Plucking the high hanging fruit: A systematic approach for targeting protein–protein interactions

The Protein Data Bank

Berman, H. M. (2000) · Nucleic Acids Research · doi:10.1093/nar/28.1.235 · Cited by 40,196 · see citing works

Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings 1PII of original article: S0169-409X(96)00423-1. The article was originally published in Advanced Drug Delivery Reviews 23 (1997) 3–25. 1

Lipinski, C. A., Lombardo, F., Dominy, B. W., & Feeney, P. J. (2001) · Advanced Drug Delivery Reviews · doi:10.1016/s0169-409x(00)00129-0 · Cited by 18,139 · see citing works

Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings

Lipinski, C. A., Lombardo, F., Dominy, B. W., & Feeney, P. J. (1997) · Advanced Drug Delivery Reviews · doi:10.1016/s0169-409x(96)00423-1 · Cited by 11,484 · see citing works

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

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

The druggable genome

Hopkins, A. L., & Groom, C. R. (2002) · Nature Reviews Drug Discovery · doi:10.1038/nrd892 · Cited by 3,305 · 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

ABT-263: A Potent and Orally Bioavailable Bcl-2 Family Inhibitor

Tse, C., Shoemaker, A. R., Adickes, J., Anderson, M. G., Chen, J., Jin, S., Johnson, E. F., Marsh, K. C., Mitten, M. J., Nimmer, P., et al. (2008) · Cancer Research · doi:10.1158/0008-5472.can-07-5836 · Cited by 1,992 · 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

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

Core Structure of gp41 from the HIV Envelope Glycoprotein

Chan, D. C., Fass, D., Berger, J. M., & Kim, P. S. (1997) · Cell · doi:10.1016/s0092-8674(00)80205-6 · Cited by 1,961 · see citing works

RAS oncogenes: weaving a tumorigenic web

Pylayeva-Gupta, Y., Grabocka, E., & Bar-Sagi, D. (2011) · Nature Reviews Cancer · doi:10.1038/nrc3106 · Cited by 1,789 · 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

Atomic structure of the ectodomain from HIV-1 gp41

Weissenhorn, W., Dessen, A., Harrison, S. C., Skehel, J. J., & Wiley, D. C. (1997) · Nature · doi:10.1038/387426a0 · Cited by 1,625 · see citing works

Privileged scaffolds for library design and drug discovery

Welsch, M. E., Snyder, S. A., & Stockwell, B. R. (2010) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2010.02.018 · Cited by 1,509 · see citing works

Structure of Bcl-x _L -Bak Peptide Complex: Recognition Between Regulators of Apoptosis

Sattler, M., Liang, H., Nettesheim, D., Meadows, R. P., Harlan, J. E., Eberstadt, M., Yoon, H. S., Shuker, S. B., Chang, B. S., Minn, A. J., et al. (1997) · Science · doi:10.1126/science.275.5302.983 · Cited by 1,476 · 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

Activation of Apoptosis in Vivo by a Hydrocarbon-Stapled BH3 Helix

Walensky, L. D., Kung, A. L., Escher, I., Malia, T. J., Barbuto, S., Wright, R. D., Wagner, G., Verdine, G. L., & Korsmeyer, S. J. (2004) · Science · doi:10.1126/science.1099191 · Cited by 1,349 · see citing works

Mechanisms of Viral Membrane Fusion and Its Inhibition

Eckert, D. M., & Kim, P. S. (2001) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.70.1.777 · Cited by 1,283 · 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

An All-Hydrocarbon Cross-Linking System for Enhancing the Helicity and Metabolic Stability of Peptides

Schafmeister, C. E., Po, J., & Verdine, G. L. (2000) · Journal of the American Chemical Society · doi:10.1021/ja000563a · Cited by 1,037 · see citing works

A Breathing Hybrid Organic–Inorganic Solid with Very Large Pores and High Magnetic Characteristics

Barthelet, K., Marrot, J., Riou, D., & Férey, G. (2002) · Angewandte Chemie International Edition · doi:10.1002/1521-3773(20020118)41:2 · Cited by 976 · see citing works

Foldamers as versatile frameworks for the design and evolution of function

Goodman, C. M., Choi, S., Shandler, S. J., & DeGrado, W. F. (2007) · Nature Chemical Biology · doi:10.1038/nchembio876 · Cited by 899 · see citing works

Molecular Recognition of Protein−Ligand Complexes: Applications to Drug Design

Babine, R. E., & Bender, S. L. (1997) · Chemical Reviews · doi:10.1021/cr960370z · Cited by 889 · see citing works

A simple physical model for binding energy hot spots in protein–protein complexes

Kortemme, T., & Baker, D. A. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.202485799 · Cited by 801 · see citing works

The structural basis of the activation of Ras by Sos

Boriack-Sjodin, P. A., Margarit, S. M., Bar-Sagi, D., & Kuriyan, J. (1998) · Nature · doi:10.1038/28548 · Cited by 799 · see citing works

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

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

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

Direct inhibition of the NOTCH transcription factor complex

Moellering, R. E., Cornejo, M., Davis, T. N., Bianco, C. D., Aster, J. C., Blacklow, S. C., Kung, A. L., Gilliland, D. G., Verdine, G. L., & Bradner, J. E. (2009) · Nature · doi:10.1038/nature08543 · Cited by 752 · 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

Small-Molecule Inhibitors of the MDM2-p53 Protein-Protein Interaction to Reactivate p53 Function: A Novel Approach for Cancer Therapy

Shangary, S., & Wang, S. (2009) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.48.113006.094723 · Cited by 623 · 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 611 · see citing works

Diversity-oriented synthesis: Exploring the intersections between chemistry and biology

Tan, D. S. (2005) · Nature Chemical Biology · doi:10.1038/nchembio0705-74 · Cited by 605 · see citing works

Computational Alanine Scanning of Protein-Protein Interfaces

Kortemme, T., Kim, D. E., & Baker, D. A. (2004) · Science s STKE · doi:10.1126/stke.2192004pl2 · Cited by 586 · see citing works

Reactivation of the p53 Tumor Suppressor Pathway by a Stapled p53 Peptide

Bernal, F., Tyler, A. F., Korsmeyer, S. J., Walensky, L. D., & Verdine, G. L. (2007) · Journal of the American Chemical Society · doi:10.1021/ja0693587 · Cited by 559 · see citing works

Identification of small-molecule inhibitors of interaction between the BH3 domain and Bcl-xL

Degterev, A., Lugovskoy, A. A., Cardone, M. H., Mulley, B., Wagner, G., Mitchison, T. J., & Yuan, J. (2001) · Nature Cell Biology · doi:10.1038/35055085 · Cited by 550 · see citing works

Atomic structure of a thermostable subdomain of HIV-1 gp41

Tan, K., Liu, J.-H., Wang, J., Shen, S. S., & Lu, M. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.23.12303 · Cited by 532 · see citing works

MDM2 inhibitors for cancer therapy

Vassilev, L. T. (2007) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2006.11.002 · Cited by 532 · see citing works

Discovery of Small Molecules that Bind to K‐Ras and Inhibit Sos‐Mediated Activation

Sun, Q., Burke, J. P., Phan, J., Burns, M. C., Olejniczak, E. T., Waterson, A. G., Lee, T., Rossanese, O. W., & Fesik, S. W. (2012) · Angewandte Chemie International Edition · doi:10.1002/anie.201201358 · Cited by 490 · see citing works

Enfuvirtide: the first therapy to inhibit the entry of HIV-1 into host CD4 lymphocytes

Matthews, T., Salgo, M., Greenberg, M., Chung, J., DeMasi, R. A., & Bolognesi, D. P. (2004) · Nature Reviews Drug Discovery · doi:10.1038/nrd1331 · Cited by 466 · see citing works

The MCL-1 BH3 helix is an exclusive MCL-1 inhibitor and apoptosis sensitizer

Stewart, M. L., Fire, E., Keating, A. E., & Walensky, L. D. (2010) · Nature Chemical Biology · doi:10.1038/nchembio.391 · Cited by 418 · see citing works

Finding the sweet spot: the role of nature and nurture in medicinal chemistry

Hann, M. M., & Keserű, G. M. (2012) · Nature Reviews Drug Discovery · doi:10.1038/nrd3701 · Cited by 412 · see citing works

Protein clefts in molecular recognition and function.

Laskowski, R. A., Luscombe, N. M., Swindells, M. B., & Thornton, J. M. (1996) · PubMed Central · doi:10.1002/pro.5560051206 · Cited by 409 · see citing works

On-resin N-methylation of cyclic peptides for discovery of orally bioavailable scaffolds

White, T. R., Renzelman, C. M., Rand, A. C., Rezai, T., McEwen, C. M., Gelev, V., Turner, R. A., Linington, R. G., Leung, S. S. F., Kalgutkar, A. S. S., et al. (2011) · Nature Chemical Biology · doi:10.1038/nchembio.664 · Cited by 391 · 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

Translating p53 into the clinic

Cheok, C. F., Verma, C. S., Baselga, J., & Lane, D. P. (2011) · Nature Reviews Clinical Oncology · doi:10.1038/nrclinonc.2010.174 · Cited by 381 · see citing works

Bcl-2 inhibitors: small molecules with a big impact on cancer therapy

Vogler, M., Dinsdale, D. D., Dyer, M. J. S., & Cohen, G. M. (2008) · Cell Death and Differentiation · doi:10.1038/cdd.2008.137 · Cited by 359 · see citing works

Intramolecular hydrogen bonding to improve membrane permeability and absorption in beyond rule of five chemical space

Alex, A., Millan, D. S., Perez, M., Wakenhut, F., & Whitlock, G. A. (2011) · MedChemComm · doi:10.1039/c1md00093d · Cited by 334 · see citing works

Single Turn Peptide Alpha Helices with Exceptional Stability in Water

Shepherd, N. E., Hoang, H. N., Abbenante, G., & Fairlie, D. P. (2005) · Journal of the American Chemical Society · doi:10.1021/ja0456003 · Cited by 327 · see citing works

Helical β-Peptide Inhibitors of the p53-hDM2 Interaction

Kritzer, J. A., Lear, J. D., Hodsdon, M. E., & Schepartz, A. (2004) · Journal of the American Chemical Society · doi:10.1021/ja031625a · Cited by 314 · 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

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

An orthosteric inhibitor of the Ras-Sos interaction

Patgiri, A., Yadav, K. K., Arora, P. S., & Bar‐Sagi, D. (2011) · Nature Chemical Biology · doi:10.1038/nchembio.612 · Cited by 294 · see citing works

Contemporary strategies for the stabilization of peptides in the α-helical conformation

Henchey, L. K., Jochim, A. L., & Arora, P. S. (2008) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2008.08.019 · Cited by 289 · see citing works

On the nature of cavities on protein surfaces: Application to the identification of drug‐binding sites

Nayal, M., & Honig, B. H. (2006) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.20897 · Cited by 285 · see citing works

Inhibition of Protein−Protein Association by Small Molecules: Approaches and Progress

Toogood, P. L. (2002) · Journal of Medicinal Chemistry · doi:10.1021/jm010468s · Cited by 281 · see citing works

Structural and biological mimicry of protein surface recognition by α/β-peptide foldamers

Horne, W. S., Johnson, L. M., Ketas, T. J., Klasse, P. J., Lu, M., Moore, J. P., & Gellman, S. H. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0902663106 · Cited by 277 · see citing works

Oxindole-Based Inhibitors of Cyclin-Dependent Kinase 2 (CDK2): Design, Synthesis, Enzymatic Activities, and X-ray Crystallographic Analysis

Bramson, H. N., Corona, J. A., Davis, S. T., Dickerson, S. H., EDELSTEIN, M. P., Frye, S. V., Gampe, R. T., Harris, P. A., Hassell, A. M., Holmes, W. D., et al. (2001) · Journal of Medicinal Chemistry · doi:10.1021/jm010117d · Cited by 271 · see citing works

A Hydrogen Bond Surrogate Approach for Stabilization of Short Peptide Sequences in α-Helical Conformation

Patgiri, A., Jochim, A. L., & Arora, P. S. (2008) · Accounts of Chemical Research · doi:10.1021/ar700264k · Cited by 255 · 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

Development of a Potent Bcl-x L Antagonist Based on α-Helix Mimicry

Kutzki, O., Park, H. S., Ernst, J. T., Orner, B. P., Yin, H. H., & Hamilton, A. D. (2002) · Journal of the American Chemical Society · doi:10.1021/ja026861k · Cited by 253 · see citing works

Protein‐Reactive Natural Products

DRAHL, C., Cravatt, B. F., & Sorensen, E. J. (2005) · Angewandte Chemie International Edition · doi:10.1002/anie.200500900 · Cited by 251 · see citing works

Nonpeptidic Foldamers from Amino Acids: Synthesis and Characterization of 1,3-Substituted Triazole Oligomers

Angelo, N. G., & Arora, P. S. (2005) · Journal of the American Chemical Society · doi:10.1021/ja056406z · Cited by 227 · see citing works

Computational approaches to identifying and characterizing protein binding sites for ligand design

Henrich, S., Salo‐Ahen, O. M. H., Huang, B., Rippmann, F., Cruciani, G., & Wade, R. C. (2009) · Journal of Molecular Recognition · doi:10.1002/jmr.984 · Cited by 225 · see citing works

Chemical and structural lessons from recent successes in protein–protein interaction inhibition (2P2I)

Morelli, X., Bourgeas, R., & Roche, P. (2011) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2011.05.024 · Cited by 223 · see citing works

Beta-Strand Mimetics

Loughlin, W. A., Tyndall, J. D. A., Glenn, M. P., & Fairlie, D. P. (2004) · Chemical Reviews · doi:10.1021/cr040648k · Cited by 218 · see citing works

Efficient p53 Activation and Apoptosis by Simultaneous Disruption of Binding to MDM2 and MDMX

Hu, B., Gilkes, D. M., & Chen, J. (2007) · Cancer Research · doi:10.1158/0008-5472.can-07-1140 · Cited by 214 · see citing works

Disrupting protein–protein interactions with non-peptidic, small molecule α-helix mimetics

Cummings, C. G., & Hamilton, A. D. (2010) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2010.04.001 · Cited by 199 · see citing works

Short constrained peptides that inhibit HIV-1 entry

Sia, S. K., Carr, P. A., Cochran, A. G., Malashkevich, V. N., & Kim, P. S. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.232566599 · Cited by 195 · see citing works

Systematic Analysis of Helical Protein Interfaces Reveals Targets for Synthetic Inhibitors

Jochim, A. L., & Arora, P. S. (2010) · ACS Chemical Biology · doi:10.1021/cb1001747 · Cited by 191 · see citing works

Targeting protein–protein interactions: Lessons from p53/MDM2

Murray, J. K., & Gellman, S. H. (2007) · Biopolymers · doi:10.1002/bip.20741 · Cited by 186 · see citing works

Using a β‐Hairpin To Mimic an α‐Helix: Cyclic Peptidomimetic Inhibitors of the p53–HDM2 Protein–Protein Interaction

Fasan, R., Dias, R. L. A., Moehle, K., Zerbe, O., Vrijbloed, J. W., Obrecht, D., & Robinson, J. A. (2004) · Angewandte Chemie International Edition · doi:10.1002/anie.200353242 · Cited by 183 · see citing works

Downsizing human, bacterial, and viral proteins to short water-stable alpha helices that maintain biological potency

Harrison, R. S., Shepherd, N. E., Hoang, H. N., Ruiz-Gómez, G., Hill, T. A., Driver, R. W., Desai, V. S., Young, P. R., Abbenante, G., & Fairlie, D. P. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1002498107 · Cited by 182 · see citing works

Inhibiting HIV Fusion with a β-Peptide Foldamer

Stephens, O. M., Kim, S., Welch, B. D., Hodsdon, M. E., Kay, M. S., & Schepartz, A. (2005) · Journal of the American Chemical Society · doi:10.1021/ja053444+ · Cited by 174 · see citing works

Direct and selective small-molecule activation of proapoptotic BAX

Gavathiotis, E., Reyna, D. E., Bellairs, J. A., Leshchiner, E. S., & Walensky, L. D. (2012) · Nature Chemical Biology · doi:10.1038/nchembio.995 · Cited by 169 · see citing works

Enhanced Metabolic Stability and Protein‐Binding Properties of Artificial α Helices Derived from a Hydrogen‐Bond Surrogate: Application to Bcl‐xL

Wang, D., Liao, W., & Arora, P. S. (2005) · Angewandte Chemie International Edition · doi:10.1002/anie.200501603 · Cited by 156 · see citing works

Atomic Interactions and Profile of Small Molecules Disrupting Protein–Protein Interfaces: the TIMBAL Database

Higueruelo, A. P., Schreyer, A. M., Bickerton, G. R., Pitt, W. R., Groom, C. R., & Blundell, T. L. (2009) · Chemical Biology & Drug Design · doi:10.1111/j.1747-0285.2009.00889.x · Cited by 155 · see citing works

Universal Peptidomimetics

Ko, E., Liu, J., Pérez, L. M., Lu, G., Schaefer, A., & Burgess, K. (2010) · Journal of the American Chemical Society · doi:10.1021/ja1071916 · Cited by 151 · 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

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

Selection of gp41-mediated HIV-1 cell entry inhibitors from biased combinatorial libraries of non-natural binding elements.

Harrison, S. C., Ferrer, M., Kapoor, T. M., Strassmaier, T., Weissenhorn, W., Skehel, J. J., Oprian, D., Schreiber, S. L., & Wiley, D. C. (1999) · Nature Structural Biology · doi:10.1038/13324 · Cited by 138 · see citing works

Design of Cyclic Peptides That Bind Protein Surfaces with Antibody-Like Affinity

Millward, S. W., Fiacco, S. V., Austin, R. J., & Roberts, R. W. (2007) · ACS Chemical Biology · doi:10.1021/cb7001126 · Cited by 137 · see citing works

Inhibition of Hypoxia Inducible Factor 1—Transcription Coactivator Interaction by a Hydrogen Bond Surrogate α-Helix

Henchey, L. K., Kushal, S., Dubey, R., Chapman, R. N., Olenyuk, B. Z., & Arora, P. S. (2009) · Journal of the American Chemical Society · doi:10.1021/ja9082864 · Cited by 136 · see citing works

Design, synthesis, and crystal structure of a pyrrolinone-based peptidomimetic possessing the conformation of a .beta.-strand: potential application to the design of novel inhibitors of proteolytic enzymes

Smith, A. B., Keenan, T. P., Holcomb, R. C., Sprengeler, P. A., Guzman, M. C., Wood, J. L., Carroll, P. J., & Hirschmann, R. F. (1992) · Journal of the American Chemical Society · doi:10.1021/ja00052a093 · Cited by 136 · see citing works

Small molecules that bind the inner core of gp41 and inhibit HIV envelope-mediated fusion

Frey, G., Rits‐Volloch, S., Zhang, X.-Q., Schooley, R. T., Chen, B., & Harrison, S. C. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0601036103 · Cited by 135 · see citing works

Assessment of helical interfaces in protein–protein interactions

Jochim, A. L., & Arora, P. S. (2009) · Molecular BioSystems · doi:10.1039/b903202a · Cited by 134 · see citing works

Structure-based Mutagenesis Reveals Distinct Functions for Ras Switch 1 and Switch 2 in Sos-catalyzed Guanine Nucleotide Exchange

Hall, B. E., Yang, S. S., Boriack‐Sjodin, P. A., Kuriyan, J., & Bar‐Sagi, D. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m101727200 · Cited by 132 · 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

Design and synthesis of α-helical peptides and mimetics

Garner, J., & Harding, M. M. (2007) · Organic & Biomolecular Chemistry · doi:10.1039/b710425a · Cited by 126 · see citing works

Atomic Analysis of Protein-Protein Interfaces with Known Inhibitors: The 2P2I Database

Bourgeas, R., Basse, M.-J., Morelli, X., & Roche, P. (2010) · PLoS ONE · doi:10.1371/journal.pone.0009598 · Cited by 126 · 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 119 · see citing works

Solution- and Solid-Phase Synthesis of Triazole Oligomers That Display Protein-Like Functionality

Angelo, N. G., & Arora, P. S. (2007) · The Journal of Organic Chemistry · doi:10.1021/jo701292h · Cited by 112 · see citing works

High Specificity in Protein Recognition by Hydrogen‐Bond‐Surrogate α‐Helices: Selective Inhibition of the p53/MDM2 Complex

Henchey, L. K., Porter, J. R., Ghosh, I., & Arora, P. S. (2010) · ChemBioChem · doi:10.1002/cbic.201000378 · Cited by 102 · see citing works

Minimalist and universal peptidomimetics

Ko, E., Liu, J., & Burgess, K. (2011) · Chemical Society Reviews · doi:10.1039/c0cs00218f · Cited by 99 · 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

PocketQuery: protein-protein interaction inhibitor starting points from protein-protein interaction structure

Koes, D. R., & Camacho, C. J. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks336 · Cited by 91 · see citing works

Inhibition of HIV‐1 Fusion by Hydrogen‐Bond‐Surrogate‐Based α Helices

Wang, D., Lu, M., & Arora, P. S. (2008) · Angewandte Chemie International Edition · doi:10.1002/anie.200704227 · Cited by 87 · see citing works

Helix-mediated protein–protein interactions as targets for intervention using foldamers

Edwards, T. A., & Wilson, A. J. (2011) · Amino Acids · doi:10.1007/s00726-011-0880-8 · Cited by 82 · see citing works

Modulating Protein–Protein Interactions with Small Molecules: The Importance of Binding Hotspots

Thangudu, R. R., Bryant, S. H., Panchenko, A. R., & Madej, T. (2012) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.12.026 · Cited by 71 · see citing works

β Strand Peptidomimetics as Potent PDZ Domain Ligands

Hammond, M. C., Harris, B. Z., Lim, W. A., & Bartlett, P. A. (2006) · Chemistry & Biology · doi:10.1016/j.chembiol.2006.11.010 · 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

Paralog-Selective Ligands for Bcl-2 Proteins

Gemperli, A. C., Rutledge, S. E., Maranda, A. M., & Schepartz, A. (2005) · Journal of the American Chemical Society · doi:10.1021/ja0441211 · Cited by 65 · see citing works

HIV-1 gp41 Fusion Intermediate: A Target for HIV Therapeutics

Pan, C., Liu, S., & Jiang, S. (2010) · Journal of the Formosan Medical Association · doi:10.1016/s0929-6646(10)60029-0 · Cited by 65 · see citing works

Methods for the synthesis of macrocycle libraries for drug discovery

Terrett, N. K. (2010) · Drug Discovery Today Technologies · doi:10.1016/j.ddtec.2010.06.002 · Cited by 61 · see citing works

Small-molecule inhibitor starting points learned from protein–protein interaction inhibitor structure

Koes, D. R., & Camacho, C. J. (2011) · Bioinformatics · doi:10.1093/bioinformatics/btr717 · Cited by 61 · see citing works

Structural Signatures of Enzyme Binding Pockets from Order-Independent Surface Alignment: A Study of Metalloendopeptidase and NAD Binding Proteins

Dundas, J., Adamian, L., & Liang, J. (2010) · Journal of Molecular Biology · doi:10.1016/j.jmb.2010.12.005 · Cited by 52 · see citing works

The Overlap of Small Molecule and Protein Binding Sites within Families of Protein Structures

Davis, F., & Sali, A. (2010) · PLoS Comput. Biol. · doi:10.1371/journal.pcbi.1000668 · Cited by 50 · 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

Synthesis and helical structure of lactam bridged BH3 peptides derived from pro-apoptotic Bcl-2 family proteins

Yang, B. S., Liu, D., & Huang, Z. (2004) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2003.09.101 · Cited by 43 · see citing works

Broad Distribution of Energetically Important Contacts across an Extended Protein Interface

Johnson, L. M., Horne, W. S., & Gellman, S. H. (2011) · Journal of the American Chemical Society · doi:10.1021/ja203358t · Cited by 41 · see citing works

Discovery of a novel class of 2-aminopyrimidines as CDK1 and CDK2 inhibitors

Lee, J., Kim, K.-H., & Jeong, S. (2011) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2011.05.081 · Cited by 35 · see citing works

A Notch above other inhibitors

Arora, P. S., & Ansari, A. Z. (2009) · Nature · doi:10.1038/462171a · Cited by 27 · see citing works

The Trp Cage Motif as a Scaffold for the Display of a Randomized Peptide Library on Bacteriophage T7

Herman, R. E., Badders, D., Fuller, M., Makienko, E. G., Houston, M. E., Quay, S. C., & Johnson, P. H. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m610722200 · Cited by 27 · see citing works

Evolution of Class-Specific Peptides Targeting a Hot Spot of the Gαs Subunit

Austin, R. J., Ja, W. W., & Roberts, R. W. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.01.032 · Cited by 25 · see citing works

Functionalized Analogues of an Unnatural Amino Acid that Mimics a Tripeptide β-Strand

Khasanova, T. V., Khakshoor, O., & Nowick, J. S. (2008) · Organic Letters · doi:10.1021/ol8021897 · Cited by 18 · 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

How proteins bind macrocycles

Villar, E. A., Beglov, D., Chennamadhavuni, S., Porco, J. A. J., Kozakov, D., Vajda, S., & Whitty, A. (2014) · Nature Chemical Biology · doi:10.1038/nchembio.1584 · Cited by 401 · 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

Comparative ACE2 variation and primate COVID-19 risk

Melin, A. D., Janiak, M. C., Marrone, F., Arora, P. S., & Higham, J. P. (2020) · Communications Biology · doi:10.1038/s42003-020-01370-w · Cited by 178 · see citing works

Flexibility and small pockets at protein–protein interfaces: New insights into druggability

Jubb, H. C., Blundell, T. L., & Ascher, D. B. (2015) · Progress in Biophysics and Molecular Biology · doi:10.1016/j.pbiomolbio.2015.01.009 · Cited by 154 · see citing works

Inhibitor of MYC identified in a Kröhnke pyridine library

Hart, J. R., Garner, A. L., Yu, J., Ito, Y., Sun, M., Ueno, L. A., Rhee, J., Baksh, M. M., Stefan, E., Hartl, M., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1319488111 · Cited by 150 · see citing works

Peptide-based inhibitors of protein–protein interactions: biophysical, structural and cellular consequences of introducing a constraint

Wang, H., Dawber, R. S., Zhang, P., Walko, M., Wilson, A. J., & Wang, X. (2021) · Chemical Science · doi:10.1039/d1sc00165e · Cited by 138 · see citing works

Anatomy of β-Strands at Protein–Protein Interfaces

Watkins, A. M., & Arora, P. S. (2014) · ACS Chemical Biology · doi:10.1021/cb500241y · 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

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

The Extended Transmembrane Orai1 N-terminal (ETON) Region Combines Binding Interface and Gate for Orai1 Activation by STIM1

Derler, I., Plenk, P., Fahrner, M., Muik, M., Jardín, I., Schindl, R., Gruber, H. J., Groschner, K., & Romanin, C. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.501510 · Cited by 111 · see citing works

New Frontiers in Druggability

Kozakov, D., Hall, D. R., Napoleon, R. L., Yueh, C., Whitty, A., & Vajda, S. (2015) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5b00586 · Cited by 111 · see citing works

Using Peptidomimetics and Constrained Peptides as Valuable Tools for Inhibiting Protein–Protein Interactions

Robertson, N., & Spring, D. R. (2018) · Molecules · doi:10.3390/molecules23040959 · Cited by 112 · see citing works

iPPI-DB: a manually curated and interactive database of small non-peptide inhibitors of protein–protein interactions

Labbé, C. M., Laconde, G., Kuenemann, M. A., Villoutreix, B. O., & Sperandio, O. (2013) · Drug Discovery Today · doi:10.1016/j.drudis.2013.05.003 · Cited by 104 · see citing works

Protein Domain Mimics as Modulators of Protein–Protein Interactions

Sawyer, N., Watkins, A. M., & Arora, P. S. (2017) · Accounts of Chemical Research · doi:10.1021/acs.accounts.7b00130 · Cited by 103 · see citing works

Alternative modulation of protein–protein interactions by small molecules

Fischer, G., Rossmann, M., & Hyvönen, M. (2015) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2015.04.006 · Cited by 97 · see citing works

The design and development of covalent protein-protein interaction inhibitors for cancer treatment

Cheng, S.-S., Yang, G.-J., Wang, W., Leung, C.-H., & Ma, D.-L. (2020) · Journal of Hematology & Oncology · doi:10.1186/s13045-020-00850-0 · Cited by 98 · see citing works

Direct Targeting of Rab‐GTPase–Effector Interactions

Spiegel, J., Cromm, P. M., Itzen, A., Goody, R. S., Grossmann, T. N., & Waldmann, H. (2014) · Angewandte Chemie International Edition · doi:10.1002/anie.201308568 · Cited by 86 · see citing works

Macrocyclic Control in Helix Mimetics

Guarracino, D. A., Riordan, J. A., Barreto, G. M., Oldfield, A. L., Kouba, C. M., & Agrinsoni, D. (2019) · Chemical Reviews · doi:10.1021/acs.chemrev.8b00623 · Cited by 86 · see citing works

Peptide to Peptoid Substitutions Increase Cell Permeability in Cyclic Hexapeptides

Schwochert, J. A., Turner, R. A., Thang, M., Berkeley, R. F., Ponkey, A. R., Rodriguez, K. M., Leung, S. S. F., Khunte, B., Goetz, G. H., Limberakis, C., et al. (2015) · Organic Letters · doi:10.1021/acs.orglett.5b01162 · Cited by 85 · see citing works

Peptidomimetics: A Synthetic Tool for Inhibiting Protein–Protein Interactions in Cancer

Mabonga, L., & Kappo, A. P. (2019) · International Journal of Peptide Research and Therapeutics · doi:10.1007/s10989-019-09831-5 · Cited by 78 · see citing works

Protein–Protein Interactions Mediated by Helical Tertiary Structure Motifs

Watkins, A. M., Wuo, M. G., & Arora, P. S. (2015) · Journal of the American Chemical Society · doi:10.1021/jacs.5b05527 · Cited by 77 · see citing works

Structure Based Design of Non-Natural Peptidic Macrocyclic Mcl-1 Inhibitors

Johannes, J. W., Bates, S. M., Beigie, C., Belmonte, M. A., Breen, J. N., Cao, S., Centrella, P. A., Clark, M., Cuozzo, J. W., Dumelin, C. E., et al. (2016) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.6b00464 · Cited by 67 · see citing works

AlphaSpace: Fragment-Centric Topographical Mapping To Target Protein–Protein Interaction Interfaces

Rooklin, D. W., Wang, C., Katigbak, J., Arora, P. S., & Zhang, Y. (2015) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.5b00103 · Cited by 66 · see citing works

Covalent peptides and proteins for therapeutics

Berdan, V. Y., Klauser, P. C., & Wang, L. (2020) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2020.115896 · Cited by 59 · see citing works

Crystal Structures of Stapled and Hydrogen Bond Surrogate Peptides Targeting a Fully Buried Protein–Helix Interaction

Douse, C. H., Maas, S. J., Thomas, J. C., Garnett, J. A., Sun, Y., Cota, E., & Tate, E. W. (2014) · ACS Chemical Biology · doi:10.1021/cb500271c · Cited by 56 · see citing works

Bridged bicyclic peptides as potential drug scaffolds: synthesis, structure, protein binding and stability

Bartoloni, M., Jin, X., Marcaida, M. J., Banha, J., Bonaventura, I. D., Bongoni, S., Bartho, K., Gräbner, O., Sefkow, M., Darbre, T., et al. (2015) · Chemical Science · doi:10.1039/c5sc01699a · Cited by 46 · see citing works

Small‐Molecule and Peptide Inhibitors of the Pro‐Survival Protein Mcl‐1

Beekman, A. M., & Howell, L. A. (2015) · ChemMedChem · doi:10.1002/cmdc.201500497 · Cited by 42 · see citing works

High-resolution structures of a heterochiral coiled coil

Mortenson, D. E., Steinkruger, J. D., Kreitler, D. F., Perroni, D. V., Sorenson, G. P., Huang, L., Mittal, R., Yun, H. G., Travis, B. R., Mahanthappa, M. K., et al. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1507918112 · Cited by 44 · see citing works

From Concepts to Inhibitors: A Blueprint for Targeting Protein–Protein Interactions

Hong, S. H., Nguyễn, T. T., Ongkingco, J. F., Nazzaro, A., & Arora, P. S. (2025) · Chemical Reviews · doi:10.1021/acs.chemrev.5c00046 · Cited by 44 · see citing works

HippDB: a database of readily targeted helical protein–protein interactions

Bergey, C. M., Watkins, A. M., & Arora, P. S. (2013) · Bioinformatics · doi:10.1093/bioinformatics/btt483 · Cited by 38 · see citing works

The oncogenic potential of small nuclear ribonucleoprotein polypeptide G: a comprehensive and perspective view.

Mabonga, L., & Kappo, A. P. (2019) · PubMed Central · Cited by 29 · 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

Protein/peptide secondary structural mimics: design, characterization, and modulation of protein–protein interactions

Wang, Z. A., Ding, X., Tian, C., & Zheng, J. (2016) · RSC Advances · doi:10.1039/c6ra13976k · Cited by 22 · see citing works

Diversity-Oriented Synthesis of a Library of Star-Shaped 2H-Imidazolines

Yu, X., Guttenberger, N., Fuchs, E., Peters, M., Weber, H., & Breinbauer, R. (2015) · ACS Combinatorial Science · doi:10.1021/acscombsci.5b00107 · Cited by 21 · see citing works

RNA Polymerase Tags To Monitor Multidimensional Protein–Protein Interactions Reveal Pharmacological Engagement of Bcl-2 Proteins

Pu, J., Dewey, J. A., Hadji, A., LaBelle, J. L., & Dickinson, B. C. (2017) · Journal of the American Chemical Society · doi:10.1021/jacs.7b06152 · Cited by 20 · see citing works

Conformational Strain of Macrocyclic Peptides in Ligand–Receptor Complexes Based on Advanced Refinement of Bound-State Conformers

Brueckner, A. C., Deng, Q., Cleves, A. E., Lesburg, C. A., Alvarez, J. C., Reibarkh, M., Sherer, E. C., & Jain, A. N. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.0c02159 · Cited by 18 · see citing works

Advances in the synthesis of glycosidic macrolides: clavosolides A–D and cyanolide A

Lee, K., Lanier, M. L., Kwak, J., Kim, H., & Hong, J. (2016) · Natural Product Reports · doi:10.1039/c6np00073h · Cited by 18 · see citing works

Synthesis of Hydrogen‐Bond Surrogate α‐Helices as Inhibitors of Protein‐Protein Interactions

Miller, S. E., Thomson, P. F., & Arora, P. S. (2014) · Current Protocols in Chemical Biology · doi:10.1002/9780470559277.ch130202 · Cited by 17 · see citing works

Investigation and Prediction of Human Interactome Based on Quantitative Features

Pan, X., Zeng, T., Zhang, Y., Chen, L., Feng, K., Huang, T., & Cai, Y. (2020) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2020.00730 · Cited by 15 · see citing works

Direkte Modulation von Rab‐GTPase‐Effektor‐Wechselwirkungen

Spiegel, J., Cromm, P. M., Itzen, A., Goody, R. S., Grossmann, T. N., & Waldmann, H. (2014) · Angewandte Chemie · doi:10.1002/ange.201308568 · Cited by 13 · see citing works

Variation in predicted COVID‐19 risk among lemurs and lorises

Melin, A. D., Orkin, J. D., Janiak, M. C., Valenzuela, A., Kuderna, L. F. K., Marrone, F., Ramangason, H., Horvath, J. E., Roos, C., Kitchener, A. C., et al. (2021) · American Journal of Primatology · doi:10.1002/ajp.23255 · Cited by 12 · see citing works

Computer aided design and NMR characterization of an oligopeptide targeting the Ebola virus VP24 protein

Dapiaggi, F., Pieraccini, S., Potenza, D., Vasile, F., Macut, H., Pellegrino, S., Aliverti, A., & Sironi, M. (2017) · New Journal of Chemistry · doi:10.1039/c6nj04014d · Cited by 11 · see citing works

Synthesis of Chiral Alkenyl Cyclopropane Amino Acids for Incorporation into Stapled Peptides

Yuen, T. Y., Brown, C. J., Tan, Y. S., & Johannes, C. W. (2019) · The Journal of Organic Chemistry · doi:10.1021/acs.joc.9b02659 · Cited by 9 · see citing works

Structure–activity relationship of ipglycermide binding to phosphoglycerate mutases

Wiedmann, M. M., Dranchak, P. K., Aitha, M., Queme, B., Collmus, C. D., Kashipathy, M. M., Kanter, L., Lamy, L., Rogers, J. M., Tao, D., et al. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.100628 · Cited by 8 · see citing works

Peptidomimetics II

Lubell, W. D. (2016) · Topics in heterocyclic chemistry · doi:10.1007/978-3-319-49124-0 · Cited by 7 · see citing works

Conformational Switching in Heterochiral α,β2,3‐Hybrid Peptides in Response to Solvent Polarity

Dhayalan, B., & Muraleedharan, K. M. (2015) · European Journal of Organic Chemistry · doi:10.1002/ejoc.201500534 · Cited by 6 · see citing works

Exploration of α/β/γ-peptidomimetics design for BH3 helical domains

Shin, Y., & Yang, H. (2021) · Chemical Communications · doi:10.1039/d1cc05758h · Cited by 4 · see citing works

Influence of Amino Acid Mutations and Small Molecules on Targeted Inhibition of Proteins Involved in Cancer

Kanakaveti, V., Anoosha, P., Sakthivel, R., Rayala, S. K., & Gromiha, M. M. (2019) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026619666190304143354 · Cited by 3 · see citing works

Exploiting endogenous opioids: Lessons learned from endomorphin 2 in the female rat

Gintzler, A. R., Liu, N., Storman, E. M., & Wessendorf, M. W. (2018) · Peptides · doi:10.1016/j.peptides.2018.12.002 · Cited by 3 · see citing works

Oligooxopiperazines as Topographical Helix Mimetics

Lao, B. B., & Arora, P. S. (2016) · Topics in heterocyclic chemistry · doi:10.1007/7081_2015_195 · Cited by 1 · see citing works

Future of Medicinal Chemistry: Next-Generation Therapeutics

Tsomaia, N., Ufret, M. D. L., Bhat, A., & Nakhlé, J. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-409547-2.12294-2 · Cited by 1 · see citing works

Detection of the in vitro modulation of Plasmodium falciparum Arf1 by Sec7 and ArfGAP domains using a colorimetric plate-based assay

Swart, T., Khan, F. D., Ntlantsana, A., Laming, D., Veale, C. G. L., Przyborski, J. M., Edkins, A. L., & Hoppe, H. C. (2020) · Scientific Reports · doi:10.1038/s41598-020-61101-3 · Cited by 1 · see citing works

Designing Antiviral Substances Targeting the Ebola Virus Viral Protein 24

Dapiaggi, F., Pieraccini, S., Potenza, D., Vasile, F., & Podlipnik, Č. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-814966-9.00009-3 · Cited by 1 · see citing works

Conversion of 3,6‐O‐Dimethylfluorescein to Fluorescein‐Based Xanthylium Derivative: Characterization and Covalent Attachment to Bovine Serum Albumin

Kalhor, H. R., & Rezaei, M. (2019) · ChemistrySelect · doi:10.1002/slct.201902296 · Cited by 1 · see citing works

Synthesis of C2-symmetric carbohydrate-based macrocycles by introduction of methylene/p-xylene linkers

Hudait, N., Bhuyan, S., Roy, B., & Sengupta, J. (2022) · ARKIVOC · doi:10.24820/ark.5550190.p011.716 · Cited by 1 · see citing works

A Structural View on Druggability

Egner, U., & Hillig, R. C. (2020) · Wiley eBooks · doi:10.1002/9781118681121.ch2 · Cited by 1 · see citing works

187 Plucking the high hanging fruit: a systematic approach for targeting protein interfaces

Arora, P. S. (2013) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2013.786429

In Silico Approaches Assisting the Rational Design of Low Molecular Weight Protein–Protein Interaction Modulators

Villoutreix, B. O., Kuenemann, M. A., Lagorce, D., Spérandio, O., & Miteva, M. A. (2015) · CRC Press eBooks · doi:10.1201/b18799-21

Tailoring Hit Identification and Qualification Methods for Targeting Protein–Protein Interactions

Walse, B., Turnbull, A. P., & Boyd, S. M. (2017) · doi:10.1002/9781119099512.ch3

PROTEINATOR: Web-UI exploring repurposing hypotheses of PROTEIN InhibiTORs based on protein interactionsPreprint

Tangadu, S., Shankar, S., Varanasi, B. V., & Athri, P. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/667329

Hydrogen Bond Surrogate Stabilized Helices as Protein–Protein Interaction Inhibitors

Yoo, D. Y., & Arora, P. S. (2020) · Royal Society of Chemistry eBooks · doi:10.1039/9781788016544-00124

Inhibition d'interactions protéine-protéine par des foldamères mixtes oligoamide/oligourée

Cussol, L. (2018) · theses.fr (ABES) · doi:10.70675/62850694z3137z483azba4cz469886420469

Synthesis and conformational analysis of peptidomimetic foldamers containing diaza-peptide units : application in protein-protein interactions

Shi, C. (2022) · theses.fr (ABES) · doi:10.70675/1f5ac7fdz098fz4bf5z9333z19213aedfbe2

Protein–protein interaction inhibitors in the human proteome: lessons from 117 targeted interactions

Hyde, E., & Beekman, A. M. (2026) · RSC Medicinal Chemistry · doi:10.1039/d6md00552g

Targeting Aberrant Protein-Protein Interactions in Cancer and Neurodegenerative Diseases

Ball, T. D. (2025) · doi:10.56902/etdcrp.2025.222

BindingDB Entry 50019097: Structure Based Design of Non-Natural Peptidic Macrocyclic Mcl-1 Inhibitors.

BindingDB (2024) · UC San Diego · doi:10.7270/q2vd73r8

BindingDB Entry 50006473: New Frontiers in Druggability.

BindingDB (2020) · UC San Diego · doi:10.7270/q24t6nc6

Modeling and Design of Peptidomimetics to Modulate Protein–Protein Interactions

Watkins, A. M., Bonneau, R., & Arora, P. S. (2017) · Methods in molecular biology · doi:10.1007/978-1-4939-6798-8_17 · Cited by 4 · see citing works

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

Protein Surface Recognition by Synthetic Molecules

Samanta, K., Jana, P., Hirschhäuser, C., & Schmuck, C. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-409547-2.12533-8 · Cited by 1 · see citing works

Target-directed synthesis of protein-protein interaction inhibitors

Sharma, S. (2024) · doi:10.25560/131040

Structure-based inhibition of protein–protein interactions

Watkins, A. M., & Arora, P. S. (2014) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2014.09.047 · Cited by 52 · see citing works