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Identification of a Lacosamide Binding Protein Using an Affinity Bait and Chemical Reporter Strategy: 14-3-3 ζ

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A Binary Bivalent Supramolecular Assembly Platform Based on Cucurbit[8]uril and Dimeric Adapter Protein 14‐3‐3

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Structure, Function, Involvement in Diseases and Targeting of 14-3-3 Proteins: An Update

Cau, Y., Valensin, D., Mori, M., Draghi, S., & Botta, M. (2017) · Current Medicinal Chemistry · doi:10.2174/0929867324666170426095015 · Cited by 87 · see citing works

Tyrosine and tryptophan hydroxylases as therapeutic targets in human disease

Waløen, K., Kleppe, R., Martı́nez, A., & Haavik, J. (2016) · Expert Opinion on Therapeutic Targets · doi:10.1080/14728222.2017.1272581 · Cited by 85 · see citing works

Toward Small-Molecule Inhibition of Protein–Protein Interactions: General Aspects and Recent Progress in Targeting Costimulatory and Coinhibitory (Immune Checkpoint) Interactions

Bojadzic, D., & Buchwald, P. (2018) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026618666180531092503 · Cited by 81 · see citing works

Protein–protein interfaces in molecular glue-induced ternary complexes: classification, characterization, and prediction

Rui, H., Ashton, K. S., Min, J., Wang, C. W., & Potts, P. R. (2023) · RSC Chemical Biology · doi:10.1039/d2cb00207h · Cited by 82 · see citing works

Structure and Function of Fusicoccadiene Synthase, a Hexameric Bifunctional Diterpene Synthase

Chen, M., Chou, W. K. W., Toyomasu, T., Cane, D. E., & Christianson, D. W. (2016) · ACS Chemical Biology · doi:10.1021/acschembio.5b00960 · Cited by 79 · see citing works

Direct Modulation of Small GTPase Activity and Function

Cromm, P. M., Spiegel, J., Grossmann, T. N., & Waldmann, H. (2015) · Angewandte Chemie International Edition · doi:10.1002/anie.201504357 · Cited by 78 · see citing works

Synthesis of 2-alkoxy and 2-benzyloxy analogues of estradiol as anti-breast cancer agents through microtubule stabilization

Kumar, B. S., Kumar, A., Singh, J., Hasanain, M., Singh, A., Fatima, K., Yadav, D. K., Shukla, V., Luqman, S., Khan, F., et al. (2014) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2014.09.033 · Cited by 72 · see citing works

Structural Revisions of a Class of Natural Products: Scaffolds of Aglycon Analogues of Fusicoccins and Cotylenins Isolated from Fungi

Tang, Y., Xue, Y., Du, G., Wang, J., Liu, J., Sun, B., Li, X., Yao, G., Luo, Z., & Zhang, Y. (2016) · Angewandte Chemie International Edition · doi:10.1002/anie.201600313 · Cited by 72 · see citing works

Structural basis of O-GlcNAc recognition by mammalian 14-3-3 proteins

Toleman, C. A., Schumacher, M. A., Yu, S., Zeng, W., Cox, N. J., Smith, T. J., Soderblom, E. J., Wands, A. M., Kohler, J. J., & Boyce, M. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1722437115 · Cited by 69 · see citing works

Escape from planarity in fragment-based drug discovery: A synthetic strategy analysis of synthetic 3D fragment libraries

Klein, H. F., Hamilton, D. J. C., de Esch, I. J. P., Wijtmans, M., & O’Brien, P. (2022) · Drug Discovery Today · doi:10.1016/j.drudis.2022.05.021 · Cited by 67 · see citing works

A Thermodynamic Model for Multivalency in 14-3-3 Protein–Protein Interactions

Stevers, L. M., de Vink, P. J., Ottmann, C., Huskens, J., & Brunsveld, L. (2018) · Journal of the American Chemical Society · doi:10.1021/jacs.8b09618 · Cited by 61 · see citing works

14-3-3 adaptor protein-protein interactions as therapeutic targets for CNS diseases

Kaplan, A., Ottmann, C., & Fournier, A. E. (2017) · Pharmacological Research · doi:10.1016/j.phrs.2017.09.007 · Cited by 61 · see citing works

Direct and Propagated Effects of Small Molecules on Protein–Protein Interaction Networks

Cesa, L. C., Mapp, A. K., & Gestwicki, J. E. (2015) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2015.00119 · Cited by 58 · see citing works

Fusicoccane-Derived Diterpenoids from Alternaria brassicicola: Investigation of the Structure–Stability Relationship and Discovery of an IKKβ Inhibitor

Hu, Z., Sun, W., Li, F., Guan, J., Lu, Y., Liu, J., Tang, Y., Du, G., Xue, Y., Luo, Z., et al. (2018) · Organic Letters · doi:10.1021/acs.orglett.8b02137 · Cited by 56 · see citing works

Stabilization of protein–protein interactions by small molecules

Giordanetto, F., Schäfer, A., & Ottmann, C. (2014) · Drug Discovery Today · doi:10.1016/j.drudis.2014.08.005 · Cited by 55 · see citing works

Cooperativity basis for small-molecule stabilization of protein–protein interactions

de Vink, P. J., Andrei, S. A., Higuchi, Y., Ottmann, C., Milroy, L. ‐., & Brunsveld, L. (2019) · Chemical Science · doi:10.1039/c8sc05242e · Cited by 53 · see citing works

Protein–Protein Interactions as Drug Targets

Skwarczynska, M., & Ottmann, C. (2015) · Future Medicinal Chemistry · doi:10.4155/fmc.15.138 · Cited by 50 · see citing works

Novel toll-like receptor 4 (TLR4) antagonists identified by structure- and ligand-based virtual screening

Švajger, U., Brus, B., Turk, S., Sova, M., Hodnik, V., Anderluh, G., & Gobec, S. (2013) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2013.10.019 · Cited by 46 · see citing works

The Surprising Story of Fusicoccin: A Wilt-Inducing Phytotoxin, a Tool in Plant Physiology and a 14-3-3-Targeted Drug

Marra, M., Camoni, L., Visconti, S., Fiorillo, A., & Evidente, A. (2021) · Biomolecules · doi:10.3390/biom11091393 · Cited by 46 · see citing works

Identification of Two Secondary Ligand Binding Sites in 14-3-3 Proteins Using Fragment Screening

Sijbesma, E., Skóra, L., Leysen, S., Brunsveld, L., Koch, U., Nußbaumer, P., Jahnke, W., & Ottmann, C. (2017) · Biochemistry · doi:10.1021/acs.biochem.7b00153 · Cited by 46 · see citing works

Escape from planarity in fragment-based drug discovery: A physicochemical and 3D property analysis of synthetic 3D fragment libraries

Hamilton, D. J. C., Dekker, T., Klein, H. F., Janssen, G. V., Wijtmans, M., O’Brien, P., & de Esch, I. J. P. (2020) · Drug Discovery Today Technologies · doi:10.1016/j.ddtec.2021.05.001 · Cited by 45 · see citing works

14-3-3 and aggresome formation: Implications in neurodegenerative diseases

Jia, B., Wu, Y., & Zhou, Y. (2014) · Prion · doi:10.4161/pri.28123 · Cited by 43 · see citing works

Intracellular Generation of a Diterpene-Peptide Conjugate that Inhibits 14-3-3-Mediated Interactions

Parvatkar, P. T., Kato, N., Uesugi, M., Sato, S., & Ohkanda, J. (2015) · Journal of the American Chemical Society · doi:10.1021/jacs.5b09817 · Cited by 42 · see citing works

Focused Chemical Libraries – Design and Enrichment: An Example of Protein–Protein Interaction Chemical Space

Zhang, X., Betzi, S., Morelli, X., & Roche, P. (2014) · Future Medicinal Chemistry · doi:10.4155/fmc.14.57 · Cited by 41 · see citing works

Structural insight on assembly-line catalysis in terpene biosynthesis

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The phytotoxin fusicoccin differently regulates 14-3-3 proteins association to mode III targets

Paiardini, A., Aducci, P., Cervoni, L., Cutruzzolà, F., Lucente, C. D., Janson, G., Pascarella, S., Rinaldo, S., Visconti, S., & Camoni, L. (2014) · IUBMB Life · doi:10.1002/iub.1239 · Cited by 38 · see citing works

Fluorescence Anisotropy-Based Tethering for Discovery of Protein–Protein Interaction Stabilizers

Sijbesma, E., Somsen, B. A., Miley, G. P., de Gevel, I. A. L.-V., Brunsveld, L., Arkin, M. R., & Ottmann, C. (2020) · ACS Chemical Biology · doi:10.1021/acschembio.0c00646 · Cited by 38 · see citing works

Small molecules that target phosphorylation dependent protein–protein interaction

Watanabe, N., & Osada, H. (2016) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2016.03.023 · Cited by 37 · see citing works

14‐3‐3 Protein‐Protein Interactions: From Mechanistic Understanding to Their Small‐Molecule Stabilization

Somsen, B. A., Cossar, P. J., Arkin, M. R., Brunsveld, L., & Ottmann, C. (2024) · ChemBioChem · doi:10.1002/cbic.202400214 · Cited by 36 · see citing works

Discovery of 14‐3‐3 Protein–Protein Interaction Inhibitors that Sensitize Multidrug‐Resistant Cancer Cells to Doxorubicin and the Akt Inhibitor GSK690693

Mori, M., Vignaroli, G., Cau, Y., Dinić, J., Hill, R., Rossi, M., Colecchia, D., Pešić, M., Link, W., Chiariello, M., et al. (2014) · ChemMedChem · doi:10.1002/cmdc.201400044 · Cited by 33 · see citing works

TNF Superfamily Protein-Protein Interactions: Feasibility of Small- Molecule Modulation

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Chimeric 14-3-3 proteins for unraveling interactions with intrinsically disordered partners

Sluchanko, N. N., Tugaeva, K. V., Greive, S. J., & Antson, A. A. (2017) · Scientific Reports · doi:10.1038/s41598-017-12214-9 · Cited by 31 · see citing works

A structured proteomic approach identifies 14-3-3Sigma as a novel and reliable protein biomarker in panel based differential diagnostics of liver tumors

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The role of protein–protein interactions in the intracellular traffic of the potassium channels TASK-1 and TASK-3

Kilisch, M., Lytovchenko, O., Schwappach, B., Renigunta, V., & Daut, J. (2015) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-014-1672-2 · Cited by 28 · see citing works

Small‐molecule modulators of the OX 40– OX40 ligand co‐stimulatory protein–protein interaction

Song, Y. G., Margolles‐Clark, E., Bayer, A. L., & Buchwald, P. (2014) · British Journal of Pharmacology · doi:10.1111/bph.12819 · Cited by 28 · see citing works

A Binary Bivalent Supramolecular Assembly Platform Based on Cucurbit[8]uril and Dimeric Adapter Protein 14‐3‐3

de Vink, P. J., Briels, J. M., Schrader, T. H., Milroy, L. ‐., Brunsveld, L., & Ottmann, C. (2017) · Angewandte Chemie · doi:10.1002/ange.201701807 · Cited by 28 · see citing works

Recent advances in structural studies of 14-3-3 protein complexes

Sluchanko, N. N. (2022) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2021.12.004 · Cited by 27 · see citing works

Yeast functional screen to identify genes conferring salt stress tolerance in Salicornia europaea

Nakahara, Y., Sawabe, S., Kainuma, K., Katsuhara, M., Shibasaka, M., Suzuki, M., Yamamoto, K., Oguri, S., & Sakamoto, H. (2015) · Frontiers in Plant Science · doi:10.3389/fpls.2015.00920 · Cited by 23 · see citing works

Supramolecular Enhancement of a Natural 14–3–3 Protein Ligand

Guillory, X., Hadrović, I., de Vink, P. J., Sowislok, A., Brunsveld, L., Schrader, T. H., & Ottmann, C. (2021) · Journal of the American Chemical Society · doi:10.1021/jacs.1c07095 · Cited by 22 · see citing works

Insight into Conformational Change for 14-3-3σ Protein by Molecular Dynamics Simulation

Hu, G., Li, H., Liu, J., & Wang, J. (2014) · International Journal of Molecular Sciences · doi:10.3390/ijms15022794 · Cited by 22 · see citing works

Small‐Molecule‐Induced and Cooperative Enzyme Assembly on a 14‐3‐3 Scaffold

den Hamer, A., Lemmens, L. J. M., Nijenhuis, M. A. D., Ottmann, C., Merkx, M., de Greef, T. F. A., & Brunsveld, L. (2016) · ChemBioChem · doi:10.1002/cbic.201600631 · Cited by 21 · see citing works

Versatility of 14-3-3 proteins and their roles in bone and joint-related diseases

Zhou, R., Hu, W., Ma, P. X., & Liu, C.-J. (2024) · Bone Research · doi:10.1038/s41413-024-00370-4 · Cited by 22 · see citing works

From plant physiology to pharmacology: fusicoccin leaves the leaves

Camoni, L., Visconti, S., Aducci, P., & Marra, M. (2018) · Planta · doi:10.1007/s00425-018-3051-2 · Cited by 21 · see citing works

Structural Revisions of a Class of Natural Products: Scaffolds of Aglycon Analogues of Fusicoccins and Cotylenins Isolated from Fungi

Tang, Y., Xue, Y., Du, G., Wang, J., Liu, J., Sun, B., Li, X., Yao, G., Luo, Z., & Zhang, Y. (2016) · Angewandte Chemie · doi:10.1002/ange.201600313 · Cited by 21 · see citing works

The phytotoxin fusicoccin, a selective stabilizer of 14‐3‐3 interactions?

Camoni, L., Visconti, S., & Aducci, P. (2013) · IUBMB Life · doi:10.1002/iub.1167 · Cited by 21 · see citing works

Rational Design, Binding Studies, and Crystal‐Structure Evaluation of the First Ligand Targeting the Dimerization Interface of the 14‐3‐3ζ Adapter Protein

Ehlers, M., Grad, J., Mittal, S., Bier, D., Mertel, M., Ohl, L., Bartel, M., Briels, J. M., Heimann, M., Ottmann, C., et al. (2017) · ChemBioChem · doi:10.1002/cbic.201700588 · Cited by 20 · see citing works

Revealing the binding modes and the unbinding of 14-3-3σ proteins and inhibitors by computational methods

Hu, G., Cao, Z., Xu, S., Wang, W., & Wang, J. (2015) · Scientific Reports · doi:10.1038/srep16481 · Cited by 19 · see citing works

The 14-3-3 Protein Homolog ArtA Regulates Development and Secondary Metabolism in the Opportunistic Plant Pathogen Aspergillus flavus

Ibarra, B. A., Lohmar, J. M., Satterlee, T. R., McDonald, T., Cary, J. W., & Calvo, A. M. (2017) · Applied and Environmental Microbiology · doi:10.1128/aem.02241-17 · Cited by 17 · see citing works

Novel immunohistochemical markers differentiate intrahepatic cholangiocarcinoma from benign bile duct lesions

Bertram, S., Padden, J., Kälsch, J., Ahrens, M., Pott, L. L., Canbay, A. E., Weber, F., Fingas, C. D., Hoffmann, A.-C., Vietor, A., et al. (2016) · Journal of Clinical Pathology · doi:10.1136/jclinpath-2015-203418 · Cited by 17 · see citing works

Engineering substrate channeling in a bifunctional terpene synthase

Wenger, E. S., Schultz, K. C., Marmorstein, R., & Christianson, D. W. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2408064121 · Cited by 15 · see citing works

Identification of molecular glues of the SLP76/14-3-3 protein–protein interaction

Soini, L., Redhead, M. A., Westwood, M., Leysen, S., Davis, J., & Ottmann, C. (2021) · RSC Medicinal Chemistry · doi:10.1039/d1md00172h · Cited by 15 · see citing works

Enantioselective preparation of C-ring fragment of cotylenin A via catalytic asymmetric intramolecular cyclopropanation of α-diazo β-keto ester

Nagatani, K., Hoshino, Y., Tezuka, H., & Nakada, M. (2017) · Tetrahedron Letters · doi:10.1016/j.tetlet.2017.01.076 · Cited by 14 · see citing works

Understanding the interaction of 14‐3‐3 proteins with h DMX and h DM2: a structural and biophysical study

Srdanović, S., Wolter, M., Trinh, C. H., Ottmann, C., Warriner, S. L., & Wilson, A. J. (2022) · FEBS Journal · doi:10.1111/febs.16433 · Cited by 12 · see citing works

Recent Developments in 14–3–3 Stabilizers for Regulating Protein–Protein Interactions: An Update

Tian, Y., Li, L., Wu, L., Xu, Q., Li, Y. M., Pan, H., Bing, T., Bai, X., Finko, A. V., Li, Z., et al. (2025) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.4c01936 · Cited by 12 · see citing works

Recent total syntheses of fusicoccanes

Liu, Y., & Hong, R. (2024) · Cell Reports Physical Science · doi:10.1016/j.xcrp.2024.102141 · Cited by 10 · see citing works

A Modular Synthesis of Teraryl‐Based α‐Helix Mimetics, Part 5: A Complete Set of Pyridine Boronic Acid Pinacol Esters Featuring Side Chains of Proteinogenic Amino Acids

Trobe, M., Schreiner, T., Vareka, M., Grimm, S., Wölfl, B., & Breinbauer, R. (2022) · European Journal of Organic Chemistry · doi:10.1002/ejoc.202101280 · Cited by 9 · see citing works

Direkte Modulation von Aktivität und Funktion kleiner GTPasen

Cromm, P. M., Spiegel, J., Grossmann, T. N., & Waldmann, H. (2015) · Angewandte Chemie · doi:10.1002/ange.201504357 · Cited by 9 · see citing works

Discovery of 14‐3‐3 PPI Stabilizers by Extension of an Amidine‐Substituted Thiophene Fragment

Wu, Q., Centorrino, F., Guillory, X., Wolter, M., Ottmann, C., Cossar, P. J., & Brunsveld, L. (2023) · ChemBioChem · doi:10.1002/cbic.202300636 · Cited by 9 · see citing works

Small molecule microarray screening methodology based on surface plasmon resonance imaging

Singh, V., Singh, K., Nand, A., Dai, H., Wang, J., Zhang, L., Merino, A., & Zhu, J. (2015) · Arabian Journal of Chemistry · doi:10.1016/j.arabjc.2014.12.020 · Cited by 7 · see citing works

A study on the effect of synthetic α-to-β 3 -amino acid mutations on the binding of phosphopeptides to 14-3-3 proteins

Andrei, S. A., Thijssen, V., Brunsveld, L., Ottmann, C., & Milroy, L. ‐. (2019) · Chemical Communications · doi:10.1039/c9cc07982c · Cited by 7 · see citing works

Modulation of the 14-3-3σ/C-RAF “Auto”inhibited Complex by Molecular Glues

Konstantinidou, M., Vickery, H. R., Pennings, M. A. M., Virta, J. M., Luo, S., Visser, E. J., Bannier, S. D., Srikanth, M., Cismoski, S. Z., Young, L. C., et al. (2026) · Journal of the American Chemical Society · doi:10.1021/jacs.5c12622 · Cited by 6 · see citing works

A Modular Synthesis of Teraryl‐Based α‐Helix Mimetics, Part 3: Iodophenyltriflate Core Fragments Featuring Side Chains of Proteinogenic Amino Acids

Trobe, M., Vareka, M., Schreiner, T., Dobrounig, P. S., Doler, C., Holzinger, E. B., Steinegger, A., & Breinbauer, R. (2022) · European Journal of Organic Chemistry · doi:10.1002/ejoc.202101278 · Cited by 5 · see citing works

A Modular Synthesis of Teraryl‐Based α‐Helix Mimetics, Part 4: Core Fragments with Two Halide Leaving Groups Featuring Side Chains of Proteinogenic Amino Acids

Trobe, M., Blesl, J., Vareka, M., Schreiner, T., & Breinbauer, R. (2022) · European Journal of Organic Chemistry · doi:10.1002/ejoc.202101279 · Cited by 4 · see citing works

Protein–Protein Interaction Inhibitors in Cancer

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Manumycin Polyketides Act as Molecular Glues Between UBR7 and P53 to Impair Breast Cancer PathogenicityPreprint

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Self-Assembled Receptors for Protein Surface Recognition

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14-3-3γ affects eIF5 to regulate β-casein synthesis in bovine mammary epithelial cells

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Biofunctional peptide design

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Chemical Biology – Current and Next Challenges

Rauh, D. (2013) · ACS Chemical Biology · doi:10.1021/cb400013t · Cited by 1 · see citing works

Modulation of protein : protein interactions in inflammatory diseases

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Protein-guided Self-Assembly for Controlling Protein–Protein Interactions

Ohkanda, J. (2017) · Journal of The Society of Japanese Women Scientists · doi:10.5939/sjws.17001

Current Challenges in the Computational Modelling of Molecular Recognition Processes

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Development of a fluorescent three‐hybrid system for the identification of protein‐protein associators

Foster, A. D., Chung, C., Hann, M. M., Simpson, G. L., & Tavassoli, A. (2020) · Peptide Science · doi:10.1002/pep2.24178

Chemical Approach Toward Controlling of Transient Protein Interactions

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Engineering Substrate Channeling in Assembly-Line Terpene BiosynthesisPreprint

Wenger, E. S., Schultz, K. C., Marmorstein, R., & Christianson, D. W. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.03.25.586617

Synthetic studies on fusicoccin A: Alternative synthetic approach to the C-ring fragment

Oshima, R., & Nakada, M. (2025) · Tetrahedron Letters · doi:10.1016/j.tetlet.2025.155631

NMR study of 14-3-3 protein-protein interactions and modulation thereof by small molecules

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BindingDB Entry 50023432: Recent Developments in 14-3-3 Stabilizers for Regulating Protein-Protein Interactions: An Update.

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BindingDB Entry 50047589: Small molecules that target phosphorylation dependent protein-protein interaction.

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BindingDB Entry 50043595: Novel toll-like receptor 4 (TLR4) antagonists identified by structure- and ligand-based virtual screening.

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Modulators of 14-3-3 Protein–Protein Interactions

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Modulators of Protein–Protein Interactions

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14‐3‐3 Protein‐Protein Interactions: From Mechanistic Understanding to Their Small‐Molecule Stabilization

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Small-molecule Modulators of Protein–Protein Interactions: Focus on 14-3-3 PPIs

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