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Discovery of a new class of 4-anilinopyrimidines as potent c-Jun N-terminal kinase inhibitors: Synthesis and SAR studies

Liu, M., Wang, S., Clampit, J. E., Gum, R. J., Haasch, D. L., Rondinone, C. M., Trevillyan, J. M., Abad‐Zapatero, C., Fry, E. H., Sham, H. L., et al. (2006) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2006.10.093 · Cited by 53 · see citing works

In-silico drug repurposing and molecular dynamics puzzled out potential SARS-CoV-2 main protease inhibitors

Ibrahim, M. A. A., Abdelrahman, A. H. M., & Hegazy, M. F. (2020) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2020.1791958 · Cited by 52 · see citing works

Protein Kinase Inhibitors: Structural Insights Into Selectivity

Thaimattam, R., Banerjee, R., Miglani, R., & Javed Iqbal, M. (2007) · Current Pharmaceutical Design · doi:10.2174/138161207781757042 · Cited by 52 · see citing works

Automating crystallographic structure solution and refinement of protein–ligand complexes

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How many kinases are druggable? A review of our current understanding

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c-Jun N-Terminal Kinase Inhibitors as Potential Leads for New Therapeutics for Alzheimer’s Diseases

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Signal Transduction Therapy with Rationally Designed Kinase Inhibitors

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Ensemble Docking into Flexible Active Sites. Critical Evaluation of FlexE against JNK-3 and β-Secretase

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Biological Evaluation and Structural Determinants of p38α Mitogen‐Activated‐Protein Kinase and c‐Jun‐N‐Terminal Kinase 3 Inhibition by Flavonoids

Goettert, M. I., Schattel, V., Koch, P., Merfort, I., & Laufer, S. (2010) · ChemBioChem · doi:10.1002/cbic.201000487 · Cited by 43 · see citing works

Highly selective c-Jun N-terminal kinase (JNK) 2 and 3 inhibitors with in vitro CNS-like pharmacokinetic properties prevent neurodegeneration

Probst, G. D., Bowers, S., Sealy, J. M., Truong, A. P., Hom, R. K., Galemmo, R. A., Konradi, A. W., Sham, H. L., Quincy, D. A., Pan, H., et al. (2010) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2010.11.010 · Cited by 43 · see citing works

Therapeutic promise of JNK ATP-noncompetitive inhibitors

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Blocking UV‐Induced eIF2α Phosphorylation with Small Molecule Inhibitors of GCN2

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Design and synthesis of a novel, orally active, brain penetrant, tri-substituted thiophene based JNK inhibitor

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3,5-Disubstituted quinolines as novel c-Jun N-terminal kinase inhibitors

Jiang, R., Duckett, D. R., Chen, W., Habel, J. E., Ling, Y. Y., LoGrasso, P. V., & Kamenecka, T. M. (2007) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2007.08.054 · Cited by 39 · see citing works

1-Aryl-3,4-dihydroisoquinoline inhibitors of JNK3

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Biphenyl amide p38 kinase inhibitors 1: Discovery and binding mode

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New insights into the structural dynamics of the kinase JNK3

Mishra, P., & Günther, S. (2018) · Scientific Reports · doi:10.1038/s41598-018-27867-3 · Cited by 37 · see citing works

c-Jun N-terminal kinase regulates lamellipodial protrusion and cell sheet migration during epithelial wound closure by a gene expression-independent mechanism

Altan, Z. M., & Fenteany, G. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.07.079 · Cited by 35 · see citing works

Inhibition of Oncogenic Kinases: An In Vitro Validated Computational Approach Identified Potential Multi-Target Anticancer Compounds

Ikram, N., Mirza, M. U., Vanmeert, M., Froeyen, M., Salo‐Ahen, O. M. H., Tahir, M., Qazi, A. M., & Ahmad, S. (2019) · Biomolecules · doi:10.3390/biom9040124 · Cited by 34 · see citing works

Anatomy of Fingerprint Search Calculations on Structurally Diverse Sets of Active Compounds

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Three-dimensional quantitative structure–activity relationship (3 D-QSAR) and docking studies on (benzothiazole-2-yl) acetonitrile derivatives as c-Jun N-terminal kinase-3 (JNK3) inhibitors

Shaikh, A. R., Ismael, M., Carpio, C. A. D., Tsuboi, H., Koyama, M., Endou, A., Kubo, M., Brocławik, E., & Miyamoto, A. (2006) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2006.06.039 · Cited by 32 · see citing works

Synthesis and SAR of 1,9-dihydro-9-hydroxypyrazolo[3,4-b]quinolin-4-ones as novel, selective c-Jun N-terminal kinase inhibitors

Liu, M., Xin, Z., Clampit, J. E., Wang, S., Gum, R. J., Haasch, D. L., Trevillyan, J. M., Abad‐Zapatero, C., Fry, E. H., Sham, H. L., et al. (2006) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2006.02.046 · Cited by 31 · see citing works

Structural Optimization of a Pyridinylimidazole Scaffold: Shifting the Selectivity from p38α Mitogen-Activated Protein Kinase to c-Jun N-Terminal Kinase 3

Ansideri, F., Macedo, J. T., Eitel, M., El‐Gokha, A., Zinad, D. S., Scarpellini, C., Kudolo, M., Schollmeyer, D., Boeckler, F. M., Blaum, B. S., et al. (2018) · ACS Omega · doi:10.1021/acsomega.8b00668 · Cited by 30 · see citing works

Arrestin-Dependent Activation of JNK Family Kinases

Zhan, X., Kook, S., Gurevich, E. V., & Gurevich, V. V. (2013) · Handbook of experimental pharmacology · doi:10.1007/978-3-642-41199-1_13 · Cited by 27 · see citing works

Dissection of the Recognition Properties of p38 MAP Kinase. Determination of the Binding Mode of a New Pyridinyl−Heterocycle Inhibitor Family

Soliva, R., Gelpí, J. L., Almansa, C., Virgili, M., & Orozco, M. (2006) · Journal of Medicinal Chemistry · doi:10.1021/jm061073h · Cited by 25 · see citing works

Enzyme Kinetics and Interaction Studies for Human JNK1β1 and Substrates Activating Transcription Factor 2 (ATF2) and c-Jun N-terminal kinase (c-Jun)

Figuera-Losada, M., & LoGrasso, P. V. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.323766 · Cited by 23 · see citing works

Discovery of new JNK3 inhibitory chemotypes via QSAR-Guided selection of docking-based pharmacophores and comparison with other structure-based pharmacophore modeling methods

Tuffaha, G. O., Hatmal, M. M., & Taha, M. O. (2019) · Journal of Molecular Graphics and Modelling · doi:10.1016/j.jmgm.2019.05.015 · Cited by 23 · see citing works

Seven Cysteine-Deficient Mutants Depict the Interplay between Thermal and Chemical Stabilities of Individual Cysteine Residues in Mitogen-Activated Protein Kinase c-Jun N-Terminal Kinase 1

Nakaniwa, T., Fukada, H., Inoue, T., Gouda, M., Nakai, R., Kirii, Y., Adachi, M., Tamada, T., Segawa, S.-I., Kuroki, R., et al. (2012) · Biochemistry · doi:10.1021/bi300918w · Cited by 23 · see citing works

Fluorescence polarization-based assays for detecting compounds binding to inactive c-Jun N-terminal kinase 3 and p38α mitogen-activated protein kinase

Ansideri, F., Lange, A., El‐Gokha, A., Boeckler, F. M., & Koch, P. (2016) · Analytical Biochemistry · doi:10.1016/j.ab.2016.02.018 · Cited by 22 · see citing works

Exploration of a Binding Mode of Benzothiazol-2-yl Acetonitrile Pyrimidine Core Based Derivatives as Potent c-Jun N-Terminal Kinase-3 Inhibitors and 3D-QSAR Analyses

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A direct ELISA assay for quantitative determination of the inhibitory potency of small molecules inhibitors for JNK3

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Aminopyridine carboxamides as c-Jun N-terminal kinase inhibitors: Targeting the gatekeeper residue and beyond

Liu, G., Zhao, H., Liu, B., Xin, Z., Liu, M., Kosogof, C., Szczepankiewicz, B. G., Wang, S., Clampit, J. E., Gum, R. J., et al. (2006) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2006.08.097 · Cited by 21 · see citing works

Discovery of Bis-imidazolecarboxamide Derivatives as Novel, Potent, and Selective TNIK Inhibitors for the Treatment of Idiopathic Pulmonary Fibrosis

Aladinskiy, V., Kruse, C. G., Qin, L., Babin, E., Fan, Y., Andreev, G., Zhao, H., Fu, Y., Zhang, M., Ivanenkov, Y. A., et al. (2024) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.4c01580 · Cited by 19 · see citing works

Identifying, cloning and structural analysis of differentially expressed genes upon Puccinia infection of Festuca rubra var. rubra

Ergen, N. Z., Doğanay, G. D., Shearman, R. C., & Budak, H. (2007) · Gene · doi:10.1016/j.gene.2007.02.005 · Cited by 19 · see citing works

The use of biophysical methods increases success in obtaining liganded crystal structures

Chung, C. (2006) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444906051869 · Cited by 19 · see citing works

Enhancing Industrial Hemp (Cannabis sativa) Leaf By-Products: Bioactive Compounds, Anti-Inflammatory Properties, and Potential Health Applications

Frusciante, L., Geminiani, M., Shabab, B., Olmastroni, T., Roncucci, N., Mastroeni, P., Salvini, L., Lamponi, S., Trezza, A., & Santucci, A. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26020548 · Cited by 20 · see citing works

Assessing potency of c-Jun N-terminal kinase 3 (JNK3) inhibitors using 2D molecular descriptors and binary QSAR methodology

Ijjaali, I., Petitet, F., Dubus, E., Barberan, O., & Michel, A. G. (2007) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2007.03.062 · Cited by 18 · see citing works

Disruption of the EGFR E884–R958 ion pair conserved in the human kinome differentially alters signaling and inhibitor sensitivity

Tang, Z., Jiang, S., Du, R., Petri, E. T., El-Telbany, A., Chan, P. S. O., Kijima, T., Dietrich, S., Matsui, K., Kobayashi, M., et al. (2008) · Oncogene · doi:10.1038/onc.2008.411 · Cited by 18 · see citing works

On the in silico and in vitro anticancer activity of sulfonamide chalcones: potential JNKK3 inhibitors

Custódio, J. M. F., Moura, A. F., de Moraes, M. O., Pérez, C. N., & Napolitano, H. B. (2020) · New Journal of Chemistry · doi:10.1039/c9nj05612b · Cited by 17 · see citing works

Crystallization of MAP kinases

Lee, S., Zhou, T., & Goldsmith, E. J. (2006) · Methods · doi:10.1016/j.ymeth.2006.05.003 · Cited by 17 · see citing works

Cross-Reactivity Virtual Profiling of the Human Kinome by X-ReactKIN: A Chemical Systems Biology Approach

Bryliński, M., & Skolnick, J. (2010) · Molecular Pharmaceutics · doi:10.1021/mp1002976 · Cited by 16 · see citing works

Novel Tryptanthrin Derivatives with Selectivity as c–Jun N–Terminal Kinase (JNK) 3 Inhibitors

Schepetkin, I. A., Karpenko, O. S., Kovrizhina, A. R., Kirpotina, L. N., Khlebnikov, А. I., Chekal, S. I., Radudik, A. V., Shybinska, M. O., & Quinn, M. T. (2023) · Molecules · doi:10.3390/molecules28124806 · Cited by 15 · see citing works

Discovery of a novel small molecule PT109 with multi-targeted effects against Alzheimer's disease in vitro and in vivo

Chen, Q., Tu, Y., Mak, S., Chen, J., Lu, J., Chen, C., Yang, X., Wang, S., Wen, S., Ma, S., et al. (2020) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2020.173361 · Cited by 15 · see citing works

Considerations of Protein Subpockets in Fragment‐Based Drug Design

Bartolowits, M. D., & Davisson, V. J. (2015) · Chemical Biology & Drug Design · doi:10.1111/cbdd.12631 · Cited by 13 · see citing works

Ligand-based and structure-based approaches in identifying ideal pharmacophore against c-Jun N-terminal kinase-3

Suneel Kumar, B. V. S., Kotla, R., Buddiga, R., Roy, J., Singh, S. S., Gundla, R., Ravikumar, M., & Sarma, J. A. R. P. (2010) · Journal of Molecular Modeling · doi:10.1007/s00894-010-0701-0 · Cited by 14 · see citing works

Hemodynamic effects of potent and selective JNK inhibitors in anesthetized rats: Implication for targeting protein kinases in metabolic diseases

Liu, G., Zhao, H., Liu, B., Xin, Z., Liu, M., Serby, M. D., Lubbers, N. L., Widomski, D. L., Polakowski, J. S., Beno, D. W. A., et al. (2006) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2006.10.013 · Cited by 14 · see citing works

c-Jun N-terminal kinases 3 (JNK3) from orange-spotted grouper, Epinephelus coioides, inhibiting the replication of Singapore grouper iridovirus (SGIV) and SGIV-induced apoptosis

Guo, M., Wei, J., Zhou, Y., & Qin, Q. (2016) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2016.06.009 · Cited by 13 · see citing works

Identifying New Ligands for JNK3 by Fluorescence Thermal Shift Assays and Native Mass Spectrometry

Cheng, C., Liu, M., Gao, X., Wu, D., Pu, M., Ma, J., Quinn, R. J., Xiao, Z., & Liu, Z. (2022) · ACS Omega · doi:10.1021/acsomega.2c00340 · Cited by 12 · see citing works

Bioactive Potential of Sweet Cherry (Prunus avium L.) Waste: Antioxidant and Anti-Inflammatory Properties for Sustainable Applications

Frusciante, L., Nyong'a, C. N., Trezza, A., Shabab, B., Olmastroni, T., Barletta, R., Mastroeni, P., Visibelli, A., Orlandini, M., Raucci, L., et al. (2025) · Foods · doi:10.3390/foods14091523 · Cited by 11 · see citing works

LASSBio‐1829 Hydrochloride: Development of a New Orally Active N‐Acylhydrazone IKK2 Inhibitor with Anti‐inflammatory Properties

Guedes, I. A., de Freitas, R. H. C. N., Cordeiro, N. D. M., do Nascimento, T. S., Valerio, T. S., Fernandes, P. D., Dardenne, L. E., & Fraga, C. A. M. (2015) · ChemMedChem · doi:10.1002/cmdc.201500266 · Cited by 11 · see citing works

Substituting c-Jun N-terminal kinase-3 (JNK3) ATP-binding site amino acid residues with their p38 counterparts affects binding of JNK- and p38-selective inhibitors

Fricker, M., LoGrasso, P. V., Ellis, S., Wilkie, N. M., Hunt, P. A., & Pollack, S. J. (2005) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2005.04.013 · Cited by 11 · see citing works

JNK Mediates Differentiation, Cell Polarity and Apoptosis During Amphioxus Development by Regulating Actin Cytoskeleton Dynamics and ERK Signalling

Somorjai, I. M. L., Ehebauer, M., Escrivá, H., & Garcia-Fernàndez, J. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.749806 · Cited by 7 · see citing works

Targeting JNK3 for Alzheimer's disease: Design and synthesis of novel inhibitors with aryl group diversity utilizing wide pocket

Kim, H., Park, H., Jun, J., Moon, J., Oh, J., Bhujbal, S. P., & Hah, J. (2025) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2024.117209 · Cited by 10 · see citing works

Anthrapyrazolone analogues intercept inflammatory JNK signals to moderate endotoxin induced septic shock

Karothu, D. P., Trinath, J., Biswas, A., Sekar, K., Balaji, K. N., & Row, T. N. G. (2014) · Scientific Reports · doi:10.1038/srep07214 · Cited by 10 · see citing works

Achieving High Quality Ligand Chemistry in Protein-Ligand Crystal Structures for Drug Design

Smart, O. S., & Bricogne, G. (2015) · NATO science for peace and security series. A, Chemistry and biology · doi:10.1007/978-94-017-9719-1_13 · Cited by 10 · see citing works

Lead Generation and Optimization Based on Protein-Ligand Complementarity

Ogata, K., Isomura, T., Kawata, S., Yamashita, H., Kubodera, H., & Wodak, S. J. (2010) · Molecules · doi:10.3390/molecules15064382 · Cited by 10 · see citing works

Dihydroartemisinin as a potential drug candidate for cancer therapy: a structural-based virtual screening for multitarget profiling

Malami, I., Bunza, A. M., Alhassan, A. M., Muhammad, A. I., Abubakar, I. B., Yunusa, A., Waziri, P. M., & Etti, I. C. (2020) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2020.1824811 · Cited by 9 · see citing works

Explaining Isoform Selectivity of c-Jun N-Terminal Kinase 3 (JNK3) Inhibitors through Its Development and Structural Insights

Yu, H., Zhang, X., Liu, Z., & Zhang, L. (2025) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5c01488 · Cited by 4 · see citing works

Fragment-Based and Structural Investigation for Discovery of JNK3 Inhibitors

Duong, M. T. H., & Ahn, H. (2022) · Pharmaceutics · doi:10.3390/pharmaceutics14091900 · Cited by 4 · see citing works

C-Jun N-terminal kinase inhibitors: Structural insight into kinase-inhibitor complexes

Duong, M. T. H., Lee, J., & Ahn, H. (2020) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2020.06.013 · Cited by 34 · see citing works

Insight into the selective inhibition of JNK family members through structure-based drug design

Messoussi, A., Chevé, G., Bougrin, K., & Yasri, A. (2016) · MedChemComm · doi:10.1039/c5md00562k · Cited by 3 · see citing works

N-(3-Cyano-4,5,6,7-tetrahydro-1-benzothien-2-yl)amides as potent, selective, inhibitors of JNK2 and JNK3

Angell, R. M., Atkinson, F. L., Brown, M. J. B., Chuang, T. T., Christopher, J. A., Cichy-Knight, M. A., Dunn, A. K., Hightower, K. E., Malkakorpi, S., Musgrave, J. R., et al. (2006) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2006.12.003 · Cited by 95 · see citing works