Log in

Relevant bibliographies by topics / Dual-specificity Tyrosine Phosphorylation-Regulated Kinase / Journal articles

To see the other types of publications on this topic, follow the link: Dual-specificity Tyrosine Phosphorylation-Regulated Kinase.

Journal articles on the topic 'Dual-specificity Tyrosine Phosphorylation-Regulated Kinase'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Consult the top 50 journal articles for your research on the topic 'Dual-specificity Tyrosine Phosphorylation-Regulated Kinase.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Browse journal articles on a wide variety of disciplines and organise your bibliography correctly.

1

LOCHHEAD, Pamela A., Gary SIBBET, Ross KINSTRIE, et al. "dDYRK2: a novel dual-specificity tyrosine-phosphorylation-regulated kinase in Drosophila." Biochemical Journal 374, no. 2 (2003): 381–91. http://dx.doi.org/10.1042/bj20030500.

Full text

Abstract:

Dual-specificity tyrosine-phosphorylation-regulated kinases (DYRKs) are an emerging family of protein kinases that have been identified in all eukaryotic organisms examined to date. DYRK family members are involved in regulating key developmental and cellular processes such as neurogenesis, cell proliferation, cytokinesis and cellular differentiation. Two distinct subgroups exist, nuclear and cytosolic. In Drosophila, the founding family member minibrain, whose human orthologue maps to the Down syndrome critical region, belongs to the nuclear subclass and affects post-embryonic neurogenesis. I

APA, Harvard, Vancouver, ISO, and other styles

2

Qian, Wei, Nana Jin, Jianhua Shi, et al. "Dual-specificity Tyrosine Phosphorylation-regulated Kinase 1A (Dyrk1A) Enhances Tau Expression." Journal of Alzheimer's Disease 37, no. 3 (2013): 529–38. http://dx.doi.org/10.3233/jad-130824.

Full text

APA, Harvard, Vancouver, ISO, and other styles

3

Czarna, Anna, Jinhua Wang, Diana Zelencova, et al. "Novel Scaffolds for Dual Specificity Tyrosine-Phosphorylation-Regulated Kinase (DYRK1A) Inhibitors." Journal of Medicinal Chemistry 61, no. 17 (2018): 7560–72. http://dx.doi.org/10.1021/acs.jmedchem.7b01847.

Full text

APA, Harvard, Vancouver, ISO, and other styles

4

Adayev, Tatyana, Mo-Chou Chen-Hwang, Noriko Murakami, Eric Lee, David C. Bolton, and Yu-Wen Hwang. "Dual-Specificity Tyrosine Phosphorylation-Regulated Kinase 1A Does Not Require Tyrosine Phosphorylation for Activity in Vitro†." Biochemistry 46, no. 25 (2007): 7614–24. http://dx.doi.org/10.1021/bi700251n.

Full text

APA, Harvard, Vancouver, ISO, and other styles

5

Menegay, H. J., M. P. Myers, F. M. Moeslein, and G. E. Landreth. "Biochemical characterization and localization of the dual specificity kinase CLK1." Journal of Cell Science 113, no. 18 (2000): 3241–53. http://dx.doi.org/10.1242/jcs.113.18.3241.

Full text

Abstract:

CLK1 was one of the first identified dual specificity kinases and is the founding member of the ‘LAMMER’ family of kinases. We have established the substrate site specificity of CLK1. We report here that truncation of the N terminus of CLK1 resulted in a dramatic increase in CLK1 enzymatic activity, indicating that the N terminus acts as a negative regulatory domain. The N-terminal truncation resulted in a 45-fold increase in V(max), suggesting that this domain does not contain a pseudo-substrate motif, but may act to conformationally constrain the catalytic activity of CLK1. Tyrosine phosphor

APA, Harvard, Vancouver, ISO, and other styles

6

Jarhad, Dnyandev B., Karishma K. Mashelkar, Hong-Rae Kim, Minsoo Noh, and Lak Shin Jeong. "Dual-Specificity Tyrosine Phosphorylation-Regulated Kinase 1A (DYRK1A) Inhibitors as Potential Therapeutics." Journal of Medicinal Chemistry 61, no. 22 (2018): 9791–810. http://dx.doi.org/10.1021/acs.jmedchem.8b00185.

Full text

APA, Harvard, Vancouver, ISO, and other styles

7

Qian, Wei, Xiaoxia Jin, Nana Jin, Shibao Wang, and Fei Liu. "P4-041: Dual specificity tyrosine-phosphorylation-regulated kinase 1A upregulates tau expression." Alzheimer's & Dementia 9 (July 2013): P718. http://dx.doi.org/10.1016/j.jalz.2013.05.1429.

Full text

APA, Harvard, Vancouver, ISO, and other styles

8

Elangovan, Allimuthu, Monika Dalal, Gopinathan Kumar Krishna, et al. "Characterization of Atypical Protein Tyrosine Kinase (PTK) Genes and Their Role in Abiotic Stress Response in Rice." Plants 9, no. 5 (2020): 664. http://dx.doi.org/10.3390/plants9050664.

Full text

Abstract:

Tyrosine phosphorylation constitutes up to 5% of the total phophoproteome. However, only limited studies are available on protein tyrosine kinases (PTKs) that catalyze protein tyrosine phosphorylation in plants. In this study, domain analysis of the 27 annotated PTK genes in rice genome led to the identification of 18 PTKs with tyrosine kinase domain. The kinase domain of rice PTKs shared high homology with that of dual specificity kinase BRASSINOSTEROID-INSENSITIVE 1 (BRI1) of Arabidopsis. In phylogenetic analysis, rice PTKs clustered with receptor-like cytoplasmic kinases-VII (RLCKs-VII) of

APA, Harvard, Vancouver, ISO, and other styles

9

Huang, Wen-Yu, Yi-Chen Wu, Hsin-Yi Pu, Ying Wang, Geng-Jen Jang, and Shu-Hsing Wu. "Plant dual-specificity tyrosine phosphorylation-regulated kinase optimizes light-regulated growth and development in Arabidopsis." Plant, Cell & Environment 40, no. 9 (2017): 1735–47. http://dx.doi.org/10.1111/pce.12977.

Full text

APA, Harvard, Vancouver, ISO, and other styles

10

Kaczmarski, Wojciech, Madhabi Barua, Bozena Mazur‐Kolecka, et al. "Intracellular distribution of differentially phosphorylated dual‐specificity tyrosine phosphorylation‐regulated kinase 1A (DYRK1A)." Journal of Neuroscience Research 92, no. 2 (2013): 162–73. http://dx.doi.org/10.1002/jnr.23279.

Full text

APA, Harvard, Vancouver, ISO, and other styles

11

Murakami, Noriko, Wen Xie, Renne Chen Lu, Mo-Chou Chen-Hwang, Andrzej Wieraszko, and Yu Wen Hwang. "Phosphorylation of Amphiphysin I by Minibrain Kinase/Dual-specificity Tyrosine Phosphorylation-regulated Kinase, a Kinase Implicated in Down Syndrome." Journal of Biological Chemistry 281, no. 33 (2006): 23712–24. http://dx.doi.org/10.1074/jbc.m513497200.

Full text

APA, Harvard, Vancouver, ISO, and other styles

12

Song, Woo-Joo, Eun-Ah Christine Song, Min-Su Jung та ін. "Phosphorylation and Inactivation of Glycogen Synthase Kinase 3β (GSK3β) by Dual-specificity Tyrosine Phosphorylation-regulated Kinase 1A (Dyrk1A)". Journal of Biological Chemistry 290, № 4 (2014): 2321–33. http://dx.doi.org/10.1074/jbc.m114.594952.

Full text

APA, Harvard, Vancouver, ISO, and other styles

13

Rossomando, A. J., P. Dent, T. W. Sturgill, and D. R. Marshak. "Mitogen-activated protein kinase kinase 1 (MKK1) is negatively regulated by threonine phosphorylation." Molecular and Cellular Biology 14, no. 3 (1994): 1594–602. http://dx.doi.org/10.1128/mcb.14.3.1594.

Full text

Abstract:

Mitogen-activated protein kinase kinase 1 (MKK1), a dual-specificity tyrosine/threonine protein kinase, has been shown to be phosphorylated and activated by the raf oncogene product as part of the mitogen-activated protein kinase cascade. Here we report the phosphorylation and inactivation of MKK1 by phosphorylation on threonine 286 and threonine 292. MKK1 contains a consensus phosphorylation site for p34cdc2, a serine/threonine protein kinase that regulates the cell division cycle, at Thr-286 and a related site at Thr-292. p34cdc2 catalyzes the in vitro phosphorylation of MKK1 on both of thes

APA, Harvard, Vancouver, ISO, and other styles

14

Rossomando, A. J., P. Dent, T. W. Sturgill, and D. R. Marshak. "Mitogen-activated protein kinase kinase 1 (MKK1) is negatively regulated by threonine phosphorylation." Molecular and Cellular Biology 14, no. 3 (1994): 1594–602. http://dx.doi.org/10.1128/mcb.14.3.1594-1602.1994.

Full text

Abstract:

Mitogen-activated protein kinase kinase 1 (MKK1), a dual-specificity tyrosine/threonine protein kinase, has been shown to be phosphorylated and activated by the raf oncogene product as part of the mitogen-activated protein kinase cascade. Here we report the phosphorylation and inactivation of MKK1 by phosphorylation on threonine 286 and threonine 292. MKK1 contains a consensus phosphorylation site for p34cdc2, a serine/threonine protein kinase that regulates the cell division cycle, at Thr-286 and a related site at Thr-292. p34cdc2 catalyzes the in vitro phosphorylation of MKK1 on both of thes

APA, Harvard, Vancouver, ISO, and other styles

15

Trojanek, Joanna B., Maria M. Klimecka, Anna Fraser, Grazyna Dobrowolska, and Grazyna Muszyńska. "Characterization of dual specificity protein kinase from maize seedlings." Acta Biochimica Polonica 51, no. 3 (2004): 635–47. http://dx.doi.org/10.18388/abp.2004_3549.

Full text

Abstract:

A protein kinase of 57 kDa, able to phosphorylate tyrosine in synthetic substrates pol(Glu4,Tyr1) and a fragment of Src tyrosine kinase, was isolated and partly purified from maize seedlings (Zea mays). The protein kinase was able to phosphorylate exogenous proteins: enolase, caseins, histones and myelin basic protein. Amino acid analysis of phosphorylated casein and enolase, as well as of phosphorylated endogenous proteins, showed that both Tyr and Ser residues were phosphorylated. Phosphotyrosine was also immunodetected in the 57 kDa protein fraction. In the protein fraction there are presen

APA, Harvard, Vancouver, ISO, and other styles

16

王, 勇. "The Dual-Specificity Tyrosine Phosphorylation Regulated Kinase 1A and the Advances of Its Inhibitors." Hans Journal of Medicinal Chemistry 08, no. 02 (2020): 38–50. http://dx.doi.org/10.12677/hjmce.2020.82006.

Full text

APA, Harvard, Vancouver, ISO, and other styles

17

Jin, Nana, Xiaomin Yin, Jianlan Gu, et al. "Truncation and Activation of Dual Specificity Tyrosine Phosphorylation-regulated Kinase 1A by Calpain I." Journal of Biological Chemistry 290, no. 24 (2015): 15219–37. http://dx.doi.org/10.1074/jbc.m115.645507.

Full text

APA, Harvard, Vancouver, ISO, and other styles

18

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 (2010): 720–24. http://dx.doi.org/10.1007/s00343-010-9073-7.

Full text

APA, Harvard, Vancouver, ISO, and other styles

19

Derrien, M., A. Punjabi, M. Khanna, O. Grubisha, and P. Traktman. "Tyrosine Phosphorylation of A17 during Vaccinia Virus Infection: Involvement of the H1 Phosphatase and the F10 Kinase." Journal of Virology 73, no. 9 (1999): 7287–96. http://dx.doi.org/10.1128/jvi.73.9.7287-7296.1999.

Full text

Abstract:

ABSTRACT Vaccinia virus encodes two protein kinases (B1 and F10) and a dual-specificity phosphatase (VH1), suggesting that phosphorylation and dephosphorylation of substrates on serine/threonine and tyrosine residues are important in regulating diverse aspects of the viral life cycle. Using a recombinant in which expression of the H1 phosphatase can be regulated experimentally (vindH1), we have previously demonstrated that repression of H1 leads to the maturation of noninfectious virions that contain several hyperphosphorylated substrates (K. Liu et al., J. Virol. 69:7823–7834). In this report

APA, Harvard, Vancouver, ISO, and other styles

20

Oi, Ami, Syouichi Katayama, Naoya Hatano, Yasunori Sugiyama, Isamu Kameshita, and Noriyuki Sueyoshi. "Subcellular distribution of cyclin-dependent kinase-like 5 (CDKL5) is regulated through phosphorylation by dual specificity tyrosine-phosphorylation-regulated kinase 1A (DYRK1A)." Biochemical and Biophysical Research Communications 482, no. 2 (2017): 239–45. http://dx.doi.org/10.1016/j.bbrc.2016.11.048.

Full text

APA, Harvard, Vancouver, ISO, and other styles

21

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 (2020): 4747–63. http://dx.doi.org/10.1007/s00018-020-03556-1.

Full text

Abstract:

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

APA, Harvard, Vancouver, ISO, and other styles

22

Liu, F., J. J. Stanton, Z. Wu, and H. Piwnica-Worms. "The human Myt1 kinase preferentially phosphorylates Cdc2 on threonine 14 and localizes to the endoplasmic reticulum and Golgi complex." Molecular and Cellular Biology 17, no. 2 (1997): 571–83. http://dx.doi.org/10.1128/mcb.17.2.571.

Full text

Abstract:

Entry into mitosis requires the activity of the Cdc2 kinase. Cdc2 associates with the B-type cyclins, and the Cdc2-cyclin B heterodimer is in turn regulated by phosphorylation. Phosphorylation of threonine 161 is required for the Cdc2-cyclin B complex to be catalytically active, whereas phosphorylation of threonine 14 and tyrosine 15 is inhibitory. Human kinases that catalyze the phosphorylation of threonine 161 and tyrosine 15 have been identified. Here we report the isolation of a novel human cDNA encoding a dual-specificity protein kinase (designated Myt1Hu) that preferentially phosphorylat

APA, Harvard, Vancouver, ISO, and other styles

23

Nguyen, Thu Lan, Corinne Fruit, Yann Hérault, Laurent Meijer, and Thierry Besson. "Dual-specificity tyrosine phosphorylation-regulated kinase 1A (DYRK1A) inhibitors: a survey of recent patent literature." Expert Opinion on Therapeutic Patents 27, no. 11 (2017): 1183–99. http://dx.doi.org/10.1080/13543776.2017.1360285.

Full text

APA, Harvard, Vancouver, ISO, and other styles

24

Guterman-Ram, Gali, Milena Pesic, Ayelet Orenbuch, Tal Czeiger, Anastasia Aflalo, and Noam Levaot. "Dual-specificity tyrosine phosphorylation-regulated kinase 2 regulates osteoclast fusion in a cell heterotypic manner." Journal of Cellular Physiology 233, no. 1 (2017): 617–29. http://dx.doi.org/10.1002/jcp.25922.

Full text

APA, Harvard, Vancouver, ISO, and other styles

25

Banerjee, Sourav, Tiantian Wei, Jue Wang, 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 (2019): 24881–91. http://dx.doi.org/10.1073/pnas.1912033116.

Full text

Abstract:

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

APA, Harvard, Vancouver, ISO, and other styles

26

Adayev, Tatyana, Jerzy Wegiel, and Yu-Wen Hwang. "Harmine is an ATP-competitive inhibitor for dual-specificity tyrosine phosphorylation-regulated kinase 1A (Dyrk1A)." Archives of Biochemistry and Biophysics 507, no. 2 (2011): 212–18. http://dx.doi.org/10.1016/j.abb.2010.12.024.

Full text

APA, Harvard, Vancouver, ISO, and other styles

27

Morrugares, Rosario, Alejandro Correa-Sáez, Rita Moreno, et al. "Phosphorylation-dependent regulation of the NOTCH1 intracellular domain by dual-specificity tyrosine-regulated kinase 2." Cellular and Molecular Life Sciences 77, no. 13 (2019): 2621–39. http://dx.doi.org/10.1007/s00018-019-03309-9.

Full text

Abstract:

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 degr

APA, Harvard, Vancouver, ISO, and other styles

28

Bhardwaj, Vijay Kumar, Rahul Singh, Jatin Sharma, Pralay Das, and Rituraj Purohit. "Structural based study to identify new potential inhibitors for dual specificity tyrosine-phosphorylation- regulated kinase." Computer Methods and Programs in Biomedicine 194 (October 2020): 105494. http://dx.doi.org/10.1016/j.cmpb.2020.105494.

Full text

APA, Harvard, Vancouver, ISO, and other styles

29

Hoekstra, M. F., N. Dhillon, G. Carmel, et al. "Budding and fission yeast casein kinase I isoforms have dual-specificity protein kinase activity." Molecular Biology of the Cell 5, no. 8 (1994): 877–86. http://dx.doi.org/10.1091/mbc.5.8.877.

Full text

Abstract:

We have examined the activity and substrate specificity of the Saccharomyces cerevisiae Hrr25p and the Schizosaccharomyces pombe Hhp1, Hhp2, and Cki1 protein kinase isoforms. These four gene products are isotypes of casein kinase I (CKI), and the sequence of these protein kinases predicts that they are protein serine/threonine kinases. However, each of these four protein kinases, when expressed in Escherichia coli in an active form, was recognized by anti-phosphotyrosine antibodies. Phosphoamino acid analysis of 32P-labeled proteins showed phosphorylation on serine, threonine, and tyrosine res

APA, Harvard, Vancouver, ISO, and other styles

30

Llorach-Pares, Laura, Alfons Nonell-Canals, Conxita Avila, and Melchor Sanchez-Martinez. "Kororamides, Convolutamines, and Indole Derivatives as Possible Tau and Dual-Specificity Kinase Inhibitors for Alzheimer’s Disease: A Computational Study." Marine Drugs 16, no. 10 (2018): 386. http://dx.doi.org/10.3390/md16100386.

Full text

Abstract:

Alzheimer’s disease (AD) is becoming one of the most disturbing health and socioeconomic problems nowadays, as it is a neurodegenerative pathology with no treatment, which is expected to grow further due to population ageing. Actual treatments for AD produce only a modest amelioration of symptoms, although there is a constant ongoing research of new therapeutic strategies oriented to improve the amelioration of the symptoms, and even to completely cure the disease. A principal feature of AD is the presence of neurofibrillary tangles (NFT) induced by the aberrant phosphorylation of the microtub

APA, Harvard, Vancouver, ISO, and other styles

31

Annunziata, Maria Carmela, Melania Parisi, Gabriella Esposito, Gabriella Fabbrocini, Rosario Ammendola, and Fabio Cattaneo. "Phosphorylation Sites in Protein Kinases and Phosphatases Regulated by Formyl Peptide Receptor 2 Signaling." International Journal of Molecular Sciences 21, no. 11 (2020): 3818. http://dx.doi.org/10.3390/ijms21113818.

Full text

Abstract:

FPR1, FPR2, and FPR3 are members of Formyl Peptides Receptors (FPRs) family belonging to the GPCR superfamily. FPR2 is a low affinity receptor for formyl peptides and it is considered the most promiscuous member of this family. Intracellular signaling cascades triggered by FPRs include the activation of different protein kinases and phosphatase, as well as tyrosine kinase receptors transactivation. Protein kinases and phosphatases act coordinately and any impairment of their activation or regulation represents one of the most common causes of several human diseases. Several phospho-sites has b

APA, Harvard, Vancouver, ISO, and other styles

32

Her, J. H., S. Lakhani, K. Zu, et al. "Dual phosphorylation and autophosphorylation in mitogen-activated protein (MAP) kinase activation." Biochemical Journal 296, no. 1 (1993): 25–31. http://dx.doi.org/10.1042/bj2960025.

Full text

Abstract:

p42mapk [mitogen activated protein (MAP) kinase; extracellular signal-regulated protein kinase (ERK)] is a serine/threonine-specific protein kinase that is activated by dual tyrosine and threonine phosphorylation in response to diverse agonists. Both the tyrosine and threonine phosphorylations are necessary for full enzymic activity. A MAP kinase activator recently purified and cloned has been shown to be a protein kinase (MAP kinase kinase) that is able to induce the dual phosphorylation of MAP kinase on both the regulatory tyrosine and threonine sites in vitro. In the present paper we have u

APA, Harvard, Vancouver, ISO, and other styles

33

Wang, Q. M., C. J. Fiol, A. A. DePaoli-Roach, and P. J. Roach. "Glycogen synthase kinase-3 beta is a dual specificity kinase differentially regulated by tyrosine and serine/threonine phosphorylation." Journal of Biological Chemistry 269, no. 20 (1994): 14566–74. http://dx.doi.org/10.1016/s0021-9258(17)36661-9.

Full text

APA, Harvard, Vancouver, ISO, and other styles

34

Hamilton, Stuart T., Corina Hutterer, Ece Egilmezer, et al. "Human cytomegalovirus utilises cellular dual-specificity tyrosine phosphorylation-regulated kinases during placental replication." Placenta 72-73 (December 2018): 10–19. http://dx.doi.org/10.1016/j.placenta.2018.10.002.

Full text

APA, Harvard, Vancouver, ISO, and other styles

35

Ma, Fei, Yuekun Zhu, Xing Liu, et al. "Dual‐Specificity Tyrosine Phosphorylation–Regulated Kinase 3 Loss Activates Purine Metabolism and Promotes Hepatocellular Carcinoma Progression." Hepatology 70, no. 5 (2019): 1785–803. http://dx.doi.org/10.1002/hep.30703.

Full text

APA, Harvard, Vancouver, ISO, and other styles

36

WOODS, Yvonne L., Philip COHEN, Walter BECKER та ін. "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, № 3 (2001): 609–15. http://dx.doi.org/10.1042/bj3550609.

Full text

Abstract:

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 o

APA, Harvard, Vancouver, ISO, and other styles

37

Kim, Kyeongmin, Sungmin Lee, Hyunkoo Kang, et al. "Dual Specificity Kinase DYRK3 Promotes Aggressiveness of Glioblastoma by Altering Mitochondrial Morphology and Function." International Journal of Molecular Sciences 22, no. 6 (2021): 2982. http://dx.doi.org/10.3390/ijms22062982.

Full text

Abstract:

Glioblastoma multiforme (GBM) is a malignant primary brain tumor with poor patient prognosis. Although the standard treatment of GBM is surgery followed by chemotherapy and radiotherapy, often a small portion of surviving tumor cells acquire therapeutic resistance and become more aggressive. Recently, altered kinase expression and activity have been shown to determine metabolic flux in tumor cells and metabolic reprogramming has emerged as a tumor progression regulatory mechanism. Here we investigated novel kinase-mediated metabolic alterations that lead to acquired GBM radioresistance and mal

APA, Harvard, Vancouver, ISO, and other styles

38

Bokemeyer, D., A. Sorokin, and M. J. Dunn. "Differential regulation of the dual-specificity protein-tyrosine phosphatases CL100, B23, and PAC1 in mesangial cells." Journal of the American Society of Nephrology 8, no. 1 (1997): 40–50. http://dx.doi.org/10.1681/asn.v8140.

Full text

Abstract:

The extracellular-signal-regulated kinase (ERK), the best described MAP kinase cascade, is a major signaling system by which cells transduce extracellular cues into intracellular responses. ERK is activated by phosphorylation both on tyrosine and threonine residues. Therefore, a new clas of protein-tyrosine phosphatases (PTPases) that exhibit dual catalytic activity toward both regulatory sites on ERK is of special interest in the control of intracellular signaling. This study examined the expression and regulation of the dual-specificity PTPases CL100, B23, and PAC1. Findings included differe

APA, Harvard, Vancouver, ISO, and other styles

39

Kawakubo, Takashi, Ryotaro Mori, Keiro Shirotani, Nobuhisa Iwata, and Masashi Asai. "Neprilysin Is Suppressed by Dual-Specificity Tyrosine-Phosphorylation Regulated Kinase 1A (DYRK1A) in Down-Syndrome-Derived Fibroblasts." Biological & Pharmaceutical Bulletin 40, no. 3 (2017): 327–33. http://dx.doi.org/10.1248/bpb.b16-00825.

Full text

APA, Harvard, Vancouver, ISO, and other styles

40

Sitz, J. H., K. Baumgärtel, B. Hämmerle, et al. "The down syndrome candidate dual-specificity tyrosine phosphorylation-regulated kinase 1A phosphorylates the neurodegeneration-related septin 4." Neuroscience 157, no. 3 (2008): 596–605. http://dx.doi.org/10.1016/j.neuroscience.2008.09.034.

Full text

APA, Harvard, Vancouver, ISO, and other styles

41

Alvarez, Mónica, Xavier Altafaj, Sergi Aranda, and Susana de la Luna. "DYRK1A Autophosphorylation on Serine Residue 520 Modulates Its Kinase Activity via 14-3-3 Binding." Molecular Biology of the Cell 18, no. 4 (2007): 1167–78. http://dx.doi.org/10.1091/mbc.e06-08-0668.

Full text

Abstract:

Dual-specificity tyrosine-phosphorylated and regulated kinase (DYRK) proteins are an evolutionarily conserved family of protein kinases, with members identified from yeast to humans, that participate in a variety of cellular processes. DYRKs are serine/threonine protein kinases that are activated by autophosphorylation on a tyrosine residue in the activation loop. The family member DYRK1A has been shown to phosphorylate several cytosolic proteins and a number of splicing and transcription factors, including members of the nuclear factor of activated T cells family. In the present study, we sho

APA, Harvard, Vancouver, ISO, and other styles

42

Nuckolls, G. H., N. Osherov, W. F. Loomis, and J. A. Spudich. "The Dictyostelium dual-specificity kinase splA is essential for spore differentiation." Development 122, no. 10 (1996): 3295–305. http://dx.doi.org/10.1242/dev.122.10.3295.

Full text

Abstract:

We have studied the structure and function of the Dictyostelium kinase splA. A truncated form of the splA protein exhibited primarily tyrosine kinase activity in vitro; however, it also autophosphorylated on serine and threonine residues. The kinase domain of splA exhibits approximately 38% identity to the CTR1 kinase of Arabidopsis, which is a member of the Raf family. Outside its kinase domain, splA shares homology with the byr2 kinase of S. pombe. By aligning the sequences of splA, byr2 and STE11, a homologue of byr2 in S. cerevisiae, we have identified a conserved motif that is also found

APA, Harvard, Vancouver, ISO, and other styles

43

Yoon, Hye Ree, Anand Balupuri, Kwang-Eun Choi, and Nam Sook Kang. "Small Molecule Inhibitors of DYRK1A Identified by Computational and Experimental Approaches." International Journal of Molecular Sciences 21, no. 18 (2020): 6826. http://dx.doi.org/10.3390/ijms21186826.

Full text

Abstract:

Dual-specificity tyrosine phosphorylation-regulated kinase 1A (DYRK1A) is a protein kinase with diverse functions in cell regulation. Abnormal expression and activity of DYRK1A contribute to numerous human malignancies, Down syndrome, and Alzheimer’s disease. Notably, DYRK1A has been proposed as a potential therapeutic target for the treatment of diabetes because of its key role in pancreatic β-cell proliferation. Consequently, DYRK1A is an attractive drug target for a variety of diseases. Here, we report the identification of several DYRK1A inhibitors using our in-house topological water netw

APA, Harvard, Vancouver, ISO, and other styles

44

Tian, Shijiao, Wenming Jia, Mei Lu, Juan Zhao, and Xiulian Sun. "Dual-specificity tyrosine phosphorylation-regulated kinase 1A ameliorates insulin resistance in neurons by up-regulating IRS-1 expression." Journal of Biological Chemistry 294, no. 52 (2019): 20164–76. http://dx.doi.org/10.1074/jbc.ra119.010809.

Full text

APA, Harvard, Vancouver, ISO, and other styles

45

Yan, Haiyan, Kaishun Hu, Wenjing Wu, et al. "Low Expression of DYRK2 (Dual Specificity Tyrosine Phosphorylation Regulated Kinase 2) Correlates with Poor Prognosis in Colorectal Cancer." PLOS ONE 11, no. 8 (2016): e0159954. http://dx.doi.org/10.1371/journal.pone.0159954.

Full text

APA, Harvard, Vancouver, ISO, and other styles

46

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

Full text

Abstract:

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

APA, Harvard, Vancouver, ISO, and other styles

47

Hutterer, Corina, Jens Milbradt, Stuart Hamilton, et al. "Inhibitors of dual-specificity tyrosine phosphorylation-regulated kinases (DYRK) exert a strong anti-herpesviral activity." Antiviral Research 143 (July 2017): 113–21. http://dx.doi.org/10.1016/j.antiviral.2017.04.003.

Full text

APA, Harvard, Vancouver, ISO, and other styles

48

Banerjee, Sourav, Chenggong Ji, Joshua E. Mayfield, et al. "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 (2018): 8155–60. http://dx.doi.org/10.1073/pnas.1806797115.

Full text

Abstract:

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 p

APA, Harvard, Vancouver, ISO, and other styles

49

BÖRSCH-HAUBOLD, Angelika G., Ruth M. KRAMER, and Steve P. WATSON. "Inhibition of mitogen-activated protein kinase kinase does not impair primary activation of human platelets." Biochemical Journal 318, no. 1 (1996): 207–12. http://dx.doi.org/10.1042/bj3180207.

Full text

Abstract:

Mitogen-activated protein kinases (MAPKs), a family of protein serine/threonine kinases regulating cell growth and differentiation, are activated by a dual-specificity kinase through phosphorylation at threonine and tyrosine. We used a recently described selective inhibitor of the p42/p44mapk-activating enzyme, PD 98059 [2-(2´-amino-3´-methoxyphenyl)-oxanaphthalen-4-one], to investigate the role of the p42/p44mapk pathway in human platelets. PD 98059 inhibited p42/p44mapk activation in thrombin-, collagen- and phorbol ester-stimulated platelets, as determined from in-gel renaturation kinase as

APA, Harvard, Vancouver, ISO, and other styles

50

Alexeeva, Marina, Espen Åberg, Richard A. Engh, and Ulli Rothweiler. "The structure of a dual-specificity tyrosine phosphorylation-regulated kinase 1A–PKC412 complex reveals disulfide-bridge formation with the anomalous catalytic loop HRD(HCD) cysteine." Acta Crystallographica Section D Biological Crystallography 71, no. 5 (2015): 1207–15. http://dx.doi.org/10.1107/s1399004715005106.

Full text

Abstract:

Dual-specificity tyrosine phosphorylation-regulated kinase 1A (DYRK1A) is a protein kinase associated with neuronal development and brain physiology. The DYRK kinases are very unusual with respect to the sequence of the catalytic loop, in which the otherwise highly conserved arginine of the HRD motif is replaced by a cysteine. This replacement, along with the proximity of a potential disulfide-bridge partner from the activation segment, implies a potential for redox control of DYRK family activities. Here, the crystal structure of DYRK1A bound to PKC412 is reported, showing the formation of th

APA, Harvard, Vancouver, ISO, and other styles

We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!