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Journal articles on the topic 'DYRK2'

Author: Grafiati

Published: 1 April 2023

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1

Correa-Sáez, Alejandro, Rafael Jiménez-Izquierdo, Martín Garrido-Rodríguez, Rosario Morrugares, Eduardo Muñoz, and Marco A. Calzado. "Updating dual-specificity tyrosine-phosphorylation-regulated kinase 2 (DYRK2): molecular basis, functions and role in diseases." Cellular and Molecular Life Sciences 77, no. 23 (May 27, 2020): 4747–63. http://dx.doi.org/10.1007/s00018-020-03556-1.

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Abstract Members of the dual-specificity tyrosine-regulated kinase (DYRKs) subfamily possess a distinctive capacity to phosphorylate tyrosine, serine, and threonine residues. Among the DYRK class II members, DYRK2 is considered a unique protein due to its role in disease. According to the post-transcriptional and post-translational modifications, DYRK2 expression greatly differs among human tissues. Regarding its mechanism of action, this kinase performs direct phosphorylation on its substrates or acts as a priming kinase, enabling subsequent substrate phosphorylation by GSK3β. Moreover, DYRK2 acts as a scaffold for the EDVP E3 ligase complex during the G2/M phase of cell cycle. DYRK2 functions such as cell survival, cell development, cell differentiation, proteasome regulation, and microtubules were studied in complete detail in this review. We have also gathered available information from different bioinformatic resources to show DYRK2 interactome, normal and tumoral tissue expression, and recurrent cancer mutations. Then, here we present an innovative approach to clarify DYRK2 functionality and importance. DYRK2 roles in diseases have been studied in detail, highlighting this kinase as a key protein in cancer development. First, DYRK2 regulation of c-Jun, c-Myc, Rpt3, TERT, and katanin p60 reveals the implication of this kinase in cell-cycle-mediated cancer development. Additionally, depletion of this kinase correlated with reduced apoptosis, with consequences on cancer patient response to chemotherapy. Other functions like cancer stem cell formation and epithelial–mesenchymal transition regulation are also controlled by DYRK2. Furthermore, the pharmacological modulation of this protein by different inhibitors (harmine, curcumine, LDN192960, and ID-8) has enabled to clarify DYRK2 functionality.

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2

Kinstrie, Ross, Pamela A. Lochhead, Gary Sibbet, Nick Morrice, and Vaughn Cleghon. "dDYRK2 and Minibrain interact with the chromatin remodelling factors SNR1 and TRX." Biochemical Journal 398, no. 1 (July 27, 2006): 45–54. http://dx.doi.org/10.1042/bj20060159.

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The DYRKs (dual specificity tyrosine phosphorylation-regulated kinases) are a conserved family of protein kinases that autophosphorylate a tyrosine residue in their activation loop by an intra-molecular mechanism and phosphorylate exogenous substrates on serine/threonine residues. Little is known about the identity of true substrates for DYRK family members and their binding partners. To address this question, we used full-length dDYRK2 (Drosophila DYRK2) as bait in a yeast two-hybrid screen of a Drosophila embryo cDNA library. Of 14 independent dDYRK2 interacting clones identified, three were derived from the chromatin remodelling factor, SNR1 (Snf5-related 1), and three from the essential chromatin component, TRX (trithorax). The association of dDYRK2 with SNR1 and TRX was confirmed by co-immunoprecipitation studies. Deletion analysis showed that the C-terminus of dDYRK2 modulated the interaction with SNR1 and TRX. DYRK family member MNB (Minibrain) was also found to co-precipitate with SNR1 and TRX, associations that did not require the C-terminus of the molecule. dDYRK2 and MNB were also found to phosphorylate SNR1 at Thr102in vitro and in vivo. This phosphorylation required the highly conserved DH-box (DYRK homology box) of dDYRK2, whereas the DH-box was not essential for phosphorylation by MNB. This is the first instance of phosphorylation of SNR1 or any of its homologues and implicates the DYRK family of kinases with a role in chromatin remodelling.

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3

Banerjee, Sourav, Chenggong Ji, Joshua E. Mayfield, Apollina Goel, Junyu Xiao, Jack E. Dixon, and Xing Guo. "Ancient drug curcumin impedes 26S proteasome activity by direct inhibition of dual-specificity tyrosine-regulated kinase 2." Proceedings of the National Academy of Sciences 115, no. 32 (July 9, 2018): 8155–60. http://dx.doi.org/10.1073/pnas.1806797115.

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Curcumin, the active ingredient in Curcuma longa, has been in medicinal use since ancient times. However, the therapeutic targets and signaling cascades modulated by curcumin have been enigmatic despite extensive research. Here we identify dual-specificity tyrosine-regulated kinase 2 (DYRK2), a positive regulator of the 26S proteasome, as a direct target of curcumin. Curcumin occupies the ATP-binding pocket of DYRK2 in the cocrystal structure, and it potently and specifically inhibits DYRK2 over 139 other kinases tested in vitro. As a result, curcumin diminishes DYRK2-mediated 26S proteasome phosphorylation in cells, leading to reduced proteasome activity and impaired cell proliferation. Interestingly, curcumin synergizes with the therapeutic proteasome inhibitor carfilzomib to induce apoptosis in a variety of proteasome-addicted cancer cells, while this drug combination exhibits modest to no cytotoxicity to noncancerous cells. In a breast cancer xenograft model, curcumin treatment significantly reduces tumor burden in immunocompromised mice, showing a similar antitumor effect as CRISPR/Cas9-mediated DYRK2 depletion. These results reveal an unexpected role of curcumin in DYRK2-proteasome inhibition and provide a proof-of-concept that pharmacological manipulation of proteasome regulators may offer new opportunities for anticancer treatment.

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4

Seo, D. H., H. W. Ma, S. Kim, D. H. Kim, H. K. Kim, S. H. Lee, S. Kim, et al. "P001 The novel DYRK1a inhibitor VRN024219 alleviates disease severity on the IBD mouse models by modulating T-cell differentiation." Journal of Crohn's and Colitis 14, Supplement_1 (January 2020): S129. http://dx.doi.org/10.1093/ecco-jcc/jjz203.130.

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Abstract Background DYRK1A belongs to dual-specificity tyrosine (Y) phosphorylation regulated kinase (DYRK) family which is known to be activated through autophosphorylation of tyrosine residues in the activation loop and phosphorylates their substrates on serine and threonine residues. Other members of this family include DYRK1B, DYRK2, DYRK3, and DYRK4. Studies have revealed that DYRK kinase family plays an important role in regulating cell proliferation and apoptosis. DYRK1A has been reported to be strongly expressed in the brain and known to regulate various functions. However, the role and underlying mechanisms of DYRK1a in inflammation in general, specifically in IBD, remain poorly understood. Accordingly, we present the underlying mechanisms of DYRK1a on the course of IBD by using the novel DYRK1a inhibitor VRN024219. Methods First, we tested the effects of our compound VRN024219 on T-cell differentiation using naïve CD4 T cells extracted from the mouse spleen. Then we assessed the efficacy and mechanism of VRN024219 on the dextran sodium sulphate (DSS) and T-cell transfer-induced experimental colitis that mimics human ulcerative colitis (UC), comparing to that of Tofacitinib. Finally, we evaluated the effect of VRN024219 on pro-inflammatory cytokines such as interleukin (IL) −17A, IL-6, and tumour necrosis factor (TNF) α expressed by peripheral blood mononuclear cells (PBMCs) from 20 UC patient samples (Severance Hospital, Seoul, Korea). Results When VRN024219 was treated to splenocyte, the compound significantly downregulated Th17 and enhanced T reg cell differentiation. Protein levels of IL-17a, IL-6, and TNF α were increased in the DSS-induced colitis mice, whereas administration of DYRK1a inhibitor VRN024219 substantially improved clinical score than that of Tofacitinib-treated group. Additionally from T-cell transfer-induced colitis model, VRN024219 treated group demonstrated a larger population of ROR γ T-cell than that of tofacitinib Finally, the protein levels of proinflammatory cytokines were significantly down-regulated in VRN024219 treated 20 patient samples. Conclusion Our data provide clear evidence that the novel DYRK1a inhibitor plays a protective role in DSS- and T-cell transfer-induced colitis which was closely related to a Th17/Treg modulation. Thus, VRN024219 might a promising candidate for a new drug for IBD.

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5

Banerjee, Sourav, Tiantian Wei, Jue Wang, Jenna J. Lee, Haydee L. Gutierrez, Owen Chapman, Sandra E. Wiley, et al. "Inhibition of dual-specificity tyrosine phosphorylation-regulated kinase 2 perturbs 26S proteasome-addicted neoplastic progression." Proceedings of the National Academy of Sciences 116, no. 49 (November 21, 2019): 24881–91. http://dx.doi.org/10.1073/pnas.1912033116.

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Dependence on the 26S proteasome is an Achilles’ heel for triple-negative breast cancer (TNBC) and multiple myeloma (MM). The therapeutic proteasome inhibitor, bortezomib, successfully targets MM but often leads to drug-resistant disease relapse and fails in breast cancer. Here we show that a 26S proteasome-regulating kinase, DYRK2, is a therapeutic target for both MM and TNBC. Genome editing or small-molecule mediated inhibition of DYRK2 significantly reduces 26S proteasome activity, bypasses bortezomib resistance, and dramatically delays in vivo tumor growth in MM and TNBC thereby promoting survival. We further characterized the ability of LDN192960, a potent and selective DYRK2-inhibitor, to alleviate tumor burden in vivo. The drug docks into the active site of DYRK2 and partially inhibits all 3 core peptidase activities of the proteasome. Our results suggest that targeting 26S proteasome regulators will pave the way for therapeutic strategies in MM and TNBC.

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6

Park, Chun Shik, Ye Shen, Koramit Suppipat, Andrew Lewis, Julie Tomolonis, Monica Puppi, toni-Ann Mistretta, Leyuan Ma, Michael R. Green, and Daniel Lacorazza. "DYRK2 Inhibits the Self-Renewal of Leukemic Stem Cells in Chronic Myeloid Leukemia By Inducing Degradation of c-Myc Downstream of the Reprogramming Factor KLF4." Blood 128, no. 22 (December 2, 2016): 1879. http://dx.doi.org/10.1182/blood.v128.22.1879.1879.

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Abstract Chronic myeloid leukemia (CML) is a blood cancer originated by expression of BCR-ABL, a constitutively activated kinase product of the chromosomal translocation t(9;22), in hematopoietic stem cells (HSC). Although tyrosine kinase inhibitors (TKI) can efficiently induce molecular remission in CML patients, drug discontinuation often leads to relapse caused by reactivation of leukemic stem cells (LSC) spared from TKI therapy via BCR-ABL-independent mechanisms of self-renewal and survival. Thus, there is a need for alternative drugs for relapse patients to prevent expansion of BCR-ABL-positive LSC during discontinuation of chemotherapy or emergence of chemoresistance. We found that somatic deletion of the reprogramming factor Krüppel-like factor 4 (KLF4) in BCR-ABL(p210)-induced CML severely impaired disease maintenance. This inability to sustain CML in the absence of KLF4 was caused by a progressive attrition of LSCs in bone marrow and the spleen and impaired ability of LSCs to recapitulate leukemia in secondary recipients. Analyses of global gene expression and genome-wide binding of KLF4 revealed that the dual-specificity tyrosine-(Y)-phosphorylation regulated kinase 2 (DYRK2) is repressed by KLF4 in CML LSCs. Immunoblots revealed elevated levels of DYRK2 protein that were associated with a reduction of c-Myc protein and increased levels of p53 (S46) phosphorylation and PARP cleavage in KLF4-deficient LSCs purified from the bone marrow of CML mice. Genomic silencing of KLF4 in the murine CML cell line 32D-BCR-ABL resulted in increased levels of DYRK2 and phosphorylated c-Myc (S62) leading to diminished levels of c-Myc protein, which was reverted by treatment with a proteasome inhibitor, suggesting that KLF4 prevents c-Myc degradation triggered by DYRK2-mediated priming phosphorylation. Consistent with an inhibitory role in leukemia, DYRK2 levels are significantly reduced both in CD34+CD38+ and CD34+CD38− cells from CML patients compared to normal stem/progenitor cells. Aiming at pharmacological activation of DYRK2 to abrogate self-renewal and survival of CML cells, we treated CML cells with vitamin K3 that inhibits Siah2, an ubiquitin E3 ligase involved in Dyrk2 proteolysis. Vitamin K3, and not Vitamin K1 and K2, induces dose-dependent cytotoxicity in a panel of human-derived CML cell lines by stabilizing Dyrk2 protein and consequently promoting c-Myc degradation. Interestingly, combination of vitamin K3 with Imatinib exhibit additive effect inducing cytotoxicity in CML cells. Collectively, the identification of Dyrk2 as a critical mediator of LSC downfall is a novel paradigm poised to support the development of LSC-specific therapy to induce treatment-free remission in conjunction with Imitinib in CML patients. Disclosures No relevant conflicts of interest to declare.

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7

Mao, Cui, Xing Ju, Haijian Cheng, Xixia Huang, Fugui Jiang, Yuni Yao, Xianyong Lan, and Enliang Song. "Determination of genetic variation within the <i>DYRK2</i> gene and its associations with milk traits in cattle." Archives Animal Breeding 63, no. 2 (September 9, 2020): 315–23. http://dx.doi.org/10.5194/aab-63-315-2020.

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Abstract. To speed up the progress of marker-assisted selection (MAS) in cattle breeding, the dual-specificity tyrosine phosphorylation-regulated kinase 2 (DYRK2), cadherin 2 (CDH2), and kinesin family member 1A (KIF1A) genes were chosen based on our pervious genome-wide association study (GWAS) analysis results. DYRK2 is a kinase that may participate in cell growth and/or development; it shows phosphorylation activity toward serine, threonine, and tyrosine fragments of proteins, and it is different from other protein kinases. The CDH2 gene encodes a classic cadherin, which is a member of the cadherin superfamily. The protein encoded by KIF1A is a member of the kinesin family and plays a role in the transportation of membrane organelles along axon microtubules. We detected insertion/deletion (InDel) variation in these three candidate genes in 438 individual cattle (Xinjiang Brown cattle and Wagyu × Luxi crossbreed cattle). Only DYRK2-P3-11 bp was polymorphic and genotyped. The polymorphism information content of DYRK2-P3-11 bp was 0.336. Correlation analyses showed that InDel polymorphism was significantly associated with six different milk traits. These findings may aid future analyses of InDel genotypes in cattle breeds, and speed up the progress of MAS in cattle breeding.

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8

Morrugares, Rosario, Alejandro Correa-Sáez, Rita Moreno, Martín Garrido-Rodríguez, Eduardo Muñoz, Laureano de la Vega, and Marco A. Calzado. "Phosphorylation-dependent regulation of the NOTCH1 intracellular domain by dual-specificity tyrosine-regulated kinase 2." Cellular and Molecular Life Sciences 77, no. 13 (October 11, 2019): 2621–39. http://dx.doi.org/10.1007/s00018-019-03309-9.

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Abstract NOTCH proteins constitute a receptor family with a widely conserved role in cell cycle, growing and development regulation. NOTCH1, the best characterised member of this family, regulates the expression of key genes in cell growth and angiogenesis, playing an essential role in cancer development. These observations provide a relevant rationale to propose the inhibition of the intracellular domain of NOTCH1 (Notch1-IC) as a strategy for treating various types of cancer. Notch1-IC stability is mainly controlled by post-translational modifications. FBXW7 ubiquitin E3 ligase-mediated degradation is considered one of the most relevant, being the previous phosphorylation at Thr-2512 residue required. In the present study, we describe for the first time a new regulation mechanism of the NOTCH1 signalling pathway mediated by DYRK2. We demonstrate that DYRK2 phosphorylates Notch1-IC in response to chemotherapeutic agents and facilitates its proteasomal degradation by FBXW7 ubiquitin ligase through a Thr-2512 phosphorylation-dependent mechanism. We show that DYRK2 regulation by chemotherapeutic agents has a relevant effect on the viability, motility and invasion capacity of cancer cells expressing NOTCH1. In summary, we reveal a novel mechanism of regulation for NOTCH1 which might help us to better understand its role in cancer biology.

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9

Shen, Yifen, Li Zhang, Donglin Wang, Yifeng Bao, Chao Liu, Zhiwei Xu, Wei Huang, and Chun Cheng. "Regulation of Glioma Cells Migration by DYRK2." Neurochemical Research 42, no. 11 (July 4, 2017): 3093–102. http://dx.doi.org/10.1007/s11064-017-2345-2.

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10

Aman, La Ode, Rahmana Emran Kartasasmita, and Daryono Hadi Tjahjono. "Virtual screening of curcumin analogues as DYRK2 inhibitor: Pharmacophore analysis, molecular docking and dynamics, and ADME prediction." F1000Research 10 (May 17, 2021): 394. http://dx.doi.org/10.12688/f1000research.28040.1.

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Background: Curcumin reduces the proliferation of cancer cells through inhibition of the DYRK2 enzyme, which is a positive regulator of the 26S proteasome. Methods: In the present work, curcumin analogues have been screened from the MolPort database using a pharmacophore model that comprised a ligand-based approach. The result of the screening was then evaluated by molecular docking and molecular dynamics based on binding the free energy of the interaction between each compound with the binding pocket of DYRK2. The hit compounds were then confirmed by absorption, distribution, metabolism, and excretion (ADME) prediction. Results: Screening of 7.4 million molecules from the MolPort database afforded six selected hit compounds. By considering the ADME prediction, three prospective curcumin analogues have been selected. These are: 2‐[2‐(1‐methylpyrazol‐4‐yl)ethyl]‐1H,5H,6H,7H,8H‐imidazo[4,5‐c]azepin‐4‐one (Molport-035-369-361), methyl 4‐(3‐hydroxy‐1,2‐oxazol‐5‐yl)piperidine‐1‐carboxylate (Molport-000-004-273) and (1S)‐1‐[5‐(furan‐3‐carbonyl)‐4H,6H,7H‐pyrazolo[1,5‐a]pyrazin‐2‐yl]ethanol (MolPort-035-585-822). Conclusion: Pharmacophore modelling, combined with molecular docking and molecular dynamics simulation, as well as ADME prediction were successfully applied to screen curcumin analogues from the MolPort database as DYRK2 inhibitors. All selected compounds that have better predicted pharmacokinetic properties than that of curcumin are considered for further study.

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Ong, Su Sien, Asli N. Goktug, Ayesha Elias, Jing Wu, Darren Saunders, and Taosheng Chen. "Stability of the human pregnane X receptor is regulated by E3 ligase UBR5 and serine/threonine kinase DYRK2." Biochemical Journal 459, no. 1 (March 14, 2014): 193–203. http://dx.doi.org/10.1042/bj20130558.

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Mass spectrometry analysis and a kinome-wide siRNA screen revealed that phosphorylation of pregnane X receptor, a major chemical toxin sensor, by the serine/threonine kinase DYRK2 facilitates its subsequent ubiquitination by the E3 ligase UBR5.

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Erickson-Miller, Connie L., Caretha Creasy, Antony Chadderton, Christopher B. Hopson, Elizabeth I. Valoret, Michele Gorczyca, Louis Elefante, et al. "GSK626616: A DYRK3 Inhibitor as a Potential New Therapy for the Treatment of Anemia." Blood 110, no. 11 (November 16, 2007): 510. http://dx.doi.org/10.1182/blood.v110.11.510.510.

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Abstract Through both in vitro and in vivo validation studies, such as antisense RNA and gene knock-out experiments, DYRK3 has been implicated as a negative regulator of erythropoiesis. DYRK3, a member of the dual-specificity tyrosine phosphorylation-regulated kinase family, is expressed at low levels in erythroid progenitors and plays a regulatory role in their cellular proliferation and differentiation. High-throughput screening at GSK resulted in the identification of a novel series of thiazolidinone inhibitors of DYRK3. Lead optimization efforts then led to the discovery of GSK626616 as a potent, orally bioavailable inhibitor of DYRK3. GSK626616, inhibits DYRK3 in vitro with an IC50of 0.7 nM. This low molecular weight compound (401 Da) inhibits other members of the DYRK family, e.g., DYRK1A and DYRK2, with similar potency and with an approximate 20-fold selectivity versus the next most potently inhibited kinase, casein kinase 2. GSK626616AC, the meglumine, monohydrate salt form, has high oral bioavailability in all pre-clinical species studied (e.g. canine AUC = 23.64 ± 2.84 μghr/mL for a 30 mg/kg dose presented as crystalline material packed within a capsule). In cellular assays, GSK626616 enhances the number of CFU-E stimulated by Epo from human marrow, although it has no CFU-E activity on its own, consistent with the target’s functional role as a negative regulator. GSK626616 is specific for the erythroid lineage and does not stimulate CFU-GM colonies, either alone or in the presence of G-CSF or GM-CSF. There is also no direct effect on megakaryocyte colony growth from progenitor cells. 3H-thymidine incorporation in kit+ murine marrow is also stimulated after 3 days by exposure to GSK626616 in the presence of SCF and EPO. Similarly, 3 day treatment with GSK626616 increased the percentage, as well as the absolute number, of Ter119+/CD71+ erythroid progenitors derived from kit+ mouse marrow in the presence of SCF and Epo. GSK626616 (0.0001 to 30 uM) dosed i.p., daily for 14 days had no effect on the blood counts of normal mice, either alone or in the presence of 200 or 600 U/kg Epo. This was not unexpected based upon the very low levels of DYRK3 expression in the bone marrow of normal, non-anemic mice and on results previously reported for knock-out mice. These mice have normal erythropoiesis, but demonstrate an enhanced recovery from erythropoietic stress (Wojchowski, Blood 2005). Anemic mice, treated with a daily dose of GSK626616, i.p., had a statistically significant increase in hemoglobin compared to those dosed with vehicle alone at day 15 after anemia was induced through carboplatin/radiation treatment. Platelet levels were also elevated compared to vehicle control at day 15. These data suggest that treatment with GSK626616, through inhibition of DYRK3 activity, leads to an increase in the proliferation of kit+ cells producing an increased number of Ter119+/CD71+ erythroblasts, thereby accelerating recovery from the anemic insult in a carboplatin/radiation mouse model. It is hypothesized that this mechanism may only function under anemic conditions when DYRK3 is elevated and therefore, that the effects will be self-regulated as hemoglobin and EPO levels approach the normal range.

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Park, Chun Shik, and H. Daniel Lacorazza. "DYRK2 controls a key regulatory network in chronic myeloid leukemia stem cells." Experimental & Molecular Medicine 52, no. 10 (October 2020): 1663–72. http://dx.doi.org/10.1038/s12276-020-00515-5.

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Abstract Chronic myeloid leukemia is a hematological cancer driven by the oncoprotein BCR-ABL1, and lifelong treatment with tyrosine kinase inhibitors extends patient survival to nearly the life expectancy of the general population. Despite advances in the development of more potent tyrosine kinase inhibitors to induce a durable deep molecular response, more than half of patients relapse upon treatment discontinuation. This clinical finding supports the paradigm that leukemia stem cells feed the neoplasm, resist tyrosine kinase inhibition, and reactivate upon drug withdrawal depending on the fitness of the patient’s immune surveillance. This concept lends support to the idea that treatment-free remission is not achieved solely with tyrosine kinase inhibitors and that new molecular targets independent of BCR-ABL1 signaling are needed in order to develop adjuvant therapy to more efficiently eradicate the leukemia stem cell population responsible for chemoresistance and relapse. Future efforts must focus on the identification of new targets to support the discovery of potent and safe small molecules able to specifically eradicate the leukemic stem cell population. In this review, we briefly discuss molecular maintenance in leukemia stem cells in chronic myeloid leukemia and provide a more in-depth discussion of the dual-specificity kinase DYRK2, which has been identified as a novel actionable checkpoint in a critical leukemic network. DYRK2 controls the activation of p53 and proteasomal degradation of c-MYC, leading to impaired survival and self-renewal of leukemia stem cells; thus, pharmacological activation of DYRK2 as an adjuvant to standard therapy has the potential to induce treatment-free remission.

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Sun, Yuxiang, Xin Ge, Mengmeng Li, Li Xu, and Yaodong Shen. "Dyrk2 involved in regulating LPS-induced neuronal apoptosis." International Journal of Biological Macromolecules 104 (November 2017): 979–86. http://dx.doi.org/10.1016/j.ijbiomac.2017.06.087.

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Park, Chun Shik, Andrew H. Lewis, Taylor J. Chen, Cory S. Bridges, Ye Shen, Koramit Suppipat, Monica Puppi, et al. "A KLF4-DYRK2–mediated pathway regulating self-renewal in CML stem cells." Blood 134, no. 22 (November 28, 2019): 1960–72. http://dx.doi.org/10.1182/blood.2018875922.

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Park et al describe a novel KLF4-mediated pathway that promotes chromic myeloid leukemia (CML) stem cell (LSC) survival. Deletion of KLF4 in a mouse model of CML decreases LSC survival through repression of Dyrk2, resulting in c-Myc depletion and increased p53 activity.

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WOODS, Yvonne L., Philip COHEN, Walter BECKER, Ross JAKES, Michel GOEDERT, Xuemin WANG, and Christopher G. PROUD. "The kinase DYRK phosphorylates protein-synthesis initiation factor eIF2Bɛ at Ser539 and the microtubule-associated protein tau at Thr212: potential role for DYRK as a glycogen synthase kinase 3-priming kinase." Biochemical Journal 355, no. 3 (April 24, 2001): 609–15. http://dx.doi.org/10.1042/bj3550609.

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The substrate specificity of glycogen synthase kinase 3 (GSK3) is unusual in that efficient phosphorylation only occurs if another phosphoserine or phosphothreonine residue is already present four residues C-terminal to the site of GSK3 phosphorylation. One such substrate is the ε-subunit of rat eukaryotic protein-synthesis initiation factor 2B (eIF2Bε), which is inhibited by the GSK3-catalysed phosphorylation of Ser535. There is evidence that GSK3 is only able to phosphorylate eIF2Bε at Ser535 if Ser539 is already phosphorylated by another protein kinase. However, no protein kinases capable of phosphorylating Ser539 have so far been identified. Here we show that Ser539 of eIF2Bε, which is followed by proline, is phosphorylated specifically by two isoforms of dual-specificity tyrosine phosphorylated and regulated kinase (DYRK2 and DYRK1A), but only weakly or not at all by other ‘proline-directed’ protein kinases tested. We also establish that phosphorylation of Ser539 permits GSK3 to phosphorylate Ser535in vitro and that eIF2Bε is highly phosphorylated at Ser539in vivo. The DYRK isoforms also phosphorylate human microtubule-associated protein tau at Thr212in vitro, a residue that is phosphorylated in foetal tau and hyperphosphorylated in filamentous tau from Alzheimer's-disease brain. Phosphorylation of Thr212 primes tau for phosphorylation by GSK3 at Ser208in vitro, suggesting a more general role for DYRK isoforms in priming phosphorylation of GSK3 substrates.

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Li, Xu, Min Wang, Jian-Xin Jiang, Rui Tian, Cheng-Jian Shi, and Ren-Yi Qin. "Clinical significance of expression of DYRK2 in pancreatic cancer." World Chinese Journal of Digestology 21, no. 15 (2013): 1442. http://dx.doi.org/10.11569/wcjd.v21.i15.1442.

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Nihira, Naoe Taira, and Kiyotsugu Yoshida. "Engagement of DYRK2 in proper control for cell division." Cell Cycle 14, no. 6 (March 19, 2015): 802–7. http://dx.doi.org/10.1080/15384101.2015.1007751.

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Yoshida, Saishu, and Kiyotsugu Yoshida. "Multiple functions of DYRK2 in cancer and tissue development." FEBS Letters 593, no. 21 (September 18, 2019): 2953–65. http://dx.doi.org/10.1002/1873-3468.13601.

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Laham, Amina Jamal, Raafat El-Awady, Jean-Jacques Lebrun, and Maha Saber Ayad. "A Bioinformatics Evaluation of the Role of Dual-Specificity Tyrosine-Regulated Kinases in Colorectal Cancer." Cancers 14, no. 8 (April 18, 2022): 2034. http://dx.doi.org/10.3390/cancers14082034.

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Colorectal cancer (CRC) is the third most common cancer worldwide and has an increasing incidence in younger populations. The dual-specificity tyrosine-regulated kinase (DYRK) family has been implicated in various diseases, including cancer. However, the role and contribution of the distinct family members in regulating CRC tumorigenesis has not been addressed yet. Herein, we used publicly available CRC patient datasets (TCGA RNA sequence) and several bioinformatics webtools to perform in silico analysis (GTEx, GENT2, GEPIA2, cBioPortal, GSCALite, TIMER2, and UALCAN). We aimed to investigate the DYRK family member expression pattern, prognostic value, and oncological roles in CRC. This study shed light on the role of distinct DYRK family members in CRC and their potential outcome predictive value. Based on mRNA level, DYRK1A is upregulated in late tumor stages, with lymph node and distant metastasis. All DYRKs were found to be implicated in cancer-associated pathways, indicating their key role in CRC pathogenesis. No significant DYRK mutations were identified, suggesting that DYRK expression variation in normal vs. tumor samples is likely linked to epigenetic regulation. The expression of DYRK1A and DYRK3 expression correlated with immune-infiltrating cells in the tumor microenvironment and was upregulated in MSI subtypes, pointing to their potential role as biomarkers for immunotherapy. This comprehensive bioinformatics analysis will set directions for future biological studies to further exploit the molecular basis of these findings and explore the potential of DYRK1A modulation as a novel targeted therapy for CRC.

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Karpov, Pavel, Aleksey Raevsky, Maxim Korablyov, and Yaroslav Blume. "Identification of Plant Homologues of Dual Specificity Yak1-Related Kinases." Computational Biology Journal 2014 (December 8, 2014): 1–14. http://dx.doi.org/10.1155/2014/909268.

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Currently, Dual Specificity YAK1-Related Kinases (MNB/DYRK) were found in slime molds, protista, fungi, and animals, but the existence of plant homologues is still unclear. In the present study, we have identified 14 potential plant homologues with the previously unknown functions, based on the strong sequence similarity. The results of bioinformatics analysis revealed their correspondence to DYRK1A, DYRK1B, DYRK3, and DYRK4. For two plant homologues of animal DYRK1A from Physcomitrella patens and Arabidopsis thaliana spatial structures of catalytic domains were predicted, as well as their complexes with ADP and selective inhibitor d15. Comparative analysis of 3D-structures of the human DYRK1A and plant homologues, their complexes with the specific inhibitors, and results of molecular dynamics confirm their structural and functional similarity with high probability. Preliminary data indicate the presence of potential MNB/DYRK specific phosphorylation sites in such proteins associated with plant cytoskeleton as plant microtubule-associated proteins WVD2 and WDL1, and FH5 and SCAR2 involved in the organization and polarity of the actin cytoskeleton and some kinesin-like microtubule motor proteins.

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22

Hossain, Delowar, Jérémy A. Ferreira Barbosa, Éric A. Cohen, and William Y. Tsang. "HIV-1 Vpr hijacks EDD-DYRK2-DDB1DCAF1to disrupt centrosome homeostasis." Journal of Biological Chemistry 293, no. 24 (May 3, 2018): 9448–60. http://dx.doi.org/10.1074/jbc.ra117.001444.

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23

Sun, Wei, Shuang Jiao, Xungang Tan, Peijun Zhang, and Feng You. "DYRK2 displays muscle fiber type specific function during zebrafish early somitogenesis." International Journal of Developmental Biology 61, no. 6-7 (2017): 459–63. http://dx.doi.org/10.1387/ijdb.160175sj.

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24

Luebbering, Nathan, Mark Charlton-Perkins, Justin P. Kumar, Stephanie M. Rollmann, Tiffany Cook, and Vaughn Cleghon. "Drosophila Dyrk2 Plays a Role in the Development of the Visual System." PLoS ONE 8, no. 10 (October 11, 2013): e76775. http://dx.doi.org/10.1371/journal.pone.0076775.

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25

Bahl, Anu, Prashant Joshi, Sandip B. Bharate, and Harish Chopra. "Pharmacophore modeling and 3D-QSAR studies of leucettines as potent Dyrk2 inhibitors." Medicinal Chemistry Research 23, no. 4 (September 26, 2013): 1925–33. http://dx.doi.org/10.1007/s00044-013-0767-1.

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26

Mimoto, Rei, Naoe Taira, Hiroyuki Takahashi, Tomoko Yamaguchi, Masataka Okabe, Ken Uchida, Yoshio Miki, and Kiyotsugu Yoshida. "DYRK2 controls the epithelial–mesenchymal transition in breast cancer by degrading Snail." Cancer Letters 339, no. 2 (October 2013): 214–25. http://dx.doi.org/10.1016/j.canlet.2013.06.005.

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27

Jung, Hae-Yun, Xin Wang, Sohee Jun, and Jae-Il Park. "Dyrk2-associated EDD-DDB1-VprBP E3 Ligase Inhibits Telomerase by TERT Degradation." Journal of Biological Chemistry 288, no. 10 (January 28, 2013): 7252–62. http://dx.doi.org/10.1074/jbc.m112.416792.

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28

Pérez, Moisés, Carmen García-Limones, Inés Zapico, Anabel Marina, M. Lienhard Schmitz, Eduardo Muñoz, and Marco A. Calzado. "Mutual regulation between SIAH2 and DYRK2 controls hypoxic and genotoxic signaling pathways." Journal of Molecular Cell Biology 4, no. 5 (August 9, 2012): 316–30. http://dx.doi.org/10.1093/jmcb/mjs047.

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29

Xu, Li, Yuxiang Sun, Mengmeng Li, and Xin Ge. "Dyrk2 mediated the release of proinflammatory cytokines in LPS-induced BV2 cells." International Journal of Biological Macromolecules 109 (April 2018): 1115–24. http://dx.doi.org/10.1016/j.ijbiomac.2017.11.095.

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30

VerPlank, Jordan J. S., and Alfred L. Goldberg. "Regulating protein breakdown through proteasome phosphorylation." Biochemical Journal 474, no. 19 (September 25, 2017): 3355–71. http://dx.doi.org/10.1042/bcj20160809.

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The ubiquitin proteasome system degrades the great majority of proteins in mammalian cells. Countless studies have described how ubiquitination promotes the selective degradation of different cell proteins. However, there is a small but growing literature that protein half-lives can also be regulated by post-translational modifications of the 26S proteasome. The present study reviews the ability of several kinases to alter proteasome function through subunit phosphorylation. For example, PKA (protein kinase A) and DYRK2 (dual-specificity tyrosine-regulated kinase 2) stimulate the proteasome's ability to degrade ubiquitinated proteins, peptides, and adenosine triphosphate, while one kinase, ASK1 (apoptosis signal-regulating kinase 1), inhibits proteasome function during apoptosis. Proteasome phosphorylation is likely to be important in regulating protein degradation because it occurs downstream from many hormones and neurotransmitters, in conditions that raise cyclic adenosine monophosphate or cyclic guanosine monophosphate levels, after calcium influx following synaptic depolarization, and during phases of the cell cycle. Beyond its physiological importance, pharmacological manipulation of proteasome phosphorylation has the potential to combat various diseases. Inhibitors of phosphodiesterases by activating PKA or PKG (protein kinase G) can stimulate proteasomal degradation of misfolded proteins that cause neurodegenerative or myocardial diseases and even reduce the associated pathology in mouse models. These observations are promising since in many proteotoxic diseases, aggregation-prone proteins impair proteasome function, and disrupt protein homeostasis. Conversely, preventing subunit phosphorylation by DYRK2 slows cell cycle progression and tumor growth. However, further research is essential to determine how phosphorylation of different subunits by these (or other) kinases alters the properties of this complex molecular machine and thus influence protein degradation rates.

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31

Maddika, Subbareddy, and Junjie Chen. "Protein kinase DYRK2 is a scaffold that facilitates assembly of an E3 ligase." Nature Cell Biology 11, no. 4 (March 15, 2009): 409–19. http://dx.doi.org/10.1038/ncb1848.

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32

Cuny, Gregory D., Maxime Robin, Natalia P. Ulyanova, Debasis Patnaik, Valerie Pique, Gilles Casano, Ji-Feng Liu, et al. "Structure–activity relationship study of acridine analogs as haspin and DYRK2 kinase inhibitors." Bioorganic & Medicinal Chemistry Letters 20, no. 12 (June 2010): 3491–94. http://dx.doi.org/10.1016/j.bmcl.2010.04.150.

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33

Mimoto, R., Y. Imawari, S. Hirooka, H. Takeyama, and K. Yoshida. "Impairment of DYRK2 augments stem-like traits by promoting KLF4 expression in breast cancer." Oncogene 36, no. 13 (October 10, 2016): 1862–72. http://dx.doi.org/10.1038/onc.2016.349.

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34

An, Tai, Shu Li, Wei Pan, Po Tien, Bo Zhong, Hong-Bing Shu, and Shuwen Wu. "DYRK2 Negatively Regulates Type I Interferon Induction by Promoting TBK1 Degradation via Ser527 Phosphorylation." PLOS Pathogens 11, no. 9 (September 25, 2015): e1005179. http://dx.doi.org/10.1371/journal.ppat.1005179.

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35

Weiss, Celine S., Marco M. Ochs, Marco Hagenmueller, Marcus R. Streit, Pratima Malekar, Johannes H. Riffel, Sebastian J. Buss, et al. "DYRK2 Negatively Regulates Cardiomyocyte Growth by Mediating Repressor Function of GSK-3β on eIF2Bε." PLoS ONE 8, no. 9 (September 4, 2013): e70848. http://dx.doi.org/10.1371/journal.pone.0070848.

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36

Enomoto, Yasuko, Shin-ichi Yamashita, Yasuteru Yoshinaga, Yasuyoshi Fukami, So Miyahara, Kazuki Nabeshima, and Akinori Iwasaki. "Downregulation of DYRK2 can be a predictor of recurrence in early stage breast cancer." Tumor Biology 35, no. 11 (August 6, 2014): 11021–25. http://dx.doi.org/10.1007/s13277-014-2413-z.

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37

Zhang, Xiubing, Pan Xu, Wenkai Ni, Hui Fan, Jian Xu, Yongmei Chen, Wei Huang, et al. "Downregulated DYRK2 expression is associated with poor prognosis and Oxaliplatin resistance in hepatocellular carcinoma." Pathology - Research and Practice 212, no. 3 (March 2016): 162–70. http://dx.doi.org/10.1016/j.prp.2016.01.002.

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38

Yamaguchi, Noriko, Rei Mimoto, Nozomu Yanaihara, Yoshimi Imawari, Shinichi Hirooka, Aikou Okamoto, and Kiyotsugu Yoshida. "DYRK2 regulates epithelial-mesenchymal-transition and chemosensitivity through Snail degradation in ovarian serous adenocarcinoma." Tumor Biology 36, no. 8 (February 25, 2015): 5913–23. http://dx.doi.org/10.1007/s13277-015-3264-y.

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39

Wang, Yuchan, Yaxun Wu, Xiaobing Miao, Xinghua Zhu, Xianjing Miao, Yunhua He, Fei Zhong, et al. "Silencing of DYRK2 increases cell proliferation but reverses CAM-DR in Non-Hodgkin's Lymphoma." International Journal of Biological Macromolecules 81 (November 2015): 809–17. http://dx.doi.org/10.1016/j.ijbiomac.2015.08.067.

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40

Sun, Wei, Xungang Tan, Peijun Zhang, Yuqing Zhang, and Yongli Xu. "Characterization of DYRK2 (dual-specificity tyrosine-phosphorylation-regulated kinase 2) from Zebrafish (Dario rerio)." Chinese Journal of Oceanology and Limnology 28, no. 4 (June 29, 2010): 720–24. http://dx.doi.org/10.1007/s00343-010-9073-7.

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41

Yokoyama-Mashima, Shiho, Satomi Yogosawa, Yumi Kanegae, Shinichi Hirooka, Saishu Yoshida, Takashi Horiuchi, Toya Ohashi, et al. "Forced expression of DYRK2 exerts anti-tumor effects via apoptotic induction in liver cancer." Cancer Letters 451 (June 2019): 100–109. http://dx.doi.org/10.1016/j.canlet.2019.02.046.

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42

Auld, Gillian C., David G. Campbell, Nick Morrice, and Philip Cohen. "Identification of calcium-regulated heat-stable protein of 24 kDa (CRHSP24) as a physiological substrate for PKB and RSK using KESTREL." Biochemical Journal 389, no. 3 (July 26, 2005): 775–83. http://dx.doi.org/10.1042/bj20050733.

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A substrate for PKBα (protein kinase Bα) was detected in liver extracts, and was purified and identified as CRHSP24 (calcium-regulated heat-stable protein of apparent molecular mass 24 kDa). PKBα, as well as SGK1 (serum- and glucocorticoid-induced protein kinase 1) and RSK (p90 ribosomal S6 kinase), phosphorylated CRHSP24 stoichiometrically at Ser52in vitro and its brain-specific isoform PIPPin at the equivalent residue (Ser58). CRHSP24 became phosphorylated at Ser52 when HEK-293 (human embryonic kidney) cells were stimulated with IGF-1 (insulin-like growth factor-1) and this was prevented by inhibitors of PI3K (phosphoinositide 3-kinase), but not by rapamycin [an inhibitor of mTOR (mammalian target of rapamycin)] or PD 184352, an inhibitor of the classical MAPK (mitogen-activated protein kinase) cascade and hence the activation of RSK. IGF-1 induced a similar phosphorylation of CRHSP24 in ES (embryonic stem) cells from wild-type mice or mice that express the PDK1 (3-phosphoinositide-dependent kinase 1) mutant (PDK1[L155E]) that activates PKBα normally, but cannot activate SGK. CRHSP24 also became phosphorylated at Ser52 in response to EGF (epidermal growth factor) and this was prevented by blocking activation of both the classical MAPK cascade and the activation of PKBα, but not if just one of these pathways was inhibited. DYRK2 (dual-specificity tyrosine-phosphorylated and -regulated protein kinase 2) phosphorylated CRHSP24 at Ser30, Ser32 and Ser41in vitro, and Ser41 was identified as a site phosphorylated in cells. These and other results demonstrate that CRHSP24 is phosphorylated at Ser52 by PKBα in response to IGF-1, at Ser52 by PKBα and RSK in response to EGF, and at Ser41 in the absence of IGF-1/EGF by a DYRK isoform or another proline-directed protein kinase(s).

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43

Boni, Jacopo, Carlota Rubio-Perez, Nuria López-Bigas, Cristina Fillat, and Susana de la Luna. "The DYRK Family of Kinases in Cancer: Molecular Functions and Therapeutic Opportunities." Cancers 12, no. 8 (July 29, 2020): 2106. http://dx.doi.org/10.3390/cancers12082106.

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DYRK (dual-specificity tyrosine-regulated kinases) are an evolutionary conserved family of protein kinases with members from yeast to humans. In humans, DYRKs are pleiotropic factors that phosphorylate a broad set of proteins involved in many different cellular processes. These include factors that have been associated with all the hallmarks of cancer, from genomic instability to increased proliferation and resistance, programmed cell death, or signaling pathways whose dysfunction is relevant to tumor onset and progression. In accordance with an involvement of DYRK kinases in the regulation of tumorigenic processes, an increasing number of research studies have been published in recent years showing either alterations of DYRK gene expression in tumor samples and/or providing evidence of DYRK-dependent mechanisms that contribute to tumor initiation and/or progression. In the present article, we will review the current understanding of the role of DYRK family members in cancer initiation and progression, providing an overview of the small molecules that act as DYRK inhibitors and discussing the clinical implications and therapeutic opportunities currently available.

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44

Taira, Naoe, Hiroyuki Yamamoto, Tomoko Yamaguchi, Yoshio Miki, and Kiyotsugu Yoshida. "ATM Augments Nuclear Stabilization of DYRK2 by Inhibiting MDM2 in the Apoptotic Response to DNA Damage." Journal of Biological Chemistry 285, no. 7 (December 4, 2009): 4909–19. http://dx.doi.org/10.1074/jbc.m109.042341.

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45

Mimoto, Rei, Naoe T. Nihira, Shinichi Hirooka, Hiroshi Takeyama, and Kiyotsugu Yoshida. "Diminished DYRK2 sensitizes hormone receptor-positive breast cancer to everolimus by the escape from degrading mTOR." Cancer Letters 384 (January 2017): 27–38. http://dx.doi.org/10.1016/j.canlet.2016.10.015.

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46

TANAKA, MASUMI, SHIN-ICHI YAMASHITA, YASUTERU YOSHINAGA, YASUKO ENOMOTO, YUKI NOHARA, SYUKO ONO, KAZUKI NABESHIMA, AKINORI IWASAKI, and TOSHIHIKO SATO. "Combination of DYRK2 and TERT Expression Is a Powerful Predictive Marker for Early-stage Breast Cancer Recurrence." Anticancer Research 42, no. 4 (March 28, 2022): 2079–85. http://dx.doi.org/10.21873/anticanres.15689.

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47

Zhang, Xiaojing, Runze Xiao, Bing Lu, Han Wu, Chunyi Jiang, Peng Li, and Jianfei Huang. "Kinase DYRK2 acts as a regulator of autophagy and an indicator of favorable prognosis in gastric carcinoma." Colloids and Surfaces B: Biointerfaces 209 (January 2022): 112182. http://dx.doi.org/10.1016/j.colsurfb.2021.112182.

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48

Taira, Naoe, Rei Mimoto, Morito Kurata, Tomoko Yamaguchi, Masanobu Kitagawa, Yoshio Miki, and Kiyotsugu Yoshida. "DYRK2 priming phosphorylation of c-Jun and c-Myc modulates cell cycle progression in human cancer cells." Journal of Clinical Investigation 122, no. 3 (March 1, 2012): 859–72. http://dx.doi.org/10.1172/jci60818.

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49

Ryu, Ki-Jun, Sun-Mi Park, Seung-Ho Park, In-Kyu Kim, Hyeontak Han, Hyo-Jin Kim, Seon-Hee Kim, et al. "p38 Stabilizes Snail by Suppressing DYRK2-Mediated Phosphorylation That Is Required for GSK3β-βTrCP–Induced Snail Degradation." Cancer Research 79, no. 16 (June 17, 2019): 4135–48. http://dx.doi.org/10.1158/0008-5472.can-19-0049.

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50

Nishi, Y., E. Rogers, S. M. Robertson, and R. Lin. "Polo kinases regulate C. elegans embryonic polarity via binding to DYRK2-primed MEX-5 and MEX-6." Development 135, no. 4 (February 15, 2008): 687–97. http://dx.doi.org/10.1242/dev.013425.

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