Cited by 220Protein Kinase Regulation and GTPase SignalingMelanoma and MAPK PathwaysProtein Tyrosine Phosphatases

The DOI matches its Crossref record; 44 of the 45 references it cites were found in a registry or an index.

Identification of the Critical Features of a Small Peptide Inhibitor of JNK Activity

Open access

Barr, Renae K., Kendrick, Tulene S., Bogoyevitch, Marie A.·2002·Journal of Biological Chemistry

Open this paper in CoChat — free account Open PDF

Abstract

The c-Jun N-terminal kinases (JNKs) are a subfamily of the mitogen-activated protein kinases (MAPKs). Although progress in evaluating the functions of other MAPKs has been facilitated by the characterization of specific inhibitors, no JNK-directed inhibitor is commercially available. We have identified a 21-amino acid peptide inhibitor of activated JNKs, based on amino acids 143-163 of the JNK-binding domain (JBD) of the JNK scaffolding protein, JNK-interacting protein-1 (JIP-1). This peptide, I-JIP (Inhibitor of JNK-based on JIP-1), inhibited JNK activity in vitro toward recombinant c-Jun, Elk, and ATF2 up to 90%. A truncated I-JIP (TI-JIP), the C-terminal 11 amino acids of I-JIP, directly interacted with recombinant JNKs but not its substrates as shown by surface plasmon resonance analysis. Scanning alanine replacement within truncated I-JIP identified 4 residues (Arg-156, Pro-157, Leu-160, or Leu-162) as independently critical for inhibition. JBD peptide sequences from JIP-2 and JIP-3 shared these critical residues and accordingly were effective JNK inhibitors. In contrast, peptides based on the JBDs of ATF2 and c-Jun inhibited JNK activity by <40%, which agreed with their lack of homology to the critical Arg-156 and Pro-157. These studies thus define a small peptide inhibitor sequence of JNKs based on the JIP proteins.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1074/jbc.m107565200

Cites

44 of 44 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Signal transduction by the JNK group of MAP kinases
Davis, R. J. (2000) · Cell · doi:10.1016/s0092-8674(00)00116-1 · Cited by 4,237
PD 098059 Is a Specific Inhibitor of the Activation of Mitogen-activated Protein Kinase Kinase in Vitro and in Vivo
Alessi, D. R., Cuenda, A., Cohen, P., Dudley, D. T., & Saltiel, A. R. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.46.27489 · Cited by 3,374
A protein kinase involved in the regulation of inflammatory cytokine biosynthesis
Lee, J. C., Laydon, J. T., McDonnell, P., Gallagher, T. F., Kumar, S., Green, D., McNulty, D. E., Blumenthal, M. J., Keys, J., vatter, S. W. L., et al. (1994) · Nature · doi:10.1038/372739a0 · Cited by 3,266
JNK1: A protein kinase stimulated by UV light and Ha-Ras that binds and phosphorylates the c-Jun activation domain
Dérijard, B., Hibi, M., Wu, I.-H., Barrett, T., Su, B., Deng, T., Karin, M., & Davis, R. J. (1994) · Cell · doi:10.1016/0092-8674(94)90380-8 · Cited by 3,188
The stress-activated protein kinase subfamily of c-Jun kinases
Kyriakis, J. M., Banerjee, P. T., Nikolakaki, E., Dai, T., Rubie, E. A., Ahmad, M. F., Avruch, J., & Woodgett, J. R. (1994) · Nature · doi:10.1038/369156a0 · Cited by 2,601
SP600125, an anthrapyrazolone inhibitor of Jun N-terminal kinase
Bennett, B. L., Sasaki, D. T., Murray, B. W., O'Leary, E. C., Sakata, S. T., Xu, W., Leisten, J. C., Motiwala, A., Pierce, S., Satoh, Y., et al. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.251194298 · Cited by 2,558
Signal Transduction through MAP Kinase Cascades
Lewis, T. S., Shapiro, P. S., & Ahn, N. G. (1998) · Advances in cancer research · doi:10.1016/s0065-230x(08)60765-4 · Cited by 1,759
Selective interaction of JNK protein kinase isoforms with transcription factors.
Gupta, S., Barrett, T., Whitmarsh, A. J., Cavanagh, J., Sluss, H. K., Dérijard, B., & Davis, R. J. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00636.x · Cited by 1,341
Organization and regulation of mitogen-activated protein kinase signaling pathways
Garrington, T. P., & Johnson, G. L. (1999) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(99)80028-3 · Cited by 1,268
Absence of excitotoxicity-induced apoptosis in the hippocampus of mice lacking the Jnk3 gene
Yang, D. D., Kuan, C.-Y., Whitmarsh, A. J., Rinócn, M., Zheng, T. S., Davis, R. J., RAKIC, P. T., & Flavell, R. A. (1997) · Nature · doi:10.1038/39899 · Cited by 1,230

Show all 45 references

Research works printed but not linked: 1

Elion, 1998, Nature, 281, 1625

Sorted by citations

Endoplasmic Reticulum Stress Links Obesity, Insulin Action, and Type 2 Diabetes
Özcan, U., Cao, Q., Yilmaz, E., Lee, A.-H., Iwakoshi, N. N., Özdelen, E., Tuncman, G., Görgün, C., Glimcher, L. H., & Hotamisligil, G. S. (2004) · Science · doi:10.1126/science.1103160 · Cited by 3,844
Excitotoxicity and stroke: Identifying novel targets for neuroprotection
Lai, T. W., Zhang, S., & Wang, Y. T. (2014) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2013.11.006 · Cited by 1,106
A peptide inhibitor of c-Jun N-terminal kinase protects against excitotoxicity and cerebral ischemia
Borsello, T., Clarke, P. G. H., Hirt, L., Vercelli, A., Repici, M., Schorderet, D. F., Bogousslavsky, J., & Bonny, C. (2003) · Nature Medicine · doi:10.1038/nm911 · Cited by 658
Uses for JNK: the Many and Varied Substrates of the c-Jun N-Terminal Kinases
Bogoyevitch, M. A., & Kobe, B. (2006) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00025-06 · Cited by 584
Self-citation
JNK Signaling: Regulation and Functions Based on Complex Protein-Protein Partnerships
Zeke, A., Misheva, M., Reményi, A., & Bogoyevitch, M. A. (2016) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00043-14 · Cited by 552
Self-citation
Survey of the year 2003 commercial optical biosensor literature
Rich, R. L., & Myszka, D. G. (2004) · Journal of Molecular Recognition · doi:10.1002/jmr.726 · Cited by 506
Block of Long-Term Potentiation by Naturally Secreted and Synthetic Amyloid β-Peptide in Hippocampal Slices Is Mediated via Activation of the Kinases c-Jun N-Terminal Kinase, Cyclin-Dependent Kinase 5, and p38 Mitogen-Activated Protein Kinase as well as Metabotropic Glutamate Receptor Type 5
Wang, Q., Walsh, D. M., Rowan, M. J., Selkoe, D. J., & Anwyl, R. (2004) · The Journal of Neuroscience · doi:10.1523/jneurosci.1633-03.2004 · Cited by 437
c-Jun N-terminal Kinase (JNK) Signaling as a Therapeutic Target for Alzheimer’s Disease
Yarza, R., Vela, S., Solas, M., & Ramírez, M. J. (2016) · Frontiers in Pharmacology · doi:10.3389/fphar.2015.00321 · Cited by 428
Advanced glycation end products stimulate osteoblast apoptosis via the MAP kinase and cytosolic apoptotic pathways
Alikhani, M., Alikhani, Z., Boyd, C. M., MacLellan, C. M., Raptis, M., Liu, R., Pischon, N., Trackman, P. C., Gerstenfeld, L. C., & Graves, D. T. (2006) · Bone · doi:10.1016/j.bone.2006.09.011 · Cited by 376
A Peptide Inhibitor of c-Jun N-Terminal Kinase Protects against Both Aminoglycoside and Acoustic Trauma-Induced Auditory Hair Cell Death and Hearing Loss
Wang, J., Water, T. R. V. D., Bonny, C., de Ribaupierre, F., Puel, J., & Zine, A. (2003) · Journal of Neuroscience · doi:10.1523/jneurosci.23-24-08596.2003 · Cited by 366
JNK signalling in cancer: in need of new, smarter therapeutic targets
Bubici, C., & Papa, S. (2013) · British Journal of Pharmacology · doi:10.1111/bph.12432 · Cited by 355
BACH2 regulates CD8+ T cell differentiation by controlling access of AP-1 factors to enhancers
Roychoudhuri, R., Clever, D. C., Li, P., Wakabayashi, Y., Quinn, K. M., Klebanoff, C. A., Ji, Y., Sukumar, M., Eil, R. L., Yu, Z., et al. (2016) · Nature Immunology · doi:10.1038/ni.3441 · Cited by 317
c-Jun N-terminal kinase (JNK) signaling: Recent advances and challenges
Bogoyevitch, M. A., Ngoei, K. R. W., Zhao, T. T., Yeap, Y. Y. C., & Ng, D. C. H. (2009) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2009.11.002 · Cited by 335
Self-citation
Targeting NMDA receptors in stroke: new hope in neuroprotection
Wu, Q. J., & Tymianski, M. (2018) · Molecular Brain · doi:10.1186/s13041-018-0357-8 · Cited by 338
The JNK Signaling Pathway in Inflammatory Skin Disorders and Cancer
Hammouda, M., Ford, A. E., Liu, Y., & Zhang, J. Y. (2020) · Cells · doi:10.3390/cells9040857 · Cited by 296
Pathogenic huntingtin inhibits fast axonal transport by activating JNK3 and phosphorylating kinesin
Morfini, G. A., You, Y., Pollema, S. L., Kaminska, A., Liu, K., Yoshioka, K., Björkblom, B., Coffey, E. T., Bagnato, C., Han, D. K. M., et al. (2009) · Nature Neuroscience · doi:10.1038/nn.2346 · Cited by 276
Structural basis for the selective inhibition of JNK1 by the scaffolding protein JIP1 and SP600125
Heo, Y., Kim, S., Seo, C. I., Kim, Y. K., Sung, B., Lee, H. S., Lee, J. I., Park, S., Kim, J. H., Hwang, K. Y., et al. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600212 · Cited by 275
Targeting the JNK MAPK cascade for inhibition: basic science and therapeutic potential
Bogoyevitch, M. A., Boehm, I., Oakley, A. J., Ketterman, A. J., & Barr, R. K. (2003) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2003.11.016 · Cited by 270
Self-citation
JNK3 Perpetuates Metabolic Stress Induced by Aβ Peptides
Yoon, S. O., Park, D. J., Ryu, J. C., Özer, H. G., Tep, C., Shin, Y. J., Lim, T. H., Pastorino, L., Kunwar, A. J., Walton, J. C., et al. (2012) · Neuron · doi:10.1016/j.neuron.2012.06.024 · Cited by 243
JNK Signalling: A Possible Target to Prevent Neurodegeneration
Borsello, T., & Forloni, G. (2007) · Current Pharmaceutical Design · doi:10.2174/138161207780858384 · Cited by 226
Neuroprotection against Focal Ischemic Brain Injury by Inhibition of c-Jun N-Terminal Kinase and Attenuation of the Mitochondrial Apoptosis-Signaling Pathway
Gao, Y., Signore, A. P., Yin, W., Cao, G., Yin, X., Sun, F., Luo, Y., Graham, S. H., & Chen, J. (2005) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/sj.jcbfm.9600062 · Cited by 219
Mitogen-activated protein kinase pathways in redox signaling
Torrès, M. (2003) · Frontiers in bioscience · doi:10.2741/999 · Cited by 221
JNK pathway: diseases and therapeutic potential
Cui, J., Zhang, M., Zhang, Y., & Xu, Z. (2007) · Acta Pharmacologica Sinica · doi:10.1111/j.1745-7254.2007.00579.x · Cited by 202
The PPE18 of Mycobacterium tuberculosis Interacts with TLR2 and Activates IL-10 Induction in Macrophage
Nair, S., Ramaswamy, P. A., Ghosh, S., Joshi, D., Pathak, N., Siddiqui, I., Sharma, P., Hasnain, S. E., Mande, S. C., & Mukhopadhyay, S. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0901367 · Cited by 198
JNK mediates pathogenic effects of polyglutamine-expanded androgen receptor on fast axonal transport
Morfini, G. A., Pigino, G. F., Szebenyi, G., You, Y., Pollema, S. L., & Brady, S. T. (2006) · Nature Neuroscience · doi:10.1038/nn1717 · Cited by 202
Approaches to discover non-ATP site kinase inhibitors
Gavrin, L. K., & Saiah, E. (2012) · MedChemComm · doi:10.1039/c2md20180a · Cited by 186
Identification of a new JNK inhibitor targeting the JNK-JIP interaction site
Stebbins, J. L., De, S. K., Machleidt, T., Becattini, B., Vazquez, J., Kuntzen, C., Chen, L.-H., Cellitti, J. F., Riel-Mehan, M., Emdadi, A., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0805677105 · Cited by 186
PLD1 and ERK2 regulate cytosolic lipid droplet formation
Andersson, L. K., Boström, P., Ericson, J., Rutberg, M., Magnusson, B., Marchesan, D., Ruiz, M., Asp, L., Huang, P. C., Frohman, M. A., et al. (2006) · Journal of Cell Science · doi:10.1242/jcs.02941 · Cited by 180
ERK1/2 Activation Mediates Aβ Oligomer-induced Neurotoxicity via Caspase-3 Activation and Tau Cleavage in Rat Organotypic Hippocampal Slice Cultures
Chong, Y. H., Shin, Y. J., Lee, E. O., Kayed, R., Glabe, C. G., & Tenner, A. J. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m601016200 · Cited by 165
A new paradigm for protein kinase inhibition: blocking phosphorylation without directly targeting ATP binding
Bogoyevitch, M. A., & Fairlie, D. P. (2007) · Drug Discovery Today · doi:10.1016/j.drudis.2007.06.008 · Cited by 164
Self-citation
Advanced glycation end products induce apoptosis in fibroblasts through activation of ROS, MAP kinases, and the FOXO1 transcription factor
Alikhani, M., MacLellan, C. M., Raptis, M., Vora, S. R., Trackman, P. C., & Graves, D. T. (2006) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00356.2006 · Cited by 162
Role of NF-κB in transcriptional regulation of the phagocyte NADPH oxidase by tumor necrosis factor-α
Gauss, K. A., Nelson-Overton, L. K., Siemsen, D. W., Gao, Y., DeLeo, F. R., & Quinn, M. T. (2007) · Journal of Leukocyte Biology · doi:10.1189/jlb.1206735 · Cited by 157
Expression of IL-24, an Activator of the JAK1/STAT3/SOCS3 Cascade, Is Enhanced in Inflammatory Bowel Disease
Andoh, A., Shioya, M., Nishida, A., Bamba, S., Tsujikawa, T., Kim‐Mitsuyama, S., & Fujiyama, Y. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0804169 · Cited by 156
Leptin enhances TNF-α production via p38 and JNK MAPK in LPS-stimulated Kupffer cells
Shen, J., Sakaida, I., Uchida, K., Terai, S., & OKITA, K. (2005) · Life Sciences · doi:10.1016/j.lfs.2005.04.004 · Cited by 163
12-O-tetradecanoylphorbol-13-acetate (TPA) Inhibits Osteoclastogenesis by Suppressing RANKL-Induced NF-κB Activation
Wang, C., Steer, J. H., Joyce, D. A., Yip, K. H. M., Zheng, M., & Xu, J. (2003) · Journal of Bone and Mineral Research · doi:10.1359/jbmr.2003.18.12.2159 · Cited by 138
Cooperation between JNK1 and JNK2 in activation of p53 apoptotic pathway
Oleinik, N. V., Krupenko, N. I., & Krupenko, S. A. (2007) · Oncogene · doi:10.1038/sj.onc.1210526 · Cited by 133
Inhibitors of c-Jun N-terminal kinases—JuNK no more?
Bogoyevitch, M. A., & Arthur, P. G. (2007) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2007.09.013 · Cited by 129
Self-citation
Targeting JNK3 for the treatment of neurodegenerative disorders
Resnick, L., & Fennell, M. (2004) · Drug Discovery Today · doi:10.1016/s1359-6446(04)03251-9 · Cited by 128
Glucocorticoid receptor–JNK interaction mediates inhibition of the JNK pathway by glucocorticoids
Bruna, A., Nicolàs, M., Muñoz, A., Kyriakis, J. M., & Caelles, C. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg590 · Cited by 130
Inhibition of Fast Axonal Transport by Pathogenic SOD1 Involves Activation of p38 MAP Kinase
Morfini, G. A., Bosco, D. A., Brown, H. E., Gatto, R. G., Kamińska, A., Song, Y., Molla, L., Baker, L. M., Marangoni, N., Berth, S. H., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0065235 · Cited by 121
A Docking Site in MKK4 Mediates High Affinity Binding to JNK MAPKs and Competes with Similar Docking Sites in JNK Substrates
Ho, D. T., Bardwell, A. J., Abdollahi, M., & Bardwell, L. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304229200 · Cited by 108
Characterization of the molecular mechanisms underlying increased ischemic damage in the aldehyde dehydrogenase 2 genetic polymorphism using a human induced pluripotent stem cell model system
Ebert, A., Kodo, K., Liang, P., Wu, H., Huber, B. C., Riegler, J., Churko, J. M., Lee, J., de Almeida, P. E., Lan, F., et al. (2014) · Science Translational Medicine · doi:10.1126/scitranslmed.3009027 · Cited by 102
PepCrawler: a fast RRT-based algorithm for high-resolution refinement and binding affinity estimation of peptide inhibitors
Donsky, E., & Wolfson, H. J. (2011) · Bioinformatics · doi:10.1093/bioinformatics/btr498 · Cited by 103
A peptide inhibitor of c-Jun NH2-terminal kinase reduces myocardial ischemia-reperfusion injury and infarct size in vivo
Milano, G., Morel, S., Bonny, C., Samaja, M., von Segesser, . K., NICOD, P. H., & Vassalli, G. (2006) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.01117.2006 · Cited by 97
Design, Synthesis, and Structure−Activity Relationship of Substrate Competitive, Selective, and in Vivo Active Triazole and Thiadiazole Inhibitors of the c-Jun N-Terminal Kinase
De, S. K., Stebbins, J. L., Chen, L., Riel-Mehan, M. M., Machleidt, T., Dahl, R. S., Yuan, H., Emdadi, A., Barile, E., Chen, V., et al. (2009) · Journal of Medicinal Chemistry · doi:10.1021/jm801503n · Cited by 95
Inhibition of JNK by a Peptide Inhibitor Reduces Traumatic Brain Injury–Induced Tauopathy in Transgenic Mice
Tran, H., Sanchez, L., & Brody, D. L. (2012) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e3182456aed · Cited by 93
A survey of the year 2002 commercial optical biosensor literature
Rich, R. L., & Myszka, D. G. (2003) · Journal of Molecular Recognition · doi:10.1002/jmr.649 · Cited by 93
The cell cycle as a therapeutic target for Alzheimer's disease
Neve, R. L., & McPhie, D. L. (2006) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2005.09.005 · Cited by 92
FOXO1 constrains activation and regulates senescence in CD8 T cells
Delpoux, A., Marcel, N., Michelini, R. H., Katayama, C. D., Allison, K. A., Glass, C. K., Quiñones‐Parra, S. M., Murre, C., Loh, L., Kedzierska, K., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2020.108674 · Cited by 92
Inhibition of the JNK/AP-1 pathway reduces neuronal death and improves behavioral outcome after neonatal hypoxic–ischemic brain injury
Nijboer, C. H. A., van der Kooij, M. A., van Bel, F., Ohl, F., Heijnen, C. J., & Kavelaars, A. (2009) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2009.09.008 · Cited by 87
JNK3 as a Therapeutic Target for Neurodegenerative Diseases
Antoniou, X., Falconi, M., Marino, D. D., & Borsello, T. (2011) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-091567 · Cited by 87
Small molecules from natural sources, targeting signaling pathways in diabetes
Liu, Q., Chen, L., Hu, L., Guo, Y., & Shen, X. (2010) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2010.06.004 · Cited by 86
Therapeutic peptides for cancer therapy. Part I – peptide inhibitors of signal transduction cascades
Bidwell, G. L., & Raucher, D. (2009) · Expert Opinion on Drug Delivery · doi:10.1517/17425240903143745 · Cited by 85
Bone morphogenetic protein 4 mediates myocardial ischemic injury through JNK-dependent signaling pathway
Pachori, A. S., Custer, L. M., Hansen, D., Clapp, S., Kemppa, E., & Klingensmith, J. (2010) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2010.01.010 · Cited by 84
Implication of the JNK pathway in a rat model of Huntington's disease
Perrin, V., Dufour, N., Raoul, C., Hässig, R., Brouillet, E., Aebischer, P., Luthi‐Carter, R., & Déglon, N. (2008) · Experimental Neurology · doi:10.1016/j.expneurol.2008.10.008 · Cited by 83
Inhibition of c-Jun kinase provides neuroprotection in a model of Alzheimer's disease
Braithwaite, S. P., Schmid, R. S., Dong, H., Sung, M.-L. A., Cho, S., Resnick, L., Monaghan, M. M., Hirst, W. D., Essrich, C., Reinhart, P. H., et al. (2010) · Neurobiology of Disease · doi:10.1016/j.nbd.2010.04.015 · Cited by 82
Suppressive Effects of Statins on Acute Promyelocytic Leukemia Cells
Sassano, A., Katsoulidis, E., Antico, G., Altman, J. K., Redig, A. J., Minucci, S., Tallman, M. S., & Platanias, L. C. (2007) · Cancer Research · doi:10.1158/0008-5472.can-06-3686 · Cited by 80
Serpin squamous cell carcinoma antigen inhibits UV-induced apoptosis via suppression of c-JUN NH2-terminal kinase
Katagiri, C., Nakanishi, J., Kadoya, K., & Hibino, T. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200508064 · Cited by 80
Discovery and Characterization of Non-ATP Site Inhibitors of the Mitogen Activated Protein (MAP) Kinases
Comess, K. M., Sun, C. C., Abad‐Zapatero, C., Goedken, E. R., Gum, R. J., Borhani, D. W., Argiriadi, M. A., Groebe, D. R., Jia, Y., Clampit, J. E., et al. (2010) · ACS Chemical Biology · doi:10.1021/cb1002619 · Cited by 80
Mitogen activated protein kinase inhibitors: where are we now and where are we going?
Sweeney, S. E., & Firestein, G. S. (2006) · Annals of the Rheumatic Diseases · doi:10.1136/ard.2006.058388 · Cited by 78
Small Molecule JNK (c-Jun N-Terminal Kinase) Inhibitors
Siddiqui, M. A., & Reddy, P. A. (2010) · Journal of Medicinal Chemistry · doi:10.1021/jm9003279 · Cited by 76
JNK- and IκB-dependent pathways regulate MCP-1 but not adiponectin release from artificially hypertrophied 3T3-L1 adipocytes preloaded with palmitate in vitro
Takahashi, K., Yamaguchi, S., Shimoyama, T., Seki, H., Miyokawa, K., Katsuta, H., Tanaka, T., Yoshimoto, K., Ohno, H., Nagamatsu, S., et al. (2008) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00131.2007 · Cited by 79
Docking Interactions in the c-Jun N-terminal Kinase Pathway
Mooney, L. M., & Whitmarsh, A. J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m311841200 · Cited by 73
Mitochondrial JNK phosphorylation as a novel therapeutic target to inhibit neuroinflammation and apoptosis after neonatal ischemic brain damage
Nijboer, C. H. A., Bonestroo, H. J. C., Zijlstra, J., Kavelaars, A., & Heijnen, C. J. (2013) · Neurobiology of Disease · doi:10.1016/j.nbd.2013.01.017 · Cited by 76
Peptide inhibitors of protein kinases—discovery, characterisation and use
Bogoyevitch, M. A., Barr, R. K., & Ketterman, A. J. (2005) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2005.07.025 · Cited by 77
Self-citation
Single-domain near-infrared protein provides a scaffold for antigen-dependent fluorescent nanobodies
Oliinyk, O. S., Baloban, M., Clark, C. L., Carey, E. M., Pletnev, S. V., Nimmerjahn, A., & Verkhusha, V. V. (2022) · Nature Methods · doi:10.1038/s41592-022-01467-6 · Cited by 73
Blocking c-Jun N-terminal Kinase (JNK) Translocation to the Mitochondria Prevents 6-Hydroxydopamine-induced Toxicity in Vitro and in Vivo
Chambers, J. W., Howard, S., & LoGrasso, P. V. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.421354 · Cited by 72
Inhibition of Tumor Growth, Angiogenesis, and Tumor Cell Proliferation by a Small Molecule Inhibitor of c-Jun N-terminal Kinase
Ennis, B. W., Fultz, K. E., Smith, K. A., Westwick, J. K., Zhu, D., Boluro-Ajayi, M., Bilter, G. K., & Stein, B. (2005) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.104.078873 · Cited by 70
Induction of Apoptosis in BCR/ABL+ Cells By Histone Deacetylase Inhibitors Involves Reciprocal Effects on the RAF/MEK/ERK and JNK Pathways
Yu, C., Subler, M. A., Rahmani, M., Reese, E., Krystal, G. W., Conrad, D. H., Dent, P., & Grant, S. (2003) · Cancer Biology & Therapy · doi:10.4161/cbt.2.5.454 · Cited by 70
The proinflammatory cytokines IL-1β and TNF-α induce the expression of Synoviolin, an E3 ubiquitin ligase, in mouse synovial fibroblasts via the Erk1/2-ETS1 pathway
Gao, B., Calhoun, K. H., & Fang, D. (2006) · Arthritis Research & Therapy · doi:10.1186/ar2081 · Cited by 68
Revisiting protein kinase–substrate interactions: Toward therapeutic development
de Oliveira, P. S. L., Ferraz, F. A. N., Pena, D. A., Pramio, D. T., Morais, F. A., & Schechtman, D. (2016) · Science Signaling · doi:10.1126/scisignal.aad4016 · Cited by 69
FOXO1 plays an essential role in apoptosis of retinal pericytes.
Alikhani, M., Roy, S., & Graves, D. T. (2010) · PubMed Central · Cited by 63
A Novel c-Jun-dependent Signal Transduction Pathway Necessary for the Transcriptional Activation of Interferon γ Response Genes
Gough, D. J., Sabapathy, K., Ko, E. Y.-N., Arthur, H. A., Schreiber, R. D., Trapani, J. A., Clarke, C. J. P., & Johnstone, R. W. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m607674200 · Cited by 62
Regulation of Cell Survival and Death Signals Induced by Oxidative Stress
Kuwabara, M., Asanuma, T., Niwa, K., & Inanami, O. (2008) · Journal of Clinical Biochemistry and Nutrition · doi:10.3164/jcbn.2008045 · Cited by 62
Non-ATP competitive protein kinase inhibitors as anti-tumor therapeutics
Kirkland, L. O., & McInnes, C. (2009) · Biochemical Pharmacology · doi:10.1016/j.bcp.2008.12.022 · Cited by 60
The Critical Features and the Mechanism of Inhibition of a Kinase Interaction Motif-based Peptide Inhibitor of JNK
Barr, R. K., Boehm, I., Attwood, P. V., Watt, P. M., & Bogoyevitch, M. A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m402181200 · Cited by 61
Self-citation
Control of Paneth Cell Fate, Intestinal Inflammation, and Tumorigenesis by PKCλ/ι
Nakanishi, Y., Reina‐Campos, M., Nakanishi, N., Lladó, V., Elmeń, L., Peterson, S. N., Campos, A. R., De, S. K., Leitges, M., Ikeuchi, H., et al. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.08.054 · Cited by 62
Clinically Precedented Protein Kinases: Rationale for Their Use in Neurodegenerative Disease
Benn, C., & Dawson, L. A. (2020) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2020.00242 · Cited by 59
D-JNKi, a peptide inhibitor of c-Jun N-terminal kinase, promotes functional recovery after transient focal cerebral ischemia in rats
Esneault, E., Castagné, V., Moser, P. C., Bonny, C., & Bernaudin, M. (2008) · Neuroscience · doi:10.1016/j.neuroscience.2007.12.036 · Cited by 57
Identification of small-molecule inhibitors of the JIP–JNK interaction
Chen, T. X., Kablaoui, N. M., Little, J., Timofeevski, S. L., Tschantz, W. R., Chen, P., Feng, J., Charlton, M. E., Stanton, R. V., & Bauer, P. H. (2009) · Biochemical Journal · doi:10.1042/bj20081899 · Cited by 55
The scaffold protein IB1/JIP-1 is a critical mediator of cytokine-induced apoptosis in pancreatic β cells
Haefliger, J., Tawadros, T., Meylan, L., Gurun, S. L., Roehrich, M.-E., Martin, D., Thorens, B., & Waeber, G. (2003) · Journal of Cell Science · doi:10.1242/jcs.00356 · Cited by 55
Selective Inhibition of Mitochondrial JNK Signaling Achieved Using Peptide Mimicry of the Sab Kinase Interacting Motif-1 (KIM1)
Chambers, J. W., Cherry, L., Laughlin, J. D., Figuera-Losada, M., & LoGrasso, P. V. (2011) · ACS Chemical Biology · doi:10.1021/cb200062a · Cited by 54
Triterpenoid saponin, oleanolic acid 3-O-β-d-glucopyranosyl(1→3)-α-l-rhamnopyranosyl(1→2)-α-l-arabinopyranoside (OA) from Aralia elata inhibits LPS-induced nitric oxide production by down-regulated NF-κB in raw 264.7 cells
Suh, S., Jin, U., Kim, K., Son, J., Lee, S. H., Son, K.-H., Chang, H. W., Lee, Y., & Kim, C. (2007) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2007.08.025 · Cited by 54
Targeting the JNK Pathway as a Therapeutic Protective Strategy for Nervous System Diseases
Bonny, C., Borsello, T., & Zine, A. (2005) · Reviews in the Neurosciences · doi:10.1515/revneuro.2005.16.1.57 · Cited by 54
Defective Osteoclastogenesis by IKKβ-null Precursors Is a Result of Receptor Activator of NF-κB Ligand (RANKL)-induced JNK-dependent Apoptosis and Impaired Differentiation
Otero, J. E., Dai, S., Foglia, D., Alhawagri, M., Vacher, J., Pasparakis, M., & Abu‐Amer, Y. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m800434200 · Cited by 51
Anti-tumor chemotherapy utilizing peptide-based approaches--apoptotic pathways, kinases, and proteasome as targets.
Mendoza, F. J., Espino, P. S., Cann, K. L., Bristow, N. A., McCrea, K., & Łoś, M. (2005) · PubMed · Cited by 52
JNK signaling as a target for anticancer therapy
Abdelrahman, K. S., Hassan, H. A., Abdel‐Aziz, S. A., Marzouk, A. A. E., Narumi, A., Konno, H., & Abdel‐Aziz, M. (2021) · Pharmacological Reports · doi:10.1007/s43440-021-00238-y · Cited by 52
Characterizing the mode of action of extracellular Connexin43 channel blocking mimetic peptides in an in vitro ischemia injury model
Kim, Y., Griffin, J. M., Harris, P. W. R., Chan, S. H. C., Nicholson, L. F. B., Brimble, M. A., O’Carroll, S. J., & Green, C. R. (2016) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2016.11.001 · Cited by 53
Wandering beyond small molecules: peptides as allosteric protein modulators
Mannes, M., Martin, C., Menet, C. J., & Ballet, S. (2021) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2021.10.011 · Cited by 50
Pneumocystisstimulates MCP-1 production by alveolar epithelial cells through a JNK-dependent mechanism
Wang, J., Gigliotti, F., Bhagwat, S. P., Maggirwar, S. B., & Wright, T. W. (2007) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00452.2006 · Cited by 49
Development of JNK2-Selective Peptide Inhibitors That Inhibit Breast Cancer Cell Migration
Kaoud, T. S., Mitra, S., Lee, S., Taliaferro, J. M., Cantrell, M. A., Linse, K. D., Berg, C. L. V. D., & Dalby, K. N. (2011) · ACS Chemical Biology · doi:10.1021/cb200017n · Cited by 49
JNK Regulation of Depression and Anxiety
Hollós, P., Marchisella, F., & Coffey, E. T. (2017) · Brain Plasticity · doi:10.3233/bpl-170062 · Cited by 55
GSTpi modulates JNK activity through a direct interaction with JNK substrate, ATF2
Thévenin, A. F., Zony, C. L., Bahnson, B. J., & Colman, R. F. (2011) · Protein Science · doi:10.1002/pro.609 · Cited by 45
Constitutive JNK Activation in NIH 3T3 Fibroblasts Induces a Partially Transformed Phenotype
Rennefahrt, U. E. E., Illert, B., Kerkhoff, E., Troppmair, J., & Rapp, U. R. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m203010200 · Cited by 44
Use of cell-permeable peptides to prevent neuronal degeneration
Borsello, T., & Bonny, C. (2004) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2004.03.008 · Cited by 44
Facilitation of Stress-induced Phosphorylation of β-Amyloid Precursor Protein Family Members by X11-like/Mint2 Protein
Taru, H., & Suzuki, T. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m312007200 · Cited by 44
Therapeutic promise of JNK ATP-noncompetitive inhibitors
Bogoyevitch, M. A. (2005) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2005.03.005 · Cited by 43
Self-citation
Activation of p38 and N-acetylcysteine-sensitive c-Jun NH2-terminal kinase signaling cascades is required for induction of apoptosis in Parkinson's disease cybrids
Onyango, I. G., Tuttle, J. B., & Bennett, J. P. (2004) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2004.10.006 · Cited by 43
IL-1β–Induced Transcriptional Up-Regulation of Bradykinin B1 and B2 Receptors in Murine Airways
Zhang, Y., Mikael Adner, A., & Cardell, L. (2007) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2005-0369oc · Cited by 43
Novel Strategy for Treatment of Viral Central Nervous System Infection by Using a Cell-Permeating Inhibitor of c-Jun N-Terminal Kinase
Beckham, J. D., Goody, R. J., Clarke, P., Bonny, C., & Tyler, K. L. (2007) · Journal of Virology · doi:10.1128/jvi.00467-07 · Cited by 43

Authors: Barr, R. K., Kendrick, T. S., & Bogoyevitch, M. A.
Affiliations: The University of Western Australia (AU)
Corresponding author: Bogoyevitch, Marie A.
ORCID: Barr, Renae K.
Kendrick, Tulene S.
Bogoyevitch, Marie A.
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 2002-03
Volume: 277
Issue: 13
Pages: 10987-10997
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1074/jbc.m107565200
OpenAlex: W2035262124
Cited by: 211
References: 45
Citations by year: 2026: 1 · 2025: 4 · 2024: 5 · 2023: 2 · 2022: 5 · 2021: 3 · 2020: 3 · 2018: 4 · 2017: 6 · 2016: 12 · 2015: 2 · 2014: 2 · 2013: 13 · 2012: 9
FWCI: 4.97
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 6800 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed (publishedVersion)
UWA Profiles and Research Repository (UWA) (submittedVersion)
Funders: National Heart Foundation of Australia
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Melanoma and MAPK Pathways
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
Keywords: JNK, c-Jun N-terminal kinase, peptide inhibitors, JIP1, MAPK inhibitors, c-Jun, elk, ATF2, critical residues, alanine scanning, protein-protein interaction, kinase inhibition
MeSH terms: Amino Acid Sequence, Animals, DNA-Binding Proteins, Enzyme Inhibitors, Kinetics, Molecular Sequence Data, Peptides, Phosphorylation, Proto-Oncogene Proteins, Recombinant Proteins, Substrate Specificity, Transcription Factors, Cyclic AMP Response Element-Binding Protein, Sequence Homology, Amino Acid, COS Cells, Surface Plasmon Resonance, Mitogen-Activated Protein Kinases, JNK Mitogen-Activated Protein Kinases, p38 Mitogen-Activated Protein Kinases, ets-Domain Protein Elk-1, Activating Transcription Factor 2

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Identification of the Critical Features of a Small Peptide Inhibitor of JNK Activity

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks