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Multiple conformational selection and induced fit events take place in allosteric propagation

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Nonlocal Helix Formation Is Key to Understanding S-Adenosylmethionine-1 Riboswitch Function

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Structurally encoded intraclass differences in EphA clusters drive distinct cell responses

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NMR resonance assignments of thrombin reveal the conformational and dynamic effects of ligation

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Selective Molecular Recognition in Amyloid Growth and Transmission and Cross-Species Barriers

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Disparate Degrees of Hypervariable Loop Flexibility Control T-Cell Receptor Cross-Reactivity, Specificity, and Binding Mechanism

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EphB and Ephrin-B Interactions Mediate Human Mesenchymal Stem Cell Suppression of Activated T-Cells

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Bound Water at Protein-Protein Interfaces: Partners, Roles and Hydrophobic Bubbles as a Conserved Motif

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Effects of Cancer-Associated EPHA3 Mutations on Lung Cancer

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Of Ephs and Ephrins: Companies Target Guidance Molecules in Cancer

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Pathway-specific engagement of ephrinA5-EphA4/EphA5 system of the substantia nigra pars reticulata in cocaine-induced responses

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Protein Ensembles: How Does Nature Harness Thermodynamic Fluctuations for Life? The Diverse Functional Roles of Conformational Ensembles in the Cell

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Eph receptor signalling: from catalytic to non-catalytic functions

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Ligand-receptor promiscuity enables cellular addressing

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Local and global anatomy of antibody‐protein antigen recognition

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Antigen binding allosterically promotes Fc receptor recognition

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EphB and Ephrin-B Interactions Mediate Human Mesenchymal Stem Cell Suppression of Activated T-Cells

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Molecular identity of arteries, veins, and lymphatics

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Targeting receptor tyrosine kinase EphB4 in cancer therapy

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Ephrins and Eph Receptor Signaling in Tissue Repair and Fibrosis

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Development of non-viral, ligand-dependent, EPHB4-specific chimeric antigen receptor T cells for treatment of rhabdomyosarcoma

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EphB4: A promising target for upper aerodigestive malignancies

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EPHB4-RASA1-Mediated Negative Regulation of Ras-MAPK Signaling in the Vasculature: Implications for the Treatment of EPHB4- and RASA1-Related Vascular Anomalies in Humans

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Optogenetic activation of EphB2 receptor in dendrites induced actin polymerization by activating Arg kinase

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EphA4 regulates Aβ production via BACE1 expression in neurons

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Tyrosine phosphorylation of DEPTOR functions as a molecular switch to activate mTOR signaling

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Targeting EphA2: a promising strategy to overcome chemoresistance and drug resistance in cancer

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TrkB-dependent EphrinA reverse signaling regulates callosal axon fasciculate growth downstream of Neurod2/6

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EPHB4-RASA1 Inhibition of PIEZO1 Ras Activation Drives Lymphatic Valvulogenesis

Chen, D., Tang, Y., Lapinski, P. E., Wiggins, D., Sevick-Muraca, E. M., Davis, M. J., & King, P. D. (2024) · Circulation Research · doi:10.1161/circresaha.124.325383 · Cited by 15 · see citing works

The first identification of complete Eph-ephrin signalling in ctenophores and sponges reveals a role for neofunctionalization in the emergence of signalling domains

Krishnan, A., Degnan, B. M., & Degnan, B. M. (2019) · BMC Evolutionary Biology · doi:10.1186/s12862-019-1418-z · Cited by 14 · see citing works

The EphB6 Receptor: Kinase-Dead but Very Much Alive

Strozen, T. G., Sharpe, J. C., Harris, E. D., Uppalapati, M., & Toosi, B. M. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22158211 · Cited by 14 · see citing works

Potential role of the Eph/ephrin system in colorectal cancer: emerging druggable molecular targets

Scarini, J. F., Gonçalves, M. W. A., de Lima‐Souza, R. A., Lavareze, L., Kimura, T. D. C., Yang, C.-C., ALTEMANI, A. M. D. A. M., Mariano, F. V., Soares, H. P., Fillmore, G. C., et al. (2024) · Frontiers in Oncology · doi:10.3389/fonc.2024.1275330 · Cited by 12 · see citing works

Mechanistic and therapeutic implications of EphA‐4 receptor tyrosine kinase in the pathogenesis of Alzheimer's disease

Ganguly, D., Thomas, J. A., Ali, A., & Kumar, R. K. (2022) · European Journal of Neuroscience · doi:10.1111/ejn.15591 · Cited by 12 · see citing works

Investigation of the interactions between the EphB2 receptor and SNEW peptide variants

Ma, B., Kolb, S., Diprima, M., Karna, M., Tosato, G., Yang, Q., Huang, Q., & Nussinov, R. (2014) · Growth Factors · doi:10.3109/08977194.2014.985786 · Cited by 10 · see citing works

Inhibition of Ephrin B2 Reverse Signaling Abolishes Multiple Myeloma Pathogenesis

Sasine, J. P., Kozlova, N. Y., Valicente, L., Dukov, J. E., Tran, D. H., Himburg, H. A., Kumar, S., Khorsandi, S., Chan, A., Grohe, S., et al. (2024) · Cancer Research · doi:10.1158/0008-5472.can-23-1950 · Cited by 9 · see citing works

Ephrin-Eph signaling: an important regulator of epithelial integrity and barrier function

Liu, M., Charek, J. G., Miguel, R. D. V., & Cherpes, T. L. (2025) · Tissue Barriers · doi:10.1080/21688370.2025.2462855 · Cited by 9 · see citing works

Expression of the Receptor Tyrosine Kinase EphB2 on Dendritic Cells Is Modulated by Toll-Like Receptor Ligation but Is Not Required for T Cell Activation

Mimche, P. N., Brady, L. M., Keeton, S., Fenne, D. S. J., King, T., Quicke, K. M., Hudson, L. E., & Lamb, T. J. (2015) · PLoS ONE · doi:10.1371/journal.pone.0138835 · Cited by 9 · see citing works

The role of lncRNAs in the interplay of signaling pathways and epigenetic mechanisms in glioma

Yildiz, C. B., Du, J., Mohan, K. N., Zimmer‐Bensch, G., & Abdolahi, S. (2025) · Epigenomics · doi:10.1080/17501911.2024.2442297 · Cited by 7 · see citing works

Colorectal cancer-associated mutations impair EphB1 kinase function

Kim, Y., Ahmed, S., & Miller, W. T. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.105115 · Cited by 7 · see citing works

An investigation of binding interactions of tumor-targeted peptide conjugated polyphenols with the kinase domain of ephrin B4 and B2 receptors

Mitchell, S. M., Heise, R. M., Murray, M. E., Lambo, D. J., Daso, R. E., & Banerjee, I. A. (2023) · Molecular Diversity · doi:10.1007/s11030-023-10621-x · Cited by 5 · see citing works

EphB3 as a Potential Mediator of Developmental and Reparative Osteogenesis

Kamath, R. A. D., & Benson, M. D. (2021) · Cells Tissues Organs · doi:10.1159/000520369 · Cited by 3 · see citing works

Conformational Flexibility of Transmembrane Helices: How it Works and Where it Matters

Langosch, D. (2026) · Chemical Reviews · doi:10.1021/acs.chemrev.5c00581 · Cited by 3 · see citing works

Eph receptor B6 shapes a cold immune microenvironment, inhibiting anti-cancer immunity and immunotherapy response in bladder cancer

Jia, X., Zhang, D., Zhou, C., Yan, Z., Jiang, Z., Xie, L., & Jiang, J. (2023) · Frontiers in Oncology · doi:10.3389/fonc.2023.1175183 · Cited by 3 · see citing works

The multifaceted roles of receptor tyrosine pseudokinases in cellular signalling

Park, E. C., Thompson, A. P., Murphy, J. M., Liang, L., & Lucet, I. S. (2026) · Biochemical Society Transactions · doi:10.1042/bst20260770 · Cited by 2 · see citing works

The relation between neurite growth inhibitor factor and spinal cord injury

Yuan, H., & Wang, T. (2017) · Ibrain · doi:10.1002/j.2769-2795.2017.tb00015.x · Cited by 2 · see citing works

Exogenous ephrin-A3 reverses loss of vaginal epithelial barrier protection in progestin-treated mice

Liu, M., Miguel, R. D. V., Aceves, K. M., & Cherpes, T. L. (2025) · Mucosal Immunology · doi:10.1016/j.mucimm.2025.06.007 · Cited by 3 · see citing works

Database-Driven Identification of Structurally Similar Protein-Protein Interfaces

Graef, J., Ehrt, C., Reim, T., & Rarey, M. (2024) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.3c01462 · Cited by 2 · see citing works

Ephrin-A5 or EphA7 stimulation is anti-proliferative for human rhabdomyosarcoma in vitro

Cecchini, A., Ceccon, L., Calandro, S., Chen, A., Schwesig, J. K., & Cornelison, D. (2025) · Skeletal Muscle · doi:10.1186/s13395-025-00384-4 · Cited by 1 · see citing works

Eph-ephrin signaling and its potential role in female reproductive tract development

Prasun, P. (2025) · Molecular Biology Reports · doi:10.1007/s11033-025-11154-2 · Cited by 1 · see citing works

Determinants of Macromolecular Specificity from Proteomics-De rived Peptide Substrate Data

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Exogenous ephrin-A3 administration restores vaginal epithelial barrier function in progestin-treated micePreprint

Liu, M., Miguel, R. D. V., Aceves, K. M., & Cherpes, T. L. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.10.29.620915 · Cited by 1 · see citing works

Effects of Localized EphB2 Stimulation on Dendritic Filopodia of Hippocampal Neurons

Locke, C. (2018) · OpenCommons - UConn (University of Connecticut)

From genetic data and structures to drug development: New approaches to target Eph receptors

Nikolov, D. B., & Himanen, J. P. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-821310-0.00006-1

Protein Tyrosine Kinase Gene Expression Profiles in the Embryonic Bursa of Fabricius of Chicken Lines Selected for High and Low Antibody Responses

Nuthalapati, N., Burks, T. A., Siegel, P. B., Taylor, R. L., & Pharr, G. T. (2021) · International Journal of Poultry Science · doi:10.3923/ijps.2021.173.178

Resource-location patterns and state severance taxes: some empirical evidence

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Faculty Opinions recommendation of Molecular identity of arteries, veins, and lymphatics.

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An EPHB4-RASA1 signaling complex inhibits shear stress-induced Ras-MAPK activation in lymphatic endothelial cells to promote the development of lymphatic vessel valvesPreprint

Chen, D., Wiggins, D., Sevick-Muraca, E. M., Davis, M. J., & King, P. D. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.11.22.568378 · Cited by 1 · see citing works

Axon Guidance Receptor Endocytosis, Trafficking, and Signaling in Health and Disease

Bues, B., O’Mahony, K. R., & Burk, K. (2025) · The Receptors · doi:10.1007/978-3-031-81991-9_16

Loss of ephrin-A5 leads to clinical signs of Peters Anomaly in a mouse model

Cheng, C., Innis, I. J., Vu, M. P., & Okada, Y. (2026) · Experimental Eye Research · doi:10.1016/j.exer.2026.111226

Targeting EphA2 with a novel EFNA3-mimetic peptide enhances vaginal epithelial barrier function

Miguel, R. D. V., Liu, M., Smedley, J. V., & Cherpes, T. L. (2026) · Mucosal Immunology · doi:10.1016/j.mucimm.2026.100406

Structural Characterization of the EphA4-Ephrin-B2 Complex Reveals New Features Enabling Eph-Ephrin Binding Promiscuity

Qin, H., Noberini, R., Huan, X., Shi, J., Pasquale, E. B., & Song, J. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.064824 · Cited by 101 · see citing works

Structural and Biophysical Characterization of the EphB4·EphrinB2 Protein-Protein Interaction and Receptor Specificity

Chrencik, J., Brooun, A., Kraus, M. L., Recht, M. I., Kolatkar, A. R., Han, G. W., Seifert, J. M., Widmer, H., Auer, M., & Kühn, P. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m605766200 · Cited by 97 · see citing works

Unique structure and dynamics of the EphA5 ligand binding domain mediate its binding specificity as revealed by X-ray crystallography, NMR andMD simulations. PLoS One. 2013; 8: e74040. doi: 10.1371/journal.pone.0074040 PMID: 24086308

Huan, X., Shi, J., Lim, L. Z., Mitra, S., Zhu, W., Qin, H., Pasquale, E. B., & Song, J. (2016)

Unique Structure and Dynamics of the EphA5 Ligand Binding Domain Mediate Its Binding Specificity as Revealed by X-ray Crystallography, NMR and MD Simulations

Huan, X., Shi, J., Lim, L., Mitra, S., Zhu, W., Qin, H., Pasquale, E. B., & Song, J. (2013) · PLoS ONE · doi:10.1371/journal.pone.0074040 · Cited by 16 · see citing works

bidirectional signal transduction

Nussinov, R., & Ma, B. (2013)