Relevant bibliographies by topics / C-Jun N-terminal kinase (JNK)

Contents

  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers
  6. Reports

Academic literature on the topic 'C-Jun N-terminal kinase (JNK)'

Author: Grafiati
Published: 4 June 2021
Last updated: 6 September 2023

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Journal articles on the topic "C-Jun N-terminal kinase (JNK)"

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Liu, Jing, Yuzuru Minemoto, and Anning Lin. "c-Jun N-Terminal Protein Kinase 1 (JNK1), but Not JNK2, Is Essential for Tumor Necrosis Factor Alpha-Induced c-Jun Kinase Activation and Apoptosis." Molecular and Cellular Biology 24, no. 24 (December 15, 2004): 10844–56. http://dx.doi.org/10.1128/mcb.24.24.10844-10856.2004.

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ABSTRACT Two ubiquitously expressed isoforms of c-Jun N-terminal protein kinase (JNK), JNK1 and JNK2, have shared functions and different functions. However, the molecular mechanism is unknown. Here we report that JNK1, but not JNK2, is essential for tumor necrosis factor alpha (TNF-α)-induced c-Jun kinase activation, c-Jun expression, and apoptosis. Using mouse fibroblasts deficient in either Jnk1 or Jnk2, we found that JNK1 was activated by TNF-α, whereas JNK2 activation was negligible. In addition, JNK2 interfered with JNK1 activation via its “futile” phosphorylation by upstream kinases. Consequently, expression and activation of c-Jun, which depends on JNK activity, were impaired in Jnk1 null cells but enhanced in Jnk2 null cells. TNF-α-induced apoptosis was also suppressed in Jnk1 null fibroblasts but increased in Jnk2 null cells. Thus, our results provide a molecular mechanism underlying the different biological functions of JNK isoforms.
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Ngoei, Kevin R. W., Bruno Catimel, Nicole Church, Daisy S. Lio, Con Dogovski, Matthew A. Perugini, Paul M. Watt, Heung-Chin Cheng, Dominic C. H. Ng, and Marie A. Bogoyevitch. "Characterization of a novel JNK (c-Jun N-terminal kinase) inhibitory peptide." Biochemical Journal 434, no. 3 (February 24, 2011): 399–413. http://dx.doi.org/10.1042/bj20101244.

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An improved understanding of the roles of protein kinases in intracellular signalling and disease progression has driven significant advances in protein kinase inhibitor discovery. Peptide inhibitors that target the kinase protein substrate-binding site have continued to attract attention. In the present paper, we describe a novel JNK (c-Jun N-terminal kinase) inhibitory peptide PYC71N, which inhibits JNK activity in vitro towards a range of recombinant protein substrates including the transcription factors c-Jun, ATF2 (activating trancription factor 2) and Elk1, and the microtubule regulatory protein DCX (doublecortin). Analysis of cell culture studies confirmed the actions of a cell-permeable version of PYC71 to inhibit c-Jun phosphorylation during acute hyperosmotic stress. The analysis of the in vitro data for the kinetics of this inhibition indicated a substrate–inhibitor complex-mediated inhibition of JNK by PYC71N. Alanine-scanning replacement studies revealed the importance of two residues (PYC71N Phe9 or Phe11 within an FXF motif) for JNK inhibition. The importance of these residues was confirmed through interaction studies showing that each change decreased interaction of the peptide with c-Jun. Furthermore, PYC71N interacted with both non-phosphorylated (inactive) JNK1 and the substrate c-Jun, but did not recognize active JNK1. In contrast, a previously characterized JNK-inhibitory peptide TIJIP [truncated inhibitory region of JIP (JNK-interacting protein)], showed stronger interaction with active JNK1. Competition binding analysis confirmed that PYC71N inhibited the interaction of c-Jun with JNK1. Taken together, the results of the present study define novel properties of the PYC71N peptide as well as differences from the characterized TIJIP, and highlight the value of these peptides to probe the biochemistry of JNK-mediated substrate interactions and phosphorylation.
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Messoussi, A., G. Chevé, K. Bougrin, and A. Yasri. "Insight into the selective inhibition of JNK family members through structure-based drug design." MedChemComm 7, no. 4 (2016): 686–92. http://dx.doi.org/10.1039/c5md00562k.

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The c-Jun N-terminal kinase (JNK) family, which comprises JNK1, JNK2 and JNK3, belongs to the mitogen-activated protein kinase (MAPK) superfamily, whose members regulate myriad biological processes, including those implicated in tumorigenesis and neurodegenerative disorders.
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Schepetkin, Igor A., Oleksander S. Karpenko, Anastasia R. Kovrizhina, Liliya N. Kirpotina, Andrei I. Khlebnikov, Stepan I. Chekal, Alevtyna V. Radudik, Maryna O. Shybinska, and Mark T. Quinn. "Novel Tryptanthrin Derivatives with Selectivity as c–Jun N–Terminal Kinase (JNK) 3 Inhibitors." Molecules 28, no. 12 (June 16, 2023): 4806. http://dx.doi.org/10.3390/molecules28124806.

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The c-Jun N-terminal kinase (JNK) family includes three proteins (JNK1-3) that regulate many physiological processes, including cell proliferation and differentiation, cell survival, and inflammation. Because of emerging data suggesting that JNK3 may play an important role in neurodegenerative diseases, such as Alzheimer’s disease (AD) and Parkinson’s disease, as well as cancer pathogenesis, we sought to identify JNK inhibitors with increased selectivity for JNK3. A panel of 26 novel tryptanthrin-6-oxime analogs was synthesized and evaluated for JNK1-3 binding (Kd) and inhibition of cellular inflammatory responses. Compounds 4d (8-methoxyindolo[2,1-b]quinazolin-6,12-dione oxime) and 4e (8-phenylindolo[2,1-b]quinazolin-6,12-dione oxime) had high selectivity for JNK3 versus JNK1 and JNK2 and inhibited lipopolysaccharide (LPS)-induced nuclear factor-κB/activating protein 1 (NF-κB/AP-1) transcriptional activity in THP-1Blue cells and interleukin-6 (IL-6) production by MonoMac-6 monocytic cells in the low micromolar range. Likewise, compounds 4d, 4e, and pan-JNK inhibitor 4h (9-methylindolo[2,1-b]quinazolin-6,12-dione oxime) decreased LPS-induced c-Jun phosphorylation in MonoMac-6 cells, directly confirming JNK inhibition. Molecular modeling suggested modes of binding interaction of these compounds in the JNK3 catalytic site that were in agreement with the experimental data on JNK3 binding. Our results demonstrate the potential for developing anti-inflammatory drugs based on these nitrogen-containing heterocyclic systems with selectivity for JNK3.
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Sedmíková, M., J. Petr, A. Dörflerová, J. Nevoral, B. Novotná, T. Krejčová, E. Chmelíková, and L. Tůmová. "Inhibition of c-Jun N-terminal kinase (JNK) suppresses porcine oocyte ageing in vitro." Czech Journal of Animal Science 58, No. 12 (November 25, 2013): 535–45. http://dx.doi.org/10.17221/7088-cjas.

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Oocyte ageing is a complex of processes that occur when matured in vitro oocytes are, after reaching the metaphase II stage, exposed to further in vitro culture. Aged oocytes remaining at the metaphase II stage undergo spontaneous parthenogenetic activation, or cellular death, through apoptosis (fragmentation) or lysis. The key factor in apoptotic pathway regulation is c-Jun-N-terminal kinase (JNK), stress kinase from the mitogene-activated protein kinase (MAPK) family. To investigate the effect of JNK inhibition on porcine oocytes ageing, cleavage rate, and embryonic development after parthenogenetic activation, DNA fragmentation, and pro-apoptotic factor Bax expression, we cultured in vitro matured oocytes for another 1&ndash;4 days in the presence of a JNK inhibitor. The inhibition of JNK significantly protected the oocytes from fragmentation (0% of fragmented oocytes under JNK inhibition vs. 13.4% of fragmented oocytes in the control group, 2<sup>nd</sup>&nbsp;day of&nbsp;ageing) and increased the percentage of parthenogenetically activated oocytes (82 vs 57.7%, 2<sup>nd</sup> day of ageing). The embryonic development of oocytes parthenogenetically activated after 24 h of ageing was influenced by JNK inhibition as well. The percentage of oocytes at the morula stage, after seven days of cultivation, was significantly increased when oocytes aged in the presence of a JNK inhibitor (42.5%) by comparison to the percentage of oocytes exposed to ageing in an inhibitor-free medium (23.3%). DNA fragmentation was significantly suppressed by JNK inhibition from the 1<sup>st</sup> day of ageing, but the expression of pro-apoptotic factor Bax in the oocytes was not influenced. On the basis of our experiments, we can conclude that JNK inhibition suppresses apoptosis and DNA fragmentation of aged oocytes and improves their embryonic development following the parthenogenetic activation. However, to completely eliminate all ageing related processes is insufficient.
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Unger, Elizabeth K., Merisa L. Piper, Louise E. Olofsson, and Allison W. Xu. "Functional Role of c-Jun-N-Terminal Kinase in Feeding Regulation." Endocrinology 151, no. 2 (February 1, 2010): 671–82. http://dx.doi.org/10.1210/en.2009-0711.

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c-Jun-N-terminal kinase (JNK) is a signaling molecule that is activated by proinflammatory signals, endoplasmic reticulum (ER) stress, and other environmental stressors. Although JNK has diverse effects on immunological responses and insulin resistance in peripheral tissues, a functional role for JNK in feeding regulation has not been established. In this study, we show that central inhibition of JNK activity potentiates the stimulatory effects of glucocorticoids on food intake and that this effect is abolished in mice whose agouti-related peptide (AgRP) neurons are degenerated. JNK1-deficient mice feed more upon central administration of glucocorticoids, and glucocorticoid receptor nuclear immunoreactivity is enhanced in the AgRP neurons. JNK inhibition in hypothalamic explants stimulates Agrp expression, and JNK1-deficient mice exhibit increased Agrp expression, heightened hyperphagia, and weight gain during refeeding. Our study shows that JNK1 is a novel regulator of feeding by antagonizing glucocorticoid function in AgRP neurons. Paradoxically, JNK1 mutant mice feed less and lose more weight upon central administration of insulin, suggesting that JNK1 antagonizes insulin function in the brain. Thus, JNK may integrate diverse metabolic signals and differentially regulate feeding under distinct physiological conditions.
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Choi, Hong Seok, Ann M. Bode, Jung-Hyun Shim, Sung-Young Lee, and Zigang Dong. "c-Jun N-Terminal Kinase 1 Phosphorylates Myt1 To Prevent UVA-Induced Skin Cancer." Molecular and Cellular Biology 29, no. 8 (February 9, 2009): 2168–80. http://dx.doi.org/10.1128/mcb.01508-08.

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ABSTRACT The c-Jun N-terminal kinase (JNK) signaling pathway is known to mediate both survival and apoptosis of tumor cells. Although JNK1 and JNK2 have been shown to differentially regulate the development of skin cancer, the underlying mechanistic basis remains unclear. Here, we demonstrate that JNK1, but not JNK2, interacts with and phosphorylates Myt1 ex vivo and in vitro. UVA induces substantial apoptosis in JNK wild-type (JNK +/+) or JNK2-deficient (JNK2 −/−) mouse embryonic fibroblasts but has no effect on JNK1-deficient (JNK1 −/−) cells. In addition, UVA-induced caspase-3 cleavage and DNA fragmentation were suppressed by the knockdown of human Myt1 in skin cancer cells. JNK1 deficiency results in suppressed Myt1 phosphorylation and caspase-3 cleavage in skin exposed to UVA irradiation. In contrast, the absence of JNK2 induces Myt1 phosphorylation and caspase-3 cleavage in skin exposed to UVA. The overexpression of JNK1 with Myt1 promotes cellular apoptosis during the early embryonic development of Xenopus laevis, whereas the presence of JNK2 reduces the phenotype of Myt1-induced apoptotic cell death. Most importantly, JNK1 −/− mice developed more UVA-induced papillomas than either JNK +/+ or JNK2 −/− mice, which was associated with suppressed Myt1 phosphorylation and decreased caspase-3 cleavage. Taken together, these data provide mechanistic insights into the distinct roles of the different JNK isoforms, specifically suggesting that the JNK1-mediated phosphorylation of Myt1 plays an important role in UVA-induced apoptosis and the prevention of skin carcinogenesis.
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LoGrasso, Philip, and Theodore Kamenecka. "Inhibitors of c-jun-N-Terminal Kinase (JNK)." Mini-Reviews in Medicinal Chemistry 8, no. 8 (July 1, 2008): 755–66. http://dx.doi.org/10.2174/138955708784912120.

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Ma, Hongpeng. "Relationship Between c-Jun N-terminal Kinase and Depression." E3S Web of Conferences 185 (2020): 03029. http://dx.doi.org/10.1051/e3sconf/202018503029.

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Depression is one of the most common emotional disorders. The cause of depression is still not clear. C-Jun N-terminal kinase (JNK) is one number of mitogen activated protein kinase (MAPK) family, which is closely related to the occurrence of many diseases. At present, it is believed that JNK plays an important role in the parthenogenesis of depression, but the specific mechanism is not clear. This review will focus on the possible mechanism of JNK protein and JNK signaling pathway affecting the parthenogenesis of depression.
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Ye, Zhiqiang, Yuxian Chen, Rongkai Zhang, Haitao Dai, Chun Zeng, Hua Zeng, Hui Feng, Gengheng Du, Hang Fang, and Daozhang Cai. "c-Jun N-terminal kinase – c-Jun pathway transactivates Bim to promote osteoarthritis." Canadian Journal of Physiology and Pharmacology 92, no. 2 (February 2014): 132–39. http://dx.doi.org/10.1139/cjpp-2013-0228.

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Osteoarthritis (OA) is a chronic degenerative joint disorder. Previous studies have shown abnormally increased apoptosis of chondrocytes in patients and animal models of OA. TNF-α and nitric oxide have been reported to induce chondrocyte ageing; however, the mechanism of chondrocyte apoptosis induced by IL-1β has remained unclear. The aim of this study is to identify the role of the c-Jun N-terminal kinase (JNK) – c-Jun pathway in regulating induction of Bim, and its implication in chondrocyte apoptosis. This study showed that Bim is upregulated in chondrocytes obtained from the articular cartilage of OA patients and in cultured mouse chondrocytes treated with IL-1β. Upregulation of Bim was found to be critical for chondrocyte apoptosis induced by IL-1β, as revealed by the genetic knockdown of Bim, wherein apoptosis was greatly reduced in the chondrocytes. Moreover, activation of the JNK–c-Jun pathway was observed under IL-1β treatment, as indicated by the increased expression levels of c-Jun protein. Suppression of the JNK–c-Jun pathway, using chemical inhibitors and RNA interference, inhibited the Bim upregulation induced by IL-1β. These findings suggest that the JNK–c-Jun pathway is involved in the upregulation of Bim during OA and that the JNK–c-Jun–Bim pathway is vital for chondrocyte apoptosis.
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Dissertations / Theses on the topic "C-Jun N-terminal kinase (JNK)"

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Arnold, Richard Graham. "The role of c-Jun-N-Terminal Kinase (JNK) in hindlimb ischaemia-reperfusion injury." Thesis, Queen's University Belfast, 2012. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.579569.

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In spite of improvements in the care of the critically ill patient, both elective and emergency vascular surgical interventions are associated with significant morbidity and mortality. Successful reperfusion of the ischaemic limb often initiates a systemic inflammatory response syndrome (SIRS), which may be complicated by multiple organ failure, including Acute Lung Injury (All) and the Acute Respiratory Distress Syndrome (ARDS). An exaggerated inflammatory response has been shown to play an integral role in the development of ARDS following lower torso or limb ischaemia-reperfusion injury. JNK enzymes, part of the Mitogen Activated Protein Kinase (MAPK) group, have been implicated in neutrophil activation as part of this response. Furthermore the role of JNK in ischaemia reperfusion injury is well established .as well as its role in All as evidenced by the attenuation of such injury with inhibitors in a number of animal models of direct lung injury. This thesis tests the hypothesis that .hibition of JNK attenuates the neutrophil-based All and ARDS associated with lower limb ischaemia-reperfusion injury. A murine model of bilateral hindlimb ischaemia-reperfusion injury was established. Lung injury was confirmed by tissue oedema, neutrophil sequestration and microvascular permeability in association with increased expression of the JNK enzymes. In a genetic JNK knockout model subjected to ischaemia-reperfusion injury, there was an attenuated lung injury as evidenced by a reduction in histology injury scores and myeloperoxidase levels. In a therapeutic inhibitor model, using the JNK inhibitor SP600125, this attenuation was observed in the histology injury scores and bronchoalveolar lavage (BAL) protein levels. These results suggest that JNK may play a role in the pathogenesis of lung injury following ischaemia-reperfusion injury and its inhibition may provide a novel therapeutic approach.
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Kyula, Joan Nduku. "HSV-1 induced activation of C-JUN-N-Terminal Kinase (JNK) and P38 MAPK." Thesis, Glasgow Caledonian University, 2005. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.413914.

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Lanuza, Masdeu Jordi. "Regulation and actions mediated by C-jun N-terminal kinase pathaway." Doctoral thesis, Universitat de Barcelona, 2013. http://hdl.handle.net/10803/110348.

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Es va generar un ratolí transgènic amb la capacitat d'activar JNK específicament al pàncrees. Tot i que aquests ratolins no tenen cap afectació morfoestructural en els seus illots pancreàtics ni diferències en el contingut total d'insulina però presenten intolerància a la glucosa i no secreten insulina en resposta a hiperglucèmia. A nivell molecular, les cèl•lules β pancreàtiques amb JNK activa, tenen un bloqueig a la via de senyalització d'insulina que fa que es redueixi la secreció d'insulina i l'expressió de gens diana de la insulina. El tractament amb rossiglitazona, un fàrmac del grup de les TZDs, aconsegueix revertir el fenotip in vivo. Tots aquests resultats indiquen que l'activació de JNK és suficient per promoure la resistència a insulina central però no n'hi ha prou per induir hiperplàsia dels illots o induir l'apoptosi de les cèl•lules β. A més a més, aquests ratolins estan protegits de la hiperinsulinèmia, la hiperglucèmia i l'obesitat induïdes per la dieta grassa o l'envelliment. També s'ha estudiat la interacció entre les vies de senyalització de JNK i NF-κB. Fins ara, s'ha va publicat que JNK pot induir l'activació de NF-κB mitjançant l'estabilització del mRNA de la βTrCP, responsable de la degradació d'IκBα. JNK va resultar fosforilar a CRD-BP, una proteïna que s'uneix al mRNA de βTrCP per protegir-li de l'atac per part del miR-183. A més, un mutant de βTrCP perquè no s'hi unís el miRNA, es seguia estabilitzant en resposta a l'activació de JNK a nivel de proteïna però no de mRNA. A part d'aquest efecte, JNK també aconsegueix estabilitzar SKP1 però la interacció SKP1-βTrCP és necessària per a una màxima estabilització. A més a més, aquest efecte podria ser extensiu a altres dianes de βTrCP com β-catenina i també estan afectades els nivells d'altres F-Box com la SKP2, i el dels seus substrats.
As a part of the research-line that deals with physiological and pharmacological (anti-inflammatory and/or anti-diabetic) actions conducted by some nuclear receptor (NR) ligands through negative interference with the c-Jun N-terminal kinase (JNK) signaling pathway, this project is focused on studying the effects of the activation of JNK in a mouse model and evaluating the capacity of those ligands to recover the homeostasis. In parallel, there is a second project about the characterization of the crosstalk between the JNK pathway and NF-κB, another major pathway in inflammation. The relevance of the activation of JNK in a wide range of pathologies with an inflammatory component, lead the group to the generation of a transgenic mouse carrying a a constitutively active form of the MAP2K of JNK, MKK7, with a conditional expression upon the regulation of the Cre recombinase. Despite these mice have no morphostructural affectation of the pancreatic islets or differences in the total insulin content, they have defective glucose homeostasis showing glucose intolerance and decreased insulin secretion in response to hyperglycemia. This reduction in glucoseinduced insulin release is β cell autonomous, as it is reproduced in isolated islets, and JNK activity dependent, as it is reverted by the specific inhibitor of JNK, TAT-JIPi. At molecular level, β-cells with activated JNK have a blockage in the insulin-signaling pathway that reduces the secretion of insulin and the expression of insulin target genes. The treatment with rosiglitazone, an insulin-sensitizing drug of the thiazolidinedione family that inhibits JNK activation, restored insulin secretion in response to glucose in isolated islets and in vivo. All these data indicate that the activation of JNK is sufficient to promote central insulin resistance but is not sufficient to induce islet hyperplasia or β-cell death. Moreover, these mice are protected from basal plasma hiperinsulinemia caused by aging or high fat diet challenge. Regarding the second project, the interaction between NF-κB.and JNK pathways, both signaling pathways are essential for the regulation of the immune and inflammatory response as well as other fundamental processes such as cell proliferation and survival. It was published that JNK was activating NF-κB. pathway by inducing the mRNA stabilization of the E3 ubiquitin ligase βTrcP. We have further reported that JNK is targeting the miRNA183/CRD-BP system to stabilize βTrCP mRNA. At a protein level we have shown that SPK1-βTrCP complex formation is required for JNKdependent SKP1 and βTrCP protein stabilization. Not only this but the βTrCP substrate β‐catenin is down regulated by the JNK-dependent increase of βTrCP and the protein levels of SKP2 and its substrate p27 are oppositely regulated by JNK
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Gourmaud, Sarah. "Expression de c-Jun N-terminal kinase (JNK) dans la maladie d'Alzheimer : intérêts diagnostiques et thérapeutiques." Paris 7, 2014. http://www.theses.fr/2014PA077106.

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La maladie d'Alzheimer (MA) se caractérise par l'accumulation de peptides d'amyloïde-β42 (Aß₄₂), de protéine tau hyperphosphorylée (ptau) et une perte neuronale. Les niveaux d'Aß₄₂ et de tau au niveau du liquide céphalo-rachidien (LCR) des patients sont utilisés comme biomarqueurs diagnostique. Les protéines PKR et JNK sont des kinases impliquées dans la production d'AE342, la phosphorylation de tau et la mort neuronale. L'accumulation de leur forme active a été mise en évidence dans le cerveau de patients MA. Il existe trois isoformes de JNK. JNK1 et JNK2 sont ubiquitaires et JNK3 est presque exclusivement exprimée au niveau du cerveau. Aucune étude n'a étudié à ce jour les variations de JNK3 dans la MA. L'objectif de notre étude était d'analyser in vitro le lien entre PKR et JNK puis de mesurer l'expression des différents isoformes de JNK dans la MA chez l'homme. Nos résultats montrent que la protéine PKR intervient à la fois dans la voie d'activation et celle de désactivation de JNK en fonction des conditions de stress. Nous mettons également en évidence la diminution de l'apoptose neuronale due à l'Aß₄₂ grâce à un peptide inhibiteur de JNK. Nous avons mesuré une augmentation de la forme totale de JNK3 dans le cortex frontal et le LCR de patients Alzheimer. Le signal de JNK3 colocalise avec celui d'Ar342 au niveau des plaques séniles. Grâce au suivi clinique des patients nous avons montré que le niveau de JNK3 mesuré dans le LCR est corrélé au déclin cognitif chez les patients. JNK3 pourrait devenir un nouveau biomarqueur diagnostique et pronostique de la MA. Ces résultats, associés à ceux de la littérature, font de JNK3 et PKR d'intéressantes cibles thérapeutiques
Alzheimer's disease (AD) is characterized by the accumulation of amyloid-β42 peptide (Aß₄₂), hyperphosphorylated tau (ptau) proteins and neuronal loss. Cerebrospinal fluid (CSF) Aß₄₂and tau levels in patients are used as diagnostic biomarkers. PKR and JNK are kinases involved in the production of Ar342, tau phosphorylation and neuronal death. The accumulation of their active form was demonstrated in AD brains. There are three isoforms of JNK. JNK1 and JNK2 are ubiquitous and JNK3 is almost exclusively expressed in brain. No studies have examined changes in JNK3 in AD. The aim of our study was to analyze in vitro the relationship between PKR and JNK and then to measure the expression of JNK isoforms in AD patients. Our results showed that PKR is involved in both JNK activation and deactivation, according to stress conditions. We also showed a decrease of neuronal apoptosis due to Aß₄₂ with a JNK inhibitor peptide. We measured an increase of the total form of JNK3 in AD frontal cortex and CSF. JNK3 signal colocalizes with Aß₄₂ in senile plaques. Thanks to the clinical monitoring of patients we have shown that the CSF level of JNK3 correlates with the cognitive decline. JNK3 could become a new diagnostic and prognostic biomarker for AD. These results, together with those of the literature, make JNK3 and PKR interesting therapeutic targets
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Smith, Abigail O. "Defining the Role of c-Jun N-terminal Kinase (JNK) Signaling in Autosomal Dominant Polycystic Kidney Disease." eScholarship@UMMS, 2021. https://escholarship.umassmed.edu/gsbs_diss/1141.

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Polycystic kidney disease is an inherited degenerative disease in which the uriniferous tubules are replaced by expanding fluid-filled cysts that ultimately destroy organ function. Autosomal dominant polycystic kidney disease (ADPKD) is the most common form, afflicting approximately 1 in 1,000 people. It primarily is caused by mutations in the transmembrane proteins Polycystin-1 (PKD1) and Polycystin-2 (PKD2). The most proximal effects of polycystin mutations leading to cyst formation are not known, but pro-proliferative signaling must be involved for the tubule epithelial cells to increase in number over time. The stress-activated mitogen-activated protein kinase (MAPK) pathway c-Jun N-terminal kinase (JNK) promotes proliferation in specific contexts and is activated in acute and chronic kidney disease. Previous work found evidence of JNK activation in cystic tissues (Le et al., 2005) and others showed that JNK signaling is activated by aberrant expression of PKD1 and PKD2 in cell culture (Arnould et al., 1998; Arnould et al., 1999; Parnell et al., 2002; Yu et al., 2010) but the contribution of JNK signaling to cystic disease in vivo has not been investigated. This body of work describes the use of conditional and germline deletion of Pkd2, Jnk1 and Jnk2 to model ADPKD and JNK signaling inhibition in juvenile and adult mice. Immunoblots and histological staining were used to measure JNK activation and evaluate the effect of JNK deletion on cystic disease. Results show that Pkd2 deletion activated JNK signaling in juvenile and adult mice. Reduction of JNK activity significantly reduced cystic burden in kidneys of juvenile Pkd2 mutant mice. This correlated with reduced tubule cell proliferation and reduced kidney fibrosis. The improvement in cystic phenotype was driven primarily by Jnk1 deletion rather than Jnk2. JNK signaling inhibition in adult Pkd2 mutants significantly reduced liver cysts when mice were aged six months. JNK inhibition reduces the severity of cystic disease caused by the loss of Pkd2 suggesting that the JNK pathway should be explored as a potential therapeutic target for ADPKD.
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Santos, Fernando Reyes, Maggie K. Diamond-Stanic, Mujalin Prasannarong, and Erik J. Henriksen. "The Serine Kinase C-Jun N-Terminal Kinase (JNK) Contributes to Oxidant-Induced Insulin Resistance in Isolated Rat Skeletal Muscle." Thesis, The University of Arizona, 2012. http://hdl.handle.net/10150/244754.

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Insulin resistance of the mammalian skeletal muscle glucose transport system, one cause of which is oxidative stress, leads to the development of type 2 diabetes. While the direct contributions to insulin resistance of certain stress-activated serine kinases have been described previously, the specific contribution of c-Jun N-terminal kinase (JNK) is not fully understood. Therefore, we assessed the role of JNK in insulin resistance caused by in vitro exposure to the oxidant hydrogen peroxide (H₂O₂). Soleus muscles from lean Zucker rats were incubated in low levels (~30 μM) of H₂O₂ in the absence or presence of insulin for up to 6 hr. Decreases in insulin-stimulated glucose transport activity (ISGTA) were observed at all time points and were associated with similar diminutions in insulin stimulation of Akt Ser⁴⁶⁷ phosphorylation. Phosphorylation (Thr¹⁸³/Tyr¹⁸⁵) of JNK isoforms (JNK1 and JNK2/3) was increased by H₂O₂ in the absence and presence of insulin at all time points. To determine the specific contribution of JNK to oxidant-induced insulin resistance, the JNK inhibitor SP600125 was used. ISGTA in the presence of H₂O₂ was improved when the inhibitor was added during the 6-hr incubation. These results indicate that JNK contributes to oxidative stress-induced insulin resistance in mammalian skeletal muscle.
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Wang, Fang St George Clinical school UNSW. "Oxidative stress induced C-Jun N-terminal Kinase (JNK) activation in tendon cells upregulates MMP1 mRNA and protein expression." Awarded by:University of New South Wales. St George Clinical school, 2006. http://handle.unsw.edu.au/1959.4/28815.

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To explore the potential mechanisms of tendon degeneration, we investigated the role of c-Jun N-terminal Kinase (JNK) activation and the regulation of matrix metalloproteinase 1 (MMP1) in tendon matrix degradation under oxidative stress. JNK and MMP1 activity in samples from normal and ruptured human supraspinatus tendons were evaluated by immunohistochemistry. Real-time quantitative PCR was utilized to evaluate MMP1 mRNA expression and western blotting for MMP1 and JNK protein detection. JNK activation and increased MMP1 activity were found in the torn human supraspinatus tendon tissue, as well as in human tendon cells under in vitro oxidative stress. Inhibition of JNK prevented MMP1 over-expression in oxidative stressed human tendon cells. Results from the current study indicated that stress activated JNK plays an important role in tendon matrix degradation, possibly through upregulating of MMP1.
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Yu, Lola. "Investigating the role of the c-Jun NH2-terminal kinase pathway in ErbB2-driven breast cancer and macrophage polarization." eScholarship@UMMS, 2020. https://escholarship.umassmed.edu/gsbs_diss/1094.

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Breast cancer is the second most common malignancy in the world, accounting for over 1.7 million new diagnoses and an estimated 500,000 deaths per year (1). Overexpression of the receptor tyrosine kinase ErbB2, also known as Her2 or Neu, occurs in over 30% of breast cancers and correlates with metastasis, poor prognosis, and decreased survival (1, 2). Although therapeutics targeting ErbB2 show clinical efficacy, many patients display no initial response or develop drug resistance over time (2). A deeper understanding of the molecular basis of ErbB2-driven tumorigenesis is thus required for the development of improved therapeutic strategies. In vitro experiments suggest that activation of the c-Jun NH2-terminal kinase (JNK) pathway, a mitogen-activated protein kinase pathway, promotes proliferation, cellular invasion, and stem cell expansion in ErbB2-driven breast cancer (3, 4). Furthermore, unpublished data from our lab using mammary epithelial cells expressing activated ErbB2 show that JNK is required for acinus formation in in vitro 3D cultures. In contrast to these studies showing a tumorigenic role for the JNK pathway, other data from our lab show that JNK loss results in accelerated breast tumor growth, suggesting a tumor suppressive role (5, 6). However, these studies were performed in p53 knockout mice with or without a Kras mutation, where the latter required extensive aging and genomic instability to occur before differences in tumor growth were observable. To date, limited in vivo studies exist to confirm the role of JNK in more biologically relevant breast tumor models, such as in ErbB2-mediated cancer, which accounts for over 30% of all human breast cancers. In addition, the molecular mechanisms by which JNK signaling promotes ErbB2-driven tumorigenesis remains poorly understood. To address the discrepancy in JNK function between the in vitro ErbB2-driven breast cancer data and the in vivo p53 knockout tumor data, I began the development of an in vivo murine model to confirm the role of JNK in ErbB2-driven breast cancer. This mouse model will also allow us to test a potential mechanism by which JNK regulates tumorigenesis. Studies show that ErbB2-mediated secretion of the inflammatory cytokine IL6 promotes transformation and tumor growth by activation of the STAT3 transcription factor, triggering an IL6/STAT3 autocrine signaling loop (7,8). A major regulator of Il6 gene expression includes activator protein 1 (AP-1), a transcription factor composed of downstream JNK targets in the Jun protein family (9). In vitro experiments using ErbB2-overexpressing mammary epithelial cell lines show that chemical inhibition of JNK suppresses secreted IL6 protein levels, supporting a role for the JNK pathway in IL6 regulation (7). Thus, I hypothesize that JNK drives ErbB2-driven breast cancer by promoting IL6-mediated tumor progression. Addressing this will increase our understanding of the role of JNK in ErbB2-driven breast cancer and reveal a potentially new mechanism by which JNK functions in tumor progression. Additionally, I began the development of a mouse model that will allow us to investigate the role of JNK in macrophage polarization as an alternative mechanism by which JNK regulates ErbB2-driven breast cancer. In addition to promoting STAT3-dependent tumor growth, IL6 can indirectly drive tumorigenesis by promoting expression of the IL4 receptor in macrophages, triggering STAT6-mediated macrophage polarization towards the pro-tumorigenic M2 phenotype (10, 11). Unlike classically activated M1 macrophages, which promote inflammation and anti-tumor immunity, alternatively activated M2 macrophages function in immunosuppression and metastasis and correlate with advanced stages of breast cancer (12, 13). Further evidence supporting a role for the JNK pathway in macrophage polarization includes a recent study suggesting that JunB, a downstream JNK target and component of the AP-1 complex, plays a crucial role in the induction of M2 macrophage polarization in human alveolar macrophages (13). I hypothesize that activation of the JNK signaling pathway induces IL6-dependent macrophage polarization towards the pro-tumorigenic M2 phenotype. Addressing this hypothesis will determine for the first time whether JNK functions in regulating macrophage polarization within the tumor microenvironment, offering a potentially new mechanism by which JNK can promote ErbB2-driven breast cancer. Determining the role of JNK in ErbB2-mediated breast cancer will have direct therapeutic relevance, as targeting JNK has the potential to inhibit ErbB2-driven breast cancer and other IL6-mediated diseases. Investigating the underlying mechanisms by which JNK functions in ErbB2-positive breast cancer can also offer new molecular targets and further contribute to effective drug design.
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Joy, Jery 1992. "Chromosomal instability : interplay between proteotoxic and metabolic stress." Doctoral thesis, Universitat Pompeu Fabra, 2020. http://hdl.handle.net/10803/668516.

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Chromosomal Instability (CIN) and associated aneuploidy are salient features of the majority of human solid tumors. In the Drosophila epithelial model of CIN, the generation of highly aneuploid karyotypes drive cell delamination and c-Jun N-terminal Kinase (JNK) dependent cell death. Aneuploidy associated generation of Reactive Oxygen Species (ROS) plays a key role in the activation of JNK. When delaminating cells are maintained in the tissue by apoptosis inhibition, aberrant karyotypes promote a cell-autonomous malignant behavior. Here we have dissected the molecular mechanisms underlying aneuploidy-induced ROS production and cell delamination. On one hand, we have shown that aneuploidy associated proteotoxic stress is being sensed and activates the major protein quality control mechanisms in a cell. On the other hand, mitochondria act as signaling centers as well as major sensors of the unbalanced proteome in CIN tissues. Aneuploidy associated proteotoxic stress leads to mitochondrial dysfunction and ROS production, which further drives cell delamination as well as JNK activation in CIN tissues.
La inestabilidad cromosómica y la aneuploidía son características destacadas de la mayoría de los tumores sólidos en humanos. En el modelo epitelial de Drosophila, la generación de cariotipos altamente aneuploides promueve la delaminación y la muerte celular dependiente de c-Jun N-terminal Kinase (JNK). La producción de especies reactivas de oxígeno (ROS) juega un papel clave en la activación de JNK bajo dichas condiciones. Cuando las células delaminadas se mantienen en el tejido gracias a la inhibición de la apoptosis, los cariotipos aberrantes promueven un comportamiento maligno tumoral. En esta tesis hemos analizado los mecanismos moleculares subyacentes a la producción de ROS como consecuencia de la aneuploidía. Hemos demostrado que bajo una situación de inestablidad cromosómica se genera un estrés proteotóxico, detectado por la célula que activa los principales mecanismos de control de calidad de las proteínas. Además, dicho estrés, promueve la disfuncionalidad de las mitocondrias, favoreciendo la generación de ROS, que a su vez contribuye a la activación de JNK y a la delaminación celular al afectar el citoesqueleto de actina-miosina en los tejidos CIN.
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Le, Aurore. "Deciphering the role of c-Jun N-Terminal Kinase (JNK1) in an in vivo model of skin inflammation." Doctoral thesis, Universite Libre de Bruxelles, 2020. http://hdl.handle.net/2013/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/314810.

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JNK1 (c-Jun N-terminal kinase 1) has been studied in numerous biological phenomena, but its role in skin inflammation diseases has not been fully defined yet. We therefore evaluated the role of JNK1 in imiquimod-induced dermatitis, a classical model that shares many features with human psoriasis. We showed that JNK1 was necessary for the expression of inflammatory markers and for acanthosis induced by imiquimod. We demonstrated that the loss of JNK1 in dendritic cells or myeloid cells reduced inflammatory markers but did not affect acanthosis induced by imiquimod. In vitro experiments in bone marrow-derived macrophages (BMMs) supported the role of JNK1 in the activation of the inflammasome pathway by the Aldara® cream. Next, we observed that the loss of JNK1 in keratinocytes did not reduce imiquimod-induced expression of most inflammatory markers but acanthosis and proliferation of epidermal cells was decreased. To better understand the role of JNK1 in keratinocytes, we evaluated the transcriptome and the epigenomic landscape of JNK1-deficient epidermal cells from mice treated with imiquimod. These data highlighted the potential role of JNK1 downstream of the EGFR pathway. We further observed that the inhibition of the EGFR pathway decreased imiquimod-induced acanthosis. Our work shows the dual role of JNK1 in skin inflammation induced by imiquimod. On one hand, JNK1 influences the expression of inflammatory mediators by myeloid cells, probably through the inflammasome pathway. On the other hand, JNK1 modulates the response of keratinocytes to EGFR ligands. Taken together, these data suggest that JNK1 could represent a valuable therapeutic target for the management of psoriasis.
Doctorat en Sciences médicales (Médecine)
info:eu-repo/semantics/nonPublished
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Books on the topic "C-Jun N-terminal kinase (JNK)"

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Carbone, Ryan. Characterization of the role of c-Jun N-terminal kinase in L-glutamine starvation-induced apoptosis in Sp2/0-Ag14 hybridoma cells. Sudbury, Ont: Laurentian University, 2005.

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Vallerie, Sara Nicole. Regulation of metabolism by c-Jun N-terminal kinase. 2010.

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Book chapters on the topic "C-Jun N-terminal kinase (JNK)"

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Kim, Byung-Jin, and Donald J. Zack. "The Role of c-Jun N-Terminal Kinase (JNK) in Retinal Degeneration and Vision Loss." In Retinal Degenerative Diseases, 351–57. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-75402-4_43.

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Zhan, Xuanzhi, Vsevolod V. Gurevich, and Eugenia V. Gurevich. "Scaffolding c-Jun N-Terminal Kinase Cascades: Mechanistic Insights from the Reconstituted Arrestin-JNK Cascades." In The Structural Basis of Arrestin Functions, 187–98. Cham: Springer International Publishing, 2017. http://dx.doi.org/10.1007/978-3-319-57553-7_14.

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Sclip, Alessandra, Xanthi Antoniou, and Tiziana Borsello. "Cortical Neurons Culture to Study c-Jun N-Terminal Kinase Signaling Pathway." In Protein Kinase Technologies, 189–202. Totowa, NJ: Humana Press, 2012. http://dx.doi.org/10.1007/978-1-61779-824-5_10.

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Chromik, A. M., A. M. Müller, J. Körner, O. Belyaev, M. Albrecht, F. Schmitz, T. Herdegen, W. Uhl, and U. Mittelkötter. "Die genetische Inaktivierung der c-Jun N-terminalen Kinase 1 und 2 (JNK1 und JNK2) verschlimmert die chronische DSS-Colitis der Maus." In Chirurgisches Forum 2006, 215–17. Berlin, Heidelberg: Springer Berlin Heidelberg, 2006. http://dx.doi.org/10.1007/3-540-34668-6_73.

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Yatsushige, H., M. Yamaguchi-Okada, C. Zhou, J. W. Calvert, J. Cahill, A. R. T. Colohan, and John H. Zhang. "Inhibition of c-Jun N-terminal kinase pathway attenuates cerebral vasospasm after experimental subarachnoid hemorrhage through the suppression of apoptosis." In Acta Neurochirurgica Supplement, 27–31. Vienna: Springer Vienna, 2008. http://dx.doi.org/10.1007/978-3-211-75718-5_6.

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Chromik, Ansgar Michael, S. Kersting, A. M. Müller, M. Albrecht, C. Hilgert, L. Frick, T. Herdegen, U. Mittelkötter, and W. Uhl. "Knock out der c-Jun N-terminalen Kinase 2 (JNK2) aggraviert die Entwicklung der chronischen DSS Colitis unabhängig von der intestinalen Zytokin-Expression." In Chirurgisches Forum 2008, 217–19. Berlin, Heidelberg: Springer Berlin Heidelberg, 2008. http://dx.doi.org/10.1007/978-3-540-78833-1_79.

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"C-Jun N-Terminal Kinase (JNK)." In Encyclopedia of Cancer, 873. Berlin, Heidelberg: Springer Berlin Heidelberg, 2011. http://dx.doi.org/10.1007/978-3-642-16483-5_1193.

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"c-Jun N-Terminal Kinase." In Encyclopedia of Cancer, 1085. Berlin, Heidelberg: Springer Berlin Heidelberg, 2016. http://dx.doi.org/10.1007/978-3-662-46875-3_100558.

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"JNK (Jun amino terminal kinase)." In Encyclopedia of Genetics, Genomics, Proteomics and Informatics, 1047. Dordrecht: Springer Netherlands, 2008. http://dx.doi.org/10.1007/978-1-4020-6754-9_8890.

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Lam, KSL, X. Zhang, RLC Wong, and A. Xu. "Selective Inactivation of c-Jun NH2 Terminal Kinase (JNK) in the Adipose Tissue Is Sufficient To Protect Against Diet-Induced-Obesity and Its Associated Metabolic Disorders in Mice." In The Endocrine Society's 92nd Annual Meeting, June 19–22, 2010 - San Diego, P1–414—P1–414. Endocrine Society, 2010. http://dx.doi.org/10.1210/endo-meetings.2010.part1.p9.p1-414.

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Conference papers on the topic "C-Jun N-terminal kinase (JNK)"

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White, SR, MK Abe, BA Marroquin, D. Lascano, and R. Stern. "c-Jun N-Terminal Kinase (JNK) and c-Jun Mediate Early Migration after Injury in Differentiated Airway Epithelial Cells." In American Thoracic Society 2009 International Conference, May 15-20, 2009 • San Diego, California. American Thoracic Society, 2009. http://dx.doi.org/10.1164/ajrccm-conference.2009.179.1_meetingabstracts.a2391.

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Du, Lili, Tinghu Zhang, Tamer Kaoud, Nathanael Gray, Kevin Dalby, and Kenneth Y. Tsai. "Abstract 1941: Distinct roles of c-Jun N-terminal kinase (JNK) isoforms in skin cancer." In Proceedings: AACR 106th Annual Meeting 2015; April 18-22, 2015; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.am2015-1941.

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Palmieri, C., B. Rudraraju, A. Giannoudis, D. Moore, J. Shaw, S. Chan, IO Ellis, et al. "Abstract P5-08-17: A study of c-Jun N-terminal kinase (JNK) and c-Jun as biomarkers in early breast cancer." In Abstracts: Thirty-Eighth Annual CTRC-AACR San Antonio Breast Cancer Symposium; December 8-12, 2015; San Antonio, TX. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.sabcs15-p5-08-17.

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Mohamed, MR, FJ Cubero, MM Woitok, RJ Davis, and C. Trautwein. "Hepatocytic c-Jun N-terminal kinases (JNK) protect against cystogenesis in NEMO-deficient mice." In 35. Jahrestagung der Deutschen Arbeitsgemeinschaft zum Studium der Leber. Georg Thieme Verlag KG, 2019. http://dx.doi.org/10.1055/s-0038-1677220.

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Silva, Patricia M. R., Ana Carolina Arantes, Tatiana P. T. Ferreira, Cristiane Garcia, Patricia R. M. Rocco, IM Fierro, RL Simoes, Vincent Lagente, and Marco A. Martins. "EFFECT OF C-JUN NH2-TERMINAL KINASE (JNK) INHIBITOR SP600125 ON EXPERIMENTAL SILICOSIS IN MICE." In American Thoracic Society 2010 International Conference, May 14-19, 2010 • New Orleans. American Thoracic Society, 2010. http://dx.doi.org/10.1164/ajrccm-conference.2010.181.1_meetingabstracts.a1057.

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Ebelt, ND, and CL Van Den Berg. "Abstract P6-04-17: The irreversible c-Jun N-terminal kinase (JNK) inhibitor, JNK-IN-8, sensitizes basal-like breast cancer cells to lapatinib." In Abstracts: Thirty-Sixth Annual CTRC-AACR San Antonio Breast Cancer Symposium - Dec 10-14, 2013; San Antonio, TX. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/0008-5472.sabcs13-p6-04-17.

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Fanburg, Barry L., Lin Wei, and Yinglin Liu. "Interaction Of C-Jun N-terminal Kinase (JNK) And Other Serotonin Activated Signaling Pathways In Pulmonary Artery Smooth Muscle Cells." In American Thoracic Society 2010 International Conference, May 14-19, 2010 • New Orleans. American Thoracic Society, 2010. http://dx.doi.org/10.1164/ajrccm-conference.2010.181.1_meetingabstracts.a1173.

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Chu, Feng-Min, Shuang-Shii Lian, and Yen-Jen Sung. "Particulate Joint Replacement Materials Induce Apoptosis of Rabbit Synoviocytes Cell Line HIG-82 through c-Jun N-Terminal Kinase (JNK) Pathway." In 2009 2nd International Conference on Biomedical Engineering and Informatics. IEEE, 2009. http://dx.doi.org/10.1109/bmei.2009.5305639.

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Wei, L., Y. Liu, and BL Fanburg. "C-Jun N-Terminal Kinase (JNK) Regulates Serotonin-Mediated Proliferation and Migration of Pulmonary Artery Smooth Muscle Cells through the Akt Pathway." In American Thoracic Society 2009 International Conference, May 15-20, 2009 • San Diego, California. American Thoracic Society, 2009. http://dx.doi.org/10.1164/ajrccm-conference.2009.179.1_meetingabstracts.a1860.

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McCoy, Francis G. P., Ian Paul, Jane L. Hurwitz, Barry O'Hagan, Krzysztofa Odrzywol, James T. Murray, George McKerr, and Dean A. Fennell. "Abstract B30: Phosphorylation of c‐jun N terminal kinase (JNK) regulates induction of mitochondrial apoptosis by pro‐suvival BCL‐2 antagoinist obatoclax." In Abstracts: AACR-NCI-EORTC International Conference: Molecular Targets and Cancer Therapeutics--Nov 15-19, 2009; Boston, MA. American Association for Cancer Research, 2009. http://dx.doi.org/10.1158/1535-7163.targ-09-b30.

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Reports on the topic "C-Jun N-terminal kinase (JNK)"

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LoGrasso, Philip, and Serge Przedborski. c-jun-N-Terminal Kinase (JNK) for the Treatment of Amyotrophic Lateral Sclerosis. Fort Belvoir, VA: Defense Technical Information Center, October 2013. http://dx.doi.org/10.21236/ada596507.

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Chen, Yi-Rong. C-Jun N-terminal Kinase and Apoptosis in Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, June 1999. http://dx.doi.org/10.21236/ada374120.

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Chen, Yi-Rong. C-Jun N-terminal Kinase and Apoptosis in Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, June 1998. http://dx.doi.org/10.21236/ada353790.

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Chen, Yi-Rong, and Tse-Hua Tan. C-Jun N-Terminal Kinase and Apoptosis in Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, June 2000. http://dx.doi.org/10.21236/ada392179.

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Ehrlich, Marcelo, John S. Parker, and Terence S. Dermody. Development of a Plasmid-Based Reverse Genetics System for the Bluetongue and Epizootic Hemorrhagic Disease Viruses to Allow a Comparative Characterization of the Function of the NS3 Viroporin in Viral Egress. United States Department of Agriculture, September 2013. http://dx.doi.org/10.32747/2013.7699840.bard.

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Project Title: "Development of a plasmid-based reverse genetics system for the Bluetongue and Epizootic Hemorrhagic Disease viruses to allow comparative characterization of the function of the NS3 viroporin in viral egress". Project details: No - IS-4192-09; Participants – Ehrlich M. (Tel Aviv University), Parker J.S. (Cornell University), DermodyT.S. (Vanderbilt University); Period - 2009-2013. Orbiviruses are insect-borne infectious agents of ruminants that cause diseases with considerable economical impact in Israel and the United States. The recent outbreaks of BTV in Europe and of Epizootic Hemorrhagic Disease Virus (EHDV) in Israel, underscore the need for: (i) a better comprehension of the infection process of orbiviruses, (ii) the identification of unique vs. common traits among different orbiviruses, (iii) the development of novel diagnosis and treatment techniques and approaches; all aimed at the achievement of more effective control and treatment measures. It is the context of these broad goals that the present project was carried out. To fulfill our long-term goal of identifying specific viral determinants of virulence, growth, and transmission of the orbiviruses, we proposed to: (i) develop reverse genetics systems for BTV and EHDV2-Ibaraki; and (ii) identify the molecular determinants of the NS3 nonstructural protein related to viroporin/viral egress activities. The first objective was pursued with a two-pronged approach: (i) development of a plasmid-based reverse genetics system for BTV-17, and (ii) development of an "in-vitro" transcription-based reverse genetics system for EHDV2-Ibaraki. Both approaches encountered technical problems that hampered their achievement. However, dissection of the possible causes of the failure to achieve viral spread of EHDV2-Ibaraki, following the transfection of in-vitro transcribed genomic segments of the virus, revealed a novel characteristic of EHDV2-Ibaraki infection: an uncharacteristically low fold increase in titer upon infection of different cell models. To address the function and regulation of NS3 we employed the following approaches: (i) development (together with Anima Cell Metrology) of a novel technique (based on the transfection of fluorescently-labeledtRNAs) that allows for the detection of the levels of synthesis of individual viral proteins (i.e. NS3) in single cells; (ii) development of a siRNA-mediated knockdown approach for the reduction in levels of expression of NS3 in EHDV2-Ibaraki infected cells; (iii) biochemical and microscopy-based analysis of the localization, levels and post-translational modifications of NS3 in infected cells. In addition, we identified the altered regulation and spatial compartmentalization of protein synthesis in cells infected with EHDV2-Ibaraki or the mammalian reovirus. In EHDV2-Ibaraki-infected cells such altered regulation in protein synthesis occurs in the context of a cell stress reponse that includes the induction of apoptosis, autophagy and activation of the stressrelated kinase c-Jun N-terminal Kinase (JNK). Interestingly, inhibition of such stress-related cellular processes diminishes the production of infectious virions, suggesting that EHDV usurps these responses for the benefit of efficient infection. Taken together, while the present project fell short of the generation of novel reverse genetics systems for orbiviruses, the development of novel experimental approaches and techniques, and their employment in the analysis of EHDV-infected cells, yielded novel insights in the interactions of orbiviruses with mammalian cells.
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