Small molecules, big targets: drug discovery faces the protein–protein interaction challenge

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

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Selective inhibition of BET bromodomains

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New Substructure Filters for Removal of Pan Assay Interference Compounds (PAINS) from Screening Libraries and for Their Exclusion in Bioassays

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The STRING database in 2011: functional interaction networks of proteins, globally integrated and scored

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ABT-199, a potent and selective BCL-2 inhibitor, achieves antitumor activity while sparing platelets

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Principles of protein-protein interactions

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The Future of Peptide‐based Drugs

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

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

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Anatomy of hot spots in protein interfaces

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How do you mend inactive tumor suppressor mutants? You glue them!

Hata, A., & Lagna, G. (2021) · Cell chemical biology · doi:10.1016/j.chembiol.2021.04.023 · Cited by 3

Development of cyclic peptides that can be administered orally to inhibit disease targets

Merz, M. L., & Heinis, C. (2023) · Nature Chemical Biology · doi:10.1038/s41589-023-01505-0 · Cited by 3

Predicting the Dynamic Interaction of Intrinsically Disordered Proteins

Zheng, Y., Li, Q., Freiberger, M. I., Song, H., Hu, G., Zhang, M., Gu, R., & Li, J. (2024) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.4c00930 · Cited by 3

Applications of Molecular Dynamics Simulation and MM-PBSA Methods in Discovery of Veterinary Drugs

Kumar, N., Mandal, P., Kumar, B., Rani, P., & Singh, D. V. (2025) · Springer eBooks · doi:10.1007/978-981-97-7395-4_14 · Cited by 3

The neural stem cell gene PAFAH1B1 controls cell cycle progression, DNA integrity, and paclitaxel sensitivity of triple-negative breast cancer cells

Majmudar, P. R., & Keri, R. A. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.110235 · Cited by 3

Bibliometrics Analysis and Knowledge Mapping of Fragment-Based Drug Design Research: Trends from 2015 to 2024

He, C., Zhang, J., Zhang, R., Liu, L., Luo, J., Zhang, W., & Fang, B. (2025) · Drug Design Development and Therapy · doi:10.2147/dddt.s518489 · Cited by 3

Quantum mechanics-driven structure-activity relationship study of PEX5-PEX14 protein-protein interaction inhibitors based on a dibenzo[b,e]azepin-6(6H)-one scaffold

Nowacki, M., Menezes, F., Pykacz, E., Popiołek, M., Napolitano, V., Krishna, C. K., Kalel, V. C., Erdmann, R., Fröhlich, T., Plettenburg, O., et al. (2025) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2025.117979 · Cited by 4

Revisiting Protein–Protein Docking: A Systematic Evaluation Framework

Jiang, L., Zhang, K., Zhu, K., Wang, Y., Kang, Y., & Hou, T. (2025) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.5c01399 · Cited by 3

Computer-Aided Drug Design for the Identification of Novel Antischistosomal Compounds

Viana, J. D. O., Scotti, L., & Scotti, L. (2020) · Methods in molecular biology · doi:10.1007/978-1-0716-0635-3_2 · Cited by 3

Towards identification of protein–protein interaction stabilizers via inhibitory peptide-fragment hybrids using templated fragment ligation

Srdanović, S., Hegedüs, Z., Warriner, S. L., & Wilson, A. J. (2022) · RSC Chemical Biology · doi:10.1039/d2cb00025c · Cited by 3

Fragment hopping protocol for the design of small-molecule protein–protein interaction inhibitors

Kell, S. R., Wang, Z., & Ji, H. (2022) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2022.116879 · Cited by 3

Development of a novel pharmacophore model to screen specific inhibitors for the serine-threonine protein phosphatase calcineurin

Mukherjee, A., Cuanalo-Contreras, K., Sood, A., & Soto, C. A. (2022) · Biochemistry and Biophysics Reports · doi:10.1016/j.bbrep.2022.101311 · Cited by 3

FUNDAMENTALS OF PROTEIN-PROTEIN INTERACTIONS AND THEIR METHODS OF CHARACTERIZATION

Audah, K. A. (2021) · Bioinformatics and Biomedical Research Journal · doi:10.11594/bbrj.04.02.04 · Cited by 3

Unveiling the biological interface of protein complexes by mass spectrometry‐coupled methods

Shin, G., & Lim, S. I. (2022) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.26459 · Cited by 3

Atomic‐level thermodynamics analysis of the binding free energy of SARS‐CoV ‐2 neutralizing antibodies

Lee, J., Seok, C., Ham, S., & Chong, S. (2022) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.26458 · Cited by 2

Reaction Course Dependent Regiospecific Transformation of 4‐Azido‐Coumarin into Coumarin C3‐C4 Fused Imidazole and 5‐Substituted‐1,4‐Benzodiazepine Scaffolds

Nagamani, V., & Sriraghavan, K. (2024) · European Journal of Organic Chemistry · doi:10.1002/ejoc.202400575 · Cited by 3

Using site-directed mutagenesis to further the understanding of insulin receptor-insulin like growth factor-1 receptor heterodimer structure

Turvey, S., Muench, S. P., Issad, T., Fishwick, C. W. G., Kearney, M. T., & Simmons, K. J. (2024) · Growth Hormone & IGF Research · doi:10.1016/j.ghir.2024.101607 · Cited by 3

The potential of TRP channels as new prognostic and therapeutic targets against prostate cancer progression

Chinigò, G., Ruffinatti, F. A., & Munaron, L. (2024) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2024.189226 · Cited by 3

Cell-permeated peptide P-T3H2 inhibits malignancy on hepatocellular carcinoma through stabilizing HNF4α protein

Wu, S., Xiao, M., Liu, F., Hong, H.-Y., Ding, C., Zhang, X., & Xie, W. (2024) · Discover Oncology · doi:10.1007/s12672-024-01661-2 · Cited by 4

Prediction of protein interactions with function in protein (de-)phosphorylation

Vagiona, A.-C., Notopoulou, S., Zdráhal, Z., Gonçalves-Kulik, M., Petrakis, S., & Andrade-Navarro, M. A. (2025) · PLoS ONE · doi:10.1371/journal.pone.0319084 · Cited by 4

Fishing for covalent peptides

Jin, G. (2025) · Nature Chemical Biology · doi:10.1038/s41589-025-01903-6 · Cited by 3

In silico ligand‐based modeling of hBACE ‐1 inhibitors

Subramanian, G., & Poda, G. I. (2017) · Chemical Biology & Drug Design · doi:10.1111/cbdd.13147 · Cited by 3

Integrating Experimental and In Silico HTS in the Discovery of Inhibitors of Protein–Nucleic Acid Interactions

Li, Q., Constantino, L. F. D. S., & Spies, M. (2018) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2017.11.036 · Cited by 3

A Case Study on the Keap1 Interaction with Peptide Sequence Epitopes Selected by the Peptidomic mRNA Display

Hirose, H., Hideshima, T., Katoh, T., & Suga, H. (2019) · ChemBioChem · doi:10.1002/cbic.201900039 · Cited by 3

Artificial Intelligence Steering Molecular Therapy in the Absence of Information on Target Structure and Regulation

Fernández, A. (2019) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.9b00651 · Cited by 3

Evaluating domains associated with economic empowerment of small-scale female agro-processors in South Africa

Manasoe, B., Mmbengwa, V. M., & Lekunze, J. N. (2022) · Journal of Agribusiness and Rural Development · doi:10.17306/j.jard.2022.01533 · Cited by 3

Prediction and analysis of hot region in protein-protein interactions

Lin, X., & Zhang, X. (2016) · IEEE International Conference on Bioinformatics and Biomedicine (BIBM) · doi:10.1109/bibm.2016.7822758 · Cited by 3

Using Fragment Based Drug Discovery to Target Epigenetic Regulators in Cancer

Young, D. W. (2017) · MOJ Bioequivalence & Bioavailability · doi:10.15406/mojbb.2017.04.00062 · Cited by 3

High-throughput screening for intrinsically disordered proteins by using biophysical methods

Abián, O., Vega, S., Neira, J. L., & Velázquez‐Campoy, A. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-819132-3.00017-8 · Cited by 3

P53-MDM2 interaction monitoring and inhibitors potency evaluation based on CRISPR-Cas12a sensing platform

Zhu, M., Pan, J., Xu, M., Cao, J., Zhu, Y., Zhu, H., Su, G., & Yu, Y. (2022) · Sensors and Actuators B Chemical · doi:10.1016/j.snb.2022.131710 · Cited by 3

Tagging Proteins with Fluorescent Reporters Using the CRISPR/Cas9 System and Double-Stranded DNA Donors

Geny, S., Pichard, S., Brion, A., Renaud, J.-B., Jacquemin, S., Concordet, J., & Poterszman, A. (2020) · Methods in molecular biology · doi:10.1007/978-1-0716-1126-5_3 · Cited by 3

Protein–Protein Interactions and Genetic Disease

Brender, J., & Zhang, Y. (2017) · Encyclopedia of Life Sciences · doi:10.1002/9780470015902.a0026856 · Cited by 3

Predicting PROTAC-targeted Degradation and Designing Androgen Receptor Degraders with AiPROTACPreprint

Zhang, L., Sun, R., Li, X., Ren, C., Long, Y., Tan, W., Wang, X., Zou, K., Yang, X., Wu, M., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.02.26.640266 · Cited by 5

Targeting small GTPases and their downstream pathways with intracellular macromolecule binders to define alternative therapeutic strategies in cancer

Sorbara, M., & Béry, N. (2021) · Biochemical Society Transactions · doi:10.1042/bst20201059 · Cited by 2

α-Hydrazino Acid Insertion Governs Peptide Organization in Solution by Local Structure Ordering

Kavčič, L., Ilc, G., Wang, B., Vlahoviček‐Kahlina, K., Jerić, I., & Plavec, J. (2024) · ACS Omega · doi:10.1021/acsomega.4c00804 · Cited by 2

Composition effects on the self-aggregation of phenylalanine-rich oligopeptides revealed by atomic force microscopy

Liu, S., Wang, R., Wang, X., Yu, L., & Wang, C. (2024) · Colloid & Polymer Science · doi:10.1007/s00396-024-05300-8 · Cited by 2

Computational Evaluation of Fusarium nygamai Compounds as AcrD Efflux Pump Protein Inhibitors of Salmonella Typhimurium

Garrido-Palazuelos, L. I., Aguirre-Sánchez, J. R., Sandoval-González, M. F., Mukhtar, M., Guerra-Meza, O., & Khan, H. A. (2024) · Molecular Biotechnology · doi:10.1007/s12033-024-01329-w · Cited by 2

5-(3-( N -(Carboxymethyl)naphthalene-2-sulfonamido)phenyl)-1-ethyl-1 H -pyrrole-2-carboxylic acid as a Keap1–Nrf2 inhibitor for cerebral ischemia/reperfusion injury treatment

Cairang, N., Wu, Y., Zhi, S., Tang, J., Tie, X., Zhan, D., Lu, G., Shi, Y., & Zhao, Q. (2025) · RSC Advances · doi:10.1039/d4ra06512c · Cited by 2

High-Yielding Regioselective Synthesis of Coumarin/2-Quinolone C3–C4 Fused 5-Substituted-1,4-Benzodiazepine Scaffolds

Nagamani, V., & Sriraghavan, K. (2025) · Synthesis · doi:10.1055/a-2661-4104 · Cited by 2

Alphappimi: a comprehensive deep learning framework for predicting PPI-modulator interactions

Liu, D., Song, T., Wang, S., Li, X., Han, P., Wang, J., & Wang, S. (2025) · Journal of Cheminformatics · doi:10.1186/s13321-025-01077-2 · Cited by 2

Molecular basis of the activity of a photoswitchable histone deacetylase inhibitor

Queizán, M., Teijeira, M., & Hermida‐Ramón, J. M. (2025) · Journal of Molecular Liquids · doi:10.1016/j.molliq.2025.128488 · Cited by 2

Inferred global dense residue transition graphs from primary structure sequences enable protein interaction prediction via directed graph convolutional neural networks

Ebeid, I. A., Tang, H., & Gu, P. (2025) · Frontiers in Bioinformatics · doi:10.3389/fbinf.2025.1651623 · Cited by 2

Ancient and Emerging Nanostructures for Innovations to Fight Head and Neck Cancer

Kummer, N., Acet, Ö., Acet, B. Ö., Blueggel, M., Khamis, A., Gül, D., Knauer, S. K., & Stauber, R. H. (2026) · Cells · doi:10.3390/cells15040339 · Cited by 3

Single‐Molecule Analysis of Conformation Dynamics and Transition Kinetics of DNA Holliday Junction by Single‐Molecule Fluorescence Resonance Energy Transfer

Agarwala, P., Sadhukhan, S., Mondal, S., & Sasmal, D. K. (2026) · ChemBioChem · doi:10.1002/cbic.202500772 · Cited by 2

Integrated spherical nucleic acid nanoreactor mobilizes targeted PD‐L1 proteolysis and cuproptosis for robust breast cancer immunotherapy

Li, T., Huang, H., Zeng, Q., Zeng, L., Yang, Z., Shen, J., Li, S., Yang, H., Liu, Y., & Wu, C. (2026) · BMEMat · doi:10.1002/bmm2.70095 · Cited by 2

SE(3)-PROTACs: Geometric deep learning for PROTAC degradation prediction

Kothakapu, A. R., Madugula, S., Gandeed, S. B. S., Yadlapati, K. S. S., Sury, S., & Kondaparthi, V. (2026) · Briefings in Bioinformatics · doi:10.1093/bib/bbag228 · Cited by 2

HighPlay2: Structure-guided design of cyclic peptide candidates containing non-canonical amino acids

Lin, H., Wang, W. M., Ning, Z. H., Shang, T., Fan, Y., Zhang, C., Guo, J., Wang, X., & Duan, H. (2026) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2026.119160 · Cited by 2

Small Molecule Inhibitors Targeting New Targets of Protein-Protein Interactions

Yue, L., Wan, W., Xu, P., Li, L., Wang, C., Zhang, Y., Xu, H., Zhang, R., Hu, J., Lu, W., et al. (2018) · Springer eBooks · doi:10.1007/978-981-13-0773-7_7 · Cited by 2

Proteomic Comparison of the Cytotoxicology of Two Diastereomers of Citreamicin Reveals Differentially Activation of NF-κB Pathway

Liu, L.-L., Sun, J., Xu, Y., He, L., Chandramouli, K., & Qian, P. (2020) · Frontiers in Marine Science · doi:10.3389/fmars.2020.00228 · Cited by 2

PLA-PEG nanospheres decorated with phage display selected peptides as biomarkers for detection of human colorectal adenocarcinoma

de Souza, A., Castro‐Borges, W., de Andrade, M. H. G., Maia, Y. C. D. P., Goulart, L. R., Lanna, E. G., de Brito, A. C. F., Barboza, A. P. M., Mosqueira, V. C. F., & Rubio, K. T. S. (2020) · Drug Delivery and Translational Research · doi:10.1007/s13346-020-00826-0 · Cited by 2

Sulfonium-Tethered Peptide

Wang, Y., Yin, F., & Li, Z. (2022) · Methods in molecular biology · doi:10.1007/978-1-0716-2489-0_12 · Cited by 2

The potential of RANKL reverse signaling as a novel pharmacological target

Honma, M. (2023) · Folia Pharmacologica Japonica · doi:10.1254/fpj.22145 · Cited by 2

DARPins bind their cytosolic targets after having been translocated through the protective antigen pore of anthrax toxin

Becker, L., & Plückthun, A. (2023) · Scientific Reports · doi:10.1038/s41598-023-34647-1 · Cited by 2

Molecular simulation studies on a zwitterionic peptide-dendrimer conjugate for integrin αvβ3 binding

Lin, X., Xu, N., Li, C., Wu, Z., Chen, S., Shi, Y., & He, Y. (2023) · Biointerphases · doi:10.1116/6.0002713 · Cited by 2

Drug Design Methods to Regulate Protein–Protein Interactions

Poluri, K. M., Gulati, K., Tripathi, D. K., & Nagar, N. (2023) · Springer eBooks · doi:10.1007/978-981-99-2423-3_6 · Cited by 2

A Survey of Deep Learning Methods for Estimating the Accuracy of Protein Quaternary Structure Models

Chen, X., Liu, J., Park, N., & Cheng, J. (2024) · Biomolecules · doi:10.3390/biom14050574 · Cited by 2

Spor Lisesi ve Spor Bilimleri Fakültesi Öğrencilerinin Spora Bağlılık Düzeylerinin Çeşitli Değişkenler Açısından İncelenmesi

Denktaş, M., & Fişekçioğlu, İ. B. (2024) · Özgür Yayınları eBooks · doi:10.58830/ozgur.pub452.c1931 · Cited by 2

Alt Maksimum ve Maksimum Egzersiz Testlerinde Oksijen ve Laktat Kinetiği

Shahidi, S. H. (2024) · Özgür Yayınları eBooks · doi:10.58830/ozgur.pub452.c1930 · Cited by 2

Single Crystal, Spectroscopic Measurement, Quantum Chemical Studies, and Antimicrobial Potency of a new Cadmium Compound as a Potential Candidate for Therapeutic Antibacterial drug Development

Makhlouf, J., Timothy, R. A., Valkonen, A., Abuelizz, H. A., Al‐Salahi, R. A., Bakri, Y. E., & Sta, W. S. (2024) · Journal of Inorganic and Organometallic Polymers and Materials · doi:10.1007/s10904-024-03345-4 · Cited by 2

Discovery of novel 5-phenyl-1H-pyrrole-2-carboxylic acids as Keap1-Nrf2 inhibitors for acute lung injury treatment

Tang, J., Tie, X., Zhi, S., Wang, Z., Zhao, Q., Qu, Z., Lu, G., Li, Q., Wu, Y., & Shi, Y. (2024) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2024.107741 · Cited by 2

The Emergence of Oligonucleotide Building Blocks in the Multispecific Proximity-Inducing Drug Toolbox of Destruction

Zhou, K. X. T., & Bujold, K. E. (2024) · ACS Chemical Biology · doi:10.1021/acschembio.4c00311 · Cited by 2

Arginine-Rich Peptides Regulate the Pathogenic Galectin-10 Crystallization and Mitigate Crystallopathy-Associated Inflammation

Zhang, W., Li, S., Wang, Y., Liu, S., Liu, L., Deng, Z., Mo, S., Chen, M., Li, Z., Wang, R., et al. (2025) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.4c18411 · Cited by 2

Near-infrared light activatable nanoplatform for proteins labeling, enrichment and visualization in living systems

Liu, P., Zhang, S., Zhang, T., Si, Y., Liu, Z., Qian, X., Wu, Y., Liang, Y., Sun, W. C., Akkaya, E. U., et al. (2025) · Chinese Chemical Letters · doi:10.1016/j.cclet.2025.110966 · Cited by 2

Precision peptide disruptors: The next generation of targeted therapeutics in oncology

O'Gorman, B., Cooke, S. F., & Blair, C. M. (2025) · Cellular Signalling · doi:10.1016/j.cellsig.2025.111783 · Cited by 2

Synthesis, characterization, and computational exploration of Benzo[b] thiophene-incorporated amino phenol Schiff base through crystal structure analysis, Hirschfeld surface inspection, molecular docking, and dynamics simulations

Dhanya, T. M., Varughese, J. K., Rajimon, K. J., Krishna, G. A., Kurup, M. R. P., Philip, S., Augustine, M., Divya, K. M., & Mohanan, P. V. (2025) · Journal of Molecular Structure · doi:10.1016/j.molstruc.2025.142315 · Cited by 2

Bromodomain Inhibition and Its Application to Human Disease

Dupper, N. J., Zhou, Y., Govin, J., & McKenna, C. E. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-813939-4.00011-5 · Cited by 2

Protein-Protein Interactions in Malaria: Emerging Arena for Future Chemotherapeutics

Pasupureddy, R., Seshadri, S., Dixit, R., & Pandey, K. C. (2019) · IntechOpen eBooks · doi:10.5772/intechopen.89217 · Cited by 2

Design and applications of catalytic metallodrugs containing the ATCUN motif

Yu, Z., & Cowan, J. A. (2019) · Advances in inorganic chemistry · doi:10.1016/bs.adioch.2019.10.005 · Cited by 2

Thrombopoietin receptor‐based protein–protein interaction screening (THROPPIS)

Horikawa, M., Kakiuchi, Y., Kashima, D., Ogawa, K., & Kawahara, M. (2021) · Biotechnology and Bioengineering · doi:10.1002/bit.27975 · Cited by 2

Modeling the MreB-CbtA Interaction to Facilitate the Prediction and Design of Candidate Antibacterial Peptides

Awuni, E. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.814935 · Cited by 2

Peptide‐Based Inhibitors that Target the Docking Site of ERK2

Solomon, O., Shpilt, Z., Sapir, H., Marom, S., Bibas, S., Chen, Y., Tshuva, E. Y., Yitzchaik, S., & Friedler, A. (2022) · Israel Journal of Chemistry · doi:10.1002/ijch.202200041 · Cited by 2

Biological functions and structural biology of Plasmodium falciparum autophagy‐related proteins: The under‐explored options for novel antimalarial drug design

Usman, M. A., Salman, A. A., Ibrahim, M. A., Furukawa, K., & Yamasaki, K. (2023) · Chemical Biology & Drug Design · doi:10.1111/cbdd.14225 · Cited by 2

Protein–Protein Interaction for Drug Discovery

Brambila, B., Martelli, A. C. F. S., Barcelos, M. P., Antão, S. C., da Silva, C. H. T. D. P., & Novo‐Mansur, M. T. M. (2023) · Engineering materials · doi:10.1007/978-3-031-46545-1_12 · Cited by 2

Molecular Recognition of Tyrosine-Containing Polypeptides with Pseudopeptidic Cages Unraveled by Fluorescence and NMR Spectroscopies

Mirón, N. S., Tapia, L., Solà, J., Pérez, Y., & Alfonso, I. (2023) · Bioconjugate Chemistry · doi:10.1021/acs.bioconjchem.3c00455 · Cited by 2

Finding a Silver Bullet in a Stack of Proteins

Makhlynets, O. V., & Korendovych, I. V. (2017) · Biochemistry · doi:10.1021/acs.biochem.7b01177 · Cited by 2

Structural features of methionine aminopeptidase2-active core peptide essential for binding with S100A4

Katagiri, N., Nagatoishi, S., Tsumoto, K., & Endo, H. (2019) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2019.07.006 · Cited by 2

A Plasmonic Approach to Study Protein Interaction Kinetics through the Dimerization of Functionalized Ag Nanoparticles

Mercadal, P. A., Motrich, R. D., & Coronado, E. A. (2019) · Scientific Reports · doi:10.1038/s41598-019-49583-2 · Cited by 2

Structure‐Based Drug Design

Ferreira, L. L. G., & Andricopulo, A. D. (2021) · Wiley eBooks · doi:10.1002/0471266949.bmc141.pub2 · Cited by 2

A genetically encoded photo-proximity labeling approach for mapping protein territoriesPreprint

Hananya, N., Ye, X., Koren, S., & Muir, T. W. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.07.30.502153 · Cited by 2

Target-specific design of drug-like PPI inhibitors via hot-spot-guided generative deep learningPreprint

Sun, H., Li, J., Zhang, Y., Lin, S., Chen, J., Tan, H., Wang, R., Mao, X., Zhao, J., Li, R., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.10.29.620869 · Cited by 2

Affinity-based DEL Selections with Different Target Types: Overview and Achievements

Chen, Q., & Israel, D. I. (2025) · Royal Society of Chemistry eBooks · doi:10.1039/9781788016032-00001 · Cited by 2

HTS-Oracle: A Retrainable AI Platform for High-Confidence Hit Identification Across Difficult-to-Drug TargetsPreprint

Nada, H., Calvo‐Barreiro, L., Cho, S., Upadhyay, S., Meanwell, N. A., & Gabr, M. T. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.07.21.666047 · Cited by 2

Foldamers as Inhibitors of Aberrant Protein–Protein Interactions

Stillman, N. H., Dohoney, R. A., Baysah, C. Z., & Kumar, S. (2025) · Wiley eBooks · doi:10.1002/9783527845828.ch8 · Cited by 2

Stapled peptidomimetic therapeutics

Kannan, S., Lama, D., Tan, Y. S., Li, J., & Verma, C. S. (2022) · Elsevier eBooks · doi:10.1016/b978-0-12-820141-1.00022-4 · Cited by 1

Carbene Footprinting Directs Design of Genetically Encoded Proximity-Reactive Protein Binders

Ye, H., Zhu, Y., Kong, Y., Wen, H., Lu, W., Wang, D., Tang, S., Zhan, M., Lu, G., Shao, C., et al. (2024) · Analytical Chemistry · doi:10.1021/acs.analchem.4c00424 · Cited by 1

A platform of ADAPTive scaffolds: development of CDR-H3 β-hairpin mimics into covalent inhibitors of the PD1/PDL1 immune checkpoint

Naylon, S. H., Richaud, A. D., Zhao, G., Bui, L., Dufresne, C. P., Wu, C., Wangpaichitr, M., Savaraj, N., & Roche, S. P. (2024) · RSC Chemical Biology · doi:10.1039/d4cb00174e · Cited by 1

Accurate Prediction of Protein-Binding Residues in Protein Sequences Using SCRIBER

Zhang, J., Zhou, F., Liang, X., & Kurgan, L. (2024) · Methods in molecular biology · doi:10.1007/978-1-0716-4196-5_15 · Cited by 1

Constrained TACC3 peptidomimetics for a non-canonical protein–protein interface elucidate allosteric communication in Aurora-A kinase

Giménez, D., Walko, M., Miles, J. A., Bayliss, R. W., Wright, M. H., & Wilson, A. J. (2024) · Chemical Science · doi:10.1039/d4sc06100d · Cited by 1

The Role of Artificial Intelligence in the Discovery of New Drugs

Barcelos, M. P., & da Silva, C. H. T. D. P. (2024) · Engineering materials · doi:10.1007/978-3-031-75984-0_14 · Cited by 1

Structural analysis of EPOP BC-box binding to the elongin BC complex

Kim, S., Yeo, H., & Lee, B. I. (2025) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2025.151691 · Cited by 1

A BioID-based approach uncovers the interactome of hexose-6-phosphate dehydrogenase in breast cancer cells and identifies anterior gradient protein 2 as an interacting partner

Sakalauskaite, G., Weingärtner, M., Ebert, S., Boot, G. F., Bock, T., Birk, J., Tsachaki, M., Gallon, J. W., Piscuoglio, S., & Odermatt, A. (2025) · Cell & Bioscience · doi:10.1186/s13578-025-01388-9 · Cited by 1

CanGRNNA: Ensembling Message Passing and Temporal Dynamics with Attention for Prediction of Structural Cancer Protein–Protein Interactions

Jan, R., Hussain, A. B., Assad, A., & Bhat, B. A. (2025) · Arabian Journal for Science and Engineering · doi:10.1007/s13369-025-10498-y · Cited by 1

An Orally Available Grafted Peptide Targeting Epidermal Growth Factor Receptor Dimers Reduces Non-Small Cell Lung Cancer Tumors in Mouse Models

Shrestha, P., Singh, S. S., Dahal, A., Prasasty, V. D., Chowdhury, A., Majumdar, D., Gu, X., Johnson, W., Zhang, D., Billadeau, D. D., et al. (2025) · ACS Pharmacology & Translational Science · doi:10.1021/acsptsci.5c00336 · Cited by 1

Topologically Tunable α‐Helix Mimetics for Targeting Protein–Protein Interactions

Lee, T. K., Chen, L., Chen, C., Neal, H., & Ahn, J. (2025) · Angewandte Chemie International Edition · doi:10.1002/anie.202508209 · Cited by 1

Topologically Tunable α‐Helix Mimetics for Targeting Protein–Protein Interactions

Lee, T. K., Chen, L., Chen, C., Neal, H., & Ahn, J. (2025) · Angewandte Chemie · doi:10.1002/ange.202508209 · Cited by 1

Formation of complex cyclic compounds via a dehydrogenative Diels–Alder reaction

Xu, Z. Y., Yu, L., Chang, M., Qiang, R., Hu, Q., & Hu, Y. (2025) · Organic & Biomolecular Chemistry · doi:10.1039/d5ob01117e · Cited by 1

Deep learning for affinity prediction and interface prediction in molecular interactions

Bian, Y., Wu, H., & Yan, J. (2025) · Elsevier eBooks · doi:10.1016/b978-0-44-332908-1.00024-6 · Cited by 1

Potential Transmembrane Proteins-transporters of Chelidonic Acid for its Intracellular Uptake: In Silico Simulation

Nasibov, T. F., Gorokhova, A. V., Бразовский, К. С., Ryzhkova, A., Porokhova, E. D., Avdeeva, E. Y., Белоусов, М. В., Kokorev, O. V., & Хлусов, И. А. (2025) · Pharmaceutical Research · doi:10.1007/s11095-025-03934-z · Cited by 1

Molecular Docking and Simulation Analysis of Glioblastoma Cell Surface Receptors and Their Ligands: Identification of Inhibitory Drugs Targeting Fibronectin Ligand to Potentially Halt Glioblastoma Pathogenesis

Khan, M. W. A., Alam, M. J., Sherwani, S., Alouffi, S., Al-Motair, K. A., Khan, S. A., & Khan, S. N. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms262010038 · Cited by 1

LPS-focused nanomedicine for potent antibacterial therapy

Choudhury, S., Mishra, R. R., Maji, S., Arora, K., Singh, M. P., Mishra, J., & Panda, J. J. (2025) · Nanomedicine · doi:10.1080/17435889.2025.2574839 · Cited by 1

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

Protein-Protein Interactions as Drug Targets

Wendt, M. D. (2012) · Topics in Medicinal Chemistry · doi:10.1007/978-3-642-28965-1_1 · Cited by 9

Protein–protein interactions as targets for small molecule drug discovery

Fry, D. C. (2006) · Biopolymers · doi:10.1002/bip.20608 · Cited by 203

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 266

Small-Molecule Inhibitors of Protein–Protein Interactions as Therapeutics

Poluri, K. M., Gulati, K., Tripathi, D. K., & Nagar, N. (2023) · Springer eBooks · doi:10.1007/978-981-99-2423-3_7 · Cited by 1