries Targeting Protein–Protein Interactions

Whitby, L. R., & Boger, D. L. (2012) · Accounts of Chemical Research · doi:10.1021/ar300025n · Cited by 99 · see citing works

High-Affinity Small-Molecule Inhibitors of the Menin-Mixed Lineage Leukemia (MLL) Interaction Closely Mimic a Natural Protein–Protein Interaction

He, S., Senter, T. J., Pollock, J., Han, C., Upadhyay, S. K., Purohit, T., Gogliotti, R. D., Lindsley, C. W., Cierpicki, T., Stauffer, S. R., et al. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm401868d · Cited by 99 · see citing works

The Making of I-BET762, a BET Bromodomain Inhibitor Now in Clinical Development

Zhao, Y., Yang, C., & Wang, S. (2013) · Journal of Medicinal Chemistry · doi:10.1021/jm4014407 · Cited by 98 · see citing works

Crystal Structure of the E2 Transactivation Domain of Human Papillomavirus Type 11 Bound to a Protein Interaction Inhibitor

Wang, Y., Coulombe, R., Cameron, D. R., Thauvette, L., Massariol, M.-J., Amon, L. M., Fink, D., Titolo, S., Welchner, E., Yoakim, C., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m311376200 · Cited by 98 · see citing works

Selective and Potent Proteomimetic Inhibitors of Intracellular Protein–Protein Interactions

Barnard, A., Long, K., Martin, H. L., Miles, J. A., Edwards, T. A., Tomlinson, D. C., Macdonald, A., & Wilson, A. J. (2015) · Angewandte Chemie International Edition · doi:10.1002/anie.201410810 · Cited by 96 · see citing works

Perturbation of the c-Myc–Max Protein–Protein Interaction via Synthetic α-Helix Mimetics

Jung, K., Wang, H., Teriete, P., Yap, J. L., Chen, L., Lanning, M. E., Hu, A., Lambert, L. J., Holien, T., Sundan, A., et al. (2015) · Journal of Medicinal Chemistry · doi:10.1021/jm501440q · Cited by 94 · see citing works

Oligooxopiperazines as Nonpeptidic α-Helix Mimetics

Tošovská, P., & Arora, P. S. (2010) · Organic Letters · doi:10.1021/ol1003143 · Cited by 93 · see citing works

Discovery of novel inhibitors of the ZipA/FtsZ complex by NMR fragment screening coupled with structure-based design

Tsao, D. H. H., Sutherland, A. G., Jennings, L. D., Li, Y., Rush, T. S., Alvarez, J. C., Ding, W., Dushin, E. G., Dushin, R. G., Haney, S. A., et al. (2006) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2006.07.050 · Cited by 93 · see citing works

Identification of Small Molecule Agonists of the Orphan Nuclear Receptors Liver Receptor Homolog-1 and Steroidogenic Factor-1

Whitby, R. J., Dixon, S., Maloney, P., Delerive, P., Goodwin, B. J., Parks, D. J., & Willson, T. M. (2006) · Journal of Medicinal Chemistry · doi:10.1021/jm060990k · Cited by 92 · see citing works

Druggable Protein Interaction Sites Are More Predisposed to Surface Pocket Formation than the Rest of the Protein Surface

Johnson, D. K., & Karanicolas, J. (2013) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1002951 · Cited by 92 · see citing works

Catalytic Asymmetric Synthesis of Mixed 3,3′‐Bisindoles and Their Evaluation as Wnt Signaling Inhibitors

Arai, T., Yamamoto, Y., Awata, A., Kamiya, K., Ishibashi, M., & Arai, M. A. (2013) · Angewandte Chemie International Edition · doi:10.1002/anie.201208918 · Cited by 87 · see citing works

Pharmacophore identification of c-Myc inhibitor 10074-G5

Yap, J. L., Wang, H., Hu, A., Chauhan, J., Jung, K.-Y., Gharavi, R. B., Prochownik, E. V., & Fletcher, S. (2012) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2012.10.013 · Cited by 83 · see citing works

Small molecule modulators of protein-protein interactions: selected case studies

Aeluri, M., Chamakuri, S., Dasari, B., Guduru, S. K. R., Jimmidi, R., Jogula, S., & Arya, P. (2014) · Chemical Reviews · doi:10.1021/cr4004049 · Cited by 79 · see citing works

Identification of the first non-peptidic small molecule inhibitor of the c-Abl/14-3-3 protein–protein interactions able to drive sensitive and Imatinib-resistant leukemia cells to apoptosis

Corradi, V., Mancini, M., Manetti, F., Petta, S., Santucci, M. A., & Botta, M. (2010) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2010.08.019 · Cited by 77 · see citing works

An MDM2 antagonist (MI-319) restores p53 functions and increases the life span of orally treated follicular lymphoma bearing animals

Mohammad, R. M., Wu, J., Azmi, A. S., Aboukameel, A., Sosin, A. M., Wu, S., Yang, D., Wang, S., & Al-Katib, A. M. (2009) · Molecular Cancer · doi:10.1186/1476-4598-8-115 · Cited by 77 · see citing works

Development of a fluorescence polarization assay to screen for inhibitors of the FtsZ/ZipA interaction

Kenny, C. H., Ding, W., Kelleher, K. S., Benard, S., Dushin, E. G., Sutherland, A. G., Mosyak, L., Kriz, R., & Ellestad, G. A. (2003) · Analytical Biochemistry · doi:10.1016/j.ab.2003.08.033 · Cited by 76 · see citing works

Drug-Like Inhibitors of Protein-Protein Interactions: A Structural Examination of Effective Protein Mimicry

Fry, D. C. (2008) · Current Protein and Peptide Science · doi:10.2174/138920308784533989 · Cited by 76 · see citing works

Divergent Cascade Construction of Skeletally Diverse “Privileged” Pyrazole‐Derived Molecular Architectures

Zhang, Y., Wu, S., Wang, S., Fang, K., Dong, G., Liu, N., Miao, Z., Yao, J., Li, J., Zhang, W., et al. (2015) · European Journal of Organic Chemistry · doi:10.1002/ejoc.201403673 · Cited by 74 · see citing works

Fragment Library Screening and Lead Characterization Using SPR Biosensors

Danielson, U. H. (2009) · Current Topics in Medicinal Chemistry · doi:10.2174/156802609790102392 · Cited by 70 · see citing works

A Leap into the Chemical Space of Protein-Protein Interaction Inhibitors

Villoutreix, B. O., Labbé, C. M., Lagorce, D., Laconde, G., & Spérandio, O. (2012) · Current Pharmaceutical Design · doi:10.2174/138161212802651571 · Cited by 70 · see citing works

Design, Synthesis, and Structure−Activity Relationship Exploration of 1-Substituted 4-Aroyl-3-hydroxy-5-phenyl-1 H -pyrrol-2(5 H )-one Analogues as Inhibitors of the Annexin A2−S100A10 Protein Interaction

Reddy, T. R. K., Li, C., Guo, X., Myrvang, H. K., Fischer, P. M., & Dekker, L. V. (2011) · Journal of Medicinal Chemistry · doi:10.1021/jm101212e · Cited by 68 · see citing works

Synthesis and Biological Evaluation of a 5-6-5 Imidazole-Phenyl-Thiazole Based α-Helix Mimetic

Cummings, C. G., Ross, N. T., Katt, W. P., & Hamilton, A. D. (2008) · Organic Letters · doi:10.1021/ol8022962 · Cited by 68 · see citing works

Discovery of Modulators of Protein-Protein Interactions: Current Approaches and Limitations

Meireles, L., & Mustata, G. I. (2010) · Current Topics in Medicinal Chemistry · doi:10.2174/156802611794072632 · Cited by 68 · see citing works

Discovery of the first series of inhibitors of human papillomavirus type 11: inhibition of the assembly of the E1–E2–Origin DNA complex

Yoakim, C., Ogilvie, W. W., Goudreau, N., Naud, J., Haché, B., O’Meara, J. A., Cordingley, M. G., Archambault, J., & White, P. W. (2003) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/s0960-894x(03)00510-9 · Cited by 67 · see citing works

Updated Research and Applications of Small Molecule Inhibitors of Keap1-Nrf2 Protein-Protein Interaction: a Review

Zhuang, C., Miao, Z., Sheng, C., & Zhang, W. (2014) · Current Medicinal Chemistry · doi:10.2174/0929867321666140217104648 · Cited by 65 · see citing works

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

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

Targeting the Tcf4 G13ANDE17 Binding Site To Selectively Disrupt β-Catenin/T-Cell Factor Protein–Protein Interactions

Huang, Z., Zhang, M., Burton, S. D., Katsakhyan, L., & Ji, H. (2013) · ACS Chemical Biology · doi:10.1021/cb400795x · Cited by 63 · see citing works

Diversity‐Oriented Synthesis of Drug‐Like Macrocyclic Scaffolds Using an Orthogonal Organo‐ and Metal Catalysis Strategy

Grossmann, A., Bartlett, S., Janecek, M., Hodgkinson, J. T., & Spring, D. R. (2014) · Angewandte Chemie International Edition · doi:10.1002/anie.201406865 · Cited by 63 · see citing works

Fragment-Based Discovery of 8-Hydroxyquinoline Inhibitors of the HIV-1 Integrase–Lens Epithelium-Derived Growth Factor/p75 (IN–LEDGF/p75) Interaction

Serrao, E., Debnath, B., Otake, H., Kuang, Y., Christ, F., Debyser, Z., & Neamati, N. (2013) · Journal of Medicinal Chemistry · doi:10.1021/jm301632e · Cited by 63 · see citing works

What induces pocket openings on protein surface patches involved in protein–protein interactions?

Eyrisch, S., & Helms, V. (2008) · Journal of Computer-Aided Molecular Design · doi:10.1007/s10822-008-9239-y · Cited by 62 · see citing works

Biology‐Oriented Synthesis of a Withanolide‐Inspired Compound Collection Reveals Novel Modulators of Hedgehog Signaling

Švenda, J., Sheremet, M., Kremer, L., Maier, L., Bauer, J. O., Carsten Strohmann, B., Ziegler, S., Kumar, K., & Waldmann, H. (2015) · Angewandte Chemie International Edition · doi:10.1002/anie.201500112 · Cited by 62 · see citing works

In Silico-In Vitro Screening of Protein-Protein Interactions: Towards the Next Generation of Therapeutics

Villoutreix, B. O., Bastard, K., Spérandio, O., Fåhræus, R., Poyet, J., Calvo, F. M., Deprez, B. P., & Miteva, M. A. (2008) · Current Pharmaceutical Biotechnology · doi:10.2174/138920108783955218 · Cited by 62 · see citing works

Rational Design of Small-Molecule Inhibitors for β-Catenin/T-Cell Factor Protein–Protein Interactions by Bioisostere Replacement

Yu, B., Huang, Z., Zhang, M., Dillard, D. R., & Ji, H. (2012) · ACS Chemical Biology · doi:10.1021/cb300564v · Cited by 62 · see citing works

Targeting Multiple Conformations Leads to Small Molecule Inhibitors of the uPAR·uPA Protein–Protein Interaction That Block Cancer Cell Invasion

Khanna, M., Wang, F., Jo, I., Knabe, W. E., Wilson, S. M., Li, L., Bum‐Erdene, K., Li, J., Sledge, G. W., Khanna, R., et al. (2011) · ACS Chemical Biology · doi:10.1021/cb200180m · Cited by 58 · see citing works

Hydrophobic Binding Hot Spots of Bcl-xL Protein−Protein Interfaces by Cosolvent Molecular Dynamics Simulation

Yang, C.-Y., & Wang, S. (2011) · ACS Medicinal Chemistry Letters · doi:10.1021/ml100276b · Cited by 57 · see citing works

Sekikaic Acid and Lobaric Acid Target a Dynamic Interface of the Coactivator CBP/p300

Majmudar, C. Y., Højfeldt, J. W., Arewång, C.-J., Pomerantz, W. C. K., Gagnon, J. K., Schultz, P. J., Cesa, L. C., Doss, C. H., Rowe, S. P., Vásquez, V., et al. (2012) · Angewandte Chemie International Edition · doi:10.1002/anie.201206815 · Cited by 56 · see citing works

Protein-Protein Interactions in Receptor Activation and Intracellular Signalling

Blundell, T. L., Burke, D. F., Chirgadze, D. Y., Dhanaraj, V., Hyvönen, M., Innis, C. A., Parisini, E., Pellegrini, L., Sayed, M., & Sibanda, B. L. (2000) · Biological Chemistry · doi:10.1515/bc.2000.117 · Cited by 55 · see citing works

Identification of small-molecule inhibitors of the JIP–JNK interaction

Chen, T. X., Kablaoui, N. M., Little, J., Timofeevski, S. L., Tschantz, W. R., Chen, P., Feng, J., Charlton, M. E., Stanton, R. V., & Bauer, P. H. (2009) · Biochemical Journal · doi:10.1042/bj20081899 · Cited by 55 · see citing works

Structure-Based Design of Small-Molecule Protein–Protein Interaction Modulators: The Story so Far

Falchi, F., Caporuscio, F., & Recanatini, M. (2014) · Future Medicinal Chemistry · doi:10.4155/fmc.13.204 · Cited by 54 · see citing works

Facile Construction of Structurally Diverse Thiazolidinedione-Derived Compounds via Divergent Stereoselective Cascade Organocatalysis and Their Biological Exploratory Studies

Zhang, Y., Wang, S., Wu, S., Zhu, S., Dong, G., Miao, Z., Yao, J., Zhang, W., Sheng, C., & Wang, W. (2013) · ACS Combinatorial Science · doi:10.1021/co400022r · Cited by 51 · see citing works

High-Throughput Screen for Escherichia coli Heat Shock Protein 70 (Hsp70/DnaK): ATPase Assay in Low Volume by Exploiting Energy Transfer

Miyata, Y., Chang, L., Bainor, A. J., McQuade, T. J., Walczak, C. P., Zhang, Y., Larsen, M. J., Kirchhoff, P. D., & Gestwicki, J. E. (2010) · SLAS DISCOVERY · doi:10.1177/1087057110380571 · Cited by 51 · see citing works

Fragment-Based Drug Discovery of 2-Thiazolidinones as BRD4 Inhibitors: 2. Structure-Based Optimization

Zhao, L., Wang, Y.-Q., Cao, D., Chen, T., Wang, Q., Li, Y., Xu, Y., Zhang, N., Wang, X., Chen, D., et al. (2015) · Journal of Medicinal Chemistry · doi:10.1021/jm501504k · Cited by 50 · see citing works

Inhibitors of Difficult Protein–Protein Interactions Identified by High-Throughput Screening of Multiprotein Complexes

Cesa, L. C., Patury, S., Komiyama, T., Ahmad, A., Zuiderweg, E. R. P., & Gestwicki, J. E. (2013) · ACS Chemical Biology · doi:10.1021/cb400356m · Cited by 50 · see citing works

Double-Edged Swords as Cancer Therapeutics: Novel, Orally Active, Small Molecules Simultaneously Inhibit p53–MDM2 Interaction and the NF-κB Pathway

Zhuang, C., Miao, Z., Wu, Y., Guo, Z., Li, J., Yao, J., Xing, C., Sheng, C., & Zhang, W. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm401800k · Cited by 50 · see citing works

Drug for an 'undruggable' protein

Baker, N. M., & Der, C. J. (2013) · Nature · doi:10.1038/nature12248 · Cited by 49 · see citing works

Identification of an Atg8-Atg3 Protein–Protein Interaction Inhibitor from the Medicines for Malaria Venture Malaria Box Active in Blood and Liver Stage Plasmodium falciparum Parasites

Hain, A. U. P., Bartee, D., Sanders, N. G., Miller, A. S., Sullivan, D. J., Levitskaya, J., Meyers, C. L. F., & Bosch, J. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm401675a · Cited by 49 · see citing works

Design and modular parallel synthesis of a MCR derived α-helix mimetic protein–protein interaction inhibitor scaffold

Antuch, W., Menon, S., Chen, Q., Lu, Y., Sakamuri, S., Beck, B., Schauer-Vukašinović, V., Agarwal, S., Hess, S., & Dömling, A. S. S. (2006) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2005.11.102 · Cited by 48 · see citing works

Regulating the ARNT/TACC3 Axis: Multiple Approaches to Manipulating Protein/Protein Interactions with Small Molecules

Guo, Y., Partch, C. L., Key, J., Card, P. B., Pashkov, V., Patel, A., Bruick, R. K., Wurdak, H., & Gardner, K. H. (2012) · ACS Chemical Biology · doi:10.1021/cb300604u · Cited by 47 · see citing works

Diversity-oriented synthesis of a cytisine-inspired pyridone library leading to the discovery of novel inhibitors of Bcl-2

Marcaurelle, L. A., Johannes, C. W., Yohannes, D., Tillotson, B. P., & Mann, D. (2009) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2009.03.037 · Cited by 46 · see citing works

Synthesis of an Oxazole–Pyrrole–Piperazine Scaffold as an α‐Helix Mimetic

Moisan, L., Odermatt, S., Gombosuren, N., Carella, A., & REBEK, J. J. (2008) · European Journal of Organic Chemistry · doi:10.1002/ejoc.200701164 · Cited by 45 · see citing works

Differences between High- and Low-Affinity Complexes of Enzymes and Nonenzymes

Carlson, H. A., Smith, R. D., Khazanov, N. A., Kirchhoff, P. D., Dunbar, J. B., & Benson, M. L. (2008) · Journal of Medicinal Chemistry · doi:10.1021/jm8006504 · Cited by 45 · see citing works

Structure and Function of Benzoylurea‐Derived α‐Helix Mimetics Targeting the Bcl‐xL/Bak Binding Interface

Rodriguez, J. M., Ross, N. T., Katt, W. P., Dhar, D., Lee, G., & Hamilton, A. D. (2009) · ChemMedChem · doi:10.1002/cmdc.200800387 · Cited by 44 · see citing works

Small molecule inhibitor of the RPA70 N-terminal protein interaction domain discovered using in silico and in vitro methods

Glanzer, J. G., Liu, S., & Oakley, G. G. (2011) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2011.03.012 · Cited by 44 · see citing works

Druggability Assessment of Protein–Protein Interfaces

Wanner, J., Fry, D. C., Peng, Z., & Roberts, J. (2011) · Future Medicinal Chemistry · doi:10.4155/fmc.11.156 · Cited by 44 · see citing works

Structure-Guided Optimization of Small Molecules Inhibiting Human Immunodeficiency Virus 1 Tat Association with the Human Coactivator p300/CREB Binding Protein-Associated Factor

Pan, C., Mezei, M., Mujtaba, S., Müller, M., Zeng, L., Li, J., Wang, Z., & Zhou, M. (2007) · Journal of Medicinal Chemistry · doi:10.1021/jm070014g · Cited by 43 · see citing works

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

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

Orally Absorbed Cyclic Peptides

Nielsen, D. S., Shepherd, N. E., Xu, W., Lucke, A. J., Stoermer, M. J., & Fairlie, D. P. (2017) · Chemical Reviews · doi:10.1021/acs.chemrev.6b00838 · Cited by 451 · see citing works

Recent advances in targeting the “undruggable” proteins: from drug discovery to clinical trials

Xie, X., Yu, T., Li, X., Zhang, N., Foster, L. J., Peng, C., Huang, W., & He, G. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01589-z · Cited by 396 · see citing works

New insights into protein–protein interaction modulators in drug discovery and therapeutic advance

Nada, H., Choi, Y., Kim, S.-D., Jeong, K. S., Meanwell, N. A., & Lee, K. (2024) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-02036-3 · Cited by 233 · see citing works

Drugging Ras GTPase: a comprehensive mechanistic and signaling structural view

Lu, S., Jang, H., Gu, S., Zhang, J., & Nussinov, R. (2016) · Chemical Society Reviews · doi:10.1039/c5cs00911a · Cited by 188 · see citing works

Nrf2 activation through the inhibition of Keap1–Nrf2 protein–protein interaction

Lee, S., & Hu, L. (2020) · Medicinal Chemistry Research · doi:10.1007/s00044-020-02539-y · Cited by 136 · see citing works

Allosteric Activation Dictates PRC2 Activity Independent of Its Recruitment to Chromatin

Lee, C., Yu, J.-R., Kumar, S., Jin, Y., LeRoy, G., Bhanu, N. V., Kaneko, S., Garcia, B. A., Hamilton, A. D., & Reinberg, D. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.03.020 · Cited by 135 · see citing works

Small Molecule Inhibition of Ligand-Stimulated RAGE-DIAPH1 Signal Transduction

Manigrasso, M. B., Pan, J., Rai, V., Zhang, J., Reverdatto, S., Quadri, N., DeVita, R. J., Ramasamy, R., Shekhtman, A. G., & Schmidt, A. M. (2016) · Scientific Reports · doi:10.1038/srep22450 · Cited by 121 · see citing works

Emerging roles of allosteric modulators in the regulation of protein‐protein interactions (PPIs): A new paradigm for PPI drug discovery

Ni, D., Lu, S., & Zhang, J. (2019) · Medicinal Research Reviews · doi:10.1002/med.21585 · Cited by 116 · see citing works

Network analysis and in silico prediction of protein–protein interactions with applications in drug discovery

Murakami, Y., Tripathi, L. P., Prathipati, P., & Mizuguchi, K. (2017) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2017.02.005 · Cited by 111 · see citing works

Non-covalent Small-Molecule Kelch-like ECH-Associated Protein 1–Nuclear Factor Erythroid 2-Related Factor 2 (Keap1–Nrf2) Inhibitors and Their Potential for Targeting Central Nervous System Diseases

Pallesen, J. S., Tran, K. T., & Bach, A. (2018) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.8b00358 · Cited by 111 · see citing works

Development of potent small-molecule inhibitors to drug the undruggable steroid receptor coactivator-3

Song, X., Chen, J., Zhao, M., Zhang, C., Yu, Y., Lonard, D. M., Chow, D., Palzkill, T. G., Xu, J., O’Malley, B. W., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1604274113 · Cited by 94 · see citing works

Advances of Artificial Intelligence in Anti-Cancer Drug Design: A Review of the Past Decade

Wang, L., Song, Y., Wang, H., Zhang, X., Wang, M., He, J., Li, S., Zhang, L., Li, K., & Cao, L. (2023) · Pharmaceuticals · doi:10.3390/ph16020253 · Cited by 86 · see citing works

A Gold Nanocage/Cluster Hybrid Structure for Whole‐Body Multispectral Optoacoustic Tomography Imaging, EGFR Inhibitor Delivery, and Photothermal Therapy

Zhan, C., Huang, Y. X., Lin, G., Huang, S., Zeng, F., & Wu, S. (2019) · Small · doi:10.1002/smll.201900309 · Cited by 83 · see citing works

Recent progress in Keap1-Nrf2 protein-protein interaction inhibitors

Mou, Y., Wen, S., Li, Y., Gao, X., Zhang, X., & Jiang, Z. (2020) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2020.112532 · Cited by 83 · see citing works

Small molecules inhibiting Keap1-Nrf2 protein-protein interactions: A novel approach to activate Nrf2 function

Zhuang, C., Wu, Z., Xing, C., & Miao, Z. (2017) · MedChemComm · doi:10.1039/c6md00500d · Cited by 84 · see citing works

Anticancer drug discovery by targeting cullin neddylation

Yu, Q., Jiang, Y., & Sun, Y. (2019) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2019.09.005 · Cited by 77 · see citing works

Cytotoxicity of Pyrazine-Based Cyclometalated (C^Npz^C)Au(III) Carbene Complexes: Impact of the Nature of the Ancillary Ligand on the Biological Properties

Bertrand, B., Fernández‐Cestau, J., Angulo, J., Cominetti, M. M. D., Waller, Z. A. E., Searcey, M., O'Connell, M. A., & Bochmann, M. (2017) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.7b00339 · Cited by 73 · see citing works

Computer-Aided Drug Discovery for Undruggable Targets

Sun, Q., Wang, H., Xie, J., Wang, L., Mu, J., Li, J., Ren, Y., & Lai, L. (2025) · Chemical Reviews · doi:10.1021/acs.chemrev.4c00969 · Cited by 69 · see citing works

Fragment-based drug discovery supports drugging ‘undruggable’ protein–protein interactions

Wang, Z.-Z., Shi, X.-X., Huang, G.-Y., Hao, G., & Yang, G. (2023) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2023.01.008 · Cited by 64 · see citing works

The Potential of the Cyclotide Scaffold for Drug Development

Camarero, J. A., & Campbell, M. J. (2019) · Biomedicines · doi:10.3390/biomedicines7020031 · Cited by 62 · see citing works

Tumor Inhibition Achieved by Targeting and Regulating Multiple Key Elements in EGFR Signaling Pathway Using a Self‐Assembled Nanoprodrug

Li, B., Xie, X., Chen, Z., Zhan, C., Zeng, F., & Wu, S. (2018) · Advanced Functional Materials · doi:10.1002/adfm.201800692 · Cited by 60 · see citing works

Computational approaches for the design of modulators targeting protein-protein interactions

Rehman, A. U., Khurshid, B., Ali, Y., Rasheed, S., Wadood, A., Ng, H. L., Chen, H., Wei, Z., Luo, R., & Zhang, J. (2023) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2023.2171396 · Cited by 62 · see citing works

The Trafficking of the Water Channel Aquaporin-2 in Renal Principal Cells—a Potential Target for Pharmacological Intervention in Cardiovascular Diseases

Vukićević, T., Schulz, M., Faust, D., & Klußmann, E. (2016) · Frontiers in Pharmacology · doi:10.3389/fphar.2016.00023 · Cited by 59 · see citing works

Emerging Screening Approaches in the Development of Nrf2–Keap1 Protein–Protein Interaction Inhibitors

Leung, C., Zhang, J.-T., Yang, G., Liu, H., Han, Q., & Ma, D. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20184445 · Cited by 55 · see citing works

Recent progress in the development of small molecule Nrf2 activators: a patent review (2017-present)

Zhou, H.-S., Wang, Y., You, Q., & Jiang, Z. (2020) · Expert Opinion on Therapeutic Patents · doi:10.1080/13543776.2020.1715365 · Cited by 53 · see citing works

Emerging roles of A-kinase anchoring proteins in cardiovascular pathophysiology

Diviani, D., Reggi, E., Arambasic, M., Caso, S., & Maric, D. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2015.11.024 · Cited by 51 · see citing works

Artificial Intelligence–Driven Computational Approaches in the Development of Anticancer Drugs

Garg, P. K., Singhal, G., Kulkarni, P., Horne, D. A., Salgia, R., & Singhal, S. S. (2024) · Cancers · doi:10.3390/cancers16223884 · Cited by 49 · see citing works

Fr-PPIChem: An Academic Compound Library Dedicated to Protein–Protein Interactions

Bosc, N., Müller, C., Hoffer, L., Lagorce, D., Bourg, S., Derviaux, C., Gourdel‐Martin, M., Rain, J., Miller, T. W., Villoutreix, B. O., et al. (2020) · ACS Chemical Biology · doi:10.1021/acschembio.0c00179 · Cited by 48 · see citing works

A yeast two-hybrid system for the screening and characterization of small-molecule inhibitors of protein–protein interactions identifies a novel putative Mdm2-binding site in p53

Wong, J. H., Alfatah, M., Sin, M. F., Sim, H. M., Verma, C. S., Lane, D. P., & Arumugam, P. (2017) · BMC Biology · doi:10.1186/s12915-017-0446-7 · Cited by 45 · see citing works

Side-Chain Conformational Preferences Govern Protein–Protein Interactions

Watkins, A. M., Bonneau, R., & Arora, P. S. (2016) · Journal of the American Chemical Society · doi:10.1021/jacs.6b04892 · Cited by 45 · see citing works

Targeting Unoccupied Surfaces on Protein–Protein Interfaces

Rooklin, D. W., Modell, A. E., Li, H., Berdan, V. Y., Arora, P. S., & Zhang, Y. (2017) · Journal of the American Chemical Society · doi:10.1021/jacs.7b05960 · Cited by 45 · see citing works

Scanning Protein Surfaces with DNA‐Encoded Libraries

Kunig, V. B. K., Potowski, M., Škopić, M. K., & Brunschweiger, A. (2020) · ChemMedChem · doi:10.1002/cmdc.202000869 · Cited by 44 · see citing works

Virtual Screening Approaches towards the Discovery of Toll-Like Receptor Modulators

Pérez-Regidor, L., Zarioh, M., Ortega, L. G., & Martín‐Santamaría, S. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17091508 · Cited by 43 · see citing works

In silico identification of essential proteins in Corynebacterium pseudotuberculosis based on protein-protein interaction networks

Folador, E. L., de Carvalho, P. V. S. D., da Silva, W. M., Ferreira, R. S., Silva, A., Gromiha, M. M., Ghosh, P., Barh, D., Azevedo, V., & Röttger, R. (2016) · BMC Systems Biology · doi:10.1186/s12918-016-0346-4 · Cited by 43 · see citing works

Reasonably activating Nrf2: A long-term, effective and controllable strategy for neurodegenerative diseases

Li, Q., Xing, S., Chen, Y., Liao, Q., Li, Q., Liu, Y., He, S., Feng, F., Chen, Y., Zhang, J., et al. (2019) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2019.111862 · Cited by 43 · see citing works

Emerging Pharmacotherapeutic Strategies to Overcome Undruggable Proteins in Cancer

Lu, Y., Yang, Y., Zhu, G., Zeng, H., Fan, Y., Guo, F., Xu, D., Wang, B., Chen, D., & Ge, G. (2023) · International Journal of Biological Sciences · doi:10.7150/ijbs.83026 · Cited by 41 · see citing works

Computational methods-guided design of modulators targeting protein-protein interactions (PPIs)

Qiu, Y., Li, X., He, X., Pu, J., Zhang, J., & Lu, S. (2020) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2020.112764 · Cited by 41 · see citing works

Multitargeted molecular docking and dynamics simulation of thymol-based chalcones against cancer protein markers: Synthesis, characterization, and computational study

Laamari, Y., Bimoussa, A., Fawzi, M., Chagaleti, B. K., Saravanan, V., Alossaimi, M. A., Riadi, Y., Kathiravan, M. K., Oubella, A., Itto, M. Y. A., et al. (2024) · Journal of Molecular Structure · doi:10.1016/j.molstruc.2024.139116 · Cited by 40 · see citing works

Targeting Helicobacter pylori urease activity and maturation: In-cell high-throughput approach for drug discovery

Tarsia, C., Danielli, A., Florini, F., Cinelli, P., Ciurli, S., & Zambelli, B. (2018) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2018.07.020 · Cited by 40 · see citing works

Pyrrolopyrimidine vs Imidazole-Phenyl-Thiazole Scaffolds in Nonpeptidic Dimerization Inhibitors of Leishmania infantum Trypanothione Reductase

Revuelto, A., Ruiz‐Santaquiteria, M., de Lucio, H., Gamo, A. M., Carriles, A. A., Gutiérrez, K. J., Sánchez‐Murcia, P. A., Hermoso, J. A., Gago, F., Camarasa, M., et al. (2019) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.8b00355 · Cited by 40 · see citing works

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 40 · see citing works

Using backbone-cyclized Cys-rich polypeptides as molecular scaffolds to target protein–protein interactions

Chaudhuri, D., Aboye, T. L., & Camarero, J. A. (2019) · Biochemical Journal · doi:10.1042/bcj20180792 · Cited by 39 · see citing works

Stabilized cyclic peptides as modulators of protein–protein interactions: promising strategies and biological evaluation

Cheng, J., Zhou, J., Kong, L., Wang, H., Zhang, Y., Wang, X., Liu, G., & Chu, Q. (2023) · RSC Medicinal Chemistry · doi:10.1039/d3md00487b · Cited by 39 · see citing works

Allosteric Modulators of Protein–Protein Interactions (PPIs)

Ni, D., Liu, N., & Sheng, C. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-13-8719-7_13 · Cited by 37 · see citing works

Modulators of protein–protein interactions as antimicrobial agents

Kahan, R., Worm, D. J., Castro, G. V., Ng, S., & Barnard, A. (2021) · RSC Chemical Biology · doi:10.1039/d0cb00205d · Cited by 36 · see citing works

Hot Spot Analysis of YAP-TEAD Protein-Protein Interaction Using the Fragment Molecular Orbital Method and Its Application for Inhibitor Discovery

Kim, J., Lim, H., Moon, S., Cho, S. Y., Kim, M., Park, J. H., Park, H. W., & No, K. T. (2021) · Cancers · doi:10.3390/cancers13164246 · Cited by 37 · see citing works

Protein–protein interactions in bacteria: a promising and challenging avenue towards the discovery of new antibiotics

Carro, L. (2018) · Beilstein Journal of Organic Chemistry · doi:10.3762/bjoc.14.267 · Cited by 35 · see citing works

Mimicking Strategy for Protein–Protein Interaction Inhibitor Discovery by Virtual Screening

Wu, K., Lei, P.-M., Liu, H., Chun, W., Leung, C., & Ma, D. (2019) · Molecules · doi:10.3390/molecules24244428 · Cited by 35 · see citing works

Exploitation of the Ugi–Joullié reaction in drug discovery and development

Gazzotti, S., Rainoldi, G., & Silvani, A. (2019) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2019.1604676 · Cited by 32 · see citing works

Abrogating the Interaction Between p53 and Mortalin (Grp75/HSPA9/mtHsp70) for Cancer Therapy: The Story so far

Elwakeel, A. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.879632 · Cited by 32 · see citing works

Screening-based approaches to identify small molecules that inhibit protein–protein interactions

Choi, S., & Choi, K.-Y. (2017) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2017.1280456 · Cited by 29 · see citing works

Several inhibitors of the Plk1 Polo-Box Domain turn out to be non-specific protein alkylators

Archambault, V., & Normandin, K. (2017) · Cell Cycle · doi:10.1080/15384101.2017.1325043 · Cited by 29 · 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

Discovery of a Small-Molecule Inhibitor of Interleukin 15: Pharmacophore-Based Virtual Screening and Hit Optimization

Quéméner, A., Maillasson, M., Arzel, L., Sicard, B., Vomiandry, R., Mortier, E., Dubreuil, D., Jacques, Y., Lebreton, J., & Mathé‐Allainmat, M. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.7b00485 · Cited by 28 · see citing works

Medicinal Chemistry Insights into the Development of Small-Molecule Kelch-Like ECH-Associated Protein 1-Nuclear Factor Erythroid 2-Related Factor 2 (Keap1–Nrf2) Protein–Protein Interaction Inhibitors

Zhao, Z., Dong, R., You, Q., & Jiang, Z. (2023) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.3c00712 · Cited by 28 · see citing works

In Silico Discovery of Plant-Origin Natural Product Inhibitors of Tumor Necrosis Factor (TNF) and Receptor Activator of NF-κB Ligand (RANKL)

Melagraki, G., Ntougkos, E., Papadopoulou, D., Rinotas, V. E., Leonis, G., Douni, E. K., Afantitis, A., & Kollias, G. A. (2018) · Frontiers in Pharmacology · doi:10.3389/fphar.2018.00800 · Cited by 27 · see citing works

Applications of Solution NMR in Drug Discovery

Li, S., & Zhang, N. (2021) · Molecules · doi:10.3390/molecules26030576 · Cited by 26 · see citing works

Using the Cyclotide Scaffold for Targeting Biomolecular Interactions in Drug Development

Jacob, B., Vogelaar, A., Cadenas, E., & Camarero, J. A. (2022) · Molecules · doi:10.3390/molecules27196430 · Cited by 26 · see citing works

Development of Protein–Protein Interaction Inhibitors for the Treatment of Infectious Diseases

Voter, A. F., & Keck, J. L. (2017) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2017.07.005 · Cited by 25 · see citing works

A Bionic‐Homodimerization Strategy for Optimizing Modulators of Protein–Protein Interactions: From Statistical Mechanics Theory to Potential Clinical Translation

Yan, J., Zheng, X., You, W., He, W., & Xu, G. (2022) · Advanced Science · doi:10.1002/advs.202105179 · Cited by 24 · see citing works

Engineered protein scaffolds as leads for synthetic inhibitors of protein–protein interactions

Wuo, M. G., & Arora, P. S. (2018) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2018.05.013 · Cited by 25 · see citing works

A new strategy for the in vitro selection of stapled peptide inhibitors by mRNA display

Iqbal, E. S., Richardson, S. L., Abrigo, N. A., Dods, K. K., Franco, H. E. O., Gerrish, H. S., Kotapati, H. K., Morgan, I. M., Masterson, D. S., & Hartman, M. C. T. (2019) · Chemical Communications · doi:10.1039/c8cc10192b · Cited by 25 · see citing works

The impact of AI on modern oncology from early detection to personalized cancer treatment

Li, J., Zhang, L., Yu, Z., Bao, Z., Li, D., & Wang, L. (2026) · npj Precision Oncology · doi:10.1038/s41698-026-01276-6 · Cited by 24 · see citing works

The future of therapeutic options for hereditary angioedema

Smith, T., & Riedl, M. A. (2024) · Annals of Allergy Asthma & Immunology · doi:10.1016/j.anai.2024.04.029 · Cited by 24 · see citing works

Flexibility is important for inhibition of the MDM2/p53 protein–protein interaction by cyclic β-hairpins

Danelius, E., Pettersson, M., Bred, M., Min, J., Waddell, M. B., Guy, R. K., Grøtli, M., & Erdélyi, M. (2016) · Organic & Biomolecular Chemistry · doi:10.1039/c6ob01510g · Cited by 24 · see citing works

Waste-Minimized Continuous-Flow Synthesis of Oxindoles Exploiting a Polymer-Supported N Heterocyclic Palladium Carbene Complex in a CPME/Water Azeotrope

Salameh, N., Ferlin, F., Valentini, F., Anastasiou, I., & Vaccaro, L. (2022) · ACS Sustainable Chemistry & Engineering · doi:10.1021/acssuschemeng.2c00550 · Cited by 23 · see citing works

Therapeutic perspectives of heat shock proteins and their protein-protein interactions in myocardial infarction

Wu, J., Chen, S., Liu, Y., Liu, Z., Wang, D., & Cheng, Y. (2020) · Pharmacological Research · doi:10.1016/j.phrs.2020.105162 · Cited by 22 · see citing works

Mdm2 inhibitors as a platform for the design of P-glycoprotein inhibitors

Grigoreva, T. A., Romanova, A. A., Sagaidak, A. V., Владимировна, В. С., Novikova, D., & Tribulovich, V. G. (2020) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2020.127424 · Cited by 21 · see citing works

In Silico Identification and Evaluation of Natural Products as Potential Tumor Necrosis Factor Function Inhibitors Using Advanced Enalos Asclepios KNIME Nodes

Papadopoulou, D., Drakopoulos, A., Lagarias, P. I., Melagraki, G., Kollias, G. A., & Afantitis, A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms221910220 · Cited by 20 · see citing works

Bifunctional Ligands for Inhibition of Tight-Binding Protein–Protein Interactions

Ivan, T., Enkvist, E., Viira, B., Manoharan, G. B., Raidaru, G., Pflug, A., Alam, K. A., Zaccolo, M., Engh, R. A., & Uri, A. (2016) · Bioconjugate Chemistry · doi:10.1021/acs.bioconjchem.6b00293 · Cited by 20 · see citing works

Methods for the Discovery and Identification of Small Molecules Targeting Oxidative Stress-Related Protein–Protein Interactions: An Update

Wu, X., Zhang, Q., Guo, Y., Zhang, H., Guo, X., You, Q., & Wang, L. (2022) · Antioxidants · doi:10.3390/antiox11040619 · Cited by 19 · see citing works

Targeting protein-protein interactions with low molecular weight and short peptide modulators: insights on disease pathways and starting points for drug discovery

Trisciuzzi, D., Villoutreix, B. O., Siragusa, L., Baroni, M., Cruciani, G., & Nicolotti, O. (2023) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2023.2218641 · Cited by 19 · see citing works

Computational Tools and Strategies to Develop Peptide-Based Inhibitors of Protein-Protein Interactions

Delaunay, M., & Ha‐Duong, T. (2021) · Methods in molecular biology · doi:10.1007/978-1-0716-1855-4_11 · Cited by 17 · see citing works

Inhibition of HSP90 sensitizes a novel Raf/ERK dual inhibitor CY-9d in triple-negative breast cancer cells

Chen, Y., Wang, X., Cao, C., Wang, X., Liang, S., Peng, C., Fu, L., & He, G. (2017) · Oncotarget · doi:10.18632/oncotarget.22119 · Cited by 18 · see citing works

Investigation of Hot Spot Region in XIAP Inhibitor Binding Site by Fragment Molecular Orbital Method

Lim, H., Jin, X., Kim, J., Hwang, S., Shin, K. B., Choi, J., Nam, K.-Y., & No, K. T. (2019) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2019.08.004 · Cited by 17 · see citing works

Network Analysis Identifies Drug Targets and Small Molecules to Modulate Apoptosis Resistant Cancers

Fathima, S., Sinha, S., & Donakonda, S. (2021) · Cancers · doi:10.3390/cancers13040851 · Cited by 16 · see citing works

Selected Approaches to Disrupting Protein–Protein Interactions within the MAPK/RAS Pathway

Harwood, S. J., Smith, C. R., Lawson, J. D., & Ketcham, J. M. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24087373 · Cited by 16 · see citing works

Natural products used as a chemical library for protein–protein interaction targeted drug discovery

Jin, X., Lee, K., Kim, N. H., Kim, H. S., Yook, J. I., Choi, J., & No, K. T. (2017) · Journal of Molecular Graphics and Modelling · doi:10.1016/j.jmgm.2017.10.015 · Cited by 16 · see citing works

Synthesis, docking, SAR and ADMET evaluation of novel pyrrolo[3,4-c]pyrazole-4,6-dione derivatives

Zaki, Y. H., Zaki, M., Farag, B., & Gomha, S. M. (2026) · Scientific Reports · doi:10.1038/s41598-025-33678-0 · Cited by 15 · see citing works

PPI Modulators of E6 as Potential Targeted Therapeutics for Cervical Cancer: Progress and Challenges in Targeting E6

Chitsike, L., & Duerksen-Hughes, P. J. (2021) · Molecules · doi:10.3390/molecules26103004 · Cited by 15 · see citing works

Small Molecules as Toll-like Receptor 4 Modulators Drug and In-House Computational Repurposing

Pérez-Regidor, L., Guzman‐Caldentey, J., Oberhauser, N., Punzón, C., Balogh, B., Pedro, J. R., Falomir, E., Nurisso, A., Mátyus, P., Menéndez, J. C., et al. (2022) · Biomedicines · doi:10.3390/biomedicines10092326 · Cited by 15 · see citing works

Medicinal Chemistry Strategies for the Development of Inhibitors Disrupting β-Catenin’s Interactions with Its Nuclear Partners

Zhang, H., Liu, C., Zhu, D., Zhang, Q., & Li, J. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.2c01016 · Cited by 15 · see citing works

Using machine‐learning‐driven approaches to boost hot‐spot's knowledge

Rosário‐Ferreira, N., Bonvin, A. M. J. J., & Moreira, I. S. (2022) · Wiley Interdisciplinary Reviews Computational Molecular Science · doi:10.1002/wcms.1602 · Cited by 14 · see citing works

Production of marine-derived bioactive peptide molecules for industrial applications: A reverse engineering approach

Surwase, A. J., & Thakur, N. L. (2024) · Biotechnology Advances · doi:10.1016/j.biotechadv.2024.108449 · Cited by 13 · see citing works

Mapping Protein–Protein Interactions of the Resistance-Related Bacterial Zeta Toxin–Epsilon Antitoxin Complex (ε2ζ2) with High Affinity Peptide Ligands Using Fluorescence Polarization

Fernández‐Bachiller, M. I., Brzozowska, I., Odolczyk, N., Zielenkiewicz, U., Zielenkiewicz, P., & Rademann, J. (2016) · Toxins · doi:10.3390/toxins8070222 · Cited by 13 · see citing works

Targeting Protein Neddylation to Inactivate Cullin-RING Ligases by Gossypol: A Lucky Hit or a New Start?

Yu, Q., & Sun, Y. (2021) · Drug Design Development and Therapy · doi:10.2147/dddt.s286373 · Cited by 13 · see citing works

Exploring the chemical space of protein–protein interaction inhibitors through machine learning

Choi, J., Yun, J. S., Song, H., Kim, N. H., Kim, H. S., & Yook, J. I. (2021) · Scientific Reports · doi:10.1038/s41598-021-92825-5 · Cited by 13 · see citing works

Identification of a short ACE2-derived stapled peptide targeting the SARS-CoV-2 spike protein

Calugi, L., Sautariello, G., Lenci, E., Mattei, M. L., Coppa, C., Cini, N., Contini, A., & Trabocchi, A. (2023) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2023.115118 · Cited by 13 · see citing works

Synthesis of Three‐Dimensional (Di)Azatricyclododecene Scaffold and Its Application to Peptidomimetics

Umedera, K., Morita, T., Yoshimori, A., Yamada, K., Katoh, A., Kouji, H., & Nakamura, H. (2021) · Chemistry - A European Journal · doi:10.1002/chem.202101440 · Cited by 13 · see citing works

Glutamine Synthetase Drugability beyond Its Active Site: Exploring Oligomerization Interfaces and Pockets

Moreira, C., Ramos, M. J., & Fernandes, P. A. (2016) · Molecules · doi:10.3390/molecules21081028 · Cited by 12 · see citing works

A small-molecule inhibitor targeting the AURKC-IκBα interaction decreases transformed growth of MDA-MB-231 breast cancer cells

Han, E. H., Min, J.-Y., Yoo, S.-A., Park, S.-J., Choe, Y.-J., Yun, H. S., Lee, Z., Jin, S. W., Kim, H. G., Jeong, H. G., et al. (2017) · Oncotarget · doi:10.18632/oncotarget.18883 · Cited by 12 · see citing works

Fragment‐Based Protein–Protein Interaction Antagonists of a Viral Dimeric Protease

Gable, J. E., Lee, G., Acker, T. M., Hulce, K. R., Gonzalez, E. R., Schweigler, P., Melkko, S., Farady, C. J., & Craik, C. S. (2016) · ChemMedChem · doi:10.1002/cmdc.201500526 · Cited by 12 · see citing works

Solid-phase parallel synthesis of 1,3,4-oxadiazole based peptidomimetic library as a potential modulator of protein-protein interactions

Abdildinova, A., Yang, S., & Gong, Y.-D. (2017) · Tetrahedron · doi:10.1016/j.tet.2017.12.055 · Cited by 12 · see citing works

Des3PI: a fragment-based approach to design cyclic peptides targeting protein–protein interactions

Delaunay, M., & Ha‐Duong, T. (2022) · Journal of Computer-Aided Molecular Design · doi:10.1007/s10822-022-00468-z · Cited by 11 · see citing works

Small molecule–based targeting of TTD-A dimerization to control TFIIH transcriptional activity represents a potential strategy for anticancer therapy

Gervais, V., Muller, I., Mari, P., Mourcet, A., Movellan, K. T., Ramos, P., Marcoux, J., Guillet, V., Javaid, S., Burlet‐Schiltz, O., et al. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.003444 · Cited by 11 · see citing works

Computational design of cyclic peptides to inhibit protein-peptide interactions

Delaunay, M., & Ha‐Duong, T. (2023) · Biophysical Chemistry · doi:10.1016/j.bpc.2023.106987 · Cited by 10 · see citing works

Structural insights for peptide and small molecules based drug discovery targeting the KEAP1 Kelch domain: A review

Sinha, S., Kumar, R., Singh, N. K., & Babu, M. A. (2025) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2025.118329 · Cited by 9 · see citing works

Probing the Druggablility on the Interface of the Protein–Protein Interaction and Its Allosteric Regulation Mechanism on the Drug Screening for the CXCR4 Homodimer

Shen, L., Yuan, Y., Guo, Y., Li, M., Li, C., & Pu, X. (2019) · Frontiers in Pharmacology · doi:10.3389/fphar.2019.01310 · Cited by 9 · see citing works

Small-molecule inhibitors of protein-protein interactions

Vassilev, L. (2011)

Strategies for Targeting Protein–Protein Interactions With Synthetic Agents

Yin, H. H., & Hamilton, A. D. (2005) · Angewandte Chemie International Edition · doi:10.1002/anie.200461786 · Cited by 453 · 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

Targeting Protein-Protein Interactions by Small Molecules

(2018) · Springer eBooks · doi:10.1007/978-981-13-0773-7 · Cited by 14 · see citing works

Recent advances in the development of small molecule inhibitors for targeting protein-protein interactions in drug discovery

Rawat, S. N. S., Nath, R. R. T. M., Singh, P. B. K. S. P., & Bagade, M. M. O. M. (2023) · Biochemical and Cellular Archives/Biochemical and cellular archives · doi:10.51470/bca.2023.23.2.1199